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Title:
STRUCTURE OF THE C-TERMINAL REGION OF THE INSULIN RECEPTOR α-CHAIN AND OF THE INSULIN-LIKE GROWTH FACTOR RECEPTOR α-CHAIN
Document Type and Number:
WIPO Patent Application WO/2010/121288
Kind Code:
A1
Abstract:
The present invention relates generally to structural studies of the insulin binding site of the insulin receptor (IR) and the insulin-like growth factor 1 receptor (IGF-1R). More particularly, the present invention relates to the crystal structure of the low affinity insulin binding site of the IR ectodomain comprising the C-terminal region of the IR α-chain, as well as the corresponding region of IGF-1R, and to methods of using the crystal and related structural information to screen for and design compounds that interact with or modulate the function of IR and/or IGF-1R.

Inventors:
LAWRENCE, Michael, Colin (Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade Parkvill, Melbourne Victoria 3052, AU)
SMITH, Brian, John (Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade Parkvill, Melbourne Victoria 3052, AU)
MENTING, John, Gerbrandt, Tasman (Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade Parkvill, Melbourne Victoria 3052, AU)
WARD, Colin, Wesley (Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade Parkvill, Melbourne Victoria 3052, AU)
Application Number:
AU2010/000271
Publication Date:
October 28, 2010
Filing Date:
March 09, 2010
Export Citation:
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Assignee:
WALTER AND ELIZA HALL INSTITUTE OF MEDICAL RESEARCH (Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade Parkvill, Melbourne Victoria 3052, AU)
LAWRENCE, Michael, Colin (Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade Parkvill, Melbourne Victoria 3052, AU)
SMITH, Brian, John (Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade Parkvill, Melbourne Victoria 3052, AU)
MENTING, John, Gerbrandt, Tasman (Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade Parkvill, Melbourne Victoria 3052, AU)
WARD, Colin, Wesley (Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade Parkvill, Melbourne Victoria 3052, AU)
International Classes:
G01N33/68; C07K14/72; C40B30/04; G01N23/20; G06F17/50; G06Q50/00
Domestic Patent References:
2007-12-27
1999-06-10
1999-06-10
2007-12-27
Foreign References:
EP0957164B12001-03-21
US7173005B22007-02-06
US20080153802A12008-06-26
US5223409A1993-06-29
Other References:
MENTING, J. ET AL.: 'A Thermodynamic Study of Ligand Binding to the First Three Domains of the Human Insulin Receptor: Relationship between the Receptor a-Chain C-Terminal Peptide and the Site 1 Insulin Mimetic Peptides' BIOCHEMISTRY vol. 48, no. 23, 2009, pages 5492 - 5500, XP055043611
MCKERN, N. M. ET AL.: 'Structure of the Insulin Receptor Ectodomain Reveals a Folded-Over Conformation' NATURE vol. 443, 2006, pages 218 - 221, XP008102956
LOU, M. ET AL.: 'The First Three Domains of the Insulin Receptor Differ Structurally from the Insulin-Like Growth Factor 1 Receptor in the Regions Governing Ligand Specificity' PROC. NATL. ACAD. SCI. USA vol. 103, no. 33, 2006, pages 12429 - 12434, XP008102973
MUNSHI, S. ET AL.: 'Crystal Structure of the Apo, Unactivated Insulin-Like Growth Factor-I Receptor Kinase. Implication for Inhibitor Specificity' J. BIOL. CHEM. vol. 277, no. 41, 2002, pages 38797 - 38802, XP055043633
See also references of EP 2422201A1
Attorney, Agent or Firm:
MONGER, Carmela (Abstract, Walter and Eliza Hall Institute of Medical Research1G Royal Parade, Parkvill, Melbourne Victoria 3052, AU)
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Claims:
Claims

1. A method of identifying, designing or screening for a compound that can potentially interact with insulin receptor (IR) and/or insulin-like growth factor- 1 receptor (IGF- 1 R), comprising performing structure-based identification, design or screening of a compound based on the compound's interactions with a structure defined by the atomic coordinates of one or more of Appendixes I to VI, or a subset of atomic coordinates of one or more thereof at least representing the C-terminal region of the α-chain of IR, the C-terminal region of the α-chain of IGF-IR, or a mimetic of the C-terminal region of the α-chain of IR and/or IGF-IR.

2. The method according to claim 1, comprising identifying, designing or screening for a compound which interacts with the three-dimensional structure of;

(i) the low affinity insulin binding site of IR, the structure being defined by the atomic coordinates shown in one or more of Appendixes I, III and V; and/or (ii) the low affinity insulin-like growth factor (IGF) binding site of IGF-IR, the structure being defined by the atomic coordinates shown in one or more of Appendixes II, IV and VI, wherein interaction of the compound with the structure is favoured energetically.

3. The method according to claim 1 or claim 2, further comprising synthesising or obtaining an identified or designed candidate compound and determining the ability of the candidate compound to interact with IR and/or IGF-IR.

4. The method according to any one of claims 1 to 3, wherein the atomic coordinates define one or more regions of the low affinity binding site of IR for insulin, and/or the low affinity binding site of IGF-IR for IGF, comprising the C-terminal region of the α- chain of IR, the C-terminal region of the α-chain of IGF-IR, or a mimetic of the C- terminal region of the α-chain of IR and/or IGF-IR.

5. The method according to claim 4, wherein the C-terminal region of the α-chain of IR comprises amino acids 693 to 710 of IR α-chain (SEQ ID NO: 13).

6. The method according to claim 5, wherein the atomic coordinates defining the low affinity insulin binding site of IR further comprise the leucine-rich repeat 1 (Ll) domain and/or the cysteine-rich (CR) domain of the IR ectodomain.

7. The method according to claim 6, wherein the atomic coordinates define portions of the molecular surface of the central β-sheet of the Ll domain and portions of the molecular surface of the second leucine-rich repeat (LRR) which contain Phe39 and/or the loop in the fourth LRR rung of the Ll domain.

8. The method according to claim 6 or claim 7, wherein the atomic coordinates define module'6 of the CR domain of IR.

9. The method according to any one of claims 4 to 8, wherein the atomic coordinates further define one or more amino acid sequences selected from IR amino acid residues 1- 156, 157-310, 594 and 794.

10. The method according to claim 9, wherein the one or more amino acids selected from IR amino acid residues 1-156 comprise at least one amino acid selected from Argl4, Asnl5, Gln34, Leu36, Leu37, Phe39, Pro43, Phe46, Leu62, Phe64, ,Leu87, Phe88, Phe89, Asn90, Phe96, Glu97, Argl 18, Glul20 and Hisl44.

11. The method according to claim 9 or claim 10, wherein the one or more amino acids selected from IR amino acid residues 157-310 comprise at least one of the amino acid sequences selected from 192-310, 227-303 and 259-284.

12. ' The method according to claim 4, wherein the C-terminal region of the α-chain of IGF-IR comprises amino acids 681 to 697 of IGF-IR α-chain (SEQ ID NO: 15).

13. The method according to claim 12, wherein the atomic coordinates defining the low affinity IGF binding site of IGF-IR further comprise the Ll domain and/or the CR domain of IGF- 1 R ectodomain.

14. The method according to claim 13, wherein the atomic coordinates define the central β-sheet of the Ll domain, and/or that part of the second LRR containing Ser35, and/or the loop in the fourth LRR rung of the Ll domain.

15. The method according to claim 13 or claim 14, wherein the atomic coordinates define module 6 of the CR domain of IGF-IR.

16. The method according to any one of claims 4 to 15, wherein the mimetic of the C- terminal region of the α-chain of IR and/or IGF-IR is S519C16 (SEQ ID NO: 18).

17. The method of claim 2, wherein the compound substitutes for the C-terminal region of the α-chain of IR and/or the C-terminal region of the α-chain of IGF-IR in the formation of the low affinity binding site of IR or IGF-IR.

18. The method according to any one of claims 1 to 17, wherein a candidate compound for interacting with IR and/or IGF-IR is chemically modified as a result of structure-based evaluation.

19. The method according to claim 18, wherein the chemical modification is designed to either:

(i) reduce the potential for the candidate compound to bind to IR whilst maintaining binding to IGF-IR; or

(ii) reduce the potential for the candidate compound to bind to IGF-IR, whilst maintaining binding to IR.

20. A method of redesigning a compound which is known to bind to IR and/or IGF- IR comprising performing structure-based evaluation of the compound based on the compound's interactions with a structure defined by the atomic coordinates of one or more of Appendixes I to VI, or a subset of atomic coordinates of one or more thereof at least representing the C-terminal region of the α-chain of IR, the C-terminal region of the α-chain of IGF-IR, or a mimetic of the C-terminal region of the α-chain of IR and/or IGF-IR, and redesigning or chemically modifying the compound as a result of the evaluation.

21. The method according to claim 20, wherein the compound is redesigned or chemically modified to (i) improve affinity for binding to IR, and/or (ii) lower affinity for binding to IGF-IR.

22. The method according to claim 20, wherein the compound is redesigned or chemically modified to (i) improve affinity for binding to IGF-IR, and/or (ii) lower affinity for binding to IR.

23. The method according to claim 21 or claim 22, wherein the compound is redesigned or modified so as to lower the affinity to IR or IGF- IR by virtue of the structural differences between IR and IGF-IR at or in the vicinity of the C-terminal region of the α-chain of IR and the C-terminal region of the α-chain of IGF-IR.

24. A computer system for identifying one or more compounds that can potentially interact with IR and/or IGF-IR, the system containing data representing the structure of: (i) the low affinity insulin binding site of IR, the structure being defined by the atomic coordinates shown in one or more of Appendixes I, III and V;

(ii) the low affinity IGF binding site of IGF-IR, the structure being defined by the atomic coordinates shown in one or more of Appendixes II, IV and VI; and/or (iii) the C-terminal region of the α-chain of IR, the C-terminal region of the α-chain of IGF-IR, or a mimetic of the C-terminal region of the α-chain of IR and/or IGF-IR, the structure being defined by a subset of atomic coordinates shown in one or more of Appendixes I to VI.

25. A computer-readable medium having recorded thereon data representing a model and/or the atomic coordinates as shown in one or more of Appendixes I to VI, or a subset of atomic coordinates of one or more thereof at least representing:

(i) the C-terminal region of the α-chain of IR; (ii) the C-terminal region of the α-chain of IGF-IR; and/or (iii) a mimetic of the C-terminal region of the α-chain of IR and/or IGF-IR, as any one of (i) to (iii) associates with IR and/or IGF-IR.

26. A set of coordinates as shown in one or more of Appendixes I to VI, or a subset of atomic coordinates of one or more thereof at least representing:

(i) the C-terminal region of the α-chain of IR; (ii) the C-terminal region of the α-chain of IGF- 1 R; and/or (iii) a mimetic of the C-terminal region of the α-chain of IR and/or IGF-IR, as any one of (i) to (iii) associates with IR and/or IGF-IR.

27. A computer-assisted method of identifying a compound that potentially interacts with IR and/or IGF-IR, which method comprises fitting the structure of:

(i) the low affinity insulin binding site of IR, the structure being defined by the atomic coordinates shown in one or more of Appendixes I, III and. V; (ii) the low affinity IGF binding site of IGF-IR, the structure being defined by the atomic coordinates shown in one or more of Appendixes II, IV and VI; and/or ) the C-terminal region of the α-chain of IR, the C-terminal region of the α-chain of IGF- IR, or a mimetic of the C-terminal region of the α-chain of IR and/or IGF-IR, the structure being defined by a subset of atomic coordinates shown in one or more of Appendixes I to VI, to the structure of a candidate compound.

28. A computer-assisted method for identifying a compound able to interact with IR and/or IGF-IR using a programmed computer comprising a processor, which method comprises the steps of:

(a) generating, using computer methods, a set of atomic coordinates of a structure that possesses energetically favourable interactions with the atomic coordinates of:

(i) the low affinity insulin binding site of IR, the structure being defined by the atomic coordinates shown in one or more of Appendixes I, III and V;

(ii) the low affinity IGF binding site of IGF-IR, the structure being defined by the atomic coordinates shown in one or more of Appendixes II, IV and VI; and/or

(iii) the C-terminal region of the α-chain of IR, the C-terminal region of the α- chain of IGF-IR, or a mimetic of the C-terminal region of the α-chain of IR and/or IGF- IR, the structure being defined by a subset of atomic coordinates shown in one or more of Appendixes I to VI, which coordinates are entered into the computer thereby generating a criteria data set;

(b) comparing, using the processor, the criteria data set to a computer database of chemical structures;

(c) selecting from the database, using computer methods, chemical structures which are complementary or similar to a region of the criteria data set; and optionally,

(d) outputting, to an output device, the selected chemical structures which are complementary to or similar to a region of the criteria data set.

29. A computer-assisted method for identifying potential mimetics of IR and/or IGF- IR using a programmed computer comprising a processor, the method comprising the steps of:

(a) generating a criteria data set from a set of atomic coordinates of:

(i) the low affinity insulin binding site of IR, the structure being defined by the atomic coordinates shown in one or more of Appendixes I, III and V; (ii) the low affinity IGF binding site of IGF- 1 R, the structure being defined by the atomic coordinates shown in one or more of Appendixes II, IV and VI; and/or

(iii) the C-terminal region of the α-chain of IR, the C-terminal region of the α-chain of IGF-IR, or a mimetic of the C-terminal region of the α-chain of IR and/or

IGF-IR, the structure being defined by a subset of atomic coordinates shown in one or more of Appendixes I to VI, which coordinates are entered into the computer;

(b) (i) comparing, using the processor, the criteria data set to a computer database of chemical structures stored in a computer data storage system and selecting from the database, using computer methods, chemical structures having a region that is structurally similar to the criteria data set; or

(ii) constructing, using computer methods, a model of a chemical structure having a region that is structurally similar to the criteria data set; and, optionally,

(c) outputting to an output device:

(i) the selected chemical structures from step (b)(i) having a region similar to the criteria data set; or

(ii) the constructed model from step (b)(ii).

30. A method for evaluating the ability of a compound to interact with IR and/or IGF- IR, the method comprising the steps of:

(a) employing computational means to perform a fitting operation between the compound and the binding surface of a computer model of the low affinity binding site for insulin on IR ectodomain, and/or the low affinity binding site for IGF on IGF-IR ectodomain, using atomic coordinates wherein the root mean square deviation between the atomic coordinates and atomic coordinates of one or more of Appendixes I to VI or a subset of atomic coordinates of one or more thereof at least representing the C-terminal region of the α-chain of IR, the C-terminal region of the α-chain of IGF-IR, or a mimetic of the C-terminal region of the α-chain of IR and/or IGF-IR, is not more than 1.5 A; and

(b) analysing the results of the fitting operation to quantify the association between the compound and the binding surface model.

31. A method of using molecular replacement to obtain structural information about a molecule or a molecular complex of unknown structure, comprising the steps of:

(i) generating an X-ray diffraction pattern of the crystallized molecule or molecular complex; and (ii) applying the atomic coordinates of one or more of Appendixes I to VI, or a subset of atomic coordinates of one or more thereof at least representing the C-terminal region of the α-chain of IR, the C-terminal region of the α-chain of IGF-IR, or a mimetic of the C-terminal region of the α-chain of IR and/or IGF-IR, to the X-ray diffraction pattern to generate a three-dimensional electron density map of at least a region of the molecule or molecular complex whose structure is unknown.

32. A compound that binds to IR and/or IGF-IR ectodomain designed, redesigned or modified using a method according to any one of claims 1 to 23 or 27 to 31.

33. The compound according to claim 32 having an affinity (Kd) for IR and/or IGF- IR less than 10"5 M.

34. The compound according to claim 32 or claim 33, wherein the compound binds to the low affinity binding site of IR and/or to the low affinity binding site of IGF-IR.

35. An isolated peptide or mimetic thereof which binds the Ll domain of IR and/or the Ll domain of IGF-IR, the peptide comprising:

(i) an amino acid sequence as provided in SEQ ID NO: 13 or SEQ ID NO: 15; (ii) an amino acid sequence which is at least 50% identical to SEQ ID NO: 13 and/or SEQ ID NO: 15; or

(iii) a fragment of (i) or (ii) which binds the Ll domain of IR and/or the Ll domain of IGF-IR, wherein the peptide has a helical structure.

36. An isolated polynucleotide encoding the peptide according to claim 35.

37. A composition comprising a compound according to any one of claims 32 to 34, or a peptide or mimetic thereof according to claim 35, and/or a polynucleotide according to claim 36, and optionally an acceptable carrier or diluent.

38. A method for preventing or treating a disease associated with aberrant IR and/or IGF-IR functioning and/or signalling, the method comprising administering to a subject in need thereof a compound according to any one of claims 32 to 34, a peptide or mimetic thereof according to claim 35, and/or a polynucleotide according to claim 36.

39. Use of a compound according to any one of claims 32 to 34, a peptide or mimetic thereof according to claim 35, and/or a polynucleotide according to claim 36," for the manufacture of a medicament for treating a disease in a subject associated with aberrant IR and/or IGF-IR functioning and/or signalling.

40. The method according to claim 38 or the use according to claim 39, wherein the disease associated with aberrant IR and/or IGF-IR functioning and/or signalling is selected from obesity, type I and type II diabetes, cardiovascular disease, osteoporosis, dementia or cancer.

Description:
STRUCTURE OF THE C-TERMINAL REGION OF THE INSULIN RECEPTOR α-CHAIN AND OF THE INSULIN-LIKE GROWTH FACTOR RECEPTOR α-

CHAIN

Field of the Invention

The present invention relates generally to structural studies of the insulin binding site of the insulin receptor (IR) and the insulin-like growth factor 1 receptor (IGF-IR). More particularly, the present invention relates to the crystal structure of the low affinity insulin binding site of the IR ectodomain comprising the C-terminal region of the IR α- chain, as well as the corresponding region of IGF-IR, and to methods of using the crystal and related structural information to screen for and design compounds that interact with or modulate the function of IR and/or IGF-IR.

Background to the Invention

The insulin receptor (IR) and its homologue the type 1 insulin-like growth factor 1 receptor (IGF-IR), are closely related members of the tyrosine kinase receptor family and are large, transmembrane, glycoprotein dimers consisting of several structural domains.

The key role of the insulin receptor (IR) is in glucose uptake and metabolism by muscle and fat. Mouse knockout studies have also shown IR to be important in adipogenesis, neovascularization, the regulation of hepatic glucose synthesis and glucose- induced pancreatic insulin secretion (Kitamura et al , 2003). IR signalling is also important in the brain, being involved in the regulation of food intake, peripheral fat deposition and the reproductive endocrine axis as well as in learning and memory (Wada et al, 2005). Dysfunctional IR signalling has been implicated in diseases including type I and type II diabetes, dementia and cancer.

IR exists as two splice variant isoforms, IR-A and IR-B, which respectively lack or contain the 12 amino acids coded by exon 11. The longer variant, IR-B, is the isoform responsible for signalling metabolic responses. In contrast, IR-A signals predominantly mitogenic responses, is the preferentially expressed isoform in several cancers (Denley et al, 2003) and is capable of binding insulin-like growth factor 2 (IGF-II) with high affinity (Denley et al, 2004).

The sequence of IR is highly homologous to the sequence of IGF-IR, indicating that the three-dimensional structures of both receptors are most likely closely similar. The mature human IR and IGF-IR molecules are each homodimers comprising two α-chains and two β-chains, the α- and β-chains arising from the post-translational cleavage at the furin cleavage site at residues 720-723 (IR-A numbering with the mature N-terminal residue numbered 1) or 707-710 (IGF-IR). The structural organization of IR'and IGF-IR has been reviewed extensively (Adams et al, 2000; De Meyts and Whittaker, 2002; Ward et al, 2003; Lawrence et al, 2007; Ward and Lawrence, 2009). The sequence relationship and domain organization of these receptors are presented in Figure 1.

The extracellular part of each IR or IGF-IR monomer contains (sequentially from N- to C-terminus) a leucine-rich repeat domain (Ll), a cysteine-rich region (CR) and a second leucine-rich repeat domain (L2), followed by three fibronectin type III domains, (FnIII-I, -2 and -3). The FnIII-2 domain contains a large insert domain (ID) of approximately 120 residues, -within which lies the α-β cleavage site. Intracellular^, each monomer contains a tyrosine kinase catalytic domain flanked by two regulatory regions that contain the phosphotyrosine binding sites for signalling molecules. Each α-chain is linked to its partner β-chain via a disulphide bond between residues Cys647 and Cys860 (Sparrow et al, 1997) in the case of IR and/or Cys633-Cys849 in the case of IGF-IR. The α-chains of both IR and IGF-IR are cross-linked by disulphide bonds in two places. The first is at Cys524 (IR) or Cys514 (IGF-IR) in the FnIII-I domain, cross-linked to its counterpart in the opposite monomer, and the second involves one or more of the residues Cys682, Cys683 and Cys685 (IR) or Cys669, Cys670 and Cys672 (IGF-IR) in the insert region of each FnIII-2 domain, cross-linked to their counterparts in the opposite monomer (Sparrow et al, 1997).

The domains of IR and IGF-IR exhibit high (47-67%) amino acid sequence identity indicative of high conservation of three-dimensional structure. The crystal structure of the first three domains of IGF-IR (L1-CR-L2) has been determined (Garrett et al, 1998) and revealed that the L domains consist of a single-stranded right-handed β-helix (a helical arrangement of β-strands), while the cysteine-rich region is composed of eight related disulfide-bonded modules. The crystal structure of the first three domains of IR (Ll-CR- L2) has also been determined (WO 07/147213, Lou et al, 2006) and as anticipated is closely similar to that of its IGF-IR counterpart. Other evidence for the close structural similarity of IR and IGF-IR arises from : (i) electron microscopic analyses (Tulloch et al, 1999), (ii) the fact that hybrid receptors (heterodimers of one IR monomer disulphide- bonded to one of IGF-IR monomer) exist naturally and are commonly found in tissues expressing both receptors (Bailyes et al, 1997), and (iii) the fact that receptor chimeras can be constructed which have whole domains or smaller segments of polypeptide from one receptor replaced by the corresponding domain or sequence from the other (reviewed in Adams et al, 2000).

The current model for insulin binding proposes that, in the basal state, the IR homodimer contains two identical pairs of binding sites (referred to as Site 1 and Site 2) on each monomer (De Meyts and Whittaker, 2002; Schaffer, 1994; De Meyts, 1994; De Meyts, 2004; Kiselyov et al, 2009). Binding of insulin to a low affinity site (Site 1) on one α-subunit is followed by a second binding event between the bound insulin and a different region of the second IR α-subunit (Site 2). This ligand-mediated bridging between the two α-subunits generates the high affinity state that results in signal transduction. In contrast, soluble IR ectodomain, which is not tethered at its C-terminus, cannot generate the high affinity receptor-ligand complex. The soluble IR ectodomain can bind two molecules of insulin simultaneously at its two Site Is, but only with low affinity (Adams et al, 2000). The model for IGF-I or IGF-II binding to IGF-IR is the same as that just described for insulin binding to IR and involves IGF-I (or IGF-II) binding to an initial low affinity site (Site 1) and subsequent cross-linking to a second site (Site 2) on the opposite monomer to form the high affinity state, as described for the IR. However, the values of the kinetic parameters describing these events are somewhat different in the two systems (Surinya et al, 2008; Kiselyov et al, 2009).

While similar in structure, IGF-IR and IR serve different physiological functions. ' IGF-IR is expressed in almost all normal adult tissue except for liver, which is itself the major site of IGF-I production (Buttel et al, 1999). A variety of signalling pathways are activated following binding of IGF-I or IGF-II to IGF-IR, including Src and Ras, as well as downstream pathways, such as the MAP kinase cascade and the P13K/AKT axis (Chow et al, 1998). IR is primarily involved in metabolic functions whereas IGF-IR mediates growth and differentiation. Consistent with this, ablation of IGF-I (i.e. in IGF-I knock-out mice) results in embryonic growth deficiency, impaired postnatal growth, and infertility. In addition, IGF-IR knock-out mice were only 45% of normal size and died of respiratory failure at birth (Liu et al, 1993). However, both insulin and IGF-I can induce both mitogenic and metabolic effects.

Various non-cry stallographic 3-D structural analyses of the IR and the interaction of insulin with the IR have been undertaken using electron microscopic techniques (Luo et al, 1999; Ottensmeyer et al, 2000, 2001; Yip and Ottensmeyer, 2001). However, due to the low resolution information obtained (>20 angstrom), the conclusions of these studies have been questioned (De Meyts and Whittaker, 2002).

Crystal structures of the ectodomain of IR have been presented previously (WO 07/147213, McKern et al, 2006; Lou et al, 2006) and have elucidated some potential ligand/IR interactions, in particular part of the low affinity site on the surface of IR Ll . However, an area of ambiguous electron density on the surface of the IR Ll domain could not be resolved (WO 07/147213, McKern et al, 2006). Accordingly, there is a need in the art to more fully resolve the structures of both IR and IGF-IR in order to elucidate all potential ligand/receptor interactions. This information would provide a more complete understanding of the mechanisms of action of both IR and IGF-IR necessary for the development of IR and IGF-IR agonists/antagonists. i

Summary of the Invention

The present inventors have determined the crystal structure of the low affinity insulin binding site of human IR. In particular, the crystal structure of the low affinity insulin binding site of human IR ectodomain comprising the C-terminal region of the insulin receptor α-chain has been determined. This structure allows visualisation, for the first time, of the intact low affinity insulin receptor binding site region controlling the initial binding of insulin and the subsequent formation of the high affinity insulin-IR complex that leads to signal transduction. The structure shows, for the first time, the way in which the C-terminal region of the insulin receptor α-chain associates with the first leucine-rich repeat (Ll) domain of the receptor to form the complete low affinity insulin binding site. The structure also provides direct insight, for the first time, into the way the so-called Site 1 insulin mimetic peptides bind to the low affinity binding site of the insulin receptor and also provides a basis for designing insulin mimetic peptides that interact with the low affinity insulin binding site of IR. The structural information presented also indicates, by analogy, the corresponding regions in the closely related IGF-IR that are involved in insulin growth factor (IGF) binding.

The identification of molecular structures having a high degree of specificity for only one of IR or IGF-IR is important in the development of efficacious and safe therapeutics. For example, a molecule developed as an insulin agonist should have little or no IGF-I activity in order to avoid the mitogenic activity of IGF-I and a potential for facilitating neoplastic growth. The determination of which regions of IR and IGF-IR have sufficient differences to confer selectivity for their respective ligands or for therapeutic molecules such as chemical entities or biological reagents is therefore an important and significant advancement. Similarly, it is believed that the ability to be able to identify molecular structures that mimic the active binding regions of insulin and/or IGF-I and which impart selective agonist or antagonist activity will also aid and advance the development of new drugs.

To assist in the design of agonists/antagonists of IR and/or IGF-IR, the present inventors have used the structure of human IR ectodomain comprising the C-terminal region of the insulin receptor α-chain (Appendix I) to place a model of the C-terminal region of the insulin receptor α-chain in the 3D structure of IGF-IR ectodomain (Appendix II). The present inventors have also used these models to place a model of the C-terminal region of the IGF-IR α-chain in the 3D structure of IR ectodomain and IGF-IR ectodomain (Appendixes III and IV, respectively). The present inventors used all of these structures to place a model of an insulin mimetic peptide (S519C16) in the binding site of IR and IGF-IR (Appendixes V and VI, respectively). The models, with coordinates in Appendixes II to VI, are oriented relative to atomic coordinates found in Appendix I and may be used in conjunction with atomic coordinates of Appendix I to design a compound which binds to the insulin binding site of IR and/or a compound which binds to the IGF binding site of IGF- IR.

With regards to defining structures by combining subsets of coordinates from Appendix I to Appendix VI, such combinations may be achieved by methods such as assembling combinations of complete domains from each set, assembling combinations of complete domains from each set wherein the coordinates and corresponding amino acid sequence from one structure are transposed onto those -of the other, refining less resolved regions of one crystal using the corresponding coordinates of the other.

Accordingly, the present invention provides a method of identifying, designing or screening for a compound that can potentially interact with insulin receptor (IR) and/or insulin-like growth factor- 1 receptor (IGF-IR), comprising performing structure-based identification, design or screening of a compound based on the compound's interactions with a structure defined by the atomic coordinates of one or more of Appendixes I to VI, or a subset of atomic coordinates of one or more thereof at least representing the C- terminal region of the α-chain of IR, the C-terminal region of the α-chain of IGF-IR, or a mimetic of the C-terminal region of the α-chain of IR and/or IGF-IR.

In one embodiment, the method comprises identifying, designing or screening for a compound which interacts with the three-dimensional structure of; (i) the low affinity insulin binding site of IR, the structure being defined by the atomic coordinates shown in one or more of Appendixes I, III and V, and/or (ii) the low affinity insulin-like growth factor (IGF) binding site of IGF-IR, the structure being defined by the atomic coordinates shown in one or more of Appendixes II, IV and VI, wherein interaction of the compound with the structure is favoured energetically.

In another embodiment, the method further comprises synthesising or obtaining an identified or designed candidate compound and determining the ability of the candidate compound to interact with IR and/or IGF-IR.

In a further embodiment, the atomic coordinates define one or more regions of the low affinity binding site of IR for insulin, and/or the low affinity binding site of IGF-IR for IGF, comprising the C-terminal region of the α-chain of IR, the C-terminal region of the α-chain of IGF-IR, or a mimetic of the C-terminal region of the α-chain of IR and/or IGF-IR. In a particularly preferred embodiment, the C-terminal region of the α-chain of IR comprises amino acids 693 to 710 of IR α-chain (SEQ ID NO: 13).

In another preferred embodiment, the atomic coordinates defining the low affinity insulin binding site of IR further comprise the leucine-rich repeat 1 (L 1 ) domain and/or the cysteine-rich (CR) domain of the IR ectodomain.

In yet another preferred embodiment, the atomic coordinates define portions of the molecular surface of the central β-sheet of the Ll domain and portions of the molecular surface of the second leucine-rich repeat (LRR) which contain Phe39 and/or the loop in the fourth LRR rung of the Ll domain.

In yet another preferred embodiment, the atomic coordinates define module 6 of the CR domain of IR.

In another embodiment, the atomic coordinates further define one or more amino acid sequences selected from IR amino acid residues 1-156, 157-310, 594 and 794.

In a preferred embodiment, the one or more amino acids selected from IR amino acid residues 1-156 comprise at least one amino acid selected from Argl4, Asnl5, Gln34, Leu36, Leu37, Phe39, Pro43, Phe46, Leu62, Phe64, Leu87, Phe88, Phe89, Asn90, Phe96, Glu97, Argl l8, Glul20 and Hisl44. .

In another embodiment, the one or more amino acids selected from IR amino acid residues 157-310 comprise at least one of the amino acid sequences selected from 192- 310, 227-303 and 259-284.

The crystal structure of the first three domains of the ectodomain of IGF-IR has been previously reported (WO 99/028347). The crystal structure of the first three domains of the ectodomain of IR was subsequently reported (WO 07/147213), enabling, for the first time, direct comparison of the regions controlling ligand specificity in the closely related IGF-IR and IR. However, the structure of the intact low affinity insulin binding site (i.e. inclusive of the C-terminal region of the receptor α-chain) could not be elucidated. As will be evident to the skilled person, the findings presented here on the , intact insulin binding site of IR ectodomain structure, shape and orientation can be transposed onto the IGF binding site of IGF-IR ectodomain structure, shape and orientation.

The present invention has enabled the identification of previously unrecognised regions of the insulin binding site of IR ectodomain. By analogy, the present invention also identifies the equivalent regions in the IGF-IR, given the structural organisation of domains in the two receptors is effectively the same. The present invention has identified the critical regions of IR involved in the binding of insulin and in mediating the subsequent formation of the high affinity insulin-IR complex that leads to signal transduction. Once again, it will be evident to the skilled person that these findings can be transposed onto IGF-IR.

The present invention is therefore also useful in the identification and/or -design of compounds which bind to the low affinity IGF binding site of IGF-IR.

In one embodiment, the atomic coordinates defining one or more regions of the low affinity binding site of IGF-IR for IGF, comprise the C-terminal region of the α-chain of IGF-IR. In a preferred embodiment, the C-terminal region of the α-chain of IGF-IR comprises amino acids 681 to 697 of IGF-IR α-chain (SEQ ID NO: 15).

In another embodiment, the atomic coordinates defining the low affinity IGF binding site of IGF-IR further comprise the Ll domain and/or the CR domain of IGF-IR ectodomain.

In a preferred embodiment, the atomic coordinates define the central β-sheet of the Ll domain, and/or that part of the second LRR containing Ser35, and/or the loop in the fourth LRR rung of the Ll domain.

In another preferred embodiment, the atomic coordinates define module 6 of the CR domain of IGF- IR.

In one embodiment, the mimetic of the C-terminal region of the α-chain of IR and/or IGF-IR is S519C16 (SEQ ID NO: 18).

In further embodiment, the compound substitutes for the C-terminal region of the α-chain of IR and/or the C-terminal region of the α-chain of IGF-IR in the formation of the low affinity binding site of IR or IGF-IR. Such compounds may act as either agonists or antagonists of these receptors. In one alternative of this embodiment, insulin and/or IGF-IR binds the low affinity binding site of IR and/or IGF-IR in the presence of the compound. In another alternative of this embodiment, insulin and/or IGF-IR does not bind, or has reduced binding to, the low affinity binding site of IR and/or IGF-IR in the presence of the compound.

In another embodiment, a candidate compound for interacting with IR and/or IGF- IR is chemically modified as a result of structure-based evaluation.

In a further embodiment, the chemical modification is designed to either: i) reduce the potential for the candidate compound to bind to IR whilst maintaining binding to IGF-IR; or ii) reduce the potential for the candidate compound to bind to IGF-IR, whilst maintaining binding to IR.

Candidate compounds and compounds identified or designed using a method of the present invention may be any suitable compound, including naturally occurring compounds, de novo designed compounds, library generated compounds (chemically or recombinantly generated), mimetics etc., and include organic compounds, new chemical entities, antibodies, binding proteins other than antibody-based molecules (nonimmunoglobulin proteins) including, for example, protein scaffolds such as lipocalins, designed ankyrin repeat proteins (DARPins, Stumpp et al., 2007) and protein A domains (reviewed in Binz et al, 2005), avimers (Silverman et al., 2005), and other new biological entities such as nucleic acid aptamers (reviewed in Ulrich, 2006).

The present invention is also useful for improving the properties of known ligands for the low affinity binding sites of IR and/or IGF-IR. For example, existing IR or IGF- IR low affinity binding site ligands can be screened against the 3D structure of the insulin binding site of IR ectodomain or a region of the insulin binding site of IR ectodomain defined by the atomic coordinates of Appendix I or a portion thereof (optionally utilising the atomic coordinates given in Appendixes II to VI to further refine the screen and/or the assessment of the potential to energetically interact with IR), and an assessment made of the potential to energetically interact with the insulin binding site of IR.

Thus, the present invention also provides a method for, redesigning a compound which is known to bind to IR and/or IGF-IR comprising performing structure-based evaluation of the compound based on the compound's interactions with a structure defined by the atomic coordinates of one or more of Appendixes I to VI, or a subset of atomic coordinates of one or more thereof at least representing the C-terminal region of the α- chain of IR, the C-terminal region of the α-chain of IGF-IR, or a mimetic of the C- terminal region of the α-chain of IR and/or IGF-IR, and redesigning or chemically modifying the compound as a result of the evaluation.

In one embodiment, the compound which is known to bind to IR and/or IGF-IR is redesigned or chemically modified to (i) improve affinity for binding to IR, and/or (ii) lower affinity for binding to IGF-IR.

In another embodiment, the compound which is known to bind to IR and/or IGF- IR is redesigned or chemically modified to (i) improve affinity for binding to IGF-IR, and/or (ii) lower affinity for binding to IR.

When screening potential ligands or compounds for selectivity for binding to the insulin binding site of IR or IGF-IR, it will be important to concentrate on those areas of difference in the 3D structure between the low affinity binding site of ectodomains of IR and IGF-IR. Such areas are identified and described herein. In particular, it will be important to concentrate on those areas of difference which are identified as being potentially important in the binding of insulin to the receptors.

Accordingly, in a further embodiment the compound is redesigned or modified so as to lower the affinity to IR or IGF-IR by virtue of the structural differences between IR and IGF-IR at or in the vicinity of the C-terminal region of the. α-chain of IR and the C- terminal region of the α-chain of IGF-IR.

The present invention also provides a computer system for identifying one or more compounds that can potentially interact with IR and/or IGF-IR, the system containing data representing the structure of: (i) the low affinity insulin binding site of IR, the structure being defined by the atomic coordinates shown in one or more of Appendixes I, III and V; (ii) the low affinity IGF binding site of IGF-IR, the structure being defined by the atomic coordinates shown in one or more of Appendixes II, IV and VI; and/or (iii) the C-terminal region of the . α-chain of IR, the C-terminal region of the α-chain of IGF-IR, or a mimetic of the C-terminal region of the α-chain of IR and/or IGF- 1 R, the structure being defined by a subset of atomic coordinates shown in one or more of Appendixes I to VI.

In another aspect, the present invention provides a computer-readable medium having recorded thereon data representing a model and/or the atomic coordinates as shown in one or more of Appendixes I to VI, or a subset of atomic coordinates of one or more thereof at least representing: i) the C-terminal region of the α-chain of IR; ii) the C-terminal region of the α-chain of IGF- 1 R; and/or iii) a mimetic of the C-terminal region of the α-chain of IR and/or IGF-IR, as any one of i) to iii) associates with IR and/or IGF-IR.

Also provided are a set of coordinates as shown in one or more of Appendixes I to VI, or a subset of atomic coordinates of one or more thereof at least representing: i) the C-terminal region of the α-chain of IR; ii) the C-terminal region of the α-chain of IGF-IR; and/or iii) a mimetic of the C-terminal region of the α-chain of IR and/or IGF-IR, as any one of i) to iii) associates with IR and/or IGF-IR.

The three-dimensional structure of the C-terminal region of the IR and/or IGF-IR α-chain may be used to develop models useful for drug design and/or in silico screening of candidate compounds that interact with and/or modulate IR and/or IGF-IR. Other physicochemical characteristics may also be used in developing the model, e.g. bonding, electrostatics, etc.

Generally the term "in silico" refers to the creation in a computer memory, i.e., on a silicon or other like chip. Stated otherwise "in silico" means "virtual". When used herein the term "in silico" is intended to refer to screening methods based on the use of computer models rather than in vitro or in vivo experiments.

Accordingly, the present invention also provides a computer-assisted method of identifying a compound that potentially interacts with IR and/or IGF-IR, which method comprises fitting the structure of: (i) the low affinity insulin binding site of IR, the structure being defined by the atomic coordinates shown in one or more of Appendixes I, III and V; (ii) the low affinity IGF binding site of IGF-IR, the structure being defined by the atomic coordinates shown in one or more of Appendixes H, IV and VI; and/or (iii) the C-terminal region of the α-chain of IR, the C-terminal region of the α-chain of IGF-IR, or a mimetic of the C-terminal region of the α-chain of IR and/or IGF-IR, the structure being defined by a subset of atomic coordinates shown in one or more of Appendixes I to VI, to the structure of a candidate compound.

Also provided by the present invention is a computer-assisted method for identifying a compound able to interact with IR and/or IGF-IR using a programmed computer comprising a processor, which method comprises the steps of: (a) generating, using computer methods, a set of atomic coordinates of a structure that possesses energetically favourable interactions with the atomic coordinates of: (i) the low affinity insulin binding site of IR, the structure being defined by the atomic coordinates shown in one or more of Appendixes I, III and V; (ii) the low affinity IGF binding site of IGF-IR, the structure being defined by the atomic coordinates shown in one or more of Appendixes II, IV and VI; and/or (iii) the C-terminal region of the α-chain of IR, the C-terminal region of the α-chain of IGF-IR, or a mimetic of the C-terminal region of the α-chain of IR and/or IGF-IR, the structure being defined by a subset of atomic coordinates shown in one or more of Appendixes I to VI, which coordinates are entered into the computer thereby generating a criteria data set; (b) comparing, using the processor, the criteria data set to a computer database of chemical structures; (c) selecting from the database, using computer methods, chemical structures which are complementary or similar to a region of the criteria data set; and optionally, (d) outputting, to an output device, the selected chemical structures which are complementary to or similar to a region of the criteria data set.

The present invention further provides a computer-assisted method for identifying potential mimetics of IR and/or IGF-IR using a programmed computer comprising a processor, the method comprising the steps of: (a) generating a criteria data set from a set of atomic coordinates of: (i) the low affinity insulin binding site of IR, the structure being defined by the atomic coordinates shown in one or more of Appendixes I, III and V; (ii) the low affinity IGF binding site of IGF-IR, the structure being defined by the atomic coordinates shown in one or more of Appendixes II, IV and VI; and/or (iii) the C-terminal region of the α-chain of IR, the C-terminal region of the α-chain of IGF-IR, or a mimetic of the C-terminal region of the α-chain of IR and/or IGF-IR, the structure being defined by a subset of atomic coordinates shown in one or more of Appendixes I to VI, which coordinates are entered into the computer; (b) (i) comparing, using the processor, the criteria data set to a computer database of chemical structures stored in a computer data storage system and selecting from the database, using computer methods, chemical structures having a region that is structurally similar to the criteria data set; or (ii) constructing, using computer methods, a model of a chemical structure having a region that is structurally similar to the criteria data set; and, optionally, (c) outputting to an output device: (i) the selected chemical structures from step (b)(i) having a region similar to the criteria data set; or (ii) the constructed model from step (b)(ii).

The present invention further provides a method for evaluating the ability of a compound to interact with IR and/or IGF-IR, the method comprising the steps of: (a) employing computational means to perform a fitting operation between the compound and the binding surface of a computer model of the low affinity binding site for insulin on IR ectodomain, and/or the low affinity binding site for IGF on IGF-IR ectodomain, using atomic coordinates wherein the root mean square deviation between the atomic coordinates and a subset of atomic coordinates of one or more of Appendixes I to VI or a subset of atomic coordinates of one or more thereof at least representing the C-terminal region of the α-chain of IR, the C-terminal region of the α-chain of IGF-IR, or a mimetic of the C-terminal region of the α-chain of IR and/or IGF-IR, is not more than 1.5 A; and (b) analysing the results of the fitting operation to quantify the association between the compound and the binding surface model.

The present invention also provides a method of using molecular replacement to obtain structural information about a molecule or a molecular complex of unknown structure, comprising the steps of: (i) generating an X-ray diffraction pattern of the crystallized molecule or molecular complex; and (ii) applying the atomic coordinates of one or more of Appendixes I to VI, or a subset of atomic coordinates of one or more thereof at least representing the C-terminal region of the α-chain of IR, the C-terminal region of the α-chain of IGF-IR, or a mimetic of the C-terminal region of the α-chain of IR and/or IGF-IR, to the X-ray diffraction pattern to generate a three-dimensional electron density map of at least a region of the molecule or molecular complex whose structure is unknown.

The present invention provides a compound that binds to IR and/or IGF-IR ectodomain designed, redesigned or modified using the methods of the invention. Preferably, such compounds have an affinity (Kj) for IR and/or IGF-IR of less than 10 ~5 M. In a particularly preferred embodiment, the compound binds to the low affinity binding site of IR and/or to the low affinity binding site of IGF- 1 R.

The present invention also provides an isolated peptide or mimetic thereof which binds the Ll domain of IR and/or the Ll domain of IGF-IR, the peptide comprising: (i) an amino acid sequence as provided in SEQ ID NO: 13 or SEQ ID NO: 15; (ii) an amino acid sequence which is at least 50% identical, more preferably at least 80% identical, more preferably at least 90% identical, more preferably at least 95% identical, to SEQ ID NO: 13 and/or SEQ ID NO: 15; or (iii) a fragment of i) or ii) which binds the Ll domain of IR and/or the Ll domain of IGF-IR, wherein the peptide has a helical structure.

Further provided is an isolated polynucleotide encoding the isolated peptide or mimetic thereof, as well as a vector comprising said polynucleotide and a host cell comprising said vector.

The present invention also provides a composition comprising a compound of the invention, a peptide or mimetic of the invention, and/or a polynucleotide of the invention, and optionally an acceptable carrier or diluent, more preferably a pharmaceutically acceptable carrier or diluent.

The present invention further provides a method for preventing or treating a disease associated with aberrant IR and/or IGF-IR functioning and/or signalling, the method comprising administering to a subject in need thereof a compound of the invention, a peptide or mimetic of the invention, and/or a polynucleotide of the invention.

Also provided by the present invention is use of a compound of the invention, a peptide or mimetic of the invention, and/or a polynucleotide of the invention, for the manufacture of a medicament for treating a disease in a subject associated with aberrant IR and/or IGF-IR functioning and/or signalling.

Examples of diseases associated with aberrant IR and/or IGF-IR functioning and/or signalling include, but are not limited to, obesity, type I and type II diabetes, cardiovascular disease, osteoporosis, dementia and cancer.

It is also intended that embodiments of the present invention include manufacturing steps such as incorporating the compound, such as a peptide, into a pharmaceutical composition in the manufacture of a medicament.

Throughout this specification, preferred aspects and embodiments apply, as appropriate, separately, or in combination, to other aspects and embodiments, mutatis mutandis, whether or not explicitly stated as such.

The present invention will now be described further with reference to the following examples, which are illustrative only and non-limiting.

Brief Description of the Figures

Some figures contain colour representations or entities. Coloured versions of the figures are available from the Patentee upon request or from an appropriate patent Office. A fee may be imposed if obtained from a Patent Office. Figure 1: Shows the sequence alignment of the ectodomains of human insulin receptor (IR, exon 1 1-isoform) and human IGFl receptor (IGF-IR). Residues conserved between the sequences are indicated by vertical bars and potential N-linked glycosylation sites are indicated by shading. Disulphide links are indicated by square braces above the alignment. Sequence sources were: IR (Ullrich et al., 1985), human type 1 IGF receptor (Ullrich et al., 1986).

Figure 2. ITC curves for the titration of (a) IR classical αCT peptide against IR485, (b) IGF-IR classical αCT peptide against IR485, and (c) IR classical αCT.714A peptide against IR485.

Figure 3. ITC curves for the titration of (a) ZFP-insulin against IR485 pre-complexed with a 10-fold molar ratio of IR classical αCT peptide, (b) ZFP-insulin against IR485 pre- complexed with a 10- fold molar ratio of IGF-IR classical αCT peptide, (c) IGF-IR against IR485 pre-complexed with a 10-fold molar ratio of IR classical αCT peptide, and (d) IGF- IR against IR485 pre-complexed with a 10-fold molar ratio of IGF-IR classical αCT peptide.

Figure 4. ITC curves for the titration of (a) S519C16 against IR485, (b) S519C16 against IR485 pre-complexed with a 10-fold molar ratio of IR classical αCT peptide, (c) S519N20 against IR485, and (d) S519 against IR485.

Figure 5. Dynamic light scattering volume distribution curves obtained from samples of (a) IR485 at 6 mg/ml, (b) IR485 at 0.5 mg/ml, (c) IR485 at 6 mg/ml plus a 3-fold molar ratio of IR αCT peptide, (d) IR485 at 6 mg/ml plus a 3-fold molar ratio of IR classical αCT peptide and a 2-fold molar ratio of ZFP-insulin.

Figure 6. The crystal structure of IR ectodomain comprising the C-terminal region of the α- chain of IR. (a) Negative B-factor enhanced (F 0 -F c ) electron density overlaid with the final model of IR residues 693-710; (b) Detail of the interaction between IR residues 693-710 (yellow backbone, green carbons, non-bold numbering) and the surface of Ll-β2 (pink backbones, cyan carbons, bold numbering); (c) Sequence alignment of the C-terminal regions of the α-chains of IR and IGF-IR and the S519C16 peptide (Menting et al., 2009). Shaded regions show conservation between the three sequences and boxed regions show segments predicted to be helical in conformation (Menting et al., 2009). Figure 7. Model structure of the C-terminal region of IR α-chain bound to the Ll domain of IGF-IR (Appendix II) generated from the crystal structure of IRectodomain inclusive of residues 693-710. The backbone of the respective Ll domain is shown as an orange coil, the side chains of residues within the Ll domain that interact with the respective bound peptide are shown with green carbon atoms, red oxygen atoms and blue nitrogen atoms, and the backbone of the bound peptide helix is shown as a blue coiL Selected peptide residues that interact with the Ll domain are shown with cyan carbon atoms, red oxygen atoms and blue nitrogen atoms. The remaining peptide residues, which have more limited or no interaction with the Ll domain are represented only by their α-carbon atoms shown as spheres embedded in the peptide coil, with other atoms within these residues omitted for clarity. Residues that lie in the C-terminal region of IR α-chain are underlined for clarity.

Figure 8. Model structure of the C-terminal region of IGF-IR α-chain bound to the Ll domain of IR (Appendix III). Colouring and style is as described above for Figure 7.

Figure 9. Model structure of the C-terminal region of IGF-IR α-chain bound to the Ll domain of IGF-IR (Appendix IV). Colouring and style is as described above for Figure 7.

Figure 10. Model structure of the S519C16 peptide bound to the Ll domain of IR (Appendix V). Colouring and style is as described above for Figure 7.

Figure 11. Model structure of the S519C16 peptide bound to the Ll domain of IGF-IR (Appendix VI). Colouring and style is as described above for Figure 7.

Figure 12. Sample isothermal titration calorimetry curves obtained for the titration against insulin mini-receptor IR485 of N-terminally biotinylated αCT peptide 698-719 containing the following respective mutations: (A) wild type, (B) T704Y, (C) R702W, (D) R702Y, (E) T704W and (F) R702Y / T704W.

Key to the Sequence Listing

SEQ ID NO: 1 - Amino acid sequence of mature human insulin receptor ectodomain

(isoform A).

SEQ ID NO: 2 - Amino acid sequence of mature human insulin receptor ectodomain

(isoform B).

SEQ ID NO: 3 - Amino acid sequence of mouse insulin receptor. SEQ ID NO: 4 - Amino acid sequence of rhesus monkey insulin receptor, predicted.

SEQ ID NO: 5 - Amino acid sequence of bovine insulin receptor, predicted.

SEQ ID NO: 6 - Amino acid sequence of mature human insulin-like growth factor receptor 1 (IGF-IR) ectodomain.

SEQ ID NO: 7 - Amino acid sequence of mouse insulin-like growth factor receptor 1

(IGF-IR).

SEQ ID NO: 8 - Amino acid sequence of rhesus monkey insulin-like growth factor receptor 1 (IGF-IR), predicted.

SEQ ID NO: 9 - Amino acid sequence of bovine insulin-like growth factor receptor 1

(IGF-IR), predicted.

SEQ ID NO: 10 - Amino acid sequence of IR485.

SEQ ID NO: 11 - Amino acid sequence of the classical α-chain C-terminal peptide (αCT) of human IR.

SEQ ID NO: 12 - Amino acid sequence of the F714A mutant of the classical α-chain C- terminal peptide ('αCT') of human IR.

SEQ ID NO: 13 - Amino acid sequence of the C-terminal region of the α-chain of human

IR.

SEQ ID NO: 14 - Amino acid sequence of the classical α-chain C-terminal peptide (αCT) of human IGF-IR.

SEQ ID NO: 15 - Amino acid sequence of the C-terminal region of the α-chain of human

IGF-IR.

SEQ ID NO: 16 - Amino acid sequence of the S519 peptide.

SEQ ID NO: 17 - Amino acid sequence of the S519N20 peptide.

SEQ ID NO: 18 - Amino acid sequence of the S519C16 peptide.

SEQ ID NO: 19 - FYXWF motif.

Detailed Description of the Invention

Unless defined otherwise, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art (e.g. in molecular biology, biochemistry, structural biology, and computational biology). Standard techniques are used for molecular and biochemical methods (see generally, Sambrook et al., 2001, and Ausubel et al., 1999, which are incorporated herein by reference) and chemical methods.

Throughout this specification the word "comprise", or variations such as "comprises" or "comprising", will be understood to imply the inclusion of a stated element, integer or step, or group of elements, integers or steps, but not the exclusion of any other element, integer or step, or group of elements, integers or steps.

IR ectodomain crystals and crystal structure

The present invention provides a crystal comprising a C-terminal region of the IR α-chain based on the IRΔβ construct (see Examples).

As used herein, the term "crystal" means a structure (such as a three dimensional (3D) solid aggregate) in which the plane faces intersect at definite angles and in which there is a regular structure (such as internal structure) of the constituent chemical species. The term "crystal" refers in particular to a solid physical crystal form such as an experimentally prepared crystal.

• Crystals according to the invention may be prepared using any IR ectodomain, i.e. the IR polypeptide containing the extracellular domain and lacking the transmembrane domain and the intracellular tyrosine kinase domain. Typically, the extracellular domain comprises residues 1 to 917 (mature receptor numbering) of human IR, or the equivalent thereof together with any post-translational modifications of these residues such as N- or O-linked glycosylation.

In a preferred embodiment the IR polypeptide is human IR (SEQ ID NOs: 1 and 2). However, the IR polypeptide may also be obtained from other species, such as other mammalian, vertebrate or invertebrate species. Examples of IR polypeptides from other species are given in SEQ ID NOs: 3 to 5.

Crystals may be constructed with wild-type IR polypeptide ectodomain sequences or variants thereof, including allelic variants and naturally occurring mutations as well as genetically engineered variants. Typically, variants have at least 95 or 98% sequence identity with a corresponding wild-type IR ectodomain polypeptide.

Optionally, the crystal of IR ectodomain may comprise one or more molecules which bind to the ectodomain, or otherwise soaked into the crystal or cocrystallised with IR ectodomain. Such molecules include ligands or small molecules, which may be candidate pharmaceutical agents intended to modulate the interaction between IR and its biological targets. The crystal of IR ectodomain may also be a molecular complex with other receptors of the IGF receptor family such as IGF-IR. The complex may also . comprise additional molecules such as the ligands to these receptors.

The production of IR ectodomain crystals is described below. In a preferred embodiment, an IR ectodomain crystal of the invention comprising the C-terminal segment of the IR α-chain has the atomic coordinates set forth in Appendix I. As used herein, the term "atomic coordinates" or "set of coordinates" refers to a set of values which define the position of one or more atoms with reference to a system of axes. It will be understood by those skilled in the art that atomic coordinates may be varied, without affecting significantly the accuracy of models derived therefrom. Thus, although the invention provides a very precise definition of a preferred atomic structure, it will be understood that minor variations are envisaged and the claims are intended to encompass such variations.

It will be understood that any reference herein to the atomic coordinates or subset of the atomic coordinates shown in Appendix I shall include, unless specified otherwise, atomic coordinates having a root mean square deviation of backbone atoms of not more than 1.5 A, preferably not more than 1 A, when superimposed on the corresponding backbone atoms described by the atomic coordinates shown in Appendix I. Also, any reference to the atomic coordinates or subset of the atomic coordinates shown in Appendixes II to VI shall include, unless specified otherwise, atomic coordinates having a root mean square deviation of backbone atoms of not more than 2.5 A when superimposed on the corresponding backbone atoms described by the atomic coordinates shown in Appendixes II to VI.

The following defines what is intended by the term "root mean square deviation (RMSD)" between two data sets. For each element in the first data set, its deviation from the corresponding item in the second data set is computed. The squared deviation is the square of that deviation, and the mean squared deviation is the mean of all these squared deviations. The root mean square deviation is the square root of the mean squared deviation.

Preferred variants are those in which the RMSD of the x, y and z coordinates for all backbone atoms other than hydrogen is less than 1.5 A (preferably less than 1 A, 0.7 A or less than 0.3 A) compared with the coordinates given in Appendix I. It will be readily appreciated by those skilled in the art that a 3D rigid body rotation and/or translation of the atomic coordinates does not alter the structure of the molecule concerned.

In a highly preferred embodiment, the crystal has the atomic coordinates as shown in Appendix I.

The present invention also provides a crystal structure of the low affinity insulin binding site of IR ectodomain polypeptide comprising the C-terminal region of the IR α- chain, or a region thereof. The atomic coordinates obtained experimentally for amino acids 4 to 655, 693 to 710 (the "C-terminal region of the IR α-chain"), and 755 to 909 of human IR-A (mature receptor numbering; SEQ ID NO: 1) are shown in Appendix I. However, a person skilled in the art will appreciate that a set of atomic coordinates determined by X-ray crystallography is not without standard error. Accordingly, any set of structure coordinates for an IR ectodomain polypeptide comprising the C-terminal region of the IR α-chain that has a root mean square deviation of protein backbone atoms of less than 0.75 A when superimposed (using backbone atoms) on the atomic coordinates listed in Appendix I shall be considered identical.

The present invention also comprises the atomic coordinates of the C-terminal region of the IR α-chain that substantially conforms to the atomic coordinates listed in Appendix I.

A structure that "substantially conforms" to a given set of atomic coordinates is a structure wherein at least about 50% of such structure has an RMSD of less than about 1.5 A for the backbone atoms in secondary structure elements in each domain, and more preferably, less than about 1.3 A for the backbone atoms in secondary structure elements in each domain, and, in increasing preference, less than about 1.0 A, less than about 0.7 A, less than about 0.5 A, and most preferably, less than about 0.3 A for the backbone atoms in secondary structure elements in each domain.

In a more preferred embodiment, a structure that substantially conforms to a given set of atomic coordinates is a structure wherein at least about 75% of such structure has the recited RMSD value, and more preferably, at least about 90% of such structure has the recited RMSD value, and most preferably, about 100% of such structure has the recited RMSD value.

In an even more preferred embodiment, the above definition of "substantially conforms" can be extended to include atoms of amino acid side chains. As used herein, the phrase "common amino acid side chains" refers to amino acid side chains that are common to both the structure which substantially conforms to a given set of atomic coordinates and the structure that is actually represented by such atomic coordinates.

The present invention also provides a preferred subset of the atomic coordinates listed in Appendixes I and II comprising the C-terminal region of the IR ectodomain α- chain spanning residues 693 to 710 (SEQ ID NO: 13).

As used herein, the term "IR ectodomain" refers to the extracellular domain of IR lacking the transmembrane domain and the intracellular tyrosine kinase domain of IR, typically comprising residues 1 to 917 (mature IR-A receptor numbering) of human IR, or the equivalent thereof, together with any post-translational modifications of these residues such as N- or O-linked glycosylation.

As used herein, the term "low affinity binding site" for IR means the regions of IR involved in forming the low affinity binding site (also known as "Site 1 ") of IR for insulin, comprising the C-terminal region of the IR α-chain and additionally one or both of the L 1 domain of IR and the CR domain of IR. Insulin binding to the low affinity binding site of IR induces formation of the high affinity insulin binding site of IR and subsequent signal transduction.

As used herein, the term "C-terminal region" of the IR α-chain refers to amino acids 693-710 of isoform A (IR-A) of the human IR α-chain as given in SEQ ID NO: 13, with numbering according to mature isoform A of human IR (SEQ ID NO: 1). However, a person skilled in the art will appreciate that the corresponding region (amino acids 693- 710) of the IR α-chain from isoform B of the mature human IR (SEQ ID NO: 2) could alternatively be used in the present invention.

As used herein, the term "classical α-chain C-terminal peptide", or "αCT", refers in IR to a region of the C-terminal α-chain of IR previously described in the literature as being important for insulin binding (Kurose et al., 1994; Kristensen et al, 2002), and comprising amino acids 704-719 (mature IR-A receptor numbering) as given in SEQ ID NO: 1 1.

As used herein, the term "leucine-rich repeat domain 1" or "Ll domain" refers in IR to a leucine-rich domain comprising amino acids 1-156 of mature human IR (SEQ ID NO: 1). The Ll domain of IR comprises a central β-sheet, which comprises amino acids selected from 10-15, 32-37, 60-65, 88-97, 116-121 and 142-147 of mature human IR (SEQ ID NO: 1).

As used herein, the term "leucine-rich repeat domain 2" or "L2 domain" refers in IR to a leucine-rich domain comprising amino acids 310-469 of mature human IR (SEQ ID NO: 1).

As used herein, the term "loop in the fourth leucine-rich repeat (LRR) rung of the Ll domain", or variations thereof, refers in IR to a leucine-rich domain comprising amino acids 85-91 of mature human IR (SEQ ID NO: 1).

As used herein, the term "cysteine-rich domain" or "CR domain" refers in IR to a cysteine-rich domain comprising amino acids 157-309 of mature human IR (SEQ ID NO: 1). The CR domain contains many different modules. As used herein, the term "module 6 of the CR domain" refers in IR to amino acids 256-286 of mature human IR (SEQ ID NO: IGF-IR ectodomain structure

Due to the high sequence homology and structural similarity between IR and IGF- IR, the present invention also provides a model for the C-terminal region of IGF-IR α- chain as it associates with IGF-IR to form the low affinity IGF binding site. The present invention provides a preferred subset of the atomic coordinates listed in Appendixes III and IV comprising the C-terminal region of the IGF-IR ectodomain α-chain spanning residues 681-697 (SEQ ID NO: 15).

As used herein, the term "IGF-IR ectodomain" refers to the extracellular domain of IGF-IR lacking the transmembrane domain and the intracellular tyrosine kinase domain of IGF-IR, typically comprising residues 1 to 905 (mature receptor numbering) of human IGF-IR, or the equivalent thereof, together with any post-translational modifications of these residues such as N- or 0-linked glycosylation.

As used herein, the term "low affinity binding site" for IGF-IR means the regions of IGF-IR involved in forming the low affinity binding site (also known as "Site 1") of IGF-IR for IGF, comprising the C-terminal region of the IGF-IR α-chain and additionally one or both of the Ll domain of IGF-IR and the CR domain of IGF-IR. IGF binding to the low affinity binding site of IGF-IR induces formation of the high affinity IGF binding site of IGF-IR and subsequent signal transduction.

As used herein, the term "C-terminal region" of the IGF-IR α-chain refers to amino acids 681-697 of human IGF-IR α-chain as given in SEQ ID NO: 15, with numbering according to mature human IGF-IR (SEQ ID NO: 6).

As used herein, the term "classical α-chain C-terminal peptide", or "αCT", refers in IGF-IR to a region of IGF-IR corresponding to the C-terminal α-chain of IR previously described in the literature as being important for insulin binding (Kurose et al., 1994; Kristensen et al, 2002), and comprising amino acids 691-706 of IGF-IR (mature IGF-IR numbering) as given in SEQ ID NO: 14.

As used herein, the term "leucine-rich repeat domain 1" or "Ll domain" refers in IGF-IR to a leucine-rich domain comprising amino acids 1-149 of mature human IGF-IR (SEQ ID NO: 6).

As used herein, the term "leucine-rich repeat domain 2" or "L2 domain" refers in IGF-IR to a leucine-rich domain comprising amino acids 300-459 of mature human IGF- IR (SEQ ID NO: 6).

As used herein, the term "that part of the second LRR containing Ser35" refers in IGF-IR to amino acids 35-41 of mature human IGF-IR (SEQ ID NO: 6).

As used herein, the term "cysteine-rich domain" or "CR domain" refers in IGF-IR to a cysteine-rich domain comprising amino acids 150-299 of mature human IGF-IR (SEQ ID NO: 6). The CR domain contains many different modules. As used herein, the term "module 6 of the CR domain" refers to amino acids 249-275 of mature human IGF-IR (SEQ ID NO: 6).

Manipulation of the atomic coordinates of the invention

It will be appreciated that a set of atomic coordinates for a polypeptide is a relative set of points that define a shape in three dimensions. Thus, it is possible that an entirely different set of coordinates could define a similar or identical shape. Moreover, slight variations in the individual coordinates will have little effect on overall shape.

The variations in coordinates may be generated due to mathematical manipulations of the atomic coordinates. For example, the atomic coordinates set forth in Appendix I could be manipulated by crystallographic permutations of the atomic coordinates, fractionalisation of the atomic coordinates, integer additions or subtractions to sets of the structure coordinates, inversion of the atomic coordinates, or any combination thereof.

Alternatively, modification in the crystal structure due to mutations, additions, substitutions, and/or deletions of amino acids, or other changes in any of the components that make up the crystal could also account for variations in atomic coordinates.

Various computational analyses are used to determine whether a molecular complex or a portion thereof is sufficiently similar to all or parts of the structure of the extracellular domain of IR described above. Such analyses may be carried out in current software applications, such as the Sequoia program (Bruns et al., 1999).

The Molecular Similarity program permits comparisons between different structures, different conformations of the same structure, and different parts of the same structure.

Comparisons typically involve calculation of the optimum translations and rotations required such that the root mean square deviation of the fit over the specified pairs of equivalent atoms is an absolute minimum. This number is given in Angstroms.

Accordingly, atomic coordinates of an IR and/or IGF-IR ectodomain comprising the low affinity binding site of the present invention include atomic coordinates related to the atomic coordinates listed in Appendixes I to VI by whole body translations and/or rotations. Accordingly, RMSD values listed above assume that at least the backbone atoms of the structures are optimally superimposed which may require translation and/or rotation to achieve the required optimal fit from whi.ch to calculate the RMSD value.

A three dimensional structure of an IR and/or IGF-IR ectodomain polypeptide or region thereof which substantially conforms to a specified set of atomic coordinates can be modelled by a suitable modeling computer program such as MODELLER (SaIi & Blundell, 1993), using information, for example, derived from the following data: (1) the amino acid sequence of the human IR and/or IGF-IR ectodomain polypeptide; (2) the amino acid sequence of the related portion(s) of the protein represented by the specified set of atomic coordinates having a three dimensional configuration; and, (3) the atomic coordinates of the specified three dimensional configuration. A three dimensional structure of an IR and/or IGF-IR ectodomain polypeptide which substantially conforms to a specified set of atomic coordinates can also be calculated by a method such as molecular replacement, which is described in detail below.

Atomic coordinates are typically loaded onto a machine-readable medium for subsequent computational manipulation. Thus models and/or atomic coordinates are advantageously stored on machine-readable media, such as magnetic or optical media and random-access or read-only memory, including tapes, diskettes, hard disks, CD-ROMs and DVDs, flash memory cards or chips, servers and the internet. The machine is typically a computer.

The atomic coordinates may be used in a computer to generate a representation, e.g. an image, of the three-dimensional structure of the IR and/or IGF-IR ectodomain crystal which can be displayed by the computer and/or represented in an electronic file.

The atomic coordinates and models derived therefrom may also - be used for a variety of purposes such as drug discovery, biological reagent (binding protein) selection and X-ray crystallographic analysis of other protein crystals.

Molecular replacement/binding

The structure coordinates of IR and/or IGF-IR comprising the C-terminal region of the α-chain, such as those set forth in Appendixes I to IV, can also be used for determining the three-dimensional structure of a molecular complex which contains at least the C- terminal region of the α-chain of IR and/or IGF-IR. In particular, structural information about another crystallised molecular complex may be obtained. This may be achieved by any of a number of well-known techniques, including molecular replacement.

Methods of molecular replacement are generally known by those of skill in the art (generally described in Brunger, 1997; Navaza & Saludjian, 1997; Tong & Rossmann, 1997; Bentley, 1997; Lattman, 1985; Rossmann, 1972; McCoy, 2007).

Generally, X-ray diffraction data are collected from the crystal of a crystallised target structure. The X-ray diffraction data is transformed to calculate a Patterson function. The Patterson function of the crystallised target structure is compared with a Patterson function calculated from a known structure (referred to herein as a search structure). The Patterson function of the search structure is rotated on the target structure Patterson function to determine the correct orientation of the search structure in the crystal. A translation function is then calculated to determine the location of the search structure with respect to the crystal axes. Once the search structure has been correctly positioned in the unit cell, initial phases for the experimental data can be calculated. These phases are necessary for calculation of an electron density map from which structural differences can be observed and for refinement of the structure. Preferably, the structural features (e.g., amino acid sequence, conserved di-sulphide bonds, and beta-strands or beta-sheets) of the search molecule are related to the crystallised target structure.

The electron density map can, in turn, be subjected to any well-known model building and structure refinement techniques to provide a final, accurate structure of the unknown (i.e. target) crystallised molecular complex (e.g. see Jones et ai, 1991; Brϋnger et al, 1998).

Obtaining accurate values for the phases, by methods other than molecular replacement, is a time-consuming process that involves iterative cycles of approximations and refinements and greatly hinders the solution of crystal structures. However, when the crystal structure of a protein containing at least a homologous portion has been solved, the phases from the known structure provide a satisfactory starting estimate of the phases for the unknown structure.

By using molecular replacement, all or part of the structure coordinates of IR and/or IGF-IR comprising the C-terminal region of the α-chain provided herein (and set forth in Appendixes I to IV) can be used to determine the structure of a crystallised molecular complex whose structure is unknown more rapidly and efficiently than attempting to determine such information ab initio. This method is especially useful in determining the structure of IR and/or IGF-IR mutants and homologues.

The structure of any portion of any crystallised molecular complex that is sufficiently homologous to any portion of the extracellular domain of IR and/or IGF-IR can be solved by this method.

Such structure coordinates are also particularly useful to solve the structure of crystals of IR and/or IGF-IR co-complexed with a variety of molecules, such as chemical entities. For example, this approach enables the determination of the optimal sites for the interaction between chemical entities, and the interaction of candidate IR and/or IGF-IR agonists or antagonists.

All of the complexes referred to above may be studied using well-known X-ray diffraction techniques and may be refined against 1.5-3.5 A resolution X-ray data to an R value of about 0.25 or less using computer software, such as X-PLOR (Yale University, distributed by Molecular Simulations, Inc.; see Brϋnger, 1996). This information may thus be used to optimize known IR and/or IGF-IR agonist/antagonists, such as anti-IR and/or anti-IF-lR antibodies, and more importantly, to design new or improved IR and/or IGF-IR agonists/antagonists.

Target sites for compound identification, design or screening

The three-dimensional structure of the low affinity binding site of IR and/or IGF- IR provided by the present invention (Appendixes I to IV) can be used to identify potential target binding sites in the low affinity insulin binding site of IR and/or IGF-IR (i.e. to identify those regions of the low affinity binding site of IR and/or IGF-IR involved in and important to the binding of insulin and/or IGF and subsequent signal transduction) as well as in methods for identifying or designing compounds which interact with the low affinity binding site of IR and/or IGF-IR e.g. potential modulators of IR and/or IGF-IR.

The three-dimensional structure of IR and/or IGF-IR provided by the present invention (Appendixes I to IV) can be used to identify potential target binding sites in the Ll domain of IR and/or IGF-IR important for binding to the C-terminal region of the IR and/or IGF-IR α-chain (i.e. to identify those regions of the Ll domain of IR and/or IGF- IR involved in and important to the binding of C-terminal region of the IR and/or IGF-IR α-chain) as well as in methods for identifying or designing compounds which interact with the Ll domain of IR and/or IGF-IR in a manner similar to the C-terminal region of the IR and/or IGF-IR α-chain e.g. potential modulators of IR and/or IGF-IR.

The low affinity binding site of IR is a region of IR ectodomain involved in insulin docking to the receptor. Preferred low affinity target binding sites comprise the C- terminal region of the α-chain and and one or more regions from the Ll domain and/or the CR domain of IR ectodomain. With regards to the Ll domain, the target binding site preferably comprises portions of the molecular surface of the central β-sheet of Ll and portions of the molecular surface of the second leucine-rich repeat (LRR) which contain Phe39 or the loop in the fourth LRR rung of Ll, or preferably both, as defined above. With regards the CR domain, the target binding site preferably comprises module 6 of the CR domain, as defined above.

Alternatively, the low affinity target binding site in IR may comprise one or more amino acids from amino acids 693-710 (encompassing the C-terminal region of the IR α- chain) plus one or more of the following amino acid sequences: (i) amino acids 1-156; (ii) amino acids 157-310, and; (iii) amino acids 594 and 794.

With regards to amino acids 1-156, the target binding site preferably comprises at least one amino acid selected from Argl4, Asnl5, Gln34, Leu36, Leu37, Phe39, Pro43, Phe46, Leu62, Phe64, Leu87, Phe88, Phe89, Asn90, Phe96, Glu97, Argl l8, Glul20 or Hisl44.

With regards to amino acids 157-310, the target binding site preferably comprises at least one amino acid from the amino acid sequence 192-310, more preferably at least one amino acid from the sequence 227-303, yet more preferably least one amino acid selected from the sequence 259-284.

With regards to amino acids 594 arid 794, the target binding site preferably comprises at least one amino acid selected from Asn594 or Arg794.

In a preferred embodiment, van der Waals and/or hydrophobic interactions account for the major portion of the binding energy between a compound and a low affinity insulin binding site of IR.

The three-dimensional structure of the C-terminal region of the IR α-chain provided by the present invention can also be used to identify or more clearly elucidate potential target binding sites on IGF-IR ectodomain (i.e. to identify those regions, or at least more accurately elucidate those regions, of IGF-IR ectodomain involved in and important to the binding of IGF and signal transduction) as well as in methods used for identifying or designing compounds which interact with potential target binding sites of IGF-IR ectodomain, e.g. potential modulators of IGF-IR.

Preferred target binding sites are those governing specificity, i.e. those regions of IGF-IR ectodomain involved in the initial low affinity binding of IGF (i.e. the initial binding of IGF to IGF-IR).

The low affinity binding site of IGF-IR is a region of IGF-IR ectodomain involved in IGF-I binding to the receptor. Preferred low affinity target binding sites comprise the C-terminal region of IGF-IR α-chain and one or more regions from the Ll domain and/or the CR domain of IGF-IR ectodomain. With regards to the Ll domain, the target binding site preferably comprises the central β-sheet of the Ll domain, and/or that part of the second LRR containing Ser35, and/or the loop in the fourth LRR rung of the Ll domain, or preferably all of these, as defined above. With regards the CR domain, the target binding site preferably comprises module 6 of the CR domain, as defined above.

Alternatively, the low affinity IGF binding site may comprise one or more amino acids from amino acids 681-697 (encompassing the C-terminal region of the IGF-IR α- chain) plus one or more amino acids from the following amino acid sequences: (i) amino acids 1-149; and (ii) amino acids 150-298.

With regards to amino acids 1-149, the target binding site preferably comprises at least one amino acid from the amino acid sequence 1-62, preferably 1-49, and more preferably amino acid sequence 23-49. With regards to amino acids 150-298, the target binding site preferably comprises at least one amino acid from the amino acid sequence 185-298, more preferably at least one amino acid from the sequence 220-294, yet more preferably least one amino acid selected from the sequence 252-273. The target binding site preferably comprises at least one amino acid selected from ArglO, His30, Leu32, Leu33, Leu56, Phe58, Arg59, Phe82, Tyr83, Asn84, Tyr85, Val88, Phe90, Argl l2 and Asnl36.

In a preferred embodiment, van der Waals and/or hydrophobic interactions account for the major portion of the binding energy between a compound and a low affinity binding site of IGF- IR.

Additional preferred binding sites in the case of both IR and IGF-IR, particularly for biological macromolecules such as proteins or aptamers, are those that are devoid of glycosylation or devoid of steric hindrance from glycan covalently attached to the polypeptide at sites in the spatial vicinity.

Design, selection, fitting and assessment of chemical entities that bind IR and/or IGF-IR

Using a variety of known modelling techniques, the crystal structure of the present invention can be used to produce a model for the low affinity binding site of IR and/or IGF-IR, or at least part of the C-terminal region of the α-chain of IR or IGF-IR.

As used herein, the term "modelling" includes the quantitative and qualitative analysis of molecular structure and/or function based on atomic structural information and interaction models. The term "modelling" includes conventional numeric-based molecular dynamic and energy minimisation models, interactive computer graphic models, modified molecular mechanics models, distance geometry and other structure-based constraint models.

Molecular modelling techniques can be applied to the atomic coordinates of the low affinity binding site of IR and/or IGF-IR, or at least part of the C-terminal region of the α- chain of IR or IGF-IR, or a region thereof to derive a range of 3D models and to investigate the structure of binding sites, such as the binding sites of monoclonal antibodies, nonimmunoglobulin binding proteins and inhibitory peptides.

These techniques may also be used to screen for or design small and large chemical entities which are capable of binding IR and modulating the ability of IR to interact with extracellular biological targets, such as insulin or members of the IGF receptor family e.g. which modulate the ability of IR to heterodimerise. The screen may employ a solid 3D screening system or a computational screening system.

Such modelling methods are to design or select chemical entities that possess stereochemical complementary to the low affinity binding site of IR and/or IGF-IR, or to the regions of the Ll domain of IR and/or IGF-IR with which the C-terminal region of the α-chain of IR and/or IGF-IR interact. By "stereochemical complementarity" we mean that the compound or a portion thereof makes a sufficient number of energetically favourable contacts with the receptor as to have a net reduction of free energy on binding to the receptor.

Such stereochemical complementarity is characteristic of a molecule that matches intra-site surface residues lining the groove of the receptor site as enumerated by the coordinates set out in Appendix I, optionally also utilising the coordinates set out in Appendixes II to VI. By "match" we mean that the identified portions interact with the surface residues, for example, via hydrogen bonding or by non-covalent Van der Waals and Coulomb interactions (with surface or residue) which promote desolvation of the molecule within the site, in such a way that retention of the molecule at the binding site is favoured energetically.

It is preferred that the stereochemical complementarity is such that the compound has a K(j for the receptor site of less than 10 "4 M, more preferably less than 10 "5 M and more preferably 10 "6 M. In a most preferred embodiment, the K d value is less than 10 "8 M and more preferably less than 10 "9 M.

Chemical entities which are complementary to the shape and electrostatics or chemistry of the receptor site characterised by amino acids positioned at atomic coordinates set out in Appendixes I to IV will be able to bind to the receptor, and when the binding is sufficiently strong, substantially prohibit the interaction of the IR and/or IGF- 1 R ectodomain with biological target molecules such as insulin or IGF.

It will be appreciated that it is not necessary that the complementarity between chemical entities and the receptor site extend over all residues of the receptor site in order to inhibit binding of a molecule or complex that naturally interacts with IR and/or IGF-IR ectodomain.

A number of methods may be used to identify chemical entities possessing stereochemical complementarity to the low affinity binding site of IR and/or IGF-IR, or to the regions of the Ll domain of IR and/or IGF-IR with which the C-terminal region of the α-chain of IR and/or IGF-IR interact. For instance, the process may begin by visual inspection of the entire low affinity insulin binding site comprising the C-terminal region of the α-chain of IR, or the equivalent region in IGF-IR, on the computer screen based on the coordinates in Appendixes I to IV generated from the machine-readable storage medium. Alternatively, selected fragments or chemical entities may then be positioned in a variety of orientations, or docked, within the low affinity binding site of IR and/or IGF- IR, or within the Ll domain of IR and/or IGF-IR in a manner similar to the C-terminal region of the α-chain of IR or IGF-IR, as defined supra. Similar methods could be used to identify chemical entities or compounds that may interact with the Ll domain of IR and/or IGF-IR in a manner similar to that of the C-terminal region of the α-chain of IR and/or IGF-IR.

Modelling software that is well known and available in the art may be used (Guida, 1994). These include Discovery Studio (Accelrys Software Inc., San Diego), SYBYL (Tripos Associates, Inc., St. Louis, Mo., 1992), Maestro (Schrόdinger LLC, Portland), MOE (Chemical Computing Group Inc., Montreal, Canada). This modelling step may be followed by energy minimization with standard molecular mechanics force fields such as AMBER (Weiner et al, 1984), OPLS (Jorgensen and Tirado-Rives, 1988) and CHARMM (Brooks et al, 1983). In addition, there are a number of more specialized computer programs to assist in the process of selecting the binding moieties of this invention.

Specialised computer programs may also assist in the process of selecting fragments or chemical entities. These include, inter alia:

1. GRID (Goodford, 1985). GRID is available from Molecular Discovery Ltd., Italy.

2. AUTODOCK (Goodsell & Olsen, 1990). AUTODOCK is available from Scripps Research Institute, La Jolla, CA.

3. DOCK (Kuntz et al, 1982). DOCK is available from University of California, San Francisco, CA.

4. GLIDE (Friesner et al, 2004). GLIDE is available from Schrόdinger LLC, Portland.

5. GOLD (Cole et al, 2005). GOLD is avaible from The Cambridge Crystallographic Data Centre, Cambridge, UK.

Once suitable chemical entities or fragments have been selected, they can be assembled into a single compound. In one embodiment, assembly may proceed by visual inspection of the relationship of the fragments to each other on the three-dimensional image displayed on a computer screen in relation to the structure coordinates of the low affinity binding site of IR and/or IGF-IR, or the Ll domain to which the C-terminal region of the α-chain of IR or IGF-IR binds. This is followed by manual model building using software such as Discovery Studio, Maestro, MOE or Sybyl. Alternatively, fragments may be joined to additional atoms using standard chemical geometry.

The above-described evaluation process for chemical entities may be performed in a similar fashion for chemical compounds. Useful programs to aid one of skilled in the art in connecting the individual chemical entities or fragments include:

1. CAVEAT (Bartlett et al, 1989). CAVEAT is available from the University of California, Berkeley, CA.

2. GANDI (Day and Caflisch, 2008). GANDI is available from the University of Zurich.

Other molecular modeling techniques may also be employed in accordance with this invention, see, e.g., Cohen et al. (1990) and Navia & Murcko (1992).

There are two preferred approaches to designing a molecule according to the present invention that complement the stereochemistry of the low affinity binding site of IR and/or IGF-IR, or the Ll domain to which the C-terminal region of the α-chain of IR or IGF-IR binds. The first approach is to in silico directly dock molecules from a three- dimensional structural database, to the target binding site, using mostly, but not exclusively, geometric criteria to assess the goodness-of-fit of a particular molecule to the site. In this approach, the number of internal degrees of freedom (and the corresponding local minima in the molecular conformation space) is reduced by considering only the geometric (hard-sphere) interactions of two rigid bodies, where one body (the active site) contains "pockets" or "grooves" that form binding sites for the second body (the complementing molecule).

Flexibility of the receptor, IR or IGFR, can be incorporated into the in silico screening by the application of multiple conformations of the receptor (Totrov and Abagyan, 2008). The multiple conformations of the receptor can be generated from the coordinates listed in Appendixes 1 to VI computationally by use of molecular dynamics simulation or similar approaches.

This approach is illustrated by Kuntz et al. (.1982) and Ewing et al. (2001), the contents of which are hereby incorporated by reference, whose algorithm for ligand design is implemented in a commercial software package, DOCK version 4.0, distributed by the Regents of the University of California and further described in a document, provided by the distributor, which is entitled "Overview of the DOCK program suite" the contents of which are hereby incorporated by reference. Pursuant to the Kuntz algorithm, the shape of the cavity in which the C-terminal region of the α-chain of IR or IGF-IR fits is defined as a series of overlapping spheres of different radii. One or more extant databases of crystallographic data, such as the Cambridge Structural Database System (The Cambridge Crystallographic Data Centre, Cambridge, U.K.), the Protein Data Bank maintained by the Research Collaboratory for Structural Bioinformatics (Rutgers University, N.J., U.S.A.), LeadQuest (Tripos Associates, Inc., St. Louis, MO), Available Chemicals Directory (Symyx Technologies Inc.), and the NCI database (National Cancer Institute, U.S.A) is then searched for molecules which approximate the shape thus defined.

Molecules identified on the basis of geometric parameters, can then be modified to satisfy criteria associated with chemical complementarity, such as hydrogen bonding, ionic interactions and van der Waals interactions. Different scoring functions can be employed to rank and select the best molecule from a database. See for example Bohm & Stahl (1999). The software package FlexX, marketed by Tripos Associates, Inc. (St. Louis, MO) is another program that can be used in this direct docking approach (see Rarey et al, 1996).

The second preferred approach entails an assessment of the interaction of respective chemical groups ("probes") with the active site at sample positions within and around the site, resulting in an array of energy values from which three-dimensional contour surfaces at selected energy levels can be generated. The chemical-probe approach to ligand design is described, for example, by Goodford, (1985), the contents of which are hereby incorporated by reference, and is implemented in several commercial software packages, such as GRID (product of Molecular Discovery Ltd., Italy).

Pursuant to this approach, the chemical prerequisites for a site-complementing molecule are identified at the outset, by probing the active site with different chemical probes, e.g., water, a methyl group, an amine nitrogen, a carboxyl oxygen, or a hydroxyl. Favoured sites for interaction between the active site and each probe are thus determined, and from the resulting three-dimensional pattern of such sites a putative complementary molecule can be generated. This may be done either by programs that can search three- dimensional databases to identify molecules incorporating desired pharmacophore patterns or by programs which use the favoured sites and probes as input to perform de novo design. Suitable programs for determining and designing pharmacophores include CATALYST (Accelrys Software, Inc), and CERIUS2, DISCO (Abbott Laboratories, Abbott Park, IL; distributed by Tripos Associates Inc.).

The pharmacophore can be used to screen in silico compound libraries/ three- dimensional databases, using a program such as CATALYST (Accelrys Software, Inc) and Sybyl/3DB Unity (Tripos Associates, Inc., St. Louis, MO).

Databases of chemical structures are available from a number of sources including Cambridge Crystallographic Data Centre (Cambridge, U.K.), Molecular Design, Ltd., (San Leandro; CA), Tripos Associates, Inc. (St. Louis, MO), Chemical Abstracts Service (Columbus, OH), the Available Chemical Directory (Symyx Technologies, Inc.), the Derwent World Drug Index (WDI), BioByteMasterFile, the National Cancer Institute database (NCI), Medchem Database (BioByte Cortp.), and the Maybridge catalogue. De novo design programs include LUDI (Accelrys Software Inc., San Diego, CA), Leapfrog (Tripos Associates, Inc.), and LigBuilder (Peking University, China).

Once an entity or compound has been designed or selected by the above methods, the efficiency with which that entity or compound may bind to IR and/or IGF-IR can be tested and optimised by computational evaluation. For example, a compound that has been designed or selected to function as an IR binding compound must also preferably traverse a volume not overlapping that occupied by the binding site when it is bound to the native IR. An effective IR binding compound must preferably demonstrate a relatively small difference in energy between its bound and free states (i.e., a small deformation energy of binding). Thus, the most efficient IR and/or IGF-IR binding compound should preferably be designed with a deformation energy of binding of not greater than about 10 kcal/mole, preferably, not greater than 7 kcal/mole. IR and/or IGF-IR binding compounds may interact with IR and/or IGF-IR in more than one conformation that are similar in overall binding energy. In those cases, the deformation energy of binding is taken to be the difference between the energy of the free compound and the average energy of the conformations observed when the compound binds to the protein.

A compound designed or selected as binding to IR and/or IGF-IR may be further computationally optimised so that in its bound state it would preferably lack repulsive electrostatic interaction with the target protein.

Such non-complementary (e.g., electrostatic) interactions include repulsive charge- charge, dipole-dipole and charge-dipole interactions. Specifically, the sum of all electrostatic interactions between the compound and the protein when the compound is bound to IR and/or IGF-IR, preferably make a neutral or favourable contribution to the enthalpy of binding.

Once an IR and/or IGF- 1 R-binding compound has been optimally selected or designed, as described above, substitutions may then be made in some of its atoms or side groups to improve or modify its binding properties. Generally, initial substitutions are conservative, i.e., the replacement group will have approximately the same size, shape, hydrophobicity and charge as the original group. It should, of course, be understood that components known in the art to alter conformation should be avoided. Such substituted chemical compounds may then be analysed for efficiency of fit to IR by the same computer methods described in detail above.

Specific computer software is available in the art to evaluate compound deformation energy and electrostatic interaction. Examples of programs designed for such uses include: Gaussian 03, (Frisch, Gaussian, Inc., Pittsburgh, PA); GAMESS (Gordon et al., Iowa State University); Jaguar (Schrόdinger LLC, Portland); AMBER, version 9.0 (Case et al, University of California at San Francisco); CHARMM (Accelrys Software, Inc., San Diego, CA); and.GROMACS version 4.0 (van der Spoel et al.).

The screening/design methods may be implemented in hardware or software, or a combination of both. However, preferably, the methods are implemented in computer programs executing on programmable computers each comprising a processor, a data storage system (including volatile and non-volatile memory and/or storage elements), at least one input device, and at least one output device. Program code is applied to input data to perform the functions described above and generate output information. The output information is applied to one or more output devices, in known fashion. The computer may be, for example, a personal computer, microcomputer, or workstation of conventional design.

Each program is preferably implemented in a high level procedural or object- oriented programming language to communicate with a computer system. However, the programs can be implemented in assembly or machine language, if desired. In any case, the language may be compiled or interpreted language.

Each such computer program is preferably stored on a storage medium or device (e.g., ROM or magnetic diskette) readable by a general or special purpose programmable computer, for configuring and operating the computer when the storage media or device is read by the computer to perform the procedures described herein. The system may also be considered to be implemented as a computer-readable storage medium, configured with a computer program, where the storage medium so configured causes a computer to operate in a specific and predefined manner to perform the functions described herein.

Compounds

Compounds of the present invention include both those designed or identified using a screening method of the invention and those which are capable of recognising and binding to the low affinity binding sites of IR and/or IGF-IR, as defined above. Also encompassed by the present invention are compounds that bind to the Ll domain of IR and/or IGF-IR in a manner similar to that of the C-terminal region of the α-chain of IR and/or IGF-IR, i.e. compounds which mimic the C-terminal region of the α-chain of IR and/or IGF-IR.

Compounds capable of recognising and binding to the low affinity binding site of IR and/or IGF-IR may be produced using a screening method based on use of the atomic coordinates corresponding to the 3D structure of the the low affinity binding site of IR and/or IGF-IR, or alternatively may be identified by screening against a specific target molecule which is indicative of the capacity to bind to the low affinity binding site of IR and/or IGF-IR.

Compounds capable of recognising and binding to the Ll domain of IR and/or IGF- IR in a manner similar- to that of the C-terminal region of the α-chain of IR and/or IGF-IR (i.e. compounds which mimic the C-terminal region of the α-chain of IR and/or IGF-IR) may be produced using a screening method based on use of the atomic coordinates corresponding to the 3D structure of the the C-terminal region of the α-chain of IR and/or IGF-IR in isolation or as it associates with IR and/or IGF-IR, or alternatively may be identified by screening against a specific target molecule which is indicative of the capacity to bind to the low affinity binding site of IR and/or IGF-IR.

The candidate compounds and/or compounds identified or designed using a method of the present invention may be any suitable compound, synthetic or naturally occurring, preferably synthetic. In one embodiment, a synthetic compound selected or designed by the methods of the invention preferably has a molecular weight equal to or less than about 5000, 4000, 3000, 2000, 1000 or 500 daltons. A compound of the present invention is preferably soluble under physiological conditions.

The compounds may encompass numerous chemical classes, though typically they are organic molecules, preferably small organic compounds having a molecular weight of more than 50 and less than about 2,500 daltons, preferably less than 1500, more preferably less than 1000 and yet more preferably less than 500. Such compounds can comprise functional groups necessary for structural interaction with proteins, particularly hydrogen bonding, and typically include at least an amine, carbonyl, hydroxyl or carboxyl group, preferably at least two of the functional chemical groups. The compound may comprise cyclical carbon or heterocyclic structures and/or aromatic or polyaromatic structures substituted with one or more of the above functional groups. Compounds can also comprise biomolecules including peptides, saccharides, fatty acids, steroids, purines, pyrimidines, derivatives, structural analogs, or combinations thereof.

Compounds may include, for example: (1) Peptides such as soluble peptides, including Ig-tailed fusion peptides and members of random peptide libraries (see, e.g., Lam et ah, 1991; Houghten et ah, 1991) and combinatorial chemistry-derived molecular libraries made of D-anα7or L-configuration amino acids; (2) Phosphopeptides (e.g., members of random and partially degenerate, directed phosphopeptide libraries, see, e.g., Songyang et ah, 1993); (3) Antibodies (e.g., polyclonal, monoclonal, humanized, anti- idiotypic, chimeric, and single chain antibodies as well as Fab, (Fab) 2' , Fab expression library and epitope-binding fragments of antibodies); (4) Nonimmunoglobulin binding proteins such as but not restricted to avimers, DARPins and lipocalins; (5) Nucleic acid- based aptamers; and (6) Small organic and inorganic molecules.

Ligands can be obtained from a wide variety of sources including libraries of synthetic or natural compounds. Synthetic compound libraries are commercially available from, for example, Maybridge Chemical Co. (Tintagel, Cornwall, UK), AMRI (Budapest, Hungary) and ChemDiv (San Diego, CA), Specs (Delft, The Netherlands).

Natural compound libraries comprising bacterial, fungal, plant or animal extracts are available from, for example, Pan Laboratories (Bothell, WA), TimTec (Newark, DE). In addition, numerous means are available for random and directed synthesis of a wide variety of organic compounds and biomolecules, including expression of randomized oligonucleotides.

Alternatively, libraries of natural compounds in the form of bacterial, fungal, plant and animal extracts can be readily produced. Methods for the synthesis of molecular libraries are readily available (see, e.g., De Witt et al., 1993; Erb et al, 1994; Zuckermann et al, 1994; Cho et al, 1993; Carell et al, 1994a; Carell et al, 1994b; and Gallop et al, 1994). In addition, natural or synthetic compound libraries and compounds can be readily modified through conventional chemical, physical and biochemical means (see, e.g., Blondelle and Houghton, 1996), and may be used to produce combinatorial libraries. In another approach, previously identified pharmacological agents can be subjected to directed or random chemical modifications, such as acylation, alkylation, esterification, amidification, and the analogs can be screened for IR and/or IGF-lR-modulating activity.

Numerous methods for producing combinatorial libraries are known in the art, including those involving biological libraries; spatially addressable parallel solid phase or solution phase libraries ; synthetic library methods requiring deconvolution ; the "one-bead one-compound" library method; and synthetic library methods - using affinity chromatography selection. The biological library approach is limited to polypeptide or peptide libraries, while the other four approaches are applicable to polypeptide, peptide, nonpeptide oligomer, or small molecule libraries of compounds (Lam, 1997).

, Compounds also include those that may be synthesized from leads generated by fragment-based drug design, wherein the binding of such chemical fragments is assessed by soaking or co-crystallizing such screen fragments into crystals provided by the invention and then subjecting these to an X-ray beam, and obtaining diffraction data. Difference Fourier techniques are readily applied by those skilled in the art to determine the location within the IR ectodomain and/or IGF-IR ectodomain structure at which these fragments bind, and such fragments can then be assembled by synthetic chemistry into larger compounds with increased affinity for the receptor. Isolated peptides or mimetics thereof

Compounds identified or designed using the methods of the invention can be a peptide or a mimetic thereof. Furthermore, in one aspect the present invention provides an isolated peptide or mimetic thereof which binds the Ll domain of IR and/or the Ll domain of IGF-IR, the peptide comprising: i) an amino acid sequence as provided in SEQ ID NO: 13 or SEQ ID NO: 15; ii) an amino acid sequence which is at least 50% identical to SEQ ID NO: 13 and/or SEQ ID NO: 15; or iii) a fragment of i) or ii) which binds the Ll domain of IR and/or the Ll domain of IGF-

IR, wherein the peptide has a helical structure.

The isolated peptides or mimetics of the invention may be conformationally constrained molecules or alternatively molecules which are not conformationally constrained such as, for example, non-constrained peptide sequences. The term "conformationally constrained molecules" means conformationally constrained peptides and conformationally constrained peptide analogues and derivatives.

The term "analogues" refers to molecules having a chemically analogous structure to naturally occurring α-amino acids. Examples include molecules containing gem- diaminoalkyl groups or alklylmalonyl groups.

The term "derivatives" includes α-amino acids wherein one or more side groups found in the naturally occurring α-amino acids have been modified. Thus, for example the amino acids may be replaced with a variety of uncoded or modified amino acids such as the corresponding D-amino acid or N-methyl amino acid. Other modifications include substitution of hydroxyl, thiol, amino and carboxyl functional groups with chemically similar groups.

With regard to peptides and mimetics thereof, other examples of other unnatural amino acids or chemical amino acid analogues/derivatives which can be introduced as a substitution or addition include, but are not limited to, 2,4-diaminobutyric acid, α-amino isobutyric acid, 4-aminobutyric acid, 2-aminobutyric acid, 6-amino hexanoic acid, 2- amino isobutyric acid, 3-amino propionic acid, ornithine, norleucine, norvaline, hydroxyproline, sarcosine, citrulline, homocitrulline, cysteic acid, t-butylglycine, t- butylalanine, phenylglycine, cyclohexylalanine, β-alanine, fluoro-amino acids, designer amino acids such as β-methyl amino acids, Cα-methyl amino acids, Nα-methyl amino acids, and amino acid analogues in general. The mimetic may be a peptidomimetic. A "peptidomimetic" is a molecule that mimics the biological activity of a peptide but is no longer peptidic in chemical nature. By strict definition, a peptidomimetic is a molecule that no longer contains any peptide bonds (that is, amide bonds between amino acids). However, the term peptide mimetic is sometimes used to describe molecules that are no longer completely peptidic in nature, such as pseudo-peptides, semi-peptides and peptoids. Whether completely or partially non-peptide, peptidomimetics for use in the methods of the invention, and/or of the invention, provide a spatial arrangement of reactive chemical moieties that closely resembles the three-dimensional arrangement of active groups in the peptide on which the peptidomimetic is based. As a result of this similar active-site geometry, the peptidomimetic has effects on biological systems which are similar to the biological activity of the peptide.

There are sometimes advantages for using a mimetic of a given peptide rather than the peptide itself, because peptides commonly exhibit two undesirable properties: (1) poor bioavailability; and (2) short duration of action. Peptide mimetics offer an obvious route around these two major obstacles, since the molecules concerned are small enough to be both orally active and have a long duration of action. There are also considerable cost savings and improved patient compliance associated with peptide mimetics, since they can be administered orally compared with parenteral administration for peptides. Furthermore, peptide mimetics are generally cheaper to produce than peptides.

Suitable peptidomimetics based on the C-terminal region of the α-chain of IR and/or IGR-IR can be developed using readily available techniques. Thus, for example, peptide bonds can be replaced by non-peptide bonds that allow the peptidomimetic to adopt a similar structure, and therefore biological activity, to the original peptide. Further modifications can also be made by replacing chemical groups of the amino acids with other chemical groups of similar structure. The development of peptidomimetics derived from peptides of the C-terminal region of the IR and/or IGF-IR α-chain can be aided by reference to the three dimensional structure of these residues as provided in Appendixes I to IV. This structural information can be used to search three-dimensional databases to identify molecules having a similar structure, using programs such as Sybyl/3DB Unity (Tripos Associates, St. Louis, MO).

Those skilled in the art will recognize that the design of a peptidomimetic may require slight structural alteration or adjustment of a chemical structure designed or identified using the methods of the invention. In general, chemical compounds identified or designed using the methods of the invention can be synthesized chemically and then tested for ability to modulate IR and/or IGF-IR activity using any of the methods described herein. The methods of the invention are particularly useful because they can be used to greatly decrease the number potential mimetics which must be screened for their ability to modulate IR and/or IGF-IR activity.

The peptides or peptidomimetics of the present invention can be used in assays for screening for candidate compounds which bind to regions of IR and/or IGF-IR and potentially interfere with the binding of insulin to IR and/or signal transduction and/or the binding of IGF to IGF-IR and/or signal transduction. Peptides or peptidomimetics which mimic target binding sites are particularly useful as specific target molecules for identifying potentially useful ligands for IR and/or IGFrIR.

Standard solid-phase ELISA assay formats are particularly useful for identifying compounds that bind to the receptor. In accordance with this embodiment, the peptide or peptidomimetic immobilized on a solid matrix, such as, for example an array of polymeric pins or a glass support. Conveniently, the immobilized peptide or peptidomimetic is a fusion polypeptide comprising Glutathione-S-transferase (GST; e.g. a CAP-ERK fusion),, wherein the GST moiety facilitates immobilization of the protein to the solid phase support. This assay format can then be used to screen for candidate compounds that bind to the immobilised peptide or peptidomimetic and/or interefere with binding of a natural binding partner of IR and/or IGF-IR to the immobilised peptide or peptidomimetic.

As used herein a "fragment" is a portion of a peptide of the invention which maintains a defined activity of the "full-length" peptide, namely the ability to bind to the low affinity binding site of IR and/or IGF-IR, or to bind to the Ll domain of IR and/or IGF-IR. Fragments can be any size as long as they maintain the defined activity. Preferably, the fragment maintains at least 50%, more preferably at least 75%, of the activity of the full length polypeptide.

The % identity of a peptide is determined by GAP (Needleman and Wunsch, 1970) analysis (GCG program) with a gap creation penalty=5, and a gap extension penalty^OJ. The query sequence is at least 10 amino acids in length, and the GAP analysis aligns the two sequences over a region of at least 10 amino acids. More preferably, the GAP analysis aligns two sequences over their entire length.

With regard to a defined peptide, it will be appreciated that % identity figures higher than those provided above will encompass preferred embodiments. Thus, where applicable, in light of the minimum % identity figures, it is preferred that the peptide comprises an amino acid sequence which. is at least 50%, more preferably at least 55%, more preferably at least 60%, more preferably at least 65%, more preferably at least 70%, more preferably at least 75%, more preferably at least 80%, more preferably at least 85%, more preferably at least 90%, more preferably at least 91%, more preferably at least 92%, more preferably at least 93%, more preferably at least 94%, more preferably at least 95%, more preferably at least 96%, more preferably at least 97%, more preferably at least 98%, more preferably at least 99%, more preferably at least 99.1%, more preferably at least 99.2%, more preferably at least 99.3%, more preferably at least 99.4%, more preferably at least 99.5%, more preferably at least 99.6%, more preferably at least 99.7%, more preferably at least 99.8%, and even more preferably at least 99.9% identical to the relevant nominated SEQ ID NO.

Amino acid sequence mutants of the peptides identified or designed using the methods of the invention, and/or of the present invention, can be prepared by introducing appropriate nucleotide changes into a nucleic acid of the present invention, or by in vitro synthesis of the desired peptide. Such mutants include, for example, deletions, insertions or substitutions of residues within the amino acid sequence. A combination of deletion, insertion and substitution can be made to arrive at the final construct, provided that the final peptide product possesses the desired characteristics.

In designing amino acid sequence mutants, the location of the mutation site and the nature of the mutation will depend on characteristic(s) to be modified. The sites for mutation can be modified individually or in series, e.g., by (1) substituting first with conservative amino acid choices and then with more radical selections depending upon the results achieved, (2) deleting the target residue, or (3) inserting other residues adjacent to the located site.

Substitution mutants have at least one amino acid residue in the peptide removed and a different residue inserted in its place. Sites of interest are those in which particular residues obtained from various strains or species are identical. These sites, especially those falling within a sequence of at least three other identically conserved sites, are preferably substituted in a relatively conservative manner. Such conservative substitutions are shown in Table 1 under the heading of "exemplary substitutions".

Table 1 - Exemplary substitutions.

In a preferred embodiment a mutant/variant peptide has one or two or three or four conservative amino acid changes when compared to a peptide defined herein. Details of conservative amino acid changes are provided in Table 1.

Also included within the scope of the invention are peptides which are differentially modified during or after synthesis, e.g., by biotinylation, benzylation, glycosylation, acetylation, phosphorylation, amidation, derivatization by known protecting/blocking groups, proteolytic cleavage, linkage to an antibody molecule or other cellular ligand, etc. These modifications may serve to increase the stability and/or bioactivity of the peptide.

The residues that form the IR segment 693-710 can be grouped into three classes :- Class A: those whose side chains are completely buried in the interface with Ll (viz. F701 and F705); Class B: those whose side chains lie at the periphery of the interface with Ll (viz. K694, E697, E698, S700, R702, T704, Y708 and L709); and Class C: those whose side chains appear to have no interaction with Ll (viz. L693, E695, L696, S699, K703, E706, D707 and H710). In terms of using the 693-710 peptide itself as a scaffold for mimetics that might compete with the C-terminal region of the IR α-chain peptide in its binding to the L 1 domain, design might focus in the first instance on substitution of those residues in belonging to Class B, given that the two residues lying in Class A are relatively optimally packed within the interface and already have few degrees of freedom. Higher affinity binding might be achieved by substitution of one or more of the Class B residues with either naturally-occuring amino acids or non-natural amino acids. For example, the substitution of one or more of the charged residues K694, E697, E698 and R702 with residues that have reduced rotameric degrees of freedom (i.e. reduced entropy) may lead to higher affinity binding or altered physicochemical properties of the compound. Such modification for example may include substitution by the naturally occuring amino acids Phe, Tyr or Trp. As a further example, in the case of K.694 and R702, it may be possible to substitute these residues by more bulky non-natural amino acids that retain the terminal cationic character, for example substitution by the basic phenyl propanoic acid derivatives App (L-2-amino-3-(4-aminophenyl)propanoic acid) and/or Gpp, (L-2-amino-3-(4- guanidinophenyl)propanoic acid) (Svenson et al., 2009). A further strategy for design might involve substitutions to improve the overall stability of the helical structure (for example helix stapling - see Danial et al. , 2008). Such substiutions would likely be made within Class C residues. A yet further strategy to improve affinity or physicochemical properties might involve truncation of the helical segment and/or attaching an N- or C- terminal group also designed to improve affinity. Similar principles of design may be applied to generate modified peptides based on the native IGF-IR peptide 681-697 as outlined above for the IR peptide.

In a particularly preferred embodiment, a peptide or mimetic thereof of the invention does not comprise any one of the following described in US 7,173,005: a) X 1 X 2 X 3 X 4 X 5 wherein Xi, X 2 , X 4 and X 5 are aromatic amino acids, and X 3 is any polar amino acid; b) X 6 X 7 X 8 X9 Xi 0 Xn X 12 Xi 3 wherein X 6 and X 7 are aromatic amino acids, X 8 , X9, X) 1 and Xi 2 are any amino acid, and Xi 0 and Xn are hydrophobic amino acids; c) X H X I 5 Xi 6 Xi 7 Xi 8 X 19 X 20 X 2 i wherein X1 4 , and X] 7 are hydrophobic amino acids, X) 5 , X i6, Xiβ and X 19, are any amino acid, and X 20 and X 21 , are aromatic amino acids; d) X 22 X 23 X 24 X 25 X 26 X27 X28 X29 X30 X31 X32 X33 X34 X3 5 X36 X37 X38 X39 X40 X41 wherein X 22 , X 25 , X 28 , X 2 9, X 30 , X33, X34, X3s, X36, X37, X38 > X40, and X41 are any amino acid, X 35 and X 37 may be any amino acid for binding to IR, whereas X 35 is preferably a hydrophobic amino acid and X 37 is preferably glycine for binding to IGF-IR and possess agonist or antagonist activity. X 23 and X 26 are hydrophobic amino acids. This sequence further comprises at least two cysteine residues, preferably at X 25 and X 40 X 31 and X 32 are small amino acids; e) X 42 X 43 X 44 S 45 X 46 X 47 X 48 X 49 Xj 0 X 51 X 52 X 53 X 54 X 55 X 56 X 57 X 58 X 59 X 60 X 6 ] wherein X 42 , X 43 , X 44 , Xi 5 , X 5 3, X 55 , X 56 , X 5 8, XOO and X 6 i may be any amino acid, X 43 , X 46 , X 49 , X 50 , X 54 are hydrophobic amino acids, X 47 and X59 are preferably cysteines, X 48 is a polar amino acid, and X 5 ], X 52 and X 57 are small amino acids; f) X 62 X 6 3 X 64 X 6 5 X 66 X 6 7 X 6 8 Xό9 X70 X7] X72 X73 X74 X7 5 X76 X77 X78 X79 XβO Xδl wherein X 62 , X 65 , X 68 , X 6 9, X71, X73, X76, X77, X78, Xso, and X 8 1. may be any amino acid; X 63 , X 70 , X 74 are hydrophobic amino acids; X 64 is a polar amino acid^ X 67 and X 75 are aromatic amino acids and X 72 and X 79 are preferably cysteines capable of forming a loop; g) H X 82 X 83 X 84 X 85 X 86 X 87 X 88 X 8 9 X9 0 X9 1 X9 2 wherein X 82 is proline or alanine, X 83 is a small amino acid, X 84 is selected from leucine, serine or threonine, X 85 is a polar amino acid, X 86 , X 88 , X 89 and X 90 are any amino acid, and X 87 , X9 1 and X 92 are an aliphatic amino acid; h) Xi 04 Xi 05 Xi 06 X107 X108 X109 Xi iQ X] 11 Xi 12 Xi 13 X114 wherein at least one of the amino acids of Xio 6 through Xm, and preferably two, are tryptophan separated by three amino acids, and wherein at least one of Xio 4 ,.Xio 5 and Xio 6 and at least one of Xn 2 , Xn 3 and Xn 4 are cysteine; i) an amino acid sequence comprising the sequence JB A5: DYKDLCQSWGVRIGWLAGLCPKK or JBA5 minus FLAG® tag and terminal lysines: LCQSWGVRIGWLAGLCP (Formula 9); and j) W X 123 G Y X] 24 W Xi 25 X] 26 wherein Xi 23 is selected from proline, glycine, serine, arginine, alanine or leucine, but more preferably proline; Xi 24 is any amino acid, but preferably a charged or aromatic amino acid; Xi 25 is a hydrophobic amino acid preferably leucine or phenylalanine, and most preferably leucine. Xi 26 is any amino acid, but preferably a small amino acid.

In a further preferred embodiment, a peptide or mimetic thereof of the invention is more structurally similar to the native C-terminal region of the α-chain of IR and/or the C- terminal region of the α-chain of IGF-IR than it is to any one of a) to j) above (such as the peptides provided as SEQ ID Nos: 16 to 18).

The design of synthetic non-peptide mimetics of α-helices is an established art (see for example Davis et al , 2006). In particular, methods of mimicry of i, i+4, i+7 motifs (such as those identified within the C-terminal helical region of the α-chain of IR and IGF- IR and which interact the respective Ll domains (i.e. IR residues Phe701, Phe705, Tyr708 and IGF-IR residues Tyr688, Phe 692, Phe 695) are known. For example, these motifs may be mimicked by terphenyl, oligophenyl, chalcone or l,4-benzodiazepine-2,5-dione scaffolds (Davis et al, 2006) or by benzoylurea scaffolds (US 2008153802). Non-peptide mimetics of α-helices have been investigated as therapeutics in a number of disease contexts, for example HIVl infection (disruption of the assembly of the hexameric helical bundle (Ernst et al, 2001)) and cancer (disruption of the assembly of the HDM2-p53 complex (Yin et al. , 2005); inhibitors of Bcl-2 family heterodimerisation (Degterev et al. , 2001).

With regard to redesigning compounds using a method of the invention, in an embodiment the compound is redesigned to be more structurally similar to the native C- terminal region of the α-chain of IR and/or the C-terminal region of the α-chain of IGF- 1 R. Examples of peptides which could be redesigned in this manner include, but are not limited to, those described by Schaffer et al. (2003) and/or US 7,173,005 (see above).

Interaction of compounds with IR and/or IGF-IR

A compound may interact with the low affinity binding site of IR and/or IGF-IR by binding either directly or indirectly to that region. A compound which binds directly, binds to the specified region. A compound which binds indirectly, binds to a region in close proximity to or adjacent to the low affinity binding site of IR and/or IGF-IR with the result that it interferes with the ability of IR to bind to insulin, or IGF-IR to bind IGF, either antagonistically or agonistically. Such interference may be steric, electrostatic, or allosteric. Preferably, a compound interacts with the low affinity binding site of IR and/or IGF-IR by binding directly to the specified region. In the case of compounds that bind to specific target molecules, such compounds bind directly to the specific target molecule.

A compound may alternatively interact with the Ll domain of IR and/or IGF-IR in " a manner similar to that of the C-terminal region of the α-chain of IR and/or IGF-IR by binding either directly or indirectly to that region. A compound which binds directly, binds to the specified region. A compound which binds indirectly, binds to a region in close proximity to or adjacent to the Ll domain of IR and/or IGF-IR in a manner similar to that of the C-terminal region of the α-chain of IR and/or IGF-IR with the result that it interferes with the ability of IR to bind to insulin, or IGF-IR to bind IGF, either antagonistically or agonistically. Such interference may be steric, electrostatic, or allosteric. Preferably, a compound interacts with the Ll domain of IR and/or IGF-IR in a manner similar to that of the C-terminal region of the α-chain of IR and/or IGF-IR by binding directly to the specified region. In the case of compounds that bind to specific target molecules, such compounds bind directly to the specific target molecule.

Binding can be either by covalent or non-covalent interactions, or both. Examples of non-covalent interactions include electrostatic interactions, van der Waals interactions, hydrophobic interactions and hydrophilic interactions.

When a compound of the invention interacts with IR and/or IGF-IR, it preferably "modulates" IR or IGF-IR, respectively. By "modulate" we mean that the compound changes an activity of IR or IGF-IR by at least 10%. Suitably, a compound modulates IR or IGF-IR by increasing or decreasing signal transduction via IR or IGF-IR, respectively. The phrase "decreases signal transduction" is intended to encompass partial or complete inhibition of signal transduction via IR or IGF-IR. The ability of a candidate compound to increase or decrease signal transduction via IR or IGF-IR can be assessed by any one of the IR or IGF-IR cell-based assays described herein.

Compounds may act as antagonists or agonists for insulin binding to IR or as antagonists or agonists for IGF binding to IGF-IR.

Compounds of the present invention preferably have an affinity for IR or IGF-IR sufficient to provide adequate binding for the intended purpose. Suitably, such compounds and compounds which bind to specific target molecules of IR or IGF-IR have an affinity (K < i) of from 10 '5 to 10 "15 M. For use as a therapeutic, the compound suitably has an affinity (IQ) of from 10 "7 to 10 "15 M, preferably from 10 '8 to 10 "12 M and more preferably from 10 "10 to 10 ~12 M. Where a compound is to be used as a reagent in a competitive assay to identify other ligands, the compound suitably has an affinity (K 4 )) of from lO^ to 10 "12 M.

As will be evident to the skilled person, the crystal structures presented herein have enabled, for the first time, direct comparison of the regions controlling insulin or IGF binding in the closely related IR and IGF-IR. The structures have enabled the identification of the C-terminal region of the α-chain of IR and IGF-IR, critical for the initial binding of insulin or IGF, respectively, and in the subsequent formation of the high affinity insulin-IR or IGF-IGF-IR complex that leads to signal transduction.

In one preferred embodiment, a compound has a high specificity for IR and/or a specific target molecule of IR but not for IGF-IR, i.e. a compound selectively binds to IR or has enhanced selectivity for IR over IGF-IR. In this respect, a compound suitably has an affinity (Kj) for IR and/or a specific target molecule of IR of no more than 10 "5 M, preferably no more than 10 ~7 M, and an affinity for IGF-IR of at least 10 "5 M, preferably at least 10 ~3 M. Such compounds are desirable as, for example, IR agonists where the propensity to interact with IGF-IR and thus, for example, promote undesirable cell proliferation, is reduced.

In a preferred embodiment, the (IR or specific target molecule of IR)/IGF-1R binding affinity ratio for a compound is at least 10 and preferably at least 100.

In another preferred embodiment, a compound has a high specificity for IGF-IR and/or a specific target molecule of IGF-IR but not for IR, i.e. a compound selectively binds to IGF-IR or has enhanced selectivity for IGF-IR over IR. In this respect, a compound suitably has an affinity (K d ) for IGF-IR and/or a specific target molecule of IGF-IR of no more than 10 "5 M, preferably no more than 10 "7 M, and an affinity for IR of at least 10 "5 M, preferably at least 10 "3 M. Such compounds are desirable as, for example, IGF-IR agonists where there propensity to interact with IR and thus, for example, promote glucose uptake and metabolism, is reduced.

In a preferred embodiment, the (IGF-IR or specific target molecule of IGF- 1R)/(IR) binding affinity ratio for a compound is at least 10 and preferably at least 100.

Screening assays and confirmation of binding

Compounds of the invention may be subjected to further confirmation of binding to IR and/or IGF-IR by cocrystallization of the compound with IR and/or IGF-IR and structural determination, as described herein.

Compounds designed or selected according to the methods of the present invention are preferably assessed by a number of in vitro and in vivo assays of IR and/or IGF- 1 R function to confirm their ability to interact with and modulate IR and/or IGF-IR activity. For example, compounds may be tested for their ability to bind to IR and/or IGF-IR and/or for their ability to modulate e.g. disrupt, IR and/or IGF-IR signal transduction.

Libraries may be screened in solution by methods generally known in the art for determining whether ligands competitively bind at a common binding site. Such methods may include screening libraries in solution (e.g., Houghten, 1992), or on beads (Lam, 1991), chips (Fodor, 1993), bacteria or spores (U.S. 5,223,409), plasmids (Cull et al, 1992), or on phage (Scott & Smith, 1990; Devlin, 1990; Cwirla et al, 1990; Felici, 1991 ; U.S. 5,223,409).

Where the screening assay is a binding assay, IR or IGF-IR may be joined to a label, where the label can directly or indirectly provide a detectable signal. Various labels include radioisotopes, fluorescent molecules, chemiluminescent molecules, enzymes, specific binding molecules, particles, e.g., magnetic particles, and the like. Specific binding molecules include pairs, such as biotin and streptavidin, digoxin and antidigoxin, etc. For the specific binding members, the complementary member would normally be labeled with a molecule that provides for detection, in accordance with known procedures.

A variety of other reagents may be included in the screening assay. These include reagents like salts, neutral proteins, e.g., albumin, detergents, etc., which are used to facilitate optimal protein-protein binding and/or reduce non-specific or background interactions. Reagents that improve the efficiency of the assay, such as protease inhibitors, nuclease inhibitors, antimicrobial agents, etc., may be used. The components are added in any order that produces the requisite binding. Incubations are performed at any temperature that facilitates optimal activity, typically between 4 and 40 0 C. Direct binding of compounds to IR or IGF-IR can also be done by Surface Plasmon Resonance (BIAcore) (reviewed in Morton & Myszka, 1998). Here the receptor is immobilized on a CM5 or other sensor chip by either direct chemical coupling using amine or thiol-disulphide exchange coupling (Nice & Catimel, 1999) or by capturing the receptor ectodomain as an Fc fusion protein to an appropriately derivatised sensor surface (Morten & Myszka, 1998). The potential binding molecule (called an analyte) is passed over the sensor surface at an appropriate flow rate and a range of concentrations. The classical method of analysis is to collect responses for a wide range of analyte concentrations. A range of concentrations provides sufficient information about the reaction, and by using a fitting algorithm such as CLAMP (see Morton & Myszka, 1998), rate constants can be determined (Morton & Myszka, 1998; Nice & Catimel, 1999). Normally, the ligand surface is regenerated at the end of each analyte binding cycle. Surface regeneration ensures that the same number of ligand binding sites is accessible to the analyte at the beginning of each cycle.

Incubation periods are selected for optimum activity, but may also be optimized to facilitate rapid high-throughput screening. Normally, between 0.1 and 1 hour will be sufficient. In general, a plurality of assay mixtures is run in parallel with different test agent concentrations to obtain a differential response to these concentrations. Typically, one of these concentrations serves as a negative control, i.e. at zero concentration or below the level of detection.

The basic format of an in vitro competitive receptor binding assay as the basis of a heterogeneous screen for small organic molecular replacements for insulin may be as follows: occupation of the low affinity binding site of IR and/or IGF-IR is quantified by time-resolved fluorometric detection (TRFD) as described by Denley et al, 2004. RTR-A, RTR-B and P6 cells are used as sources of IR-A, IR-B and IGF-IR respectively. Cells are lysed with lysis buffer (20 mM HEPES, 150 mM NaCl, 1.5 mM MgCl 2 , 10% (v/v) glycerol, 1% (v/v) Triton X-100, 1 mM EGTA pH 7.5) for 1 hour at 4°C. Lysates are centrifuged for 10 minutes at 3500 rpm and then 100 μl is added per well to a white Greiner Lumitrac 600 plate previously coated with anti-insulin receptor antibody 83-7 or anti-IGF-lR antibody 24-31. Neither capture antibody interferes with receptor binding by insulin, IGF-I or IGF-II. Approximately 100,000 fluorescent counts of europium-labelled insulin or europium-labelled IGF-I are added to each well along with various amounts of unlabelled competitor and incubated for 16 hours at 4°C. Wells are washed with 20 mM Tris, 150 mM NaCl, 0.05% (v/v) Tween 20 (TBST) and DELFIA enhancement solution (100 μl/well) is added. Time-resolved fluorescence is measured using 340 ran excitation and 612 run emission filters with a BMG Lab Technologies Polarstar™ Fluorimeter or a Wallac Victor II (EG & G Wallac, Inc.).

Examples of other suitable assays which may be employed to assess the binding and biological activity of compounds to and on IR are well known in the art. For example, suitable assays may be found in PCT International Publication Number WO 03/027246. Examples of suitable assays include the following:

(i) Receptor autophosphorylation (as described by Denley et al., 2004). R " IR-A, R ' IR-B cells or P6 cells are plated in a Falcon 96 well flat bottom plate at 2.5 x 10 4 cells/well and grown overnight at 37°C, 5% CO 2 . Cells are washed for 4 hours in serum- free medium before treating with one of either insulin, IGF-I or IGF-II in lOOμl DMEM with 1% BSA for 10 minutes at 37°C, 5% CO 2 . Lysis buffer containing 2mM Na 3 VO 4 and 1 mg/ml NaF is added to cells and receptors from lysates are captured on 96 well plates precoated with antibody 83-7 or 24-31 and blocked with Ix TBST/0.5% BSA. After overnight incubation at 4°C, the plates are washed with 1 x TBST. Phosphorylated receptor is detected with europium-labelled antiphosphotyrosine antibody PY20 (130 ng/well, room temperature, 2 hours). DELFIA enhancement solution (100 μl/well) is added and time resolved fluorescence detected as described above.

(ii) Glucose uptake using 2-deoxy-[U-14C] glucose (as described by Olefsky, 1978). Adipocytes between days 8-12 post-differentation in 24-well plates are washed twice in Krebs-Ringer Bicarbonate Buffer (25mM Hepes, pH 7.4 containing 130 mM NaCl, 5 mM KCl, KH 2 PO 4 , 1.3 mM MgSO 4 JH 2 O, 25-mM NaHCO 3 and 1.15 mM CaCl 2 ) supplemented with 1% (w/v) RIA-grade BSA and 2 mM sodium pyruvate. Adipocytes are equilibrated for 90 min at 37°C prior to insulin addition, or for 30 min prior to agonist or antagonist addition. Insulin (Actrapid, Novogen) is added over a concentration range of 0.7 to 70 nM for 30 min at 37°C. Agonist or antagonist (0 to 500 μM) is added to adipocytes for 90 min followed by the addition of insulin in the case of antagonists. Uptake of 50 μM 2-deoxy glucose and 0.5 μCi 2-deoxy-[U- 14 C] glucose (NEN, PerkinElmer Life Sciences) per well is measured over the final 10 min of agonist stimulation by scintillation counting.

(iii) Glucose transporter GLUT4 translocation using plasma membrane lawns (as described by Robinson & James (1992) and Marsh et al. (1995)).

(iv) GLUT4 translocation using plasma membrane lawns (as described by Marsh et al., 1995). 3T3-L1 fibroblasts are grown on glass coverslips in 6-well plates and differentiated into adipocytes. After 8-12 days post-differentiation, adipocytes are serum- starved for 18 hrs in DMEM containing 0.5% FBS. Cells are washed twice in Krebs- Ringer Bicarbonate Buffer, pH 7.4 and equilibrated for 90 min at 37°C prior to insulin (10OnM) addition, or for 30 min prior to compound (lOOμM) addition. After treatments, adipocytes are washed in 0.5 mg/ml poly-L-lysine in PBS, shocked hypotonically by three washes in 1 :3 (v/v) membrane buffer (30 mM Hepes, pH 7.2 containing 70 mM KCl, 5 mM MgCl 2 , 3 mM EGTA and freshly added 1 mM DTT and 2 mM PMSF) on ice. The washed cells are then sonicated using a probe sonicator (Microson) at setting 0 in 1 :1 (v/v) membrane buffer on ice, to generate a lawn of plasma membrane fragments that remain attached to the coverslip. The fragments are fixed in 2% (w/v) paraformaldehyde in membrane buffer for 20 min at 22°C and the fixative quenched by 100 mM glycine in PBS. The plasma membrane fragments are then blocked in 1% (w/v) Blotto in membrane buffer for 60 min at 22°C and immunolabelled with an in-house rabbit affinity purified anti-GLUT4 polyclonal antibody (clone RlO, generated against a peptide encompassing the C-terminal 19 amino acids of GLUT4) and Alexa 488 goat anti-rabbit secondary antibody (Molecular Probes; 1 :200). Coverslips are mounted onto slides using FluoroSave reagent (Calbiochem), and imaged using an OptiScan confocal laser scanning immunofluorescence microscope (Optiscan, VIC, Australia). Data are analysed using ImageJ (NIH) imaging software. At least six fields are examined within each experiment for each condition, and the confocal microscope gain settings over the period of experiments are maintained to minimise- between-experiment variability.

Insulin agonist activity may be determined using an adipocyte assay. Insulin increases uptake of 3 H glucose into adipocytes and its conversion into lipid. Incorporation of 3 H into a lipid phase is determined by partitioning of lipid phase into a scintillant mixture, which excludes water-soluble 3 H products. The effect of compounds on the incorporation of 3 H glucose at a sub-maximal insulin dose is determined, and the results expressed as increase relative to full insulin response. The method is adapted from Moody et al., (1974). Mouse epididymal fat pads are dissected out, minced into digestion buffer (Krebs-Ringer 25 mM HEPES, 4% HSA, 1.1 mM glucose, 0.4 mg/ml Collagenase Type 1, pH 7.4), and digested for up to 1.5 hours at 36.5 C. After filtration, washing (Krebs- Ringer HEPES, 1% HSA) and resuspension in assay buffer (Krebs-Ringer HEPES, 1% HSA), free fat cells are pipetted into 96-well Picoplates containing test solution and approximately an ED 20 insulin.

The assay is started by addition of 3 H glucose (e.g. ex. Amersham TRK 239), in a final concentration of 0.45 mM glucose. The assay is incubated for 2 hours at 36.5 0 C, in a Labshaker incubation tower, 400 rpm, then terminated by the addition of Permablend/Toluene scintillant (or equivalent), and the plates sealed before standing for at least 1 hour and detection in a Packard Top Counter or equivalent. A full insulin standard curve (8 dose) is run as control on each plate. Data are presented graphically, as the effect of the compound on an (approximate) ED 20 insulin response, with data normalized to a full insulin response. The assay can also be run at basal or maximal insulin concentration.

To test the in vivo activity of a compound, an intravenous blood glucose test may be carried out on Wistar rats as follows. Male Mol:Wistar rats, weighing about 300 g, are divided into two groups. A 10 μl sample of blood is taken from the tail vein for determination of blood glucose concentration. The rats are then anaesthetized (e.g. with Hypnorm/Dormicum) at t =30 min and blood glucose measured again at t =-20 min and at t = 0 min. After the t = 0 sample is taken, the rats are injected into the tail vein with vehicle or test substance in an isotonic aqueous buffer at a concentration corresponding to a 1 ml/kg volume of injection. Blood glucose is measured at times 10, 20, 30, 40, 60, 80, 120 and 180 min. The anaesthetic administration is repeated at 20 min intervals.

Additional assays to determine the effect of binding molecules on IGF-IR activity are as follows:

(i) Cell Viability Assay on HT29 cells with induction of Apoptosis: The ability of compounds to inhibit IGF-mediated rescue from apoptosis is measured using the colorectal cell line HT29 cells (ATCC: HTB 38) after induction with Na Butyrate. The HT29 cells are plated out onto white Fluoronunc 96 well plates (Nunc) at 12,000cells/ml and incubated at 37 0 C, 5% CO 2 for 48 hours. Media is aspirated and lOOμl/well of serum free DMEM/F12 is added for 2 hours to serum starve cells. IGF (lOOμl/ well 0.05-50 nM dilutions) in the presence and the absence of inhibitory compound is added in 0.1% BSA solution (Sigma) in DMEM/F12 (Gibco) in triplicate. A final concentration of 5mM Butyrate (Sigma) is added to each well. Plates are incubated at 37 0 C, 5% CO 2 for a further 48 hours. Plates are brought to room temperature and developed (as per instructions for CTG Assay (Promega)). Luminescence signal is measured on the Polarstar plate reader and data is evaluated using table curve to obtain the specific ED50.

(ii) Cell Migration Assay: The migration assays are performed in the modified 96-well Boyden chamber (Neuroprobe, Bethesda, MA). An 8 μM polycarbonate filter, which is pre-soaked in 25 μg/ml of collagen in 10 mM acetic acid overnight at 4 0 C, is placed so as to divide the chamber into an upper & lower compartment. Varying concentrations of the IGF-I- analogues (25 μl of 0-100 nM) diluted in RPMI (Gibco) with 0.5% BSA (Sigma) tested for their migration inducing ability, are placed in the lower compartment in quadruplicates. The wells of the upper chamber are seeded with 50μl/well of 2x10 5 SW480 (ATCC:CCL 228) pre-incubated for 30mins/37°C with 1.1 μl of 2μM Calcein (Molecular Probes). Cells migrate for 8 hours at 37 0 C, 5% CO 2 . Unmigrated cells are removed by wiping the filter. The filter is then analysed in the Polarstar for fluorescence at excitation wavelength of 485nm and emission wavelength of 520nm. Data is evaluated using table curve to obtain the specific ED50 value.

(iii) Mouse Xenograft studies for anti-IGF-lR antibodies: In vivo studies are performed in 56-week-old female athymic BALBc nude mice, homozygous for the nunu allele. Mice are maintained in autoclaved micro-isolator cages housed in a positive pressure containment rack (Thoren Caging Systems Inc., Hazelton, PA, USA. To establish xenografts, mice are injected subcutaneously into the left inguinal mammary line with 3 x 10 6 or 5 x 10 6 cells in 100 μl of PBS. Tumour volume (TV) is calculated by the formula (length x width 2 )/2 (Clarke et al., 2000), where length is the longest axis and width the measurement at right angles to length.

Initial biodistribution of potential binding molecules are ascertained by injecting 40 BALBc nude mice with established xenografts with radiolabeled " 1 In- or 125 I-anti-IGFR antibody (3 μg, 10 μCi) intravenously via the tail vein (total volume=0.1 ml). At designated time points after injection of the radioconjugates (t=4 h, days 1, 2, 3, 5 and 7), groups of mice («=35) are killed by Ethrane anaesthesia. Mice are then exsanguinated by cardiac puncture, and tumours and organs (liver, spleen, kidney, muscle, skin, bone (femur), lungs, heart, stomach, brain, small bowel, tail and colon) are resected immediately. All samples are counted in a dual gamma scintillation counter (Packard Instruments). Triplicate standards prepared from the injected material are counted at each time point with tissue and tumour samples enabling calculations to be corrected for the physical decay of the isotopes. The tissue distribution data are calculated as the mean ± s.d. percent injected dose per gram tissue (%ID g "1 ) for the candidate molecule per time point.

Pharmacokinetics for the candidate compounds are ascertained as follows: Serum obtained from mice bearing xenografts, following infusion of radiolabelled-binding molecule as described above, is aliquoted in duplicate and counted in a gamma scintillation counter (Packard Instruments, Melbourne, Australia). Triplicate standards prepared from the injected material are counted at each time point with serum samples to enable calculations to be corrected for the isotope physical decay. The results of the serum are expressed as % injected dose per litre (% ID l '1 ). Pharmacokinetic calculations are performed of serum data using a curve fitting program (WinNonlin, Pharsight Co., Mountain View, CA, USA). A two- compartment model is used to calculate serum pharmacokinetic parameters of AUC (area under the serum concentration curve extrapolated to infinite time), CL (total serum clearance), T) 20 and T| 2 p (half-lives of the initial and terminal phases of disposition) for 125 I- and '"in-labelled molecule.

(iv) Therapeutic in vivo studies: Tumour cells (3 x 10 6 ) in 100 μl of media are inoculated subcutaneously into both flanks of 46-week-old female nude mice («=5 group " '). Candidate molecule treatment commences day 7 post-tumour cell inoculations (mean ± s.e. tumour volume=60xl5 mm 3 ) and consists of six intraperitoneal injections over 2 weeks of appropriate amounts of the candidate molecule or vehicle control. Tumour volume in mm 3 is determined as described previously. Data is expressed as mean tumour volume for each treatment group. Differences in tumour size between control and test groups are tested for statistical significance (f<0.05) by /-test.

Uses of compounds

Compounds/chemical entities designed or selected by the methods of the invention described above may be used to modulate IR and/or IGF-IR activity in cells, i.e. activate or inhibit IR and/or IGF-IR activity. Such compounds may interact with the low affinity binding sites of IR and/or IGF-IR as defined herein, or mimic the C-terrninal region of the α-chain of IR and/or IGF-IR as defined herein. They may also be used to modulate homodimerisation of IR and/or IGF-IR.

Modulation of homodimerisation of IR and/or IGF-IR may be achieved by direct binding of the chemical entity to a homodimerisation surface of IR and/or IGF-IR, and/or by an allosteric interaction elsewhere in the IR and/or IGF-IR extracellular domain.

Given that aberrant IR and/or IGF-IR activity is implicated in a range of disorders, the compounds described above may also be used to treat, ameliorate or prevent disorders characterised by abnormal IR and/or IGF-IR signalling. Examples of such disorders include malignant conditions including tumours of the brain, head and neck, prostate, ovary, breast, cervix, lung, pancreas and colon; and melanoma, rhabdomyosarcoma, mesothelioma, squamous carcinomas of the skin and glioblastoma.

The compounds designed to interact or identified as interacting with the extracellular domain of IR and/or IGF-IR, and in particular to interact with the target binding sites, are useful as agonists or antagonists against the action of insulin on IR and/or IGF on IGF-IR. The compounds are useful as assay reagents for identifying other useful ligands by, for example, competition assays, as research tools for further analysis of IR and/or IGF-IR and as potential therapeutics in pharmaceutical compositions.

Compounds provided by this invention are also useful as lead compounds for identifying other more potent or selective compounds. ' The mimetic compounds of the present invention are also potentially useful as inhibitors of the action of insulin and in the design of assay kits directed at identifying compounds capable of binding to the low affinity binding site for insulin on IR. The mimetic compounds of the present invention are also potentially useful as inhibitors of the action of IGF and in the design of assay kits directed at identifying compounds capable of binding to the low affinity binding site for IGF on IGF-IR. In particular, it is envisaged that compounds of the present invention will prove particularly useful in selecting/designing ligands which are specific for IR or IGF- IR.

In one embodiment, one or more of the compounds can be provided as components in a kit for identifying other ligands (e.g., small, organic molecules) that bind to IR or IGF- IR. Such kits may also comprise IR or IGF-IR, or functional fragments thereof. The compound and receptor components of the kit may be labeled (e.g. by radioisotopes, fluorescent molecules, chemiluminescent molecules, enzymes or other labels), or may be unlabeled and labelling reagents may be provided. The kits may, also contain peripheral reagents such as buffers, stabilizers, etc. Instructions for use can also be provided.

IR and IGF-IR agonists and antagonists, and in particular antagonists, provided by this invention are potentially useful as therapeutics. For example, compounds are potentially useful as treatments for cancers, including, but not limited to, breast, prostate, colorectal, and ovarian cancers. Human and breast cancers are responsible for over 40,000 deaths per year, as present treatments such as surgery, chemotherapy, radiation therapy, and immunotherapy show limited success. Recent reports have shown that a previously identified IGF-IR antagonist can suppress retinal neovascularization, which causes diabetic retinopathy (Smith et al., 1999). IGF-IR agonist compounds (i.e. existing IGF- 1 R compounds which have been modified employing methods of the present invention) are useful for development as treatments for neurological disorders, including stroke and diabetic neuropathy. Reports of several different groups implicate IGF-IR in the reduction of global brain ischemia, and support the use of IGF-I for the treatment of diabetic neuropathy (reviewed in Auer et al., 1998; Apfel, 1999). A number of therapeutics directed against IGF-IR are currently undergoing clinical trial as anti-cancer agents (Hewish et al, 2009)

The IGF-IR agonist peptides of the invention may be useful for enhancing the survival of cells and/or blocking apoptosis in cells.

Administration

Compounds of the invention, i.e. ligands of the invention or modulators of IR and/or IGF-IR identified or identifiable by the screening methods of the invention, may preferably be combined with various components to produce compositions of the invention. Preferably the compositions are combined with a pharmaceutically acceptable carrier or diluent to produce a pharmaceutical composition (which may be for human or animal use).

The formulation will depend upon the nature of the compound and the route of administration but typically they can be formulated for topical, parenteral, intramuscular, oral, intravenous, intra-peritoneal, intranasal inhalation, lung inhalation, intradermal or intra-articular administration. The compound may be used in an injectable form. It may therefore be mixed with any vehicle which is pharmaceutically acceptable for an injectable formulation, preferably for a direct injection at the site to be treated, although it may be administered systemically.

The pharmaceutically acceptable carrier or diluent may be, for example, sterile isotonic saline solutions, or other isotonic solutions such as phosphate-buffered saline. The compounds of the present invention may be admixed with any suitable binder(s), lubricant(s), suspending agent(s), coating agent(s), solubilising agent(s). It is also preferred to formulate the compound in an orally active form.

In general, a therapeutically effective daily oral or intravenous dose of the compounds of the invention, including compounds of the invention and their salts, is likely to range from 0.01 to 50 mg/kg body weight of the subject to be treated, preferably 0.1 to 20 mg/kg. The compounds of the invention and their salts may also be administered by intravenous infusion, at a dose which is likely to range from 0.001-10 mg/kg/hr.

Tablets or capsules of the compounds may be administered singly or two or more at a time, as appropriate. It is also possible to administer the compounds in sustained release formulations.

Typically, the physician will determine the actual dosage which will be most suitable for an individual patient and it will vary with the age, weight and response of the particular patient. The above dosages are exemplary of the average .case. There can, of course, be individual instances where higher or lower dosage ranges are merited, and such are within the scope of this invention.

For some applications, preferably the compositions are administered orally in the form of tablets containing excipients such as starch or lactose, or in capsules or ovules either alone or in admixture with excipients, or in the form of elixirs, solutions or suspensions containing flavouring or colouring agents.

The compositions (as well as the compounds alone) can also be injected parenterally, for example intravenously, intramuscularly or subcutaneously. In this case, the compositions will comprise a suitable carrier or diluent.

For parenteral administration, the compositions are best used in the form of a sterile aqueous solution which may contain other substances, for example enough salts or monosaccharides to make the solution isotonic with blood.

For buccal or sublingual administration the compositions may be administered in the form of tablets or lozenges which can be formulated in a conventional manner. For oral, parenteral, buccal and sublingual administration to subjects (such as patients), the daily dosage level of the compounds of the present invention and their pharmaceutically acceptable salts and solvates may typically be from 10 to 500 mg (in single or divided doses). Thus, and by way of example, tablets or capsules may contain from 5 to 100 mg of active compound for administration singly, or two or more at a time, as appropriate. As indicated above, the physician will -determine the actual dosage which will be most suitable for an individual patient and it will vary with the age, weight and response of the particular patient.

The routes of administration and dosages described are intended only as a guide since a skilled practitioner will be able to determine readily the optimum route of administration and dosage for any particular patient depending on, for example, the age, weight and condition of the patient.

Examples

Example 1; A thermodynamic study of Iigand binding to the first three domains of the human insulin receptor (IR): relationship between the IR α-chain C-terminal peptide fαCT) and the Site 1 insulin mimetic peptides

/./ Introduction

In order to study Iigand binding to the first three domains of IR ectodomain, isothermal titration calorimetry (ITC) was used. ITC allowed a direct assay of the interactions between the IR ectodomain classical αCT peptide (residues 704-719; SEQ ID NO: 11) and IR485 (a construct consisting of the first three N-terminal domains of the IR; SEQ ID NO: 10), as well as the interaction between the analogous peptide of human IGF- IR and IR485. At the same time the thermodynamics of binding of the N- and C-terminal segments of the insulin mimetic peptide S519 (Schaffer et al., 2003) to IR485, as well as the binding of S519 itself to IR485 were examined. S519 (SLEEEWAQVECEVYGRGCPSGSLDESFYDWFERQLG; SEQ ID NO: 16) is a 36-residue peptide resulting from the affinity-optimization of two covalently-linked peptides, S371, a so-called "Site 1" peptide, and S446, a so-called "Site 2" peptide (Pillutla et al., 2002). S519 binds human IR with K < ι=2.0 x 10 "11 (Schaffer et al., 2003). Taken together, the results revealed a remarkable relationship between the IR αCT peptide and the Site 1 mimetic peptide, and suggested a previously undetected structural similarity between the mimetic peptides and insulin itself (Ward and Lawrence, 2009). Finally, the binding to IR485 of the IR αCT peptide carrying a F714A mutation (residues 704-719, TFEDYLHNVVAVPRPS; SEQ ID NO: 12) was examined. 1.2 Materials and methods/or thermodynamic experiments .

Reagents

The IR485 construct of human IR was expressed in Lec8 mutant CHO cells and purified by gel filtration chromatography as described previously (Lou et al., 2006). IR485 consists of the first 485 residues of the mature human insulin receptor followed by the 16- residue sequence SDDDDKEQKLI SEEDLN (SEQ ID NO: 10), which comprises a serine residue followed by an enterokinase cleavage site and a c-myc epitope tag. The c-myc tag was not removed for the ITC studies described here. IR485 was concentrated to 30 mg/ml in Tris-buffered saline (TBSA; 24.8 mM Tris-HCl (pH 8.0), 137 mM NaCl, 2.7 mM KCl and 0.02% sodium azide) using an Ultrafree centrifugal concentrator (Millipore, USA). Porcine insulin (Sigma-Aldrich, USA) was prepared in a zinc-free-form (termed ZFP- insulin) by extensive dialysis against 0.1% (v/v) acetic acid followed by lyophilization. Human IGF-I was obtained from Novozymes GroPep (Australia) as "receptor grade" material.

The IR classical αCT peptide (residues 704-719, TFEDYLHNVVFVPRPS; SEQ ID NO: 1 1), the IGF-IR classical αCT peptide (residues 691-706, VFENFLHNSIFVPRPE; SEQ ID NO: 14) as well as the F714A mutant of IR αCT (denoted IR αCT.714A; SEQ ID NO: 12) were obtained from Genscript Corporation (USA) at the >98% level of purity. The S519N20 peptide (SLEEEWAQVECEVYGRGCPS; SEQ ID NO: 17) and the S519C16 peptide (GSLDESFYDWFERQLG; SEQ ID NO: 18) were obtained from AusPep (Australia) at the >90% level of purity. The S519 peptide

(SLEEEWAQVECEVYGRGCPSGSLDESFYDWFERQLG; SEQ ID NO: 16) was obtained from Activotec (UK) at the >85% purity. Peptides were prepared by dissolving in 10 mM HCl at ~4 mg/ml concentration and then diluting with TBSA. Oxidation of peptides S519N20 and S519 (which contain two cysteine residues) was carried out by incubating the respective peptide (prepared at 1 mg/ml in 50 mM ammonium bicarbonate adjusted to pH 8.5 with ammonia solution) in the dark at room temperature for 2 days and then lyophilizing before use. Oxidation was complete as determined by analysis with Ellman's reagent (5,5'-dithiobis-2-nitrobenzoate). All protein concentrations were determined by absorbance measurement at 280 nm using a NanoDrop 1000 spectrophotometer (Thermo Scientific, USA).

Isothermal Titration Calorimetry

ITC experiments were performed using a VP-ITC isothermal titration calorimeter (MicroCal Inc., USA) with the calorimeter cell held at 25 0 C. All samples were degassed prior to injection or placement into the cell, and the instrument was temperature equilibrated prior to the start of the injections. In all experiments the volume of sample placed in the cell was 1.4 ml and the titrant was injected in 7 μl volumes over 14 s at 3 min intervals, with the total number of injections being 40. The sample contents were stirred at a speed of 310 rpm over the duration of the titration. All titrants (i.e. ZFP-insulin, IGF-I, IR αCT peptide, IGF-IR αCT peptide, IR αCT.714A peptide, S519, S519N20, and S519C20) were first injected into a solution of TBSA alone in order ascertain the heat of dilution, which was then subtracted from the data of interest as appropriate. Data were analyzed using the instrument's software incorporated within the Origin 7 software (OriginLab, USA) and in all cases fitted as a single-site interaction using the methodologies outlined in the instrument's manual. All measurements showing quantifiable interaction were done in triplicate (in some cases at varying concentrations) and the resultant ITC-derived thermodynamic parameters averaged.

Dynamic light scattering (DLS)

DLS measurements were carried out using a Zetasizer NanoZS (Malvern Instruments Ltd, England). Samples of IR485 and IR485 in combination with IR αCT and/or ZFP-insulin at various concentrations were prepared in TBSA and equilibrated overnight at 4 0 C. Samples were spun at 13,000 g using a benchtop centrifuge to pellet any macroscopic particulates and then pipetted into a 45 μl glass cuvette held at 20 0 C. Data were analysed using the instrument's Dispersion Technology Software version 5.0.2 to yield a volume distribution for the scattering particles present in the solution. The results presented were representative of several sets of experiments.

1.3 Results from thermodynamic experiments

The pairwise interactions ofIR485, hormones and aCT peptides

ITC experiments investigated the pairwise interaction between selected combinations of IR485, ZFP-insulin, IGF-I, IR αCT peptide, IGF-IR αCT peptide and IR αCT.714A peptide. The results of the analyses are presented in Table 2. The mean dissociation constants (IQ) of the interaction between (i) IR αCT and IR485, (ii) IGF-IR αCT and IR 485, and (iii) IR αCT.714A and IR485 were determined to be 3.9 ± 1.1 μM, 17.6 ± 2.1 μM and 6.5 ± 1.7 μM respectively. Representative ITC profiles for these measurements are presented in Figure 2. The dissociation constant (K d ) for the interactions between (i) ZFP-insulin and the IR αCT peptide, (ii) IGF-I and the IGF-IR αCT peptide, (iii) ZFP-insulin and IR485 and (iv) IGF-I and IR485 was in all cases estimated to be weaker than 1 mM. Table 2 - ITC analysis of pairwise interactions of IR485, hormone and αCT peptides 0 . Sample [Sample] (μM) Titrant [Titrant] (μM) K d (μM)

ZFP-insulin 20 IR-αCT 200 1000

IGF-IR 20 IGFlR-αCT 200 1000

IR485 5 ZFP-insulin 50 1000

IR485 10 IGF-IR 100 1000

IR485 10 IR-αCT 60 3.9 ± 1.1

IR485 20 IGFlR-αCT 120 - 150* 17.6 ± 2.1

IR485 10 IR-αCT.714A 60 6.5 ± 1.7

" K d values are of the mean of three experiments with each set of experimental data being modeled as a single-site interaction between titrant and sample (see Materials and Methods). The error stated is the standard error of the mean. The relatively low value of the Wiseman parameter c coupled with the noise in the data precludes accurate determination of ΔH° (and hence of -TΔS°). * Ranges are quoted for sample or titrant concentration where these vary across the three measurements.

The interaction of hormone with aCT peptide pre-complexed IR485

ITC experiments investigated the interaction of ZFP-insulin and IGF-I with IR485 pre-complexed with a ten-fold molar ratio of either IR αCT or IGF-IR αCT peptide. Given that the αCT . peptides displayed micromolar affinity for IR485 (see above), it was calculated that, at the concentrations of IR485 and αCT peptide employed in this set of experiments, >90% of the IR485 molecules within the ITC cell were in complex with αCT peptide prior to injection of hormone. The results of the ITC investigations are presented in Table 3 with representative ITC curves being presented in Figure 3. The dissociation constant of ZFP-insulin with respect to IR485 in the presence of a 10-fold molar ratio of IR αCT peptide was 17 ± 4nM and in the presence of a 10-fold molar ratio of IGF-IR αCT peptide was 5.7 ± 1.InM. In contrast, the dissociation constant of IGF-I with respect to IR485 in the presence of a 10-fold excess of IR αCT peptide was 490 ± 75nM and in the presence of a 10-fold excess of IGF-IR αCT peptide was 22 ± 3nM, with no correction being made for the incomplete saturation of IR485 with peptide prior to injection. The thermodynamic parameters presented in Table 3 show that in all four cases the binding of hormone to αCT peptide pre-complexed IR485 is enthalpically driven. Table 3 - Isothermal titration of ZFP-insulin and IGF-IR against IR485 pre-mixed with a 10-fold molar ratio of either IR or IGF-IR αCT peptide".

Sample [Sample] Titrant [TitrantJ K d ΔH° -TΔS° (μM) (μM) (nM) (kJ/mol) (kJ/mol)

IR485 5 ZFP-insulin 50 17 ± 4 -67 ± 1 22 ± 2

+(1OxIR aCT)

IR485 4 - 10* ZFP-insulin 32 - 60 5.7 ± 1.1 -97 ± 2 50 ± 2

+(10xIGFlR-aCT)

IR485 5 - 10 IGF-IR 50 - 80 490 ± 75 -89 ± 2 53 ± 2

+(10xIR-aCT)

IR485 4 - 5 IGF-IR 40 - 50 22 ± 3 -101 ± 1 57 ± 1

+(1OxIGFl R-aCT)

" K d , ΔH° and -TΔS° values are of the mean of three experiments with each set of experimental data being modeled as a single-site interaction between titrant and sample (see Materials and Methods). The error stated is the standard error of the mean. * Ranges are quoted for sample or titrant concentration where these vary across the three measurements.

The interaction of insulin mimetic peptides with IR485

ITC experiments investigated the interaction of the insulin mimetic peptides S519 (SEQ ID NO: 16), S519N20 (a Site 2 peptide, corresponding to the 20 N-terminal residues of S519; SEQ ID NO: 17) and S519C16 (a Site 1 peptide, corresponding to the 16 C- terminal residues of S519; SEQ ID NO: 18) with IR485. The results are presented in Table 4, with representative ITC curves being presented in Figure 4. S519 was found to bind IR485 with a dissociation constant of 1 1 ± 3nM, whilst S519C16 bound IR485 with somewhat higher affinity (IQ = 2.6 ± 0.7nM). The binding of both S519 and S519C16 to IR485 appeared to be enthalpically driven. When IR485 was in the presence of a 10-fold molar ratio of IR αCT peptide, the dissociation constant of S519C16 increased to 16 ± 6nM. The dissociation constant for the interaction between S519N20 and IR485 was estimated to be weaker than ImM, with accurate determination of IQ precluded at the concentrations of reactants employed. Table 4 - Isothermal titration of insulin mimetics peptides S519, S519N20 and S519C16 against IR485 α sample [Sample] Titrant [Titrant] κ d ΔH° -TΔS°

(μM) (μM) (nM) (kJ/mol) (kJ/mol)

R485 4.5-5* S519 40-50 11 ± 3 -69 ± 6 24 ± 6

R485 5 S519C16 50 2.6 ± 0.7 -61 ± 4 12 ± 4

R485 + 3-5 S519C16 45-50 16 ± 6 -33 ± 2 -11 ± 3

10xIR-αCT)

R485 5 S519N20 50 I mM <c)

' Kj, ΔH° and -TΔS° values are of the mean of three experiments with each set of experimental data being modeled as a single-site interaction between titrant and sample (see Materials and Methods). The error stated is the standard error of the mean. *Ranges are quoted for sample or titrant concentration where these vary across the three measurements . c The affinity of interaction of S519N20 with IR485 is too weak to allow meaningful calculation of either ΔH° or -TΔS°.

The multimeήc state ofIR485 in the presence of IR aCT peptide

The DLS-determined volume distribution of IR485 at 6 mg/ml (a concentration at which IR485 is overwhelmingly dimeric (Lou et al., 2006) showed a single broad peak centred at a particle diameter of 9.7 run (Figure 5a). The half-width of the peak was 3.1 nm and the assumption of a spherical particle lead to a calculated scattering particle molecular weight of 136 kDa, closely similar to the molecular weight of -140 kDa estimated by size-exclusion chromatography. Instrumental limitations precluded DLS measurement of IR485 at concentrations at which IR485 was known to be overwhelmingly monomeric (i e. at < 0.025 mg/ml, (Lou et al., 2006). However, at 0.5 mg/ml, the DLS-determined volume distribution of IR485 showed a single broad peak at a particle diameter of 8.2 nm (Figure 5b). The half-width of the peak was 2.2 nm and the assumption that the scattering arose from a single species of spherical scattering particle lead to a calculated molecular weight of 91 kDa, consistent with the solution being predominantly monomeric. Using this pair of observations as reference values, it was then observed that (i) an addition of a three-fold molar ratio of IR αCT peptide to a 6 mg/ml solution of IR485 resulted in a DLS-determined volume distribution which had a single peak centred at 8.6 nm (Figure 5c), and (ii) an addition of a three-fold molar ratio of IR αCT peptide together with a 2- fold molar ratio of ZFP-insulin to a 6 mg/ml solution of IR485 resulted in a volume distribution which had a single peak centred at 8.2 nm (Figure 5d). The half-width of these latter two peaks was 2.4 nm and the calculated molecular weights of the scattering particles (again assuming a single species_of spherical scatterers) was 102 kDa and 92 kDa respectively. These data implied that addition of either (i) IR αCT peptide or (ii) IR αCT peptide plus ZFP-insulin to a 6 mg/ml solution of IR485 resulted in a change in its hydrodynamic diameter consistent with the construct undergoing a transition from being overwhelmingly dimeric in solution to predominantly monomeric in solution.

Example 2: Solving the crystal structure of the C-terminal region of the α-chain of IR

2.1 Introduction: ambiguous electron density

As described previously (WO 07/147213), an area of strand-like ambiguous electron density was present near the Ll-β2 face of IR. However, despite numerous different processing and refinement protocols, the density was impossible to interpret in terms of any peptide sequence. The data described in Example 1 above implied a surprising and previously unexpected sequence relationship between the S519C16 peptide (SEQ ID NO: 18) and the 'classical' αCT peptide region (residues 704-719; SEQ ID NO: 1 1) described previously in the literature (Kurose et al., 1994). X-ray data obtained in WO 07/147213 were revisited and further reviewed with the possibility then in mind that the ambiguous electron density near the Ll-β2 face of IR could have been due to the 'classical' αCT peptide region of the IR α-chain.

2.2 Protein production, crystallisation and data collection from IR ectodomain crystals

Production of IR ectodomain protein, subsequent crystallization and data collection were performed as described previously (WO 07/147213).

2.3 Diffraction data processing and crystallographic refinement

The diffraction images used were those used in the native structure determination of the human insulin receptor ectodomain homodimers ("Native 2" data set, see Table 3 of WO 07/147213). The diffraction images were re-processed using XDS (version 10- September-2008; Kabsch, 1993), including reflections to a maximum resolution of 3.8 A. Diffraction data processing statistics from XDS are shown in Table 5. About a 1 A difference in the longest cell dimension was observed as compared to analysis previously with the D*trek (Pflugrath, 1999) program.

The receptor ectodomain monomer complexed with Fab 83-7 and Fab 83-14 (Protein Data Bank entry 2DTG, with minor prior in house improvement) was subjected to individual domain rigid body crystallographic refinement against the XDS-processed diffraction data set using PHENIX vl.3b (Adams et al., 2002). A total of fourteen rigid body domains were defined for this purpose (i) chain E and residues 4-191, (ii) chain E and residues 192-311, (iii) chain E and residues 312-464, (iv) chain E and residues 465- 594, (v) chain E and residues 595-817, (vi) chain E and residues 818-909, (vii) chain A and residues 1-112, (viii) chain B and residues 1-109, (ix) chain A and residues 1 13-220, (x) chain B and residues 1 10-219, (xi) chain C and residues 1-109, (xii) chain C and residues 110-207, (xiii) chain D and residues 1-106, (xiv) chain D and residues 107-214}. Rigid body refinement was then followed by atomic coordinate refinement and finally by TLS (translation, libration and screw-rotation displacement) refinement, using default protocols within PHENIX. A σ A -weighted 2F O -F C difference electron map was then calculated using structure factors whose amplitudes had been artificially inflated by the application of a B value (-153 A 2 ) equal to the negative of that determined by a Wilson plot (Briinger et al., 2009). The map was then visually inspected using O vl2.0 (Jones, 2004). At this stage the segment of electron density previously discerned on the Ll-β2 face of IR (WO 07/147213) had a surprisingly clear helical conformation with sufficient variation in side chain electron density to suggest that sequence assignment was possible (see below). O was then used for all subsequent model building of the IR segment 693- 710, with model building being iterated with crystallographic refinement within PHENIX. Final crystallographic refinement statistics are shown in Table 5.

2.4 Assigning structure to the C-terminal region of the IR a-chain

Following the refinement protocol detailed above, sequence assignment to the C- terminal region of the IR α-chain was possible and based on the following observations (i) the segment Glu698 to Tyr708 was the only region of the insert domain predicted to have helix-forming propensity (Ward and Lawrence, 2009), (ii) inspection of the density at the side-chain positions i, i+4 and i+7 showed that they likely arose from three large (most likely aromatic) residues, that these could in all likelihood be used to define the sequence register, and that the discerned helix would then span residues i-8 to i+9, (iii) the direction of the polypeptide chain within the helix was readily apparent from helical "tree" averaging of the difference electron density (Jones, 2004), and (iv) the only possible assignment of the sequence to the i, i+4, i+7 all-aromatic motif of (ii) above was to associate these residues with Phe701, Phe705 and Tyr708, respectively. Table 5 - Data processing and crystallographic refinement statistics from IR ectodomain crystal IR IRΔβ data processed using XDS.

Data processing

Space group C222,

Cell dimensions a, b, c (A) 123.03, 318.65, 204.64

Resolution (A) 30.64 (3.80)*

Λsym 14.6 (198.9)

11 ol 0.96

Completeness (%) 93.8 (93.4)

Redundancy 5.47 (5.35)

Refinement

Resolution (A) 30.64 - 3.80

No. reflections 39268

^work / ^free 0.225 / 0.289

No. atoms

Protein 13041

Z?-factors

Protein (A 2 ) 180.68

R.m.s. deviations

Bond lengths (A) 0.011

Bond angles (°) 1.558

*Values in parentheses are for highest-resolution shell. Data were collected from a single crystal.

The observed helical region of density spanned IR residues 693 to 710 (SEQ ID NO: 13; Figure 6). The direction of the polypeptide was consistent with having the inter-monomer disulphide bond-forming triplet Cys682 / Cys683 / Cys685 (Sparrow et al., 1997) in close proximity to the ectodomain two-fold axis (McKern et al., 2006). Subsequent model-building of insulin receptor residues 693-710 (SEQ ID NO: 13) into the difference electron density further supported the correctness of the sequence register assignment by virtue of the shape and electrostatic complementarity of the packing at the interface between Ll and the helical segment.

The side-chains of Phe701 and Phe705 pack adjacent to each other into a hydrophobic pocket formed by the side-chains of the Ll residues Phe64, Phe88, Phe96, Tyr91 and Arg 118 (Figure 6b). The side-chain of Tyr708 is packed approximately parallel to the surface and interacts with the Ll residues Leu62, Gln34 and Phe64. The side-chains of the residue pair Glu698 and Arg702 lie in close proximity and are juxtaposed against the side chains of the Ll residue pair Argl 18 and Asp 120 respectively, the four side chains forming a symmetric charge-compensating cluster. The final interaction between the helix and the surface of the central b-sheet of Ll arises from an interaction between the side chain of Leu709 with the side chains of the Ll residues Leu37 and Phe64. On the opposite surface of the helix side chains of the residue pair Lys703 and Asp707 are in proximity to each other and also likely charge compensate. Further crystallographic refinement of the (IR + Fab 83-7 + Fab 83-14) structure, now inclusive of IR residues 693-710, lead to a reduction of 0.5% in the free R-factor. The shape complementarity (Lawrence and Colman, 1993) of the interface between the insulin receptor residues 693-710 and the Ll domain of the receptor, computed after crystallographic refinement, is high (0.72). Taken together, these results gave overwhelming support to the correctness of the assignment of sequence to the helical density segment.

The structure provided herein (Appendix I) enables, for the first time, a view of the intact low affinity insulin receptor binding site that includes the critically-important C- terminal region of the receptor α-chain (SEQ ID NO: 13). The atomic coordinates of IR + Fab 83-7 + Fab 83-14 inclusive of the helical segment are now included in Appendix I and are depicted in Figure 6. The modelled helical segment of the IR α-chain (residues 693- 710, herein termed 'the C-terminal region of the α-chain of IR'; LKELEESSFRKTFEDYLH; SEQ ID NO: 13) surprisingly encompasses residues N- terminal . of the "classical" αCT peptide of IR (residues 704-719; TFEDYLHNVVFVPRPS; SEQ ID NO: 11) described previously in the literature (Kurose et al., 1994; Figure 6c). The original demarcation of this segment arose from a tryptic digest aimed at isolating receptor segments that were experimentally cross-linked to bound insulin. Tryptic cleavage at Lys703 resulted in the isolation of the segment 704-719 crosslinked to insulin. The involvement of residues immediately N-terminal of 704 in both the formation of the low affinity insulin binding site and in attachment of α-chain C- terminus to the first three domains of the receptor had not been contemplated previously.

Example 3: Molecular modelling 3.1 Introduction

There is a high level of sequence identity between, on the one hand, the Ll domains of IGF-IR and IR, and, on the other hand, between the C-terminal regions of the α-chain of IGF-IR and IR (Figure 1 and Figure 6c). Accordingly, models of IR in complex with S519C16 and the IGF-IR α-chain residues 681-697, respectively, were constructed using the MODELLER program (SaIi and Blundell, 1993) with the crystallographic structure of IR ectodomain presented in the main text as a template. Models of the.ectodomain of IGF- IR in complex, respectively, with the IGF-IR α-chain residues 681-697 (SEQ ID NO: 15), S519C16 (SEQ ID NO: 18) and the IR α-chain residues 693-710 (SEQ ID NO: 13) were constructed employing the crystal structure of the first three domains of IGF-IR (Garrett et al., 1998), the structure of the IR ectodomain presented here and the known sequence relationship between IR and IGF-IR (Adams et al., 2000).

3.2 Materials and methods for modelling

Twenty-five instances of each model were prepared and the structure with lowest DOPE score (Eramian et al., 2006) selected for further molecular dynamics (MD) simulation. The Ll -domains of IR and IGF-IR, residues Pro4-Glnl89 and residues GIu 1- GIn 189, respectively, in complex with the various peptides were excised from the full- length models prepared by MODELLER for use in the MD calculations. MD simulations were performed using the GROMACS v4.0 suite (van der Spoel et al., 2005) with the OPLS-aa force field (Jorgensen and Tirado-Rives, 1988). The proteins were solvated in a box of water and the total charge of the system neutralized by replacing water molecules with sodium ions. The LINCS algorithm was used to constrain bond lengths (Hess et al., 1977). Protein and solvent (including ions) were coupled separately to a thermal bath at 300 K using velocity rescaling (Bussi et al., 2007) applied with a coupling time of 0.1 ps. All simulations were performed with a single non-bonded cutoff of 10 A, applying a neighbour-list update frequency of 10 steps (20 fs). The particle mesh Ewald method was applied to deal with long-range electrostatics with a grid width of 1.2 A and fourth-order spline interpolation. All simulations consisted of an initial minimization to remove close contacts, followed by 100 ps of positional restrained MD to equilibrate the water molecules with the protein fixed. The time step used in all the simulations was 2 fs. MD simulations for each system were run for a total length of 2.0 ns.

3.3 Molecular models

The following models were created using MODELLER and subjected to MD simulations as described above: the C-terminal region of IR α-chain (SEQ ID NO: 13) bound to the Ll domain of IGF-IR (Appendix II; Figure 7), the C-terminal region of IGF-IR α-chain (SEQ ID NO: 15) bound to the Ll domain of IR (Appendix III; Figure 8), the C-terminal region of IGF-IR α-chain (SEQ ID NO: 15) bound to the Ll domain of IGF-IR (Appendix IV; Figure 9),

S519C16 mimetic peptide (SEQ ID NO: 18) bound to the Ll domain of IR (Appendix V; Figure 10), and S519C16 mimetic peptide (SEQ ID NO: 18) bound to the Ll domain of IGF-IR (Appendix VI; Figure 11).

The above models are presented schematically in Figures 7 to 11, with coordinates in Appendixes II to VI, respectively. These models define a common binding surface on IR and IGF-IR capable of binding the C-terminal region of the α-chain of the receptors. The following interactions were observed:

(i) IGF-1R/IR a-chain residues 693-710 (Figure 7): This interaction is characterized by several polar and ionic interactions - Y83 of the receptor hydrogen bonds the hydroxyl side-chains of S700 and T704 of the ligand, and E698 and R702 of the ligand form salt bridges with Rl 12 and El 14 of the receptor, respectively. Hydrophobic residues on the ligand pack into a hydrophobic pocket on the receptor formed by in part by L32, L33, L56, F58, F82, Y83, Y85, V88 and F90.

(H) IR/IGF-IR a-chain residues 681-697 (Figure 8): The complex between IR and the IGF-IR α-chain (residues 681-697) consists of charged interactions between Rl 18 and E 120 of IR, and E685 and Y688 of the peptide, respectively - the latter of these interactions can be mediated by a water molecule. There are a large • number of hydrophobic residues on IR that contact the peptide, formed in part by L36, L37, L62, F64, F88, F89, Y91, V94 and F96.

(Hi) IGF-IR/IGF-IR a-chain residues 681-697 (Figure 9): This interaction is characterized by a salt bridge between Rl 12 of the receptor and E685 of the peptide. Additionally, the hydroxy group on the side-chain of Y688 in hydrogen bonded to a water molecule (not shown) that is itself hydrogen bonded to El 14 of the receptor. The hydrophobic resides Y688, F 192, F 195 and L 196 pack into the hydrophobic pocket on the surface of the receptor formed in part by the side-chains of L32, L56, F58, F82, Y83, Y85, V88 and F90.

(iv) IR/S519C16 (Figure W): Throughout the MD simulation of the complex between IR (Ll domain) and the S519C16 peptide several hydrogen-bond interactions are observed - between Rl 19 of IR and D4 of the peptide, between El 20 of IR and Y8 of the peptide, and between Q14 of the peptide with both residues Rl 4 and Q34 of- IR. The interaction between receptor and peptide involves the aromatic side-chains of several residues - F7 and Fl 1 of the peptide bind a pocket on the surface of IR flanked by the residues L62, F64, F88, F89, Y91 and F96. Additionally, Ll 5 of the peptide packs against the hydrophobic side-chains of L37 and F64.

(v) IGF-1R/S519C16 (Figure U): D4 and Y8 of the peptide hydrogen bonds Rl 12 and El 14 of the receptor, respectively. The aromatic side-chains of F7 and FI l of the peptide bind the hydrophobic pocket on the receptor formed by L56, F58, F82, Y83, V88 and F90. WlO of the peptide can conceivably contact the hydrophobic side-chains of L32 and F82, increasing its affinity.

The models presented herein can now be used to improve the insulin mimetic peptides developed by Schaffer and co-workers (Schaffer et al., 2003). Isothermal titration calorimetry experiments (see Example 1 above) indicated that a prototypical Site 1 mimetic peptide S519C16 competes with the IR C-terminal peptide 704-719 in binding to a construct consisting of the first three domains of the insulin receptor. The two major residues involved in the interaction between the C-terminal segment of the insulin receptor α-chain and the Ll domain (viz. Phe701 and Phe705) are conserved in S519C16 (Figure 3) . . Of the remaining residues involved in the interaction between the C-terminus of the α-chain and Ll, Tyr708 is replaced with an asparagine residue in S519C16, Glu698 is either conserved or replaced by an aspartate residue, Arg702 is replaced by a tyrosine residue and Leu709 is conserved. The two phenylalanine residues form part of the motif FYXWF (SEQ ID NO: 19) that characterizes the Site 1 mimetic peptides (Schaffer et al., 2003). Modelling undertaken with MODELLER and subsequent MD showed that it is possible to dock the S519C16 peptide onto the Ll surfaces of IR and IGF-IR in a way analogous to the docking of cognate peptides (see Figures 6-11).

Example 4: Binding of mutant αCT peptides to an insulin mini-receptor (IR485 construct)

4.1 Introduction

Insulin-mimetic peptides have been discovered by phage display technology and classified as "Site" 1, 2 or 3 on the basis of competition of binding to insulin receptor (Pillutla et al, 2002). The affinity-matured Site 1 peptides are characterized by a FYXWF motif (SEQ ID NO: 19) (Pillutla et al, 2002); selected Site 1 and 2 peptides have been covalently tethered to yield agonists with up to picomolar affinity for insulin receptor (Schaffer et al, 2003). A sequence relationship has been shown (see Figure 6c) between the αCT region and the prototypic Site 1 mimetic peptide that places the αCT region residues Phe701 and Phe705 in respective alignment with the two flanking phenylalanine residues in the FYXWF motif. This relationship was used to explain the competitive binding of the αCT peptide and the prototypic Site 1 mimetic peptide to the insulin mini- receptor IR485, a construct which consists of the receptor L1-CR-L2 domains only. If this relationship was correct, then mutation of Arg702 and/or Thr704 within the αCT segment to either tyrosine or tryptophan would lead to significantly higher affinity of the segment for the insulin mini-receptor. It would also then be possible to model these substitutions directly onto the structure reported here. These hypotheses were tested as follows.

4.2 Materials and methods for thermodynamic experiments

Biotinylated αCT peptides at >75 % purity spanning residues 698-719 of the insulin receptor were obtained from Genscript Inc. (USA). The insulin mini-receptor IR485 construct was produced and purified as previously described (Lou et al., 2006), omitting the final ion-exchange chromatography step. Isothermal titration calorimetry (ITC) experiments were performed using a VP-ITC isothermal titration calorimeter (MicroCal Inc., USA) with the calorimeter cell held at about 25° C. The ITC cell contained insulin mini-receptor IR485 prepared at about 10 μM concentration in Tris-buffered saline plus azide (TBSA; about 24.8 mM Tris-HCl (pH 8.0), 137 mM NaCl, 2.7 mM KCl, and 0.02% sodium azide), and the syringe contained the peptide prepared at about 60 μM concentration in TBSA. All samples were degassed prior to injection or placement into the cell, and the instrument was temperature equilibrated prior to the start of the injections.

In all experiments the volume of the insulin mini-receptor IR485 sample placed in the cell was about 1.4 ml and the titrant was injected in about 7 μl volumes over 14 s at 3 min intervals, with the total number of injections being 40. The sample contents were stirred at a speed of about 310 rpm over the duration of the titration. All titrants were first injected into a solution of TBSA alone in order ascertain the heat of dilution, which was then subtracted from the data of interest as appropriate. Each experiment was performed three times, except for that employing the native peptide, which was performed twice. Data were analyzed using the instrument's software incorporated within the Origin 7 software (OriginLab, USA) and in all cases fitted as a single-site interaction using the methodologies outlined in the instrument's manual.

4.3 Results from thermodynamic experiments

Sample individual titration curves are provided in Figure 12. Table 6 below presents ITC-derived dissociation constants and thermodynamic parameters for a set of mutant αCT peptides titrated against the insulin mini-receptor IR485. Table 6 - Derived thermodynamic parameters for the titration against IR485 of the N- terminally biotinylated IR peptide 698-719 containing the following respective mutations: wild-type, T704 . Y, R702W, R702Y, T704W and R702Y / T704W.

Titrant peptide * K d peptide Mf T\S° AG"

(nM) (kJ mol "1 ) (kJ mol 1 ) (kJ mol "1 )

Wt 1340 ± 230 T -48 ± 1 -14 ± 1 -33.5 ± 0.4

T704Y 740 ± 210 -46 ± 9 -11 ± 9 -35. ± 0.7

R702W 309 ± 36 -35 ± 5 -3 ± 5 -37.2 ± 0.3

R702Y 249 ± 3 -50 ± 3 ' -12 ± 2 -37.67 ± 0.03

T704W 201 ± 16 -26 ± 2 11 ± 2 -38.2 ± 0.2

R702Y / T704W 18 ± 3 -49 ± 2 -5 ± 2 -44.2 ± 0.4 αCT peptides span residues 698-719 and have a biotin moiety attached at the N- terminus.

* Error estimates are the standard error of the mean.

Progressive inclusion of aromatic residues at positions 702 and 704 is seen to result in an up to 100-fold increase in affinity, supporting the view that there is a structural relationship between the Site- 1 mimetic peptides and the native αCT segment. The docking of the single- and double-mutant αCT peptides to the surface of the Ll domain was investigated by molecular dynamics simulation using the GROMACS v4.0 suite (van der Spoel et al, 2005) with the OPLS-aa force field (Jorgensen et al, 1988) and revealed that the aromatic side chains of mutant αCT residues Trp702 and Tyr704 are likely to interact with the surface of the L 1 domain and enhance the affinity of the interaction. At position 702 the aromatic side chain is docked into a pocket formed by the Phe96 and the alkyl portion of Ll side-chain Lysl21; the hydroxyl group of a variant tyrosine residue can in addition form a hydrogen bond with the Lysl21 ε-amino group. At position 704 the aromatic side chain of the variants is docked against Ll side chains Phe88 and Phe89. It will be appreciated by persons skilled in the art that numerous variations and/or modifications may be made to the invention as shown in the specific embodiments without departing from the spirit or scope of the invention as broadly described. The present embodiments are, therefore, to be considered in all respects as illustrative and not restrictive.

This application claims priority from US 61/214,472 filed 22 April 2009, the entire contents of whioch are incorporated herein by reference.

All publications discussed and/or referenced herein are incorporated herein in their entirety.

Any discussion of documents, acts, materials, devices, articles or the like which has been included in the present specification is solely for the purpose of providing a context for the present invention. It is not to be taken as an admission that any or all of these matters form part of the prior art base or were common general knowledge in the field relevant to the present invention as it existed before the priority date of each claim of this application.

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APPENDIX I : ATOMIC COORDINATES FOR IRΔβ MONOMER (CHAIN CONTAINING THE C-TERMINAL REGION OF THE IR α-CHAIN (CHAE WITH ATTACHED Fab 83-7 (CHAINS A AND B) AND Fab 83-14 (CHAIlS AND D)

Note: The coordinates in this Appendix describe the asymmetric unit of the cη unit cell. The coordinates of the dimeric form of the above are generated by tr application of the appropriate crystallographic two-fold operation, and these coordinates are hence included implicitly in this Appendix.

CRYSTl 123 .030 318 .650 204.640 90.00 90.00 90.00 C 2 2 21

SCALEl 0.008128 -0. 000000 -0.000000 0.00000

SCALE2 0.000000 0. 003138 -0.000000 0.00000

SCALE3 0.000000 0. 000000 0.004887 0.00000

ATOM 1 N GLN A 1 48.566 131.102 0.611 1.00203.59 N

ANISOU 1 N GLN A 1 28786 25452 23117 -3630 1876 -631 N

ATOM 2 CA GLN A 1 49.363 130.177 1.395 1.00203.76 C

ANISOU 2 CA GLN A 1 28682 25628 23108 -3812 1622 -502 C

ATOM 3 C GLN A 1 49.121 128.735 0.964 1.00199.48 C

ANISOU 3 C GLN A 1 27804 25158 '22830 -3613 ' 1501 -399 C

ATOM 4 O GLN A 1 50.044 127.931 1.012 1.00198.80 O

ANISOU 4 O GLN A 1 27516 25207 22813 -3698 1267 -283 O

ATOM 5 CB GLN A 1 49.056 130.326 2.884 1.00221.32 C

ANISOU 5 CB GLN A 1 31227 27827 25036 -4070 1653 -480 C

ATOM 6 CG GLN A 1 49.113 131.756 3.412 1.00234.00 C

ANISOU 6 CG GLN A 1 33230 29310 26369 -4237 1847 -603 C

ATOM 7 CD GLN A 1 48.474 131.910 4.799 1.00247.36 C

ANISOU 7 CD GLN A 1 35282 30892 27812 -4369 2024 -623 C

ATOM 8 OEl GLN A 1 47.989 130.941 5.397 1.00249.66 O

ANISOU 8 OEl GLN A 1 35541 31220 28097 -4390 1965 -533 O

ATOM 9 NE2 GLN A 1 48.472 133.137 5.310 1.00244.43 N

ANISOU 9 NE2 GLN A 1 35269 30371 27231 -4460 _ 2259 -745 N

ATOM 10 N VAL A 2 - 47.888 128.401 0.567 1.00162.79 N

ANISOU 10 N VAL A 2 23099 20418 18337 -3357 1659 -433 N

ATOM 11 CA VAL A 2 47.570 127.052 0.052 1.00151.02 C

ANISOU 11 CA VAL A 2 21285 18979 17117 -3146 1561 -354 C

ATOM 12 CB VAL A 2 46.352 126.406 0.734 1.00144.90 C

ANISOU 12 CB VAL A 2 20546 18137 16371 -3039 1679. -324 C

ATOM 13 CGl VAL A 2 45.615 125.495 -0.233 1.00134.23 C

ANISOU 13 CGl VAL A 2 18925 16765 15311 -2753 1689 -313 C

ATOM 14 CG2 VAL A 2 46.800 125.608 1.930 1.00147.72 C

ANISOU 14 CG2 VAL A 2 20900 18585 16641 -3205 1527 -201 C

ATOM 15 C VAL A 2 47.265 127.089 -1.421 1.00151.62 C

ANISOU 15 C VAL A 2 21189 19011 17409 -2908 1613 -420 C

ATOM 16 O VAL A 2 46.531 127.966 -1.867 1.00153.80 O

ANISOU 16 O VAL A 2 21604 191.63 17669 -2800 1807 -517 O

ATOM 17 N GLN A 3 47.798 126.123 -2.168 1.00162.78 N

ANISOU 17 N GLN A 3 22310 20515 19024 -2827 1444 -364 N

ATOM 18 CA GLN A 3 47.741 126.166 -3.626 1.00163.31 C

ANISOU 18 CA GLN A 3 22235 20543 19271 -2637 1475 -427 C

ATOM 19 CB GLN A 3 48.652 127.286 -4.115 1.00172.63 C

ANISOU 19 CB GLN A 3 23538 21715 20339 -2751 1503 -511 C

ATOM 20 CG GLN A- 3 49.795 127.571 -3.127 1.00176.66 C

ANISOU 20 CG GLN A 3 24102 22332 20687 -3031 1366 -459 C

ATOM 21 CD GLN A 3 50.800 128.595 -3.629 1.00179.12 C

ANISOU 21 CD GLN A 3 24497 22646 20916 -3150 1378 -534 C

ATOM 22 OEl GLN A 3 50.881 128.872 -4.831 1.00181.01 O

ANISOU 22 OEl GLN A 3 24703 22824 21250 -3012 1460 -614 O

ATOM 23 NE2 GLN A 3 51.585 129.154 -2.705 1.00173.97 N

ANISOU 23 NE2 GLN A 3 23959 22062 20078 -3420 1288 -504 N

ATOM 24 C GLN A 3 48.181 124.841 -4.227 1.00156.26 C

ANISOU 24 C GLN A 3 21021 19736 18615 -2534 1309 -347 C

ATOM 25 O GLN A 3 48.867 124.063 -3.570 1.00150.84 O

ANISOU 25 O GLN A 3 20214 19152 17915 -2637 1151 -240 O

ATOM 26 N LEU A 4 47.795 124.595 -5.478 1.00163.88 N

ANISOU 26 N LEU A 4 21860 20649 19757 -2336 1346 -393 N

ATOM 27 CA LEU A 4 48.052 123.312 -6.144 1.00161.52 C

ANISOU 27 CA LEU A 4 21283 20398 19690 -2212 1228 -331 C

ATOM 28 CB LEU A 4 46.776 122.455 -6.111 1.00158.01 C ANISOU 28 CB LEU A 4 20767 19907 19364 -2048 1258 -292 C

ATOM 29 CG LEU A 4 46.255 121.705 -4.876 1.00153 .77 C

ANISOU 29 CG LEU A 4 20257 19393 18775 -2097 1243 -207 C

ATOM 30 CDl LEU A 4 46.483 122.454 -3.595 1.00161 .42 C

ANISOU 30 CDl LEU A 4 21496 20335 19502 -2250 1347 -235 C

ATOM 31 CD2 LEU A 4 44.779 121.415 -5.033 1.00147 .78 C

ANISOU 31 CD2 LEU A 4 19418 18564 18166 -1903 1305 -197 C

ATOM 32 C LEU A 4 48.498 123.474 -7.613 1.00156 .90 C

ANISOU 32 C LEU A 4 20612 19778 19226 -2107 1245 -402 C

ATOM 33 O LEU A 4 47.804 124.093 -8.414 1.00155 02 O

ANISOU 33 O LEU A 4 20464 19439 18996 -1987 1357 -485 O

ATOM 34 N LYS A 5 49.639 122.909 -7.987 1.00139 46 N

ANISOU 34 N LYS A 5 18230 17643 17117 -2151 1138 -363 N

ATOM 35 CA LYS A 5 50.027 122.951 -9.398 1.00143 17 C

ANISOU 35 CA LYS A 5 18622 18068 17708 -2050 1170 -429 C

ATOM 36 CB LYS A 5 51.336 123.720 -9.596 1.00154 23 C

ANISOU 36 CB LYS A 5 20062 19505 ' 19034 -2197 1173 -471 C

ATOM 37 CG LYS A 5 51.145 125.184 -9.973 1.00159. 82 C

ANISOU 37 CG LYS A 5 21041. 20146 19538 -2268 1295 -575 C

ATOM 38 CD LYS A 5 52.465 125.955 -10.027 1.00162. 82 C

ANISOU 38 CD LYS A 5 21467 20576 19823 -2457 1283 -603 C

ATOM 39 CE LYS A 5 52.203 127.459 -9.966 1.00166. .65 C

ANISOU 39 CE LYS A 5 22244 21015 20060 -2588 1377 -673 C

ATOM 40 NZ LYS A 5 53.429 128.272 -9.749 1.00162. 97 N

ANISOU 40 NZ LYS A 5 21845 20589 19488 -2785 1370 -706 N

ATOM 41 C LYS A 5 50.131 121.561 -10.020 1.00138. 54 C

ANISOU 41 C LYS A 5 17790 17498 17350 -1928 1092 -367 C

ATOM 42 O LYS A 5 50.503 120.604 -9.354 '1.00135. 96 O

ANISOU 42 O LYS A 5 17305 17252 17102 -1973 981 -259 O

ATOM 43 N GLU A 6 49.814 121.448 -11.302 1.00144. 77 N

ANISOU 43 N GLU A 6 18562 18202 18241 -1780 1152 -432 N

ATOM 44 CA GLU A 6 49.802 120.143 -11.943 1.00139. 87 C

ANISOU 44 CA GLU A 6 17751 ' 17567 17826 -1657 1105 -392 C

ATOM 45 CB GLU A 6 48.448 119.894 -12.598 1.00140. 81 C

ANISOU 45 CB GLU A 6 17916 17590 17996 -1497 1146 -427 C

ATOM 46 CG GLU A 6 47.261 119.986 -11.659 1.00137. 92 C

ANISOU 46 CG GLU A 6 17655 17212 17536 -1484 1171 -407 C

ATOM 47 CD GLU A 6 46.606 121.345 -11.685 1.00140. 65 C

ANISOU 47 CD GLU A 6 18218 17491 17731 -1497 1278 -495 C

ATOM 48 OEl GLU A 6 47.314 122.332 -11.981 1.00147. 48 O

ANISOU 48 OEl GLU A 6 19160 18338 18537 -1545 1318 -566 O

ATOM 49 0E2 GLU A 6 45.387 121.422 -11.415 1.00134. .47 O

ANISOU 49 0E2 GLU A 6 17528 16667 16898 -1457 1334 -491 O

ATOM 50 C GLU A 6 50.886 120.030 -12.995 1.00141. 57 C

ANISOU 50 C GLU A 6 17893 17767 18131 -1659 1132 -436 C

ATOM 51 O GLU A 6 50.866 120.766 -13.978 1.00141. 21 O

ANISOU 51 O GLU A 6 17971 17645 18038 -1628 1219 -537 O

ATOM 52 N SER A 7 51.819 119.101 -12.803 1.00142. 17 N

ANISOU 52 N SER A 7 17768 17908 18341 -1694 1063 -354 N

ATOM 53 CA SER A 7 52.899 118.894 -13.768 1.00143. 65 C

ANISOU 53 CA SER A 7 17854 18075 18650 -1689 1108 -382 C

ATOM 54 CB SER A 7 54.186 118.455 -13.059 1.00143. 77 C

ANISOU 54 CB SER A 7 17664 18196 18766 -1794 1020 -267 C

ATOM 55 OG SER A 7 54.512 119.307 -11.970 1.00145. 01 O

ANISOU 55 OG SER A 7 17881 18448 18767 -1951 937 -213 O

ATOM 56 C SER A 7 52.507 117.846 -14.803 1.00142. 90 C

ANISOU 56 C SER A 7 17683 17890 18723 -1530 1144 -398 C

ATOM 57 O SER A 7 52.673 116.652 -14.565 1.00140. 32 O

ANISOU 57 O SER A 7 17182 17582 18552 -1476 1084 -307 O

ATOM 58 N GLY A 8 51.991 118.294 -15.946 1.00153. 79 N

ANISOU 58 N GLY A 8 19205 19164 20063 -1463 1238 -511 N

ATOM 59 CA GLY A 8 51.546 117.390 -16.994 1.00154 ' . 59 C

ANISOU 59 CA GLY A 8 19278 19166 20295 -1334 1272 -537 C

ATOM 60 C GLY A 8 52.532 117.330 -18.140 1.00161. 24 C

ANISOU 60 C GLY A 8 20118 19938 21208 -1333 1382 -607 C

ATOM 61 O GLY A 8 53.448 118.137 ' -18.188 1.00172. 29 O

ANISOU 61 O GLY A 8 21550 21365 22547 -1429 1435 -643 O

ATOM 62 N PRO A 9 52.375 116.354 -19.051 1.00163. 10 N

ANISOU 62 N PRO A 9 20322 20077 21570 -1236 1425 -625 N

ATOM 63 CA PRO A 9 53.183 116.277 -20.273 1.00167. 27 C

ANISOU 63 CA PRO A 9 20887 20510 22157 -1230 1560 -705 C

ATOM 64 CB PRO A 9 53.213 114.773 -20.593 1.00162. 54 C

ANISOU 64 CB PRO A 9 20155 19847 21757 -1135 1577 -660 C

ATOM 65 CG PRO A 9 52.574 114.089 -19.436 1.00163. 50 C

ANISOU 65 CG PRO A 9 20135 20054 21935 -1105 1440 -542 C

ATOM 66 CD PRO A 9 51.656 115.098 -18.819 1.00161. 37 C

ANISOU 66 CD PRO A 9 19990 19845 21479 -1144 1356 -550 C ATOM 67 C PRO A 9 52.557 117.021 -21.452 1.00165.72 C

ANISOU 67 C PRO A 9 20948 20200 21818 -1217 1627 -829 C

ATOM 68 O PRO A 9 53.228 117.186 -22.470 1.00164.80 O

ANISOϋ 68 O PRO A 9 20900 20000 21715 -1235 1751 -904 O

ATOM 69 N GLY A 10 51.296 117.434 -21.326 1.00155.54 N

ANISOU 69 N GLY A 10 19795 18898 20407 -1185 1550 -843 N

ATOM 70 CA GLY A 10 50.625 118.212 -22.360 1.00153.16 C

ANISOU 70 CA GLY A 10 19733 18492 19968 -1175 1584 -938 C

ATOM 71 C GLY A 10 50.435 117.567 -23.733 1.00150.49 C

ANISOU 71 C GLY A 10 19501 18013 19665 -1130 1641 -1002 C

ATOM 72 O GLY A 10 49.576 117.997 -24.513 1.00144.13 O

ANISOU 72 O GLY A 10 18895 17119 18748 -1115 1622 -1057 O

ATOM 73 N LEU A 11 51.240 116.550 -24.038 1.00146.55 N

ANISOU 73 N LEU A 11 18882 17483 19317 -1113 1712 -991 N

ATOM 74 CA LEU A 11 51.115 115.802 -25.288 1.00146.14 C

ANISOU 74 CA LEU A 11 18941 17285 19301 -1078 1782 -1052 C

ATOM 75 CB LEU A 11 52.120 116.329 -26.315 1.00144.12 C

ANISOU 75 CB LEU A 11 18809 16946 19005 -1141 1954 -1149 C

ATOM 76 CG LEU A 11 51.753 116.183 -27.792 1.00145.79 C

ANISOU 76 CG LEU A 11 19290 16989 19115 -1149 2013 -1248 C

ATOM 77 CDl LEU A 11 52.996 115.873 -28.610 1.00149.38 C

ANISOU 77 CDl LEU A 11 19785 17340 19631 -1185 2226 -1321 C

ATOM 78 CD2 LEU A 11 50.710 115.101 -27.994 1.00146.40 C

ANISOU 78 CD2 LEU A 11 19404 16998 19222 -1085 1907 -1221 C

ATOM 79 C LEU A 11 51.353 114.302 -25.041 1.00151.84 C

ANISOU 79 C LEU A 11 19478 17994 20219 -1014 1784 -985 C

ATOM 80 O LEU A 11 52.442 113.905 -24.612 1.00152.47 O

ANISOU 80 O LEU A 11 19372 18114 20446 -1017 1858 -942 O

ATOM 81 N VAL A 12 50.337 113.476 -25.296 1.00147.34 N

ANISOU 81 N VAL A 12 18955 17365 19661 -958 1698 -969 N

ATOM 82 CA VAL A 12 50.473 112.027 -25.145 1.00147.61 C

ANISOU 82 CA VAL A 12 18851 17364 19869 -897 1703 -912 C

ATOM 83 CB VAL A 12 49.629 111.482 -23.990 1.00141.87 C

ANISOU 83 CB VAL Α 12 17986 16729 19188 -850 1540 -806 C

ATOM 84 CGl VAL A 12 50.254 110.217 -23.448 1.00143.08 C

ANISOU 84 CGl VAL A 12 17951 16873 19538 -794 1556 -728 C

ATOM 85 CG2 VAL A 12 49.504 112.502 -22.896 1.00143.56 C

ANISOU 85 CG2 VAL A 12 18105 17097 19343 -882 1468 -750 C

ATOM 86 C VAL A 12 49.998 111.317 -26.397 1.00149.68 C

ANISOU 86 C VAL A 12 19308 17454 20111 -889 1759 -990 C

ATOM 87 O VAL A 12 48.890 111.567 -26.871 1.00145.36 O

ANISOU 87 O VAL A 12 18953 16853 19426 -907 1676 -1030 O

ATOM 88 N ALA A 13 50.820 110.413 -26.916 1.00136.91 N

ANISOU 88 N ALA A 13 17647 15742 18632 -867 1900 -1004 N

ATOM 89 CA ALA A 13 50.494 109.709 -28.152 1.00133.28 C

ANISOU 89 CA ALA A 13 17395 15097 18148 -876 1987 -1087 C

ATOM 90 CB ALA A 13 51.745 109.095 -28.715 1.00137.84 C

ANISOU 90 CB ALA A 13 17922 15579 18871 -864 2215 -1119 C

ATOM 91 C ALA A 13 49.409 108.636 -27.971 1.00131.25 C

ANISOU 91 C ALA A 13 17147 14794 17928 -838 1866 -1043 C

ATOM 92 O ALA A 13 49.500 107.824 -27.057 1.00131.39 O

ANISOU 92 O ALA A 13 16959 14860 18104 -778 1834 -953 O

ATOM 93 N PRO A 14 48.403 108.605 -28.872 1.00136.95 N

ANISOU 93 N PRO A 14 18115 15414 18505 -882 1795 -1102 N

ATOM 94 CA PRO A 14 47.219 107.742 -28.738 1.00137.95 C

ANISOU 94 CA PRO A 14 18261 15514 18640 -868 1639 -1055 C

ATOM 95 CB PRO A 14 46.688 107.642,-30.165 1.00137.45 C

ANISOU 95 CB PRO A 14 18515 15280 18428 -946 1647 -1150 C

ATOM 96 CG PRO A 14 47.094 108.909 -30.786 1.00144.85 C

ANISOU 96 CG PRO A 14 19603 16209 19226 -999 1726 -1228 ; C

ATOM 97 CD PRO A 14 48.426 109.285 -30.177 1.00142.02 C

ANISOU 97 CD PRO A 14 19045 15934 18982 -961 1881 -1218 C

ATOM 98 C PRO A 14 47.549 106.362 -28.200 1.00142.15 C

ANISOU 98 C PRO A 14 18628 16018 19365 -807 1689 -996 C

ATOM 99 O PRO A 14 48.278 105.603 -28.828 1.00141.70 O

ANISOU 99 O PRO A 14 18653 15816 19369 -811 1849 -1049 O

ATOM 100 N SER A 15 46.987 106.050 -27.038 1.00157.83 N

ANISOU 100 N SER A 15 20396 18131 21442 ' -754 1561 -885 N

ATOM 101 CA SER A 15 47.338 104.852 -26.284 1.00159.80 C

ANISOU 101 CA SER A 15 20452 18379 21884 -689 1591 -804 C

ATOM 102 CB SER A 15 47.271 103.600 -27.158 1.00165.14 C

ANISOU 102 CB SER A 15 21272 18864 22611 -696 1680 -853 C

ATOM 103 OG SER A 15 45.946 103.094 -27.225 1.00167.53 O

ANISOU 103 OG SER A 15 21662 19133 22858 -723 1522 -834 O

ATOM 104 C SER A 15 48.722 105.014 -25.693 1.00155.87 C

ANISOU 104 C SER A 15 19758 17947 21518 -650 1716 -767 C

ATOM 105 O SER A 15 49.717 104.751 -26.362 1.00153.32 O ANISOU 105 O SER A 15 19473 17521 21260 -647 1902 -823 O

ATOM 106 N GLN A 16 48.777 105.459 -24.440 1.00155 .09 N

ANISOU 106 N GLN A 16 19451 18018 21458 -627 1613 -667 N

ATOM 107 CA GLN A 16 50.055 105.733 -23.797 1.00157 .48 C

ANISOU 107 CA GLN A 16 19554 18407 21876 -610 1688 -611 C

ATOM 108 CB GLN A 16 50.914 106.640 -24.689 1.00158 .35 C

ANISOU 108 CB GLN A 16 19766 18475 21925 -656 1838 -710 C

ATOM 109 CG GLN A 16 52.386 106.259 -24.739 1.00163 .00 C

ANISOU 109 CG GLN A 16 20185 19037 22709 -624 2003 -677 C

ATOM 110 CD GLN A 16 52.621 105.003 -25.547 1.00172 72 C

ANISOU 110 CD GLN A 16 21447 20088 24090 -565 2147 -695 C

ATOM 111 OEl GLN A 16 52.134 104.878 -26.667 1.00174 .26 O

ANISOU 111 OEl GLN A 16 21888 20131 24192 -590 2224 -803 O

ATOM 112 NE2 GLN A 16 53.366 104.063 -24.983 1.00178. 34 N

ANISOU 112 NE2 GLN A 16 21920 20808 25033 -493 2183 -583 N

ATOM 113 C GLN A 16 49.917 106.350 -22.402 1.00154 .34 C

ANISOU 113 C GLN A 16 18995 18199 21450 -620 1539 -512 C

ATOM 114 O GLN A 16- 48.940 107.031 -22.088 1.00151. 88 O

ANISOU 114 O GLN A 16 18754 17950 21003 -644 1415 -514 O

ATOM 115 N SER A 17 50.933 106.114 -21.583 1.00176. 41 N

ANISOU 115 N SER A 17 21576 21078 24374 -607 1558 -422 N

ATOM 116 CA SER A 17 50.943 106.547 -20.194 1.00180, 74 C

ANISOU 11 * 6 CA SER A 17 21978 21796 24900 -630 1415 -315 C

ATOM 117 CB SER A 17 52.183 105.997 -19.467 1.00195. 82 C

ANISOU 117 CB SER A 17 23636 23761 27005 -608 1424 -189 C

ATOM 118 OG ' SER A 17 53.340 106.016 -20.297 1.00204. 13 O

ANISOU 118 OG SER A 17 . 24645 24754 28160 -607 1582 -226 O

ATOM 119 C SER A 17 50.866 108.055 -20.024 1.00176. 01 C

ANISOU 119 C SER A 17 21459 21299 24118 -709 1378 -361 C

ATOM 120 O SER A 17 • 51.865 108.765 -20.128 1.00181. 01 O

ANISOU 120 O SER A 17 22053 21972 24752 -755 1445 -377 O

ATOM 121 N LEU A 18 49.669 108.550 -19.764 1.00135. 35 N

ANISOU 121 N LEU A 18 16420 16187 18821 -724 1279 -378 N

ATOM 122 CA LEU A 18 49.555 109.906 -19.261 1.00134. 26 C

ANISOU 122 CA LEU A 18 16329 16156 18528 -792 1236 -392 C

ATOM 123 CB LEU A 18 48.140 110.443 -19.421 1.00128. 93 C

ANISOU 123 CB LEU A 18 15806 15472 17711 -788 1166 -430 C

ATOM 124 CG LEU A 18 47.789 111.726 -18.682 1.00117. 54 C

ANISOU 124 CG LEU A 18 14427 14123 16110 -847 1136 -441 C

ATOM 125 CDl LEU A 18 48.661 112.869 -19.122 1.00119. .03 C

ANISOU 125 CDl LEU A 18 14697 14306 16222 -907 1227 -521 C

ATOM 126 CD2 LEU A 18 46.363 112.029 -18.974 1.00116. 12 C

ANISOU 126 CD2 LEU A 18 14376 13907 15837 -819 1084 -470 C

ATOM 127 C LEU A 18 49.858 109.816 -17.793 1.00129. 38 C

ANISOU 127 C LEU A 18 15531 15670 17957 -820 1151 -266 C

ATOM 128 O LEU A 18 49.180 109.083 -17.079 1.00129. 44 O

ANISOU 128 O LEU Ά 18 15448 15697 18036 -784 1074 -178 O

ATOM 129 N SER A 19 50.884 110.531 -17.345 1.00145. 62 N

ANISOU 129 N SER A 19 17544 17815 19970 -897 1162 -254 N

ATOM 130 CA SER A 19 51.143 110.668 --15.919 1.00144. 49 C

ANISOU 130 CA SER A 19 17265 17804 19830 -957 1062 -135 C

ATOM 131 CB SER A 19 52.508 110.098 -15.549 1.00146. 89 C

ANISOU 131 CB SER A 19 17357 18132 20322 -962 1073 -44 C

ATOM 132 OG SER A 19 52.673 108.796 -16.092 1.00147. 01 O

ANISOU 132 OG SER A 19 17296 18040 20521 -858 1125 -24 O

ATOM 133 C SER A 19 51.096 112.139 -15.618 1.00143. 79 C

ANISOU 133 C SER A 19 17292 17793 19548 -1059 1054 -182- C

ATOM 134 O SER A 19 51.546 112.937 -16.420 1.00152. 33 O

ANISOU 134 O SER A 19 18466 18841 20570 -1091 1140 -276 O

ATOM 135 N ILE A 20 50.513 112.514 -14.493 1.00125. 95 N

ANISOU 135 N ILE A 20 15053 15621 17180 -1113 965 -124 N

ATOM 136 CA ILE A 20 50.527 113.911 -14.100 1.00124. 86 C

ANISOU 136 CA ILE A 20 15048 15543 16851 -1215 971 -172 C

ATOM 137 CB ILE A 20 49.163 114.597 -14.238 1.00119. 14 C

ANISOU 137 CB ILE A 2Q 14508 14773 15988 -1179 993 -243 C

ATOM 138 CGl ILE A 20 48.639 114.525 -15.673 1.00111. 81 C

ANISOU 138 CGl ILE A 20 13679 13723 15080 -1094 1068 -348 C

ATOM 139 CDl ILE A 20 47.254 115.141 -15.838 1.00107. 95 C

ANISOU 139 CDl ILE A 20 13349 13189 14478 -1057 1075 -399 C

ATOM 140 CG2 ILE A 20 49.282 116.040 -13.824 1.00124. 52 C

ANISOU 140 CG2 ILE A 20 15329 15505 16479 -1284 1013 -282 C

ATOM 141 C ILE A 20 50.910 113'.927 -12.654 1.00123. 75 C

ANISOU 141 C ILE A 20 14830 15520 16670 -1315 869 -57 C

ATOM 142 O ILE A 20 50.687 112.954 -11.953 1.00124. 80 O

ANISOU 142 O ILE A 20 14859 15677 16884 -1285 791 44 O

ATOM 143 N THR A 21 51.497 115.021 -12.203 1.00126. 68 N

ANISOU 143 N THR A 21 15265 15960 16906 -1445 863 -70 N ATOM 144 CA THR A 21 51.886 115.108 -10.808 1.00131.04 C

ANISOU 144 CA THR A 21 15790 16621 17378 -1567 755 36 C

ATOM 145 CB THR A 21 53.405 114.848 -10.611 1.00133.44 C

ANISOϋ 145 CB THR A 21 15907 17008 17786 -1664 676 138 C

ATOM 146 OGl THR A 21 53.808 113.731 -11.414 1.00131.67 O

ANISOϋ 146 OGl THR A 21 15487 16735 17807 -1547 690 183 O

ATOM 147 CG2 THR A 21 53.722 114.539 -9.161 1.00133.83 C

ANISOU 147 CG2 THR A 21 15914 17162 17773 -1784 526 279 C

ATOM 148 C THR A 21 51.427 116.434 -10.200 1.00130.23 C

ANISOU 148 C THR A 21 15908 16539 17033 -1668 785 -27 C

ATOM 149 O THR A 21 51.862 117.520 -10.587 1.00131.83 O

ANISOU 149 O THR A 21 16220 16733 17135 -1732 851 -113 O

ATOM 150 N CYS A 22 50.506 116.322 -9.260 1.00135.61 N

ANISOU 150 N CYS A 22 16664 17234 17626 -1676 755 14 N

ATOM 151 CA CYS A 22 49.984 117.469 -8.560 1.00138.65 C

ANISOU 151 CA CYS A 22 17264 17628 17789 -1772 799 -32 C

ATOM 152 CB CYS A 22 48.508 117.237 -8.257 1.00137.94 C

ANISOU 152 CB CYS A 22 17259 17483 17670 -1682 846 -38 C

ATOM 153 SG CYS A 22 47.677 118.552 -7.357 1.00141.01 S

ANISOU 153 SG CYS A 22 17911 17858 17809 -1780 936 -82 S

ATOM 154 C CYS A 22 50.774 117.651 -7.270 1.00142.44 C

ANISOU 154 C CYS A 22 17741 18215 18166 -1960 692 65 C

ATOM 155 O CYS A 22 50.795 116.767 -6.418 1.00141.82 O

ANISOU 155 O CYS A 22 17557 18187 18140 -1983 585 186 O

ATOM 156 N THR A 23 51.437 118.797 -7.140 1.00138.85 N

ANISOU 156 N THR A 23 17406 17790 17559 -2105 712 17 N

ATOM 157 CA THR A 23 52.217 119.115 -5.947 1.00137.62 C

ANISOU 157 CA THR A 23 17282 17734 17274 -2316 599 106 C

ATOM 158 CB THR A 23 53.679 119.462 -6.300 1.00133.07 C

ANISOU 158 CB THR A 23 16584 17222 16754 -2424 533 130 C

ATOM 159 OGl THR A 23 53.977 119.018 -7.629 1.00131.26 O

ANISOU 159 OGl THR A 23 16181 16946 16747 -2267 585 96 O

ATOM 160 CG2 THR A 23 54.622 118.783 -5.337 1.00134.36 C

ANISOU 160 CG2 THR A 23 16600 17497 16953 -2566 340 300 C

ATOM 161 C THR A 23 51.558 120.260 -5.172 1.00137.81 C

ANISOU . 161 C THR A 23 17595 17736 17029 -2437 676 40 C

ATOM 162 O THR A 23 51.402 121.377 -5.671 1.00134.50 O

ANISOU 162 O THR A 23 17340 17259 16505 -2444 799 -81 O

ATOM 163 N VAL A 24 51.159 119.963 -3.947 1.00136.87 N

ANISOU 163 N VAL A 24 17552 17654 16799 -2535 613 124 N

ATOM 164 CA VAL A 24 50.366 120.895 -3.177 1.00142.52 C

ANISOU 164 CA VAL A 24 18552 18322 17278 -2619 721 66 C

ATOM 165 CB VAL A 24 49.114 120.213 -2.645 1.00139.97 C

ANISOU 165 CB VAL A 24 18247 17948 16986 -2502 774 96 C

ATOM 166 CGl VAL A 24 48.421 119.469 -3.771 1.00131.47 C

ANISOU 166 CGl VAL A 24 17037 16797 16118 -2255 853 42 C

ATOM 167 CG2 VAL A 24 49.481 119.269 -1.508 1.00138.84 C

ANISOU 167 CG2 VAL A 24 17976 17888 16888 -2573 603 253 C

ATOM 168 C VAL A 24 51.147 121.470 -2.009 1.00145.08 C

ANISOU 168 C VAL A 24 19022 18721 17380 -2890 623 128 C

ATOM 169 O VAL A 24 52.138 120.900 -1.573 1.00142.19 O

ANISOU 169 O VAL A 24 18510 18455 17061 -3003 435 257 O

ATOM 170 N SER A 25 50.667 122.591 -1.489 1.00138.45 N

ANISOU 170 N SER A 25 18480 17824 16302 -2997 752 42 - N

ATOM 171 CA SER A 25' 51.399 123.358 -0.502 1.00136.35 C

ANISOU 171 CA SER A 25 18410 17608 15787 -3278 680 75 C

ATOM 172 CB SER A 25 52.117 124.471 -1.216 1.00138.44 C

ANISOU 172 CB SER A 25 18724 17884 15991 -3381 693 -3 C

ATOM 173 OG SER A 25 51.148 125.424 -1.619 1.00140.92 O

ANISOU 173 OG SER A 25 19250 18075 16220 -3293 921 -156 O

ATOM 174 C SER A 25 50.439 124.044 0.434 1.00141.04 C

ANISOU 174 C SER A 25 19338 18111 16141 -3347 849 8 C

ATOM 175 O SER A 25 49.386 124.520 -0.003 1.00137.38 O

ANISOU 175 O SER A 25 18987 17532 15679 -3199 1059 -108 O

ATOM 176 N GLY A 26 50.818 124.135 1.707 1.00146.79 N

ANISOU 176 N GLY A 26 20230 18882 16661 -3579 762 85 N

ATOM 177 CA GLY A 26 50.074 124.931 2.669 1.00149.87 C

ANISOU 177 CA GLY A 26 20981 19176 16785 -3692 937 18 C

ATOM 178 C GLY A 26 49.183 124.153 3.620 1.00147.49 C

ANISOU 178 C GLY A 26 20741 18844 16455 -3664 976 84 C

ATOM 179 O GLY A 26 49.023 124.537 4.769 1.00151.65 O

ANISOU 179 O GLY A 26 21575 19312 16734 -3823 1078 65 O

ATOM 180 N PHE A 27 48.578 123.077 3.137 1.00154.40 N

ANISOU 180 N PHE A 27 21337 19749 17579 -3465 910 156 N

ATOM 181 CA PHE A 27 47.815 122.173 3.983 1.00151.48 C

ANISOU 181 CA PHE A 27 20982 19359 17216 -3429 928 233 C

ATOM 182 CB PHE A 27 46.398 122.023 3.436 1.00152.05 C ANISOU 182 CB PHE A 27 21013 19316 17442 -3161 1154 151 C

ATOM 183 CG PHE A 27 46.349 121.483 2.037 1.00147.57 C

ANISOU 183 CG PHE A 27 20135 18760 17173 -2915 1116 131 C

ATOM 184 CDl PHE A 27 46.273 120.124 1.808 1.00143.34 C

ANISOU 184 CDl PHE A 27 19320 18287 16857 -2802 965 235 C

ATOM 185 CEl PHE A 27 46.246 119.631 0.539 1.00138.62 C

ANISOU 185 CEl PHE A 27 18474 17685 16509 -2595 944 209 C

ATOM 186 CZ PHE A 27 46.294 120.488 -0.525 1.00139.63 C

ANISOU 186 CZ PHE A 27 18630 17754 16670 -2499 1060 . 86 C

ATOM 187 CE2 PHE A 27 46.368 121.842 -0.318 1.00143.38 C

ANISOU 187 CE2 PHE A 27 19368 18171 16940 -2599 1202 -11 C

ATOM 188 CD2 PHE A 27 46.398 122.335 0.954 1.00147.64 C

ANISOU 188 CD2 PHE A 27 20156 18707 17232 -2803 1237 8 C

ATOM 189 C PHE A 27 48.562 120.851 3.910 1.00150.81 C

ANISOU 189 C PHE A 27 20592 19391 17319 -3403 670 388 C

ATOM 190 O PHE A 27 49.437 120.708 3.065 1.00156.45 O

ANISOU 190 O PHE A 27 21065 20168 18210 -3336 550 406 O

ATOM 191 N PRO A 28 48.237 119.884 4.788 1.00130.01 N

ANISOU 191 N PRO A 28 17969 16775 14652 -3455 596 503 N

ATOM 192 CA PRO A 28 48.925 118.584 4.837 1.00132.14 C

ANISOU 192 CA PRO A 28 17954 17145 15109 -3426 352 664 C

ATOM 193 CB PRO A 28 48.863 118.219 6.318 1.00137.62 C

ANISOU 193 CB PRO A 28 18826 17859 15604 -3626 263 783 C

ATOM 194 CG PRO A 28 48.143 119.368 6.999 1.00146.20 C

ANISOU 194 CG PRO A 28 20310 18856 16384 -3777 471 672 C

ATOM 195 CD PRO A 28 47.364 120.057 5.948 1.00134.44 C

ANISOU 195 CD PRO A 28 18831 17267 14984 -3574 727 500 C

ATOM 196 C PRO A 28 48.203 117.497 4.059 1.00131.24 C

ANISOU 196 C PRO A 28 17595 16991 15281 -3139 414 660 C

ATOM 197 O PRO A 28 47.013 117.322 4.282 1.00129.44 O

ANISOU 197 O PRO A 28 17463 16675 15045 -3038 593 608 O

ATOM 198 N LEU A 29 48.901 116.768 3.189 1.00147.84 N

ANISOU 198 N LEU A 29 19389 19149 17634 -3017 276 716 N

ATOM 199 CA LEU A 29 48.249 115.746 2.365 1.00151.23 C

ANISOU 199 CA LEU A 29 19601 19532 18329 -2758 331 707 C

ATOM 200 CB LEU A 29 49.201 115.189 1.313 1.00147.81 C

ANISOU 200 CB LEU A 29 18868 19147 18146 -2649 205 744 C

ATOM 201 CG LEU A 29 49.138 115.871 -0.049 1.00136.98 C

ANISOU 201 CG LEU A 29 17455 17733 16860 -2527 324 599 C

ATOM 202 CDl LEU A 29 49.340 114.819 -1.105 1.00139.68 C

ANISOU 202 CDl LEU A 29 17506 18081 17485 -2362 255 635 C

ATOM 203 CD2 LEU A 29 47.811 116.569 -0.256 1.00130.74 C

ANISOU 203 CD2 LEU A 29 16812 16834 16028 -2403 545 464 C

ATOM 204 C LEU A 29 47.735 114.605 3.217 1.00157.49 C

ANISOU 204 C LEU A 29 20375 20319 19145 -2747 284 822 C

ATOM 205 O LEU A 29 46.810 113.874 2.831 1.00153.71 O

ANISOU 205 O LEU A 29 19821 19774 18807 -2567 388 797 O

ATOM 206 N THR A 30 48.367 114.469 4.376 1.00169.83 N

ANISOU 206 N THR A 30 22010 21952 20567 -2954 115 955 N

ATOM 207 CA THR A 30 48.037 113.468 5.376 1.00166.71 C

ANISOU 207 CA THR A 30 21639 21559 20146 -2996 44 1085 C

ATOM 208 CB THR A 30 48.853 113.731 6.638 1.00169.75 C

ANISOU 208 CB THR A 30 22175 22021 20302 -3282 -148 1217 C

ATOM 209 OGl THR A 30 48.026 114.390 7.605 1.00166.40 O

ANISOU 209 OGl THR A 30 22097 21537 19589 -3431 ' -4 1168 O

ATOM 210 CG2 THR A 30 50.049 114.620 6.314 1.00166.75 C

ANISOU 210 CG2 THR A 30 21770 21718 19870 -3417 -269 1208 C

ATOM 211 C THR A 30 46.581 113.530 5.809 1.00160.60 C

ANISOU 211 C THR A 30 21070 20685 19267 -2954 .274 1008 C

ATOM 212 O THR A 30 45.980 112.509 6.131 1.00160.76 O

ANISOU 212 O THR A 30 21021 20674 19385 -2866 286 1071 O

ATOM 213 N ALA A 31 46.029 114.741 5.823, 1.00143.09 N

ANISOU 213 N ALA A 31 19104 18410 16855 -3022 463 876 N

ATOM 214 CA ALA A 31 44.751 115.023 6.470 1.00137.87 C

ANISOU 214 CA ALA A 31 18655 17643 16086 -3001 706 807 C

ATOM 215 CB ALA A 31 44.988 115.851 7.710 1.00142.60 C

ANISOU 215 CB ALA A 31 19607 18229 16346 -3269 747 812 C

ATOM 216 C ALA A 31 43.766 115.741 5.559 1.00133.01 C

ANISOU 216 C ALA A 31 18037 16935 15564 -2815 943 646 C

ATOM 217 O ALA A 31 42.882 116.453 6.036 1.00130.62 O

ANISOU 217 O ALA A 31 17959 16540 15131 -2834 1171 563 O

ATOM 218 N TYR A 32 43.932 115.554 4.253 ' 1.00134.60 N

ANISOU 218 N TYR A 32 17994 17154 15992 -2640 893 607 N

ATOM 219 CA TYR A 32 43.083 116.187 3.256 1.00130.80 C

ANISOU 219 CA TYR A 32 17482 16588 15627 -2450 1081 475 C

ATOM 220 CB TYR A 32 43.648 117.551 2.843 1.00130.62 C

ANISOU 220 CB TYR A 32 17586 16558 15484 -2513 1134 366 C ATOM 221 CG TYR A 32 43.212 118.720 3.705 1.00132.56 C

ANISOU 221 CG TYR A 32 18166 16733 15468 -2657 1321 297 C

ATOM 222 CDl TYR A 32 43.933 119.089 4.830 1.00137 .96 C

ANISOU 222 CDl TYR A 32 19064 17464 15891 -2920 1242 339 C

ATOM 223 CEl TYR A 32 43.540 120.156 5.611 1.00135. .89 C

ANISOU 223 CEl TYR A 32 19140 17121 15372 -3064 1429 269 C

ATOM 224 CZ TYR A 32 42.418 120.868 5.267 1.00135 .34 C

ANISOU 224 CZ TYR A 32 19175 16920 15329 -2928 1710 162 C

ATOM 225 OH TYR A 32 42.019 121.936 6.038 1.00141 .22 O

ANISOU 225 OH TYR A 32 20265 17564 15828 -3063 1926 89 O

ATOM 226 CE2 TYR A 32 41.690 120.522 4.157 1.00131 57 C

ANISOU 226 CE2 TYR A 32 18462 16401 15128 -2660 1776 132 C

ATOM 227 CD2 TYR A 32 42.090 119.462 3.384 1.00129 65 C

ANISOU 227 CD2 TYR A 32 17904 16242 15115 -2536 1576 197 C

ATOM 228 C TYR A 32 42.991 115.304 2.032 1.00129. 06 C

ANISOU 228 C TYR A 32 16962 16373 15701 -2234 1009 486 C

ATOM 229 O TYR A 32 43.912 114.546 1.724 1.00128, 80 O

ANISOU 229 O TYR A 32 16743 16413 15783 -2230 819 577 O

ATOM 230 N GLY A 33 41.879 115.414 1.325 1.00128. 28 N

ANISOU 230 N GLY A 33 16824 16189 15726 -2056 1164 397 N

ATOM 231 CA GLY A 33 41.741 114.710 0.073 1.00129, 18 C

ANISOU 231 CA GLY A 33 16693 16294 16095 -1865 1106 390 C

ATOM 232 C GLY A 33 42.183 115.571 -1.090 1.00128. 30 C

ANISOU 232 C GLY A 33 16553 16171 16025 -1799 1117 288 C

ATOM 233 O GLY A 33 42.090 116.792 -1.038 1.00127. 36 O

ANISOU 233 O GLY A 33 16605 16013 15773 -1841 1235 201 O

ATOM 234 N VAL A 34 42.668 114.929 -2.144 1.00126. 48 N

ANISOU 234 N VAL A 34 16121 15963 15974 -1701 1003 298 N

ATOM 235 CA VAL A 34 42.961 115.626 -3.381 1.00123. 90 C

ANISOU 235 CA VAL A 34 15767 15610 15699 -1626 1025 200 C

ATOM 236 CB VAL A 34 44.450 115.617 -3.641 1.00121. 83 C

ANISOU 236 CB VAL A 34 15418 15425 15445 -1702 890 223 C

ATOM 237 CGl VAL A 34 44.755 116.361 -4.905 1.00124. 98 C

ANISOU 237 CGl VAL A 34 15854 15793 15839 -1665 944 111 C

ATOM 238 CG2 VAL A 34 45.162 116.252 -2.487 1.00125. 03 C

ANISOU 238 CG2 VAL A 34 15932 15907 15666 -1905 825 285 C

ATOM 239 C VAL A 34 42.256 114.930 -4.543 1.00126. 11 C

ANISOU 239 C VAL A 34 15895 15828 16192 -1438 1032 178 C

ATOM 240 O VAL A 34 42.587 113.790 -4.858 1.00125. 39 O

ANISOU 240 O VAL A 34 15636 15757 16248 -1387 925 238 O

ATOM 241 N ASN A 35 41.283 115.602 -5.163 1.00130. 48 N

ANISOU 241 N ASN A 35 16513 16299 16765 -1341 1153 100 N

ATOM 242 CA ASN A 35 40.520 115.035 -6.280 1.00125. 40 C

ANISOU 242 CA ASN A 35 15746 15593 16309 -1182 1145 82 C

ATOM 243 CB ASN A 35 39.145 115.691 -6.381 1.00126. 35 C

ANISOU 243 CB ASN A 35 15937 15627 16444 -1099 1280 46 C

ATOM 244 CG ASN A 35 38.160 115.142 -5.376 1.00133. 31 C

ANISOU 244 CG ASN A 35 16803 16496 17354 -1097 1340 117 C

ATOM 245 ODl ASN A 35 38.535 114.391 -4.483 1.00138. 24 O

ANISOU 245 ODl ASN A 35 17481 17171 17873 -1209 1337 170 O

ATOM 246 ND2 ASN A 35 36.888 115.516 -5.513 1.00133. 85 N

ANISOU 246 ND2 ASN A 35 16801 16493 17562 -978 1394 124 N

ATOM 247 C ASN A 35 41.227 115.241 -7.604 1.00126. 23 C

ANISOU 247 C ASN A 35 15816 15684 16462 -1138 1099 13 C

ATOM 248 O ASN A 35 42.261 115.892 -7.652 1.00132. 62 O

ANISOU 248 O ASN A 35 16700 16526 17163 -1220 1099 -30 O

ATOM 249 N TRP A 36 40.655 114.705 -8.680 1.00110. 82 N

ANISOU 249 N TRP A 36 13766 13676 .14663 -1020 1065 -1 N

ATOM 250 CA TRP A 36 41.111 114.996 -10.043 1.00108. 09 C

ANISOU 250 CA TRP A 36 13429 13293 14346 -977 1048 -79 C

ATOM 251 CB TRP A 36 41.923 113.843 -10.605 1.00105. 30 C

ANISOU 251 CB TRP A 36 12943 12954 14113 -959 954 -55 C

ATOM 252 CG TRP A 36 43.297 113.679 -10.080 1.00110. 39 C

ANISOU 252 CG TRP A 36 13538 13680 14725 -1054 904 -14 C

ATOM 253 CDl TRP A 36 43.713 112.763 -9.174 1.00112. 46 C

ANISOU 253 CDl TRP A 36 13696 14000 15035 -1093 833 87 C

ATOM 254 NEl TRP A 36 45.060 112.887 -8.952 1.00113. 32 N

ANISOU 254 NEl TRP A 36 13765 14178 15115 -1184 783 116 N

ATOM 255 CE2 TRP A 36 45.544 113.895 -9.738 1.00117. 07 C

ANISOU 255 CE2 TRP A 36 14322 14640 15520 -1208 835 22 C

ATOM 256 CD2 TRP A 36 44.460 114.413 -10.469 1.00116. 91 C

ANISOU 256 CD2 TRP A 36 14404 14537 15478 -1126 912 -63 C

ATOM 257 CE3 TRP A 36 44.690 115.471 -11.358 1.00116. 97 C

ANISOU 257 CE3 TRP A 36 14523 14510 15410 -1134 974 -164 C

ATOM 258 CZ3 TRP A 36 45.984 115.964 -11.491 1.00119. 85 C

ANISOU 258 CZ3 TRP A 36 14891 14924 15724 -1225 969 -184 C

ATOM 259 CH2 TRP A 36 47.041 115.425 -10.747 1.00125. 03 C ANISOU 259 CH2 TRP A 36 15424 15666 16415 -1307 891 -95 C

ATOM 260 CZ2 TRP A 36 46.841 114.393 -9.865 1.00120 .77 C

ANISOU 260 CZ2 TRP A 36 14777 15161 15949 -1298 817 13 C

ATOM 261 C ' TRP A 36 39.914 115.180 -10.955 1.00104 .52 C

ANISOU 261 C TRP A 36 12991 12751 13972 -866 1078 -112 C

ATOM 262 O TRP A 36 39.170 114.252 -11.214 1.00107 .19 O

ANISOU 262 O TRP A 36 13237 13060 14429 -801 1047 -64 O

ATOM 263 N VAL A 37 39.715 116.367 -11.470 1.00120 .04 N

ANISOU 263 N VAL A 37 15067 14668 15874 -848 1127 -188 " N

ATOM 264 CA VAL A 37 38.635 116.524 -12.411 1.00126 09 C

ANISOU 264 CA VAL A 37 15839 15346 16724 -745 1127 -205 C

ATOM 265 CB VAL A 37 37.760 117.716 -12.031 1.00127 06 C

ANISOU 265 CB VAL A 37 16066 15424 16786 -720 1240 -215 C

ATOM 266 CGl VAL A 37 36.731 118.008 -13.108 1.00124. 44 C

ANISOU 266 CGl VAL A 37 15724 15000 16559 -611 1223 -213 C

ATOM 267 CG2 VAL A 37 37.083 117.431 -10.723 1.00126, 98 C

ANISOU 267 CG2 VAL A 37 16030 15449 16768 -748 1308 -150 C

ATOM 268 C VAL A 37 39.253 116.738 -13.773 1.00129. 13 C

ANISOU 268 C VAL A 37 16276 15686 17101 -731 1087 -278 C

ATOM 269 O VAL A 37 40.286 117.403 -13.888 1.00131, 71 O

ANISOU 269 O VAL A 37 16684 16037 17322 -796 1117 -334 O

ATOM 270 N ARG A 38 38.658 116.167 -14.814 1.00115, 09 N

ANISOU 270 N ARG A 38 14463 13840 15426 -660 1019 -277 N

ATOM 271 CA ARG A 38 39.092 116.540 -16.155 1.00117. 24 C

ANISOU 271 CA ARG A 38 14834 14052 15661 -655 998 -351 C

ATOM 272 CB ARG A 38 39.525 115.321 -16.962 1.00118. 00 C

ANISOU 272 CB ARG A 38 14875 14118 15840 -651 920 -361 C

ATOM 273 CG ARG A 38 38.462 114.297 -17.244 1.00113. 55 C

ANISOU 273 CG ARG A 38 14194 13534 15414 -605 842 -292 C

ATOM 274 CD ARG A 38 39.091 113.217 -18.078 1.00111. 23 C

ANISOU 274 CD ARG A 38 13878 13206 15180 -617 795 -315 C

ATOM 275 NE ARG A 38 38.097 112.363 -18.694 1.00117. 19 N

ANISOU 275 NE ARG A 38 14608 13888 16031 -582 705 -285 N

ATOM 276 CZ ARG A 38 38.386 111.224 -19.312 1.00124. 44 C

ANISOU 276 CZ ARG A 38 15523 14748 17009 -591 660 -299 C

ATOM 277 NHl ARG A 38 39.651 110.818 -19.389 1.00125. 18 N

ANISOU 277 NHl ARG A 38 15623 14843 17096 -619 712 -340 N

ATOM 278 NH2 ARG A 38 37.409 110.492 -19.845 1.00124. 48 N

ANISOU 278 NH2 ARG A 38 15520 14688 17088 -576 568 -268 N

ATOM 279 C ARG A 38 38.035 117.363 -16.889 1.00119. 28 C

ANISOU 279 C ARG A 38 15180 14227 15914 -594 1001 -361 C

ATOM 280 O ARG A 38 36.906 117.513 -16.414 1.00118. 88 O

ANISOU 280 O ARG A 38 15086 14161 15922 -541 1020 -304 O

ATOM 281 N GLN A 39 38.405 117.919 -18.035 1.00116. 25 N

ANISOU 281 N GLN A 39 14919 13784 15466 -601 989 -427 N

ATOM 282 CA GLN A 39 37.453 118.695 -18.810 1.00118. 29 C

ANISOU 282 CA GLN A 39 15264 13954 15725 -543 965 -425 C

ATOM 283 CB GLN A 39 37.364 120.102 -18.256 1.00118. 36 C

ANISOU 283 CB GLN A 39 15379 13957 15636 -542 1079 -445 C

ATOM 284 CG GLN A 39 36.241 120.900 -18.834 1.00121. 75 C

ANISOU 284 CG GLN A 39 15843 14300 16117 -454 1072 -402 C

ATOM 285 CD GLN A 39 36.104 122.237 -18.152 1.00125. 21 C

ANISOU 285 CD GLN A 39 16398 14717 16458 -451 1212 -426 C

ATOM 286 OEl GLN A 39 37.101 122.825 -17.710 1.00122. 60 O

ANISOU 286 OEl GLN A 39 16166 14427 15989 -533 1292 -495 O

ATOM 287 NE2 GLN A " 39 34.866 122.731 -18.054 1.00123. 46 N

ANISOU 287 NE2 GLN A 39 16166 14426 16319 -359 1247 -365 N

ATOM 288 C GLN A 39 37.809 118.742 -20.285 1.00120. 02 C

ANISOU 288 C GLN A 39 15598 14100 15903 -561 899 -483 C

ATOM 289 O GLN A 39 38.734 119.442 -20.680 1.00119. 35 O

ANISOU 289 O GLN A 39 15636 14009 15701 -614 957 -559 O

ATOM 290 N PRO A 40 37.070 117.990 -21.108 1.00128. 27 N

ANISOU 290 N PRO A 40 16613 15085 17037 -531 780 -446 N

ATOM 291 CA PRO A 40 37.362 118.020 -22.542 1.00131. 11 C

ANISOU 291 CA PRO A 40 17119 15360 17335 -564 717 -501 C

ATOM 292 CB PRO A 40 36.374 117.007 -23.131 1.00135. 08 C

ANISOU 292 CB PRO A 40 17559 15815 17952 -546 574 -440 C

ATOM 293 CG PRO A ' 40 35.826 116.225 -21.931 1.00132. 43 C

ANISOU 293 CG PRO A 40 17017 15552 17747 -508 579 -361 C

ATOM 294 CD PRO A 40 35.878 117.186 -20.792 1.00130. 17 C

ANISOU 294 CD PRO A 40 16706 15325 17428 -479 698 -351 C

ATOM 295 C PRO A 40 37.024 119.418 -22.984 1.00135. 48 C

ANISOU 295 C PRO A 40 17813 15853 17810 -539 728 -509 C

ATOM 296 O PRO A 40 36.079 119.982 -22.438 1.00137. 59 O

ANISOU 296 O PRO A 40 18024 16108 18145 -470 715 -437 O

ATOM 297 N PRO A 41 37.769 119.970 -23.948 1.00139. 87 N

ANISOU 297 N PRO A 41 18547 16363 .18234 -592 764 -593 N ATOM 298 CA PRO A 41 37.705 121.410 -24.168 1.00139.56 C

ANISOU 298 CA PRO A 41 18666 16262 18097 -579 793 -611 C

ATOM 299 CB PRO A 41 38.676 121.633 -25.324 1.00140.08 C

ANISOU 299 CB PRO A 41 18921 16260 18043 -655 785 -697 C

ATOM 300 CG PRO A 41 39. ' 353 120.322 -25.556 1.00141.96 C

ANISOU 300 CG PRO A 41 19089 16552 18296 -711 835 -748 C

ATOM 301 CD PRO A 41 38.393 119.290 -25.084 1.00140.48 ' C

ANISOU 301 CD PRO A 41 18693 16422 18260 -665 773 -669 C

ATOM 302 C PRO A 41 36.304 121.755 -24.597 1.00144.15 C

ANISOU 302 C PRO A 41 19229 16775 18767 -502 676 -515 C

ATOM 303 O PRO A 41 35.759 121.070 -25.472 1.00143.05 O

ANISOU 303 O PRO A 41 19083 16587 18683 -508 532 -476 O

ATOM 304 N GLY A 42 35.731 122.780 -23.970 1.00139.28 N

ANISOU 304 N GLV A 42 18602 16149 18169 -435 740 -472 N

ATOM 305 CA GLY A 42 34.346 123.160 -24.202 1.00144.73 C

ANISOU 305 CA GLY A 42 19244 16769 18977 -346 643 -362 C

ATOM 306 C GLY A 42 33.336 122.081 -23.838 1.00136.83 C

ANISOU 306 C GLY A 42 18034 15799 18157 -307 541 -267 C

ATOM 307 O GLY A 42 32.490 121.690 -24.639 1.00131.83 O

ANISOU 307 O GLY A 42 17388 15117 17585 -316 371 -214 O

ATOM 308 N LYS A 43 33.412 121.600 -22.611 1.00141.58 N

ANISOU 308 N LYS A 43 18484 16475 18834 -275 646 -244 N

ATOM 309 CA LYS A 43 32.596 120.482 -22.213 1.00141.10 C

ANISOU 309 CA LYS A 43 18224 16457 18930 -255 580 -169 C

ATOM 310 CB LYS A 43 33.108 119.212 -22.898 1.00139.59 C

ANISOU 310 CB LYS A 43 18038 16285 18714 -337 478 -211 C

ATOM 311 CG LYS A 43 32.889 119.155 -24.430 1.00146.85 C

ANISOU 311 CG LYS A 43 19042 17117 19637 -366 292 -187 C

ATOM 312 CD LYS A 43 33-.375 117.831 -25.036 1.00152.07 C

ANISOU 312 CD LYS A 43 19719 17785 20277 -449 224 -234 C

ATOM 313 CE LYS A 43 32.344 117.214 -25.981 1.00152.24 C

ANISOU 313 CE LYS A 43 19754 17731 20361 -480 18 -167 C

ATOM 314 NZ LYS A 43 32.092 115.773 -25.642 1.00150.62 N

ANISOU 314 NZ LYS A 43 19457 17549 20221 -528 -27 -167 N

ATOM 315 C LYS A 43 32.692 120.372 -20.700 1.00144.75 C

ANISOU 315 C LYS A 43 18585 17002 19411 -242 741 -172 C

ATOM 316 O LYS A 43 33.788 120.379 -20.142 1.00141.56 O

ANISOU 316 O LYS A 43 18262 16651 18875 -298 856 -255 O

ATOM 317 N GLY A 44 31.540 120.294 -20.040 1.00161.33 N

ANISOU 317 N GLY A 44 20513 19112 21674 -180 747 -77 N

ATOM 318 CA GLY A 44 31.473 120.261 -18.587 1.00157.59 C

ANISOU 318 CA GLY A 44 19958 18702 21218 -171 904 -68 C

ATOM 319 C GLY A 44 32.554 119.443 -17.909 1.00150.70 C

ANISOU 319 C GLY A 44 19096 17924 20238 -260 955 -137 C

ATOM 320 O GLY A 44 33.145 118.552 -18.514 1.00149.87 O

ANISOU 320 O GLY A 44 19018 17841 20083 -321 868 -184 O

ATOM 321 N LEU A 45 32.818 119.747 -16.645 1.00123.23 N

ANISOU 321 N LEU A 45 15602 .14494 16724 -272 1101 -137 N

ATOM 322 CA LEU A 45 33.805 118.990 -15.894 1.00122.46 C

ANISOU 322 CA LEU A 45 15483 14491 16555 -356 1126 -168 C

ATOM 323 CB LEU A 45 34.028 119.615 -14.512 1.00119.20 C

ANISOU 323 CB LEU A 45 15117 14114 16060 -385 1294 -173 C

ATOM 324 CG LEU A 45 33.602 121.056 -14.237 1.00116.79 C

ANISOU 324 CG LEU A 45 14928 13732 15713 -337 1429 -185 C

ATOM 325 CDl LEU A 45 33.446 121.263 -12.764 1.00117.13 C

ANISOU 325 CDl LEU A 45 15002 13795 15708 -364 1601 -172 C

ATOM 326 CD2 LEU A 45 34.620 122.010 -14.771 1.00122.43 C

ANISOU 326 CD2 LEU A 45 15817 14430 16271 -383 1440 -274 C

ATOM 327 C LEU A 45 33.298 117.559 -15.723 1.00121.18 C

ANISOU 327 C LEU A 45 15151 14355 16538 -345 1033 -99 C

ATOM 328 O LEU A 45 32.099 117.300 -15.844 1.00122.21 O

ANISOU 328 O LEU A 45 15181 14439 16816 -280 980 -26 O

ATOM 329 N GLU A 46 34.204 116.630 -15.442 1.00123.94 N

ANISOU 329 N GLU A 46 15463 14776 16853 -411 1008 -115 N

ATOM 330 CA GLU A 46 33.802 115.288 -15.045 1.00119.84 C

ANISOU 330 CA GLU A 46 14795 14283 16457 -410 942 -49 C

ATOM 331 CB GLU A 46 33.602 114.366 -16.261 1.00122.25 C

ANISOU 331 CB GLU A 46 15065 14541 16844 -402 790 -47 C

ATOM 332 CG GLU A 46 34.854 113.646 -16.797 1.00123.59 C

ANISOU 332 CG GLU A 46 15269 14733 16955 -461 746 -104 C

ATOM 333 CD GLU A 46 34.529 112.280 -17.445 1.00131.15 C

ANISOU 333 CD GLU A 46 16175 15643 18012 -464 623 -86 C

ATOM 334 OEl GLU A 46 33.436 111.718 -17.169 1.00130.41 O

ANISOU 334 OEl GLU A 46 15974 15533 18043 -439 568 -11 O

ATOM 335 0E2 GLU A 46 35.368 111.761 -18.227 1.00135.73 O

ANISOU 335 0E2 GLU A 46 16829 16196 18547 -499 592 -148 O

ATOM 336 C GLU A 46 34.826 114.720 -14.078 1.00119.24 C ANISOU 336 C GLU A 46 14702 14292 16311 -483 977 -56 C

ATOM 337 O GLU A 46 36.036 114.802 -14.318 1.00118 .42 O

ANISOU 337 O GLU A 46 14655 14218 16121 -536 958 -112 O

ATOM 338 N TRP A 47 34.336 114.156 -12.978 1.00124 .60 N

ANISOU 338 N TRP A 47 15301 15007 17035 -489 1027 N

ATOM 339 CA TRP A 47 35.208 113.629 -11.933 1.00124 56 C

ANISOU 339 CA TRP A 47 15279 15081 16967 -563 1045 27 C

ATOM 340 CB TRP A 47 34.383 113.357 -10.679 1.00124 67 C

ANISOU 340 CB TRP A 47 15222 15109 ' 17039 -561 1108 106 C

ATOM 341 CG TRP A 47 35.206 112.920 -9.493 1.00126, 56 C

ANISOU 341 CG TRP A 47 15474 15425 17188 -648 1132 135 C

ATOM 342 CDl TRP A 47 36.153 113.653 -8.824 1.00128, 10 C

ANISOU 342 CDl TRP A 47 15786 15671 17217 -732 1187 104 C

ATOM 343 NEl TRP A 47 36.679 112.915 -7.788 1.00127. 67 N

ANISOU 343 NEl TRP A 47 15709 15680 17121 -811 1168 165 N

ATOM 344 CE2 TRP A 47 36.071 111.689 -7.774 1.00125, 03 C

ANISOU 344 CE2 TRP A 47 15244 15333 16929 -770 1114 232 C

ATOM 345 CD2 TRP A 47 35.138 111.659 -8.826 1.00124. 41 C

ANISOU 345 CD2 TRP A 47 15103 15184 16982 -672 1091 212 C

ATOM 346 CE3 TRP A 47 34.383 110.510 -9.022 1.00122. 11 C

ANISOU 346 CE3 TRP A 47 14685 14865 16848 -630 1030 271 C

ATOM 347 CZ3 TRP A 47 34.577 109.462 -8.196 1.00126. 17 C

ANISOU 347 CZ3 TRP A 47 15141 15416 17382 -674 1008 343 C

ATOM 348 CH2 TRP A 47 35.506 109.517 -7.161 1.00129. 18 C

ANISOU 348 CH2 TRP A 47 15587 15865 17631 -762 1029 366 C

ATOM 349 CZ2 TRP A 47 36.262 110.623 -6.936 1.00127. 19 C

ANISOU 349 CZ2 TRP A 47 15458 15647 17222 -817 1076 313 C

ATOM 350 C TRP A 47 36.005 112.374 -12.343 1.00122. 69 C

ANISOU 350 C TRP A 47 14976 14865 16777 -586 934 28 C

ATOM 351 O TRP A 47 35.613 111.637 -13.242 1.00122. 53 O

ANISOU 351 O TRP A 47 14908 14792 16855 -547 850 28 O

ATOM 352 N LEU A 48 37.131 112.134 -11.682 1.00111. 59 N

ANISOU 352 N LEU A 48 13568 13528 15302 -655 935 36 N

ATOM 353 CA LEU A 48 37.928 110.942 -11.955 1.00112. 35 C

ANISOU 353 CA LEU A 48 13590 13635 15463 -666 852 49 C

ATOM 354 CB LEU A 48 39.281 111.319 -12.551 1.00111. 91 C

ANISOU 354 CB LEU A 48 13593 13598 15329 -706 851 -17 C

ATOM 355 CG LEU A 48 39.377 112.079 -13.863 1.00112. 72 C

ANISOU 355 CG LEU A 48 13792 13637 15400 -680 858 -109 C

ATOM 356 CDl LEU A 48 40.769 111.855 -14.394 1.00111. 49 C

ANISOU 356 CDl LEU A 48 13639 13487 15237 -713 849 -152 C

ATOM 357 CD2 LEU A 48 38.349 111.583 -14.843 1.00115. 78 C

ANISOU 357 CD2 LEU A 48 14162 13940 15888 -614 803 -107 C

ATOM 358 C LEU A 48 38.182 110.146 -10.685 1.00113. 68 C

ANISOU 358 C LEU A 48 13679 13864 15649 -710 838 136 C

ATOM 359 O LEU A 48 37.922 108.949 -10.612 1.00115. 12 O

ANISOU 359 O LEU A 48 13766 14031 15943 -689 779 187 O

ATOM 360 ' N GLY A 49 38.724 110.823 -9.685 1.00129. 67 N

ANISOU 360 N GLY A 49 15762 15953 17552 -780 891 153 N

ATOM 361 CA GLY A 49 39.087 110.167 -8.454 1.00131. 18 C

ANISOU 361 CA GLY A 49 15908 16206 17729 -843 866 241 C

ATOM 362 C GLY A 49 39.470 111.109 -7.335 1.00132. 52 C

ANISOU 362 C GLY A 49 16189 16437 17725 -944 924 244 C

ATOM 363 O GLY A 49 39.735 112.295 -7.531 1.00132. 88 O

ANISOU 363 O GLY A 49 16344 16483 17662 -969 982 173 O

ATOM 364 N MET A 50 39.487 110.552 -6.136 1.00126. 21 N

ANISOU 364 N MET A 50 15379 15686 16889 -1013 906 331 N

ATOM 365 CA MET A 50 39.907 111.254 -4.940 1.00127. 46 C

ANISOU 365 CA MET A 50 15662 15902 16864 -1138 941 345 C

ATOM 366 CB MET A 50 38.691 111.574 -4.070 1.00126. 65 C

ANISOU 366 CB MET A 50 15672 15764 16687 -1150 1079 342 C

ATOM 367 CG MET A 50 38.971 111.944 -2.625 1.00130. 54 C

ANISOU 367 CG MET A 50 16271 16303 17026 -1287 1099 409 C

ATOM 368 SD MET A 50 37.475 112.642 -1.887 1.00139. 23 S

ANISOU 368 SD MET A 50 17512 17334 18056 -1289 1311 394 S

ATOM 369 CE MET A 50 36.291 111.300 -2.101 1.00134. 10 C

ANISOU 369 CE MET A 50 16673 16624 17654 -1141 1313 437 C

ATOM 370 C MET A 50 40.856 110.337 -4.199 1.00132. 79 C

ANISOU 370 C MET A 50 16275 16645 17533 -1222 829 453 C

ATOM 371 O MET A 50 40.806 109.113 -4.337 1.00134. 25 O

ANISOU 371 O MET A 50 16337 16819 17854 -1171 762 523 O

ATOM 372 N ILE A 51 41.746 110.926 -3.429 1.00127. 24 N

ANISOU 372 N ILE A 51 15660 16011 16676 -1354 798 472 N

ATOM 373 CA ILE A 51 42.568 110.130 -2.555 1.00133. 75 C

ANISOU 373 CA ILE A 51 16438 16903 17479 -1451 675 594 C

ATOM 374 CB ILE A 51 43.951 109.874 -3.167 1.00126. 48 C

ANIΞOU 374 CB ILE A 51 15391 16031 16635 -1464 550 621 C ATOM 375 CGl ILE A 51 44.861 109.177 -2.157 1.00128.71 C

ANISOU 375 CGl ILE A 51 15617 16385 16902 -1570 406 770 C

ATOM 376 CDl ILE A 51 46.235 108.930 -2.677 1.00128 .89 C

ANISOU 376 CDl ILE A 51 15478 16447 17046 -1566 291 819 C

ATOM 377 CG2 ILE A 51 44.543 111.174 -3.669 1.00124 .79 C

ANISOU 377 CG2 ILE A 51 15265 15837 16313 -1517 589 525 C

ATOM ' 378 C ILE A 51 42.619 110.869 -1.225 1.00140 .19 C

ANISOU 378 C ILE A 51 17443 17756 18067 -1614 712 624 C

ATOM 379 O ILE A 51 43..016 112.044 -1.166 1.00136 .23 O

ANISOU 379 O ILE A 51 17087 17267 17407 -1697 770 554 O

ATOM 380 N TRP A 52 42.168 110.189 -0.171 1.00142 .37 N

ANISOU 380 N TRP A 52 17735 18038 18320 -1663 688 723 N

ATOM 381 CA TRP A 52 42.007 110.813 1.140 1.00142 .39 C

ANISOU 381 CA TRP A 52 17948 18052 18100 -1817 749 750 C

ATOM 382 CB TRP A 52 41.006 110.040 1.998 1.00139 04 C

ANISOU 382 CB TRP A 52 17530 17591 17707 -1805 793 826 C

ATOM 383 CG TRP A 52 39.737 109.632 1.322 1.00132 .12 C

ANISOU 383 CG TRP A 52 16569 16632 16997 -1638 918 771 C

ATOM 384 CDl TRP A 52 39.615 108.892 0.191 1.00129, 86 C

ANISOU 384 CDl TRP A 52 16090 16320 16931 -1486 869 755 C

ATOM 385 NEl TRP A 52 38.288 108.683 -0.097 1.00127. 87 N

ANISOU 385 NEl TRP A 52 15810 15993 16783 -1381 994 719 N

ATOM 386 CE2 TRP A 52 37.527 109.286 0.866 1.00125. 62 C

ANISOU 386 CE2 TRP A 52 15688 15680 16360 -1453 1147 712 C

ATOM 387 CD2 TRP A 52 38.405 109.884 1.783 1.00126, 05 C

ANISOU 387 CD2 TRP A 52 15903 15793 16198 -1619 1108 739 C

ATOM 388 CE3 TRP A 52 37.875 110.568 2.875 1.00122. 20 C

ANISOU 388 CE3 TRP A 52 15633 15278 15521 -1732 1259 731 C

ATOM 389 CZ3 TRP A 52 36.521 110.635 3.010 1.00121. 10 C

ANISOU 389 CZ3 TRP A 52 15521 15054 15438 -1660 1456 699 C

ATOM 390 CH2 TRP A 52 35.670 110.030 2.083 1.00124. 97 C

ANISOU 390 CH2 TRP A 52 15820 15496 16168 -1488 1480 684 C

ATOM 391- CZ2 TRP A 52 36.154 109.354 1.003 1.00125. 37 C

ANISOU 391 CZ2 TRP A 52 15677 15574 16384 -1391 1319 688 C

ATOM 392 C TRP A 52 43.310 110.913 1.930 1.00148. 05 C

ANISOU 392 C TRP A 52 18728 18859 18666 -2004 598 834 C

ATOM 393 O TRP A 52 44.417 110.820 1.382 1.00148. 63 O

ANISOU 393 O TRP A 52 18682 18988 18804 -2012 468 853 O

ATOM 394 N GLY A 53 43.162 111.108 3.234 1.00149. 94 N

ANISOU 394 N GLY A 53 19159 19109 18704 -2164 617 888 N

ATOM 395 CA GLY A 53 44.312 111.104 4.101 1.00153. 59 C

ANISOU 395 CA GLY A 53 19692 19656 19011 -2365 446 991 C

ATOM 396 C GLY A 53 44.815 109.686 4.159 1.00157. 37 C

ANISOU 396 C GLY A 53 19961 20182 19652 -2338 242 1146 C

ATOM 397 O GLY A 53 45.946 109.405 3.765 1.00156. 72 O

ANISOU 397 O GLY A 53 19738 20167 19642 -2367 71 1212 O

ATOM 398 N ASP A 54 43.947 108.789 4.623 1.00168. 94 N

ANISOU 398 N ASP A 54 21397 21602 21190 -2275 272 1206 N

ATOM 399 CA ASP A 54 44.327 107.404 4.884 1.00171. 57 C

ANISOU 399 CA ASP A 54 21562 21960 21666 -2251 97 1365 C

ATOM 400 CB ASP A 54 43.304 106.681 5.779 1.00169. 22 C

ANISOU 400 CB ASP A 54 21348 21611 21338 -2260 160 1429 C

ATOM 401 CG ASP A 54 41.884 106.759 5.242 1.00168. 86 C

ANISOU 401 CG ASP A 54 21310 21473 21375 -2112 387 1306 C.

ATOM 402 ODl ASP A 54 41.597 107.688 4.460 1.00165. 88 O

ANISOU 402 ODl ASP A 54 20954 21072 21002 -2045 515 1167 O

ATOM 403 0D2 ASP A 54 41.050 105.901 5.614 1.00165. 10 O

ANISOU 403 0D2 ASP A 54 20817 20948 20966 -2068 436 1356 O

ATOM 404 C ASP A 54 44.560 106.635 3.598 1.00171. 42 C

ANISOU 404 C ASP A 54 21269 21924 21939 -2053 52 1353 C

ATOM 405 O ASP A 54 44.298 105.434 3.529 1.00171. 91 O

ANISOU 405 O ASP A 54 21194 21956 22169 -1961 -1 1438 O

ATOM 406 N GLY A 55 45.052 107.341 2.583 1.00171. 69 N

ANISOU 406 N GLY A 55 21244 21967 22023 -1995 85 1246 N

ATOM 407 CA GLY A 55 45.490 106.726 1.341 1.00172. 38 C

ANISOU 407 CA GLY A 55 21104 22031 22361 -1829 57 1223 C

ATOM 408 C GLY A 55 44.418 105.983 0.570 1.00166. 38 C

ANISOU 408 C GLY A 55 20269 21181 21768 -1653 162 1170 C

ATOM 409 O GLY A 55 44.707 105.254 -0.380 1.00157. 98 O

ANISOU 409 O GLY A 55 19029 20081 20915 -1525 127 1181 O

ATOM 410 N ASN A 56 43.172 106.155 0.985 1.00154. 14 N

ANISOU 410 N ASN A 56 18854 19587 20127 -1654 296 1116 N

ATOM 411 CA ASN A 56 42.074 105.563 0.253 1.00153. 04 C

ANISOU 411 CA ASN A 56 18641 19365 20143 -1505 388 1070 C

ATOM 412 CB ASN A 56 40.780 105.58'6 1.073 1.00155. 33 C

ANISOU 412 CB ASN A 56 19057 19619 20342 -1544 500 1084 C

ATOM 413 CG ASN A 56 40.574 104.310 1.862 1.00157. 80 C ANISOO 413 CG ASN A 56 19306 19916 20734 -1547 427 1217 C

ATOM 414 ODl ASN A 56 41.204 103.296 1.562 1.00156 .78 O

ANISOU 414 ODl ASN A 56 19014. 19776 20779 -1469 320 .1276 O

ATOM 415 ND2 ASN A 56 39.689 104.348 2.871 1.00154 .40 N

ANISOU 415 ND2 ASN A 56 19015 19475 20176 -1638 495 1264 N

ATOM 416 C ASN A 56 41.895 106.256 -1.089 1.00148. 23 C

ANISOU 416 C ASN A 56 18000 18712 19607 -1390 480 924 C

ATOM 417 O ASN A 56 42.030 107.478 -1.205 1.00143, 76 O

ANISOU 417 O ASN A 56 17552 18156 18913 -1429 562 831- O

ATOM 418 N THR A 57 41.616 105.443 -2.100 1.00146. 54 N

ANISOU 418 N THR A 57 17641 18443 19593 -1258 463 910 N

ATOM 419 CA THR A 57 41.426 105.898 -3.460 1.00135. 67 C

ANISOU 419 CA THR A 57 16234 17017 18299 -1152 524 786 C

ATOM 420 CB THR A 57 42.355105.127 -4.402 1.00135. 58 C

ANISOU 420 CB THR A 57 16075 16982 18457 -1076 445 800 C

ATOM 421 OGl THR A 57 42.524 103.787 -3.913 1.00135. 16 O

ANISOU 421 OGl THR A 57 15927 16906 18523 -1051 378 913 O

ATOM 422 CG2 THR A 57 43.718 105.788 -4.463 1.00139. 03 C

ANISOU 422 CG2 THR A 57 16487 17488 18850 -1146 .375 823 C

ATOM 423 C THR A 57 40.005 105.567 -3.836 1.00132. 34 C

ANISOU 423 C THR A 57 15805 16520 17960 -1066 606 750 C

ATOM 424 O THR A 57 39.591 104.417 -3.729 1.00133. 04 O

ANISOU 424 O THR A 57 15823 16577 18149 -1037 577 823 O

ATOM 425 N ASP A 58 39.239 106.572 -4.234 1.00125. 72 N

ANISOU 425 N ASP A 58 15035 15649 17083 -1029 705 648 N

ATOM 426 CA ASP A 58 37.934 106.328 -4.841 1.00124. 47 C

ANISOU 426 CA ASP A 58 14844 15418 17032 -941 767 617 C

ATOM 427 CB ASP A 58 36.831 107.117 -4.147 1.00121. 21 C

ANISOU 427 CB ASP A 58 14529 14995 16532 -968 897 606 C

ATOM 428 .CG ASP A 58 36.551 106.626 -2.750 1.00129. 09 C

ANISOU 428 CG ASP A 58 15555 16014 17481 -1044 918 705 C

ATOM 429 ODl ASP A 58 36.752 105.410 -2.477 1.00126. 42 O

ANISOU 429 ODl ASP A 58 15126 15673 17234 -1040 832 787 O

ATOM 430 0D2 ASP A 58 36.113 107.477 -1.935 1.00131. 20 O

ANISOU 430 0D2 ASP A 58 15950 16288 17612 -1112 1030 699 O

ATOM 431 C ASP A 58 38.041 106.804 -6.270 1.00120. 69 C

ANISOU 431 C ASP A 58 14354 14896 16605 -865 767 515 C

ATOM 432 O ASP A 58 38.453 107.935 -6.500 1.00122. 26 O

ANISOU 432 O ASP A 58 14639 15114 16701 -886 809 444 O

ATOM 433 N TYR A 59 37.697 105.963- -7.240 1.00116. 56 N

ANISOU 433 N TYR A 59 13744 14312 16232 -789 720 506 N

ATOM 434 CA TYR A 59 37.741 106.423 -8.617 1.00113. 57 C

ANISOU 434 CA TYR A 59 13380 13883 15887 -731 7Ϊ3 412 C

ATOM 435 CB TYR A 59 38.641 105.561 -9.463 1.00112. 46 C

ANISOU 435 CB TYR A 59 13178 13711 15840 -704 642 406 C

ATOM 436 CG TYR A 59 39.970 105.190 -8.886 -1.00113. 61 C

ANISOU 436 CG TYR A 59 13284 13913 15968 -749 604 460 C

ATOM 437 CDl TYR A 59 - 41.115 105.860 -9.268 1.00118. 04 C

ANISOU 437 CDl TYR A 59 13870 14502 16476 -770 607 409 C

ATOM 438 CEl TYR A 59 42.358 105.488 -8.786 1.00122. 39 C

ANISOU 438 CEl TYR A 59 14356 15106 17042 -811 561 474 C

ATOM 439 C2 TYR A 59 42.466 104.425 -7.916 1.00123. 83 C

ANISOU 439 CZ TYR A 59 14457 15309 17282 -828 501 596 C

ATOM 440 OH TYR A 59 43.709 104.064 -7.430 1.00124. 87 O

ANISOU 440 OH TYR A 59 14509 15492 17443 -869 435 683 O

ATOM 441 CE2 TYR A 59 41.336 103.732 -7.532 1.00122. 45 C

ANISOU 441 CE2 TYR A 59 14278 15103 17145 -809 502 641 C

ATOM 442 CD2 TYR A 59 40.098 104.112 -8.026 1.00117. 24 C

ANISOU 442 CD2 TYR A 59 13672 Ϊ4394 16480 -771 557 571 C

ATOM 443 C TYR A 59 36.369 106.403 -9.254 1.00114. 97 C

ANISOU 443 C TYR A 59 13543 13992 16149 -671 .731 389 C

ATOM 444 O TYR A 59 35.460 105.715 -8.786 1.00117. 70 O

ANISOU 444 O TYR A 59 13826 14317 16577 -662 732 451 O

ATOM 445 N ASN A 60 36.245 107.161 -10.335 .1.00114. 85 N

ANISOU 445 N ASN A 60 13583 13940 16115 -637 739 307 N

ATOM 446 CA ASN A 60 35.053 107.183 -11.163 1.00116. 23 C

ANISOU 446 CA ASN A 60 ' 13739 14044 16380 -583 720 289

ATOM 447 CB ASN A 60 35.235 108.243 -12.249 1.00115. 66 C

ANISOU 447 CB ASN A 60 13756 13938 16250 -561 716 199 C

ATOM 448 CG ASN A 60 34.271 108.083 -13.415 1.00115. 63 C

ANISOU 448 CG ASN A 60 13741 13854 16341 -518 650 188 C

ATOM 449 ODl ASN A 60 33.130 107.617 -13.268 1.00117. 45 O

ANISOU 449 ODl ASN A 60 13884 14057 16683 -503 618 249 O

ATOM 450 ND2 ASN A 60 34.726 108.505 -14.588 1.00116. 62 N

ANISOU 450 ND2 ASN A 60 13958 13938 16416 -509 623 114 N

ATOM 451 C ASN A 60 34.841 105.816 -11.782 1.00117. 51 C

ANISOU 451 C ASN A 60 13825 14152 ' 16672 -569 634 319 C ATOM 452 O ASN A 60 35.757 105.260 -12.383 1.00119.73 O

ANISOU 452 O ASN A 60 14115 14411 16965 -573 591 293 O

ATOM 453 N SER A 61 33.643 105.263 -11.636 1.00129.61 N

ANISOU 453 N SER A 61 15284 15655 18307 -556 619 377 N

ATOM 454 CA SER A 61 33.427 103.878 -12.055 1.00137.94 C

ANISOU 454 CA SER A 61 16278 16653 19480 -558 540 409 C

ATOM 455 CB SER A 61 32.003 103.401 -11.720 1.00150.24 C

ANISOU 455 CB SER A 61 17746 18187 21152 -554 532 478 C

ATOM 456 OG SER A 61 31.011 104.081 -12.471 1.00153.77 O

ANISOU 456 OG SER A 61 18189 18598 21639 -528 509 461 O

ATOM 457 C SER A 61 33.780 103.636 -13.526 1.00139.91 C

ANISOU 457 C SER A 61 16589 16829 19743 -550 466 337 C

ATOM 458 o ' SER A 61 34.301 102.578 -13.892 1.00141.84 O

ANISOU 458 O SER A 61 16827 17022 20042 -560 424 339 O

ATOM 459 N ALA A 62 33.518 1'04.63S -14.360 1.00130.78 N

ANISOU 459 N ALA A 62 15508 15654 18530 -535 460 273 N

ATOM 460 CA ALA A 62 33.738 104.485 -15.785 1.00126.55 C

ANISOU 460 CA ALA A 62 ' 15058 15037 17990 -543 392 205 C

ATOM 461 CB ALA A 62 32.847 105.432 -16-.573 1.00123.95 C

ANISOU 461 CB ALA A 62 14780 14674 17642 -531 348 180 C

ATOM 462 C ALA A 62 35.195 104.679 -16.164 1.00128.67 C

ANISOU 462 C ALA ' A 62 15406 15303 18178 -550 434 133 C

ATOM 463 O ALA A 62 35.509 104.730 -17.339 1.00136.89 O

ANISOU 463 O ALA A 62 16544 162 ' 70 19198 -561 407 66 O

ATOM 464 N LEU A 63 36.087 104.806 -15.186 1.00117.07 N

ANISOU 464 N LEU A 63 13904 13913 16666 -551 501 151 N

ATOM 465 CA LEU A 63 37.525 104.660 -15.467 1.00119.95 C

ANISOU 465 CA LEU A 63 14299 14277 17000 -558 537 109 C

ATOM 466 CB LEU A 63 38.312 105.949 -15.217 1.00111.39 C

ANISOU 466 CB LEU A 63 13259 13266, 15798 -572 597 71 C

ATOM 467 CG LEU A 63 37.747 107.139 -16.017 1.00107.80 C

ANISOU 467 CG LEU A 63 12915 12779 15264 -566 599 -2 C

ATOM 468 CDl LEU A 63 38.757 108.264 -16.096 1.00109.96 C

ANISOU 468 CDl LEU A 63 13265 13092 15422 -588 662 -67 C

ATOM 469 CD2 LEU A 63 37.309 106.764 -17.419 1.00105.35 C

ANISOU 469 CD2 LEU A 63 1267.7 12360 14992 -561 542 -49 C

ATOM 470 C LEU A 63 38.096 103.395 -14.780 1.00125.96 C

ANISOU 470 C LEU A 63 14963 15045 17852 -557 535 183 C

ATOM 471 O LEU A 63 38.977 103.420 -13.899 1.00115.66 O

ANISOU 471 O LEU A 63 13606 13807 16531 -567 563 223 O

ATOM 472 N LYS A 64 37.523 102.282 -15.229 1.00162.06 N

ANISOU 472 N LYS A 64 19516 19539 22520 -552 , ' 489 207 N

ATOM 473 CA LYS A 64 37.877 100.951 -14.787 1.00170.77 C

ANISOU 473 CA LYS A 64 20547 20613 23726 -545 483 273 C

ATOM 474 CB LYS A 64 37.017 99.887 -15.502 1.00174.81 C

ANISOU 474 CB LYS A 64 21078 21016 24325 -554 431 275 C

ATOM 475 CG LYS A 64 37.425 99.579 -16.955 1.00178.35 C

ANISOU 475 CG LYS A 64 21640 21341 24784 -559 441 189 C

ATOM 476 CD LYS A 64 36.403 98.687 -17.706 1.00187.02 C

ANISOU 476 CD LYS A 64 22793 22334 25932 -598 368 183 C

ATOM 477 CE LYS A 64 36.849 98.406 -19.167 1.00183.20 C

ANISOU 477 CE LYS A 64 22476 21721 25410 -626 381 79 C

ATOM 478 NZ LYS A 64 35.728 98.191 -20.149 1.00157.41 N

ANISOU 478 NZ LYS A 64 19306 18366 22136 -692 279 58 N

ATOM 479 C LYS A 64 39.343 100.706 -15.050 1.00170.92 C

ANISOU 479 C LYS A 64 20573 20606 23761 -528 534 244 C

ATOM 480 O LYS A 64 39.804 100.769 -16.194 1.00162.11 O

ANISOU 480 O LYS A 64 19550 19418 22626 -525 566 155 O

ATOM 481 N SER A 65 40.065 100.434 -13.969 1.00215.60 N

ANISOU 481 N SER A 65 26135 26323 29462 -521 544 328 N

ATOM 482 CA SER A 65 41.461 100.050 -14.053 1.00216.86 C

ANISOU 482 CA SER A' 65 26255 26452 29690 -495 589 336 C

ATOM 483 CB SER A 65 41.610 98.528 -14.126 1.00225.39 . C

ANISOU 483 CB SER A 65 27297 27424 30917 -462 593 385 C

ATOM 484 OG SER A 65 41.435 97.926 -12.852 1.00224.86 O

ANISOU 484 OG SER A 65 27125 27408 30902 -463 546 513 O

ATOM 485 C SER A 65 42.053 100.691 -15.279 1.00205.45 C

ANISOU 485 C SER A 65 24910 24955 28196 -493 649 216 C

ATOM 486 O SER A 65 42.864 100.095 -15.986 1.00202.34 O

ANISOU 486 O SER A 65 24561 24447 27871 -470 705 168 O

ATOM 487 N ARG A 66 41.605 101.906 -15.550 1.00150.40 N

ANISOU 487 N ARG A 66 17994 18056 21096 -522 648 165 N

ATOM 488 CA ARG A 66 42.254 102.705 -16.551 1.00145.75 C

ANISOU 488 CA ARG A 66 17499 17437 20444 -529 709 62 C

ATOM 489 CB ARG A 66 41.296 103.060 -17.682 1.00142.21 C

ANISOU 489 CB ARG A 66 17195 16912 19928 -541 690 -27 C

ATOM 490 CG ARG A 66 42.021 103.392 -18.978 1.00144.66 C ANISOU 490 CG ARG A 66 17627 17141 20195 -549 764 -135 C

ATOM 491 CD ARG A 66 41.078 103.513 -20.162 1.00147.14 " C

ANISOU 491 CD ARG A 66 18102 17353 20453 -573 727 -209 C

ATOM 492 NE ARG A 66 41.368 104.734 -20.904 1.00150.71 N

ANISOU 492 NE ARG A 66 18679 17806 20778 -598 757 -295 N

ATOM 493 CZ ARG A 66 40.622 105.834 -20.847 1.00148.53 C

ANISOU 493 CZ ARG A 66 18452 17575 20409 -611 696 -303 C

ATOM 494 NHl ARG A 66 39.521 105.862 -20.108 1.00148.80 N

ANISOU 494 NHl ARG A 66 18413 17653 20473 -599 610 -232 N

ATOM 495 NH2 ARG A 66 40.967 106.899 -21.544 1.00145.63 N

ANISOU 495 NH2 ARG A 66 18206 17197 19928 -632 729 -378 N

ATOM 496 C ARG A 66 42.799 103.931 -15.839 1.00144.95 C

ANISOU 496 C ARG A 66 17374 17458 20244 -560 719 69 / C

ATOM 497 O ARG A 66 43.673 104.622 -16.361 1.00147.67 O

ANISOU 497 O ARG A 66 17755 17803- 20548 -574 777 8 O

ATOM 498 N LEU A 67 42.302 104.163 -14.621 1.00137.89 N

ANISOU 498 N LEU A 67 16427 16659 19306 -583 670 142 N

ATOM 499 CA LEU A 67 42.760 105.263 -13.770 1.00129.78 C

ANISOU 499 CA LEU A 67 15394 15745 18170 -632 676 158 C

ATOM 500 CB LEU A 67 41.578 105.845 -13.036 1.00125.71 C

ANISOU 500 CB LEU A 67 14919 15282 17564 -654 657 177 C

ATOM 501 CG LEU A 67 41.642 107.348 -13.117 1.00125.77 C

ANISOU 501 CG LEU A 67 15031 15328 17426 -688 699 104 C

ATOM 502 CDl LEU A 67 42.300 107.728 -14.424 1.00129.02 C

ANISOU 502 CDl LEU A 67 15520 15669 17831 -670 735 1 C

ATOM 503 CD2 LEU A 67 40.244 107.896 -13.024 1.00121.54 C

ANISOU 503 CD2 LEU A 67 14550 14791 16839 -677 707 101 C

ATOM 504 C LEU A 67 43.804 104.787 -12.768 1.00125.34 C

ANISOU 504 C LEU A 67 14707 15251 17664 -655 648 263 C

ATOM 505 O LEU A 67 44.305 103.683 -12.914 1.00133.77 O

ANISOO 505 O LEU A 67 15688 16267 18870 -616 642 315 O

ATOM 506 N SER A 68 44.142 105.602 -11.768 1.00114.37 N

ANISOU 506 N SER A 68 13318 13969 16169 -724 629 300 N

ATOM 507 CA SER A 68 45.087 105.182 -10.715 1.00121.09 C

ANISOU 507 CA SER A 68 14057 14896 17057 -767 571 420 C

ATOM 508 CB SER A 68 46.174 104.242 -11.242 1.00130.12 C

ANISOU 508 CB SER A 68 15077 15988 18374 -718 575 460 C

ATOM 509 OG SER A 68 47.187 104.014 -10.263 1.00129.25 O

ANISOU 509 OG SER A 68 14847 15960 18303 -766 501 590 O

ATOM 510 C SER A 68 45.781 106.317 -9.988 1.00127.04 C

ANISOU 510 C SER A 68 14842 15757 17671 -867 554 431 C

ATOM 511 O SER A 68 46.950 106.629 -10.236 1.00130.33 O

ANISOU 511 O SER A 68 15199 16206 18113 -899 550 441 O

ATOM 512 N ILE A 69 45.069 106.902 -9.049 1.00130.81 N

ANIΞOU 512 N ILE A 69 15411 16284 18007 -922 550 436 N

ATOM 513 CA ILE A 69 45.625 107.957 -8.243 1.00128.98 C

ANISOU 513 CA ILE A 69 15239 16148 17618 -1038 532 456 C

ATOM 514 CB ILE A 69 44.494 108.790 -7.694 1.00128.94 C

ANISOU 514 CB ILE A 69 15372 16150 17468 -1069 581 426 C

ATOM 515 CGl ILE A 69 43.371 108.863 -8.724 1.00123.26 C

ANISOU 515 CGl ILE A 69 14725 15348 16759 -981 664 309 C

ATOM 516 CDl ILE A 69 42.008 109.079 -8.125 1.00122.66 C

ANISOU 516 CDl ILE A 69 14706 15242 16657 -953 709 313 C

ATOM 517 CG2 ILE A 69 44.988 110.155 -7.358 1.00137.07 C

ANISOU 517 CG2 ILE A 69 16509 17259 18311 -1199 583 426 C

ATOM 518 C ILE A 69 46.448 107.384 -7.085 1.00132.27 C

ANISOU 518 C ILE A 69 15556 16641 18061 -1112 424 603 C

ATOM 519 O ILE A 69 46.135 106.316 -6.554 1.00131.99 O

ANISOU 519 O ILE A 69 15448 16592 18112 -1083 372 699 O

ATOM 520 N SER A 70 47.506 108.094 -6.704 1.00135.10 N

ANISOU 520 N SER A 70 15912 17077 18343 -1216 382 626 N

ATOM 521 CA SER A 70 48.294 107.735 -5.530 1.00141.17 C

ANISOU 521 CA SER A 70 16603 17930 19104 -1319 254 776 C

ATOM 522 CB SER A 70 49.235 106.590 -5.851 1.00142.53 C

ANISOU 522 CB SER A 70 16568 18088 19498 -1259 196 860 C

ATOM 523 OG SER A 70 50.479 107.108 -6.273 1.00147.68 O

ANISOU 523 OG SER A 70 17180 18778 20154 -1309 204 825 O

ATOM 524 C SER A 70 49.124 108.922 -5.069 1.00142.93 C

ANISOU 524 C SER A 70 16919 18240 19146 -1474 227 763 C

ATOM 525 O SER A 70 49.668 109.656 -5.888 1.00143.15 O

ANISOU 525 O SER A 70 17013 18259 19120 -1479 305 647 O

ATOM 526 N LYS A 71 49.242 109.100 -3.759 1.00124.18 N

ANISOU 526 N LYS A 71 14561 15948 16672 -1612 110 884 N

ATOM 527 CA LYS A 71 49.938 110.267 -3.228 1.00128.90 C

ANISOU 527 CA LYS A 71 15263 16626 17086 -1783 73 876 C

ATOM 528 CB LYS A 71 49.029 111.037 -2.243 1.00128.62 C

ANISOU 528 CB LYS A 71 15474 16598 16798 -1888 127 834 C ATOM 529 CG LYS A 71 48.688 110.331 -0.908 1.00133.88 C

ANISOU 529 CG LYS A 71 16187 17291 17391 -1966 41 966 C

ATOM 530 CD LYS A 71 47.822 111.223 0.012 1.00132 .91 C

ANISOU 530 CD LYS A 71 16334 17181 16983 -2122 102 925 C

ATOM 531 CE LYS A 71 48.129 111.032 1.507 1.00140 .16 C

ANISOU 531 CE LYS A 71 17324 18160 17772 -2292 -36 1078 C

ATOM 532 NZ LYS A 71 49.310 111.821 2.023 1.00138 .21 N

ANISOU 532 NZ LYS A 71 17256 17979 17278 -2526 -96 1088 N

ATOM 533 C LYS A 71 51.302 109.937 -2.598 1.00142 .33 C

ANISOU 533 C LYS A 71 16825 18418 18836 -1903 -110 1042 C

ATOM 534 O LYS A 71 51.560 108.795 -2.202 1.00146 60 O

ANISOU 534 O LYS A 71 17225 18964 19512 -1869 -216 1185 O

ATOM 535 N ASP A 72 52.184 110.931 -2.530 1.00158 02 N

ANISOU 535 N ASP A 72 18846 20473 20722 -2044 -150 1030 N

ATOM 536 CA ASP A 72 53.343 110.821 -1.655 1.00163. 90 C

ANISOU 536 CA ASP A 72 19490 21317 21466 -2204 -347 1198 C

ATOM 537 CB ASP A 72 54.660 111.006 -2.404 1.00169. 87 C

ANISOU 537 CB ASP A 72 20040 22102 22402 -2196 -376 1216 C

ATOM 538 CG ASP A 72 55.865 110.506 -1.598 1.00184. 71 C

ANISOU 538 CG ASP A 72 21717 24070 24393 -2304 -598 1434 C

ATOM 539 ODl ASP A 72 55.648 109.891 -0.528 1.00183. 86 O

ANISOU 539 ODl ASP A 72 21682 24014 24163 -2427 -747 1562 O

ATOM 540 0D2 ASP A 72 57.025 110.719 -2.032 1.00191. 84 p

ANISOU 540 0D2 ASP A 72 22392 24987 25511 -2269 -622 1482 O

ATOM 541 C ASP A 72 53.224 111.818 -0.506 1.00168. 19 C

ANISOU 541 C ASP A 72 20280 21925 21699 -2433 -395 1194 C

ATOM 542 O ASP A ■72 53.673 112.961 -0.598 1.00164! 58 O

ANISOU 542 O ASP A 72 19913 21502 21119 -2549 -372 1121 O

ATOM 543 N ASN A 73 52.587 111.360 0.568 1.00182. .84 N

ANISOU 543 N ASN A 73 22261 23784 23425 -2498 -446 1269 N

ATOM 544 CA ASN A 73 52.409 112.122 1.796 1.00179. 32 C

ANISOU 544 CA ASN A 73 22089 23376 22668 -2717 -473 1271 C

ATOM 545 CB ASN A 73 52.185 111.157 2.972 1.00181. 97 C

ANISOU 545 CB ASN A 73 22460 23727 22955 -2781 -596 1428 C

ATOM 546 CG ASN A 73 52.945 109.817 2.806 1.00191. 86 C

ANISOU 546 CG ASN A 73 23408 24998 24492 -2677 -755 1601 C

ATOM 547 ODl ASN A 73 53.933 109.551 3.502 1.00188. 82 O

ANISOU 547 ODl ASN A 73 22879 24693 24171 -2786 -959 1757 O

ATOM 548 ND2 ASN A 73 52.474 108.975 1.886 1.00191. 27 N

ANISOU 548 ND2 ASN A 73 23234 24843 ' 24595 -2466 -661 1579 N

ATOM 549 C ASN A 73 53.583 113.049 2.083 1.00183. 35 C

ANISOU 549 C ASN A 73 22642 23975 23047 -2940 -594 1306 C

ATOM 550 O ASN A 73 53.386 114.199 2.466 1.00181. 61 O

ANISOU 550 O ASN A 73 22684 23757 22562 -3096 -531 1219 O

ATOM 551 N SER A 74 54.798 112.541 1.870 1.00178. 43 N

ANISOU 551 N SER A 74 21757 23419 22621 -2955 -762 1437 N

ATOM 552 CA SER A 74 56.029 113.230 2.272 1.00176. 10 C

ANISOU 552 CA SER A 74 21447 23221 22242 -3180 -921 1511 C

ATOM 553 CB SER A 74 57.207' 112.245 2.481 1.00178. 85 C

ANISOU 553 CB SER A 74 21477 23644 22832 -3200 -1162 1739 C

ATOM 554 OG SER A 74 57.581 111.538 1.305 1.00172. 14 O

ANISOU 554 OG SER A 74 20330 22754 22323 -2969 -1090 1731 O

ATOM 555 C SER A 74 56.422 114.373 1.348 1.00171. 50 C

ANISOU 555 C SER A 74 20888 22627 21646 -3176 -785 1348 C

ATOM 556 O SER A 74 56.688 115.474 1.814 1.00171. 00 O

ANISOU 556 O SER A 74 21052 22588 21332 -3366 -768 1278 O

ATOM 557 N LYS A 75 56.452 114.111 0.044 1.00169. 13 N

ANISOU 557 N LYS A 75 20375 22280 21606 -2966 -678 1285 N

ATOM 558 CA LYS A 75 56.843 115.125 -0.939 1.00163. 91 C

ANISOU 558 CA LYS A 75 19731 21595 20951 -2944 -536 1130 C

ATOM 559 CB LYS A 75 57.475 114.475 -2.186 1.00162. 02 C

ANISOU 559 CB LYS A 75 19209 21311 21040 -2730 -465 1119 C

ATOM 560 CG LYS A 75 58.395 113.270 -1.917 1.00166. 72 C

ANISOU 560 CG LYS A 75 .19488 21954 21905 -2699 -638 1328 C

ATOM 561 CD LYS A 75 59.860 113.662 -1.711 1.00178. 94 C

ANISOU 561 CD LYS A 75 20906 23613 23469 -2909 -822 1462 C

ATOM 562 CE LYS A 75 60.743 112.432 -1.460 1.00188. 06 C

ANISOU 562 CE LYS A 75 21695 24798 24963 -2838 -963 1668 C

ATOM 563 NZ LYS A 75 62.203 112.744 -1.353 1.00185. 56 N

ANISOU 563 NZ LYS A 75 21190 24579 24735 -3009 -1112 1789 N

ATOM 564 C LYS A 75 .55.653 116.018 -1.336 1.00157. 88 C

ANISOU 564 C LYS A 75 19261 20747 19979 -2899 -318 923 C

ATOM 565 O LYS A 75 55.717 116.753 -2.323 1.00153. 52 O

ANISOU 565 O LYS A 75 18745 20151 19436 -2841 -175 780 O

ATOM 566 N SER A 76 54.573 115.942 -0.560 1.00150. 50 N

ANISOU 566 N SER A 76 18534 19785 18865 -2927 -291 916 N

ATOM 567 CA SER A 76 53.392 116.788 -0.750 1.00143. 55 C ANISOU 567 CA SER A 76 17924 18818 17802 -2885 -84 744 C

ATOM 568 CB SER A 76 53.682 118.231 -0.353 1.00145.19 C

ANISOU .568 CB SER A 76 18381 19046 17739 -3104 -56 671 C

ATOM 569 OG SER A 76 54.457 118.287 0.829 1.00149.91 O

ANISOU 569 OG SER A 76 19027 19736 18196 -3351 -254 812 ' O

ATOM 570 C SER A 76 52.881 116.761 -2.171 1.00138.37 C

ANISOU 570 C SER A 76 17196 18072 17306 -2652 90 606 C

ATOM 571 O SER A 76 52.453 117.779 -2.706 1.00135.81 O

ANISOU 571 O SER A 76 17047 17687 16868 -2632 247 ' 457 O

ATOM 572 N GLN A 77 52.917 115.587 -2.778 1.00141.88 N

ANISOU 572 N GLN A 77 17393 18501 18013 -2483 60 660 N

ATOM 573 CA GLN A 77 52.445 115.442 -4.141 1.00141.70 C

ANISOU 573 CA GLN A 77 17313 18387 18138 -2274 209 537 C

ATOM 574 CB GLN A 77 53.639 115.417 -5.109 1.00144.73 C

ANISOU 574 CB GLN A 77 17505 18785 18700 -2245 200 532 C

ATOM 575 CG GLN A 77 54.891 114.737 -4.547 1.00151.61 C

ANISOU 575 CG GLN A 77 18098 19716 19790 -2246 45 704 C

ATOM 576 CD GLN A 77 56.110 114.849 -5.456 1.00151.83 C

ANISOU 576 CD GLN A 77 17950 19771 19966 -2273 39 711 C

ATOM 577 OEl GLN A 77 56.319 115.868 -6.118 1.00147.65 O

ANISOU 577 OEl GLN A 77 17527 19232 19343 -2327 133 593 O

ATOM 578 NE2 GLN A 77 56.930 113.799 -5.475 1.00154.65 N

ANISOU 578 NE2 GLN A 77 18037 20157 20565 -2234 -62 858 N

ATOM 579 C GLN A 77 51.531 114.214 -4.318 1.00141.37 C

ANISOU 579 C GLN A 77 17185 18285 18246 -2093 233 567 C

ATOM 580 O GLN A 77 51.882 113.096 -3.921 1.00141.83 O

ANISOU 580 O GLN A 77 17091 18375 18423 -2082 112 706 O

ATOM 581 N VAL A 78 50.342 114.450 -4.877 1.00137.69 N

ANISOU 581 N VAL A 78 16823 17727 17766 -1961 382 441 N

ATOM 582 CA VAL A 78 49.443 113.388 -5.316 1.00133.08 C

ANISOU 582 CA VAL A 78 16161 17072 17332 -1785 419 445 C

ATOM 583 CB VAL A 78 47.966 113.816 -5.243 1.00126.49 C

ANISOU 583 CB VAL A 78 15509 16172 16380 -1735 540 362 C

ATOM 584 CGl VAL A 78 47.089 112.621 -5.127 1.00124.47 C

ANISOU 584 CGl VAL A 78 15162 15845 16287 -1568 567 368 C

ATOM 585 CG2 VAL A 78 47.730 114.710 -4.072 1.00129.41 C

ANISOU 585 CG2 VAL A 78 16026 16584 16559 -1877 518 419 C

ATOM 586 C VAL A 78 49.772 113.146 -6.779 1.00133.01 C

ANISOU 586 C VAL A 78 16041 16999 17499 -1645 483 368 C

ATOM 587 O VAL A 78 49.870 114.094 -7.551 1.00133.14 O

ANISOU 587 O VAL A 78 16141 16989 17459 -1650 568 256 ' O

ATOM 588 N PHE A 79 49.960 111.892 -7.165 1.00140.99 N

ANISOU 588 N PHE A 79 16883 17973 18714 -1527 452 426 N

ATOM 589 CA PHE A 79 50.284 111.574 -8.547 1.00137.53 C

ANISOU 589 CA PHE A 79 16350 17462 18444 -1408 518 361 C

ATOM 590 CB PHE A 79 51.274 110.417 -8.587 1.00140.25 C

ANISOU 590 CB PHE A 79 16466 17822 19002 -1378 440 484 C

ATOM 591 CG PHE A 79 52.595 110.712 -7.924 1.00148.36 C

ANISOU 591 CG PHE A 79 17399 18954 20018 -1519 337 584 C

ATOM 592 CDl PHE A 79 53.659 109.822 -8.047 1.00157.99 C

ANISOU 592 CDl PHE A 79 18446 20174 21409 -1507 344 612 C

ATOM 593 CEl PHE A 79 54.884 110.080 -7.440 1.00165.84 C

ANISOU 593 CEl PHE A 79 19334 21269 22409 -1646 235 111 C

ATOM 594 CZ PHE A 79 55.059 111.246 -6.707 1.00160.30 C

ANISOU 594 CZ PHE A 79 18726 20666 21516 -1812 109 790 C

ATOM 595 CE2 PHE A 79 54.009 112.142 -6.585 1.00156.05 C

ANISOU 595 CE2 PHE A 79 18385 20118 20789 -1827 120 751 C

ATOM 596 CD2 PHE A 79 52.785 111.874- -7.195 1.00152.53 C

ANISOU 596 CD2 PHE A 79 18018 19574 20364 -1675 238 651 C

ATOM 597 C PHE A 79 48.993 111.220 -9.297 1.00137.77 C

ANISOU 597 C PHE A 79 16447 17390 18511 -1269 602 277 C

ATOM 598 O PHE A 79 47.907 111.412 -8.758 1.00139.41 O

ANISOU 598 O PHE A 79 16765 17588 18615 -1268 619 264 O

ATOM 599 N LEU A 80 49.106 110.730 -10.535 1.00131.49 N

ANISOU 599 N LEU A 80 15593 16510 17858 -1163 659 222 N

ATOM 600 CA LEU A 80 47.955 110.251 -11.324 1.00126.42 C

ANISOU 600 CA LEU A 80 15003 15766 17263 -1046 710 159 C

ATOM 601 CB LEU A 80 47.132 111.418 -11.866 1.00119.37 c

ANISOU 601 CB LEU A 80 14293 14835 16227 -1040 782 40 C

ATOM 602 CG LEU A 80 45.684 111.109 -12.253 1.00116.91 C

ANISOU 602 CG LEU A 80 14025 14440 15954 -943 796 12 C

ATOM 603 CDl LEU A 80 45.122 112.242 -13.056 1.00114.49 C

ANISOU 603 CDl LEU A 80 13878 14098 15525 -936 854 -82 C

ATOM 604 CD2 LEU A 80 45.554 109.818 -13.025 1.00122.24 C

ANISOU 604 CD2 LEU A 80 14640 15022 16782 -857 805 -10 C

ATOM 605 C LEU A 80 48.455 109.455 -12.510 1.00126.82 C

ANISOU 605 C LEU A 80 14978 15730 17477 -962 758 125 C ATOM 606 O LEU A 80 49.359 109.913 -13.194 1.00134.10 O

ANISOU 606 O LEU A 80 15913 16637 18401 -980 819 61 O

ATOM 607 N LYS A 81 47.872 108.286 -12.771 1.00124 .65 N

ANISOO 607 N LYS A 81 14641 15387 17334 -875 745 160 N

ATOM 608 CA LYS A 81 48.243 107.508 -13.957 1.00132 .41 C

ANISOU 608 CA LYS A 81 15584 16262 18464 -797 812 118 C

ATOM 609 CB LYS A 81 49.100 106.302 -13.578 1.00141 .02 C

ANISOU 609 CB LYS A 81 16485 17353 19742 -769 783 237 C

ATOM 610 CG LYS A 81 50.133 105.906 -14.644 1.00149 .99 C

ANISOU 610 CG LYS A 81 17559 18402 21028 -721 889 200 C

ATOM 611 CD LYS A 81 51.532 105.659 -14.009 1.00156 26 C

ANISOU 611 CD LYS A 81 18151 19267 21954 -750 855 323 C

ATOM 612 CE LYS A 81 51.938 106.781 -13.009 1.00149 .08 C

ANISOU 612 CE LYS A 81 17241 18505 20896 -875 765 365 C

ATOM 613 NZ LYS A 81 53.295 106.636 -12.376 1.00144. 12 N

ANISOU 613 NZ LYS A 81 16412 17966 20382 -926 672 522 N

ATOM 614 C LYS A 81 47.040 107.054 -14.759 1.00133 45 C

ANISOU 614 C LYS A 81 15808 16287 18610 -725 832 57 C

ATOM 615 O LYS A 81 46.046 106.616 -14.202 1.00136. 65 O

ANISOU 615 O LYS A 81 16212 16700 19007 -709 774 105 O

ATOM 616 N MET A 82 47.137 107.165 -16.075 1.00147. 57 N

ANISOU 616 N MET A 82 17682 17972 20415 -693 914 -46 N

ATOM 617 CA MET A 82 46.040 106.789 -16.953 1.00151. 46 C

ANISOU 617 CA MET A 82 18287 18358 20901 -647 918 -109 C

ATOM 618 CB MET A 82 45.194 108.010 -17.320 1.00143. 76 C

ANISOU 618 CB MET A 82 17466 17392 19764 -674 907 -187 C

ATOM 619 CG MET A 82 43.991 107.666 -18.166 1.00146. 22 C

ANISOU 619 CG MET A 82 17873 17613 20072 -640 872 -223 C

ATOM 620 SD MET A 82 42.593 108.764 -17.898 1.00150. 33 S

ANISOU 620 SD MET A 82 18515 18161 20443 -655 834 -261 S

ATOM 621 CE MET A 82 42.901 109.988 -19.157 1.00153. 91 C

ANISOU 621 CE MET A 82 19156 18511 20812 -669 887 -388 C

ATOM 622 C MET A 82 46.607 106.140 -18.204 1.00155. 75 C

ANISOU 622 C MET A 82 18874 18769 21534 -612 1012 -177 C

ATOM 623 O MET A 82 47.434 106.740 -18.890 1.00159. 67 O

ANISOU 623 O MET A 82 19403 19247 22019 -632 1101 -238 O

ATOM 624 N ASN A 83 46.170 104.917 -18.498 1.00153. 58 N

ANISOU 624 N ASN A 83 18617 18395 21342 -569 1003 -171 N

ATOM 625 CA ASN A 83 46.766 104.123 -19.572 1.00154. 51 C

ANISOU 625 CA ASN A 83 18777 18370 21559 -538 1109 -223 C

ATOM 626 CB ASN A 83 46.921 102.688 -19.112 1.00149. 12 C

ANISOU 626 CB ASN A 83 17967 17644 21048 -485 1102 -128 C

ATOM 627 CG ASN A 83 46.703 102.558 -17.630 1.00162. 21 C

ANISOU 627 CG ASN A 83 19447 19439 22745 -485 1005 C

ATOM 628 ODl ASN A 83 45.729 101.947 -17.188 1.00163. 86 O

ANISOU 628 ODl ASN A 83 19634 19674 22950 -481 914 68 O

ATOM 629 ND2 ASN A 83 47.579 103.183 -16.844 1.00166. 18 N

ANISOU 629 ND2 ASN A 83 19833 20033 23274 -503 1019 56 N

ATOM 630 C ASN A 83 45.904 104.159 -20.806 1.00154. 27 C

ANISOU 630 C ASN A 83 18956 18221 21440 -555 1120 -330 C

ATOM 631 O ASN A 83 44.799 104.709 -20.775 1.00151. 64 O

ANISOU 631 O ASN A 83 18698 17916 21003 -577 1023 -340 O

ATOM 632 N SER A 84 46.407 103.574 -21.888 1.00140. 32 N

ANISOU 632 N SER A 84 17287 16315 19713 -550 1241 -405 N

ATOM 633 CA SER A 84 45.661 103.559 -23.133 1.00141. 57 C

ANISOU 633 CA SER A 84 17669 16344 19777 -585 1242 -502 C

ATOM 634 CB SER A 84 44.771 102.319 -23.194 1.00142. 41 C

ANISOU 634 CB SER A 84 17783 16373 19955 -572 1176 -462 C

ATOM 635 OG SER A 84 43.812 102.441 -24.227 1.00141. 52 O

ANISOU 635 OG SER A 84 17884 16155 19734 -627 ' 1127 -536 O

ATOM 636 C SER A 84 44.800 104.817 -23.246 1.00142. 58 C

ANISOU 636 C SER A 84 17903 16536 19734 -629 1140 -538 C

ATOM 637 O SER A 84 43.591 104.779 -23.011 1.00142. 95 O

ANISOU 637 O SER A 84 17980 16591 19744 -638 ' lO14 -510 O

ATOM 638 N LEU A 85 •45.426 105.936 -23.587 1.00131. 20 N

ANISOU 638 N LEU A 85 16510 15139 18201 -655 1196 -591 N

ATOM 639 CA LEU A 85 44.706 107.186 -23.746 1.00128. 30 C

ANISOU 639 CA LEU A 85 16254 14816 17679 -689 1114 -623 C

ATOM 640 CB LEU A 85 45.661 108.338 -23.602 1.00128. 31 C

ANISOU 640 CB LEU A 85 16258 14893 17601 ^ " -714 1181 -658 C

ATOM 641 CG LEU A 85 45.447 109.045 -22.287 1.00128. 71 C

ANISOU 641 CG LEU A 85 16149 15100 17656 -703 1114 -572 C

ATOM 642 CDl LEU A 85 46.774 109.591 -21.866 1.00129. 81 C

ANISOU 642 CDl LEU A 85 16118 15301 17901 -699 1186 -524 C

ATOM 643 CD2 LEU A 85 44.418 110.140 -22.479 1.00126. 00 C

ANISOU 643 CD2 LEU A 85 15908 14807 17160 -736 1097 -612 C

ATOM 644 C LEU A 85 44.048 107.303 -25.090 1.00128. 73 C ANISOU 644 C LEU A 85 16539 14736 17636 -731 1096 -705 C

ATOM 645 O LEU A 85 44.486 106.695 -26.049 1.00130.49 O

ANISOU 645 O LEU A 85 16869 14829 17883 -749 1183 -762 O

ATOM 646 N GLN A 86 43.004 108.113 -25.172 1.00149.78 N

ANISOU 646 N GLN A 86 19291 17426 20191 -751 986 -706 N

ATOM 647 CA GLN A 86 42.326 108.267 -26.447 1.00155.98 C

ANISOU 647 CA GLN A 86 20305 18090 20869 -804 934 -768 C

ATOM 648 CB GLN A 86 41.208 107.239 -26.612 1.00162.16 C

ANISOU 648 CB GLN A 86 21100 18807 21706 -815 814 -724 C

ATOM 649 CG GLN A 86 41.732 105.878 -27.071 1.00164.97 C

ANISOU 649 CG GLN A 86 21515 19037 22129 -834 911 -765 C

ATOM 650 CD GLN A 86 42.767 105.995 -28.192 1.00166.60 C

ANISOU 650 CD GLN A 86 21917 19131 22254 -878 1071 -879 C

ATOM 651 OEl GLN A 86 43.739 105.239 -28.232 1.00164.64 O

ANISOU 651 OEl GLN A 86 21627 18835 22093 -855 1235 -907 O

ATOM 652 NE2 GLN A 86 42.563 106.953 -29.102 1.00166.31 N

ANISOU 652 NE2 GLN A ' 86 22093 19044 22055 -941 1030 -939 N

ATOM 653 C GLN A 86 41.848 109.669 -26.768 1.00152.14 C

ANISOU 653 C GLN A 86 19930 17632 20246 -825 869 -787 C

ATOM 654 O GLN A 86 41.792 110.538 -25.907 1.00150.22 O

ANISOU 654 O GLN A 86 19585 17501 19990 -794 867 -753 O

ATOM ' 655 N THR A 87 41.506 109.863 -28.032 1.00161.19 N

ANISOU 655 N THB A 87 21300 18661 21284 -884 819 -840 N

ATOM 656 ' CA THR A 87 41.391 111.190 -28.594 1.00164.07 C

ANISOU 656 CA THR A 87 21822 19013 21505 -914 795 -878 C

ATOM 657 CB THR A 87 41.058 111.128 -30.084 1.00172.71 C

ANISOU 657 CB THR A 87 23185 19956 22482 -997 725 -927 C

ATOM 658 OGl THR A 87 39.663 110.853 -30.245 1.00177.82 O

ANISOU 658 OGl THR A 87 23804 20589 23172 -1003 532 -846 O

ATOM 659 CG2 THR A 87 41.887 110.040 -30.773 1.00174.26 C

ANISOU 659 CG2 THR A 87 23508 20029 22673 -1049 867 -1014 C

ATOM 660 C THR A 87 40.366 112.051 -27.881 1.00166.46 C

ANISOU 660 C THR A 87 22018 19417 21813 -864 681 -797 C

ATOM 661 O THR A 87 40.280 113.248 -28.140 1.00168.15 O

ANISOU 661 O THR A 87 22329 19637 21925 -870 678 -816 O

ATOM 662 N ASP A 88 39.590 111.467 -26.97,8 1.00182.23 N

ANISOU 662 N ASP A 88 23823 21484 23931 -815 603 -706 N

ATOM 663 CA ASP A 88 38.627 112.278 -26.239 1.00185.69 C

ANISOU 663 CA ASP A 88 24157 22005 24391 -763 525 -628 C

ATOM 664 CB ASP A 88 37.217 111.725 -26.381 1.00190.52 C

ANISOU 664 CB ASP A 88 24723 22586 25079 -756 357 -543 C

ATOM 665 CG ASP A 88 37.163 110.246 -26.159 1.00196.49 C

ANISOU 665 CG ASP A 88 25431 23302 25924 -781 328 -530 C

ATOM 666 ODl ASP A 88 37.793 109.758 -25.191 1.00190.80 O

ANISOU 666 ODl ASP A 88 24581 22637 25279 -755 423 -527 O

ATOM 667 0D2 ASP A 88 36.491 109.573 -26.963 1.00210.48 O

ANISOU 667 0D2 ASP A 88 27301 24983 27687 -834 203 -517 O

ATOM 668 C ASP A 88 38.988 112.480 -24.770 1.00177.42 C

ANISOU 668 C ASP A 88 22914 21089 23409 -711 604 -586 C

ATOM 669 O ASP A 88 38.260 113.157 -24.044 1.00172.17 O

ANISOU 669 O ASP A 88 22177 20485 22754 -670 578 -531 O

ATOM 670 N ASP A 89 40.102 111,888 -24.340 1.00149.93 N

ANISOU 670 N ASP A 89 , 19352 17640 19973 -717 701 -606 N

ATOM 671 CA ASP A 89 40.710 112.232 -23.056 1.00143.40 C

ANISOU 671 CA ASP A 89 18381 16933 19171 -697 776 -577 C

ATOM 672 CB ASP A 89 41.600 111.117 -22.550 1.00139.89 C

ANISOU 672 CB ASP A 89 17814 16510 18829 -695 831 -560 C

ATOM 673 CG ASP A 89 40.906 109.789 -22.539 1.00146.65 C

ANISOU 673 CG ASP A 89 18623 17309 19788 -679 756 -516 C

ATOM 674 ODl ASP A 89 39.658 109.757 -22.443 1.00143.39 O

ANISOU 674 ODl ASP A 89 18205 16887 19391 -666 650 -469 O

ATOM 675 0D2 ASP A 89 41.619 108.773 -22.635 1.00154.21 O

ANISOU 675 0D2 ASP A 89 19548 18223 20820 -681 809 -526 O

ATOM 676 C ASP A 89 41.545 113.476 -23.271 1.00141.76 C

ANISOU 676 C ASP A 89 18280 16742 18842 -728 865 -645 C

ATOM 677 O ASP A 89 42.105 114.051 -22.333 1.00137.54 O

ANISOU 677 O ASP A 89 17672 16301 18286 -734 924 -632 O

ATOM 678 N THR A 90 41.651 113.857 -24.536 1.00147.92 N

ANISOU 678 N THR A 90 19247 17423 19531 -760 870 -717 N

ATOM 679 CA THR A 90 42.078 115.186 -24.899 1.00144.15 C

ANISOU 679 CA THR A 90 18900 16944 18925 -789 932 -776 C

ATOM 680 CB THR A 90 41.671 115.486 -26.345 1.00144.58 C

ANISOU 680 CB THR A 90 19182 16872 18879 -825 899 -837 C

ATOM 681 OGl THR A 90 42.607 114.876 -27.237 1.00148.13 O

ANISOU 681 OGl THR A 90 19720 17251 19310 -876 1001 -917 O

ATOM 682 CG2 THR A 90 41.669 116.959 -26.599 1.00149.22 C

ANISOU 682 CG2 THR A 90 19899 17456 19341 -836 921 -866 C ATOM 683 C THR A 90 41.306 116.095 -23.970 1.00142.30 C

ANISOU " 683 C THR A 90 18620 16779 18669 -752 896 -721 C

ATOM 684 O THR A 90 40.107 116.297 -24.167 1.00144 .88 O

ANISOU 684 O THR A 90 18980 17065 19002 -717 800 -679 O

ATOM 685 N ALA A 91 41.967 116.611 -22.936 1.00130 .80 N

ANISOU 685 N ALA A 91 17083 15420 17194 -763 973 -714 N

ATOM 686 CA ALA A 91 41.261 117.398 -21.930 1.00128 .13 C

ANISOU 686 CA ALA A 91 16723 15133 16826 -735 970 -669 C

ATOM 687 CB ALA A 91 40.353 116.514 -21.134 1.00126 25 C

ANISOU 687 CB ALA A 91 16332 14934 16704 -681 904 -578 C

ATOM 688 C ALA A 91 42.160 118.164 -20.979 1.00130 09 C

ANISOU 688 C ALA A 91 16963 15467 16998 -785 1067 -690 C

ATOM 689 O ALA A 91 43.375 117.971 -20.947 1.00132 32 O

ANISOU 689 O ALA A 91 17250 15774 17251 -845 1130 -738 O

ATOM 690 N ARG A 92 41.525 119.026 -20.190 1.00130. 61 N

ANISOU 690 N ARG A 92 17019 15571 17035 -765 1083 -650 N

ATOM 691 CA ARG A 92 42.184 119.783 -19.140 1.00127, 96 C

ANISOU 691 CA ARG A 92 16701 15310 16608 -826 1167 -662 C

ATOM 692 CB ARG A 92 41.558 121.175 -19.066 1.00128. 56 C

ANISOU 692 N CB ARG A 92 16917 15337 16592 -804 1216 -678 C

ATOM 693 CG ARG A 92 42.143 122.080 -18.018 1.00130. 73 C

ANISOU 693 CG ARG A 92 17252 15670 16750 -877 1312 -696 C

ATOM 694 CD ARG A 92 41.729 123.545 -18.222 1.00131. 59 C

ANISOU 694 CD ARG A 92 17553 15701 16745 -873 1382 -747 C

ATOM 695 NE ARG A 92 42.759 124.300 -18.930 1.00134. 63 N

ANISOU 695 NE ARG A 92 18047 16080 17025 -960 1422 -828 N

ATOM 696 CZ ARG A 92 43.953 124.584 -18.420 1.00134. 72 C

ANISOU 696 CZ ARG A 92 18078 16163 16947 -1073 1483 -859 C

ATOM 697 NHl ARG A 92 44.267 124.175 -17.198 1.00136. 88 N

ANISOU 697 NHl ARG A 92 18287 16516 17206 -1116 1500 -814 N

ATOM 698 NH2 ARG A 92 44.840 125.265 -19.132 1.00134. 48 N

ANISOU 698 NH2 ARG A 92 18134 16124 16840 -1152 1525 -929 N

ATOM 699 C ARG A 92 42.052 119.014 -17.814 1.00124. 95 C

ANISOU 699 C ARG A 92 16163 15018 16296 -828 1151 -583 C

ATOM 700 O ARG A 92 40.953 118.700 -17.361 1.00123. 25 O

ANISOU 700 O ARG A 92 15888 14792 16148 -766 1121 -523 O

ATOM 701 N TYR A 93 43.186 118.682 -17.212 1.00120. 25 N

ANISOU 701 N TYR A 93 15495 14506 15690 -903 1167 -576 N

ATOM 702 CA TYR A 93 43.209 117.815 -16.046 1.00116. 80 C

ANISOU 702 CA TYR A 93 14909 14146 15324 -912 1129 -493 C

ATOM 703 CB TYR A 93 44.254 116.706 -16.235 1.00113. 96 C

ANISOU 703 CB TYR A 93 14422 13818 15060 -934 1092 -474 C

ATOM 704 CG TYR A 93 43.758 115.650 -17.179 1.00117. 47 C

ANISOU 704 CG TYR A 93 14824 14184 15625 -855 1046 -475 C

ATOM 705 CDl TYR A 93 44.088 115.667 -18.524 1.00119. 79 C

ANISOU 705 CDl TYR A 93 15191 14400 15922 -850 1070 -549 C

ATOM . 706 CEl TYR A 93 43.586 114.715 -19.389 1.00119. 21 C

ANISOU 706 CEl TYR A 93 15113 14243 15938 -797 1029 -554 C

ATOM 707 CZ TYR A 93 42.738 113.739 -18.903 1.00118. 29 C

ANISOU 707 CZ TYR A 93 14902 14125 15918 -746 957 -482 C

ATOM 708 OH TYR A 93 42.214 112.767 -19.716 1.00123. 95 O

ANISOU 708 OH TYR A 93 15625 14756 16714 -710 910 -486 O

ATOM 709 CE2 TYR A 93 42.399 113.715 -17.584 1.00117. 05 C

ANISOU 709 CE2 TYR A 93 14656 14047 15769 -743 938 -407 C

ATOM 710 CD2 TYR A 93 42.898 114.670 -16.737 1.00117. 97 C

ANISOU 710 CD2 TYR A 93 14795 14241 15787 -797 986 -406 C

ATOM 711 C TYR A 93 43.520 118.617 -14.809 1.00123. 56 C

ANISOU 711 C TYR A 93 15803 15077 16068 -995 1176 -473 C

ATOM 712 O TYR A 93 44.692 118.770 -14.468 1.00128. 77 O

ANISOU 712 O- TYR A 93 16430 15807 16688 -1088 1173 -470 O

ATOM 713 N TYR A 94 42.478 119.141 -14.153 1.00128. 04 N

ANISOU 713 N TYR A 94 16441 15624, 16586 -970 1221 -458 N '

ATOM 714 CA TYR A 94 42.622 119.850 -12.875 1.00128. 19 C

ANISOU 714 CA TYR A 94 16526 15700 16480 -1062 1280 -442 C

ATOM 715 CB TYR A 94 41.358 120.615 -12.536 1.00120. 33 C

ANISOU 715 CB TYR A 94 15639 14641 15439 -1014 1373 -445 C

ATOM 716 CG TYR A 94 40.961 121.666 -13.507 1.00128. 77 C

ANISOU 716 CG TYR A 94 16830 15614 16483 -950 1423 -508 C

ATOM 717 CDl TYR A 94 41.527 122.926 -13.469 1.00137. 03 C

ANISOU 717 CDl TYR A 94 18047 16639 17379 -1019 1506 -575 C

ATOM 718 CEl TYR A 94 41.135 123.920 -14.362 1.00138. 39 C

ANISOU 718 CEl TYR A 94 18343 16711 17528 -955 1552 -625 C

ATOM 719 CZ TYR A 94 40.157 123.648 -15.300 1.00137. 61 C

ANISOU 719 CZ TYR A 94 18190 16538 17558 -828 1498 -600 C

ATOM 720 OH TYR A 94 39.750 124.610 -16.206 1.00138. 98 O

ANISOU 720 OH TYR A 94 18483 16609 17715 -765 1521 -631 O

ATOM 721 CE2 TYR A 94 39.580 122.398 -15.340 1.00135. 89 C ANISOU 721 CE2 TYR A 94 17802 16344 17486 -770 1410 -534 C

ATOM 722 CD2 TYR A 94 39.982 121.420 -14.440 1.00132.33 C

ANISOϋ 722 CD2 TYR A 94 17235 15988 17056 -828 1381 -493 C

ATOM 723 C TYR A 94 42.859 118.887 -11.714 1.00132.44 C

ANISOU 723 C TYR A 94 16939 16322 17060 -1108 1225 -353 C

ATOM 724 O TYR A 94 42.489 117.712 -11.778 1.00128.16 O

ANISOU 724 O TYR A 94 16260 15780 16655 -1042 1159 -298 O

ATOM 725 N CYS A 95 43.444 119.388 -10.632 1.00127.17 N

ANISOU 725 N CYS A 95 16334 15720 16263 -1232 1248 -335 N

ATOM 726 CA CYS A 95 43.480 118.619 -9.398 1.00123.44 C

ANISOU 726 CA CYS A 95 15786 15319 15796 -1289 1199 -243 C

ATOM 727 CB CYS A 95 44.848 118.024 -9.184 1.00122.75 C

ANISOU 727 CB CYS A 95 15588 15323 15730 -1382 1094 - -194 C

ATOM 728 SG CYS A 95 45.865 119.021 -8.154 1.00136.21 S

ANISOU 728 SG CYS A 95 17414 17106 17233 -1583 1093 -194 S

ATOM 729 C CYS A 95 43.141 119.546 -8.256 1.00125.49 , C

ANISOU 729 C CYS A 95 16215 15581 15886 -1380 1292 -247 C

ATOM 730 O CYS A 95 43.654 120.652 -8.195 1.00132.76 O

ANISOU 730 O CYS A 95 17274 16510 16660 -1481 1337 -300 O

ATOM 731 N ALA A 96 42.264 119.115 -7.359 1.00119.63 N

ANISOU 731 N ALA A 96 15474 14821 15158 -1351 1335 -195 N

ATOM 732 CA ALA A 96 41.761 120.024 -6.333 1.00123.93 C

ANISOU 732 CA ALA A 96 16203 15339 15547 -1424 1463 -208 C

ATOM 733 CB ALA A 96 40.501 120.720 -6.800 1.00121.48 C

ANISOU 733 CB ALA A 96 15954 14915 15289 -1291 1601 -250 C

ATOM 734 C ALA A 96 41.536 119.355 -4.987 1.00127.08 C

ANISOU 734 C ALA A 96 16593 15786 15905 -1504 1445 -119 C

ATOM 735 O ALA A 96 41.340 118.141 -4.907 1.00121.29 O

ANISOU 735 O ALA A 96 15695 15101 15289 -1478 1333 -41 O

ATOM 736 N ARG A 97 41.558 120.176 -3.939 1.00135.95 N

ANISOU 736 N ARG A 97 17914 16886 16854 -1607 1565 -132 N

ATOM 737 CA ARG A 97 41.575 119.695 -2.563 1.00136.18 C

ANISOU 737 CA ARG A 97 17997 16964 16783 -1734 1548 -54 C

ATOM 738 CB ARG A 97 42.281 120.703 -1.660 1.00132.22 C

ANISOU 738 CB ARG A 97 17718 16493 16028 -1944 1568 -78 C

ATOM 739 CG ARG A 97 42.824 120.079 -0.391 1.00134.95 C

ANISOU 739 CG ARG A 97 18081 16927 16267 -2116 1449 24 C

ATOM 740 CD ARG A 97 43.096 121.131 0.628 1.00137.67 C

ANISOU 740 CD ARG A 97 18712 17266 16330 -2333 1518 -2 C

ATOM 741 NE ARG A 97 41.979 122.053 0.646 1.00138.58 N

ANISOU 741 NE ARG A 97 19032 17253 16368 -2285 1770 -91 N

ATOM 742 CZ ARG A 97 41.915 123.113 1.430 1.00136.85 C

ANISOU 742 CZ ARG A 97 19108 16985 15905 -2449 1901 -135 C

ATOM 743 NHl ARG A 97 42.913 123.375 2.263 1.00133.83 N

ANISOU 743 NHl ARG A 97 18852 16680 15316 -2690 1779 -95 N

ATOM 744 NH2 ARG A 97 40.853 123.902 1.379 1.00133.74 N

ANISOU 744 NH2 ARG A 97 18880 16456 15479 -2376 2153 -213 N

ATOM 745 C ARG A 97 40.190 119.392 -1.999 1.00137.61 C

ANISOU 745 C ARG A 97 18212 17072 17001 -1668 1690 -25 C

ATOM 746 O ARG A 97 39.246 120.162 -2.192 1.00132.44 O

ANISOU 746 O ARG A 97 17672 16318 16333 -1602 1874 -83 O

ATOM 747 N ASP A 98 40.084 118.270 -1.291 1.00144.58 N

ANISOU 747 N ASP A 98 18992 18002 17940 -1686 1608 71 N

ATOM 748 CA ASP A 98 38.825 117.859 -0.685 1.00144.26 C

ANISOU 748 CA ASP A 98 18962 17903 17948 -1636 1732 112 C

ATOM 749 CB ASP A 98 38.408 116.471 -1.189 1.00142.72 C

ANISOU 749 CB ASP A 98 18514 17721 17992 -1500 1629 180 C

ATOM 750 CG ASP A 98 36.898 116.228 -1.088 1.00146.90 C

ANISOU 750 CG ASP A 98 19004 18160 18651 -1379 1784 192 C

ATOM 751 ODl ASP A 98 36.203 116.415 -2.120 1.00144.86 O

ANISOU 751 ODl ASP A 98 18637 17845 18559 -1226 1813 158 O

ATOM 752 0D2 ASP A 98 36.411 115.859 0.013 1.00143.18 O

ANISOU 752- 0D2 ASP A 98 18609 17674 18119 -1444 1875 242 O

ATOM 753 C ASP A 98 38.930 117.847 0.831 1.00144.16 C

ANISOU 753 C ASP A 98 19127 17917 17729 -1826 1760 167 C

ATOM 754 O ASP A 98 39.429 116.874 1.403 1.00138.59 O

ANISOU 754 O ASP A 98 18355 17298 17003 -1916 1592 256 O

ATOM 755 N PRO A 99 38.476 118.942 1.482 1.00122.57 N

ANISOU 755 N PRO A 99 16636 15101 14834 -1893 1973 115 ' N

ATOM 756 CA PRO A 99 38.333 118.990 2.937 1.00117.60 C

ANISOU 756 CA PRO A 99 16222 14459 14003 -2064 2060 155 C

ATOM 757 CB PRO A 99 37.991 120.459 3.218 1.00125.88 C

ANISOU 757 CB PRO A 99 17549 15404 14874 -2123 2296 53 C

ATOM 758 CG PRO A 99 38.258 121.200 1.969 1.00117.64 C

ANISOU 758 CG PRO A 99 16427 14336 13936 -1992 2299 -29 C

ATOM 759 CD PRO A 99 38.072 120.215 0.860 1.00118.90 C

ANISOU 759 CD PRO A 99 16271 14533 14374 -1803 2162 13 C ATOM 760 C PRO A 99 37.132 118.152 3.258 1.00120.29 C

ANISOU 760 C PRO A 99 16468 14742 14493 -1953 2171 206 C

ATOM 761 O PRO A 99 36.043 118.700 3.320 1.00120.29 O

ANISOU 761 O PRO A 99 16528 14629 14546 -1859 2405 158 O

ATOM 762 N TYR A 100 37.307 116.851 3.434 1.00130.91 N

ANISOU 762 N TYR A 100 17657 16157 15927 -1957 2012 306 N

ATOM 763 CA TYR A 100 36.151 115.992 3.542 ' 1.00129.16 C

ANISOU 763 CA TYR A 100 17294 15886 15896 -1828 2092 355 C

ATOM 764 CB TYR A 100 36.509 114.555 3.253 1.00126.12 C

ANISOU 764 CB TYR A 100 16684 15584 15651 -1799 1865 455 C

ATOM 765 CG TYR A 100 37.767 114.028 3.865 1.00120.62 C

ANISOU 765 CG TYR A 100 16020 14993 14816 -1962 1646 529 C

ATOM 766 CDl TYR A 100 38.990 114.255 3.269 1.00128.10 C

ANISOU 766 CDl TYR A 100 16860 16019 15795 -1962 1456 522 C

ATOM 767 CEl TYR A 100 40.146 113.730 3.790 1.00132.99 C

ANISOU 767 CEl TYR A 100 17470 16733 16326 -2101 1248 610 C

ATOM 768 CZ TYR A 100 40.080 112.946 4.908 1.00132.17 C

ANISOU 768 CZ TYR A 100 17478 16652 16090 -2248 1207 711 C

ATOM 769 OH TYR A 100 ■ 41.234 112.410 5.422 1.00133.66 O

ANISOU 769 OH TYR A 100 17642 16935 16206 -2386 976 819 O

ATOM 770 CE2 TYR A 100 38.869 112.694 5.504 1.00128-.69 C

ANISOU 770 CE2 TYR A 100 17169 16132 15596 -2258 1397 712 C

ATOM 771 CD2 TYR A 100 37.725 113.228 4.978 1.00120.49 C

ANISOU 771 CD2 TYR A 100 16123 14997 14662 -2111 1623 620 C

ATOM 772 C TYR A 100 35.410 116.105 4.859 1.00129.91 C

ANISOU 772 C TYR A 100 17592 15897 15869 -1909 2325 367 C

ATOM 773 O TYR A 100 34.604 115.248 5.213 1.00128.58 O

ANISOU 773 O TYR A 100 17329 15678 15847 -1823 2427 408 O

ATOM 774 N GLY A 101 35.660 117.187 5.574 1.00138.65 N

ANISOU 774 N GLY A 101 18992 16981 16708 -2084 2423 325 N

ATOM 775 CA GLY A 101 34.921 117.446 6.788 1.00144.66 C

ANISOU 775 CA GLY A 101 19998 17647 17320 -2183 2671 324 C

ATOM 776 C GLY A 101 33.778 118.394 . 6.533 1.00140.41 C

ANISOU 776 C GLY A 101 19521 16967 16861 -2054 2977 234 C

ATOM 777 O GLY A 101 32.610 118.006 6.581 1.00138.75 O

ANISOU 777 O GLY A 101 19214 16676 16828 -1927 3154 254 O

ATOM 778 N SER A 102 34.136 119.640 6.249 1.00138.43 N

ANISOU 778 N SER A 102 . 19417 16685 16496 -2081 3034 143 N

ATOM 779 CA SER A 102 33.161 120.699 6.077 1.00147.73 C

ANISOU 779 CA SER A 102 20712 17711 17709 -1984 3347 60 C

ATOM 780 CB SER A 102 33.642 121.973 . 6.795 1.00156.97 C

ANISOU 780 CB SER A 102 22274 18819 18549 -2189 3495 -17 C

ATOM 781 OG SER A 102 32.591-122.651 7.482 1.00158.78 O

ANISOU 781 OG SER A 102 22697 ' 18871 18763 -2147 3870 -77 O

ATOM 782 C SER A 102 32.885 120.958 4.592 1.00141.16 C

ANISOU 782 C SER A 102 19653 16856 17127 -1756 3323 19 C

ATOM 783 O SER A 102 31.755 120.830 4.133 1.00141.58 O

ANISOU 783 O SER A 102 19625 16797 17372 -1588 3529 9 O

ATOM 784 N LYS A 103 33.918 121.282 3.831 1.00136.56 N

ANISOU 784 N LYS A 103 18962 16375 16550 -1752 3073 4 N

ATOM 785 CA LYS A 103 33.708 121.754 2.472 1.00138.24 C

ANISOU 785 CA LYS A 103 19031 16555 16940 ,-1572 3059 -46 C

ATOM 786 CB LYS A 103 34.572 123.004 2.251 1.00139.32 C

ANISOU 786 CB LYS A 103 19386 16674 16874 -1667 3081 -138 C

ATOM 787 CG LYS A 103 34.278 124.160 3.226 1.00139.15 C

ANISOU 787 CG LYS A 103 19700 16520 16651 -1766 3381 203 C

ATOM 788 CD LYS A 103 35.297 125.313 3.132 1.00141.56 C

ANISOU. 788 CD LYS A 103 20211 16814 16761 -1867 3374 -294 C

ATOM 789 CE LYS A 103 35.045 126.364 4.216 1.00150.60 C

ANISOU 789 CE LYS A 103 21741 17852 17629 -2044 3622 -355 C

ATOM 790 NZ LYS A 103 36.299 126.833 4.870 1.00157.89 N

ANISOU 790 NZ LYS A 103 22870 18869 18253 -2309 3458 •379 N

ATOM 791 C LYS A 103 33.958 120.693 1.374 1.00137.70 C

ANISOU 791 C LYS A 103 18653 16587 17080 -1455 2788 -2 C

ATOM 792 O LYS A 103 34.844 119.859 1.515 1.00135.41 O

ANISOU 792 O LYS A 103 18298 16414 16736 -1549 2566 40 O

ATOM 793 N PRO A 104 33.170 120.731 0.277 1.00139.49 N

ANISOU 793 N PRO A 104 18697 16757 17544 -1254 2808 ' -10 N

ATOM 794 CA PRO A 104- 33.408 119.962 -0.951 1.00137.06 C

ANISOU 794 CA PRO A 104 .18142 16512 17424 -1136 2583 7 C

ATOM 795 CB PRO A 104 32.231 120.338 -1.843 1.00135.25 C

ANISOU 795 CB PRO A 104 17841 16171 17377 -954 2700 -15 C

ATOM 796 CG PRO A 104 31.299 121.081 -0.999 1.00138.86 C

ANISOU 796 CG PRO A 104 18407 16515 17839 -935 2982 -7 C

ATOM 797 CD PRO A 104 32.070 121.681 0.103 1.00139.18 C

ANISOU 797 CD PRO A 104 18709 16570 17602 -1136 3079 -32 C

ATOM 798 C PRO A 104 34.646 120.548 -1.565 1.00139.25 C ANISOU 798 C PRO A 104 18490 16866 17552 -1229 2424 -47 C

ATOM 799 O PRO A 104 35.125 121.513 -0.995 1.00142 62 O

ANISOU 799 O PRO A 104 19130 17311 17748 -1392 2466 -79 O

ATOM 800 N MET A 105 35.151 120.049 -2.687 1.00139 .43 N

ANISOU 800 N MET A 105 18355 16927 17694 -1143 2252 -59 N

ATOM 801 CA MET A 105 36.433 120.575 -3.155 1.00137. 12 C

ANISOU 801 CA MET A 105 18139 16698 17264 -1237 ,2135 -114 C

ATOM 802 CB MET A 105 36:817 120.057 -4.531 1.00133. 21 C

ANISOU 802 CB MET A 105 17458 16241 16914 -1144 1951 -120 C-

ATOM 803 CG MET A 105 36.189 118.773 -4.952 1.00134, 01 C

ANISOU 803 CG MET A 105 17332 16355 17232 -1033 1852 -50 C

ATOM 804 SD MET A 105 36.897 118.399 -6.558 1.00128. 89 S

ANISOU 804 SD MET A 105 16532 15748 16693 -974 1646 -71 S

ATOM 805 CE MET A 105 35.420 118.304 -7.544 1.00122. 80 C

ANISOU 805 CE MET A 105 15618 14885 16154 -789 1650 -50 C

ATOM 806 C MET A 105 36.442 122.100 -3.196 1.00139, 19 C

ANISOU 806 C MET A 105 18625 16877 17384 -1266 2302 -200 C

ATOM 807 O MET A 105 35.575 122.723 -3.800 1.00139. 66 O

ANISOU 807 O MET A 105 18679 16838 17548 -1130 2407 -229 O

ATOM 808 N ASP A 106 37.428 122.689 -2.532 1.00140. 69 N

ANISOU 808 N ASP A 106 19016 17103 17337 -1450 2320 -231 N

ATOM 809 CA ASP A 106 37.703 124.112 -2.641 1.00139. 34 C

ANISOU 809 CA ASP A 106 19071 16869 17004 -1511 2439 -320 C

ATOM 810 CB ASP A 106 37.403 124.825 -1.321 1.00142. 82 C

ANISOU 810 CB ASP A 106 19783 17247 17234 -1652 2641 -339 C

ATOM 811 CG ASP A 106 38.226 124.286 -0.140 1.00142. 54 C

ANISOU 811 CG ASP A 106 19824 17322 17013 -1873 2522 -291 C

ATOM 812 ODl ASP A 106 38.888 123.230 -0.260 1.00136. 38 O

ANISOU 812 ODl ASP A 106 18845 16656 16318 -1881 2310 -217 O

ATOM 813 OD2 ASP A 106 38.198 124.936 0.929 1.00141. 87 O

ANISOU 813 OD2 ASP A 106 20013 17199 16691 -2045 2644 -322 O

ATOM 814 C ASP A 106 39.176 124.204 -2.971 1.00142. 93 C

ANISOU 814 C ASP A 106 19520 17429 17356 -1633 2250 -344 C

ATOM 815 O ASP A 106 39.920 123.256 -2.718 1.00146. 58 O

ANISOU 815 O ASP A 106 19882 18006 17807 -1724 2079 -284 O

ATOM 816 N TYR A 107 39.616 125.316 -3.538 1.00136. 87 N

ANISOU 816 N TYR A 107 18849 16623 16531 -1632 2278 -423 N

ATOM 817 CA TYR A 107 41.036 125.446 -3.855 1.00141. 17 C

ANISOU 817 CA TYR A 107 19396 17264 16978 -1762 2122 -448 C

ATOM 818 CB TYR A 107 41.905 125.260 -2.594 1.00139. 92 C

ANISOU 818 CB TYR A 107 19350 17196 16618 -1998 2058 -411 C

ATOM 819 CG TYR A 107 41.957 126.459 -1.657 1.00143. 24 C

ANISOU 819 CG TYR A 107 20092 17542 16791 -2150 2234 -470 C

ATOM 820 CDl TYR A 107 43.151 126.856 -1.072 1.00141. 23 C

ANISOU 820 CDl TYR A 107 19995 17356 16309 -2398 2159 -473 C

ATOM 821 CEl TYR A 107 43.207 127.953 -0.220 1.00151. 76 C

ANISOU 821 CEl TYR A 107 21654 18609 17397 -2554 2326 -533 C

ATOM 822 CE TYR A 107 42.048 128.671 0.061 1.00160. 54 C

ANISOU 822 CZ TYR A 107 22929 19561 18509 -2443 2594 -593 C

ATOM 823 OH TYR A 107 42.091 129.760 0.912 1.00166. 45 O

ANISOU 823 OH TYR A 107 24021 20205 19019 -2589 2792 -661 O

ATOM 824 CE2 TYR A 107 40.845 128.298 -0.509 1.00153. 39 C

ANISOU 824 CE2 TYR A 107 21843 18588 17851 -2184 2669 -581 C

ATOM 825 CD2 TYR A 107 40.808 127.196 -1.363 1.00151. 05 C

ANISOU 825 CD2 TYR A 107 21230 18382 17781 -2048 2479 -520 C

ATOM 826 C TYR A 107 41.432 124.430 -4.930 1.00137. 80 C

ANISOU 826 C TYR A 107 18705 16913 16739 -1668 1929 -414 C

ATOM 827 O TYR A 107 42.087 123.420 -4.643 1.00131. 31 O

ANISOU 827 O TYR A 107 17754 16200 15939 -1741 1772 -350 O

ATOM 828 N TRP A 108 41.009 124.702 -6.162 1.00139. 89 N

ANISOU 828 N TRP A 108 18901 17112 17139 -1507 1945 -452 N

ATOM 829 CA TRP A 108 41.431 123.928 -7.324 1.00141. 35 C

ANISOU 829 Ch TRP A 108 18895 17346 17466 -1437 1787 -445 C

ATOM 830 CB TRP A 108 40.457 124.123 -8.476 1.00139. 15 C

ANISOU 830 CB TRP A 108 18559 16972 17341 -1251 1815 -469 C

ATOM 831 CG TRP A 108 39.161 123.479 -8.303 1.00133. 42 C

ANISOU 831 CG TRP A 108 17737 16195 16760 -1122 1857 -410 C

ATOM 832 CDl TRP A 108 38.323 123.620 -7.259 1.00136. 80 C

ANISOU 832 CDl TRP A 108 18240 16577 17159 -1122 1999 -383 C

ATOM 833 ' NEl TRP A 108 37.195 122.876 -7.457 1.00133. 99 N

ANISOU 833 NEl TRP A 108 17735 16181 16994 -983 ' 2003 -323 N

ATOM 834 CE2 TRP A 108 37.293 122.248 -8.662 1.00126. 16 C

ANISOU 834 CE2 TRP A 108 16584 15208 16143 -900 1850 -313 C

ATOM 835 CD2 TRP A 108 38.517 122.613 -9.225 1.00127. 11 C

ANISOU 835 CD2 TRP A 108 16755 15377 16164 -980 1768 -370 C

ATOM 836 CE3 TRP A 108 38.867 122.099 -10.466 1.00130. 41 C

ANISOU " 836 CE3 TRP A 108 17057 15808 16686 -925 1631 -378 C ATOM 837 CZ3 TRP A 108 37.992 121.250 -11.097 1.00129.73 C

ANISOU 837 CZ3 TRP A 108 16823 15687 16781 -803 1565 -329 C

ATOM . 838 CH2 TRP A 108 36.778 120.906 -10.511 1.00129 .91 C

ANISOU 838 CH2 TRP A 108 16785 15671 16903 -731 1631 -266 C

ATOM 839 CZ2 TRP A 108 36.416 121.392 -9.291 1.00127 .77 C

ANISOU 839 CZ2 TRP A 108 16613 15385 16548 -773 1782 -257 C

ATOM 840 C TRP A 108 42.759 124.454 -7.808 1.00147 99 C

ANISOU 840 C TRP A 108 19804 18231 18196 -1554 1736 -503 C

ATOM 841 O TRP A 108 43.082 125.619 -7.587 1.00157 .91 O

ANISOU 841 O TRP A 108 21262 19441 19297 -1632 1840 -568 O

ATOM 842 N GLY A 109 43.512 123.612 -8.505 1.00144, 64 N

ANISOU 842 N GLY A 109 19213 17883 17859 -1564 1591 -480 N

ATOM 843 CA GLY A 109 44.705 124.063 -9.196 1.00144. 06 C

ANISOU 843 CA GLY A 109 19167 17837 17732 -1640 1554 -536 C

ATOM 844 C GLY A 109 44.321 124.911 -10.393 1.00143. 60 C

ANIΞOU 844 C GLY A 109 19191 17673 17697 -1531 1629 -618 C

ATOM 845 O GLY A 109 43.206 125.421 -10.463 1.00140. 27 O

ANISOU 845 O GLY A 109 18848 17156 17292 -1424 1725 -632 O

ATOM 846 N GLN A 110 45.246 125.073 -11.330 1.00152. 59 N

ANISOU 846 N GLN A 110 20311 18824 18842 -1559 1588 -665 N

ATOM 847 CA GLN A 110 44.958 125.762 -12.581 1.00148. 65 C

ANISOU 847 CA GLN A 110 19898 18227 18356 -1469 1640 -738 C

ATOM 848 CB GLN A ' " no 46.124 126.664 -12.958 1.00155. 73 C

ANISOU 848 CB GLN A 110 20906 19135 19131 -1596 1668 -808 C

ATOM 849 CG GLN A 110 47.435 126.232 -12.304 1.00162. 29 C

ANISOU 849 CG GLN A 110 21622 20091 19949 -1748 1583 -772 C

ATOM 850 CD GLN A 110 48.655 126.423 -13.197 1.00177. 83 C

ANISOU 850 CD GLN A 110 23599 22073 21897 -1829 1583 -829 C

ATOM 851 OEl GLN A 110 48.745 127.383 -13.974 1.00180. 48 O

ANISOU 851 OEl GLN A 110 24101 22330 22145 -1833 1668 -910 O

ATOM 852 NE2 GLN A 110 49.609 125.499 -13.085 1.00175. 36 N

ANISOU 852 NE2 GLN A 110 23101 21853 21674 -1892 1495 -780 N

ATOM 853 C GLN A 110 44.738 124.716 -13.656 1.00144. 74 C

ANIΞOU 853 C GLN A 110 19243 17713 18038 -1341 1556 -720 C

ATOM 854 O GLN A 110 44.032 124.952 -14.626 1.00139. 99 O

ANISOU 854 O GLN A 110 18684 17018 17488 -1224 ' 1573 -743 O

ATOM 855 N GLY A 111 45.356 123.553 -13.461 1.00145. 08 N

ANISOU 855 N GLY A 111 19112 17840 18173 -1371 1462 -674 N

ATOM 856 CA GLY A 111 45.183 122.409 -14.339 1.00140. 14 C

ANISOU 856 CA GLY A 111 18337 17196 17715 -1263 1388 -649 C

ATOM 857 C GLY A 111 46.221 122.334 -15.436 1.00140. 02 C

ANISOU 857 C GLY A 111 18313 17159 17731 -1274 1382 -707 C

ATOM 858 O GLY A 111 46.792 123.350 -15.806 1.00144. 79 O

ANISOU 858 O GLY A 111 19065 17706 18243 -1296 1444 -781 O

ATOM 859 N THR A 112 46.475 121.133 -15.950 1.00142. 43 N

ANISOU 859 N THR A 112 18454 17497 18166 -1260 1322 -673 N

ATOM 860 CA THR A 112 47.300 120.979 -17.152 1.00152. 92 C

ANISOU 860 CA THR A 112 19777 18780 19546 -1252 1342 -729 C

ATOM 861 CB THR A 112 48.315 119.810 -17.027 1.00150. 86 C

ANISOU 861 CB THR A 112 19313 18579 19427 -1273 1302 -676 C

ATOM 862 OGl THR A 112 48.819 119.434 -18.325 1.00142. 70 O

ANISOU 862 OGl THR A 112 18279 17470 18472 -1234 1344 -731 ' O

ATOM 863 CG2 THR A 112 47.653 118.617 -16.354 1.00148. 01 C

ANISOU 863 CG2 THR A 112 18808 18254 ' 19175 -1212 1221 -581 C

ATOM 864 C THR A 112 46.417 120.781 -18.385 1.00146. 37 C

ANISOU 864 C THR A 112 19024 17834 18755 -1141 1338 -769 C

ATOM 865 O THR A 112 45.200 120.618 -18.276 1.00141. 89 O

ANISOU 865 O THR A 112 18463 17234 18213 -1061 1300 -735 O

ATOM 866 N SER •A 113 47.022 120.805 -19.562 1.00136. 40 N

ANISOU 866 N SER A 113 18047 17987 15792 -49 907 1873 N

ATOM 867 CA SER A 113 46.243 120.619 -20.757 1.00135: 45 C

ANISOU 867 CA SER A 113 18240 17577 15647 136 943 1850 C

ATOM 868 CB SER A 113 46.268 121.890 -21.594 1.00137. 90 C

ANISOU 868 CB SER A 113 18747 17694 15953 154 1145 1670 C

ATOM 869 OG SER A 113 44.962 122.243 -22.019 1.00140. 67 O

ANISOU 869 OG SER A 113 19340 17897 16211 209 1120 1609 O

ATOM 870 C SER A 113 46.829 119.449 -21.512 1.00135. 21 C

ANISOU 870 C SER A 113 18265 17376 15731 310 960 2010 C

ATOM 871 O SER A 113 47.764 119.600 -22.285 1.00141. 70 O

ANISOU 871 O SER A 113 19113 18058 16670 386 1134 2012 O

ATOM 872 N VAL A 114 46.280 118.270 -21.272 1.00140. 95 N

ANISOU 872 N VAL A 114 19015 18118 16421 371 779 2146 N

ATOM 873 CA VAL A 114 46.769 117.065 -21.917 1.00143. 21 C

ANISOU 873 CA VAL A 114 19354 18244 16817 532 789 2305 C

ATOM 874 CB VAL A 114 46.672 115.875 -20.974 1.00142. 46 C

ANISOU 874 CB VAL A 114 19048 18348 16732 501 553 2485 C

ATOM 875 CGl VAL A 114 46.828 114.594 -21.731 1.00141. 49 C ANISOU 875 CGl VAL A 114 19056 18007 16698 689 562 2635 C

ATOM 876 CG2 VAL A 114 47.739 115.985 -19.939 1.00140 .52 C

ANISOU 876 CG2 VAL A 114 18426 18377 16588 346 536 2538 C

ATOM 877 C VAL A 114 46.031 116.761 -23.219 1.00135 .53 C

ANISOU 877 C VAL A 114 18750 16950 15794 691 847 2303 C

ATOM 878 O VAL A 114 44.809 116.632 -23.237 1.00134 >58 O

ANISOU 878 O VAL A 114 18794 16812 15528 683 722 2301 O

ATOM 879 N THR A 115 46.794 116.638 -24.303 1.00143 99 N

ANISOU 879 N THR A 115 19951 17775 16983 820 1043 2313 N

ATOM 880 CA THR A 115 46.253 116.420 -25.642 1.00144, 55 C

ANISOU 880 CA THR A 115 20390 17519 17015 941 1142 2302 C

ATOM ' 881 CB THR A 115 46.753 117.495 -26.580 1.00146 26 C

ANISOU 881 CB THR A 115 20741 17557 17276 941 1382 2143 C

ATOM 882 OGl THR A 115 ■36.664 118.759 -25.917 1.00145, 04 O

ANISOU 882 OGl THR A 115 20407 17603 17099 801 1391 2009 O

ATOM 883 CG2 THR A 115 45.932 117.509 -27.859 1.00144, 15 C

ANISOU 883 CG2 THR A 115 20844 17018 16910 974 1430 2109 C

ATOM 884 C THR A 115 46.702 115.099 -26.236 1.00142. 51 C

ANISOU 884 C THR A 115 20235 17067 16844 1095 1181 2447 C

ATOM 885 O THR A 115 47.894 114.789 -26.238 1.00143, 78 O

ANISOU 885 O THR A 115 20230 17231 17169 1157 1286 2501 O

ATOM 886 N VAL A 116 45.753 114.331 -26.762 1.00135. 63 N

ANISOU 886 N VAL A 116 19655 16016 15861 1155 1110 2516 N

ATOM 887 CA VAL A 116 46.087 113.036 -27.352 1.00138. 76 C

ANISOU 887 CA VAL A 116 20189 16216 16317 1294 1139 2653 C

ATOM 888 CB VAL A 116 45.248 111.883 -26.772 1.00140. 49 C

ANISOU 888 CB VAL A 116 20423 16535 16421 1297 863 2815 C

ATOM 889 CGl VAL A 116 45.960 110.577 -27.001 1.00143. 56 C

ANISOU 889 CGl VAL A 116 20827 16793 16928 1434 883 2962 C

ATOM 890 CG2 VAL A 116 45.032 112.081 -25.289 1.00139. 22 C

ANISOU 890 CG2 VAL A 116 19908 16755 16233 1170 638 2829 C

ATOM 891 C VAL A 116 46.053 113.037 -28.889 1.00139. 65 C

ANISOU 891 C VAL A 116 20683 15964 16415 1369 1351 2608 C

ATOM 892 O VAL A 116 45.006 112.913 -29.529 1.00135. 54 O

ANISOU 892 O VAL A 116 20472 15292 15736 1344 1301 2631 O

ATOM 893 N SER A 117 47.241 113.184 -29.454 1.00148. 08 N

ANISOU 893 N SER A 117 21711 16905 17649 1444 1588 2558 N

ATOM 894 CA SER A 117 47.450 113.217 -30.881 1.00150. 04 C

ANISOU 894 CA SER A 117 22274 16819 17917 1508 1819 2507 C

ATOM 895 CB SER A 117 47.479 114.664 -31.364 1.00155. 71 C

ANISOU 895 CB SER A 117 23088 17485 18588 1403 1934 2336 C

ATOM 896 OG SER A HI 48.063 114.785 -32.649 1.00159. 90 O

ANISOU 896 OG SER A 117 23732 17797 19225 1455 2196 2255 O

ATOM 897 C SER A 117 48.798 112.565 -31.106 1.00159. 87 C

ANISOU 897 C SER A 117 23383 17986 19373 1640 2016 2536 C

ATOM 898 O SER A 117 49.602 112.464 -30.182 1.00157. 82 O

ANISOU 898 O SER A 117 22773 17947 19245 1645 2006 2560 O

ATOM 899 N SER A 118 49.045 112.107 -32.326 1.00180. 32 N

ANISOU 899 N SER A 118 26257 20264 21994 1734 2203 2545 N

ATOM 900 CA SER A 118 50.325 111.505 -32.653 1.00182. 25 C

ANISOU 900 CA SER A 118 26406 20397 22443 1878 2423 2576 C

ATOM 901 CB SER A 118 50.134 110.356 -33.633 1.00181, 32 C

ANISOU 901 CB SER A 118 26630 19945 22318 1988 2545 2642 C

ATOM 902 OG SER A 118 49.676 110.846 -34.880 1.00185. 60 O

ANISOU 902 OG SER A 118 27567 20262 22689 1893 2604 2556 O

ATOM 903 C SER A 118 51.220 112.562 -33.270 1.00187. 42 C

ANISOU 903 C SER A 118 26997 21029 23185 1857 2646 2430 C

ATOM 904 O SER A 118 52.418 112.346 -33.432 1.00191. 77 O

ANISOU 904 O SER A 118 27360 21587 23916 1959 2806 2460 O

ATOM 905 N ALA A 119 50.622 113.708 -33.596 1.00178. 67 N

ANISOU 905 N ALA A 119 26031 19903 21951 1722 2644 2288 N

ATOM 906 CA ALA A 119 51.298 114.805 -34.300 1.00176. 53 C

ANISOU 906 CA ALA A 119 25737 19604 21734 1676 2827 2137 C

ATOM 907 CB ALA A 119 50.304 115.904 -34.646 1.00175. 28 C

ANISOU 907 CB ALA A 119 25732 19442 21425 1509 2760 2007 C

ATOM 908 C ALA A 119 52.487 115.397 -33.551 1.00174. 94 C

ANISOU 908 C ALA A 119 25143 19658 21669 1692 2853 2141 C

ATOM 909 O ALA A 119 52.661 115.166 -32.354 1.00174. 58 O

ANISOU 909 O ALA A 119 24819 19858 21657 1688 2697 2243 O

ATOM 910 N LYS A 120 53.298 116.176 -34.262 1.00184. 74 N

ANISOU 910 N LYS A 120 26365 20852 22977 1688 3042 2039 N

ATOM 911 CA LYS A 120 54.529 116.684 -33.677 1.00193. 55 C

ANISOU 911 CA LYS A 120 27133 22197 24210 1697 3086 2066 C

ATOM 912 CB LYS A 120 55.704 116.590 -34.651 1.00200. 85 C

ANISOU 912 CB LYS A 120 28079 22972 25262 1801 3348 2047 C

ATOM 913 CG LYS A 120 56.533 115.325 -34.469 1.00208. 55 C

ANISOU 913 CG LYS A 120 28931 23896 26412 1985 3455 2223 C ATOM 914 CD LYS A 120 56.666 114.944 -32.983 1.00211.99 C

ANISOU 914 CD LYS A 120 28994 24635 26917 1974 3283 2392 C

ATOM 915 CE LYS A 120 57.526 115.935 -32.195 1.00205 .71 C

ANISOU 915 CE LYS A 120 27902 24129 26131 1859 3260 2378 C

ATOM 916 NZ LYS A 120 57.677 115.532 -30.766' 1.00200. 87 N

ANISOU 916 NZ LYS A 120 26939 23827 25554 1787 3074 2538 N

ATOM 917 C LYS A 120 54.416 118.086 -33.111 1.00190, 03 C

ANISOU 917 C LYS A 120 26535 21989 23678 1529 2977 1957 C

ATOM 918 O LYS A 120 53.656 118.917 -33.608 1.00187, 16 O

ANISOU 918 O LYS A 120 26359 21560 23193 1419 2938 1818 O

ATOM 919 N THR A 121 55.196 118.317 -32.060 1.00158, 03 N

ANISOU 919 N THR A 121 22141 18209 19693 1501 2932 2037 N

ATOM 920 CA THR A 121 55.217 119.573 -31.325 1.00153. .72 C

ANISOU 920 CA THR A 121 21430 17906 19069 1335 2844 1950 C

ATOM 921 CB THR A 121 55.873 119.372 -29.958 1.00152. 10 C

ANISOU 921 CB THR A 121 20852 18016 18923 1285 2740 2105 C

ATOM 922 OGl THR A 121 55.627 118.040 -29.498 1.00156, 01 O

ANISOU 922 OGl THR A 121 21286 18510 19482 1372 2646 2269 O

ATOM 923 CG2 THR A 121 55.304. 120.330 -28.974 1.00148. 65 C

ANISOU 923 CG2 THR A 121 20303 17822 18354 1085 2582 2019 C

ATOM 924 C THR A 121 55.992 120.641 -32.097 1.00154. 66 C

ANISOU 924 C THR A 121 21589 17975 19200 1307 3007 1830 C

ATOM 925 O THR A 121 57.043 120.360 -32.681 1.00156. 58 O

ANISOU 925 O THR A 121 21740 18195 19560 1401 3161 1902 O

ATOM 926 N THR A 122 55.481 121.868 -32.094 1.00152. 18 N

ANISOU 926 N THR A 122 21407 17643 18771 1178 2971 1655 N

ATOM 927 CA THR A 122 56.034 122.917 -32.950 1.00151. 48 C

ANISOU 927 CA THR A 122 21375 17501 18678 1131 3097 1527 C

ATOM 928 CB THR A 122 55.233 123.016 -34.264 1.00147. 28 C

ANISOU 928 CB THR A 122 21184 16676 18101 1118 3162 1391 C

ATOM 929 OGl THR A 122 54.513 121.795 -34.480 1.00146. 13 O

ANISOU 929 OGl THR A 122 21218 16320 17984 1235 3196 1475 O

ATOM 930 CG2 THR A 122 56.157 123.325 -35.460 1.00146. 09 C

ANISOU 930 CG2 THR A 122 21090 16432 17984 1107 3321 1295 C

ATOM 931 C THR A 122 56.028 124.303 -32.296 1.00150. 44 C

ANISOU 931 C THR A 122 21110 17593 18456 959 3006 1429 C

ATOM 932 O THR A 122 54.961 124.850 -32.008 1.00144. 65 O

ANISOU 932 O THR A 122 20460 16873 17626 858 2891 1333 O

ATOM 933 N PRO A 123 57.221 124.891 -32.081 1.00168. 65 N

ANISOU 933 N PRO A 123 23217 20073 20788 922 3062 1461 N

ATOM 934 CA PRO A 123 57.228 126.258 -31.556 1.00165. 88 C

ANISOU 934 CA PRO A 123 22785 19910 20331 743 2984 1354 C

ATOM 935 CB PRO A 123 58.689 126.689 -31.734 1.00163. 86 C

ANISOU 935 CB PRO A 123 22371 19783 20107 732 3080 1412 C

ATOM 936 CG PRO A 123 59.461 125.425 -31.674 1.00162. 81 C

ANISOU 936 CG PRO A 123 22100 19654 20107 887 3159 1622 C

ATOM 937 CD PRO A 123 58.586 124.388 -32.330 1.00168. 23 C

ANISOϋ 937 CD PRO A 123 23001 20069 20851 1028 3190 1610 C

ATOM 938 C PRO A 123 56.295 127.136 -32.388 1.00160. 32 C

ANISOU 938 C PRO A 123 22331 19031 19554 668 2975 1148 C

ATOM 939 O PRO A 123 55.996 126.785 -33.523 1.00158. 87 O

ANISOU 939 O PRO A 123 22371 18593 19400 739 3036 1103 O

ATOM 940 N PRO A 124 55.814 128.252 -31.828 1.00151. 18 N

ANISOU 940 N PRO A 124 21139 17999 18302 513 2902 1031 N

ATOM 941 CA PRO A 124 55.030 129.099 -32.715 1.00151. 93 C

ANISOU 941 CA PRO A 124 21464 17898 18365 457 2913 856 C

ATOM 942 CB PRO A 124 54.152 129.899 -31.741 1.00146. 27 C

ANISOU 942 CB PRO A 124 20728 17288 17559 332 2795 770 C

ATOM 943 CG PRO A 124 54.600 129.519 -30.351 1.00145. 38 C

ANISOU 943 CG PRO A 124 20363 17460 17413 291 2727 883 C

ATOM 944 CD PRO A 124 55.911 128.834 -30.483 1.00149. 31 C

ANISOU 944 CD PRO A 124 20712 18034 17984 373 2803 1037 C

ATOM 945 C PRO A 124 55.970 130.051 -33.457 1.00160. 83 C

ANISOU 945 C PRO A 124 22584 19037 19486 395 2987 771 C

ATOM 946 O PRO A 124 57.111 130.260 -33.029 1.00163. 31 O

ANISOU 946 O PRO A 124 22711 19546 19792 378 3009 846 O

ATOM 947 N SER A 125 55.515 130.604 -34.573 1.00165. 50 N

ANISOU 947 N SER A 125 23371 19432 20080 350 3016 634 N

ATOM 948 CA SER A 125 56.132 131.813 -35.080 1.00168. 13 C

ANISOU 948 CA SER A 125 23692 19809 20381 246 3036 525 C

ATOM 949 CB SER A 125 56.061 131.877 -36.605 1.00172. 20 C

ANISOU 949 CB SER A 125 24381 20096 20952 262 3124 459 C

ATOM 950 OG SER A 125 56.999 130.998 -37.200 1.00177. 31 O

ANISOU 950 OG SER A 125 24990 20717 21663 394 3238 572 O

ATOM 951 C SER A 125 55.313 132.927 -34.450 1.00163. 59 C

ANISOU 951 C SER A 125 23147 19276 19734 102 2940 390 C

ATOM 952 O SER A 125 54.127 132.735 -34.165 1.00157. 38 O ANISOU 952 O SER A 125 22441 18411 18945 100 2887 371 O

ATOM 953 N VAL A 126 55.931 134.074 -34 195 1 ,00147.00 N

ANISOU 953 N VAL A 126 20982 17301 17571 -17 2919 306 N

ATOM 954 CA VAL A 126 55.159 135.198 -33 687 1 ,00145.21 C

ANISOU 954 CA VAL A 126 20775 17120 17279 -149 2844 179 C

ATOM 955 CB VAL A 126 55.490 135.513 -32 251 1 00152..83 C

ANISOU 955 CB VAL A 126 21556 18366 18146 -224 2802 230 C

ATOM 956 CGl VAL A 126 54.785 136..802 -31 844 1 00153..32 C

ANISOU 956 CGl VAL A 126 21654 18455 18144 -345 2745 100 C

ATOM 957 CG2 VAL A 126 55.063 134..358 -31 378 1 00156..35 C

ANISOU 957 CG2 VAL A 126 21873 18915 18618 -122 2802 408 C

ATOM 958 C VAL A 126 55.362 136..446 -34 509 1 00147..48 C

ANISOU 958 C VAL A 126 21149 17332 17553 -264 2838 29 C

ATOM 959 O VAL A 126 56.485 Z36..932 -34 638 1 00153..71 O

ANISOU 959 O VAL A 126 21857 18261 18283 -328 2837 21 O

ATOM 960 N TYR A 127 54.264 136..967 -35 050 1 00156..51 N

ANISOU 960 N TYR A 127 22450 18264 18751 -301 2823 -74 N

ATOM 961 CA TYR A 127 54.341 138..058 -36.009 1.00160..94 C

ANISOU 961 CA TYR A 127 23093 18724 19331 -411 2812 -202 C

ATOM 962 CB TYR A 127 53.858 137..601 -37.391 1, 00155..16 C

ANISOU 962 CB TYR A 127 22515 17736 18701 -388 2852 -199 C

ATOM 963 CG TYR A 127 54.694 136..485 -37, 987 1 00156..47 C

ANISOU 963 CG TYR A 127 22666 17897 18889 -272 2931 -87 C

ATOM 964 CDl TYR A 127 56.079 136..532 -37.957 1, 00162.60 C

ANISOU 964 CDl TYR A 127 23305 18861 19616 -246 2958 -42 C

ATOM 965 CEl TYR A 127 56.845 135..511 -38.503 1.00166.39 C

ANISOU 965 CEl TYR A 127 23759 19328 20133 -124 3051 67 C

ATOM 966 CE TYR A 127 56.227 134..433 -39.091 1.00163.86 C

ANISOU 966 CZ TYR A 127 23574 18797 19888 -37 3119 117 C

ATOM 967 OH TYR A 127 56.980 133..422 -39.634 1, 00166.46 O

ANISOU 967 OH TYR A 127 23891 19095 20262 89 3231 217 O

ATOM 968 CE2 TYR A 127 54.859 134.363 -39.138 1.00159.02 C

ANISOU 968 CE2 TYR A 127 23114 18004 19304 -80 3081 79 C

ATOM 969 CD2 TYR A 127 54.099 135.387 -38.587 1.00156.96 C

ANISOU 969 CD2 TYR A 127 22855 17767 19017 -193 2986 -15 C

ATOM 970 C TYR A 127 53.609 139.315 -35.549 1.00156.43 C

ANISOU 970 C TYR A 127 22553 18149 18736 -539 2756 -342 C

ATOM 971 O TYR A 127 52.391 139.334 -35.429 1, 00154.43 O

ANISOU 971 O TYR A 127 22382 17759 18536 -545 2745 -375 O

ATOM 972 N PRO A 128 54.375 140.366 -35.260 1.00142.88 N

ANISOU 972 N PRO A 128 20770 16583 16933 -644 2725 -414 N

ATOM 973 CA PRO A 128 53.895 141.704 -34.921 1.00140.31 C

ANISOU 973 CA PRO A 128 20486 16241 16584 -772 2684 -560 C

ATOM 974 CB PRO A 128 55.183 142.526 -34.940 1.00143.09 C

ANISOU 974 CB PRO A 128 20773 16773 16822 -875 2649 -593 C

ATOM 975 CG PRO A 128 56.233 141.564 -34.476 1.00142.09 C

ANISOU 975 CG PRO A 128 20514 16852 16623 -797 2677 -431 C

ATOM 976 CD PRO A 128 55.816 140.213 -34.987 1.00143.99 C

ANISOU 976 CD PRO A 128 20784 16947 16980 -643 2731 -334 C

ATOM 977 C PRO A 128 52.918 142.301 -35.920 1.00132.49 C

ANISOU 977 C PRO A 128 19629 14992 15721 -822 2670 -652 C

ATOM 978 O PRO A 128 53.316 142.574 -37.030 1.00133.50 O

ANISOU 978 O PRO A 128 19797 15036 15891 -865 2654 -674 O

ATOM 979 N LEU A 129 51.676 142.535 -35.522 1.00145.54 N

ANISOU 979 N LEU A 129 21338 16528 17433 -827 2674 -692 N

ATOM 980 CA LEU A 129 50.779 143.376 -36.311 1.00151.30 C

ANISOU 980 CA LEU A 129 22168 17033 18286 -907 2656 -773 C

ATOM 981 CB LEU A 129 49.346 142.916 -36.147 1.00144.77 C

ANISOU 981 CB LEU A 129 21400 16060 17545 -851 2680 -721 C

ATOM 982 CG LEU A 129 49.136 141.436 -36.348 1.00147.29 C

ANISOU 982 CG LEU A 129 21739 16360 17865 -726 2702 -568 C

ATOM 983 CDl LEU A 129 47.726 141.110 -35.898 1.00146.57 C

ANISOU 983 CDl LEU A 129 21681 16199 17810 -681 2708 -523 C

ATOM 984 CD2 LEU A 129 49.377 141.075 -37.817 1.00151.51 C

ANISOU 984 CD2 LEU A 129 22366 16724 18478 -740 2707 -502 C

ATOM 985 C LEU A 129 50.832 144.847 -35.893 1.00161.96 C

ANISOU 985 C LEU A 129 23510 18424 19605 -1029 2629 -922 C

ATOM 986 O LEU A 129 50. 462 145.186 -34.768 1.00165.04 O

ANISOU 986 O LEU A 129 23865 18925 19918 -1035 2650 -969 O

ATOM 987 N ALA A 130 51.275 145.722 -36.792 1.00171.90 N

ANISOU 987 N ALA A 130 24805 19591 20918 -1137 2580 -997 N

ATOM 988 CA ALA A 130 51.153 147.158 -36.573 1.00167.56 C

ANISOU 988 CA ALA A 130 24271 19031 20365 -1259 2546 -1141 C

ATOM 989 CB ALA A 130 52.488 147.832 -36.731 1.00168.89 C

ANISOU 989 CB ALA A 130 24405 19348 20416 -1352 2477 -1190 C

ATOM 990 C ALA A 130 50.160 147.655 -37.606 1.00169.64 C

ANISOU 990 C ALA A 130 24605 19028 20823 -1321 2529 -1168 C ATOM 991 O ALA A 130 49.882 146.945 -38.564 1.00171.91 O

ANISOU 991 O ALA A 130 24930 19174 21215 -1294 2534 -1070 O

ATOM 992 N PRO A 131 49.617 148.865 -37.422 1.00163.93 N

ANISOU 992 N PRO A 131 23904 18228 20155 -1415 2513 -1288 N

ATOM 993 CA PRO A 131 48.505 149.370 -38.238 1.00165.62 C

ANISOU 993 CA PRO A 131 24163 18183 20581 -1479 2501 -1290 C

ATOM 994 CB PRO A 131 47.984 150.557 -37.423 1.00170.73 C

ANISOU 994 CB PRO A 131 24821 18798. 21250 .-1528 2528 -1425 C

ATOM 995 CG PRO A 131 48.704 150.505 -36.110 1.00170.16 C

ANISOU 995 CG PRO A 131 24726 18968 20959 -1489 - 2567 -1486 C

ATOM 996 CD PRO A 131 49.988 149.817 -36.370 1.00168.50 C

ANISOU 996 CD PRO A 131 24472 18945 20605 -1469 2518 -1414 C

ATOM 997 C PRO A 131 48.902 149.875 -39.622 1.00167.08 C

ANISOU 997 C PRO A 131 24357 18275 20852 -1612 2405 -1296 C

ATOM 998 O PRO A 131 50.037 149.710 -40.061 1.00167.73 O

ANISOU 998 O PRO A 131 24414 18495 20820 -1642 2350 -1306 O

ATOM 999 N GLY A 132 47.948 150.503 -40.298 1.00181.97 N

ANISOU 999 N GLY A 132 26268 19933 22939 -1701 2383 -1278 N

ATOM 1000 CA GLY A 132 48.200 151.125 -41.585 1.00195.80 C

ANISOU 1000 CA GLY A 132 28016 21590 24790 -1870 2277 -1297 C

ATOM 1001 C GLY A 132 48.617 152.588 -41.498 1.00206.00 C

ANISOU 1001 C GLY A 132 29286 22908 26078 -1988 2195 -1450 C

ATOM 1002 O GLY A 132 47.927_ 153.421 -40.901 1.00205.71 O

ANISOU 1002 O GLY A i32 29256 22800 26103 -1984 2234 -1522 O

ATOM 1003 N SER A 133 49.761 152.899 -42.097 1.00223.58 N

ANISOU 1003 N SER A 133 31489 25238 28223 -2096 2083 ' -1500 N

ATOM 1004 CA SER A 133 50.253 154.266 -42.156 1.00227.81 C

ANISOU 1004 CA SER A 133 32012 25801 28746 -2231 1974 -1633 C

ATOM 1005 CB SER A 133 51.401 154.362 -43.156 1.00230.72 C

ANISOU 1005 CB SER A 133 32347 26257 29059 -2368 1830 -1645 C

ATOM 1006 OG SER A 133 50.965 153.968 -44.447 1.00238.54 O

ANISOU 1006 OG SER A 133 33328 27062 30244 -2482 1789 -1565 O

ATOM 1007 C SER A 133 49.131 155.193 -42.591 1.00233.68 C

ANISOU 1007 C SER A 133 32759 26295 29735 -2320 1965 -1656 C

ATOM 1008 O SER A 133 48.533 154.992 -43.648 1.00230.58 O

ANISOU 1008 O SER A 133 32346 25721 29541 -2429 1919 -1575 O

ATOM 1009 N SER A 139 42.653 158.303 -32.136 1.00185.37 N

ANISOU 1009 N SER A 139 26958 19759 23715 -1539 3378 -2316 N

ATOM 1010 CA SER A 139 42.744 158.535 -30.694 1.00195.99 C

ANISOU 1010 CA SER A 139 28385 21305 24778 -1600 3442 -2481 C

ATOM 1011 CB SER A 139 41.506 159.279 -30.183 1.00204.58 C

ANISOU 1011 CB SER A 139 29552 22248 25931 -1597 3636 -2645 C

ATOM 1012 OG SER A 139 40.338 158.493 -30.327 1.00200.44 O

ANISOU 1012 OG SER A 139 28977 21648 25534 -1454 3775 -2572 O

ATOM 1013 C SER A 139 42.956 157.244 -29.891 1.00195.46 C

ANISOU 1013 C SER A 139 28277 21491 24497 -1540 3453 -2408 C

ATOM 1014 O SER A 139 43.668 157.237 -28.883 1.00189.15 O

ANISOU 1014 O SER A 139 27520 20912 23435 -1621 3464 -2494 O

ATOM 1015 N MET A 140 42.335 156.159 -30.341 1.00204.73 N

ANISOU 1015 N MET A 140 29369 22634 25786 -1412 3445 -2235 N

ATOM 1016 CA MET A 140 42.460 154.867 -29.676 1.00199.81 C

ANISOU 1016 CA MET A 140 28692 22234 24992 -1346 3430 -2138 C

ATOM 1017 CB MET A 140 41.112 154.446 -29.089 1.00198.64 C

ANISOU 1017 CB MET A 140 28512 22032 24932 -1220 3554 -2081 C

ATOM 1018 CG MET A 140 40.806 155.078 -27.752 1.00197.82 C

ANISOU 1018 CG MET A 140 28457 21989 24717 -1250 3717 -2254 C

ATOM 1019 SD MET A 140 42.235 155.002 -26.648 1.00208.44 S

ANISOU 1019 SD MET A 140 29845 23648 25704 -1414 3691 . -2383 S

ATOM 1020 CE MET A 140 42.122 153.353 -25.961 1.00194.35 C

ANISOU 1020 CE MET A 140 27949 22133 23763 -1346 3623 -2221 C

ATOM 1021 C MET A 140 42.977 153.779 -30.619 1.00191.93 C

ANISOU 1021 C MET A 140 27633 21286 24004 -1313 3276 -1959- C

ATOM 1022 O MET A 140 42.194 152.998 -31.169 1.00187.67 O

ANISOU 1022 O MET A 140 27055 20622 23629 -1224 3256 -1801 O

ATOM 1023 N VAL A 141 44.295 153.720 -30.799 1.00172.53 N

ANISOU 1023 N VAL A 141 25175 19010 21367 -1393 3175 -1974 N

ATOM 1024 CA VAL A 141 44.884 152.776 -31.750 1.00166.84 C

ANISOU 1024 CA VAL A 141 24406 18342 20643 -1367 3046 -1825 C

ATOM 1025 CB VAL A 141 46.396 153.024 -31.948 1.00164.96 C

ANISOU 1025 CB VAL A 141 24176 18265 20236 -1481 2945 -1876 C

ATOM 1026 CGl VAL A 141 47.182 152.523 -30.756 1.00163.40 C

ANISOU 1026 CGl VAL A 141 23960 18351 19773 -1513 2968 -1899 C

ATOM 1027 CG2 VA-L A 141 46.878 152.349 -33.212 1.00160.71 C

ANISOU 1027 CG2 VAL A 141 23599 17713 19751 -1465 2827 -1745 C

ATOM 1028 C VAL A 141 44.666 151.340 -31.299 1.00168.92 C

ANISOU 1028 C VAL A 141 24611 18748 20822 -1256 3049 -1686 C

ATOM 1029 O VAL A 141 44.517 151.082 -30.109 1.00172.66 O ANISOU 1029 O VAL A 141 25067 19382 21153 -1245 3113 -1726 O

ATOM 1030 N THR A 142 44.628 150.406 -32.245 1.00161.57 N

ANISOU 1030 N THR A 142 23655 17759 19976 -1189 2979 -1524 N

ATOM 1031 CA THR A 142 44.573 148.985 -31.899 1.00150.43 C

ANISOU 1031 CA THR A 142 22197 16481 18478 -1087 2962 -1383 C

ATOM 1032 CB THR A 142 43.257 148.314 -32.357 1.00147.40 C

ANISOU 1032 CB THR A 142 21822 15933 18249 -988 2971 -1227 C

ATOM 1033 OGl THR A 142 42.163 149.230 -32.210 1.00155.01 O

ANISOU 1033 OGl THR A 142 22808 16731 19356 -985 3055 -1276 O

ATOM 1034 CG2 THR A 142 42.983 147.063 -31.538 1.00146.25 C

ANISOU 1034 CG2 THR A 142 21634 15949 17987 -886 2968 -1120 C

ATOM 1035 C THR A 142 45.752 148.266 -32.534 1.00142.46 C

ANISOU 1035 C THR A 142 21163 15585 17382 -1095 2871 -1307 C

ATOM 1036 O THR A 142 46.046 148.475 -33.711 1.00139.04 O

ANISOU 1036 O THR A 142 20754 15030 17044 -1132 2812 -1273 O

ATOM 1037 N LEU A 143 46.435 147.436 -31.749 1.00140.66 N

ANISOU 1037 N LEU A 143 20876 15589 16979 -1070 2863 -1275 N

ATOM 1038 CA LEU A 143 47.573 146.660 -32.244 1.00143.89 C

ANISOU 1038 CA LEU A 143 21246 16116 17311 -1057 2796 -1185 C

ATOM 1039 CB LEU A 143 48.816 146.897 -31.392 1.00140.71 C

ANISOU 1039 CB LEU A 143 20783 15973 16708 -1131 2789 -1231 C

ATOM 1040 CG LEU A 143 49.384 148.304 -31.466 1.00143.46 C

ANISOU 1040 CG LEU A 143 21171 16336 17001 -1272 2771 -1367 C

ATOM 1041 CDl LEU A 143 48.397 149.306 -30.897 1.00146.41 C

ANISOU 1041 CDl LEU A 143 21617 16567 17446 -1326 2835 -1514 C

ATOM 1042 CD2 LEU A 143 50.687 148.367 -30.716 1.00150.61 C

ANISOU 1042 CD2 LEU A 143 22020 17520 17686 -1360 2755 -1361 C

ATOM 1043 C LEU A 143 47.246 145.169 -32.283 1.00147.06 C

ANISOU 1043 C LEU A 143 21622 16527 17728 -929 2782 -1015 C

ATOM 1044 O LEU A 143 46.076 144.785 -32.219 1.00144.62 O

ANISOU 1044 O LEU A 143 21344 16095 17510 -862 2801 -952 O

ATOM 1045 N GLY A 144 48.270 144.325 -32.392 1.00180.38 N

ANISOU 1045 N GLY A 144. 25786 20892 21858 -897 2748 -931 N

ATOM 1046 CA GLY A 144 48.027 142.894 -32.432 1.00180.28 C

ANISOU 1046 CA GLY A 144 25755 20889 21853 -777 2736 -772 C

ATOM 1047 C GLY A 144 49.212 141.980 -32.677 1.00183.53 C

ANISOU 1047 C GLY A 144 26096 21451 22186 -733 2716 -676 C

ATOM 1048 O GLY A 144 49.985 142.170 -33.608 1.00184.03 O

ANISOU 1048 O GLY A 144 26165 21506 22251 -769 2703 -689 O

ATOM 1049 N CYS A 145 49.347 140.974 -31.823 1.00163.94 N

ANISOU 1049 N CYS A 145 23540 19109 19642 -654 2711 -571 N

ATOM 1050 CA CYS A 145 50.264 139.878 -32.074 1.00158.93 C

ANISOU 1050 CA CYS A 145 22840 18570 18976 --580 2702 -442 C

ATOM 1051 CB CYS A 145 50.642 139.200 -30.769 1.00157.65 C

ANISOU 1051 CB CYS A 145 22535 18658 18706 -572 2688 -370 C

ATOM 1052 SG CYS A 145 52.167 139.770 -30.079 1.00168.08 S

ANISOU 1052 SG CYS A 145 23727 20234 19900 -684 2689 -373 S

ATOM 1053 C CYS A 145 49.607 138.846 -32.965 1.00156.40 C

ANISOU 1053 C CYS A 145 22607 18068 18748 -467 2703 -329 C

ATOM 1054 O CYS A 145 48.385 138.705 -32.976 1.00152.74 O

ANISOU 1054 O CYS A 145 22222 17476 18335 -439 2693 -307 O

ATOM 1055 N LEU A 146 50.422 138.109 -33.706 1.00135.01 N

ANISOU 1055 N ' LEU- A 146 19893 15350 16053 -408 2721 -246 N

ATOM 1056 CA LEU A 146 49.924 136.929 -34.406 1.00133.82 C

ANISOU 1056 CA LEU A 146 19834 15048 15963 -305 2734 -126 C

ATOM 1057 CB LEU A 146 49.919 137.120 -35.916 1.00144.55 C

ANISOU 1057 CB LEU A 146 21326 16193 17405 -343 2766 -149 C

ATOM 1058 CG LEU A 146 49.246 135.960 -36.628 1.00133.62 C

ANISOU 1058 CG LEU A 146 20081 14620 16070 -275 2783 -28 C

ATOM 1059 'CDl LEU A 146 47.789 136.270 -36.833 1.00131.81 C

ANIΞOU 1059 CDl LEU A 146 19953 14255 " 15875 -313 2745 -10 C

ATOM 1060 CD2 LEU A 146 49.920 135.727 -37.932 1.00138.20 C

ANISOU 1060 CD2 LEU A 146 20759 15046 16704 -316 2834 -37 C

ATOM 1061 C LEU A 146 50.788 135.728 -34.067 1.00138.65 C

ANISOϋ 1061 C LEU A 146 20346 15794 16540 -199 2749 2 C

ATOM 1062 O LEU A 146 51.94 ' 8 135.654 -34.496 1.00135.88 O

ANISOU 1062 O LEU A 146 19940 15501 16188 -187 2789 19 O

ATOM 1063 N VAL A 147 50.218 134.804 -33.288 1.00152.53 N

ANISOU 1063 N VAL A 147 22071 17608 18275 -124 2713 100 N

ATOM 1064 CA VAL A 147 50.867 133.542 -32.964 1.00148.56 C

ANISOU 1064 CA VAL A 147 21483 17196 17767 -12 2720 245 C

ATOM 1065 CB VAL A 147 50.564 133.102 -31.540 1.00145.46 C

ANISOU 1065 CB VAL A 147 • 20947 17010 17312 -2 2649 311 C

ATOM 1066 CGl VAL A 147 51.429 131.924 -31.189 1.00150.57 C

ANISOU 1066 CGl VAL A 147 21441 17804 17964 73 2660 ' 452 C

ATOM 1067 CG2 VAL A 147 50.812 134.235 -30.575 1.00150.08 C

ANISOU 1067 CG2 VAL A 147 21437 17761 17824 -136 2625 196 ' C ATOM 1068 C VAL A 147 50.359 132.468 -33.909 1.00151.30 C

ANISOU 1068 C VAL A 147 21997 17320 18171 80 2743 334 C

ATOM 1069 O VAL A 147 49.227 132.009 -33.790 1.00147. 42 O-

ANISOU 1069 O VAL A 147 21605 16736 17672 93 2694 372 O

ATOM 1070 N LYS A 148 51.205 132.074 -34.852 1.00155 75 N

ANISOU 1070 N LYS A 148 22600 17798 18781 135 2823 372 N

ATOM 1071 CA LYS A 148 50.801 131.164 -35.910 1.00150. 06 C

ANISOU 1071 CA LYS A 148 22070 16841 18104 192 2869 440 C

ATOM 1072 CB LYS A 148 50.790 131.896 -37.256 1.00146, 19 C

ANISOU 1072 CB LYS A 148 21720 16166 17660 99 2931 345 C

ATOM 1073 CG LYS A 148 50.502 131.014 -38.460 1.00150. 00 C

ANISOU 1073 CG LYS A 148 22420 16397 18176 116 2994 412 C

ATOM 1074 CD LYS A 148 50.898 131.694 -39.759 1.00154. 72 C

ANISOU 1074 CD LYS A 148 23120 16847 18819 5 3063 321 C

ATOM 1075 CE LYS A 148 50.170 131.075 -40.932 1.00164. 07 C

ANISOU 1075 CE LYS A 148 24558 17761 20021 -56 3105 380 C

ATOM 1076 NZ LYS A 148 48.698 131.289 -40.825 1.00160. 42 N

ANISOU 1076 NZ LYS A 148 24206 17201 19545 -147 3017 421 N

ATOM 1077 C LYS A 148 51.770 130.000 -35.980 1.00154. 65 C

ANISOU 1077 C LYS A 148 22599 17448 18712 328 2932 561 C

ATOM 1078 O LYS A 148 52.987 130.192 -35.886 1.00149. 85 O

ANISOU 1078 O LYS A 148 21836 16979 18120 359 2981 571 O

ATOM 1079 N GLY A 149 51.217 128.795 -36.121 1.00147. 05 N

ANISOU 1079 N GLY A 149 21766 16355 17752 407 2927 669 N

ATOM 1080 CA GLY A 149 51.985 127.614 -36.490 1.00148. 11 C

ANISOU 1080 CA GLY A 149 21922 16423 17931 539 3013 780 C

ATOM 1081 C GLY A 149 52.255 126.581 -35.414 1.001 ' 44. 12 C

ANISOU 1081 C GLY A 149 21221 16102 17436 656 2976 909 C

ATOM 1082 O GLY A 149 52.881 125.566 -35.690 1.00146. 06 O

ANISOU 1082 O GLY A 149 21427 16324 17747 768 3069 994 O

ATOM 1083 N TYR A 150 51.781 126.833 -34.199 1.00153. 43 N

ANISOU 1083 N TYR A 150 22272 17463 18560 622 2844 930 N

ATOM 1084 CA TYR A 150 52.131 126.009 -33.042 1.00155. 19 C

ANISOU 1084 CA TYR A 150 22280 17891 18793 692 2782 1059 C

ATOM 1085 CB TYR A 150 52.188 126.875 -31.776 1.00150. 15 C

ANISOU 1085 CB TYR A 150 21424 17528 18099 579 2688 1013 C

ATOM 1086 CG TYR A 150 50.820 127.274 -31.266 1.00147. 38 C

ANISOU 1086 CG TYR A 150 21140 17196 17663 497 2570 950 C

ATOM 1087 CDl TYR A 150 50.104 128.293 -31.873 1.00150. 65 C

ANISOU 1087 CDl TYR A 150 21741 17444 18054 429 2587 828 C

ATOM 1088 CEl TYR A 150 48.852 128.660 -31.426 1.00143. 54 C

ANISOU 1088 CEl TYR A 150 20893 16555 17092 366 2494 788 C

ATOM 1089 CZ TYR A 150 48.299 128.012 -30.364 1.00141. 30 C

ANISOU 1089 CZ TYR A 150 2-0480 16457 16750 365 2378 854 C

ATOM 1090 OH TYR A 150 47.055 128.388 -29.924 1.00139. 25 O

ANISOU 1090 OH TYR A 150 20268 16214 16426 309 2296 815 O

ATOM 1091 CE2 TYR A 150 48.986 126.996 -29.740 1.00146. 91 C

ANISOU 1091 CE2 TYR A 150 21002 17342 17474 413 2344 966 C

ATOM 1092 CD2 TYR A 150 50.239 126.628 -30.193 1.00145. 21 C

ANISOU 1092 CD2 TYR A 150 20730 17105 17337 481 2442 1021 C

ATOM 1093 C TYR A 150 51.181 124.825 -32.814 1.00155. 72 C

ANISOU 1093 C TYR A 150 22440 17892 18834 766 2692 1176 C

ATOM 1094 O TYR A 150 50.026 124.845 -33.248 1.00152. 82 O

ANISOU 1094 O TYR A 150 22295 17355 18415 740 2659 1156 O

ATOM 1095 N PHE A 151 51.702 123.801 -32.135 1.00155. 87 N

ANISOU 1095 N PHE A 151 22281 18052 18889 845 2646 1315 N

ATOM 1096 CA PHE A 151 50.956 122.615 -31.708 1.00153. 81 C

ANISOU 1096 CA PHE A 151 22064 17772 18604 917 2536 1446 C

ATOM 1097 CB PHE A 151 50.573 121.724 -32.893 1.00154. 84 C

ANISOU 1097 CB PHE A 151 22484 17601 18746 1012 2616 1493 C

ATOM 1098 CG PHE A 151 49.782 120.492 -32.506 1.00152. 62 C

ANISOU 1098 CG PHE A 151 22278 17294 18415 1076 2487 1634 C

ATOM 1099 CDl PHE A 151 48.407 120.440 -32.700 1.00152. 30 C

ANISOU 1099 CDl PHE A 151 22474 17135 18257 1027 2394 1642 C

ATOM 1100 CEl PHE A 151 47.676 119.311 -32.346 1.00151. 91 C

ANISOO. 1100 CEl PHE A 151 22502 17077 18141 1078 2258 1784 C

ATOM 1101 CZ PHE A 151 48.318 118.217 -31.802 1.00150. 99 C

ANISOU 1101 CZ PHE A 151 22220 17059 18090 1180 2213 1908 C

ATOM 1102 CE2 PHE A 151 49.687 118.254 -31.604 1.00153. 80 C

ANISOU 1102 CE2 PHE A 151 22327 17525 18586 1230 2314 1908 C

ATOM 1103 CD2 PHE A 151 50.413 119.388 -31.955 1.00154. 30 C

ANISOU 1103 CD2 PHE A 151 22321 17607 18700 1178 2451 1777 C

ATOM 1104 C PHE A 151 51.858 121.837 -30.774 1.00154. 19 C

ANISOU 1104 C PHE A 151 21840 18015 18730 979 2504 1590 C

ATOM 1105 O PHE A 151 53.047 121.703 -31.035 1.00158. 64 O

ANISOU 1105 O PHE A 151 22302 18576 19398 1047 2631 1636 O

ATOM 1106 N PRO A 152 51.299 121.301 -29.689 1.00155. 84 N ANISOU 1106 N PRO A 152 21922 18398 18892 951 2331 1675 N

ATOM 1107 CA PRO A 152 49.884 121.278 -29.337 1.00157.40 C

ANISOU 1107 CA PRO A 152 22235 18607 18964 891 2174 1649 C

ATOM 1108 CB PRO A 152 49.820 120.057 -28.440 1.00160.03 C

ANISOU 1108 CB PRO A 152 22431 19068 19305 941 2024 1820 C

ATOM 1109 CG PRO A 152 51.103 120.150 -27.659 1.00158.09 C

ANISOU 1109 CG PRO A 152 21863 19036 19168 922 2054 1892 C

ATOM 1110 CD PRO A 152 52.124 120.724 -28.613 1.00157.70 C

ANISOU 1110 CD PRO A 152 21850 18867 19201 958 2268 1821 C

ATOM 1111 C PRO A 152 49.480 122.500 -28.535 1.00156.82 ' C

ANISOU 1111 C PRO A 152 22047 18727 18809 734 2106 1524 C

ATOM 1112 O PRO A 152 50.359 123.277 -28.171 1.00156.05 O

ANISOU 1112 O PRO A 152 21773 18773 18744 662 2167 1471 O

ATOM 1113 N GLU A 153 48.187 122.670 -28.267 1.00155.67 N

ANISOU 1113 N ,GLU A 153 22006 18588 18555 679 1988 1488 N

ATOM 1114 CA GLU A 153 47.757 123.705 -27.337 1.00156.10 C

ANISOU 1114 CA GLU A 153 21931 18843 18536 537 1922 1380 C

ATOM 1115 CB GLU A 153 46.233 123.763 -27.250 1.00153.87 C

ANISOU 1115 CB GLU A 153 21793 18526 18144 510 1809 1364 C

ATOM 1116 CG GLU A 153 45.564 124.665 -28.298 1.00156.65 C

ANISOU 1116 CG GLU A 153 22386 18649 18485 493 1903 1257 C

ATOM 1117 CD GLU A 153 45.315 126.116 -27.822 1.00162.42 C

ANISOU 1117 CD GLU A 153 23046 19468 19197 369 1947 1083 C

ATOM 1118 OEl GLU A 153 46.147 126.682 -27.077 1.00161.73 O

ANISOU 1118 OEl GLU A 153 22746 19592 19112 289 1955 1023 O

ATOM 1119 0E2 GLU A 153 44.277 126.703 -28.208 1.00160.07 O

ANISOU 1119 0E2 GLU A 153 22912 19023 18885 340 1979 1015 O

ATOM 1120 C GLU A 153 48.381 123.415 -25.972 1.00158.75 C

ANISOU 1120 C GLU A 153 21956 19481 18880 468 1831 1455 C

ATOM 1121 O GLU A 153 48.722 122.278 -25.674 1.00160.82 O

ANISOU 1121 O GLO A 153 22121 19798 19184 534 1755 1611 O

ATOM 1122 N PRO A 154 48.520 124.435 -25.124 1.00155.80 N

ANISOU 1122 N PRO A 154 21427 19303 18466 317 1836 1353 N

ATOM 1123 CA PRO A 154 48.067 125.815 -25.248 1.00156.73 C

ANISOU 1123 CA PRO A 154 21654 19368 18529 231 1905 1168 C

ATOM 1124 CB PRO A 154 47.299 126.018 -23.948 1.00158.75 C

ANISOU 1124 CB PRO A 154 21794 19845 18680 104 1775 1132 C

ATOM 1125 CG PRO A 154 47.795 124.872 -23.012 1.00167.04 C

ANISOU 1125 CG PRO A 154 22599 21128 19740 78 1643 1301 C

ATOM 1126 CD PRO A 154 48.886 124.152 -23.739 1.00158.14 C

ANISOU 1126 CD PRO A 154 21440 19908 18737 190 1727 1421 C

ATOM 1127 C PRO A 154 49.240 126.776 -25.233 ' 1.00159.61 C

ANISOU 1127 C PRO A 154 21923 19798 18922 144 2027 1081 C

ATOM 1128 O PRO A 154 50.337 126.364 -24.844 1.00159.79 O

ANISOU 1128 O PRO A 154 21765 19951 18997 132 2047 1183 O

ATOM 1129 N VAL A 155 49.004 128.029 -25.629 1.00146.41 N

ANISOU 1129 N VAL A 155 20366 18047 17217 77 2100 912 N

ATOM 1130 CA VAL A 155 50.010 129.088 -25.532 1.00147.12 C

ANISOU 1130 CA VAL A 155 20378 18222 17300 -35 2192 817 C

ATOM 1131 CB VAL A 155 50.413 129.593 -26.890 1.00142.45 C

ANISOU 1131 CB VAL A 155 19944 17405 16774 36 2316 756 C

ATOM 1132 CGl VAL A 155 51.328 128.600 -27.551 1.00143.38 C

ANISOU 1132 CGl VAL A 155 20008 17488 16980 152 2366 902 C

ATOM 1133 CG2 VAL A 155 49.172 129.848 -27.712 1.00141.91 C

ANISOU 1133 CG2 VAL A 155 20119 17081 16719 103 2322 691 C

ATOM 1134 C VAL A 155 49.459 130.288 -24.791 1.00151.04 C

ANISOU 1134 C VAL A 155 20870 18814 17703 -191 2186 655 C

ATOM 1135 O VAL A 155 48.241 130.476 -24.738 1.00145.82 O

ANISOU 1135 O VAL A 155 20324 18070 17011 -179 2151 587 O

ATOM 1136 N THR A 156 50.350 131.108 -24.233 1.00152.99 N

ANISOU 1136 N THR A 156 20994 19234 17903 -340 2227 605 N

ATOM 1137 CA THR A 156 49.905 132.304 -23.522 1.00150.44 C

ANISOU 1137 CA THR A 156 20677 18999 17483 -504 2241 442 C

ATOM 1138 CB THR A 156 50.119 132.211 -22.036 1.00151.29 C

ANISOU 1138 CB THR A 156 20577 19410 17498 -683 2174 488 C

ATOM 1139 OGl THR A 156 51.349 131.529 -21.796 1.00152.59 O

ANISOU 1139 OGl THR A 156 20575 19693 17711 -637 2099 .697 O

ATOM 1140 CG2 THR A 156 48.952 131.472 -21.398. 1.00153.52 C

ANISOU 1140 CG2 THR A 156 20881 19742 17709 ' -740 2113 398 C

ATOM 1141 C THR A 156 50.447 133.641 -24.002 1.00149.86 C

ANISOU 1141 C THR A 156 20685 18862 17394 -582 2347 302 C

ATOM 1142 O THR A 156 51.608 133.798 -24.382 1.00147.00 O

ANISOU 1142 O THR A 156 20256 18563 17033 -617 2389 353 O

ATOM 1143 N VAL A 157 49.556 134.612 -23.917 1.00147.66 N

ANISOU 1143 N VAL A 157 20542 18467 17096 -614 2383 135 N

ATOM 1144 CA VAL A 157 49.713 135.891 -24.540 1.00143.14 C

ANISOU 1144 CA VAL A 157 20082 17779 16525 -668 2471 -14 C ATOM 1145 CB VAL A 157 48.698 136.009 -25.656 1.00145.11 C

ANISOU 1145 CB VAL A 157 20522 17739 16875 -541 2497 > -72 C

ATOM 1146 CGl VAL A 157 48.484 137.452 -26.035 1.00155.31 C

ANISOU 1146 CGl VAL A 157 21926 18905 18181 -614 2573 -240 C

ATOM 1147 CG2 VAL A 157 49.145 135.167 -26.841 1.00144.20 C

ANISOU 1147 CG2 VAL A 157 20449 17493 16849 -390 2487 63 C

ATOM 1148 C VAL A 157 49. 467 136.952 -23.487 1.00149.67 C

ANISOU 1148 C VAL A 157 20892 18730 17244 -850 2500 -161 C

ATOM 1149 O VAL A 157 48.330 137.171 -23.043 1.00144.68 O

ANISOU 1149 O VAL A 157 20328 18036 16609 -853 2508 -259 O

ATOM 1150 N THR A 158 50.567 137. 572 -23.070 1..00173.56 N

ANISOU 1150 N THR A 158 23828 21938 20177 -1010 2521 -161 N

ATOM 1151 CA THR A 158 50.569 138. 662 -22.110 1..00173.54 C

ANISOU 1151 CA THR A 158 23838 22047 20051 -1216 2569 -306 C

ATOM 1152 CB THR A 158 51.452 138.325 -20.907 1..00173.70 C

ANISOU 1152 CB THR A 158 23678 22377 19944 -1413 2533 -199 C

ATOM 1153 OGl THR A 158 52.819 138.239 -21.332 1..00172.74 O

ANISOU 1153 OGl THR A 158 23500 22330 19805 -1447 2538 -86 O

ATOM 1154 CG2 THR A 158 51.040 136. 989 -20.300 1..00173.93 C

ANISOU 1154 CG2 THR A 158 23551 22530 20004 -1359 2436 -37 C

ATOM 1155 C THR A 158 51.174 139. 859 -22.818 1..00176.81 C

ANISOU 1155 C THR A 158 24374 22346 20458 -1259 2638 -422 C

ATOM 1156 O THR A 158 52.049 139.702 -23.672 1..00177.46 O

ANISOU 1156 O THR A 158 24476 22347 20605 -1170 2634 -356 O

ATOM 1157 N TRP A 159 50.715 141.055 -22.477 1..00169.72 N

ANISOU 1157 N TRP A 159 23563 21441 19483 -1401 2700 -598 N

ATOM 1158 CA TRP A 159 51.205 142.244 -23.162 1..00170.03 C

ANISOU 1158 CA TRP A 159 23727 21360 19516 -1446 2750 -715 C

ATOM 1159 CB TRP A 159 50.044 143.007 -23.785 1..00167.90 C

ANISOU 1159 CB TRP A 159 23615 20821 19359 -1360 2805 -882 C

ATOM 1160 CG TRP A 159 49.504 142.363 -25.007 1..00161.21 C

ANISOU 1160 CG TRP A 159 22813 19758 18682 -1152 2774 -814 C

ATOM 1161 CDl TRP A 159 48.569 141.381 -25.067 1..00160.08 C

ANISOU 1161 CDl TRP A 159 22649 19555 18618 -1014 2741 -726 C

ATOM 1162 NEl TRP A 159 '48.315 141.047 -26.372 1..00158.97 N

ANISOU 1162 NEl TRP A 159 22588 19199 18613 -871 2725 -673 N

ATOM 1163 CE2 TRP A 159 49.097 141.825 -27.182 1..00159.57 C

ANISOU 1163 CE2 TRP A 159 22724 19199 18708 -915 2745 -735 C

ATOM 1164 CD2 TRP A 159 49.856 142.667 -26.352 1..00160.35 C

ANISOU 1164 CD2 TRP A 159 22787 19468 18670 -1084 2770 -821 C

ATOM 1165 CE3 TRP A 159 50.741 143. 573 -26.936 1.00162.26 C

ANISOU 1165 CE3 TRP A 159 23080 19685 18885 -1164 2776 -888 C

ATOM 1166 C23 TRP A 159 50.840 143. 606 -28.304 1.00163.09 C

ANISOU 1166 CZ3 TRP A 159 23254 19603 19111 -1077 2757 -876 C

ATOM 1167 CH2 TRP A 159 50.073 142.749 -29.109 1.00159.38 C

ANISOU 1167 CH2 TRP A 159 22816 18961 18780 -924 2744 -793 C

ATOM 1168 CZ2 TRP A 159 49.198 141.854 -28.566 1.00157.95 C

ANISOU 1168 CZ2 TRP A 159 22601 18795 18616 -841 2738 -717 C

ATOM 1169 C TRP A 159 52.014 143.153 -22.239 1.00172.40 C

ANISOU 1169 C TRP A 159 24022 21850 19633 -1695 2782 -773 C

ATOM 1170 O TRP A 159 51.487 143.692 -21.261 1.00174.22 O

ANISOU 1170 O TRP A 159 24294 22126 19777 -1832 2837 -900 O

ATOM 1171 N ASN A 160 53.292 143.329 -22.566 1.00175.80 N

ANISOU 1171 N ASN A 160 24411 22390 19995 -1762 2753 -673 N

ATOM 1172 CA ASN A 160 54.207 144.038 -21.685 1.00178.53 C

ANISOU 1172 CA ASN A 160 24748 22945 20139 -2021 2767 -676 C

ATOM 1173 CB ASN A 160 53.715 145.460 -21.435 1.00180.74 C

ANISOU 1173 CB ASN A 160 25207 23111 20354 -2141' 2847 -917 C

ATOM 1174 CG ASN A 160 54.313 146.451 -22.390 1.00177.57 C

ANISOU 1174 CG ASN A 160 24934 22598 19938 -2160 2846 -998 C

ATOM 1175 ODl ASN A 160 53.653 146.911 -23.318 1.00168,.85 O

ANISOU 1175 ODl ASN A 160 23955 21245 18954 -2056 2876 -1150 O

ATOM 1176 ND2 ASN A 160 55.583 146.776 -22.181 1.00181..73 N

ANISOU 1176 ND2 ASN A 160 25421 23317 20312 -2306 2802 -879 N

ATOM 1177 C ASN A 160 54.305 143.304 -20.366 1.00180,.06 C

ANISOU 1177 C ASN A 160 24783 23400 20230 -2169 2745 -550 C

ATOM 1178 O ASN A 160 54.201 143.915 -19.309 1.00186,.02 O

ANISOU 1178 O ASN A 160 25565 24284 20830 -2401 2786 -626 O

ATOM 1179 N SER A 161 54.497 141. 990 -20.432 1.00168,.67 N

ANISOU 1179 N SER A 161 23179 22032 18876 -2048 2681 -358 N

ATOM 1180 CA SER A 161 54.429 141. 141 -19.246 1.00170,.57 C

ANISOU 1180 CA SER A 161 23253 22499 19056 -2172 2641 -241 C

ATOM 1181 CB SER A 161 55.642 141.363 -18.337 1.00175,.86 C

ANISOU 1181 CB SER A 161 23814 23462 19543 -2462 2626 -95 C

ATOM 1182 OG SER A 161 56.849 141.376 -19.083 1.00179,.40 O

ANISOU 1182 OG SER A 161 24154 23983 20026 -2399 2584 124 O

ATOM 1183 C SER A 161 53.137 141.409 -18.482 1.00167,.51 C ANISOU 1183 C SER A 161 22935 22069 18641 -2230 2683 -427 C

ATOM 1184 O SER A 161 53.153 141.591 -17.268 1.00167.31 O

ANISOU 1184 O SER A 161 22878 22230 18463 -2483 2705 -459 O

ATOM 1185 N GLY A 162 52.026 141.452 -19.210 1.00176.51 N

ANISOU 1185 N GLY A 162 24175 22966 19926 -2007 2700 -541 N

ATOM 1186 CA GLY A 162 50.716 141.608 -18.605 1.00179.40 C

ANISOU 1186 CA GLY A 162 24594 23277 20292 -2014 2740 -692 C

ATOM 1187 C GLY A 162 50.410 142.975 -18.011 1.00181.71 C

ANISOU 1187 C GLY A 162 25030 23538 20472 -2195 2855 -913 C

ATOM 1188 O GLY A 162 49.305 143.214 -17.515 1.00182.22 O

ANISOU 1188 O GLY A 162 25152 23538 20546 -2194 2915 -1056 O

ATOM 1189 N . SER A 163 51.378 143.881 -18.051 1.00180.15 N

ANISOU 1189 N SER A 163 24897 23386 20164 -2353 2890 -939 N

ATOM 1190 CA SER A 163 51.157 145.225 -17.537 1.00183.26 C

ANISOU 1190 CA SER A 163 25452 23737 20440 -2535 3004 -1150 C

ATOM 1191 CB SER A 163 52.391 146.086 -17.769 1.00184.37 C

ANISOU 1191 CB SER A 163 25655 23955 20443 -2705 3004 -1121 C

ATOM 1192 OG SER A 163 53.476 145.596 -17.000 1.00182.86 O

ANISOU 1192 OG SER A 163 25308 24064 20107 -2905 2938 -913 O

ATOM- 1193 C SER A 163 49.934 145.844 -18.195 1.00184.47 C

ANISOU 1193 C SER A 163 25765 23581 20746 -2350 3086 -1348 C

ATOM 1194 O SER A 163 49.154 146.549 -17..562 1.00188.81 O

ANISOU 1194 O SER A 163 26426 24063 21249 -2444 3199 -1537 O

ATOM 1195 N LEU A 164 49.765 145.568 -19.475 1.00186.50 N

ANISOU 1195 N LEU A 164 26028 23645 21187 -2097 3036 -1293 N

ATOM 1196 CA LEU A 164 48.554 145.960 -20.153 1.00190.39 C

ANIΞOU 1196 CA LEU A 164 26636 23853 21852 -1916 3095 -1421 C

ATOM 1197 CB LEU A 164 48.841 146.160 -21.631 1.00190.13 C

ANISOU 1197 CB LEU A 164 26669 23614 21959 -1763 3057 -1394 C

ATOM 1198 CG LEU A 164 49.805 147.295 -21.957 1.00189.56 C

ANISOQ 1198 CG LEU A 164 26698 23516 21812 -1890 3075 -1477 C

ATOM 1199 CDl LEU A 164 50.591 146.964 -23.209 1.00184.65 C

ANISOU 1199 CDl LEU A 164 26039 22874 21247 -1796 2979 -1342 C

ATOM 1200 CD2 LEU A 164 49.050 148.611 -22.110 1.00183.91 C

ANISOU 1200 CD2 LEU A 164 26144 22553 21179 -1886 3172 -1685 C

ATOM 1201 C LEU A 164 47.517 144.865 -19.970 1.00190.04 C

ANISOU 1201 C LEU A 164 26505 23802 21899 -1765 3059 -1346 C

ATOM 1202 O LEU A 164 47.860 143.690 -19.873 1.00190.69 O

ANISOU 1202 O LEU A 164 26444 24057 21951 -1751 2963 -1180 O

ATOM 1203 N SER A 165 46.248 145.247 -19.919 1.00177.74 N

ANISOU 1203 N SER A 165 25029 22048 20456 -1652 3128 -1451 N

ATOM 1204 CA SER A 165 45.172 144.270 -19.848 1.00175.80 C

ANISOU 1204 CA SER A 165 24710 21805 20282 -1511 3079 -1360 C

ATOM 1205 CB SER A 165 44.861 143.939 -18.401 1.00180.47 C

ANIΞOU 1205 CB SER A 165 25214 22630 20726 -1668 3097 -1397 C

ATOM 1206 OG SER A 165 44.389 145.102 -17.753 1.00187.98 O

ANISOU 1206 OG SER A 165 26275 23510 21638 -1777 3250 -1609 O

ATOM 1207 C SER A 165 43.920 144.817 -20.513 1.00176.90 C

ANISOU 1207 C SER A 165 24950 21675 20589 -1347 3143 -1422 C

ATOM 1208 O SER A 165 43.632 144.501 -21.661 1.00178.75 O

ANISOU 1208 O SER A 165 25191 21772 20955 -1170 3077 -1298 O

ATOM 1209 N SER A 166 43.177 145.629 -19.772 1.00194.57 N

ANISOU 1209 N SER A 166 27269 23840 22820 -1419 3280 -1602 N

ATOM 1210 CA SER A 166 41.982 146.299 -20.279 1.00205.11 C

ANISOU 1210 CA SER A 166 28678 24940 24316 -1281 3366 -1656 C

ATOM 1211 CB SER A 166 42.162 147.813 -20.160 1.00213.03 C

ANISOU 1211 CB SER A 166 29792 25843 25307 -1395 3540 -1884 C

ATOM 1212 OG SER A 166 43.539 148.146 -20.096 1.00215.34 O

ANISOU 1212 OG SER A 166 30145 26162 25513 -1539 3544 -1958 O

ATOM 1213 C SER A 166 41.535 145.920 -21.703 1.00203.89 C

ANISOU 1213 C SER A 166 28573 24529 24366 -1092 3317 -1542 C

ATOM 1214 O SER A 166 40.733 145.001 -21.889 1.00198.94 O

ANISOU 1214 O SER A 166 27925 23831 23833 -947 3277 -1418 O

ATOM 1215 N GLY A 167 42.048 146.630 -22.702 1.00182.17 N

ANISOU 1215 N GLY A 167 25892 21647 21676 "-1112 3314 -1576 N

ATOM 1216 CA GLY A 167 41.573 146.465 r 24.061 1.00172.14 C

ANISOU 1216 CA GLY A 167 24672 20136 20596 -980 3274 -1480 C

ATOM 1217 C GLY A 167 42.079 145.231 -24.782 1.00171.39 C

ANISOU 1217 C GLY A 167 24524 20090 20508 -883 3135 -1276 C

ATOM 1218 O GLY A 167 42.029 145.176 -26.012 1.00172.08 O

ANISOU 1218 O GLY A 167 24656 19988 20737 -789 3096 -1172 O

ATOM 1219 N VAL A 168 42.551 144.236 -24.032 1.00164.01 N

ANISOU 1219 N VAL A 168 23492 19402 19422 -920 3065 -1211 N

ATOM 1220 CA VAL A 168 43.138 143.037 -24.635 1.00154.66 C

ANISOU 1220 CA VAL A 168 22258 18270 18235 -837 2944 -1028 C

ATOM 1221 CB VAL A 168 44.141 142.344 -23.708 1.00153.20 C

ANISOU 1221 CB VAL A 168 21947 18375 17887 -918 2882 -976 C ATOM 1222 CGl VAL A 168 44.433 140.956 -24.212 1.00151.45 C

ANISOU 1222 CGl VAL A 168 21675 18180 17688 -804 2772 -779 C

ATOM 1223 CG2 VAL A 168 45.414 143.131 -23.640 1.00158.82 C

ANISOU 1223 CG2 VAL A 168 22654 19186 18503 -1072 2917 -1073 C

ATOM 1224 C VAL A 168 42.111 142.006 -25.067 1.00151.49 C

ANISOU 1224 C VAL A 168 21866 17778 17916 -688 2885 -867 C

ATOM 1225 O VAL A 168 41.047 141.870 -24.470 1.00150.55 O

ANISOU 1225 O VAL A 168 21733 17676 17794 ' -655 2903 -862 O

ATOM 1226 N HIS A 169 42.457 141.270 -26.111 1.00162.77 N

ANISOU 1226 N HIS A 169 23327 19114 19406 -608 2814 -732 N

ATOM 1227 CA HIS A 169 41.576 140.270 -26.669 1.00164.63 C

ANISOU 1227 CA HIS A 169 23586 19282 19682 -486 2737 -547 C

ATOM 1228 CB HIS A 169 40.678 140.903 -27.731 1.00163.77 C

ANISOϋ 1228 CB HIS A 169 23597 18899 19731 -436 2770 -500 C

ATOM 1229 CG HIS A 169 39.468 141.585 -27.180 1.00160.89 C

ANISOU 1229 CG HIS A 169 23243 18466 19422 -443 2852 -575 C

ATOM 1230 NDl HIS A 169 38.566 140.945 -26.355 1.00165.89 N

ANISOU 1230 NDl HIS A 169 23828 19208 19995 -398 2838 -526 N

ATOM 1231 CEl HIS A 169 37.593 141.781 -26.045 1.00172.53 C

ANISOU 1231 CEl HIS A 169 24691 19944 20919 -403 2941 -607 C

ATOM 1232 NE2 HIS A 169 37.828 142.936 -26.643 1.00166.55 N

ANISOU 1232 NE2 HIS A 169 23994 19006 20280 -453 3014 -703 N

ATOM 1233 CD2 HIS A 169 38.991 142.836 -27.365 1.00160.57 C

ANISOU 1233 CD2 HIS A 169 23254 18251 19503 -483 2951 -685 C

ATOM 1234 C HIS A 169 42.374 139.149 -27.318 1.00162.06 C

ANISOU 1234 C HIS A 169 23250 18990 19337 -442 2661 -423 C

ATOM 1235 O HIS A 169 42.482 139.095 -28.537 1.00160.65 O

ANISOU 1235 O HIS A 169 23150 18648 19241 -429 2670 -400 O

ATOM 1236 N THR A 170 42.938 138.249 -26.526 1.00158.35 N

ANISOU 1236 N THR A 170 22677 18725 18764 -425 2589 -341 N

ATOM 1237 CA THR A 170 43.567 137.082 -27.123 1.00155.44 C

ANISOU 1237 CA THR A 170 22308 18352 18400 -351 2526 -197 C

ATOM 1238 CB THR A 170 44.494 136.350 -26.145 1.00154.79 C

ANISOU 1238 CB THR A 170 22067 18531 18214 -385 2475 -155 C

ATOM 1239 OGl THR A 170 45.008 137.270 -25.175 1.00155.42 O

ANISOU 1239 OGl THR A 170 22068 18756 18227 -525 2532 -299 O

ATOM 1240 CG2 THR A 170 45.641 135.717 -26.901 1.00152.10 C

ANISOU 1240 CG2 THR A 170 21724 18162 17906 -319 2458 -46 C

ATOM 1241 C THR A 170 42.480 136.127 -27.620 1.00152.87 C

ANISOU 1241 C THR A 170 22072 17905 18107 -242 2460 -36 C

ATOM 1242 O THR A 170 41.820 135.453 -26.835 1.00157.05 O

ANISOU 1242 O THR A 170 22569 18516 18586 -221 2410 11 O

ATOM 1243 N PHE A 171 42.282 136.078 -28.928 1.00147.30 N

ANISOU 1243 N PHE A 171 21487 17004 17475 -190 _ 2461 54 N

ATOM 1244 CA PHE A 171 41.265 135.205 -29.498 1.00146.53 C

ANISOU 1244 CA PHE A 171 21506 16774 17395 -117 2403 220 C

ATOM 1245 CB PHE A 171 41.069 135.517 -30.981 1.00146.21 C

ANISOU 1245 CB PHE A 171 21628 16463 17464 -135 2451 256 C

ATOM 1246 CG PHE A 171 40.511 136.866 -31.235 1.00141.76 C

ANISOU 1246 CG PHE A 171 21092 15774 16995 -209 2520 150 C

ATOM 1247 CDl PHE A 171 39.164 137.105 -31.093 1.00141.92 C

ANISOU 1247 CDl PHE A 171 21197 15653 17074 -208 2515 250 C

ATOM 1248 CEΪ PHE A 171 38.634 138.348 -31.313 1.00140.71 C

ANISOU 1248 CEl PHE A 171 21056 15376 17033 -269 2585 167 C

ATOM 1249 CZ PHE A 171 39.445 139.367 -31.678 1.00144.42 C

ANISOU 1249 CZ PHE A 171 21470 15859 17544 -335 2654 -30 C

ATOM 1250 CE2 PHE A 171 40.798 139.145 -31.826 1.00148.07 C

ANISOU 1250 CE2 PHE A 171 21862 16474 ' 17925 -346 2651 -130 C

ATOM 1251 CD2 PHE A 171 41.325 137..8 " 99 -31.603 1.00144.01 C

ANISOU 1251 CD2 PHE A 171 21319 16085 17313 -282 2589 -33 C

ATOM 1252 C PHE A 171 41.558 133.714 -29.351 1.00145.57 C

ANISOU 1252 C PHE A 171 21367 16745 17197 -34 2308 379 C

ATOM 1253 O PHE A 171 42.705 133.293 -29.211 1.00146.29 O

ANISOU 1253 O PHE A 171 21362 16964 17259 -22 2299 375 O

ATOM 1254 N PRO 4 A 172 40.498 132.913 -29.371 1.00141.63 N

ANISOU 1254 N PRO A 172 20960 16185 16668 19 2231 536 N

ATOM 1255 CA PRO A 172 40.483 131.473 -29.620 1.00141.36 C

ANISOU 1255 CA PRO A 172 20987 16142 16580 97 2146 712 C

ATOM 1256 CB PRO A 172 39.040 131.239 -30.022 1.00140.91 C

ANISOU 1256 CB PRO A 172 21099 15926 16514 107 2100 866 C

ATOM 1257 CG PRO A 172 38.283 132.248 -29.194 1.00143.26 C

ANISOU 1257 CG PRO A 172 21329 16281 16823 67 2117 789 C

ATOM 1258 CD PRO A 172 39.194 133.401 -28.902 1.00141.17 C

ANISOU 1258 CD PRO A 172 20938 16091 16611 7 2217 562 C

ATOM 1259 C PRO A 172 41.347 131.123 -30.804 1.00142.96 C

ANISOU 1259 C PRO A 172 21267 16209 16843 112 2213 717 C

ATOM . 1260 O PRO A 172 41.288 131.842 -31.793 1.00147.02 O ANISOU 1260 O PRO A 172 21863 16559 17440 57 2302 643 O

ATOM 1261 N ALA A 173 42.108 130.037 -30.717 1.00151 01 N

ANISOU 1261 N ALA A 173 22255 17295 17826 183 2174 804 N

ATOM 1262 CA ALA A 173 42.955 129.592 -31.822 1.00154 79 C

ANISOU 1262 CA ALA A 173 22829 17625 18360 216 2249 831 C

ATOM 1263 CB ALA A 173 44.166 128.864 -31.286 1.00157, 30 C

ANISOU 1263 CB ALA A 173 23006 18097 18663 291 2230 874 C

ATOM 1264 C ALA A 173 42.174 128.685 -32.765 1.00154. 00 C

ANISOU 1264 C ALA A 173 22973 17294 18247 230 2235 982 C

ATOM 1265 O ALA A 173 41.077 128.258 -32.428 1.00155. 79 O -

ANISOU 1265 O ALA A 173 23278 17500 18415 221 2152 1086 O

ATOM 1266 N VAL A 174 42.724 128.404 -33.946 1.00143. 89 N

ANISOU 1266 N VAL A 174 21818 15841 17011 238 2320 1001 N

ATOM 1267 CA VAL A 174 42.099 127.457 -34.875 1.00144. 71 C

ANISOU 1267 CA VAL A 174 22170 15734 17080 233 2312 1159 C

ATOM 1268 CB VAL A 174 41.377 128.146 -36.039 l. " 00143. 17 C

ANISOU 1268 CB VAL A 174 22151 15313 16935 101 2371 1156 C

ATOM 1269 CGl VAL A 174 40.180 128.923 -35.537 1.00140. 25 C

ANISOU 1269 CGl VAL A 174 21751 14980 16557 42 2303 1174 C

ATOM 1270 CG2 VAL A 174 42.344 129.016 -36.834 1.00150. 19 C

ANISOU 1270 CG2 VAL A 174 23001 16137 17929 44 2494 992 C

ATOM 1271 C VAL A 174 43.113 126.487 -35.466 1.00152. 14 C

ANISOU 1271 C VAL A 174 23178 16597 18033 307 2379 1201 C

ATOM 1272 O VAL A 174 44.318 126.659 -35.293 1.00154. 13 O

ANISOU 1272 O VAL A 174 23292 16923 18346 351 2456 1104 O

ATOM 1273 N LEU A 175 42.622 125.490 -36.198 1.00140. 66 N

ANISOU 1273 N LEU A 175 21945 14986 16515 316 2358 1357 N

ATOM 1274 CA LEU A 175 43.447 124.361 -36.602 1.00144. 37 C

ANISOU 1274 CA LEU A 175 22480 15388 16986 410 2417 1414 C

ATOM 1275 CB LEU A 175 42.821 123.101 -36.017 1.00144. 34 C

ANISOU 1275 CB LEU A 175 22511 15456 16877 493 2279 1581 C

ATOM 1276 CG LEU A 175 43.713 122.185 -35.183 1.00146. 58 C

ANISOU 1276 CG LEU A 175 22642 15863 17189 636 2272 1607 C

ATOM 1277 CDl LEU A 175 45.081 122.785 -34.921 1.00146. 13 C

ANISOU 1277 CDl LEU A 175 22346 15924 17254 670 2378 1461 C

ATOM 1278 CD2 LEU A 175 43.006 121.893 -33.881 1.00143. 54 C

ANISOU 1278 CD2 LEU A 175 22119 15700 16720 680 2078 1700 C

ATOM 1279 C LEU A 175 43.602 124.216 -"38.12I 1.00152. 19 C

ANISOU 1279 C LEU A 175 23734 16098 17995 336 2548 1433 C

ATOM 1280 O LEU A 175 42.637 123.937 -38.822 1.00157. 75 O

ANISOU 1280 O LEU A 175 24686 16637 18616 269 2519 1572 O

ATOM 1281 N GLN A 176 44.811 124.402 -38.635 1.00211. 15 N

ANISOU 1281 N GLN A 176 31148 23519 25559 331 2688 1302 N

ATOM 1282 CA GLN A 176 45.041 124.213 -40.062 1.00223. 45 C

ANISOU 1282 CA GLN A 176 32942 24822 27135 250 2825 1303 C

ATOM 1283 CB GLN A 176 45.610 125.474 -40.711 1.00235. 99 C

ANISOU 1283 CB GLN A 176 34475 26374 28818 139 2919 1140 C

ATOM 1284 CG GLN A 176 44.746 126.721 -40.600 1.00238. 36 C

ANISOU 1284 CG GLN A 176 34747 26686 29132 -9 2842 1098 C

ATOM 1285 CD GLN A 176 45.420 127.944 -41.215 1.00245. 16 C

ANISOU 1285 CD GLN A 176 35517 27541 30091 -105 2916 927 C

ATOM 1286 OEl GLN A 176 45.751 127.951 -42.405 1.00248. 26 O

ANISOU 1286 OEl GLN A 176 36045 27766 30517 -204 3016 896 O

ATOM 1287 NE2 GLN A 176 45.630 128.984 -40.404 1.00230. 72 N

ANISOU 1287 NE2 GLN A 176 33465 25899 28299 -87 2864 815 N

ATOM 1288 C GLN A 176 46.019 123.082 -40.266 1.00221. 37 C

ANISOU 1288 C GLN A 176 32707 24513 26891 388 2926 1333 C

ATOM 1289 O GLN A 176 47.223 123.267 -40.125 1.00220. 59 O

ANISOU 1289 O GLN A 176 32433 24499 26882 472 3018 1235 O

ATOM 1290 N SER A 111 45.500 121.910 -40.599 1.00190. 36 N

ANISOU 1290 N SER A 177 29000 20450 22878 412 2911 1481 N

ATOM 1291 CA SER A 177 46.347 120.754 -40.852 1.00190. 15 C

ANISOU 1291 CA SER A 177 29040 20331 22877 541 3028 1517 C

ATOM 1292 CB SER A 177 47.162 120.952 -42.145 1.00196. 00 C

ANISOU 1292 CB SER A 177 29930 20862 23678 466 3236 1422 C

ATOM 1293 OG SER A 111 47.293 119.746 -42.896 1.00189. 30 O

ANISOU 1293 OG SER A 177 29316 19808 22803 518 3359 1497 O

ATOM 1294 C SER A 177 47.260 120.549 -39.647 1.00180. 65 C

ANISOU 1294 C SER A 111 27512 19366 21761 722 3007 1487 C

ATOM 1295 O SER A 111 48.453 120.832 -39.698 1.00179. 33 O

ANISOU 1295 O SER A 177 27185 19250 21701 774 3126 1385 O

ATOM 1296 N ASP A 178 46.673 120.072 -38.556 1.00176. 15 N

ANISOU 1296 N ASP A 178 26839 18952 21137 800 2845 1592 N

ATOM 1297 CA ASP A 178 47.390 119.804 -37.302 1.00180. 37 C

ANISOU 1297 CA ASP A 178 27062 19724 21746 943 2798 1604 C

ATOM 1298 CB ASP A 178 48.130 118.447 -37.354 1.00183. 18 C

ANISOU 1298 CB ASP A 178 27451 19979 22171 1096 2909 1687 C ATOM 1299 CG ASP A 178 47.191 117.234 -37.159 1.00183.94 C

ANISOU 1299 CG ASP A 178 27737 19986 22166 1142 2803 1851 C

ATOM 1300 ODl ASP A 178 46.584 117.067 -36.071 1.00177 03 O

ANISOU 1300 ODl ASP A 178 26750 19294 21219 1145 2595 1932 O

ATOM 1301 OD2 ASP A 178 47.083 116.420 -38.101 1.00186 62 O

ANISOU 1301 OD2 ASP A 178 28344 20072 22490 1169 2926 1899 O

ATOM 1302 C ASP A 178 48.327 120.934 -36.820 1.00175, 12 C

ANISOU 1302 C ASP A 178 26101 19264 21171 929 2828 1470 C

ATOM 1303 O ASP A 178 49.400 120.665 -36.277 1.00170. 71 O

ANISOU 1303 O ASP A 1'78 25308 18853 20702 1031 2862 1484 O

ATOM 1304 N LEU A 179 47.908 122.188 -37.002 1.00171. 35 N

ANISOU 1304 N LEU A 179 25638 18798 20671 794 2811 1359 N

ATOM 1305 CA LEU A 179 48.664 123.345 -36.508 1.00168. 77 C

ANISOU 1305 CA LEU A 179 25064 18660 20400 754 2822 1230 C

ATOM 1306 CB LEU A 179 49.691 123.795 -37.544 1.00167. 06 C

ANISOU 1306 CB LEU A 179 24882 18331 20262 733 2997 1128 C

ATOM 1307 CG LEU A 179 50.877 122.837 -37.616 1.00169. 69 C

ANISOU 1307 CG LEU A 179 25135 18661 20680 882 3120 1188 C

ATOM 1308 CDl LEU A 179 51.557 122.833 -38.981 1.00173. 44 C

ANISOU 1308 CDl LEU A 179 25760 18928 21210 874 3313 1124 C

ATOM 1309 CD2 LEU A 179 51.856 123.163 -36.514 1.00167. 56 C

ANISOU 1309 CD2 LEU A 179 ' 24530 18675 20461 930 3085 1190 C

ATOM 1310 C LEU A 179 47.751 124.510 -36.121 1.00169. .67 C

ANISOU 1310 C LEU A 179 25152 18858 20457 627 2711 1157 C

ATOM 1311 O LEU A 179 46.906 124.932 -36.917 1.00167. 22 O

ANISOU 1311 O LEU A 179 25046 18381 20108 526 2705 1151 O

ATOM 1312 N TYR A 180 47.925 125.021 -34.901 1.00159. 68 N

ANISOU 1312 N TYR A 180 23634 17849 19190 622 2632 1113 N

ATOM 1313 CA TYR A 180 47.068 126.083 -34.371 1.00155. 91 .C

ANISOU 1313 CA TYR A 180 23107 17466 18665 516 2543 1033 C

ATOM 1314 CB TYR A 180 46.996 126.023 -32.842 1.00151. 43 C

ANISOU- 1314 CB TYR A 180 22305 17178 18055 529 2420 1055 C

ATOM 1315 CG TYR A 180 46.197 124.866 -32.259 1.00156. 99 C

ANISOU 1315 CG TYR A 180 23041 17919 18688 590 2289 1205 C

ATOM 1316 CDl TYR A 180 44.813 124.929 -32.133 1.00155. 22 C

ANISOU 1316 CDl TYR A 180 22951 17645 18379 547 2189 1249 C

ATOM 1317 CEl TYR A 180 44.094 123.868 -31.580 1.00154. 84 C

ANISOU 1317 CEl TYR A 180 22934 17649 18248 598 2049 1397 C

ATOM 1318 CE TYR A 180 44.766 122.744 -31.140 1.00156. 78 C

ANISOU 1318 CZ TYR A 180 23071 17988 18509 692 2007 1493 C

ATOM 1319 OH TYR A 180 44.094 121.683 -30.594 1.00165. 89 O

ANISOU 1319 OH TYR A 180 24252 19200 19578 737 1851 1642 O

ATOM 1320 CE2 TYR A 180 46.126 122.666 -31.241 1.00157. 57 C

ANISOU 1320 CE2 TYR A 180 23028 18128 18714 739 2116 1457 C

ATOM 1321 CD2 TYR A 180 46.836 123.723 -31.796 1.00160. 96 C

ANISOU 1321 CD2 TYR A 180 23432 18515 19212 690 2256 1318 C

ATOM 1322 C TYR A 180 47.533 127.476 -34.795 1.00155. 53 C

ANISOU 1322 C TYR A 180 23021 17408 18666 420 2625 873 C

ATOM 1323 O TYR A 180 48.717 127.701 -35.020 1.00154. 43 O

ANISOU 1323 O TYR A 180 22793 17301 18581 441 2717 824 O

ATOM 1324 N THR A 181 46.591 128.409 -34.893 1.00158. 83 N

ANISOU 1324 N THR A 181 23503 17778 19066 315 2588 805 N

ATOM 1325 CA THR A 181 46.899 129.791 -35.234 1.00157. 46 C

ANISOU 1325 CA THR A 181 23308 17579 18940 210 2645 653 C

ATOM 1326 CB THR A 181 46.624 130.075 -36.711 1.00161. 73 C

ANISOU 1326 CB THR A 181 24069 17851 19529 133 2720 643 C

ATOM 1327 OGl THR A 181 47.066 128.974 -37.512 1.00166. 69 O

ANISOU 1327 OGl THR A 181 24830 18346 20157 202 2780 744 O

ATOM 1328 CG2 THR A 181 47.340 131.333 -37.142 1.00159. 26 C

ANISOU 1328 CG2 THR A 181 23698 17539 19275 51 2788 495 C

ATOM 1329 C THR A 181 46.011 130.726 -34.427 1.00157. 58 C

ANISOU 1329 C THR A 181 23262 17680 18930 131 2575 580 C

ATOM 1330 O THR A 181 44.788 130.691 -34.561 1.00155. 08 O

ANISOU 1330 O THR A 181 23073 17243 18606 90 2535 627 O

ATOM 1331 N LEU A 182 46.616 131.564 -33.590 1.00152. 51 N

ANISOU 1331 N LEU A 182 22430 17244 18273 103 2568 477 N

ATOM 1332 CA LEU A 182 45.844 132.494 -32.766 1.00148. 70 C

ANISOU 1332 CA LEO A 182 21894 16838 17769 27 2528 387 C

ATOM 1333 CB LEϋ A 182 45.865 132.086 -31.290 1.00144. 46 C

ANISOU 1333 CB LEU A 182 21191 16547 17152 50 2452 412 C

ATOM 1334 CG LEU A 182 46.759 132.934 -30.397 1.00145. 49 C

ANISOU 1334 CG LEU A 182 21122 16913 17244 -11 2466 319 C

ATOM 1335 CDl LEU A 182 45.959 134.068 -29.804 1.00142. 25 C

ANISOU 1335 CDl LEU A 182 20698 16529 16821 -122 2488 162 C

ATOM 1336 CD2 LEU A 182 47.344 132.088 -29.309 1.00148. 91 C

ANISOU 1336 CD2 LEU A 182 21399 17570 17610 20 2382 416 C

ATOM 1337 C LEU A 182 46.339 133.927 -32.926 ' 1.00147. 17 C ANISOU 1337 C LEU A 182 21661 16646 17611 -76 2584 220 C

ATOM .1338 O LEU A 182 47.509 134.175 -33.218 1.00143.63 O

ANISOU 1338 o - LEU A 182 21152 16249 17173 -93 2632 167 O

ATOM 1339 N SER A 183 45.429 134.864 -32.709 1.00167.67 N

ANISOU 1339 N SER A 183 24291 19191 20225 -143 2574 150 N

ATOM 1340 CA SER A 183 45.671 136.259 -32.991 1.00166.42 C

ANISOU 1340 CA SER A 183 24131 18986 20114 -246 ' 2619 -3 C

ATOM 1341 CB SER A 183 44.878 136.633 -34.235 1.00167.67 C

ANISOU 1341 CB SER A 183 24450 18883 20374 -297 2635 19 C

ATOM 1342 OG SER A 183 43.850 135.679 -34.481 1.00162.78 O

ANISOU 1342 OG SER A 183 23927 18171 19752 -249 2594 171 O

ATOM 1343 C SER A 183 45.206 137.077 -31.809 1.00169.74 C

ANISOU 1343 C SER A 183 24456 19549 20490 -292 2612 -104 C

ATOM 1344 O SER A 183 44.067 136.933 -31.380 1.00169.95 O

ANISOU 1344 O SER A 183 24491 19584 20499 -262 2579 -53 O

ATOM 1345 N SER A 184 46.082 137.929 -31.278 1.00156.55 N

ANISOU 1345 N SER A 184 22702 17991 18787 -373 2644 -242 N

ATOM 1346 CA SER A 184 45.760 138.727 -30.081 1.00157.00 C

ANISOU 1346 CA SER A 184 22679 18194 18781 -439 2655 -350 C

ATOM 1347 CB SER A 184 46.686 138.367 -28.915 1.00153.83 C

ANISOU 1347 CB SER A 184 22127 18063 18259 -471 2639 -345 C

ATOM 1348 OG SER A 184 46.503 139.268 -27.832 1.00155.44 O

ANISOU 1348 OG SER A 184 22272 18402 18387 -576 2664 -467 O

ATOM 1349 C SER A 184 45.762 140.252 -30.268 1.00156.19 C

ANISOU 1349 C SER A 184 22618 18006 18722 -542 2711 -518 C

ATOM 1350 O SER A 184 46.787 140.849 -30.584 1.00159.47 O

ANISOU 1350 O SER A 184 23018 18456 19117 -616 2727 -602 O

ATOM 1351 N SER A 185 44.610 140.874 -30.041 1.00158.01 N

ANISOU 1351 N SER A 185 22898 18128 19012 -546 2737 -559 N

ATOM 1352 CA SER A" 185 44.488 142.322 -30.077 1.00159.72 C

ANISOU 1352 CA SER A 185 23146 18262 19278 -637 2799 -720 C

ATOM 1353 CB SER A 185 43.090 142.715 -30.557 1.00156.25 C

ANISOU 1353 CB SER A 185 22775 17627 18964 -605 2831 -696 C

ATOM 1354 OG SER A 185 42.630 143.890 -29.905 1.00155.01 O

ANISOU 1354 OG SER A 185 22623 17434 18841. -672 2909 -854 O

ATOM 1355 C SER A 185 44.785 142.956 -28.707 1.00168.57 C

ANISOU 1355 C SER A 185 24187 19595 20266 -726 2836 -854 C

ATOM 1356 O SER A 185 44.610 142.319 -27.662 1.00168.80 O

ANISOU 1356 O SER A 185 24126 19832 20179 -721 2810 -808 O

ATOM 1357 N VAL A 186 45.256 144.205 -28.735 1.00153.07 N

ANISOU 1357 N VAL A 186 22262 17580 18317 -826 2891 -1012 N

ATOM 1358 CA VAL A 186 45.498 145.023 -27.545 1.00148.21 C

ANISOU 1358 CA VAL A 186 21612 17131 17569 -944 2943 -1153 C

ATOM 1359 CB VAL A 186 46.941 144.880 -27.011 1.00141.92 C

ANISOU 1359 CB VAL A 186 20739 16571 16614 -1026 2900 -1127 C

ATOM 1360 CGl VAL A 186 47.931 144.942 -28.130 1.00144.00 C

ANISOU 1360 CGl VAL A 186 21035 16761 16918 -1036 2858 -1110 C

ATOM 1361 CG2 VAL A 186 47.242 145.976 -26.026 1.00147.79 C

ANISOU 1361 CG2 VAL A 186 21472 17476 17207 -1188 2954 -1259 C

ATOM 1362 C VAL A 186 45.253 146.477 -27.923 1.00151.18 C

ANISOU 1362 C VAL A 186 22079 17339 18024 -1021 3008 -1313 C

ATOM 1363 O VAL A 186 45.817 146.972 -28.896 1.00150.53 O

ANISOU 1363 O VAL A 186 22038 17166 17991 -1059 2976 -1337 O

ATOM 1364 N THR A 187 44.403 147.163 -27.168 1.00161.92 N

ANISOU 1364 N THR A 187 23468 18649 19405 -1042 3100 -1421 N

ATOM 1365 CA THR A 187 44.052 148.543 -27.498 1.00162.24 C

ANISOU 1365 CA THR A 187 23595 18487 19560 -1091 3172 -1560 C

ATOM 1366 CB THR A 187 42.530 148.717 -27.623 1.00159.37 C

ANISOU 1366 CB THR A 187 23256 17920 19376 -992 3240 -1531 C

ATOM 1367 OGl THR A 187 42.002 147.694 -28.483 1.00155.44 O

ANISOU 1367 OGl THR A 187 22733 17370 18958 -875 3163 -1332 O

ATOM 1368 CG2 THR A 187 42.193 150.097 -28.180 1.00160.36 C

ANISOU 1368 CG2 THR A 187 23454 17797 19678 -1028 3291 -1623 C

ATOM 1369 C THR A 187 44.586 149.532 -26.467 1.00164.05 C

ANISOU 1369 C THR A 187 23863 18817 19653 -1237 3252 -1746 C

ATOM 1370 O THR A 187 44.199 149.487 -25.305 1.00169.62 O

ANISOU 1370 O THR A 187 24559 19611 20279 -1267 (3336 -1815 O

ATOM 1371 N VAL A 188 45.483 150.412 -26.901 1.00168.73 . N

ANISOU 1371 N VAL A 188 24504 19401 20203 -1343 3221 -1824 N

ATOM 1372 CA VAL A 188 46.044 151.451 -26.038 1.00176.95 C

ANISOU 1372 CA VAL A 188 25615 20514 21103 -1503 3293 -1997 C

ATOM 1373 CB VAL A 188 47.542 151.166 -25.685 1.00171.95 C

ANISOU 1373 CB VAL A 188 24951 20156 20227 -1642 3221 -1965 C

ATOM 1374 CGl VAL A 188 47.692 149.784 -25.062 1.00159.83 C

ANISOU 1374 CGl VAL A 188 23291 18842 18594 -1601 3181 -1815 C

ATOM 1375 CG2 VAL A 188 48.425 151.281 -26.906 1.00169.65 C

ANISOU 1375 CG2 VAL A 188 24666 19840 19954 -1657 3106 -1914 C ATOM 1376 C VAL A 188 45.852 152.852 -26.661 1.00183.48 C

ANISOU 1376 C VAL A 188 26546 21100 22068 -1541 3332 -2130 C

ATOM 1377 O VAL A 188 45.865 153.003 -27.885 1.00182.81 O

ANISOU 1377 O VAL A 188 26460 20820 22181 -1465 3279 -2072 O

ATOM 1378 N PRO A 189 45.643 153.877 -25.819 1.00194.15 N

ANISOU 1378 N PRO A 189 27990 22456 23321 -1672 3427 -2305 N

ATOM 1379 CA PRO A 189 45.387 155.256 -26.268 1.00197.07 C

ANISOU 1379 CA PRO A 189 28464 22595 23820 -1715 3469 -2441 C

ATOM 1380 CB PRO A 189 45.252 156.017 -24.949 1.00205.29 C

ANISOU 1380 CB PRO A 189 29603 23651 24748 -1818 3637 -2623 C

ATOM 1381 CG PRO A 189 44.766 154.983 -23.977 1.00196.68 C

ANISOU 1381 CG PRO A 189 28435 22761 23533 -1792 3689 -2564 C

ATOM 1382 CD PRO A 189 45.472 153.730 -24.363 1.00189.11 C

ANISOU 1382 CD PRO A 189 27368 22003 22481 -1774 3529 -2385 C

ATOM 1383 C PRO A 189 46.494 155.885 -27.131 1.00195.51 C

ANISOU 1383 C PRO A 189 28308 22421 23555 -1828 3340 -2458 C

ATOM 1384 O PRO A 189 47.668 155.636 -26.881 1.00194.44 O

ANISOU 1384 O PRO A 189 28159 22524 23195 -1927 3262 -2416 O

ATOM 1385 N SER A 190 46.117 156.697 -28.118 1.00203.70 N

ANISOU 1385 N SER A 190 29386 23222 24788 -1821 3311 -2506 N

ATOM 1386 CA SER A 190 47.083 157.373 -28.992 1.00207.06 C

ANISOU 1386 CA SER A 190 29851 23658 25163 -1936 3175 -2533 C

ATOM 1387 CB SER A 190 46.455 158.614 -29.629 1.00209.10 C

ANISOU 1387 CB SER A 190 30178 23634 25638 -1960 3195 -2644 C

ATOM 1388 OG SER A 190 45.801 158.298 -30.846 1.00210.35 O

ANISOU 1388 OG SER A 190 30255 23584 26085 -1853 3151 -2535 O

ATOM 1389 C SER A 190 48.350 157.787 -28.258 1.00205.30 C

ANISOU 1389 C SER A 190 29707 23674 24624 -2109 3164 -2607 C

ATOM 1390 O SER A 190 49.464 157.560 -28.724 1.00200.61 O

ANISOU 1390 O SER A 190 29078 23281 23863 -2176 3035 -2520 O

ATOM 1391 N SER A 191 48.155 158.397 -27.099 1.00179.30 N

ANISOU 1391 N SER A 191 26522 20350 21253 -2188 3311 -2760 N

ATOM 1392 CA SER A 191 49.237 158.952 -26.294 1.00177.73 C

ANISOU 1392 CA SER A 191 26432 20352 20746 -2387 3338 -2842 C

ATOM 1393 CB SER A 191 48.659 159.536 -24.996 1.00178.23 C

ANISOU 1393 CB SER A 191 26577 20356 20785 -2411 3553 -2983 C

ATOM 1394 OG SER A 191 47.258 159.762 -25.092 1.00171.00 O

ANISOU 1394 OG SER A 191 25667 19133 20173 -2267 3656 -3057 O

ATOM 1395 C SER A 191 50.338 157.947 -25.932 1.00175.63 C

ANISOU 1395 C SER A 191 26085 20420 20225 -2460 3240 -2687 C

ATOM 1396 O SER A 191 51.455 158.339 -25.584 1.00168.90 O

ANISOU 1396 O SER A 191 25303 19756 19116 -2646 3185 -2688 O

ATOM 1397 N THR A 192 50.022 156.659 -25.997 1.00186.15 N

ANISOU 1397 N THR A 192 27270 21825 21635 -2316 3217 -2538 N

ATOM 1398 CA THR A 192 50.899 155.641 -25.419 1.00191.89 C

ANISOU 1398 CA THR A 192 27901 22853 22155 -2367 3168 -2388 C

ATOM 1399 CB THR A 192 50.100 154.615 -24.568 1.00190.81 C

ANISOU 1399 CB THR A 192 27674 22755 22070 -2265 3264 -2344 C

ATOM 1400 OGl THR A 192 49.949 153.381 -25.286 1.00182.93 O

ANISOU 1400 OGl THR A 192 26560 21665 21280 -2055 3202 -2213 O

ATOM 1401 CG2 THR A 192 48.731 155.178 -24.185 1.00187.90 C

ANISOU 1401 CG2 THR A 192 27403 22203 21787 -2262 3436 -2525 C

ATOM 1402 C THR A 192 51.724 154.892 -26.461 1.00191.06 C

ANISOU 1402 C THR A 192 27685 22842 22067 -2297 3006 -2212 C

ATOM 1403 O THR A 192 52.591 154.079 -26.115 1.00187.28 O

ANISOU 1403 O THR A 192 27126 22619 21414 -2354 2948 -2070 O

ATOM 1404 N TRP A 193 51.453 155.176 -27.733 1.00192.48 N

ANISOU 1404 N TRP A 193 27856 22813 22465 -2183 2941 -2214 N

ATOM 1405 CA TRP A 193 52.063 154.438 -28.841 1.00190.61 C

ANISOU 1405 CA TRP A 193 27519 22620 22283 -2098 2811 -2062 C

ATOM 1406 CB TRP A 193 51.322 153.108 -29.078 1.00188.53 C

ANISOU 1406 CB TRP A 193 27146 22311 22174 -1910 2838 -1939 C

ATOM 1407 CG TRP A 193 52.008 152.168 -30.028 1.00178.93 C

ANISOU 1407 CG TRP A 193 25833 21162 20991 -1821 2735 -1772 C

ATOM 1408 CDl TRP A 193 52.982 151.252 -29.726 1.00175.66 C

ANISOU 1408 CDl TRP A 193 25321 20989 20433 -1814 2700 -1622 C

ATOM 1409 NEl TRP A 193 53.363 150.574 -30.858 1.00166.60 N

ANISOU 1409 NEl TRP A 193 24113 19806 19380 -1712 2631 -1509 N

ATOM 1410 CE2 TRP A 193 52.634 151.044 -31.920 1.00168.18 C

ANISOU 1410 CE2 TRP A 193 24372 19750 19777 -1674 2610 -1580 C

ATOM 1411 CD2 TRP A 193 51.768 152.049 -31.431 1.00170.76 C

ANISOU 1411 CD2 TRP A 193 24788 19941 20151 -1736 2670 -1736 C

ATOM 1412 CE3 TRP A 193 50.909 152.693 -32.322 1.00165.69 C

ANISOU 1412 CE3 TRP A 193 24200 19032 19723 -1720 2661 -1808 C

ATOM 1413 CZ3 TRP A 193 50.941 152.323 -33.655 1.00166.50 C

ANISOU 1413 CZ3 TRP A 193 24274 19023 19967 -1672 2585 -1728 C

ATOM 1414 CH2 TRP A 193 51.816 151.323 -34.114 1.00165.08 C ANISOU 1414 CH2 TRP A 193 24024 18981 19719 -1618 2535 -1593 C

ATOM 1415 CZ2 TRP A 193 52.666 150.674 -33.265 1.00163.63 C

ANISOU 1415 CZ2 TRP A 193 23779 19049 19345 -1606 2550 -1517 C

ATOM 1416 C TRP A 193 52.048 155.281 -30.110 1.00185.24 C

ANISOU 1416 C TRP A 193 26884 21740 21757 -2101 2723 -2123 C

ATOM 1417 O TRP A 193 51.145 156.100 -30.304 1.00182.53 O

ANISOU 1417 O TRP A 193 26610 21161 21583 -2090 2776 -2244 O

ATOM 1418 N PRO A 194 53.069 155.104 -30.964 1.00196.56 N

ANISOU 1418 N PRO A 194 28272 23272 23141 -2123 2588 -2032 N

ATOM 1419 CA PRO A 194 54.275 154.307 -30.692 1.00195.10 C

ANISOU 1419 CA PRO A 194 28002 23368 22758 -2144 2527 -1877 C

ATOM 1420 CB PRO A 194 54.929 154.193 -32.076 1.00190.73 C

ANISOU 1420 CB PRO A 194 27413 22790 22267 -2132 2390 -1823 ' C

ATOM 1421 CG PRO A 194 54.354 155.331 -32.860 1.00193.30 C

ANISOU 1421 CG PRO A 194 27823 22862 22759 -2177 2357 -1971 C

ATOM 1422 CD PRO A 194 52.936 155.378 -32.404 1.00193.91 C

ANISOU 1422 CD PRO A 194 27929 22744 23005 -2091 2494 -2041 C

ATOM 1423 C PRO A 194 55.256 154.974 -29.725 1.00198.27 C

ANISOU 1423 C PRO A 194 28454 24017 22862 -2331 2519 -1881 C

ATOM 1424 O PRO A 194 56.437 154.630 -29.725 1.00194.83 O

ANISOU 1424 O PRO A 194 27942 23823 22260 -2370 2456 -1729 O

ATOM 1425 N SER A 195 54.775 155.912 -28.9-17 1.00205.80 , N

ANISOU 1425 N SER A 195 29536 24908 23749 -2451 2587 -2037 N

ATOM 1426 CA SER A 195 55.630 156.626 -21.911 1.00209.86 C

ANISOU 1426 CA SER A 195 30137 25637 23963 -2668 2583 -2049 C

ATOM 1427 CB SER A 195 54.839 157.756 -27.314 1.00210.84 C

ANISOU 1427 CB SER A 195 30431 25604 24073 -2775 2690 -2261 C

ATOM 1428 OG SER A 195 53.442 157.515 -27.399 1.00205.85 O

ANISOU 1428 OG SER A 195 29788 24749 23678 -2627 2823 -2351 O

ATOM 1429 C SER A 195 56.269 155.708 -26.929 1.00208.20 C

ANISOU 1429 C SER A 195 29836 25711 23560 -2723 2619 -1887 C

ATOM 1430 O SER A 195 57.460 155.830 -26.634 1.00200.33 O

ANISOU 1430 O SER A 195 28824 24965 22328 -2867 2542 -1759 O

ATOM 1431 N GLU A 196 55.476 154.789 -26.382 1.00192.24 N

ANISOU 1431 N GLU A 196 27747 23656 21640 -2619 2729 -1878 N

ATOM 1432 CA GLU A 196 55.945 153.865 -25.351 1.00187,12 C

ANISOU 1432 CA GLU A 196 26990 23263 20845 -2672 2759 -1723 C

ATOM 1433 CB GLU A 196 55.214 154.120 -24.043 1.00190.39 C

ANISOU 1433 CB GLU A 196 27467 23681 21191 -2774 2898 -1837 C

ATOM 1434 CG GLU A 196 55.542 155.472 -23.439 1.00202.24 C

ANISOU 1434 CG GLU A 196 29146 25232 22463 -3031 2937 -1960 C

ATOM 1435 CD GLU A 196 54.401 156.040 -22.604 1.00221.04 C

ANISOU 1435 CD GLU A 196 31633 27505 24849 -3094 3106 -2147 C

ATOM 1436 OEl GLU A 196 53.268 156.133 -23.129 1.00214.94 O

ANISOU 1436 OEl GLU A 196 30860 26488 24321 -2908 3180 -2261 O

ATOM 1437 0E2 GLU A 196 54.637 156.404 -21.427 1.00237.02 O

ANISOU 1437 0E2 GLU A 196 33742 29690 26626 -3342 3168 -2170 O

ATOM 1438 C GLU A 196 55.812 152.398 -25.767 1.00181.88 C

ANISOU 1438 C GLU A 196 26150 22617 20338 -2464 2733 -1561 C

ATOM 1439 O GLU A 196 54.882 152.024 -26.488 1.00175.52 O

ANISOU 1439 O GLU A 196 25328 21591 19770 -2272 2748 -1605 O

ATOM 1440 N THR A 197 56.743 151.578 -25.279 1.00202.23 N

ANISOU 1440 N THR A 197 28603 25461 22776 -2519 2698 -1360 N

ATOM 1441 CA THR A 197 57.015 150.240 -25.818 1.00199.38 C

ANISOU 1441 CA THR A 197 28071 25156 22528 -2342 2661 -1171 C

ATOM 1442 ' CB THR A 197 58.286 149.636 -25.176 1.00194.79 C

ANISOU 1442 CB THR A 197 27355 24904 21753 -2469 2629 -937 C

ATOM 1443 OGl THR A 197 59.323 150.619 -25.116 1.00194.67 O

ANISOU 1443 OGl THR A 197 27352 25023 21589 -2574 2543 -846 O

ATOM 1444 CG2 THR A 197 58.771 148.453 -25.979 1.00191.92 C

ANISOU 1444 CG2 THR A 197 26813 24584 21524 -2285 2622 -755 C

ATOM 1445 C THR A 197 55.923 149.195 -25.623 1.00196.69 C

ANISOU 1445 C THR A 197 27670 24690 22372 -2168 2726 -1183 C

ATOM 1446 O THR A 197 55.953 148.451 -24.643 1.00199.82 O

ANISOU 1446 O THR A 197 27995 25227 22700 -2225 2768 -1127 O

ATOM 1447 N VAL A 198 54.982 149.101 -26.557 1.00165.20 N

ANISOU 1447 N VAL A 198 23705 20457 18608 -1975 2723 -1236 ' N

ATOM 1448 CA VAL A 198 53.993 148.030 -26.474 1.00160.15 C

ANISOU 1448 CA VAL A 198 23002 19730 18117 -1812 2765 -1198 C

ATOM 1449 CB VAL A 198 52.710 148.338 -27.241 1.00157.86 C

ANISOU 1449 CB VAL A 198 22803 19134 18042 -1678 2796 -1321 C

ATOM 1450 CGl VAL A 198 51.725 147.183 -27.069 1.00150.28 C

ANISOU 1450 CGl VAL A 198 21774 18118 17208 -1510 . 2813 -1229 C

ATOM 1451 CG2 VAL A 198 52.109 149.657 -26.768 1.00158.49 C

ANISOU 1451 CG2 VAL A 198 23003 19109 18108 -1779 2871 -1517 C

ATOM 1452 C VAL A 198 54.565 146.724 -27.002 1.00158.72 C

ANISOU 1452 C VAL A 198 22685 19635 17987 -1679 2717 -993 C ATOM 1453 O VAL A 198 54.451 146.412 -28.188 1.00159.65 O

ANISOU 1453 O VAL A 198 22812 19591 18255 -1530 2693 -965 O

ATOM 1454 N THR A 199 55.190 145.971 -26.107 1.00162 .14 N

ANISOU 1454 N THR A 199 22992 20318 18297 -1747 2708 -844 N

ATOM 1455 CA THR A 199 55.745 144.677 -26.450 1.00162 .61 C

ANISOU 1455 CA THR A 199 22911 20454 18419 -1613 2678 -641 C

ATOM 1456 CB THR A 199 56.881 144.301 -25.483 1.00160 .13 C

ANISOU 1456 CB THR A 199 22446 20454 17943 -1752 2658 -456 C

ATOM 1457 OGl THR A 199 57.573 145.486 -25.089 1.00157. 88 O

ANISOU 1457 OGl THR A 199 22212 20301 17474 -1959 2641 -480 O

ATOM 1458 CG2 THR A 199 57.869 143.370 -26.139 1.00161 43 C

ANISOU 1458 . CG2 THR A 199 22467 20691 18177 -1618 2630 -235 C

ATOM 1459 C THR A 199 54.629 143.635 -26.397 1.00161, 91 C

ANISOU 1459 C THR A 199 22805 20227 18488 -1440 2697 -631 C

ATOM 1460 O THR A 199 53.451 143.973 -26.281 1.00158. 32 O

ANISOU 1460 O THR A 199 22450 19595 18110 -1405 2729 -773 O

ATOM 1461 N CYS A 200 55.005 142.369 -26.494 1.00176. 96 N

ANISOU 1461 N CYS A 200 24584 22212 20439 -1332 2676 -450 N

ATOM 1462 CA CYS A 200 54.050 141.276 -26.455 1.00174. 50 C

ANISOU 1462 CA CYS A 200 24251 21803 20248 -1178 2674 -406 C

ATOM 1463 CB CYS A 200 53.271 141.199 -27.754 1.00173. 39 C

ANISOU 1463 CB CYS A 200 24244 21370 20267 -1024 2685 -477 C

ATOM 1464 SG CYS A 200 53.027 139.501 -28.270 1.00176. 16 S

ANISOU 1464 SG CYS A 200 24559 21623 20752 -807 2668 -310 S

ATOM 1465 . C CYS A 200 54.784 139.965 -26.260 1.00181. 07 C

ANISOU 1465 C CYS A 200 24924 22780 21096 -1103 2646 -185 C

ATOM 1466 O CYS A 200 55.648 139.599 -27.060 1.00179. 71 O

ANISOU 1466 O CYS A 200 24728 22578 20977 -1012 2649 -89 O

ATOM 1467 N ASN A 201 54.432 139.254 -25.199 1.00179. 16 N

ANISOU 1467 N ASN A 201 24565 22695 20811 -1146 2622 -105 N '

ATOM 1468 CA ASN A 201 55.101 138.010 -24.887 1.00175. 88 C

ANISOU 1468 CA ASN A 201 23971 22439 20415 -1101 2589 118 C

ATOM 1469 CB ASN A 201 55.451 137.952 -23.403 1.00179. 17 C

ANISOU 1469 CB ASN A 201 24240 23134 20702 -1305 2556 189 C

ATOM 1470 CG ASN A 201 56.045 139.243 -22.896 1.00180. 19 C

ANISOU 1470 CG ASN A 201 24414 23385 20665 -1542 2583 93 C

ATOM 1471 ODl ASN A 201 57.250 139.343 -22.681 1.00184. 35 O

ANISOU 1471 ODl ASN A 201 24833 24120 21090 -1686 2572 233 O

ATOM 1472 ND2 ASN A 201 55.199 140.244 -22.705 1.00177. 22 N

ANISOU 1472 ND2 ASN A 201 24203 22875 20258 -1589 2621 -134 N

ATOM 1473 C ASN A 201 54.246 136.816 -25.263 1.00170. 49 C

ANISOU 1473 C ASN A 201 23299 21611 19870 -898 2567 177 C

ATOM 1474 O ASN A 201 53.057 136.755 -24.931 1.00165. 75 O

ANISOU 1474 O ASN A 201 22760 20931 19285 -872 2547- 93 O

ATOM 1475 N VAL A 202 54.858 135.870 -25.968 1.00158. 05 N

ANISOU 1475 N VAL A 202 21669 19998 18386 -754 2574 328 N

ATOM 1476 CA VAL A 202 54.185 134.621 -26.274 1.00157. 29 C

ANISOU 1476 CA VAL A 202 21592 19770 18401 -574 2551 404 C

ATOM 1477 CB VAL A 202 54.066 134.355 -27.774 1.001-58. 16 C

ANISOU 1477 CB VAL A 202 21870 19603 18621 -411 2603 365 C

ATOM 1478 CGl VAL A 202 53.204 133.130 -28.013 1.00149. 39 C

ANISOU 1478 CGl VAL A 202 20772 18382 17606 -238 2588 490 C

ATOM 1479 CG2 VAL A 202 53.447 135.548 -28.464 1.00160. 50 C

ANISOU 1479 CG2 VAL A 202 22354 19710 18920 -442 2614 169 C

ATOM 1480 C VAL A 202 54.881 133.456 -25.606 1.00158. 57 C

ANISOU 1480 C VAL A 202 21552 20103 18593 -539 2517 629 C

ATOM 1481 O VAL A 202 56.090 133.477 -25.360 1.00157. 78 O

ANISOU 1481 O VAL A 202 21315 20153 18481 -585 2540 758 O

ATOM 1482 N ALA A 203 54.085 132.435 -25.324 1.00151. 77 N

ANISOU 1482 N ALA A 203 20668 19226 17773 -462 2454 687 N

ATOM 1483 CA ALA A 203 54.506 131.337 -24.484 1.00149. 08 C

ANISOU 1483 CA ALA A 203 20124 19048 17471 -441 2399 899 C

ATOM 1484 CB . ALA A 203 54.006 131.566 -23.075 1.00151. 47 C

ANISOU 1484 CB ALA A 203 20269 19612 17670 -643 2315 919 C

ATOM 1485 C ALA A 203 54.006 129.998 -25.013 1.00143. 91 C

ANISOU 1485 C ALA A 203 19530 18232 16919 -243 2366 978 C

ATOM 1486 O ALA A 203 52.805 129.783 -25.180 1.00137. 71 O

ANISOU 1486 O ALA A 203 18869 17337 16117 -203 2315 896 O

ATOM Ϊ487 N HIS A 204 54.952 129.110 -25.290 1.00167. 51 N

ANISOO 1487 N HIS A 204 22433 , 21203 20009 -122 2401 1148 N

ATOM 1488 CA HIS A 204 54.652 127.722 -25.603 1.00170. 93 C

ANISOU 1488 CA HIS A 204 22885 21524 20538 49 2367 1268 C

ATOM 1489 CB HIS A 204 55.041 127.381 -27.054 1.00169. 20 C

ANISOU 1489 CB HIS A 204 22830 21040 20419 235 2488 1273 C

ATOM 1490 CG HIS A 204 54.264 126.239 -27.647 1.00168. 37 C

ANISOU 1490 CG HIS A 204 22851 20743 20379 401 2466 1339 C

ATOM 1491 NDl HIS A 204 54.828 125.007 -27.901 1.00167. 40 N ANISOU 1491 NDl HIS A 204 22654 20580 20369 542 2506 1513 N

ATOM 1492 CEl HIS A 204 53.916 124.206 -28.422 1.00166 .54 C

ANISOU 1492 CEl HIS A 204 22716 20283 20279 658 2475 1532 C

ATOM 1493 NE2 HIS A 204 52.781 124.874 -28.521 1.00164 28 N

ANISOU 1493 NE2 HIS A 204 22601 19923 19895 596 2414 1393 N

ATOM 1494 CD2 HIS A 204 52.973 126.149 -28.043 1.00165 .24 C

ANISOU 1494 CD2 HIS A 204 22661 20176 19945 445 2414 1266 C

ATOM 1495 C HIS A 204 55.422 126.853 -24.603 1.00175, 35 C

ANISOU 1495 C HIS A 204 23160 22323 21142 4 2311 1491 C

ATOM 1496 O HIS A 204 56.666 126.858 -24.584 1.00172. 96 O

ANISOU 1496 O HIS A 204 22718 22103 20897 4 2384 1617 O

ATOM 1497 N PRO A 205 54.680 126.120 -23.753 1.00173. .12 N

ANISOU 1497 N PRO A 205 22777 22166 20835 -47 21-74 1552 N

ATOM 1498 CA PRO A 205 55.316 125.230 -22.787 1.00169. 88 C

ANISOU 1498 CA PRO A 205 22077 21995 20475 -122 2096 1774 C

ATOM 1499 CB PRO A 205 54.134 124.692 -21.969 1.00175. 00 C

ANISOU 1499 CB PRO A 205 22679 22768 21045 -220 1927 1751 C

ATOM 1500 CG PRO A 205 52.931 125.465 -22.411 1.00170. 88 C

ANISOU 1500 CG PRO A 205 22424 22077 20424 -197 1936 1515 C

ATOM 1501 CD PRO A 205 53.218 125.948 -23.776 1.00166. 78 C

ANISOϋ 1501 CD PRO A 205 22125 21279 19964 -31 2079 1439 C

ATOM 1502 C PRO A 205 55.995 124.085 -23.531 1.00169. 97 C

ANISOU 1502 C PRO A 205 22048 21882 20651 87 2136 1959 C

ATOM- 1503 O PRO A 205 57.200 123.883 -23.371 1.00172. 20 O

ANISOU 1503 O PRO A 205 22109 22293 21027 73 2170 2155 O

ATOM 1504 N ALA A 206 55.222 123.370 -24.351 1.00161. 44 N

ANISOϋ 1504 N ALA A 206 21186 20549 19603 271 2139 1907 N

ATOM 1505 CA ALA A 206 55.688 122.172 -25.044 1.00156. 40 C

ANISOU 1505 CA ALA A 206 20566 19747 19112 480 2191 2057 C

ATOM 1506 CB ALA A 206 54.649 121.705 -26.042 1.00146. 19 C

ANISOU 1506 CB ALA A 206 19588 18161 17798 632 2204 1953 C

ATOM 1507 C ALA A 206 57.040 122.366 -25.721 1.00161. 76 C

ANISOU 1507 C ALA A 206 21184 20376 19901 561 2368 2136 C

ATOM 1508 O ALA A 206 57.868 121.450 -25.716 1.00158. 52 O

ANISOU 1508 O ALA A 206 . 20644 19949 19637 680 2414 2329 O

ATOM 1509 N SER A 207 57.256 123.558 -26.288 1.00169. 29 N

ANISOU 1509 N SER A 207 22230 21307 20785 497 2462 1991 N

ATOM 1510 CA SER A 207 . 58.496 123.898 -27.004 1.00169. 56 c-

ANISOU 1510 CA SER A 207 22239 21296 20891 561 2626 2034 C

ATOM 1511 CB SER A 207 58.219 124.933 -28.097 ' 1.00163. 37 C

ANISOU 1511 CB SER A 207 21698 20357 20020 543 2706 1803 C

ATOM 1512 OG SER A 207 57.034 124.640 -28.806 1.00161. 56 O

ANISOU 1512 OG SER A 207 21749 19843 19795 662 2729 1679 O-

ATOM 1513 C SER A 207 59.558 124.463 -26.068 1.00172. 97 c '

ANISOU 1513 C SER A 207 22377 22028 21315 401 2615 2187 C

ATOM 1514 O SER A 207 60.732 124.602 -26.442 1.00168. 67 O

ANISOU 1514 O SER A 207 21714 2151-1 20861 463 2728 2330 O

ATOM 1515 N SER A 208 59.132 124.773 -24.846 1.00199. 95 N

ANISOU 1515 N SER A 208 25682 25673 24616 184 2481 2165 N

ATOM 1516 CA SER A 208 59.936 125.560 -23.931 1.00204. 29 C

ANISOU 1516 CA SER A 208 26030 26503 25089 -39 2467 2249 C

ATOM 1517 CB SER A 208 6I 1 .119 124.752 -23.383 1.00208. 00 C

ANISOU 1517 CB SER A 208 26185 27156 25689 -50 2475 2572 C

ATOM 1518 OG SER A 208 60.730 123.930 -22.289 1.00196. 51 O

ANISOU 1518 OG SER A 208 24527 25893 24246 -182 2322 2703 O

ATOM 1519 C SER A 208 60.394 126.775 ' -24.720 1.00199. 41 C

ANISOU 1519 C SER A 208 25564 25805 24397 -45 2582 2106 C

ATOM 1520 O SER A 208 61.587 127.065 -24.812 1.00198. 35 O

ANISOU 1520 O SER A 208 25307 25772 24284 -67 2659 2242 O

ATOM 1521 N THR A 209 59.426 127.456 -25.328 1.00177. 92 N

ANISOU 1521 N THR A 209 23106 22900 21595 -25 2586 1845 N

ATOM 1522 CA THR A 209 59.703 128.679 -26.069 1.00180. 98 C

ANISOU 1522 CA THR A 209 23647 23211 21907 -56 2666 1685 C

ATOM 1523 CB THR A 209 59.296 128.598 -27.570 1.00180. 68 C

ANISOU 1523 CB THR A 209 23863 22844 21943 150 2765 1551 C

ATOM 1524 OGl THR A 209 57.898 128.305 -27.685 1.00171. 93 O

ANISOU 1524 OGl THR A 209 22947 -21561 20819 190 2708 1401 O

ATOM 1525 CG2 THR A 209 60.114 127.546 -28.320 1.00177. 74 C

ANISOU 1525 ' CG2 THR A 209 23434 22367 21733 356 2869 1726 C

ATOM 1526 C THR A 209 58.962 129.844 -25.458 1.00174. 40 C

ANISOU 1526 C THR A 209 22903 22449 20911 -254 2595 1487 C

ATOM 1527 O THR A 209 57.815 129.717 -25.044 1.00172. 77 O

ANISOU 1527 O THR A 209 22802 22166 20676 -258 2529 1362 O

ATOM 1528 N LYS A 210 59.639 130.980 -25.394 1.00154. 86 N

ANISOU 1528 N LYS A 210 20386 20126 18327 -421 2611 1469 N

ATOM 1529 CA LYS A 210 58.999 132.239 -25.074 1.00155. 94 C

ANISOU 1529 CA LYS A 210 20636 20301 18313 -602 2573 1264 C ATOM 1530 CB LYS A 210 59.223 132.610 -23.611 1.00162.5t C

ANISOU 1530 CB LYS A 210 21294 21436 19035 -853 2498 1354 C

ATOM 1531 CG LYS A 210 59.225 131.412 -22.668. 1.00172.94 I C

ANISOU 1531 CG LYS A 210 22389 22888 20434 -844 2431 1572 C

ATOM 1532 CD LYS A 210 59.716 131.774 -21.260 1.00176.3C I C

ANISOU 1532 CD LYS A 210 22609 23638 20740 -1141 . 2365 1700 C

ATOM 1533 CE LYS A 210 59.861 130.541 -20.368 1.00171.46 I C

ANISOU 1533 CE LYS A 210 21771 23176 20208 -1175 2271 1900 C

ATOM 1534 NZ LYS A 210 60.207 130.933 -18.979 1.00177.07 N

ANISOU 1534 NZ LYS A 210 22335 24178 20767 -1514 2198 1951 N

ATOM 1535 C LYS A 210 59.635 133.272 -25.996 1.00162.77 C

ANISOU 1535 C LYS A 210 21609 21119 19117 -634 2636 1168 C

ATOM 1536 O LYS A 210 60.862 133.414 -26.032 1.00165.52 O

ANISOU 1536 O LYS A 210 21836 21651 19403 -739 2652 1301 O

ATOM 1537 N VAL A 211 58.803 133.966 -26.765 1.00185.31 N

ANISOU 1537 N VAL A 211 24690 23732 21989 -554 2663 955 N

ATOM 1538 CA VAL A 211 59.280 134.977 -27.698 1.00185.44 C

ANISOU 1538 CA VAL A 211 24819 23680 21959 ' -581 2706 848 C

ATOM 1539 CB VAL A 211 58.805 134.692 -29.118 1.00186.08 C

ANISOU 1539 CB VAL A 211 25074 23469 22160 -394 2763 753 C

ATOM 1540 CGl VAL A 211 59.346 133.350 -29^609 1.00186.02 C

ANISOU 1540 CGl VAL A 211 24994 23394 22293 -197 2817 928 C

ATOM 1541 CG2 VAL A 211 57.293 134.717 -29.157 1.00177.91 C

ANISOU 1541 CG2 VAL A 211 24222 222.38 21138 -387 2734 558 C

ATOM 1542 C VAL A 211 58.702 136.309 -27.279 1.00184.26 C

ANISOU 1542 C VAL A 211 24787 23540 21682 -757 2668 641 C

ATOM 1543 O VAL A 211 57.610 136.365 -26.709 1.00181.35 O

ANISOU 1543 O VAL A 211 24465 23143 21298 -797 2634 542 O

ATOM 1544 N ASP A 212 59.419 137.385 -27.570 1.00185.81 N

ANISOU 1544 N ASP A 212 25038 23773 21790 -857 2677 575 N

ATOM 1545 CA ASP A 212 59.008 138.681 -27.059 1.00188.53 C

ANISOU 1545 CA ASP A 212 25476 24160 21997 -1050 2647 403 C

ATOM 1546 CB ASP A 212 60.092 139.259 -26.141 1.00193.16 C

ANISOU 1546 CB ASP A 212 25934 25047 22410 -1272 2622 531 C

ATOM 1547 CG ASP A 212 60.060 138.647 -24.750 1.00194.81 C

ANISOU 1547 CG ASP A 212 25998 25450 22572 -1390 2594 640 C

ATOM 1548 ODl ASP A 212 61.120 138.200 -24.255 1.00193.34 O

ANISOU 1548 ODl ASP A 212 25621 25500 22338 -1482 2578 877 O

ATOM 1549 0D2 ASP A 212 58.963 138.603 -24.156 1.00190.14 O

ANISOU 1549 0D2 ASP A 212 25475 24775 21994 -1397 2584 498 O

ATOM 1550 C ASP A 212 58.589 139.699 -28.119 1.00189.74 C

ANISOU 1550 C ASP A 212 25825 24113 22156 -1048 2655' 191 C

ATOM 1551 O ASP A 212 58.130 140.779 -27.767 1.00190.91 O

ANISOU 1551 O ASP A 212 26061 24272 22203 -1199 2638 40 O

ATOM 1552 N LYS A 213 58.714 139.350 -29.400 1.00180.46 N

ANISOU 1552 N LYS A 213 24717 22748 21100 -891 2682 178 N

ATOM 1553- CA LYS A 213 58.488 140.314 -30.494 1.00180.61 C

ANISOU 1553 CA LYS A 213 24899 22587 21139 -908 2675 1 C

ATOM 1554 CB LYS A 213 58.051 139.620 -31.792 1.00174.94 C

ANISOU 1554 CB LYS A 213 24270 21613 20585 -734 2712 -19 C

ATOM 1555 CG LYS A 213 59.199 139.463 -32.778 1.00174.70 C

ANISOU 1555 CG LYS A 213 24197 21604 20578 -668 2741 77 C

ATOM 1556 CD LYS A 213 59.063-138.204 -33.601 1.00174.93 C

ANISOU 1556 CD LYS A 213 24302 21404 20760 -501 2800 94 C

ATOM 1557 CE LYS A 213 60.427 137.696 -34.036 1.00178.33 C

ANISOU 1557 CE LYS A 213 24610 21916 21231 -373 2868 285 C

ATOM 1558 NZ LYS A 213 60.330 136.292 -34.506 1.00176.75 N

ANISOU 1558 NZ LYS A 213 24456 21540 21161 -206 2930 346 N

ATOM 1559 C LYS A 213 57.604 141.535 -30.167 1.00177.77 C

ANISOU 1559 C LYS A 213 24668 22148 20728 -1038 2650 -209 C

ATOM 1560 O LYS A 213 56.390 141.421 -29.953 1.00168.83 O

ANISOU 1560 O LYS A 213 23617 20852 19677 -991 2662 -306 O

ATOM 1561 N LYS A 214 58.263 142.696 -30.155 1.00169.67 N

ANISOU 1561 N LYS A 214 23664 21233 19568 -1197 2616 -265 N

ATOM 1562 CA LYS A 214 57.716 143.975 -29.716 1.00162.51 C

ANISOU 1562 CA LYS A 214 22877 20274 18595 -1340 2601 -456 C

ATOM 1563 CB LYS A 214 58.873 144.832 -29.208 1.00160.19 C

ANISOU 1563 CB LYS A 214 22560 20209 18095 -1536 2561 -427 C

ATOM 1564 CG LYS A 214 58.742 146.313 -29.487 1.00161.20 C

ANISOU 1564 CG LYS A 214 22832 20245 18171 -1651 2521 -606 C

ATOM 1565 CD LYS A 214 60.115 146.978 -29.493 1.00167.40 C

ANISOU 1565 CD LYS A 214 23582 21257 18766 -1794 2458 -508 C

ATOM 1566 CE LYS A 214 60.019 148.485 -29.259 1.00171.57 C

ANISOU 1566 CE LYS A 214 24251 21777 19160 -1982 2411 -670 C

ATOM 1567 NZ LYS A 214 61.360 149.144 -29.276 1.00175.60 N

ANISOU 1567 NZ LYS A 214 24733 22536 19451 -2137 2335 -545 N

ATOM 1568 C LYS A 214 • 57.029 144.710 -30.848 1.00158.60 C ANISOU 1568 C LYS A 214 22523 19515 18223 -1297 2588 -615 C

ATOM 1569 O LYS A 214 57.674 145.052 -31.828 1.0016-3.32 O

ANISOU 1569 O LYS A 214 23134 20081 18838 -1284 2555 -603 O

ATOM 1570 N ILE A 215 55.731 144.970 -30.728 1.00176.01 N

ANISOU 1570 N ILE , A 215 24824 21533 20519 -1282 2613 -751 N

ATOM 1571 CA IL'E A 215 55.032 145.632 -31.825 1.00183.03 C

ANISOU 1571 CA ILE A 215 25832 22167 21544 -1262 2597 -875 C

ATOM 1572 CB ILE A 215 53.549 145.886 -31.557 1.00184.79 C

ANISOU 1572 CB ILE A 215 26138 22188 21885 -1232 2637 -982 C

ATOM 1573 CGl ILE A 215 52.715 144.717 -32.076 1.00177.40 C

ANISOU 1573 CGl ILE A 215 25199 21116 21088 -1071 2662 -884 C

ATOM 1574 CDl ILE A 215 53.291 143.366 -31.745 1.00177.42 C

ANISOU 1574 CDl ILE A 215 25089 21294 21030 -987 2676 -727 C

ATOM 1575 CG2 ILE A 215 53.102 147.130 -32.301 1.00182.29 C

ANISOU 1575 CG2 ILE A 215 25932 21671 21660 -1305 2612 -1131 C

ATOM 1576 C ILE A 215 55.689 146.950 -32.157 1.00185.60 C

ANISOU 1576 C ILE A 215 26213 22521 21787 -1409 2540 -979 C

ATOM 1577 O ILE A 215 55.640 147.900 -31.369 1.00182.59 O

ANISOU 1577 O ILE A 215 25884 22179 21314 -1536 2543 -1089 O

ATOM 1578 N VAL A 216 56.300 146.985 -33.339 1.00175.88 N

ANISOϋ 1578 N VAL A 216 24977 21268 20582 -1398 2489 -947 N

ATOM 1579 CA VAL A 216 57.013 148.157 -33.824 1.00174.10 C

ANISOU 1579 CA VAL A 216 24795 21084 20272 -1537 2407 -1028 C

ATOM 1580 CB VAL A 216 58.313 147.759 -34.519 1.00169.69 C

ANISOU 1580 CB VAL A 216 24157 20682 19634 -1528 2358 -902 ' C

ATOM 1581 CGl VAL A 216 59.474 148.538 -33.919 1.00168.69 C

ANISOU 1581 CGl VAL A 216 24011 20806 19276 -1686 2292 -877 C

ATOM 1582 CG2 VAL A 216 58.555 146.279 -34.336 1.00171.27 C

ANISOU 1582 CG2 VAL A 216 24248 20965 19860 -1380 2428 -726 C

ATOM 1583 C VAL A 216 56.087 148.945 -34.748 1.00170.83 C

ANISOU 1583 C VAL A 216 24487 20401 20020 -1566 2377 -1179 C

ATOM 1584 O VAL A 216 55.045 148.434 -35.164 1.00169.70 O

ANISOU 1584 O VAL A 216 24372 20055 20053 -1470 2419 -1178 O

ATOM 1585 N PRO A 217 56.454 150.193 -35.069 1.00145.52 N

ANISOU 1585 N PRO A 217 21341 17195 16754 -1711 2299 -1293 N

ATOM 1586 CA PRO A 217 " 55.351 151.061 -35.463 1.00144.65 C

ANISOU 1586 CA PRO A 217 21321 16830 16809 -1753 2288 -1436 C

ATOM 1587 CB PRO A 217 55.667 152.350 -34.705 1.00143.71 C

ANISOU 1587 CB PRO A 217 21268 16788 16548 -1903 2258 -1556 C

ATOM 1588 CG PRO A 217 57.138 152.186 -34.190 1.00140.68 C

ANISOU 1588 CG PRO A 217 20831 16720 15902 -1971 2220 -1455 C

ATOM 1589 CD PRO A 217 57.679 150.968 -34.837 1.00137.78 C

ANISOU 1589 CD PRO A 217 20359 16439 15554 -1854 2221 -1294 C

ATOM 1590 C PRO A 217 55.305 151.389 -36.940 1.00151.28 C

ANISOU 1590 C PRO A 217 22177 17525 17779 -1793 2199 -1464 C

ATOM 1591 O PRO A 217 55.260 152.568 -37.241 1.00154.98 O

ANISOU 1591 O PRO A 217 22698 17923 18264 -1917 2123 -1578 O

ATOM 1592 N ARG A 218 55.302 150.405 -37.832 1.00189.36 N

ANISOU 1592 N ARG A 218 26962 22297 22691 -1709 2207 -1367 N

ATOM 1593 CA ARG A 218 55.170 150.683 -39.265 1:00194.11 C

ANISOU 1593 CA ARG A 218 27584 22737 23433 -1773 ,2132 -1393 C

ATOM 1594 CB ARG A 218 53.709 151.032 -39.61.9 1.00194.07 •C

ANISOU 1594 CB ARG A 218 27641 22445 23652 -1791 2157 -1447 C

ATOM 1595 CG ARG A 218 53.141 152.262 -38.900 1.00199.43 C

ANISOU 1595 CG ARG A 218 28366 23051 24358 -1879 2139 -1579 C

ATOM •1596 CD ARG A- 218 51.681 152.097 -38.456 1.00196.67 C

ANISOU 1596 CD ARG A 218 28051 22527 24148 -1799 2250 -1582 C

ATOM 1597 NE ARG A 218 51.318 153.046 -37.398 1.00198.99 N

ANISOU 1597 NE ARG A 218 " 28384 22826 24396 -1841 2286 -1701 N

ATOM 1598 CZ ARG A 218 50.630 154.172 -37.588 1.00204.07 C

ANISOU 1598 CZ ARG A 218 29071 23270 25198 -1905 2288 -1792 C

ATOM 1599 NHl ARG A 218 50.207 154.510 -38.799 1.00204.69 N

ANISOU 1599 NHl ARG A 218 29143 -23131 25497 -1953 2241 -1761 N

ATOM 1600 NH2 ARG A 218 50.361 154.966 -36.559 1.00199.61 N

ANISOU 1600 NH2 ARG A 218 28554 22716 24574 -1934 2344 -1907 N

ATOM 1601 C ARG A 218 56.142 151.781 -39.719 1.00197.55 C

ANISOU 1601 C ARG A 218 28015 23274 23772 -1928 1990 -1465 C

ATOM 1602 O ARG A 218 57.235 151.920 -39.160 1.00187.02 O

ANISOU 1602 O ARG A 218 26642 22184 22234 -1952 1950 -1427 O

ATOM 1603 N ASP A 219 55.747 152.550 -40.734 1.00199.47 N

ANISOU 1603 N ASP A 219 28292 233-37 24161 -2045 1904 -1547 N

ATOM 1604 CA ASP A 219 ' 56.551 153.682 -41.211 1.00201.27 C

ANISOU 1604 CA ASP A 219 28523 23638 24314 -2213 1746 -1633 C

ATOM 1605 CB ASP A 219 57.431 153.252 -42.400 1.00195.95 C

ANISOU 1605 CB ASP A 219 27791 23073 23587 -2254 1657 -1575 C

ATOM 1606 CG ASP A 219 58.636 154.169 -42.621 1.00193.63 C

ANISOU 1606 CG ASP A 219 27486 22947 23138 -2412 1481 -1634 C ATOM 1607 ODl ASP A 219 58.598 155.349 -42.207 1.00192.84 O

ANISOU 1607 ODl ASP A 219 27438 22835 22996 -2509 1416 -1732 O

ATOM 1608 0D2 ASP A 219 59.625 153.706 -43.229 1.00186.81 O

ANISOU 1608 0D2 ASP A 219 26565 22227 22186 -2440 1408 - 1578 O

ATOM 1609 C ASP A 219 55.663 154.885 -41.584 1.00210.60 C

ANISOU 1609 C ASP A 219 29749 24576 25692 -2333 1684 - 1743 C

ATOM 1610 O ASP A 219 54.460 154.909 -41.287 1.00207.15 O

ANISOU 1610 O ASP A 219 29340 23928 25440 -2280 1777 -1742 O

ATOM 1611 N CYS A 220 56.264 155.882 -42.228 1.00252.01 N

ANISOU 1611 N CYS A 220 34994 29859 30899 -2497 1522 -1822 N

ATOM 1612 CA CYS A 220 55.530 157.031 -42.733 1.00259.27 C

ANISOU 1612 CA CYS A 220 35935 30557 32018 -2635 1436 - 1914 C

ATOM 1613 CB CYS A 220 54.413 156.576 -43.678 1.00269.58 C

ANISOU 1613 CB CYS A 220 37220 31620 33590 -2636 1479 -1852 C

ATOM 1614 SG ' CYS A 220 54.795 155.067 -44.632 1.00300.38 S

ANISOU 1614 SG CYS A 220 41074 35595 37463 -2601 1491 -1730 S

ATOM 1615 C CYS A 220 54.952 157.824 -41.572 1.00261.33 C

ANISOU 1615 C CYS A 220 36264 30731 32299 -2628 1498 -2010 C

ATOM 1616 O ' CYS A 220 55.457 157.745 -40.453 1.00261.88 O

ANISOU 1616 O CYS A 220 36377 30978 32147 -2609 1522 -2045 O

ATOM 1617 N ASP B 1 25.508 104.634 -8.204 1.00171.79 N

ANISOU 1617 N ASP B 1 23368 20821 21084 -370 224 1182 N

ATOM 1618 .CA ASP B 1 25.603 105.499 -9.367 1.00166.22 C

ANISOU 1618 CA ASP B 1 22569 20039 20547 -270 315 1110 C

ATOM 1619 CB ASP B 1 25.224 104.709 -10.627 1.00171.36 C

ANISOU 1619 CB ASP B 1 23478 20425 21205 -160 211 1203 C

ATOM 1620 CG ASP B 1 26.243 104.861 -11.757 1.00170.92 C

ANISOU 1620 CG ASP B 1 23454 20282 21204 109 243 1195 C

ATOM 1621 ODl ASP B 1 . 26.302 105.949 -12.384 1.00165.40 O

ANISOU 1621 ODl ASP B 1 22559 19629 20657 128 385 1091 O

ATOM 1622 0D2 ASP B 1 26.973 103.874 -12.027 1.00168.03 O

ANISOU 1622 0D2 ASP B 1 23329 19797 20718 308 125 1301 O

ATOM 1623 C ASP B 1 24.658 106.681 -9.162 1.00158.95 C

ANISOU 1623 C ASP B 1 21427 19200 19767 -463 445 994 C

ATOM 1624 O ASP B 1 23.442 106.540 -9.279 1.00158.91 O

ANISOU 1624 O ASP B 1 21462 19126 19789 -610 424 1017 O

ATOM 1625 N ILE B 2 25.216 107.838 -8.826 1.00137.67 N

ANISOU 1625 N ILE B 2 18501 16661 17146 -466 574 871 N

ATOM 1626 CA ILE B 2 24.411 109.040 -8.635 1.00138.01 C

ANISOU 1626 CA ILE B 2 18359 • 16775 17305 -615 702 751 C

ATOM 1627 CB ILE B 2 24.954 109.912 -7.485 1.00139.32 C

ANISOU 1627 CB ILE B 2 18323 17168 17445 -705 781 649 C

ATOM 1628 CGl ILE B 2 24.912 109.136 -6.167 1.00140.33 C

ANISOU 1628 CGl ILE B 2 18494 17412 17414 -816 702 713 C

ATOM 1629 CDl ILE B 2 25.961 109.563 -5.168 1.00132.48 C

ANISOU 1629 CDl ILE B 2 17386 16615 16334 -809 707 659 C

ATOM 1630 CG2 ILE B 2 24.153 111.200 -7.352 1.00132.87 C

ANISOU 1630 CG2 ILE B 2 17346 16400 16737. -815 917 516 C

ATOM 1631 C ILE B 2 24.439 109.806 -9.939 1.00135.71 C

ANISOU 1631 C ILE B 2 18038 16357 17167 -505 790 686 C

ATOM 1632 O ILE B 2 25.330 109.584 -10.749 1.00137.94 O

ANISOU 1632 o- ILE B 2 18365 16577 17469 -326 788 708 O

ATOM 1633 N VAL B 3 23.472 110.693 -10.158 1.00127.62 N

ANISOU 1633 N VAL B 3 16950 15301 16240 -593 868 613 N

ATOM 1634 CA VAL B 3 23.372 111.385 -11.438 1.00123.38 C

ANISOU 1634 CA VAL B 3 16435 14612 15833 -477 937 564 C

ATOM 1635 CB VAL B 3 22.454 110.650 -12.370 1.00124.52 C

ANISOU 1635 CB VAL B 3 16761 14566 15985 -441 835 650 C

ATOM 1636 CGl VAL B 3 22.221 111.494 -13.595 1.00125.30 C

ANISOU 1636 CGl VAL B 3 16844 14552 16214 -376 923 566 C

ATOM 1637 CG2 VAL B 3 23.049 109.315 -12.734 1.00134.88 C

ANISOU 1637 CG2 VAL B 3 18278 15739 17230 -270 712 772 C

ATOM 1638 C VAL B 3 22.805 112.784 -11.363 1.00126.18 C

ANISOU 1638 C VAL B 3 16638 15023 16283 -552 1083 420 C

ATOM 1639 O VAL B 3 21.603 112.958 -11.205 1.00128.99 O

ANISOU 1639 O VAL B 3 16971 15390 16648 -651 1093 398 O

ATOM 1640 N MET B 4 23.666 113.778 -11.530 1.00148.51 N

ANISOU 1640 N MET B 4 19367 17885 19174 -501 1196 328 N

ATOM 1641 CA MET B 4 23.253 115.173 -11.447 1.00149.60 C

ANISOU 1641 CA MET B 4 19391 18065 19384 -564 1337 182 C

ATOM 1642 CB MET B 4 24.369 116.014 -10.830 1.00149.24 C

ANISOU 1642 CB MET B 4 19224 18125 19354 -584 1416 103 C

ATOM 1643 CG MET B 4 25.028 115.375 -9.631 1.00145.90 C

ANISOU 1643 CG MET B 4 18730 17883 18823 -663 1340 139 C

ATOM 1644 SD MET B 4 23.837 115.113 -8.339 1.00149.27 S

ANISOU 1644 SD MET B 4 19125 18448 19142 -832 1299 133 S

ATOM 1645 CE MET B 4 23.091 116.731 -8.308 1.00142.70 C ANISOϋ 1645 CE MET B 4 18217 17624 18379 -893 1451 -34 C

ATOM 1646 C MET B 4 22.877 115.729 -12.820 1.00147.56 C

ANISOU 1646 C MET B 4 19207 17627 19232 -451 1406 140 C

ATOM 1647 O MET B 4 23.628 115.588 -13.788 1.00149.86 O

ANISOU 1647 O MET B 4 19577 17784 19578 -300 1416 174 O

ATOM 1648 N SER B 5 21.724 116.387 -12.886 1.00140.59 N

ANISOU 1648 N SER B 5 18300 16750 18369 -506 1459 64 N

ATOM 1649 CA SER B 5 21.150 116.807 -14.154 1.00145.17 C

ANISOϋ 1649 CA SER B 5 18963 17162 19034 -384 1512 22 C

ATOM 1650 CB SER B 5 20.004 115.865 -14.504 1.00155.42 C

ANISOU 1650 CB SER B 5 20346 18392 20314 -378 1394 105 C

ATOM 1651 OG SER B 5 20.042 114.694 -13.698 1.00155.54 O

ANISOU 1651 OG SER B 5 20452 18369 20276 -371 1251 246 O

ATOM 1652 C SER B 5 20.615 118.229 -14.071 1.00147.59 C

ANISOU 1652 C SER B 5 19213 17488 19376 -395 1660 -132 C

ATOM 1653 O SER B 5 19.663 118.489 -13.341 1.00148.64 O

ANISOU 1653 O SER B 5 19274 17745 19458 -489 1681 -187 O

ATOM 1654 N GLN B 6 21.206 119.146 -14.831 1.00145.82 N

ANISOU 1654 •N GLN B 6 19038 17137 19229 -286 1764 -195 N

ATOM 1655 CA GLN B 6 20.828 120.554 -14.726 1.00145.35 C

ANISOO 1655 CA GLN B 6 18961 17077 19188 -296 1907 -343 C

ATOM 1656 CB GLN B 6 22.044 121.429 -14.466 1.00145.13 C

ANISOU 1656 CB GLN B 6 18900 17046 19197 -326 1997 -392 C

ATOM 1657 CG GLN B 6 22.952 120.923 -13.408 1.00141.59 C

ANISOU 1657 CG GLN B 6 18328 16778 18690 -471 1944 -369 C

ATOM 1658 CD GLN B 6 23.921 121.970 -12.979 1.00139.00 C

ANISOU 1658 CD GLN B 6 17948 16485 18382 -557 2044 -471 C

ATOM 1659 OEl GLN B 6 25.025 121.654 -12.551 1.00135.58 O

ANISOU 1659 OEl GLN B 6 17432 16129 17953 -613 2019 -436 O

ATOM 1660 NE2 GLN B 6 23.519 123.237 -13.093 1.00139.42 N

ANISOU 1660 NE2 GLN B 6 18056 16480 18438 -566 2151 -60! N

ATOM 1661 C GLN B 6 20.114 121.139 -15.926 1.00148.82 C

ANISOU 1661 C GLN B 6 19514 17350 19680 -147 1973 -402 C

ATOM 1662 O GLN B 6 20.422 120.835 -17.085 1.00152.42 O

ANISOU 1662 O GLN B 6 20077- 17637 20197 -2 1958 -347 O

ATOM 1663 N SER B 7 19.183 122.030 -15.617 1.00148.51 N

ANISOU 1663 N SER B 7 19462 17362 19604 -164 2048 -518 N

ATOM 1664 CA SER B 7 18.499 122.831 -16.612 1.00152.02 C

ANISOU 1664 CA SER B 7 20017 17665 20078 -11 2128 -601 C

ATOM 1665 CB SER B 7 17.162 122.192 -16.983 1.00151.98 C

ANISOU 1665 CB SER B 7 20021 17667 20058 53 2031 -555 C

ATOM 1666 OG SER B 7 16.338 122.009 -15.840 1.00157.75 O

ANISOU 1666 OG SER B 7 20640 18596 20700 -39 2024 -595 , O

ATOM 1667 C SER B 7 18.285 124.200 -15.992 1.00152.99 C

ANISOU 1667 C SER B 7 20140 17847 20144 -41 2251 -752 C

ATOM 1668 O SER B 7 18.240 124.320 -14.772 1.00156.04 O

ANISOU 1668 O SER B 7 20426 18408 20453 -176 2244 -779 O

ATOM 1669 N PRO B 8 18.172 125.236 -16.826 1.00165.44 N

ANISOU 1669 N PRO B 8 21851 19266 21743 97 2364 -850 • N

ATOM 1670 CA PRO B 8 18.2 " 33 125.090 -18.272 1.00169.25 C

ANISOU 1670 CA PRO B 8 22459 19541 22309 271 2367 -808 C

ATOM 1671 CB PRO B 8 17.672 126.422 -18.774 1.00171.19 C

ANISOU 1671 CB PRO B 8 22843 19677 22526 422 2484 -944 C

ATOM 1672 CG PRO B 8 17.273 127.208 -17.544 1.00171.36 C

ANISOU 1672 CG PRO B 8 22814 19855 22439 325 2541 -1056 C

ATOM 1673 CD PRO B 8 18.071 126.646 -16.439 1.00166.61 C

ANISOU 1673 CD PRO B 8 22074 19401 21830 113 2492 -1002 C

ATOM 1 ' 674 C PRO B 8 19.684 124.961 -18.692 1.00172.07 C

ANISOU 1674 C PRO B 8 22852 19784 22744 262 2415 -757 C

ATOM 1675 O PRO B 8 20.554 125.454 -17.979 1.00171.05 O

ANISOU 1675 O PRO B 8 22673 19712 22607 130 2479 -799 O

ATOM 1676 N SER B 9 19.938 124.309 -19.821 1.00162.30 N

ANISOU 1676 N SER B 9 21696 18397 21573 402 2381 -667 N

ATOM 1677 CA SER B 9 21.290 124.193 -20.360 1.00163.32 C

ANISOU 1677 CA SER B 9 21859 18425 '21772 436 2438 -603 C

ATOM 1678 CB SER B 9 21.248 123.520 -21.739 1.00170.53 C

ANISOU 1678 CB SER B 9 22920 19140 22735 664 2416 -531 C

ATOM 1679 OG SER B 9 20.143 123.972 -22.511 1.00167.09 O

ANISOU 1679 OG SER B 9 22593 18613 22281 797 2415 -606 O

ATOM 1680 C SER B 9 22.037 125.538 -20.445 1.00161.36 C

ANISOU 1680 C SER B 9 21645 18120 21543 380 2607 -699 C

ATOM 1681 O SER B 9 23.266 125.565 -20.564 1.00154.10 O

ANISOU 1681 O SER B 9 20670 17213 20667 311 2651 -649 O

ATOM 1682 N SER B 10 21.288 126.640 -20.377 1.00148.58 N

ANISOU 1682 N SER B 10 20123 16447 19885 410 2697 -834 N

ATOM 1683 CA SER B 10 21.837 127.991 -20.523 1.00143.34 C

ANISOU 1683 CA SER B 10 19556 15680 19225 373 2857 -936 C ATOM 1684 CB SER B 10 22.603 128.087 -21.825 1.00145.99 C

ANISOU 1684 CB SER B 10 20012 15814 19644 510 2954 -881 C

ATOM 1685 OG SER B 10 21.707 127.961 -22.912 1.00148.70 O

ANISOU 1685 OG SER B 10 20494 16018 19989 748 2934 -874 O

ATOM 1686 C SER B 10 20.724 129.039 -20.549 1.00146.26 C

ANISOO 1686 C SER B 10 20061 15998 19514 452 2922 -1083 C

ATOM 1687 O SER B 10 19.554 128.700 -20.666 1.00147.48 O

ANISOU 1687 O SER B 10 20212 16203 19621 554 2849 -1098 O

ATOM 1688 N LEU B 11 21.075 130.315 -20.456 1.00160.26 N

ANISOU 1688 N LEU B 11 21958 17671 21262 408 3057 -1190 N

ATOM 1689 CA LEU B 11 20.053 131.355 -20.499 1.00165.61 C

ANISOU 1689 CA LEU B 11 22797 18293 21835 500 3127 -1340 C

ATOM 1690 CB LEU B 11 19.155 131.278 -19.261 1.00165.91 C

ANISOU 1690 CB LEU B 11 22713 18560 21766 407 3041 -1391 C

ATOM ' 1691 CG LEU B 11 19.823 130.904 -17.934 1.00164.78 C

ANISOU 1691 CG LEU B ' 11 22387 18592 21631 154 2975 -1346 C

ATOM 1692 CDl LEU B 11 20.907 131.899 -17.541 1.00160.86 C

ANISOU 1692 CDl LEU B 11 21976 18023 21120 -3 3069 -1429 C

ATOM 1693 CD2 LEU B 11 18.779 130.773 -16.837 1.00162.27 C

ANISOU 1693 CD2 LEU B 11 21930 18510 21214 102 2872 -1355 C

ATOM 1694 C LEU B 11 20.657 132.741 -20.629 1100168.55 C

ANISOU 1694 C LEU B 11 23361 18496 22186 450 3282 -1442 C

ATOM 1695 O LEU B 11 -. 21.849 132.918 -20.409 1.00166.40 O

ANISOU 1695 O LEU B 11 23039 18210 21974 271 3320 -1405 O

ATOM 1696. N VAL B 12 19.828 133.719 -20.982 1.00172.94 N

ANISOU 1696 N VAL B 12 24136 18926 22648 608 3366 -1567 N

ATOM 1697 CA VAL B 12 20.281 135.096 -21.150 1.00173.25 C

ANISOU 1697 CA VAL B 12 24413 18774 22640 574 3513 -1673 C

ATOM 1698 CB VAL B 12 20.104 135.558 -22.600 1.00175.92 C

ANISOU 1698 CB VAL B 12 24996 18851 22993 809 3633 -1694 C

ATOM 1699 CGl VAL B 12 20.335 134.391 -23.540 1.00178.25 C

ANISOU 1699 CGl VAL B 12 25196 19097 23433 873 3616 -1542 C

ATOM 1700 CG2 VAL B 12 18.713 136.128 -22.816 1.00178.62 C

ANISOU 1700 CG2 VAL B 12 25462 19189 23217 1077 3618 -1791 C

ATOM 1701 C VAL B 12 19.506 136.027 -20.232, 1.00171.96 C

ANISOU 1701 C VAL B 12 24366 18662 22309 568 3523 -1826 C

ATOM 1702 O VAL B 12 18.320 135.818 -20.004 1.00177.83 O

ANISOU 1702 O VAL B 12 25117 19497 22954 740 3481 -1879 O

ATOM 1703 N VAL B 13 20.172 137.049 -19.703 1.00155.29 N

ANISOU 1703 N VAL B 13 22354 16494 20157 376 3578 -1895 N

ATOM 1704 CA VAL B 13 19.530 137.998 -18.788 1.00162.06 C

ANISOU 1704 CA VAL B 13 23332 17405 20838 358 3573 -2035 C

ATOM 1705 CB VAL B 13 19.452 137.436 -17.380 1.00162.00 C

ANISOU 1705 CB VAL B 13 23068 17674 20809 190 3440 -2001 C

ATOM 1706 CGl VAL B 13 20.762 136.751 -17.018 1.00152.88 C

ANISOU 1706 CGl VAL B 13 21685 16585 19816 -44 3387 -1872 C

ATOM 1707 CG2 VAL B 13 19.156 138.560 -16.406 1.00168.92 C

ANISOU 1707 CG2 VAL B 13 24096 18567 21518 103 3445 -2139 C

ATOM 1708 C VAL B 13 20.351 139.260 -18.649 1.00170.07 C

ANISOU 1708 C VAL B 13 24588 18229 21801 200 3666 -2128 C

ATOM 1709 O VAL B 13 21.574 139.182 -18.614 1.00174.10 O

ANISOU 1709 O VAL B 13 25000 18746 22405 -63 3655 -2077 O

ATOM 1710 N SER B 14 19.711 140.421 -18.536 1.00166.83 N

ANISOU 1710 N SER B 14 24497 17659 21232 351 3750 -2267 N

ATOM 1711 CA SER B 14 20.496 141.646 -18.399 1.00168.59 C

ANISOU 1711 CA SER B 14 24999 17668 21390 193 3834 -2361 C

ATOM 1712 CB SER B 14 19.844' 142.833 -19.113 1.00173.51 C

ANISOU 1712 CB SER B 14 26024 18052 21849 442 3950 -2492 C

ATOM 1713 OG SER B 14 18.583 142.477 -19.648 1.00176.27 O

ANISOU 1713 OG SER B 14 26346 18510 22120 767 3927 -2515 O

ATOM 1714 C SER B 14 20.829 141.969 -16.955 1.00166.12 C

ANISOU 1714 C SER B 14 24641 17484 20992 -42 3743 -2420 C

ATOM 1715 O SER B 14 20.108 141.573 -16.043 1.00165.03 O

ANISOU 1715 O • SER B 14 24393 17561 20749 27 3651 -2451 O

ATOM 1716 N VAL B 15 21.944 142. ' 676 -16.772 1.00172.73 N

ANISOU 1716 N VAL B 15 25559 18192 21877 -325 3769 -2428 N

ATOM 1717 CA VAL B 15 22.466 143.018 -15.449 1.00175.97 C

ANISOU 1717 CA VAL B 15 25922 18708 22229 -585 3669 -2478 C

ATOM 1718 CB VAL B 15 23.620 144.043 -15.535 1.00169.63 C

ANISOU 1718 CB VAL B 15 25283 17696 21472 -894 3718 -2502 C

ATOM 1719 CGl VAL B 15 24.141 144.386 -14.146 1.00162.08 C

ANISOU 1719 CGl VAL B 15 24331 16827 20425 -1143 3597 -2580 C

ATOM 1720 CG2 VAL B 15 24.736 143.504 -16.397 1.00166.35 C

ANISOU 1720 CG2 VAL B 15 24613 17299 21294 -1061 3752 -2344 C

ATOM 1721 C VAL B 15 21.376 143.570 -14.544 1.00176.17 C

ANISOU 1721 C VAL B 15 26140 18786 22012 -424 3627 -2619 C

ATOM 1722 O VAL B 15 20.697 144.529 -14.888 1.00174.83 O ANISOU 1722 O VAL B 15 26295 18444 21690 -203 3711 -2723 O

ATOM 1723 N GLY B 16 21.210 142.963 -13.381 1.00185.10 N

ANISOU 1723 N GLY B 16 27072 20163 23094 -513 3499 -2618 N

ATOM 1724 CA GLY B 16 20.132 143.357 -12.505 1.00185.65 C

ANISOU 1724 CA GLY B 16 27254 20349 22937 -323 3457 -2722 C

ATOM 1725 C GLY B 16 19.117 142.245 -12.357 1.00190.00 C

ANISOU 1725 C GLY B 16 27501 21185 23507 -136 3404 -2636 C

ATOM 1726 O GLY B 16 18.888 141.778 -11.249 1.00189.72 O

ANISOU 1726 O GLY B 16 27234 21392 23459 -225 3298 -2596 O

ATOM 1727 N GLU B 17 18.516 141.811 -13.462 1.00203.96 N

ANISOU 1727 N GLU B 17 29274 22918 25302 115 3474 , -2606 N

ATOM 1728 CA GLU B 17 17.463 140.794 -13.408 1.00204.12 C

ANISOU 1728 CA GLU B 17 29031 23191 25336 297 3425 -2527 C

ATOM 1729 CB GLU B 17 17.092 140.328 -14.813 1.00203.84 C

ANISOQ 1729 CB GLQ B 17 28982 23051 25418 476 3490 -2465 C

ATOM 1730 CG GLU B 17 16.230 141.300 -15.586 1.00215.57 C

ANISOU 1730 CG GLU B 17 30766 24396 26743 787 3587 -2581 C

ATOM 1731 CD GLU B 17 15.854 140.769 -16.954 1.00222.52 C

ANISOU 1731 CD GLU B 17 31619 25193 27735 982 3632 -2520 C

ATOM 1732 OEl GLU B 17 16.637 139.979 -17.531 1.00213.02 O

ANISOU 1732 OEl GLU B 17 30210 23991 26737 864 3601 -2390 O

ATOM 1733 0E2 GLU B 17 14.772 141.149 -17.450 1.00228.56 O

ANISOU 1733 0E2 GLU B 17 32582 25890 28370 1271 3694 -2607 O

ATOM 1734 C GLU B 17 ' 17.852 139.595 -12.539 1.00202.27 C

ANISOU 1734 C GLU B 17 28425 23217 25210 105 3302 -2403 C

ATOM 1735 O GLU B 17 19.017 139.442 -12.179 1.00199.56 O

ANISOU 1735 O GLU B 17 27983 22851 24989 -154 3261 -2352 O

ATOM 1736 N LYS B 18 16.880 138.749 -12.198 1.00187.45 N

ANISOU 1-736 N LYS B 18 26342 21594 23285 233 3244 -2352 N

ATOM 1737 CA LYS B 18 17.166 137.596 -11.345 1.00183.05 C

ANISOU 1737 CA LYS B 18 25461 21282 22807 69 3130 -2234 C

ATOM 1738 CB LYS B 18 16.374 137.658 -10.037 1.00182.93 C

ANISOU 1738 CB LYS B 18 25390 21511 22603 116 3079 -2273 C

ATOM 1739 CG LYS B 18 14.910 137.348 -10.174 1.00187.34 C

ANISOU 1739 CG LYS B 18 25833 22268 23078 349 3083 -2241 C

ATOM 1740 CD LYS B 18 14.376 136.776 -8.870 1.00187.78 C

ANISOU 1740 CD LYS B 18 25664 22630 23053 289 3002 -2178 C

ATOM 1741 CE LYS B 18 13.126 135.948 -9.120 1.00189.75 C

ANISOU 1741 CE LYS B 18 25738 23100 23257 471 2999 -2111 C

ATOM 1742 NZ LYS B 18 13.302 135.022 -10.284 1.00190.81 N

ANISOU 1742 NZ LYS B 18 25781 23148 23572 508 2993 -2024 N

ATOM 1743 C LYS B 18 17.011 136.230 -12.039 1.00182.03 C

ANISOU 1743 C LYS B 18 25074 21240 22848 92 3085 -2079 C

ATOM 1744 O LYS B 18 16.090 135.999 -12.829 1.00178.50 O

ANISOU 1744 O LYS B 18 24625 20797 22401 298 3112 -2062 O

ATOM 1745 N VAL B 19 17.931 135.330 -11.714 1.00161.50 N

ANISOU 1745 N VAL B 19 22269 18712 20380 -118 3006 -1971 N

ATOM 1746 CA VAL B 19 18.099 134.083 -12.432 1.00150.77 C

ANISOU 1746 CA VAL B 19 20715 17384 19187 -128 2956 -1823 C

ATOM 1747 CB VAL B 19 19.516 133.993 -12.949 1.00147.32 C

ANISOU 1747 CB VAL B 19 20274 16797 18905 -284 2971 -1772 C

ATOM 1748 CGl VAL B 19 19.688 132.750 -13.787 1.00152.64 C

ANISOU 1748 CGl VAL B 19 20787 17484 19727 -252 2922 -1622 C

ATOM 1749 CG2 VAL B 19 19.845 135.217 -13.752 1.00155.53 C

ANISOU 1749 CG2 VAL B 19 21578 17573 19945 -232 3095 -1868 C

ATOM 1750 C VAL B 19 17.935 132.906 -11.504 1.00152.67 C

ANISOU 1750 C VAL B 19 20698 17880 19428 -231 2838 -1718 C

ATOM 1751 O VAL B 19 18.240 133.015 -10.318 1.00151.17 O

ANISOU 1751 O VAL B 19 20456 17800 19181 -384 2790 -1738 O

ATOM 1752 N THR B 20 17.486 131.774 -12.052 1.00155.92 N

ANISOU 1752 N THR B 20 20966 18374 19901 -153 2785 -1605 N

ATOM 1753 CA THR B 20 17.334 130.528 -11.293 1.00151.13 C

ANISOU 1753 CA THR B 20 20131 17988 19304 -254 2671 -1483 C

ATOM 1754 CB THR B 20 15.898 130.351 -10.794 1.00158.58 C

ANISOU 1754 CB THR B 20 20998 19141 20116 -157 2653 -1483 C

ATOM 1755 OGl THR B 20 15.659 131.219 -9.679 1.00168.74 . O

ANISOU 1755 OGl THR B 20 22396 20482 21235 -114 2714 -1615 O

ATOM 1756 CG2 THR B 20 15.668 128.910 -10.373 1.00154.53 C

ANISOU 1756 CG2 THR B 20 20268 18839 19606 -285 2543 -1350 C

ATOM 1757 C THR B 20 17.628 129.297 -12.129 1.00137.88 C

ANISOU 1757 C THR B 20 18348 16266 17773 -256 2604 -1338 C

ATOM 1758 O THR B 20 17.039 129.122 -13.185 1.00140.73 O

ANISOU 1758 O THR B 20 18775 16506 18191 -110 2629 -1324 O

ATOM 1759 N MET B 21 18.512 128.431 -11.643 1.00137.69 N

ANISOU 1759 N MET B 21 18179 16342 17796 -402 2510 -1232 N

ATOM 1760 CA MET B 21 18.822 127.170 -12.329 1.00142.84 C

ANISOU 1760 CA MET B 21 18760 16946 18566 -397 2435 -1091 C ATOM 1761 CB MET B 21 20.299 127.129 -12.727 1.00145.04 C

ANISOU 1761 CB MET B 21 19065 17096 18949 -461 2458 -1072 C

ATOM 1762 CG MET B 21 21.230 127.703 -11.671 1.00145.29 C

ANISOU 1762 CG MET B 21 19066 17200 18938 -630 2468 -1139 C

ATOM 1763 SD MET B 21 22.639 128.637 -12.333 1.00142.63 S

ANISOU 1763 SD MET B 21 18773 16708 18713 -712 2536 -1156 S

ATOM 1764 CE MET B 21 21.787 129.813 -13.387 1.00141.12 C

ANISOU 1764 CE MET B 21 18814 16274 18530 -563 2685 -1266 C

ATOM 1765 C MET B 21 18.471 125.962 -11.462 1.00146.39 C

ANISOU 1765 C MET B 21 19048 17589 18984 -493 2311 -969 C

ATOM 1766 O MET B 21 18.329 126.098 -10.257 1.00150.61 O

ANISOU 1766 O MET B 21 19508 18280 19437 -610 2283 -982 O

ATOM 1767 N SER B 22 18.323 124.783 -12.054 1.00170.89 N

ANISOU 1767 N SER B 22 22117 20670 22142 -444 2233 -850 N

ATOM 1768 CA SER B 22 17.968 123.616 -11.254 1.00171.51 C

ANISOU 1768 CA SER B 22 22076 20910 22181 -543 2114 -728 C

ATOM 1769 CB SER B 22 16.651 123.012 -11.727 1.00174.57 C

ANISOU 1769 CB SER B 22 22446 ' 21313 22568 -477 2057 -657 C

ATOM 1770 OG SER B 22 16.888 121.935 -12.614 1.00174.52 O

ANISOU 1770 OG SER B 22 22480 21181 22649 -444 1964 -539 O

ATOM 1771 C SER B 22 19.072 122.562 -11.276 1.00169.56 C

ANISOU 1771 C SER B 22 21799 20637 21990 -611 2029 -618 C

ATOM 1772 O SER B 22 19.911 122.556 -12.182 1.00169.88 O

ANISOU 1772 O SER B 22 21901 20526 22118 -553 2055 -611 O

ATOM 1773 N CYS B 23 19.060 121.680 -10.273 1.00136.14 N

ANISOU 1773 N CYS B 23 17476 16561 17691 -722 1935 -530 N

ATOM 1774 CA CYS B 23 20.074 120.636 -10.119 1.00134.07 C

ANISOU 1774 CA CYS B 23 17191 16305 17446 -771 1840 -421 C

ATOM 1775 CB CYS B 23 21.190 121.077 -9.174 1.00133.45 C

ANISOU 1775 CB CYS B 23 17050 16322 17332 -867 1856 -478 C

ATOM 1776 SG CYS B 23 22.576 119.901 -9.043 1.00146.13 S

ANISOU 1776 SG CYS B 23 18618 17958 18946 -891 1746 -356 S

ATOM 1777 C CYS B 23 19.481 119.343 -9.598 1.00136.05 C

ANISOU 1777 C CYS B 23 17408 16653 17632 -835 1719 -287 C

ATOM 1778 O CYS B 23 19.888 118.837 -8.558 1.00135.53 O

ANISOU 1778 O CYS B 23 17294 16700 17501 -923 1655 -234 O

ATOM 1779 N LYS B 24 18.534 118.802 -10.345 1.00143.06 N

ANISOU 1779 N LYS B 24 18331 17490 18536 -793 ' 1681 -232 N

ATOM 1780 CA LYS B 24 17.858 117.576 -9.959 1.00148.34 C

ANISOU 1780 CA LYS B 24 18987 18225 19149 -874 1562 -95 C

ATOM 1781 CB LYS B 24 16.714 117.314 -10.938 1.00156.30 C

ANISOU 1781 CB LYS B 24 20036 19151 20201 -820 1531 -63 C

ATOM 1782 CG LYS B 24 15.747 118.498 -11.088 1.00156.26 C

ANISOU 1782 CG LYS B 24 19982 19190 20199 -758 1647 -190 C

ATOM 1783 CD LYS B 24 14.377 118.021 -11.582 1.00169.27 C

ANISOU 1783 CD LYS B 24 21601 20871 21844 -764 1591 -137 C

ATOM 1784 CE LYS B 24 13.850 116.854 -10.724 1.00180.99 C

ANISOU 1784 CE LYS B 24 23013 22503 23251 -941 1488 3 C

ATOM 1785 NZ LYS B 24 12.667 116.129 -11.295 1.00179.69 N

ANISOU 1785 NZ LYS B 24 22808 22376 23089 -989 1410 79 N

ATOM 1786 C LYS B 24 18.788 116.354 -9.842 1.00143.32 C

ANISOU 1786 C LYS B 24 18415 17539 18500 -890 1442 32 C

ATOM 1787 O LYS B 24 19.494 116.004 -10.779 1.00140.90 O

ANISOU 1787 O LYS B 24 18206 17068 18261 -779 1408 70 O

ATOM 1788 N SER B 25 18.761 115.701 -8.685 1.00127.37 N

ANISOU 1788 N SER B 25 16354 15663 16379 -1008 1380 101 N

ATOM 1789 CA SER B 25 19.673 114.598 -8.388 1.00128.39 C

ANISOU 1789 CA SER B 25 16558 15760 16465 -1008 1265 216 C

ATOM 1790 CB SER B 25 20.440 114.894 -7.101 1.00128.05 C

ANISOU 1790 CB SER B 25 16441 15860 16352 -1053 1283 176 C

ATOM 1791 OG SER B 25 21.067 113.726 -6.592 1.00130.22 O

ANISOU 1791 OG SER B 25 16716 16259 16503 -1160 1206 264 O

ATOM 1792 C SER B 25 18.997 113.231 -8.260 1.00127.53 C

ANISOU 1792 C SER B 25 16522 15651 16284 -1095 1140. 364 C

ATOM 1793 O SER B 25 18.023 113.084 -7.534 1.00125.27 O

ANISOU 1793 O SER B 25 16168 15482 15946 -1216 1149 384 O

ATOM 1794 N SER B 26 19.558 112.226 -8.929 1.00137.86 N

ANISOU 1794 N SER B 26 17974 16828 17577 -1032 1024 473 N

ATOM 1795 CA SER B 26 18.958 110.893 -9.010 1.00137.58 C

ANISOU 1795 CA SER B 26 ' 18066 16723 17484 -1103 887 618 C

ATOM 1796 CB SER B 26 19.720 110.020 -10.015 1.00142.88 C

ANISOU 1796 CB SER B 26 18942 17190 18156 -960 769 709 C

ATOM 1797 OG SER B 26 21.011 109.658 -9.551 1.00143.06 O

ANISOU 1797 OG SER B 26 19005 17260 18093 -900 734 743 O

ATOM 1798 C SER B 26 18.851 110.162 -7.678 1.00141.54 C

ANISOU 1798 C SER B 26 18549 17379 17851 -1261 843 695 C

ATOM 1799 O SER B 26 18.192 109.129 -7.588 1.00148.24 O ANISOU 1799 O SER B 26 19468 18210 18647 -1382 757 807 O

ATOM 1800 N GLN B 27 19.514 ' 110.688 -6.656 1.00150 .74 N

ANiSOU 1800 N GLN B 27 19629 18690 18957 -1265 898 638 N

ATOM 1801 CA GLN B 27 19.444 110.123 -5.311 1.00153 .41 C

ANISOU 1801 CA GLN B 27 19944 19188 19157 -1397 875 695 C

ATOM 1802 CB GLN B 27 20.617 109.188 -5.046 1.00151 34 C

ANISOU 1802 CB GLN B 27 19813 18899 18791 -1336 772 773 C

ATOM 1803 CG GLN B 27 20.417 107.777 -5.512 1.00154 00 C

ANISOϋ 1803 CG GLN B 27 20372 19060 19082 -1321 627 922 C

ATOM 1804 CD GLN B 27 21.549 106.891 -5.063 1.00165. 33 C

ANISOU 1804 CD GLN B 27 21945 20487 20387 -1230 532 990 C

ATOM 1805 OEl GLN B 27 22.479 107.344 -4.392 1.00163. 04 O

ANISOU 1805 OEl GLN B 27 21560 20352 20037 -1208 572 929 O

ATOM 1806 NE2 GLN B 27 21.481 105.618 -5.425 1.00179, 50 N

ANISOU 1806 NE2 GLN B 27 23977 22100 22126 -1165 397 1112 N

ATOM 1807 C GLN B 27 19.459 111.241 -4.283 1.00155. 49 C

ANISOU 1807 C GLN B 27 20028 19647 19404 -1434 1002 566 C

ATOM 1808 O GLN B 27 20.016 112.311 -4.527 1.00158. 51 O

ANISOU 1808 O GLN B 27 20336 20028 19862. -1347 1081 439 O

ATOM 1809 N SER B 28 18.854 110.996 -3.128 1.00147. 64 N

ANISOU 1809 N SER B 28 18978 18816 18301 -1563 1021 601 N

ATOM 1810 CA SER B 28 18.787 112.017 -2.096 1.00147. 14 C

ANISOU 1810 CA SER B 28 18774 18940 18194 -1586 1130 485 C

ATOM 1811 CB SER B 28 17.806 111.622 -1.009 1.00155. 36 C

ANISOU 1811 CB SER B 28 19769 20151 19109 -1722 1152 .559 C

ATOM 1812 OG SER B 28 18.202 112.195 0.223 1.00156. 53 O

ANISOU 1812 OG SER B 28 19851 20463 19159 -1720 1205 479 O

ATOM 1813 C SER B 28 20.135 112.250 -1.466 1.00147. 10 C

ANISOU 1813 C SER B 28 18765 18984 ' 18143 -1522 1115 417 C

ATOM 1814 O SER B 28 20.817 111.311 -1.057 1.00144. 27 O

ANISOU 1814 O SER B 28 18492 18633 17691 -1518 1022 499 O

ATOM 1815 N LEU B 29 20.514 113.512 -1.369 1.00138. 54 N

ANISOU 1815 N LEU B 29 17584 17941 17113 -1476 1202 265 N

ATOM 1816 CA LEU B 29 21.796 113.840 -0.788 1.00140. 91 C

ANISOU 1816 CA LEU B 29 17854 18308 17378 -1438 1185 186 C

ATOM 1817 CB LEU B 29 22.508 114.902 -1.634 1.00139. 01 C

ANISOU 1817 CB LEU B 29 17563 17984 17271 -1366 1246 58 C

ATOM 1818 CG LEU B 29 22.381 114.862 -3.158 1.00130. 68 C

ANISOU 1818 CG LEU B 29 16564 16737 16350 -1283 1249 93 C

ATOM 1819' CDl LEU B 29 23.379 115.817 -3.763 1.00128. 74 C

ANISOU 1819 CDl LEU B 29 16268 16427 16221 -1229 1334 -39 C

ATOM 1820 CD2 LEU B 29 22.617 113.480 -3.686 1.00129. 53 C

ANISOU 1820 CD2 LEU B 29 16517 16512 16185 -1213 1134 219 C

ATOM 1821 C LEU B 29 21.611 114.316 0.653 1.00139. 22 C

ANISOU 1821 C LEU B 29 ' l7578 18285 17035 -1505 1220 129 C

ATOM 1822 O LEU B 29 22.323 115.188 1.135 1.00137. 13 O

ANISOU 1822 O LEU B 29 17261 18092 16751 -1489 1230 16 O

ATOM 1823 N LEU B 30 20.650 113.741 1.351 1.00150. 48 N

ANISOU 1823 N LEU B 30 19010 19798 18367 -1581 1236 210 N

ATOM 1824 CA LEU B 30 20.368 114.207 2.693 1.00150. 16 C

ANISOU 1824 CA LEU B 30 'l8921 19942 18190 -1624 1281 165 C

ATOM 1825 CB LEU B 30 18.866 114.286 2.915 1.00152. 58 C

ANISOU 1825 CB LEU B 30 19177 20342 18455 -1683 1371 205 C

ATOM 1826 CG LEU B 30 18.439 115.114 4.114 1.00149. 24 C

ANISOU 1826 CG LEU B 30 18701 20113 17890 -1692 1445 143 C

ATOM 1827 CDl LEU B 30 19.611 115.931 4.594 1.00149. 27 C

ANISOU 1827 CDl LEU B 30 18710 20137 17870 -1635 1424 -5 C

ATOM 1828 CD2 LEU B 30 17.250 115.996 3.743 1.00153. 75 C

ANISOU 1828 CD2 LEU B 30 19191 20754 18472 -1677 1566 95 C

ATOM 1829 C LEU B 30 20.994 113.274 3.694 1.00151. 83 C

ANISOU 1829 C LEU B 30 19200 20231 18259 -1642 1192 249 C

ATOM 1830 O LEU B 30 20.557 112.139 3.847 1.00153. 17 O

ANISOU 1830 O LEU B 30 19455 20370 18373 -1689 1135 401 O

ATOM 1831 N TYR B 31 22.027 113.749 4.372 1.00150. 84 N

ANISOU 1831 N TYR B 31 19048 20198 18066 -1608 1174 146 N

ATOM 1832 CA TYR B 31 22.697 112.939 5.366 1.00149. 05 C

ANISOU 1832 CA TYR B 31 18886 20044 17701 -1592 1080 198 C

ATOM 1833 CB TYR B 31 24.019 113.572 5.721 1.00143. 77 C

ANISOU 1833 CB TYR B 31 18165 19418 17043 -1531 1035 59 C

ATOM 1834~ CG TYR B 31 25.006 112.571 6.203 1.00146. 62 C

ANISOU 1834 CG . TYR B 31 18589 19821 17299 -1475 914 115 C

ATOM 1835 CDl TYR B 31 24.833 111.239 5.922 1.00147. 33 C

ANISOU 1835 CDl TYR B 31 18804 19846 17328 -1460 850 277 C

ATOM 1836 CEl TYR B 31 25.734 110.314 6.343 1.00150. 78 C

ANISOU 1836 CEl TYR B 31 19322 20318 17649 -1380 738 326 C

ATOM 1837 CZ TYR B 31 26.837 110.713 7.045 1.00148. 81 C

ANISOU 1837 CZ TYR B 31 18998 20189 17353 -1318 685 210 C ATOM 1838 OH TYR B 31 27.738 109.768 7 454 1,,00151.22 O

ANISOU 1838 OH TYR B 31 19378 20549 17529 -1216 569 255 O

ATOM 1839 CE2 TYR B 31 27.040 112..035 7 331 1. 00149 .01 C

ANISOU 1839 CE2 TYR B 31 18886 20280 17450 -1355 739 48 C

ATOM 1840 CD2 TYR B 31 26.128 112..954 6 909 1. 00151 .92 C

ANISOU 1840 CD2 TYR B 31 19205 20593 17926 -1431 854 C

ATOM 1841 C TYR B 31 21.840 112..876 6 612 1. 00137 .72 C

ANISOU 1841 C TYR B 31 17467 18762 16097 -1641 1117 237 C

ATOM 1842 O TYR B 31 21.472 113..916 7 143 1.00140 .66 O

ANISOU 1842 O TYR B 31 17777 19240 16428 -1637 1186 127 O

ATOM 1843 N SER B 32 21.519 111..672 7 090 1.00155 .53 N

ANISOU 1843 N SER B 32 19825 21027 18241 -1680 1070 395 N

ATOM 1844 CA SER B 32 20.661 111..512 8.279 1.00155 .79 C

ANISOU 1844 CA SER B 32 19885 21209 18100 -1731 1114 461 C

ATOM 1845 CB SER B 32 20.283 110.041 8.485 1.00152. 65 C

ANISOU 1845 CB SER B 32 19640 20771 17588 -1776 1039 644 C

ATOM 1846 OG SER B 32 21.291 109.170 7, 998 1.00146. 55 O

ANISOU 1846 OG SER B 32 18962 19867 16853 -1704 917 665 O

ATOM 1847 C SER B 32 21.294 112.065 9, 546 1.00151. 93 C

ANISOU 1847 C SER B 32 19370 20866 17491 -1667 1118 333 C

ATOM 1848 O SER B 32 20.622 112.651 10.377 1.00150. 60 O

ANISOU 1848 O SER B 32 19150 20819 17254 -1676 1211 287 O

ATOM 1849 N SER B 33 22.602 111.880 9.660 1.00162. 34 N

ANISOU 1849 N SER B 33 20725 22176 18779 -1592 1009 275 N

ATOM 1850 CA SER B 33 23.373 112.266 10.832 1.00161. 91 C

ANISOU 1850 CA SER B 33 20663 22252 18605 -1529 973 154 C

ATOM 1851 CB SER B 33 24.752 111.611 10.778 1.00160. 22 C

ANISOU 1851 CB SER B 33 20485 22022 18371 -1448 832 132 C

ATOM 1852 OG SER B 33 24.642 110.234 10.488 1.00161. 16 O

ANISOU 1852 OG SER B 33 20735 22075 18425 -1436 772 299 O

ATOM 1853 C SER B 33 23.582 113.764 11.004 1.00161. 03 C

ANISOU 1853 C SER B 33 20450 22190 18543 -1517 1027 -33 C

ATOM 1854 O SER B 33 24.294 114.176 11.914 1.00165. 95 O

ANISOU 1854 O SER B 33 21084 22921 19047 -1476 999 -129 O

ATOM 1855 N ASN B 34 23.004 114.584 10.134 1.00140. 99 N

ANISOU 1855 N ASN B 34 17837 19563 16168 -1546 1097 -90 N

ATOM 1856 CA ASN B 34 23.115 116.035 10.315 1.00143. 23 C

ANISOU 1856 CA ASN B 34 18067 19873 16479 -1532 1143 -267 C

ATOM 1857 CB ASN B 34 24.567 116.525 10.156 1.00142. 52 C

ANISOU 1857 CB ASN B 34 17936 19748 16466 -1517 1045 -401 C

ATOM 1858 CG ASN B 34 24.920 116.902 8.728 1.00141. 24 C

ANISOU 1858 CG ASN B 34 ' 17715 19437 16511 -1538 1065 -423 Cv

ATOM 1859 ODl ASN B 34 24.143 116.705 7.799 1.00140. 13 O

ANISOU 1859 ODl ASN B 34 17575 19210 16459 -1552 1145 -356 O

ATOM 1860 ND2 ASN B 34 26.107 117.452 8.552 1.00141. 89 N

ANISOU 1860 ND2 ASN B 34 17743 19500 16669 -1538 991 -517 N

ATOM 1861 C ASN B 34 22.151 116.861 9.469 1.00143. 94 C

ANISOU 1861 C ASN B 34 18112 19898 16679 -1552 1264 -294 C

ATOM 1862 O ASN B 34 22.384 118.043 9.247 1.00146. 45 O

ANISOU 1862 O ASN B 34 18408 20183 17053 -1539 1297 -442 O

ATOM 1863 N GLN B 35 21.070 116.228 9.018 1.00147. 17 N

ANISOU 1863 N GLN B 35 18518 20288 17110 -1586 1324 -151 N

ATOM 1864 CA GLN B 35 20.025 116.870 8.209 1.00149. 50 C

ANISOU 1864 CA GLN B 35 18763 20537 17502 -1594 1433 -160 C

ATOM 1865 CB GLN B 35 18.885 117.374 9.099 1.00151. 64 C

ANISOU 1865 CB GLN B 35 19016 20969 17633 -1576 1543 -148 C

ATOM 1866 CG GLN B 35 18.077 116.247 9.736 1.00164. 52 C

ANISOU 1866 CG GLN B 35 20661 22714 19135 -1630 1551 36 C

ATOM 1867 CD GLN B 35 17.509 115.280 8.703 1.00166. 33 C

ANISOU 1867 CD GLN B 35 20871 22864 19464 -1717 1548 199 C

ATOM 1868 OEl GLN B 35 16.739 115.679 7.820 1.00166. 30 O

ANISOU 1868 OEl GLN B 35 20795 22850 19543 -1729 1623 210 O

ATOM 1869 NE2 GLN B 35 17.883 113.998 8.812 1.00152. 72 N

ANISOU 1869 NE2 GLN B 35 19226 21082 17718 -1772 1451 324 N

ATOM 1870 C GLN B 35 20.479 117.966 7.234 1.00148. 64 C

ANISOU 1870 C GLN B 35 18629 20302 17547 -1564 1454 -309 C

ATOM 1871 O GLN B 35 19.690 118.841 6.874 1.00146. 77 O

ANISOU 1871 O GLN B 35 18374 20062 17331 -1534 1550 -379 O

ATOM 1872 N LYS B 36 21.738 117.904. 6.801 1.00148. 74 N

ANISOU 1872 N LYS B 36 18643 20216 17657 -1567 1367 -349 N

ATOM 1873 CA LYS B 36 22.262 118.825 5.796 1.00143. 97 C

ANISOU 1873 CA LYS B 36 18017 19477 17209 -1556 1385 -465 C

ATOM 1874 CB LYS B 36 23.544 119.513 6.290 1.00144. 04 C

ANISOU 1874 CB LYS B 36 18017 19506 17204 -1568 1316 -604 C

ATOM 1875 CG LYS B 36 23.288 120.767 7.127 1.00146. 83 C

ANISOU 1875 CG LYS B 36 18410 19940 17439 -1562 1349 -747 C

ATOM 1876 CD LYS B 36 24.567 121.522 7.473 1.00146. 30 C ANISOU 1876 CD LYS B 36 18338 19867 17384 -1601 1265 -895 C

ATOM 1877 CE LYS B 36 24.240 122.827 8.209 1. ,00147.78 C

ANISOU 1877 CE LYS B 36 18603 2Q055 17492 -1597 1308 -1055 C

ATOM 1878 NZ LYS B 36 25.442 123.675 8.513 1. 00148.92 N

ANISOU 1878 NZ LYS B 36 18749 20156 17678 -1670 1226 -1202 N

ATOM 1879 C LYS B 36 22.512 118.073 4.496 1. 00141.09 C

ANISOU 1879 C LYS B 36 17644 18971 16991 -1552 1352 -370 C

ATOM 1880 O LYS B 36 22.939 116.923 4.510 1. 00140.04 O

ANISOU 1880 O LYS B 36 17529 18842 16837 -1549 1262 -267 O

ATOM 1881 N ASN B 37 22.226 118.719 3.375 1. 00135.86 N

ANISOU 1881 N ASN B 37 16976 18182 16464 -1532 1422 -404 N

ATOM 1882 CA ASN B . 37 22.392 118.087 2.081 1. 00133.21 C

ANISOU 1882 CA ASN B 37 16651 17700 16264 -1506 1395 -321 C

ATOM 1883 CB ASN B 37 21.472 118.752 1.090 1. 00133.97 C

ANISOU 1883 CB ASN B 37 16754 17684 16463 -1475 1490 -345 C

ATOM 1884 CG ASN B 37 20.112 118.132 1.075 1. 00137.84 C

ANISOU 1884 CG ASN B 37 17237 18258 16879 -1489 1545 -285 C

ATOM 1885 ODl ASN B 37 19.977 116.910 1.022 1. 00136.91 O

ANISOU 1885 ODl ASN B 37 17129 18121 16770 -1510 1514 -148 O

ATOM 1886 ND2 ASN B 37 19.087 118.962 1.122 1. 00140.29 N

ANISOU 1886 ND2 ASN B 3 * 7 17531 18667 17107 -1477 1624 -385 N

ATOM 1887 C ASN B 37 23.812 118.181 1.577 1. 00135.40 C

ANISOU 1887 C ASN B 37 16904 17912 16628 -1487 1342 -372 C

ATOM 1888 O ASN B 37 24.485 119.153 1.857 1. 00139.67 O

ANISOU 1888 O ASN B 37 17416 18461 17193 -1509 1366 -508 O

ATOM 1889 N PHE B 38 24.263 117.195 0.808 1. 00133.56 N

ANISOU 1889 N PHE B 38 16691 17616 16440 -1445 1271 -261 N

ATOM 1890 CA PHE B 38 25.660 117.144 0.357 1. 00132.91 C

ANISOU 1890 CA PHE B 38 16568 17500 16433 -1407 1225 -284 C

ATOM 1891 CB PHE B 38 26.159 115.697 0.343 1. 00131.82 C

ANISOU 1891 CB PHE B 38 16471 17376 16240 -1342 1115 -145 C

ATOM 1892 CG PHE B 38 26.929 115.296 1.575 1. 00129.82 C

ANISOU 1892 CG PHE B 38 16194 17287 15843 -1351 1025 -149 C

ATOM 1893 CDl PHE B 38 28.260 115.64-2 1.716 1. 00131.91 C

ANISOU 1893 CDl PHE B 38 16374 17631 16115 -1322 966 -201 C

ATOM 1894 CEl PHE B 38 28.970 115.266 2.815 1. 00136.12 C

ANISOU 1894 CEl PHE B 38 16888 18320 16511 -1315 873 -210 C

ATOM 1895 CZ PHE B 38 28.360 114.530 3.790 1. 00137.25 C

ANISOU 1895 CZ PHE B 38 17116 18530 16504 -1334 846 -160 C

ATOM 1896 CE2 PHE B 38 „ 27.044 114.173 3.661 1. 00133.85 C

ANISOU 1896 CE2 PHE B 38 16765 18024 16069 -1375 914 -97 C

ATOM 1897 CD2 PHE B 38 26.337 114.548 2.562 1. 00135.02 C

ANISOU 1897 CD2 PHE B 38 16914 18030 16357 -1385 998 -93 C

ATOM 1898 C PHE B 38 25.933 117.774 -1.012 1. 00128.23 C

ANISOU 1898 C PHE B 38 15970 16746 16004 -1365 1296 -317 C

ATOM 1899 O PHE B 38 26.901 117.417 -1.677 1. 00127.42 O

ANISOU 1899 O PHE B 38 15860 16587 15968 -1298 1261 -261 O

ATOM 1900 N LEU B 39 25.098 118.720 -1.414 1. 00136.83 N

ANISOU 1900 N LEU B 39 17075 17769 17146 -1387 1398 -404 N

ATOM 1901 CA LEU B 39 25.131 119.247 -2.762 1. 00134.62 C

ANISOU 1901 CA LEU B 39 16820 17322 17008 -1335 1474 -427 C

ATOM 1902 CB LEU B 39 23.714 119.442 -3.240 1. 00131.63 C

ANISOU 1902 CB LEU B -39 16500 16871 16641 -1309 1545 -422 C

ATOM 1903 CG LEU B 39 ' 23.712 120.177 -4.552 1. 00133.27 C

ANISOU 1903 CG LEU B 39 16749 16904 16985 -1242 1630 -470 C

ATOM 1904 CDl LEU B 39 23.330 119.193 -5.612 1. 00133.38 C

ANISOU 1904 CDl LEU B 39 16816 16802 17062 -1153 1587 -338 C

ATOM 1905 CD2 LEU B 39 22.739 121.315 -4.484 1. 00137.52 C

ANISOU 1905 CD2 LEU B 39 17325 17416 17511 -1235 1730 -571 C

ATOM 1906 C LEU B 39 25.825 120.585 -2.825 1. 00138.29 C

ANISOU 1906 C LEU B 39 17250 17762 17532 -1383 1537 -572 C

ATOM 1907 O LEU B 39 25.389 121.513 -2.175 1. 00142.67 O

ANISOU 1907 O LEU B 39 17816 18364 18029 -1442 1575 -683 O

ATOM 1908 N ALA B 40 26.879 120.694 -3.631 1. 00131.88 N

ANISOU 1908 N ALA B 40 16408 16871 16829 -1355 1549 -565 N

ATOM 1909 CA ALA B 40 27.617 121.953 -3.813 1. 00129.57 C

ANISOU 1909 CA ALA B 40 16082 16543 16604 -1427 1609 -689 C

ATOM 1910 CB ALA B 40 29.105 121.711 -3.674 1. 00128.83 C

ANISOU 1910 CB ALA B 40 15869 16552 16530 -1462 1538 -666 C

ATOM 1911 C ALA B 40 27.329 122.648 -5.150 1. 00128.24 C

ANISOU 1911 C ALA B 40 15986 16179 16561 -1371 1724 -712 C

ATOM 1912 O ALA B 40 26.805 122.039 -6.075 1. 00128.15 O

ANISOU 1912 O ALA B 40 16026 16068 16597 -1258 1738 -618 O

ATOM 1913 N TRP B 41 27.675 123.928 -5.247 1. 00132.67 N

ANISOU 1913 N TRP B 41 16572 16673 17163 -1447 1801 -837 N

ATOM 1914 CA TRP B 41 27.563 124.666 -6.504 1. 00132.36 C

ANISOU 1914 CA TRP B 41 16615 16440 17236 * -1395 1919 -865 C ATOM 1915 CB TRP B 41 26.559 125.800 -6.374 1.00131.94 C

ANISOU 1915 CB TRP B 41 16695 16293 17142 -1400 2005 -991 C

ATOM 1916 CG TRP B 41 25.135 125.377 -6.388 1.00136.83 C

ANISOO 1916 CG TRP B 41 17373 16914 17704 -1293 2011 -956 C

ATOM 1917 CDl TRP B 41 24.343 125.153 -5.306 1.00142.41 C

ANISOU 1917 CDl TRP B 41 18059 17764 18286 -1309 1959 -955 C

ATOM 1918 NEl TRP B 41 23.080 124.795 -5.709 1.00147.55 N

ANISOU 1918 NEl TRP B 41 18753 18390 18918 -1206 1985 -908 N

ATOM 1919 CE2 TRP B 41 23.040 124.794 -7.078 1.00141.94 C

ANISOU 1919 CE2 TRP B 41 18104 17506 18320 -1110 2045 -886 C

ATOM 1920 CD2 TRP B 41 24.313 125.155 -7.537 1.00134.64 C

ANISOU 1920 CD2 TRP B 41 17174 16498 17484 -1155 2070 -912 C

ATOM 1921 CE3 TRP B 41 24.530 125.226 -8.907 1.00134.61 C

ANISOU 1921 CE3 TRP B 41 17236 16316 17594 -1062 2141 -889 C

ATOM 1922 CZ3 TRP B 41 23.484 124.940 -9.762 1.00134.27 C

ANISOU 1922 CZ3 TRP B 41 17271 16174 17571 -922 2170 -854 C

ATOM 1923 CH2 TRP B 41 22.239 124.584 -9.281 1.00135.22 C

ANISOU 1923 CH2 TRP B 41 17383 16388 17608 -893 2131 -834 C

ATOM 1924 CZ2 TRP B 41 21.993 124.505 -7.944 1.00141.47 C

ANISOU 1924 CZ2 TRP B 41 18101 17363 18287 -989 2075 -844 C

ATOM 1925 C TRP B 41 28.916 125.265 -6.852 1.00134.79 C

ANISOU 1925 C TRP B 41 16856 16724 17633 -1481 1950 -892 C

ATOM 1926 O TRP B 41 29.573 125.819 -5.983 1.00138.02 O

ANISOU 1926 O TRP B 41 17217 17213 18011 -1628 1921 -981 O

ATOM 1927 N TYR B 42 29.331 125.167 -8.112 1.00124.60 N

ANISOU 1927 N TYR B 42 15567 15327 16450 -1391 2009 -813 N

ATOM 1928 CA TYR B 42 30.615 125.709 -8.535 1.00133.32 C

ANISOU 1928 CA TYR B 42 16591 16419 17645 -1468 2057- -816 C

ATOM 1929 CB TYR B 42 31.535 124.587 -8.964 1.00126.83 C

ANISOU 1929 CB TYR B 42 15639 15693 16856 -1375 2005 -669 C

ATOM 1930 CG TYR B 42 32.036 123.785 -7.814 1.00129.52 C

ANISOU 1930 CG TYR B 42 15844 16262 17106 -1426 1864 -643 C

ATOM 1931 CDl TYR B 42 33.308 123.959 -7.334 1.00138.99 C

ANISOU 1931 CDl TYR B 42 16868 17621 18320 -1512 1821 -630 C

ATOM 1932 CEl TYR B 42 33.779 123.219 -6.273 1.00129.71 C

ANISOU 1932 CEl TYR B 42 15575 16662 170.48 -1540 1684 -613 C

ATOM 1933 CZ TYR B 42 32.967 122.301 -5.670 1.00138.81 C

ANISOU 1933 CZ TYR B 42 16800 17855 18086 -1493 1601 ' -604 C

ATOM 1934 OH TYR B 42 33.433 121.565 -4.603 1.00139.11 O

ANISOU 1934 OH TYR B 42 16743 18097 18015 -1509 1469 -587 O.

ATOM 1935 CE2 TYR B 42 31.690 122.120 -6.127 1.00126.71 C

ANISOU 1935 CE2 TYR B 42 15431 16170 16544 -1429 1650 -609 C

ATOM 1936 CD2 TYR B 42 31.234 122.863 -7.193 1.00135.00 C

ANISOU 1936 CD2 TYR B 42 16583 17020 17691 -1393 1776 -632 C

ATOM 1937 C TYR B 42 30.442 126.682 -9.680 1.00125.15 C

ANISOU 1937 C TYR B 42 15686 15165 16700 -1445 2206 -864 C

ATOM 1938 O TYR B 42 29.649 126.442 -10/584 1.00135.43 O

ANISOU 1938 O TYR B 42 17112 16320 18024 -1290 2264 -833 O

ATOM 1939 N GLN B 43 31.184 127.784 -9.634 1.00130.66 N

ANISOU 1939 N GLN B 43 16362 15840 17442 -1607 2260 -940 N

ATOM 1940 CA GLN B 43 31.163 128.784 -10.697 1.00133.44 C

ANISOU 1940 CA GLN B 43 16848 15980 17874 -1611 2408 -985 C

ATOM 1941 CB GLN B 43 30.901 130.178 -10.128 1.00131.07 C

ANISOU 1941 CB GLN B 43 16682 15595 17522 -1773 2443 -1151 C

ATOM 1942 CG GLN B 43 30.950 131.283 -11.171 1.00131.76 C

ANISOU 1942 CG GLN B 43 16954 15440 17670 -1768 2597 -1202 C

ATOM 1943 CD GLN B 43 31.535 132.581 -10.642 1.00137.84 C

ANISOU 1943 CD GLN B 43 17797 16153 18424 -2007 2620 -1328 C

ATOM 1944 OEl GLN B 43 30.858 133.611 -10.616 1.00143.90 O

ANISOU 1944 OEl GLN B 43 18801 16731 19144 -2009 2698 -1440 O

ATOM 1945 NE2 GLN B 43 32.805 132.543 -10.226 1.00137.61 N

ANISOU 1945 NE2 GLN B 43 17575 16285 18427 -2208 2546 -1310 N

ATOM 1946 C GLN B 43 32.480 128.804 -11.473 1.00139.23 C

ANISOU 1946 C GLN B 43 17450 16736 18715 -1661 2464 -901 C

ATOM 1947 O GLN B 43 33.537 129.144 -10.925 1.00138.61 O

ANISOU 1947 O GLN B 43 17210 16810 18647 -1841 2413 -912 O

ATOM 1948 N GLN B 44 32.418 128.446 -12.752 1.00139.66 N

ANISOU 1948 N GLN B 44 17570 16651 18844 -1495 2566 -814 N

ATOM 1949 CA GLN B 44 33.597 128.502 -13.604 1.00138.42 C

ANISOU 1949 CA GLN B 44 17303 16505 18784 -1509 2649 -721 C

ATOM 1950 CB GLN B 44 33.844 127.152 -14.281 1.00135.32 C

ANISOU 1950 CB GLN B 44 16824 16187 18406 -1281 2613 -555 C

ATOM 1951 CG GLN B 44 35.268 126.947 -14.778 1.00134.77 C

ANISOU 1951 CG GLN B 44 16548 16260 18397 -1301 2647 -441 C

ATOM 1952 CD GLN B 44 35.399 125.785 -15.752 1.00133.00 C

ANISOU 1952 CD GLN B 44 16321 16030 18182 -1018 2656 -278 C

ATOM 1953 OEl GLN B 44 . 34.480 125.488 -16.517 1.00130.60 O ANISOU 1953 OEl GLN B 44 16207 15541 17873 -820 2682 -255 O

ATOM 1954 NE2 GLN B 44 36.554 125.130 -15.736 1.00133.35 N

ANISOU 1954 NE2 GLN B 44 16156 16282 18230 -990 2630 -165 N

ATOM 1955 C GLN B 44 33.438 129.607 -14.645 1.00142.27 C

ANISOU 1955 C GLN B 44 17975 16742 19338 -1503 2822 -762 C

ATOM 1956 O GLN B 44 32.548 129.555 -15.497 1.00136.87 O

ANISOU 1956 O GLN B 44 17474 15874 18656 -1307 2887 -755 O

ATOM 1957 N LYS .B 45 34.295 130.618 -14.555 1.00150.33 N

ANISOU 1957 N LYS B 45 18953 17758 20409 -1726 2890 -805 N

ATOM 1958 CA LYS B 45 34.299 131.706 -15.521 1.00152.04 C

ANISOU 1958 CA LYS B 45 19348 17738 20684 -1760 3063 -838 C

ATOM 1959 CB LYS B 45 34.813 132.998 -14.880 1.00155.62 C

ANISOU 1959 CB LYS B 45 19823 18172 21135 -2080 3076 -957 C

ATOM 1960 CG LYS B 45 33.870 133.641 -13.900 1.00155.66 C

ANISOU 1960 CG LYS B 45 20037 18075 21031 -2144 3021 -1129 C

ATOM 1961 CD LYS B 45 33.918 135.148 -14.015 1.00159.53 C

ANISOU 1961 CD LYS B 45 20741 18354 21519 -2341 3123 -1242 C

ATOM 1962 CE LYS B 45 34.322 135.752 -12.695 1.00167.88 C

ANISOU 1962 CE LYS B 45 . 21840 19464 22482 -2572 3002 -1389 C

ATOM 1963 NZ LYS B 45 35.615 135.154 -12.256 1.00167.76 N

ANISOU 1963 NZ LYS B 45 21519 19730 22493 -2770 2864 -1350 N

ATOM 1964 C LYS B 45 35.190 131.357 -16.707 1.00151.94 C

ANISOU 1964 C LYS B 45 19236 17726 20768 -1662 3176 -683 C

ATOM 1965 O LYS B 45 36.315 130.907 -16.521 1.00152.52 O

ANISOU 1965 O LYS B 45 19054 18020 20877 -1735 3138 -587 O

ATOM 1966 N PRO B 46 34.695 131.572 -17.933 1.00150.22 N

ANISOU 1966 N PRO B 46 19223 17272 20583 -1482 3318 -659 N

ATOM 1967 CA PRO B 46 35.576 131.413 -19.079 1.00151.55 C

ANISOU 1967 CA PRO B 46 19317 17434 20832 -1365 3439 -506 C

ATOM 1968 CB PRO B 46 35.128 132.561 -19.979 1.00149.86 C

ANISOU 1968 CB PRO B 46 19387 16910 20642 -1312 3618 -556 C

ATOM 1969 CG PRO B 46 33.633 132.619 -19.756 1.00141.32 C

ANISOU 1969 CG PRO B 46 18537 15681 19478 -1211 3560 -691 C

ATOM 1970 CD PRO B 46 33.383 132.100 -18.345 1.00149.27 C

ANISOU 1970 CD PRO B 46 19413 16885 20419 -1383 3386 -774 C

ATOM 1971 C PRO B 46 37.058 131.539 -18.716 1.00152.86 C

ANISOU 1971 C PRO B 46 19205 17820 21055 -1601 3451 -437 C

ATOM 1972 O PRO B 46 37.497 132.540 -18.163 1.00151.41 O

ANISOU 1972 O PRO B 46 19019 17618 20891 -1892 3484 -522 O

ATOM 1973 N GLY B 47 37.813 130.489- -19.004 1.00162.11 N

ANISOU 1973 N GLY B 47 20145 19208 22240 -1476 3409 -287 N

ATOM -1974 CA GLY B 47 39.252 130.538 -18.888 1.00163.67 C

ANISOU 1974 CA GLY B 47 ' 20052 19643 22492 -1652 3434 -198 C

ATOM 1975 C GLY B 47 39.731 130.346 -17.477 1.00164.86 C

ANISOU 1975 C GLY B 47 19988 20047 22604 -1888 3262 -267 C

ATOM 1976 O GLY B 47 40.923 130.205 -17.245 1.00171.61 O

ANISOU 1976 O GLY B 47 20557 21161 23487 -2014 3238 -193 O

ATOM 1977 N GLN B 48 38.800 130.331 -16.535 1.00167.39 N

ANISOU 1977 N GLN B 48 20445 20304 22853 -1933 3142 -407 N

ATOM 1978 CA GLN B 48 39.125 130.184 -15.118 1.00172.24 C

ANISOU 1978 CA GLN B 48 20901 21133 23410 -2127 2967 -487 C

ATOM 1979 CB GLN B 48 38.226 131.122 -14.299 1.00172.36 C

ANISOU 1979 CB GLN B 48 21153 20967 23370 -2272 2930 -675 C

ATOM 1980 CG GLN B 48 38.822 131.625 -12.998 1.00184.07 C

ANISOU 1980 CG GLN B 48 22522 22609 24808 -2560 2788 -789 C

ATOM 1981 CD GLN B 48 40.095 132.413 -13.207 1.00198.47 C

ANISOU 1981 CD GLN B 48 24103 24598 26708 -2830 2805 -750 ~ C

ATOM 1982 OEl GLN B 48 40.274 133.055 -14.241 1.00199.54 O

ANISOU 1982 OEl GLN B 48 24294 24600 26924 -2953 2953 -732 O

ATOM 1983 NE2 GLN B 48 40.992 132.367 -12.224 1.00197.76 N

ANISOU 1983 NE2 GLN B 48 23741 24810 26589 -2925 2650 -736 N

ATOM 1984 C GLN B 48 38.972 128.718 -14.661 1.00168.61 C

ANISOU 1984 C GLN B 48 20320 20870 22875 -1902 2818 -408 C

ATOM 1985 O GLN B 48 38.549 127.864 -15.435 1.00168.84 O

ANISOU 1985 O GLN B 48 20438 20822 22893 -1616 2845 -313 O

ATOM 1986 N SER B 49 39.332 128.425 -13.417 1.00136.90 N

ANISOU 1986 N SER B 49 16117 17097 18800 -2026 2657 -442 N

ATOM . 1987 CA SER B 49 39.123 127.101 -12.848 1.00141.36 C

ANISOU 1987 CA SER B 49 16612 17826 19271 -1832 2507 -385 C

ATOM 1988 CB SER B 49 40.303 126.783 -11.964 1.00142.79 C

ANISOU 1988 CB SER B 49 16493 18339 19420 -1953 2383 -361 C

ATOM 1989 OG SER B 49 41.407 127.549 -12.406 1.00142.41 O

ANISOU 1989 OG SER B 49 16245 18401 19462 -2083 2478 -298 O

ATOM 1990 C SER B 49 37.837 127.161' -12.024 1.00140.26 C

ANISOU 1990 C SER B 49 16678 17565 19049 -1829 2421 -509 C

ATOM 1991 O SER B 49 37.457 128.240 -11.594 1.00144.18 O

ANISOU 1991 O SER B 49 17314 17915 19551 -1996 2457 -642 O ATOM 1992 N PRO B 50 37.144 126.023 -11.804 1.00134.82 N

ANISOU 1992 N PRO B 50 16023 16930 18274 -1635 2312 -460 N

ATOM 1993 CA PRO B 50 35.850 126.148 -11.124 1.00131.43 C

ANISOU 1993 CA PRO B 50 15782 16386 17770 -1632 2257 -564 C

ATOM 1994 CB PRO B 50 35.385 124.696 -10.994 1.00135.96 C

ANISOU 1994 CB PRO B 50 16374 17018 18267 -1400 2158 -458 C

ATOM 1995 CG PRO B 50 36.124 123.956 -11.997 1.00136.50 C

ANISOU 1995 CG PRO B 50 16334 17161 18369 -1239 2182 -307 C

ATOM 1996 CD PRO B 50 37.467 124.615 -12.066 1.00132.60 C

ANISOU 1996 CD PRO B 50 15636 16801 17944 -1412 2238 -312 C

ATOM 1997 C PRO B 50 36.041 126.739 -9.741 1.00131.82 C

ANISOU 1997 C PRO B 50 15771 16562 17751 -1855 2150 -692 C

ATOM 1998 O PRO B 50 36.992 126.345 -9.081 1.00134.82 O

ANISOU 1998 O PRO B 50 15964 17176 18085 -1893 2033 -661 O

ATOM 1999 N LYS B 51 35:185 127.665 -9.315 1.00147.73 N

ANISOU 1999 N LYS B 51 17953 18432 19746 -1978 2181 -833 N

ATOM 2000 CA LYS B 51 35.267 128.205 -7.960 1.00155.33 C

ANISOU 2000 CA LYS B 51 18897 19498 20622 -2162 2070 -960 C

ATOM 2001 CB LYS B 51 35.465 129.720 -7.984 1.00161.98 C

ANISOU 2001 CB LYS B 51 19821 20225 21500 -2402 2130 -1093 C

ATOM 2002 CG LYS B 51 35.669 130.343 -6.609 1.00166.07 C

ANISOU 2002 CG LYS B 51 20300 20868 21931 -2611 1994 -1219 C

ATOM 2003 CD LYS B 51 35.487 131.876 -6.635 1.00182.40 C

ANISOU 2003 CD LYS B 51 22570 22745 23990 -2808 2044 -1375 C

ATOM 2004 CE LYS B 51 35.388 132.463 -5.212 1.00187.59 C

ANISOU 2004 CE LYS B 51 23262 23493 24520 -2949 1896 -1510 C

ATOM 2005 NZ LYS B 51 34.984 133.898 -5.183 1.00176.02 N

ANISOU 2005 NZ LYS B 51 22041 21829 23010 -3112 1924 -1668 N

ATOM 2006 C LYS B 51 34.002 127.844 -7.200 1.00151.90 C

ANISOU 2006 C LYS B 51 18610 19030 20074 -2061 2013 -1009 C

ATOM 2007 O LYS B 51 32.937 127.718 -7.792 1.00147.27 * O

ANISOU 2007 O LYS B 51 18184 18280 19490 -1913 2088 -995 O

ATOM 2008 N LEU B 52 34.117 127.664 -5.891 1.00144.01 N

ANISOU 2008 N LEU B 52 17548 18197 18971 -2139 1880 -1063 N

ATOM 2009 CA LEU B 52 32.980 127.193 -5.098 1.00139.60 •c

ANISOU 2009 CA LEU B 52 17090 17659 18291 -2046 1819 -1086 C

ATOM 2010 CB LEU B 52 33.439 126.243 -3.967 1.00135.48 C

ANISOU 2010 CB LEU B 52 16419 17379 17680 -2029 1668 -1032 C

ATOM 2011 CG LEU B 52 32.512 125.801 -2.822 1.00134.61 ' C

ANISOU 2011 CG LEU B 52 16362 17366 17419 -2022 1571 -1080 ' C

ATOM 2012 CDl LEU B 52 31.226 125.251 -3.343 1.00135.05 C

ANISOU 2012 CDl LEU B 52 16555 17327 17432 -1869 1619 -1031 C

ATOM 2013 CD2 LEU B 52 33.183 124.765 -1.954 1.00135.16 C

ANISOU 2013 CD2 LEU B 52 16274 17666 17414 -2004 1430 -1016 C

ATOM 2014 C LEU B 52 32.136 128.349 -4.554 1.00140.74 C

ANISOU 2014 C LEU B 52 17410 17705 18361 -2141 1841 -1244 C

ATOM 2015 O LEU B 52 32.636 129.236 -3.864 1.00145.07 o

ANISOU 2015 O LEU B 52 17953 18282 18885 -2322 1797 -1352 O

ATOM 2016 N LEU B 53 30.851 128.339 -4.887 1.00132.47 N

ANISOU 2016 N LEU B 53 16523 16540 17268 -2010 1903 -1255 N

ATOM 2017 CA LEU B , 53 29.920 129.307 -4.342 1.00132.79 C

ANISOU 2017 CA LEU B 53 16744 16500 17212 -2043 1930 -1394 C

ATOM 2018 CB LEU B 53 28.781 129.584 -5.327 1.00129.88 C

ANISOU 2018 CB LEU B 53 16548 15934 16866 -1902 2062 -1403 C

ATOM 2019 CG LEU B 53 29.149 130.028 -6.736 1.00134.56 C

ANISOU 2019 CG LEU B 53 17172 16355 17600 -1870 2176 -1359 C

ATOM 2020 CDl LEU B 53 28.133 131.014 -7.306 1.00132.02 C

ANISOU 2020 CDl LEU B 53 17085 15817 17260 -1799 2300 -1453 C

ATOM 2021 CD2 LEU B 53 30.510 130.643 -6.677 1.00135.03 C

ANISOU 2021 CD2 LEU B 53 17126 16442 17737 -2061 2160 -1372 C

ATOM 2022 C LEU B 53 29.331 128.743 -3.063 1.00136.13 C

ANISOU 2022 C LEU B 53 17156 17079 17487 -1998 1835 -1400 C

ATOM 2023 O LEU B 53 29.415 129.344 -1.986 1.00139.98 O

ANISOU 2023 O LEU B 53 17706 17616 17865 -2082 1782 -1511 O

ATOM 2024 N ILE B 54 28.743 127.565 -3.185 1.00141.69 N

ANISOU 2024 N ILE B 54 17799 17854 18182 -1863 1815 -1276 N

ATOM 2025 CA ILE B 54 27.873 127.083 -2.147 1.00140.62 C

ANISOU 2025 CA ILE B 54 17681 17840 17908 -1804 1761 -1265 " C

ATOM 2026 CB ILE B 54 26.467 127.339 -2.575 1.00137.73 C

ANISOU 2026 CB ILE B 54 17441 17376 17515 -1677 1856 -1267 C

ATOM 2027 CGl ILE B 54 26.229 128.831 -2.619 1.00137.38 C

ANISOU 2027 CGl ILE B 54 17555 17164 17478 -1698 1954 -1403 C

ATOM 2028 CDl ILE B 54 25.023 129.162 -3.397 1.00146.90 C

ANISOU- 2028 CDl ILE B 54 18875 18273 18668 -1545 2054 -1403 C

ATOM 2029 CG2 ILE B 54 25.517 126.706 -1.620 1.00148.20 C

ANISOU 2029 CG2 ILE B 54 18780 18842 18688 -1633 1818 -1262 C

ATOM 2030 C ILE B 54 28.021 125.596 -1.854 1.00140.50 C ANISOU 2030 C ILE B 54 17539 17971 17872 -1748 1669 -1123 C

ATOM 2031 O •ILE B 54 28.023 124.781 -2.775 1.00138.40 O

ANISOU 2031 O ILE B 54 17235 17661 17690 -1663 1682 -1005 O

ATOM 2032 N TYR B 55 28.141 125.255 -0.568 1.00134.67 N

ANISOU 2032 N TYR B 55 16764 17398 17008 -1784 1573 -1136 N

ATOM 2033 CA TYR B 55 28.134 123.861 ' -0.114 1.00135.26 C

ANISOU 2033 CA TYR B 55 16766 17604 17024 -1721 1489 -1006 C

ATOM 2034 CB TYR B 55 29.490 123.451 0.478 1.00135.33 C

ANISOU 2034 CB TYR B 55 16647 17754 17020 -1780 1373 -993 C

ATOM 2035 CG TYR B 55 29.980 124.277 1.635 1.00137.55 C

ANISOU 2035 CG TYR B 55 16915 18123 17224 -1902 1309 -1132 C

ATOM 2036 CDl TYR B 55 30.783 ' 123.720 2.619 1.00142.36 C

ANISOU 2036 CDl TYR B 55 17435 18913 17743 -1929 1179 -1128 C

ATOM 2037 CEl TYR B 55 31.239 124.4-72 3.687 1.00146.39 C

ANISOU. 2037 CEl TYR B 55 17943 19499 18179 -2041 1104 -1262 C

ATOM 2038 CZ TYR B 55 30.886 125.800 3.776 1.00151.66 . C

ANISOU 2038 CZ TYR B 55 18719 20049 18856 -2131 1159 -1399 C

ATOM 2039 OH TYR B 55 31.325 126.586 4.825 1.00157.37 O

ANISOU 2039 OH TYR B 55 19471 20826 19497 -2246, 1071 -1539 O

ATOM 2040 CE2 TYR B 55 30.086 126.362 2.808 1.00148.20 C

ANISOU 2040 CE2 TYR B 55 18382 19429 18497 -2097 1296 -1403 C

ATOM 2041 CD2 TYR B 55 29.643 125.602 1.750 1.00140.52 C

ANISOU 2041 CD2 TYR B 55 17392 18396 17605 -1981 1,370 -1271 C

ATOM 2042 C TYR B 55 26.970 123.542 0.837 1.00134.75 C

ANISOU 2042 C TYR B 55 16762 17627 16809 -1683 1481 -998 C

ATOM 2043 O TYR B 55 26.106 124.379 1.070 1.00132.98 O

ANISOU 2043 O TYR B 55 16629 17364 16532 -1678 1550 -1085 O

ATOM 2044 N TRP B 56 26.938 122.330 1.371 1.00137.35 N

ANISOU 2044 N TRP B 56 17050 18076 17061 -1647 1402 -887 N

ATOM 2045 CA TRP B 56 2 ' 5.778 121.884 2.125 1.00137.41 C

ANISOU 2045 CA TRP B 56 17106 18167 16936 -1612 1410 -845 C

ATOM 2046 CB TRP B 56 25.891 122.227 3.610 1.00132.84 C

ANISOU 2046 CB TRP B 56 16539 17728 16205 -1657 1356 -934 C

ATOM 2047 CG TRP B 56 26.992 121.547 4.384 1.00136.70 C

ANISOU 2047 CG TRP B 56 16960 18342 16637 -1681 1228 -907 C

ATOM 2048 CDl TRP B 56 27.994 122.162 5.070 1.00141.42 C

ANISOU 2048 CDl TRP B 56 17522 19012 17198 -1749 1148 -1020 C

ATOM 2049 NEl TRP B 56 28.802 121.229 5.664 1.00146.40 N

ANISOU 2049 NEl TRP B 56 18087 19772 17767 -1731 1033 -957 N

ATOM 2050 CE2 TRP B 56 28.326 119.977 5.379 1.00142.06 C

ANISOU 2050 CE2 TRP B 56 17554 19218 17206 -1650 1039 -797 C

ATOM 2051 CD2 TRP B 56 27.182 120.134 4.582 1.00137.85 C

ANISOU 2051 CD2 TRP B 56 . 17078 18560 16740 -1630 1156 -761 C

ATOM 2052 CE3 TRP B 56 26.504 118.993 4.156 1.00135.45 C

ANISOU 2052 CE3 TRP B 56 16806 18220 16438 -1572 1169 -606 C

ATOM 2053 CZ3 TRP B 56 26.985 117.753 4.535 1.00132.27 C

ANISOU 2053 CZ3 TRP B 56 16405 17888 15964 -1531 1072 -491 C

ATOM 2054 CH2 TRP B 56 28.118 117.633 5.329 1.00132.64 C

ANISOU 2054 CH2 TRP B 56 16404 18060 15934 -1529 966 -531 C

ATOM 2055 CZ2 TRP B 56 28.805 118.727 5.758 1.00136.40 C

ANISOU 2055 CZ2 TRP B 56 16820 18591 16414 -1590 944 -684 C

ATOM 2056 C TRP B 56 24.484 122.490 1.588 1.00131.13 C

ANISOU 2056 C TRP B 56 16384 17282 16159 -1567 "1529 -868 C

ATOM 2057 O TRP B 56 23.573 122.774 2.353 1.00136.89 O

ANISOU 2057 O TRP B 56 17155 18089 16769 -1550 1565 -900 O

ATOM 2058 N ALA B 57 24.415 122.713 0.282 1.00140.32 N

ANISOU 2058 N ALA B 57 17562 18290 17462 -1531 1590 -854 N

ATOM 2059 CA ALA B 57 23.155 123.054 -0.384 1.00141.76 C

ANISOU 2059 CA ALA B 57 17805 18390 17668 -1460 1691 -852 C

ATOM 2060 CB ALA B 57 22.036 122.160 0.117 1.00142.28 C

ANISOU 2060 CB ALA B 57 17855 18571 17635 -1433 1683 -744 C

ATOM 2061 C ALA B 57 22.727 124.517 -0.302 1.00145.52 C

ANISOU 2061 C ALA B 57 18367 18807 18116 -1448 1782 -1008 C

ATOM 2062 O ALA B 57 22.234 125.070 -1.293 1.00144.28 O

ANISOU 2062 O ALA ' B 57 18270 18519 18031 -1382 1868 -1037 O

ATOM 2063 N SER B 58 22.892 125.122 0.878 1.00141.65 N

ANISOU 2063' N SER B 58 17906 18407 17507 -1496 1756 -1108 N

ATOM 2064 CA SER B 58 22.415 126.483 1.159 1.00141.80 C

ANISOU 2064 CA SER B . 58 18046 18387 17446 -1467 1828 -1254 C

ATOM 2065 CB SER B 58 21.320 126.487 2.237 1.00152.91 C

ANISOU 2065 CB SER B 58 19473 19955 18671 -1400 1849 -1249 C

ATOM 2066 OG SER B 58 20.120 125.832 1.842 1.00162.85 O

ANISOU 2066 OG SER B 58 20671 21274 19932 -1328 1893 -1123 O

ATOM 2067 C SER B 58 23.540 127.304 1.716 1.00141.15 C

ANISOU 2067 C SER B 58 18009 18278 17345 -1571 1774 -1383 C

ATOM 2068 O SER B 58 23.591 128.511 1.502 1.00144.50 O

ANISOU 2068 O SER B 58 18562 18586 17757 -1577 1825 -1512 O ATOM 2069 N THR B 59 24.411 126.628 2.466 1.00149.93 N

ANISOϋ 2069 N THR B 59 19026 19499 18440 -1652 1662 -1347 N

ATOM 2070 CA THR B 59 25.525 127.238 3.197 1.00156.14 C

ANISOU 2070 CA THR B 59 19825 20299 19203 -1771 1577 -1462 C

ATOM 2071 CB THR B 59 26.169 126.221 4.157 1.00153.35 C

ANISOϋ 2071 CB THR B 59 19347 20112 18806 -1819 1447 -1398 C

ATOM 2072 OGl THR B 59 25.287 125.980 5.262 1.00159.43 O

ANISOϋ 2072 OGl THR B 59 20145 21027 19404 -1752 1426 -1370 O

ATOM 2073 CG2 THR B 59 27.498 126.738 4.669 1.00150.98 C

ANISOU 2073 CG2 THR B 59 19026 19824 18514 -1955 1348 -1512 C

ATOM 2074 C THR B 59 26.600 127.766 2.261 1.00155.42 C

ANISOU 2074 C THR B 59 . 19725 20059 19269 -1868 1592 -1513 C

ATOM 2075 O THR B 59 27.221 127.005 1.536 1.00155.59 O

ANISOU 2075 O THR B 59 19629 20067 19420 -1882 1580 -1417 O

ATOM 2076 N ARG B 60 26.833 129.069 2.299 1.00148.12 N

ANISOϋ 2076 N ARG B 60 18935 19021 18321 -1933 1617 -1658 N

ATOM 2077 CA ARG B 60 27.599 129.735 1.257 1.00146.98 C

ANISOU 2077 CA ARG B 60 18808 18719 18317 -2041 1651 -1709 C

ATOM 2078 CB ARG B 60 26.957 131.091 1.006 1.00157.02 C

ANISOU 2078 CB ARG B 60 20310 19836 19516 -2057 1710 -1862 C

ATOM 2079 CG ARG B 60 27.686 132.052 0.107 1.00159.81 C

ANISOU 2079 CG ARG B 60 20749 19976 19994 -2129 1795 -1909 C

ATOM 2080 CD ARG B 60 26.998 133.410 0.243 1.00165.96 C

ANISOU 2080 CD ARG B 60 21804 20603 20651 -2088 1857 -2054 C

ATOM 2081 NE ARG B 60 25.561 133.230 0.454 1.00170.86 N

ANISOϋ 2081 NE ARG B 60 22489 21274 21156 -1871 1925 -2029 N

ATOM 2082 CZ ARG B 60 24.762 134.143 0.989 1.00171.40 C

ANISOU 2082 CZ ARG B 60 22775 21290, 21059 -1765 1967 -2136 C

ATOM 2083 NHl ARG B 60 25.261 135.310 1.372 1.00172.69 N

ANISOU 2083 NHl ARG B 60 23149 21320 21144 -1858 1941 -2283 N

ATOM 2084 NH2 ARG B 60 23.469 133.884 1.147 1.00168.31 N

ANISOU 2084 NH2 ARG B 60 22393 20986 20570 -1565 2032 -2093 N

ATOM 2085 C ARG B 60 29.073 129.853 1.645 1.00150.09 C

ANISOU 2085 C ARG B 60 19060 19203 18763 -2208 1530 -1720 C

ATOM 2086 O ARG B 60 29.403 129.897 2.837 1.00148.84 O

ANISOU 2086 O ARG B 60 18871 19187 18494 -2253 1414 -1759 O

ATOM 2087 N GLU B 61 29.955 129.882 0.642 1.00138.30 N

ANISOU 2087 N GLU B 61 17475 17641 17431 -2290 1557 -1681 N

ATOM 2088 CA GLU B 61 31.402 129.811 0.879 1.00140.10 C

ANISOU 2088 CA GLU B 61 17536 17977 17717 -2451 1450 -1685 C

ATOM 2089 CB GLU B 61 32.150 129.315 -0.368 .1.00135.38 C

ANISOU 2089 CB GLU B 61 16779 17368 17290 -2447 1500 -1564 C

ATOM 2090 CG GLU B 61 33.699 129.263 -0.243 1.00142.04 C

ANISOU 2090 CG GLU B 61 17421 18344 18203 -2612 1407 -1560 C

ATOM 2091 CD GLU B 61 34.239 128.200 0.751 1.00147.50 C

ANISOU 2091 CD GLU B 61 17944 19290 18811 -2583 1253 -1513 C

ATOM * 2092 OEl GLU B 61 33.685 128.069 1.865 1.00147.91 O

ANISOU 2092 OEl GLU B 61 18067 19415 18718 -2575 1167 -1582 O

ATOM 2093 OE2 GLU B 61 35.241 127.508 0.436 1.00143.49 O

ANISOU 2093 OE2 GLU B 61 17239 18911 18368 -2555 1219 -1407 O

ATOM 2094 c GLU B 61 31.970 131.140 1.334 1.00146.01 C

ANISOU 2094 C GLU B 61 18390 18642 18445 -2647 1412 -1843 C

ATOM 2095 O GLU B 61 31.433 132.188 1.006 1.00149.77 O

ANISOU 2095 O GLU B 61 19081 18934 18890 -2650 1494 -1936 O

ATOM 2096 N SER B 62 33.056 131.097 2.094 1.00167.48 N

ANISOU 2096 N SER B 62 20969 21493 21172 -2809 1282 -1877 N

ATOM 2097 CA SER B 62 33.708 132.315 2.543 1.00171.74 C

ANISOU 2097 CA SER B 62 21599 21950 21705 -3034 1226 -2021 C

ATOM 2098 CB SER B 62 34.936 131.984 3.390 1.00170.00 C

ANISOU 2098 CB SER B 62 21181 21936 21476 -3196 1048 -2048 C

ATOM 2099 OG SER B 62 36.076 131.773 2.575 1.00162.18 O

ANISOU 2099 OG SER B 62 19949 21026 20645 -3296 1057 -1959 O

ATOM 2100 C SER B 62 34.133 133.140 1.340 1.00180.07 C

ANISOU 2100 C SER B 62 22695 22812 22912 -3139 1353 -2015 C

ATOM 2101 O SER B 62 34.852 132.649 0.467 1.00184.19 O

ANISOU 2101 O SER B 62 23049 23360 23573 -3107 1424 -1891 O

ATOM 2102 N GLY B 63 33.688 134.390 1.290 1.00188.16 •N

ANISOU 2102 N GLY B 63 23967 23632 23894 -3246 1386 -2147 N

ATOM 2103 CA GLY B 63 34.074 135.289 0.217 1.00188.03 C

ANISOϋ 2103 CA GLY B 63 24033 23409 24000 -3364 1506 -2155 C

ATOM 2104 C GLY B 63 33.181 135.155 -0.995 1.00178.86 C

ANISOU 2104 C GLY B 63 23016 22076 22868 -3153 1685 -2102 C

ATOM 2105 O GLY B 63 33.647 134.968 -2.116 1.00185.15 O

ANISOU 2105 O GLY B 63 23841 22723 23785 -3189 1808 -2063 O

ATOM 2106 N VAL B 64 31.882 135.248 -0.757 1.00156.26 N

ANISOU 2106 N VAL B 64 20242 19241 19888 -2929 .1699 -2099 N

ATOM 2107 CA VAL B 64 30.897 135.060 -1.803 1.00158.10 C ANISOU 2107 CA VAL B 64 20588 19342 20140 -2717 1851 -2048 C

ATOM 2108 CB VAL B 64 30.457 133.576 -1.922 1.00155.93 C

ANISOU 2108 CB VAL B 64 20128 19227 19891 -2520 1855 -1899 C

ATOM 2109 CGl VAL B 64 29.484 133.406 -3.072 1.00155.79 C

ANISOU 2109 CGl VAL B 64 20205 19063 19926 -2327 2004 -1840 C

ATOM 2110 CG2 VAL B 64 31.653 132.655 -2.109 1.00152.20 C

ANISOU 2110 CG2 VAL B 64 19371 18916 19541 -2600 1790 -1781 C

ATOM 2111 C VAL B 64 29.665 135.923 -1.536 1.00164.83 C

ANISOϋ 2111 C VAL 64 21751 20044 20834 -2615 1901 -2174 C

ATOM 2112 O VAL B 64 29.082 135.879 -0.449 1.00170.15 O

ANISOU 2112 O VAL B 64 22497 20808 21346 -2566 1821 -2242 O

ATOM 2113 N PRO B 65 29.279 136.718 -2.538 1.00166.07 N

ANISOU 2113 N PRO B 65 22100 19972 21026 -2569 2036 -2205 N

ATOM 2114 CA PRO B 65 28.114 137.603 -2.681 1.00168.44 C

ANISOU 2114 CA PRO B 65 22723 20085 21193 -2438 2123 -2316 C

ATOM 2115 CB PRO B 65 28.167 137.985 -4.159 1.00175.50 C

ANISOU 2115 CB PRO B 65 23706 20760 22215 -2429 2270 -2287 C

ATOM 2116 CG PRO B 65 29.627 137.964 -4.487 1.00174.53 C

ANISOU 2116 CG PRO B 65 23369 20677 22268 -2662 2238 -2213 C

ATOM 2117 CD PRO B 65 30.231 136.871 -3.652 1.00164.79 C

ANISOU 2117 CD PRO B 65 21834 19725 21055 -2665 2115 -2122 C

ATOM 2118 C PRO B 65 26.756 136.965 -2.385 1.00163.36 C

ANISOU 2118 C PRO B 65 22100 19536 20434 -2163 2159 -2288 C

ATOM 2119 O PRO B 65 26.463 135.856 -2.817 1.00161.09 O

ANISOU 2119 O PRO B 65 21621 19365 20222 -2041 2184 -2160 O

ATOM 2120 N ASP B 66 25.911 137.700 -1.683 1.00163.39 N

ANISOU 2120 N ASP B 66 22352 19482 20245 -2062 2166 -2408 N

ATOM 2121 CA ASP B 66 24.636 137.159 -1.261 1.00168.25 C

ANISOU 2121 CA ASP B 66 22963 20241 20725 -1822 2186 -2384 C

ATOM 2122 CB ASP B 66 24.104 137.960 -0.094 1.00179.82 C

ANISOU 2122 CB ASP B 66 24674 21696 21952 -1770 2142 -2526 C

ATOM 2123 CG ASP B 66 25.209 138.537 0.736 1.00194.15 C

ANISOU 2123 CG ASP B 66 26522 23505 23741 -2011 2002 -2608 C

ATOM 2124 ODl ASP B 66 25.106 139.724 1.109 1.00206.29 O

ANISOU 2124 ODl ASP B 66 28355 24870 25157 -2065 1983 -2751 O

ATOM 2125 0D2 ASP B 66 26.197 137.808 0.985 1.00192.65 O

ANISOU 2125 0D2 ASP B 66 26072 23479 23647 -2145 1904 -2531 O

ATOM 2126 C ASP B 66 23.634 137.200 -2.380 1.00168.84 C

ANISOU 2126 C ASP B 66 23087 20239 20827 -1602 2325 -2339 C

ATOM 2127 O ASP B 66 22.484 136.817 -2.192 1.00170.04 O

ANISOU 2127 O ASP B 66 23217 20517 20873 -1402 2353 -2311 O

ATOM 2128 N ARG ' B 67 24.057 137.694 -3.537 1.00171.45 N

ANISOU 2128 N ARG B 67 23479 20372 21293 -1638 2412 -2330 N

ATOM 2129 CA ARG B 67 23.222 137.596 -4.726 1.00173.68 c

ANISOU 2129 CA ARG B 67 23793 20579 21618 -1425 2534 -2281 C

ATOM 2130 CB ARG B 67 23.911 138.219 -5.949 1.00170.43 C

ANISOU 2130 CB ARG B 67 23516 19910 21331 -1482 2632 -2297 C

ATOM 2131 CG ' ARG B 67 24.932 139.297 -5.636 1.00171.50 C

ANISOU 2131 CG ARG B 67 23822 19884 .21455 -1719 2606 -2401 C

ATOM 2132 CD ARG B 67 25.400 139.994 -6.900 1.00175.13 C

ANISOU 2132 CD ARG B 67 24435 20083 22025 -1764 2726 -2407 C

ATOM 2133 NE ARG B 67 26.473 139.297 -7.603 1.00174.99 N

ANISOU 2133 NE ARG B 67 24184 20085 22220 -1946 2723 -2291 N

ATOM 2134 CZ ARG B 67 27.764 139.601 -7.487 1.00178.30 C

ANISOU 2134 CZ ARG B 67 24551 20490 22706 -2232 2665 -2304 C

ATOM 2135 NHl ARG B 67 28.154 140.579 -6.679 1.00181.27 N

ANISOU 2135 NHl ARG B 67 25107 20811 22956 -2388 2589 -2435 N

ATOM 2136 NH2 ARG B 67 28.673 138.925 -8.1-74 1.00175.69 N

ANISOU 2136 NH2 ARG B 67 23987 20208 22561 -2359 2678 -2185 N

ATOM 2137 C ARG B 67 23.003 136.100 -4.950 1.00170.37 C

ANISOU 2137 C ARG B 67 23071 20351 21312 -1369 2504 -2116 C

ATOM 2138 O ARG B 67 21.943 135.661 -5.409 1.00164.00 O

ANISOU 2138 O ARG B 67 22229 19583 20500 -1176 2558 -2059 O

ATOM 2139 N PHE B 68 24.024 135.323 -4.596 1.00169.06 N

ANISOU 2139 N PHE B 68 22693 20305 21237 -1543 2406 -2042 N

ATOM 2140 CA PHE B 68 24.014 133.884 -4.779 1.00160.49 C

ANISOU 2140 CA PHE B 68 21351 19378 20251 -1509 2363 -1885 C

ATOM 2141 CB PHE B 68 25.444 133.378 -4.953 1.00158.76 C

ANISOU 2141 CB PHE B 68 20961 19179 20183 -1692 2304 -1814 C

ATOM 2142 CG PHE B 68 26.139 133.925 -6.162 1.00162.25 C

ANISOU 2142 CG PHE B 68 21476 19413 20759 -1748 2396 -1819 C

ATOM 2143 CDl PHE B 68 25.680 133.629 -7.434 1.00159.15 C

ANISOU 2143 CDl PHE B 68 21169 18873 20426 -1581 2510 -1784 C

ATOM 2144 CEl PHE B 68 26.311 134.124 -8.539 1.00152.77 C

ANISOU 2144 CEl PHE B 68 20443 17872 19732 -1621 2605 -1783 C

ATOM 2145 CZ PHE B 68 27.416 134.921 -8.391 1.00155.72 C

ANISOU 2145 CZ PHE B 68 20792 18207 20166 -1848 2590 -1809 C ATOM 2146 CE2 PHE B 68 27.888 135.221 -7.134 1.00157.51 C

ANISOU 2146 CE2 PHE B 68 20917 18588 20340 -2029 2466 -1847 C

ATOM 2147 CD2 PHE B 68 27.254 134.722 -6.028 1.00157.72 C

ANISOU 2147 CD2 PHE B 68 20881 18798 20248 -1968 2368 -1856 C

ATOM 2148 C PHE B 68 23.410 133.217 -3.565 1.00160.79 C

ANISOU 2148 C PHE B 68 21291 19645 20157 -1464 2282 -1859 C

ATOM 2149 O PHE B 68 23.872 133.437 -2.446 1.00162.64 O

ANISOU 2149 O PHE B 68 . 21522 199-70 20302 -1574 2196 -1916 O

ATOM 2150 N THR B 69 22.383 132.400 -3.770 1.00152.18 N

ANISOU 2150 N THR B 69 20125 18648 19048 -1306 2307 -1771 N

ATOM 2151 CA THR B 69 21.863 131.613 -2.657 1.00151.68 C

ANISOU 2151 CA THR B 69 19954 18811 18865 -1273 -2241 -1721 C

ATOM 2152 CB THR B 69 20.776 132.348 -1.893 1.00159.19 C

ANISOU 2152 CB THR B 69 21053 19815 19616 -1139 2290 -1818 C

ATOM 2153 OGl THR B 69 20.675 133.696 -2.375 1.00162.42 O

ANISOU 2153 OGl THR B 69 21702 20034 19975 -1137 2343 -1970 O

ATOM 2154 CG2 THR B 69 21.089 132.313 -0.389 1.00159.02 C

ANISOU 2154 CG2 THR B 69 20975 19999 19446 -1181 2205 -1819 C

ATOM 2155 C THR B 69 21.327 130.249 -3.054 1.00140.72 C

ANISOU 2155 C THR B 69 18392 17527 17548 -1207 2225 -1559 C

ATOM 2156 O THR B 69 20.387 130.130 -3.841 1.00132.93 O

ANISOU 2156 O THR B 69 17424 16482 16602 -1080 2292 -1522 O

ATOM 2157 N GLY B 70 21.933 129.220 -2.479 1.00153.94 N

ANISOU 2157 N GLY B 70 19913 19349 19227 -1295 2126 -1467 N

ATOM 2158 CA GLY B 70 21.523 127.860 -2.728 1.00152.62 C

ANISOU 2158 CA GLY B 70 19604 19270 19114 -1262 2088 -1308 C

ATOM 2159 C GLY B 70 20.347 127.541 -1.846 1.00158.55 C

ANISOU 2159 C GLY B 70 20320 20198 19722 -1193 2090 -1267 C

ATOM 2160 O GLY B 70 20.264 128.012 -0.705 1.00157.53 O

ANISOU 2160 O GLY B 70 20214 20192 19450 -1213 2070 -1324 O

ATOM 2161 N SER B 71 19.434 126.749 -2.394 1.00174.86 N

ANISOU 2161 N SER B 71 22331 22281 21825 -1114 2112- -1164 N

ATOM 2162 CA SER B 71 18.250 126.307 -1.685 1.00171.61 C

ANISOU 2162 CA SER B 71 21865 22047 21293 -1053 2131 -1109 C

ATOM 2163 CB SER B 71 17.069 127.199 -2.037 1.00172.55 C

ANISOU 2163 CB SER B 71 22051 22126 21386 -905 2232 -1169 C

ATOM 2164 OG SER B 71 16.948 127.324 - -3.440 1.00176.88 O

ANISOU 2164 OG SER B 71 22736 22461 22010 -864 2285 -1282 O

ATOM 2165 C SER B 71 17.967 124.890 -2.128 1.00171.13 C

ANISOU 2165 C SER B 71 21685 22041 21297 -1093 2064 -936 C

ATOM 2166 O SER B 71 18.613 124.393 -3.054 1.00170.08 O

ANISOU 2166 O SER B 71 21542 21784 21298 -1124 2017 -876 O

ATOM 2167 N GLY B 72 17.016 124.241 -1.462 1.00168.35 N

ANISOU 2167 N GLY B 72 21254 21872 20841 -1092 2060 -851 N

ATOM 2168 CA GLY B 72 16.593 122.901 -1.834 1.00164.42 C

ANISOU 2168 CA GLY B 72 20666 21416 20389 -1137 2001 -683 C

ATOM 2169 C GLY B 72 17.019 121.819 -0.861 1.00154.98 C

ANISOU 2169 C GLY B 72 19421 20320 19146 -1248 1908 -574 C

ATOM 2170 O GLY B 72 17.842 122.061 0.012 1.00158.51 O

ANISOU 2170 O GLY B 72 19889 20795 19544 -1290 1875 -630 O

ATOM 2171 N SER B 73 16.450 120.627 -1.010 1.00135.79 N

ANISOU 2171 N SER B 73 16935 17938 16722 -1298 1857 -419 N

ATOM 2172 CA SER B 73 16.812 119.482 -0.175 1.00141.32 C

ANISOU 2172 CA SER B 73 17619 18703 17373 -1395 1763 -300 C

ATOM 2173 CB SER B 73 16.266 119.618 1.254 1.00144.46 C

ANISOU 2173 CB SER B 73 17977 19318 17595 -1429 1791 -292 C

ATOM 2174 OG SER B 73 16.318 118.372 1.947 1.00145.05 O

ANISOU 2174 OG SER B 73 18038 19467 17607 -1521 1716 -139 O

ATOM 2175 C SER B 73 16.384 118.131 -0.740 1.00149.94 C

ANISOU 2175 C SER B 73 18702 19749 18518 -1447 1695 -134 C

ATOM 2176 O SER B 73 15.326 117.994 -l.-375 1.00146.89 O

ANISOU 2176 O SER B 73 18290 19336 18185 -1422 1725 -107 O

ATOM 2177 N GLY B 74 17.213 117.128 -0.471 1.00166.62 N

ANISOU 2177 N GLY B 74 20850 21849 20608 -1514 1594 -28 N

ATOM 2178 CA GLY B 74 16.949 115.771 -0.903 1.00166.25 C

ANISOU 2178 CA GLY B 74 20840 21737 20590 -1574 1507 135 C

ATOM 2179 C .GLY B 74 17.469 115.514 -2.300 1.00162.69 C

ANISOU 2179 C GLY B 74 20469 21064 20281 -1508 1449 145 C

ATOM 2180 O GLY B 74 18.580 115.000 -2.478 1.00154.49 O

ANISOU 2180 O GLY B 74 19503 19938 19260 -1486 1369 178 O

ATOM 2181 N THR B 75 16.657 115.883 -3.290 1.00144.68 N

ANISOU 2181 N THR B 75 18176 18703 18092 -1458 1490 117 N

ATOM 2182 CA THR B 75 16.991 115.649 -4.688 1.00142.21 C

ANISOU 2182 CA THR B 75 17952 18175 17908 -1379 1440 133 C

ATOM 2183 CB THR B 75 16.289 114.416 -5.222 1.00141.30 C

ANISOU 2183 CB THR B 75 17890 17991 17807 -1435 1341 282 C

ATOM 2184 OGl THR B 75 14.877 114.598 -5.094 1.00149.34 O ANISOO 2184 OGl THR B 75 18809 19127 18805 -1487 1392 287 O

ATOM 2185 CG2 THR B 75 16.715 113.199 -4.443 1.00137.78 C

ANISOU 2185 CG2 THR B 75 17508 17578 17263 -1537 1234 421 C

ATOM 2186 C THR B 75 16.618 116.797 -5.611 1.00140.83 C

ANISOU 2186 C THR B 75 17766 17917 17827 -1268 1535 6 C

ATOM 2187 O THR B 75 16.858 116.720 -6.805 1.00143.20 O

ANISOU 2187 O THR B 75 18141 18035 18232 -1180 1514 4 O

ATOM 2188 N ASP B 76 16.023 117.853 -5.084 1.00174.66 N

ANISOU 2188 N ASP B 76 21974 22328 22059 -1255 1642 -99 N

ATOM 2189 CA ASP B 76 15.769 119.005 -5.927 1.00179.64 C

ANISOU 2189 CA ASP B 76 22626 22871 22758 -1135 1737 -231 C

ATOM 2190 CB ASP B 76 14.281 119.199 -6.161 1.00192.03 C

ANISOU 2190 CB ASP B 76 24127 24541 24293 -1105 1788 -239 C

ATOM 2191 CG ASP B 76 13.757 118.312 -7.260 1.00200.34 C

ANISOU 2191 CG ASP B 76 25196 25499 25425 -1102 1708 -137 C

ATOM 2192 ODl ASP B 76 14.119 117.115 -7.275 1.00195.72 O

ANISOU 2192 ODl ASP B 76 24661 24838 24867 -1177 1593 -12 O

ATOM 2193 0D2 ASP B 76 12.988 118.811 -8.110 1.00210.30 O

ANISOU 2193. 0D2 ASP B 76 26433 26761 26710 -1017 1752 -185 O

ATOM 2194 C ASP B 76 16.381 120.246 -5.339 1.00179.45 C

ANISOU 2194 C ASP B 76 22610 22879 22695 ' -1109 1821 -377 C

ATOM 2195 O ASP B 76 16.147 120.576 -4.182 1.00184.83 O

ANISOU 2195 O ASP B 76 23239 23729 23258 -1159 1849 -405 O

ATOM 2196 N PHE B 77 17.178 120.930 -6.144 1.00146.95 N

ANISOU 2196 N PHE B 77 18567 18596 18670 -1035 1861 -467 N

ATOM 2197 CA PHE B 77 17.882 122.113 -5.677 1.00147.17 C

ANISOU 2197 CA PHE B 77 18620 18631 18665 -1032 1933 -609 C

ATOM 2198 CB PHE B 77 19.362 121.796 -5.439 1.00142.61 C

ANISOU 2198 CB PHE B 77 18042 18023 18122 -1100 1875 -597 C

ATOM 2199 CG PHE B 77 19.586 120.603 -4.556 1.00142.45 C

ANISOU 2199 CG PHE B 77 17964 18125 18037 -1183 1769 -471 C

ATOM 2200 CDl PHE B 77 19.278 119.332 -4.995 1.00144.56 C

ANISOU 2200 CDl PHE B 77 18245 18337 18343 -1178 1685 -327 C

ATOM 2201 CEl PHE B 77 19.473 118.231 -4.179 1.00144.93 C

ANISOU 2201 CEl PHE B 77 18274 18481 18313 -1251 1588 -210 C

ATOM 2202 CZ PHE B 77 19.977 118.391 -2.921 1.00141.65 C

ANISOU 2202 CZ PHE B 77 17811 18225 17783 -1321 1578 -236 C

ATOM 2203 CE2 PHE B 77 20.285 119.649 -2.472 1.00144.69 C

ANISOU 2203 CE2 PHE B 77 18172 18671 18131 -1324 1655 -381 C

ATOM 2204 CD2 PHE B 77 20.088 120.751 '-3.283 1.00144.85 C

ANISOU 2204 CD2 PHE B 77 18224 18587 18224 -1260 1748 -497 C

ATOM 2205 C PHE B 77 17.743 123.242 -6.676 1.00149.97 C

ANISOU 2205 C PHE B 77 19062 18836 19083 -918 2030 -724 C

ATOM 2206 O PHE B 77 17.218 123.052 -7.777 1.00150.12 O

ANISOU 2206 O PHE B 77 19116 18741 19182 -833 2033 -690 O

ATOM 2207 N THR B 78 18.191 124.426 -6.276 1.00143.82 N

ANISOU 2207 N THR B 78 18338 18052 18255 -912 2105 -864 N

ATOM 2208 CA THR B 78 18.283 125.549 -7.193 1.00144.59 C

ANISOU 2208 CA THR B 78 18555 17970 18413 -818 2196 -976 C

ATOM 2209 CB THR B 78 16.965 126.340 -7.342 1.00147.95 C

ANISOU 2209 CB THR B 78 19038 18411 18764 -681 2283 -1057 C

ATOM 2210 OGl THR B 78 16.840 127.259 -6.250 1.00149.76 O

ANISOU 2210 OGl THR B 78 19266 18801 18834 -692 2315 -1134 O

ATOM 2211 CG2 THR B 78 15.739 125.421 -7.425 1.00143.09 C

ANISOU 2211 CG2 THR B 78 . 18345 17851 18170 -619 2246 -949 C

ATOM 2212 C THR B 78. 19.304 126.532 -6.681 1.00140.51 C

ANISOU 2212 C THR B 78 18096 17409 17882 -894 2224 -1085 C

ATOM 2213 O THR B 78 19.359 126.810 -5.483 1.00142.78 O

ANISOU 2213 O THR B 78 18348 17833 18070 -978 2193 -1116 O

ATOM 2214 N LEU B 79 20.116 127.041 -7.604 1.00122.22 N

ANISOU 2214 N LEU B 79 15867 14902 15669 -872 2275 -1133 N

ATOM 2215 CA LEU B 79 20.963 128.198 -7.353 1.00122.60 C

ANISOU 2215 CA LEU B 79 15997 14877 15707 -950 2318 -1252 C

ATOM 2216 CB LEU B 79 22.293 128.077 -8.082 1.00132.59 C

ANISOU 2216 CB LEU B 79 17242 16021 17114 -1014 2312 -1210 C

ATOM 2217 CG LEU B 79 23.233 129.188 -7.659 1.00132.79 C

ANISOU 2217 CG LEU B 79 17340 15982 17133 -1-133 2349 -1329 C

ATOM 2218 CDl LEU B 79 23.082 129.419 -6.188 1.00143.11 C

ANISOU 2218 CDl LEU B 79 18640 17441 18296 -1219 2297 -1405 C

ATOM 2219 CD2 LEU B 79 24.632 128.802 -7.974 1.00135.04 C

ANISOU 2219 CD2 LEU B 79 17529 16246 17533 -1240 2317 -1267 C

ATOM 2220 C LEU B 79 20.193 129.413 -7.844 1.00123.91 C

ANISOU 2220 C LEU B 79 16335 14921 15826 -831 2429 -1376 C

ATOM 2221 O LEU B 79 19.423 129.304 -8.804 1.00125.18 O

ANISOU 2221 O LEU B 79 16541 14993 16028 -692 2475 -1355 O

ATOM 2222 N THR B 80 20.374 130.558 -7.179 1.00151.73 N

ANISOU 2222 N THR B 80 19969 18436 19247 -875 2462 -1508 N ATOM 2223 CA THR B 80 19.602 131.767 -7.493 1.00151.83 C

ANISOU 2223 CA THR B 80 20181 18332 19175 ' -746 2564 -1636 C

ATOM 2224 CB THR B 80 18.362 131.905 -6.574 1.00155.54 C

ANISOU 2224 CB THR B 80 20659 18979 19462 -639 2570 -1677 C

ATOM 2225 OGl THR B 80 18.052 130.-642 -5.964 1.00153.60 O

ANISOU 2225 OGl THR B 80 20207 18936 19219 -650 2499 -1543 O

ATOM 2226 CG2 THR B 80 17.159 132.400 -7.367 1.00154.74 C

ANISOU 2226 CG2 THR B 80 20707 18791 19295 -426 2670 -1753 C

ATOM 2227 C THR B 80 20.435 133.049 -7.393 1.00152.85 C

ANISOU 2227 C THR B 80 20488 18300 19289 -840 2607 -1764 C

ATOM 2228 O THR B 80 21.015 133.342 -6.343 1.00151.29 O

ANISOU 2228 O THR B 80 20286 18168 19028 -982 2549 -1813 O

ATOM 2229 N ILE B 81 20.493 133.802 -8.491 1.00160.74 N

ANISOU 2229 N ILE B 81 21651 19077 20345 -768 2702 -1815 N

ATOM 2230 CA ILE B 81 21.182 135.088 -8.500 1.00168.79 C

ANISOU 2230 CA ILE B 81 22883 19910 21339 -855 2757 -1939 C

ATOM 2231 CB ILE B 81 22.073 135.274 -9.731 1.00162.42 C

ANISOU 2231 CB ILE B 81 22117 18896 20700 -914 2822 -1903 C

ATOM 2232 CGl ILE B 81 22.569 133.936 -10.232 1.00159.78 C

ANISOU 2232 CGl ILE B 81 21529 18660 , 20522 -1022 2752 -1755 C

ATOM 2233 CDl ILE B 81 23.770 134.058 -11.095 1.00160.12 C

ANISOU 2233 CDl ILE B 81 21596 18531 20710 -1100 2818 -1719 C

ATOM 2234 CG2 ILE B 81 23.260 136.162 -9.403 1.00168.64 C

ANISOU 2234 ' CG2 ILE B 81 23080 19525 21469 -1084 2854 -2010 C

ATOM 2235 C ILE B 81 20.177 136.235 -8.464 1.00177.67 C

ANISOU 2235 C ILE B 81 24268 20944 22293 -681 2839 -2076 C

ATOM 2236 O ILE B 81 19.397 136.426 -9.404 1.00172.84 O

ANISOU 2236 O ILE B 81 23748 20241 21682 -484 2919 -2083 O

ATOM 2237 N SER B 82 20.209 136.989 -7.367 1.00177.95 N

ANISOU 2237 N SER B 82 24431 21008 22173 -739 2811 -2186 N

ATOM 2238 CA SER B 82 19.342 138.138 -7.171 1.00171.69 C

ANISOU 2238 CA SER B 82 23911 20144 21178 -567 2874 -2325 C

ATOM 2239 CB SER B 82 19.709 138.820 -5.865 1.00172.04 C

ANISOU 2239 CB SER B 82 24066 20242 21061 -673 2805 -2424 C

ATOM 2240 OG SER B 82 19.864 137.855 -4.841 1.00169.15 O

ANISOU 2240 OG SER B 82 23449 20065 20756 -852 2692 -2342 O

ATOM 2241 C SER B 82 19.530 139.104 -8.316 1.00170.51 C

ANISOU 2241 C SER B 82 24031 19696 21058 -530 2979 -2403 C

ATOM 2242 O SER B 82 18.762 139.097 -9.274 1.00163.16 O

ANISOU 2242 O SER B 82 23180 18686 20127 -321 3064 -2404 O

ATOM 2243 N SER B 83 20.563 139.930 -8.216 1.00174.06 N

ANISOU 2243 N SER B 83 24620 19982 21532 -745 2969 -2465 N

ATOM 2244 CA SER B 83 20.925 140.821 -9.307 1.00177.76 C

ANISOU 2244 CA SER B 83 25372 20149 22021 -755 3071 -2538 C

ATOM 2245 CB SER B 83 21.083 142.254 -8.805 1.00183.01 C

ANISOU 2245 CB SER B 83 26367 20668 22502 -829 3059 -2696 C

ATOM 2246 OG SER B 83 21.993 142.978 -9.622 1.00185.15 O

ANISOU 2246 OG SER B 83 26951 20629 22769 -828 3166 -2768 O

ATOM 2247 C SER B 83 22.220 140.374 -9.967 1.00178.00 C

ANISOU 2247 C SER B 83 25271 20081 22281 -974 3085 -2444 C

ATOM 2248 O SER B 83 23.286 140.457 -9.353 1.00178.60 O

ANISOU 2248 O SER B 83 25293 20158 22410 -1243 3020 -2446 O

ATOM 2249 N VAL B 84 22.138 139.908 -11.213 1.00156.89 N

ANISOU 2249 N VAL B 84 22543 17332 19735 -850 3167 -2360 N

ATOM 2250 CA VAL B 84 23.338 139.485 -11.921 1.00150.77 C

ANISOU 2250 CA VAL B 84 21626 16490 19171 -1010 3192 -2250 C

ATOM 2251 CB VAL B 84 23.048 139.049 -13.342 1.00144.77 C

ANISOU 2251 CB VAL B 84 20858 15635 ' 18512 -804 3285 -2170 C

ATOM 2252 CGl VAL B 84 23.943 137.892 -13.713 1.00143.81 C

ANISOU 2252 CGl VAL B 84 20564 15484 18594 -951 3305 -2041 C

ATOM 2253 CG2 VAL B 84 21.604 138.682 -13.490 1.00152.54 C

ANISOU 2253 CG2 VAL B 84 21667 16817 19475 -601 3228 -2109 C

ATOM 2254 C VAL B 84 24.247 140.675 -12.060 1.00159.40 C

ANISOU 2254 C VAL B 84 22940 17350 20273 -1210 3252 -2321 C

ATOM 2255 O VAL B 84 23.793 141.771 -12.392 1.00161.61 O

ANISOU 2255 O VAL B 84 23551 17407 20445 -1115 3344 -2427 O

ATOM 2256 N LYS B 85 25.529 140.472 -11.797 1.00184.95 N

ANISOU 2256 N LYS B 85 25994 20645 23633 -1490 3198 -2260 N

ATOM 2257 CA LYS B 85 26.526 141.438 -12.220 1.00188.04 C

ANISOU 2257 CA LYS B 85 -26534 20832 24079 -1727 3259 -2290 C

ATOM 2258 CB LYS B 85 27.564 141.703 -11.121 1.00186.27 C

ANISOU •2258 CB LYS B 85 26197 20721 23857 -2048 3132 -2319 C

ATOM 2259 CG LYS B 85 27.058 142.645 -10.026 1.00191.34 C

ANISOU 2259 CG LYS B 85 27096 21319 24287 -2075 3057 -2483 C

ATOM 2260 CD LYS B 85 28.191 143.230 -9.183 1.00202.79 C

ANISOU 2260 CD LYS B 85 28530 22780 25741 -2430 2948 -2533 C

ATOM 2261 CE LYS B 85 27.656 144.281 -8.205 1.00208.44 C ANISOU 2261 CE LYS B 85 29604 23366 26226 -2450 2889 -2710 C

ATOM 2262 NZ LYS B 85 28.517 144.454 -6.997 1.00210.25 N

ANISOU 2262 NZ LYS B 85 29758 23698 26431 -2744 2722 -2761 N

ATOM 2263 C LYS B 85 27.143 140.882 -13.499 1.00181.06 C

ANISOU 2263 C LYS B 85 25527 19880 23389 -1730 3363 -2153 C

ATOM 2264 O LYS B 85 27.088 139.683 -13.745 1.00178.65 O

ANISOU 2264 O LYS B 85 24965 19727 23187 -1616 3343 -2028 O

ATOM 2265 N ALA B 86 27.699 141.749 -14.329 1.00164.61 N

ANISOU 2265 N , ALA B 86. 23645 17558 21341 -1854 3477 -2174 N

ATOM 2266 CA ALA B 86 28.143 141.320 -15.643 1.00162.78 C

ANISOU 2266 CA ALA B 86 23348 17235 21267 -1811 3604 -2049 C

ATOM 2267 CB ALA B 86 28.438 142.512 -16.518 1.00180.48 C

ANISOU 2267 CB ALA B 86 25861 19199 23516 -1980 3734 -2089 C

ATOM 2268 C ALA B 86 29.346 140.399 -15.588 1.00157.08 C

ANISOU 2268 C ALA B 86 22222 16749 20711 -1931 3542 -1891 C

ATOM 2269 O ALA B 86 29.748 139.850 -16.614 1.00156.63 O

ANISOU 2269 O ALA B 86 22045 16700 20768 -1791 3612 -1765 O

ATOM 2270 N GLU B 87 29.934 140.243 -14.405 1.00158.41 N

ANISOU 2270 N GLU B 87 22196 17109 20883 -2172 3408 -1900 N

ATOM •2271 CA GLU B 87 31.009 139.266 -14.230 1.00160.71 C

ANISOU 2271 CA GLU B 87 22107 17644 21312 -2278 3341 -1757 C

ATOM 2272 CB GLU B 87 32.237 139.864 -13.522 1.00165.95 C

ANISOU 2272 CB GLU B 87 22658 18366 22031 -2649 ' 3298 -1761 C

ATOM . 2273 CG GLU B 87 31.986 140.418 -12.134 1.00174.03 C

ANISOU 2273 CG GLU B 87 23751 19441 22931 -2848 3153 -1904 C

ATOM 2274 CD GLU B 87 31.304 141.770 -12.161 1.00178.20 C

ANISOU 2274 CD GLU B 87 24705 19698 23306 -2830 3200 -2068 C

ATOM 2275 OEl GLU B 87 31.244 142.375 -13.253 1.00177.46 O

ANISOU 2275 OEl GLU B 87 24856 19350 23220 -2760 3356 -2075 O

ATOM 2276 OE2 GLU B 87 30.829 142.227 -11.092 1.00182.52 O

ANISOU 2276 0E2 GLU B 87 25356 20284 23710 -2867 3082 -2190 O

ATOM 2277 C GLU B 87 30.494 137.999 -13.534 1.00161.37 C

ANISOU 2277 C GLU B 87 21967 17986 21362 -2141 3197 -1720 C

ATOM 2278 O GLU B 87 31.272 137.153 -13.084 1.00159.18 O

ANISOU 2278 O GLU B 87 21394 17940 21146 -2245 3096 -1636 O

ATOM 2279 N ASP B 88 29.169 137.893 -13.454 1.00173.73 N

ANISOU 2279 N ASP B 88 23681 19511 22818 -1904 3192 -1782 N

ATOM 2280 CA ASP B 88 28.499 13 ' 6.648 τl3.103 1.00171.11 C

ANISOU 2280 CA ASP B 88 23165 19382 22466 -1727 3094 -1719 C

ATOM 2281 CB ASP B 88 27.046 136.907 -12.703 1.00170.38 C

ANISOU 2281 CB ASP B 88 23264 19255 22217 -1533 3084 -1825 C

ATOM 2282 CG ASP B 88 26.916 137.544 -11.338 1.00171.57 C

ANISOU 2282 CG ASP B 88 23477 19488 22223 -1663 2988 -1949 C

ATOM 2283 ODl ASP B 88 27.937 137.619 -10.618 1.00171.88 O

ANISOU 2283 ODl ASP B 88 23366 19652 22290 -1894 2895 -1942 O

ATOM 2284 0D2 ASP B 88 25.786 137.958 -10.988 1.00168.02 O

ANISOU 2284 0D2 ASP B 88 23227 18990 21624 -1515 3002 -2052 O

ATOM 2285 C ASP B 88 28.515 135.746 -14.331 1.00168.71 C

ANISOU 2285 C ASP B 88 22751 19067 22284 -1541 3154 -1570 C

ATOM 2286 O ASP B 88 28.019 134.617 -14.298 1.00163.97 O

ANISOU 2286 O ASP B 88 21999 18610 21691 -1396 3078 -1488 O

ATOM 2287 N LEU B 89 29.072 136.263 -15.425 1.00163.29 N

ANISOU 2287 N LEU B 89 22164 18197 21683 -1544 3291 -1535 N

ATOM 2288 CA LEU B 89 29.168 135.507 -16.663 1.00155.29 C

ANISOU 2288 CA LEU B 89 21082 17146 20776 -1358 3359 -1397 C

ATOM 2289 CB LEU B 89 29.782 136.347 -17.776 1.00159.69 C

ANISOU 2289 CB LEU B 89 21820 17461 21395 -1365 3535 -1388- C

ATOM 2290 CG LEU B 89 30.259 135.492 -18.951 1.00162.34 C

ANISOU 2290 CG LEU B 89 22081 17756 21846 -1206 3623 -1233 C

ATOM 2291 CDl LEU B 89- 29.106 135.137 -19.879 1.00162.15 C

ANISOU 2291 CDl LEU B 89 22147 17667 21795 -875 3613 -1211 C

ATOM 2292 CD2 LEU B 89 31.360 136.201 -19.709 1.00172.29 C

ANISOU 2292 CD2 LEU B 89 23513 18794 23155 -1279 3804 -1230 C

ATOM 2293 C LEU B 89 30.044 134.312 -16.424 1.00152.76 C

ANISOU 2293 C LEU B 89 20443 17055 20542 -1427 3272 -1255 C

ATOM 2294 O LEU B 89 31.217 134.461 -16.080 1.00148.38 O

ANISOU 2294 O LEU B 89 19745 16585 20046 -1649 3271 -1222 O

ATOM 2295 N ALA B 90 29.473 133.130 -16.606 1.00165.89 N

ANISOU 2295 N ALA B 90 22003 18824 22204 -1233 3192 -1173 N

ATOM 2296 CA ALA B 90 30.214 131.898 -16.406 1.00165.61 C

ANISOU 2296 CA ALA B 90 21704 18991 22228 -1231 3105 -1030 C

ATOM 2297 CB ALA B 90 30.768 131.841 -15.002 1.00159.63 C

ANISOU 2297 CB ALA B 90 20757 18462 21433 -1460 2978 -1060 C

ATOM 2298 C ALA B 90 29.344 130.686 -16.664 1.00161.05 C

ANISOU 2298 C ALA B 90 21114 18448 21630 -986 3029 -953 C

ATOM 2299 O ALA B 90 28.295 130.772 -17.301 1.00157.59 ' O

ANISOU 2299 O ALA B 90 20853 17851 21172 -795 3078 ^980 O ATOM 2300 N VAL B 91 29.798 129.546 -16.165 1.00150.70 N

ANISOU 2300 N VAL B 91 19600 17345 20316 -993 2903 -858 N

ATOM 2301 CA VAL B 91 29.009 128.335 -16.216 1.00148.22 C

ANISOU 2301 CA VAL B 91 19278 17074 19964 -810 2803 -790 C

ATOM 2302 ■CB VAL B 91 29.694 127.279 -17.050 1.00142.54 C

ANISOU 2302 CB VAL B 91 18524 16327 19308 -625 2807 -635 C

ATOM 2303 CGl VAL B 91 29.328 125.910 -16.562 1.00138.69 C

ANISOU 2303 CGl VAL B 91 17941 15983 18770 -541 2648 -536 C

ATOM 2304 CG2 VAL B 91 29.268 127.442 -18.457 1.00152.58 C

ANISOU 2304 CG2 VAL B 91 20005 17359 20608 -425 2908 -645 C

ATOM 2305 C VAL B 91 28.840 127.816 -14.810 1.00153.12 C

ANISOU 2305 C VAL B 91 19758 17916 20504 -915 2651 -797 C

ATOM 2306 O VAL B 91 ' 29.799 127.815 -14.035 1.00150.80 O

ANISOU 2306 O VAL B 91 19303 17786 20210 -1073 2598 -785 O

ATOM 2307 N TYR B 92 27.624 127.384 -14.477 1.00143.22 N

ANISOU 2307 N TYR B 92 18565 16673 19180 -829 2584 -817 N

ATOM 2308 CA TYR B 92 27.319 126.914 -13.127 1.00133.23 C

ANISOU 2308 CA TYR B 92 17202 15599 17822 -926 2461 -836 C

ATOM 2309 CB TYR B 92 26.140 127.706 -12.541 1.00126.65 C

ANISOU 2309 CB TYR B 92 16485 14736 16899 -939 2484 -967 C

ATOM 2310 CG TYR B 92 26.533 129.147 -12.363 1.00132.33 C

ANISOU 2310 CG TYR B 92 17302 15366 17613 -1059 2580 -1102 C

ATOM 2311 CDl TYR B 92 25.912 130.167 -13.063 1.00132.52 C

ANISOU 2311 CDl TYR B 92 17526 15192 17632 -969 2697 -1190 C

ATOM 2312 CEl TYR B 92 26.330 131.505 -12.908 1.00138.66 C

ANISOU 2312 CEl TYR B 92 18430 15863 18390 -1087 2781 -1312 C

ATOM 2313 CZ TYR B 92 27.390 131.806 -12.059 1.00142.80 C

ANISOU 2313 CZ TYR B 92 18862 16483 18912 -1312 2738 -1345 C

ATOM 2314 OH TYR B 92 27.835 133.093 -11.872 1.00144.16 O

ANISOU 2314 OH TYR B 92 19176 16537 19060 -1454 2804 -1464 O

ATOM 2315 CE2 TYR B 92 28.018 130.803 -11.375 1.00143.76 , C

ANISOU 2315 CE2 TYR B 92 18762 16817 19045 -1398 2618 -1263 C

ATOM 2316 CD2 TYR B 92 27.600 129.482 -11.539 1.00140.97 C

ANISOU 2316 CD2 TYR B 92 18300 16564 18700 -1263 2545 -1142 C

ATOM 2317 C TYR B 92 27.134 125.401 -13.054 1.00125.22 C

ANISOU 2317 C TYR B 92 16113 14678 16787 -823 2341 -701 C

ATOM 2318 O TYR B 92 26.132 124.859 -13.504 1.00123.46 O

ANISOU 2318 O TYR B 92 15980 14362 16568 -672 2331 -655 O

ATOM 2319 N TYR B 93 28.140 124.723 -12.522 1.00122.54 N

ANISOU 2319 N TYR B 93 15623 14514 16424 -903 2247 -638 N

ATOM 2320 CA TYR B 93 28.026 123.303 -12.293 1.00126.47 C

ANISOU 2320 CA TYR B 93 16072 15106 16874 -822 2121 -515 C

ATOM 2321 CB TYR B 93 29.348 122.596 -12.533 1.00126.80 C

ANISOU 2321 CB TYR B 93 16005 15230 16945 -783 2082 -403 C

ATOM 2322 CG TYR B 93 29.975 122.925 -13.840 1.00126.86 C

ANISOU 2322 CG TYR B 93 16049 15100 17052 -678 2192 -362 C

ATOM 2323 CDl TYR B 93 29.416 " 122.510 -15.031 1.00127.45 C

ANISOU 2323 CDl TYR B 93 16256 15010 17158 -477 2209 -284 C

ATOM 2324 CEl TYR B 93 30.013 122.827 -16.233 1.00132.27 C

ANISOU 2324 CEl TYR B 93 16913 15494 17851 -363 2319 -242 C

ATOM 2325 CZ TYR B 93 31.192 123.568 -16.240 1.00134.78 C

ANISOU 2325 CZ TYR B 93 17128 15858 18226 -472 2420 -271 C

ATOM 2326 OH TYR B 93 31.848 123.927 -17.405 1.00137.59 O

ANISOU 2326 OH TYR B 93 17518 ' 16099 18660 -371 2546 -219 O

ATOM 2327 CE2 TYR B 93 31.745 123.971 -15.064 1.00135.02 C

ANISOU 2327 CE2 TYR B 93 17018 16051 18232 -694 2394 -348 C

ATOM 2328 CD2 TYR B 93 31.140 123.646 -13.880 1.00132.24 C

ANISOU 2328 CD2 TYR B 93 16636 15816 17793 -785 2277 -398 C

ATOM 2329 C TYR B 93 27.620 123.080 -10.856 1.00129.22 C

ANISOU 2329 C TYR B 93 16355 15627 17114 -940 2025 -550 C

ATOM 2330 O TYR B 93 27.829 123.955 -10.016 1.00129.80 O

ANISOU 2330 O TYR B 93 16386 15778 17155 -1084 2042 -657 O

ATOM 2331 N CYS B 94 27.042 121.907 -10.585 1.00138.81 N

ANISOU 2331 N CYS B 94 17581 16894 18268 -879 1923 -457 N

ATOM 2332 CA CYS B 94 26.724 121.472 -9.231 1.00135.25 C

ANISOU 2332 CA CYS B 94 17069 16615 17703 -975 . 1828 -459 C

ATOM 2333 CB CYS B 94 25.220 121.406 -9.024 1.00137.26 C

ANISOU 2333 CB CYS B 94 17397 16852 17903 -959 1822 -467 C

ATOM 2334 SG CYS B 94 24.427 120.055 -9.905 1.00143.14 S

ANISOU 2334 SG CYS B 94 18248 17452 18686 -805 1779 -338 S

ATOM 2335 C CYS B 94 27.320 120.099 -9.010 1.00129.36 C

ANISOU 2335 C CYS B 94 16275 15962 16914 -927 1710 -326 C

ATOM 2336 O CYS B 94 27.315 119.265 -9.905 1.00129.94 O

ANISOU 2336 O CYS B 94 16404 15943 17026 -793 1689 -222 O

ATOM 2337 N GLN B 95 27.847 119.880 -7.815 1.00125.34 N

ANISOU 2337 N GLN B 95 15682 15630 16310 -1020 1631 -333 N

ATOM 2338 CA GLN B 95 28.422 118.605 -7.461 1.00128.60 C ANISOU 2338 CA GLN B 95 16067 16141 16656 -964 1514 -215 C

ATOM 2339 CB GLN B 95 29.832 118.785 -6.956 1.00127 .84 C

ANISOO 2339 CB GLN B 95 15830 16188 16557 -1005 1491 -238 C

ATOM 2340 CG GLN B- 95 30.220 117.736 -5.965 1.00129 .04 C

ANISOU 2340 CG GLN B- 95 15947 16493 16588 -963 1358 -149 C

ATOM 2341 CD GLN B 95 31.691 117.759 -5.690 1.00126 .37 C

ANISOU 2341 CD GLN B 95 15446 16329 16240 -1007 1328 -185 C

ATOM 2342 OEl GLN B 95 32.436 118.427 -6.394 1.00131 .92 O

ANISOO 2342 OEl GLN B 95 16059 17021 17042 -1062 1408 -250 O

ATOM 2343 NE2 GLN B 95 32.131 117.035 -4.667 1.00129 97 N

ANISOU 2343 NE2 GLN B 95 15861 16951 16570 -988 1211 -144 N

ATOM 2344 C GLN B 95 27.631 118.032 -6.337 1.00122. 65 C

ANISOO 2344 C GLN B 95 15327 15497 15776 -1030 1434 -198 C

ATOM 2345 O GLN B 95 27.109 118.769 -5.526 1.00127. 15 O

ANISOO 2345 O GLN B 95 15848 16165 16299 -1145 1452 -298 O

ATOM 2346 N GLN B 96 27.519 116.716 -6.293 1.00141. 47 N

ANISOU 2346 N GLN B 96 17796 17860 18097 -960 1345 -70 N

ATOM 2347 CA GLN B 96 27.138 116.051 -5.065 1.00142. 62 C

ANISOO 2347 CA GLN B 96 17949 18138 18103 -1020 1254 -27 C

ATOM 23.48 CB GLN B 96 26.085 114.974 -5.309 1.00142. 14 C

ANISOU 2348 CB GLN B 96 18024 17990 17991 -979 1184 106 C

ATOM 2349 CG GLN B 96 26.577 113.775 -6.101 1.00143. 61 C

ANISOU 2349 CG GLN B 96 18311 18091 18162 -833 1094 237 C

ATOM 2350 CD GLN B 96 27.555 112.910 -5.328 1.00144. 74 C

ANISOU 2350 CD GLN B 96 18445 18375 18174 -798 990 293 C

ATOM 2351 OEl GLN B 96 27.356 112.620 -4.147 1.00146. 71 O

ANISOU 2351 OEl GLN B 96 18675 18755 18314 -889 951 283 O

ATOM 2352 NE2 GLN B 96 28.625 112.500 -5.994 1.00142. 14 N

ANISOO 2352 NE2 GLN B 96 18136 18027 17844 -646 949 354 N

ATOM 2353 C GLN B 96 28.423 115.436 -4.546 1.00144. 45 C

ANISOU 2353 C GLN B 96 18113 18500 18270 -982 1173 C

ATOM 2354 O GLN B 96 29.249 114.963 -5.330 1.00142. 95 O

ANISOU 2354 O GLN B 96 17928 18269 18116 -861 1152 67 O

ATOM 2355 N TYR B 97 28.622 115.466 -3.236 1.00136. 94 N

ANISOU 2355 N TYR B 97 17095 17718 17218 -1068 1130 -50 N

ATOM 2356 CA TYR B 97 29.794 114.820 -2.686 1.00136. 32 C

ANISOU 2356 CA TYR B 97 16958 17784 17054 -1015 1034 -15 C

ATOM 2357 CB TYR B 97 30.814.115.824 -2.198 1.00140. 21 C

ANISOU 2357 CB TYR B 97 17284 18411 17577 -1094 1053 -142 C

ATOM 2358 CG TYR B 97 30.285 116.930 -1.326 1.00143. 22 C

ANISOU 2358 ' CG TYR B 97 17633 18834 17951 -1246 1103 -281 C

ATOM 2359 CDl TYR B 97 30.693 117.036 0.000 1.00147. 19 C

ANISOO 2359 CDl TYR B 97- 18083 19506 18336 -1314 1032 -344 C

ATOM 2360 CEl TYR B 97 30.249 118.067 0.800 1.00150. 30 C

ANISOU 2360 CEl TYR B 97 18470 19930 18707 -1433 1073 -473 C

ATOM 2361 CZ TYR B 97 29.384 119.010 0.275 1.00151. 17 C

ANISOU 2361 CZ TYR B 97 18626 19904 18907 -1479 1189 -540 C

ATOM 2362 OH TYR B 97 28.942 120.034 1.086 1.00149. 99 O

ANISOU 2362 OH TYR B 97 18497 19780 18711 -1569 1227 -669 O

ATOM 2363 CE2 TYR B 97 28.969 118.929 -1.046 1.00140. 96 C

ANISOU 2363 CE2 TYR B 97 17377 18448 17733 -1413 1262 -482 C

ATOM 2364 CD2 TYR B 97 29.427 117.899 -1.834 1.00138. 28 C

ANISOU 2364 CD2 TYR B 97 17,042 18076 17422 -1301 1217 -354 C

ATOM 2365 C TYR B 97 29.394 113.904 -1.580 1.00138. 01 C

ANISOU 2365 C TYR B 97 17248 18088 17101 -1024 937 51 C

ATOM 2366 O TYR B 97 30.196 113.606 -0.694 1.00139. 65 O

ANISOU 2366 O TYR B 97 17408 18449 17204 -999 .855 49 O

ATOM 2367 N PHE B 98 28.143 113.460 -1.648 1.00125. 74 N

ANISOU 2367 N PHE B 98 15812 16443 15520 -1059 948 112 N

ATOM 2368 CA PHE B 98 27.621 112.500 -0.705 1.00134. 44 C

ANISOU 2368 CA PHE B 98 17010 17606 16465 -1087 872 194 C

ATOM 2369 CB PHE B 98 26.197 112.148 -1.060 1.00133. 69 C

ANISOO 2369 CB PHE B 98 17024 17386 16388 -1139 901 271 C

ATOM 2370 CG PHE B 98 25.489 111.396 0.010 1.00131. 15 C

ANISOU 2370 CG PHE B 98 16773 17139 15919 -1221 862 341 C

ATOM 2371 CDl PHE B 98 24.160 111.649 0.289 1.00131. 51 C

ANISOO 2371 CDl PHE B 98 16793 17209 15965 -1336 939 323 C

ATOM 2372 CEl PHE B 98 23.499 110.949 1.274 1.00134. 78 C

ANISOU 2372 CEl PHE B 98 17263 17706 16242 -1416 916 402 C

ATOM 2373 CZ PHE B 98 24.170 109.993 2.001 1.00139. 66 C

ANISOU 2373 CZ PHE B 98 17989 18362 16715 -1383 812 493 C

ATOM 2374 CE2 PHE B 98 25.497 109.736 1.734 1.00132. 93 C

ANISOU 2374 CE2 PHE B 98 17175 17481 15851 -1253 727 502 C

ATOM 2375 CD2 PHE B 98 26.150 110.437 0.749 1.00131. 34 C

ANISOU 2375 CD2 PHE B 98 16893 17220 15792 -1173 754 429 C

ATOM 2376 C PHE B 98 28.497 111.258 -0.711 1.00134. 96 C

ANISOU 2376 C PHE B 98 17164 17695 16419 -960 751 305 C ATOM 2377 O PHE B 98 29.297 111.053 0.191 1.00128.60 O

ANISOO 2377 O PHE B 98 16321 17043 15497 -938 686 286 O

ATOM 2378 N ARG B 99 28.366 110.422 -1.727 1.00132 .75 N

ANISOU 2378 N ARG' B 99 17019 17262 16159 -858 712 420 N

ATOM 2379 CA ARG B 99 29.296 109.300 -1.846 1.00138 .69 C

ANISOU 2379 CA ARG B 99 17874 18026 16794 -697 598 521 C

ATOM 2380 CB ARG B 99 28.612 107.976 -1.507 1.00141 .22 C

ANISOU 2380 CB ARG B 99 18424 18265 16968 -700 505 660 C

ATOM 2381 CG ARG B 99 29.574 106.806 -1.407 1.00141 .04 C

ANISOU 2381 CG ARG B 99 18543 18262 16784 -518 380 757 C

ATOM 2382 CD ARG B 99 30.687 107.120 -0.445 1.00139 .55 C

ANISOU 2382 CD ARG B 99 18208 18305 16510 -475 356 676 C

ATOM 2383 NE ARG B 99 31.733 106.106 -0.444 1.00143 .12 N

ANISOU 2383 NE ARG B 99 18780 18800 16799 -266 239 761 N

ATOM 2384 CZ ARG B 99 32.996 106.353 -0.765 1.00146. 74 C

ANISOU 2384 CZ ARG B 99 19119 19366 17271 -101 224 736 C

ATOM 2385 NHl ARG B 99 33.363 107.589 -1.118 1.00146 04 N

ANISOU 2385 NHl ARG B 99 18790 19337 17361 -150 321 632 N

ATOM 2386 NH2 ARG B 99 33.888 105.367 -0.731 1.00147. 08 N

ANISOU 2386 NH2 ARG B 99 19284 19463 17137 115 114 819 N

ATOM 2387 C ARG B 99 29.956 109.253 -3.226 1.00137, 55 C

ANISOU 2387 C ARG B 99 17742 17774 16746 -537 607 557 C

ATOM 2388 O ARG B 99 29.277 109.076 -4.240 1.00130. 82 O

ANISOU 2388 O ARG B 99 16998 16734 15973 -516 628 611 O

ATOM 2389 N TYR B 100 31.277 109.424 -3.255 1.00135, 69 N

ANISOU 2389 N TYR B 100 17389 17668 16500 -421 591 530 N

ATOM 2390 CA TYR B 100 31.958 109.681 -4.502 1.00134. 29 C

ANISOU 2390 CA TYR B 100 17170 17424 16431 -284 635 547 C

ATOM 2391 CB TYR B 100 31.524 108.652 -5.490 1.00130. 32 C

ANISOU 2391 CB TYR B 100 16910 16712 15892 -144 578 684 C

ATOM 2392 CG TYR B 100 31.989 107.300 -5.166 1.00134. 62 C

ANISOU 2392 CG TYR B 100 17632 17282 16235 11 439 800 C

ATOM 2393 CDl TYR B 100 33.247 107.108 -4.657 1.00134. 36 C

ANISOU 2393 CDl TYR B 100 17501 17450 16101 151 392 798 C

ATOM 2394 CEl TYR B 100 33.704 105.843 -4.386 1.00145. 11 C

ANISOU 2394 CEl TYR B 100 19049 18834 17252 328 261 904 C

ATOM 2395 CZ TYR B 100 32.891 104.750 -4.635 1.00148. 71 C

ANISOU 2395 CZ TYR B 100 19813 19088 17601 345 174 1017 C

ATOM 2396 OH TYR B 100 33.360 103.485 -4.344 1.00155. 98 O

ANISOU 2396 OH TYR B 100 20959 20013 18295 528 41 1122 O

ATOM 2397 CE2 TYR B 100 31.627 104.928 -5.159 1.00140. 43 C

ANISOU 2397 CE2 TYR B 100 18853 17840 16665 179 215 1025 C

ATOM 2398 CD2 TYR B 100 31.190 106.197 -5.422 1.00131. 04 C

ANISOU 2398 CD2 TYR B 100 17455 16651 15682 24 348 915 C

ATOM 2399 C TYR B 100 31.552 111.040 -5.068 1.00126. 39 C

ANISOU 2399 C TYR B 100 16045 16357 15622 -413 774 439 C

ATOM 2400 O TYR B 100 30.467 111.538 -4.792 1.00127. 10 O

ANISOU 2400 O TYR B 100 16148 16397 15749 -567 820 385 O

ATOM 2401 N ARG B 101 32.399 111.624 -5.902 1.00131. 23 N

ANISOU 2401 N ARG B 101 16547 16968 16345 -337 845 415 N

ATOM 2402 CA ARG B 101 32.126 112.955 -6.429 1.00131. 02 C

ANISOU 2402 CA ARG B 101 16417 16875 16491 -451 981 308 C

ATOM 2403 CB ARG B 101 33.401 113.802 -6.403 1.00128. 73 C

ANISOU 2403 CB ARG B 101 15907 16739 16267 -469 1035 236 C

ATOM 2404 CG ARG B 101 33.846 114.221 -5.004 1.00128. 18 C

ANISOU 2404 CG ARG B 101 15682 16893 16128 -607 988 140 C

ATOM 2405 CD ARG B 101 34.077 113.009 -4.130 1.00136. 50 C

ANISOU 2405 CD ARG B 101 16803 18066 16993 -530 848 209 C

ATOM 2406 NE ARG B 101 33.399 113.159 -2.856 1.00129. 59 N

ANISOU 2406 NE ARG B 101 15922 17262 16053 -693 823 124 N

ATOM 2407 CZ ARG B 101 33.819 113.982 -1.911 1.00136. 79 C

ANISOU 2407 CZ ARG B 101 16679 18357 16939 -798 800 17 C

ATOM 2408 NHl ARG B 101 34.909 114.696 -2.132 1.00137. 52 N

ANISOU 2408 NHl ARG B 101 16592 18589 17069 -771 793 -11 N

ATOM 2409 NH2 ARG B 101 33.156 114.088 -0.760 1.00140. 54 N

ANISOU 2409 NH2 ARG B 101 17176 18881 17342 -924 780 -57 N

ATOM 2410 C ARG B 101 31.537 112.904 -7.836 1.00126. 35 C

ANISOU 2410 C ARG B 101 . 15957 16052 16000 -354 1038 362 C

ATOM 2411 O ARG B 101 31.981 112.133 -8.682 1.00126. 06 O

ANISOU 2411 O ARG B 101 16027 15939 15932 -164 994 473 O

ATOM 2412 N THR B 102 30.549 113.746 -8.095 1.00124. 82 N

ANISOU 2412 N THR B 102 15766 15746 15915 -466 1133 280 N

ATOM 2413 CA THR B 102 29.804 113.639 -9.337 1.00122. 07 C

ANISOU 2413 CA THR B 102 15555 15178 15649 -371 1174 325 C

ATOM 2414 CB THR B 102 28.780 112.506 -9.190 1.00123. 99 C

ANISOU 2414 CB THR B 102 15989 15316 15804 -345 1065 425 C

ATOM 2415 OGl THR B 102 29.249 111.358 -9.902 1.00125. 17 O ANISOU 2415 OGl THR B 102 16261 15438 15859 -160 960 557 O

ATOM 2416 CG2 THR B 102 27.434 112.897 -9.715 1.00130.29 C

ANISOU 2416 CG2 THR B 102 16894 15915 16696 ' -338 1110 419 C

ATOM 2417 C THR B 102 29.172 114.971 -9.797 1.00121.67 C

ANISOU 2417 C THR B 102 15464 15034 15731 -466 1309 208 C

ATOM 2418 O THR B 102 28.226 115.458 -9.189 1.00125.33 O

ANISOU 2418 O THR B 102 15924 15508 16188 -601 1329 137 O

ATOM 2419 N PHE B 103 29.701 115.550 -10.878 1.00127.73 N

ANISOU 2419 N PHE B 103 16-214 15711 16606 -376 1404 196 . N

ATOM 2420 CA PHE B 103 29.381 116.927 -11.273 1.00125.10 C

ANISOU 2420 CA PHE B 103 15845 15297 16391 -454 1544 78 C

ATOM 2421 CB PHE B 103 30.539 117.523 -12.051 1.00125.41 C

ANISOU 2421 CB PHE B 103 15802 15330 16519 -392 1643 73 C

ATOM 2422 CG PHE B 103 31.566 118.182 -11.190 1.00128.82 C

ANISOO 2422 CG PHE B 103 16041 15959 16947 -533 1660 4 C

ATOM 2423 CDl PHE B 103 32.848 117.683 -11.112 1.00129.53 C

ANISOU 2423 CDl PHE B 103 160-14 16211 16990 -467 1605 80 C

ATOM 2424 CEl PHE B 103 33.785 118.288 -10.328 1.00127.95 C

ANISOU 2424 CEl PHE B 103 15621 16205 16788 -606 1607 15 C

ATOM 2425 CZ PHE B 103 33.458 119.393 -9.608 1.00128.83 C

ANISOU 2425 CZ PHE B 103 15681 16326 16941 -817 1660 -130 C

ATOM 2426 CE2 PHE B 103 32.194 119.903 -9.674 1.00129.61 C

ANISOU 2426 CE2 PHE B 103 15916 16254 17074 -867 1723 -206 C

ATOM 2427 CD2 PHE B 103 31.252 119.302 -10.460 1.00127.97 C

ANISOU 2427 CD2 PHE B 103 15873 15878 16873 -725 1725 " -139 C

ATOM 2428 C PHE B 103 28.124 117.105 -12.098 1.00126.58 C

ANISOU 2428 C PHE B 103 16179 15285 16631 -404 1581 69 C

ATOM 2429 O PHE B 103 27.640 116.179 -12.719 1.00128.32 ' O

ANISOU 2429 O PHE B 103 16536 15389 16832 -278 1510 168 O

ATOM 2430 N GLY B 104 27.613 118.324 -12.132 1.00140.00 N

ANISOU 2430 N GLY B 104 17860 16945 18389 -499 1685 -56 N

ATOM 2431 CA GLY B 104 26.404 118.601 -12.882 1.00142.85 C

ANISOU 2431 CA GLY B 104 18342 17138 18797 -444 1730 -84 C

ATOM 2432 C GLY B 104 26.645 118.803 -14.367 1.00148.72 C

ANISOU 2432 C GLY B 104 19169 17700 19631 -282 1813 -63 C

ATOM 2433 O GLY B 104 27.790 118.884 -14.824 1.00147.54 O

ANISOU 2433 O GLY B 104 18973 17566 19518 -220 1846 -19 O

ATOM 2434 N GLY B 105 25.553 118.888 -15.122 1.00147.43 N

ANISOU 2434 N GLY B 105 19125 17376 19514 -206 1849 -92 N

ATOM 2435 CA GLY B 105 25.626 119.150 -16.547 1.00144.82 C

ANISOU 2435 CA GLY B 105 18909 16853 19264 -28 1922 -70 C

ATOM 2436 C GLY B 105 26.137 120.547 -16.817 1.00144.98 C

ANISOU 2436 C GLY B 105 18898 16831 19356 -63 2087 -176 C

ATOM 2437 O GLY B 105 26.798 120.800 -17.823 1.00146.99 O

ANISOU 2437 O GLY B 105 19205 16970 19674 61 2172 -145 O

ATOM 2438 N GLY B 106 25.828 121.453 -15.896 1.00148.79 N

ANISOU 2438 N GLY B 106 19312 17403 19817 -230 2133 -296 N

ATOM 2439 CA GLY B 106 26.231 122.841 -15.999 1.00148.18 C

ANISOU 2439 CA GLY B 106 19238 1-7275 19790 -296 2279 -412 C

ATOM 2440 C GLY B 106 25.210 123.661 -16.759 1.00151.18 " C

ANISOU 2440 C GLY B 106 19769 17482 20190 -208 2368 -502 C

ATOM 2441 O GLY B 106 24.615 123.178 -17.721 1.00154.84 O

ANISOU 2441 O GLY B 106 20345 17812 20676 -37 2349 -452 O

ATOM 2442 N THR B 107 24.994 124.897 -16.321 1.00132.86 N

ANISOU 2442 N THR B 107 17468 15160 17852 -311 2457 -638 N

ATOM 2443 CA THR B 107 24.170 125.841 -17.071 1.00136.95 C

ANISOU 2443 CA THR B 107 18150 15505 18381 -205 2563 -733 C

ATOM 2444 CB THR B 107 22.826 126.114 -16.349 1.00134.93 C

ANISOU 2444 CB THR B 107 17916 15318 18032 -223 2535 -828 C

ATOM 2445 OGl THR B 107 22.974 127.187 -15.426 1.00142.32 O

ANISOU 2445 OGl THR B 107 18789 16384 18904 -400 2546 -917 O

ATOM 2446- CG2 THR B 107 22.383 124.902 -15.569 1.00136.78 C

ANISOU 2446 CG2 THR B 107 18074 15669 18229 -202 2391 -734 C

ATOM 2447 C THR B 107 24.980 127.134 -17.379 1.00137.96 C

ANISOU 2447 C THR B 107 18341 15524 18554 -263 2712 -809 C

ATOM 2448 O THR B 107 25.802 127.575 -16.571 1.00131.52 O

ANISOU 2448 O THR B 107 17429 14807 17737 -445 2723 -837 O

ATOM 2449 N LYS B 108 24.781 127.718 -18.560 1.00139.47 N

ANISOU 2449 N LYS B 108 18699 15508 18786 -111 2821 -835 N

ATOM 2450 CA LYS B 108 25.619 128.825 -19.019 1.00138.27 C

ANISOU 2450 CA LYS B 108 18631 15223 18682 -156 2971 -882 C

ATOM 2451 CB LYS B 108 26.042 128.567 -20.462 1.00146.19 C

ANISOU 2451 CB LYS B 108 19738 16045 19761 45 3050 -796 C

ATOM 2452 CG LYS B 108 26.877 129.661 -21.142 1.00157.52 C

ANISOU 2452 CG LYS B 108 21226 17362 21262 ' -9 3212 -792 C

ATOM 2453 CD LYS B 108 27.475 129.176 -22.521 1.00172.17 C

ANISOU 2453 CD LYS B 108 23156 19074 23187 214 3282 -670 C ATOM 2454 CE LYS B 108 26.463 129.197 -23.717 1.00165.58 C

ANISOO 2454 CE LYS B 108 22576 17998 22338 457 3354 -724 C

ATOM 2455 NZ LYS B 108 26.859 128.413 -24.954 1.00139.90 N

ANISOO 2455 NZ LYS B 108 19407 14618 19131 717 3372 -604 N

ATOM 2456 C LYS B 108 24.859 130.133 -18.918 1.00145.85 C

ANISOO 2456 C LYS B 108 19755 16090 19573 -171 3052 -1043 C

ATOM 2457 O LYS B 108 23.726 130.230 -19.379 1.00146.10 O

ANISOO 2457 O LYS B 108 19911 16040 19560 -3 3057 - 1093 O

ATOM 2458 N LEU B 109 25.475 131.140 -18.310 1.00157.02 N

ANISOO 2458 N LEO B 109 21173 17522 20967 -367 3105 - 1125 N

ATOM 2459 CA LEO B 109 24.783 132.399 -18.053 1.00158.16 C

ANISOO 2459 CA LEO B 109 21505 17566 21021 -384 3178 - 1283 C

ATOM 2460 CB LEO B 109 25.078 132.900 -16.640 1.00159.66 C

ANISOO 2460 CB LEO B 109 21623 17893 21146 -626 3128 - 1361 C

ATOM 2461 CG LEU B 109 23.950 133.619 -15.890 1.00161.78 C

ANISOO 2461 CG LEU B 109 22030 18170 21268 -621 3124 -1511 C

ATOM 2462 CDl LEU B 109 ' 24.377 133.945 -14.474 1.00158.64 C

ANISOO 2462 CDl LEU B 109 21527 17937 20811 -851 3040 -1558 C

ATOM 2463 CD2 LEU B 109 23.517 134.882 -16.602 1.00169.48 C

ANISOO 2463 CD2 LEU B 109 23294 18900 22199 -553 3265 -1626 C

ATOM 2464 C LEU B 109 25.183 133.461 -19.061 1.00164.82 C

ANISOO 2464 C LEO B 109 22552 18165 21908 -340 3341 - 1315 C

ATOM 2465 O LEU B 109 26.286 134.003 -18.996 1.00168.25 O

ANISOO 2465 O LEU B 109 22949 18572 22407 -507 3402 -1286 O

ATOM 2466 N GLU B 110 24.274 133.750 -19.988 1.00179.36 N

ANISOO 2466 N GLU B 110 24958 20564 22628 -1221 836 879 N

ATOM 2467 CA GLU B 110 24.490 134.758 -21.023 1.00184.57 C

ANISOO 2467 CA GLU B 110 25749 21219 23162 -1104 928 867 C

ATOM 2468 CB GLO B 110 23.852 134.322 -22.358 1.00185.73 C

ANISOO 2468 CB GLO B 110 25857 21366 23345 -856 836 796 C

ATOM 2469 CG GLU B 110 24.079 132.860 -22.778 1.00185.51 C

ANISOO 2469 CG GLU B 110 25683 21392 23412 -794 697 766 C

ATOM 2470 CD GLU B 110 24.882 132.704 -24.066 1.00191.15 C

ANISOO 2470 CD GLU B 110 26435 22140 24054 -682 707 746 C

ATOM 2471 OEl GLU B 110 24.624 131.727 -24.801 1.00186.40 O

ANISOO 2471 OEl GLU B 110 25771 21548 23506 -552 615 683 O

ATOM 2472 0E2 GLU B 110 25.762 133.545 -24.348 1.00195.16 O

ANISOO 2472 0E2 GLU B 110 27040 22663 24448 -733 811 791 O

ATOM 2473 C GLU B 110 23.884 136.093 -20.595 1.00184.49 C

ANISOO 2473 C GLU B 110 25907 21132 23060 -1151 1098 880 C

ATOM 2474 O GLU B 110 22.674 136.212 -20.414 1.00185.58 O

ANISOO 2474 O GLU B 110 26056 21196 23261 -1115 1117 862 O

ATOM 2475 N ILE B 111 24.724 137.100 -20.425 1.00145.40 N

ANISOO 2475 N ILE B 111 21086 16190 17969 -1233 1234 919 N

ATOM 2476 CA ILE B 111 24.209 138.440 -20.265 1.00142.09 C

ANISOO 2476 CA ILE B 111 20834 15686 17467 -1258 1422 927 C

ATOM 2477 CB ILE B 111 25.306 139.407 -19.839 1.00141.69 C

ANISOO 2477 CB ILE B 111 20919 15653 17264 -1455 1572 979 C

ATOM 2478 CGl ILE B 111 26.044 138.861 -18.618 1.00141.64 C

ANISOO 2478 CGl ILE B 111 20856 15697 17265 -1725 1529 1032 C

ATOM 2479 CDl ILE B 111 27.501 139.287 -18.542 1.00144.22 C

ANISOO 2479 CDl ILE B 111 21293 16074 17431 -1953 1640 1105 C

ATOM 2480 CG2 ILE B 111 24.720 140.801 -19.595 1.00145.11 C

ANISOO 2480 CG2 ILE B 111 21533 15980 17624 -1486 1796 981 C

ATOM 2481 C ILE B 111 23.685 138.900 -21.617 1.00148.70 C

ANISOO 2481 C ILE B 111 21712 16502 18284 -1015 1443 899 C

ATOM 2482 O ILE B 111 24.173 138.453 -22.660 1.00151.77 O

ANISOO 2482 O ILE B 111 22062 16957 18648 -889 1359 879 O

ATOM 2483 N LYS B 112 22.681 139.773 -21.604 1.00165.78 N

ANISOO 2483 N LYS B 112 23949 18571 20467 -952 1559 907 N

ATOM 2484 CA LYS B 112 22.252 140.457 -22.820 1.00170.85 C

ANISOO 2484 CA LYS B 112 24646 19196 21073 -756 1618 914 C

ATOM 2485 CB LYS B 112 20.914 139.924 -23.372 1.00170.68 C

ANISOU 2485 CB LYS B 112 24532 19144 21173 -569 1523 915 C

ATOM 2486 CG LYS B 112 19.653 140.750 -23.127 1.00172.00 C

ANISOU 2486 CG LYS B 112 24733 19188 21430 -578 1648 963 C

ATOM 2487 CD LYS B 112 18.463 140.104 -23.874 1.00173.52 C

ANISOU 2487 CD LYS B 112 24807 19378 21745 -393 1511 983 C

ATOM 2488 CE LYS B 112 17.226 139.931 -22.974 1.00180/50 C

ANISOU 2488 CE LYS B 112 25677 20143 22761 -421 1580 1028 C

ATOM 2489 NZ LYS B 112 16.235 138.919 -23.479 1.00175.96 N

ANISOU 2489 NZ LYS B 112 24970 19577 22308 -260 1419 1058 N

ATOM 2490 C LYS B 112 22.229 141.937 -22.538 1.00169.32 C

ANISOU 2490 C LYS B 112 24625 18923 20786 -837 1870 955 C

ATOM 2491 O LYS B 112 22.050 142.356 -21.399 1.00164.79 O

ANISOO 2491 O LYS B 112 24128 18275 20209 -1020 2003 971 O

ATOM 2492 N ARG B 113 22.447 142.731 -23.574 1.00172.34 N ANISOU 2492 N ARG B 113 25074 19321 21087 -713 • 1945 969 N

ATOM 2493 CA ARG B 113 22.794 144.120 -23.340 1.00179.66 C

ANISOU 2493 CA ARG B 113 26169 20182 21912 -793 2195 1004 C

ATOM 2494 CB ARG B 113 24.287 144.238 -23.020 1.00178.81 C

ANISOU 2494 CB ARG B 113 26143 20136 21661 -987 2233 996 C

ATOM 2495 CG ARG B 113 25.181 143.702 -24.128 1.00176.68 C

ANISOU 2495 CG ARG B 113 25795 19992 21344 -905 -2059 974 C

ATOM 2496 CD ARG B 113 26.562 144.335 -24.119 1.00174.-46 C

ANISOU 2496 CD ARG B 113 25629 19755 20901 -1013 2161 995 C

ATOM 2497 NE ARG B 113 26.563 145.663 -24.723 1.00173.09 N

ANISOU 2497 NE ARG B 113 25571 19544 20650 -898 2323 1005 N

ATOM 2498 CZ ARG B 113 27.087 146.741 -24.154- 1.00173.44 C

ANISOU 2498 CZ ARG B 113 25778 19549 20574 -1025 2536 1030 C

ATOM 2499 NHl ARG B 113 27.666 146.647 -22.967 1.00168.71 N

ANISOU 2499 NHl ARG B 113 25254 18948 19900 -1292 2606 1050 N

ATOM 2500 NH2 ARG B 113 27.049 147.907 -24.782 1.00175.88 N

ANISOU 2500 NH2 ARG B 113 26171 19823 20831 -896 2679 1042 N

ATOM 2501 C ARG B 113 22.476 145.094 -24.459 1.00174.96 C

ANISOU 2501 C ARG B 113 25613 19578 21284 -599 2278 1035 C

ATOM 2502 O ARG B 113 22.041 144.729 -25.556 1.00164.96 O

ANISOU 2502 O ARG B 113 24247 18372 20057 -409 2130 1032 O

ATOM 2503 N ALA B 114 22.707 146.356 -24.135 1.00203.96 N

ANISOU 2503 N ALA B 114 29438 23176 24881 -666 2527 1068 N

ATOM 2504 CA ALA B 114 22.627 147.413 -25.102 1.00207.22 C

ANISOU 2504 CA ALA B 114 29900 23578 25256 -507 2645 1110 C

ATOM 2505 CB ALA B 114 23.224 148.679 -24.527 1.00207.53 C

ANISOU 2505 .CB ALA B 114 30126 23537 25190 -640 2934 1130 C

ATOM 2506 C ALA B 114 23.404 146.965 -26.322 1.00 * 204.18 C

ANISOU 2506 C ALA B 114 29'454 23330 24795 -383 2464 1076 C

ATOM 2507 O ALA B 114 24.595 146.663 -26.239 1.00202.66 O

ANISOU 2507- O ALA B 114 29288 23212 24502 -482 2402 1034 O

ATOM 2508 N ASP B 115 22.713 146.900 -27.452 1.00174.32 N

ANISOU 2508 N ASP B 115 25588 19580 21067 -176 2379 1105 N

ATOM 2509 CA ASP B 115 23.353 146.583 -28.714 1.00168.05 C

ANISOU 2509 CA ASP B 115 24754 18901 20195 -56 2236 1073 C

ATOM 2510 CB ASP B 115 22.363 146.762 -29.865 1.00164.04 C

ANISOU 2510 CB ASP B 115 24171 18413 19743 143 2191 1133 C

ATOM 2511 CG ASP B 115 21.099 145.923 -29.679 1.00170.62 C

ANISOU 2511 CG ASP B 115 24880 19227 20721 191 2065 1162 C

ATOM 2512 ODl ASP B 115 20.648 145.755 : 28.517 1.00168.66 O

ANISOU 2512 ODl ASP B 115 24637 18887 20560 98 2138 1178 O

ATOM 2513 OD2 ASP B 115 20.556 145.429 -30.695 1.00171.29 O

ANISOU 2513 OD2 ASP B 115 24868 19390 20826 " 312 1892 1170 O

ATOM 2514 C ASP B 115 24.590 147.452 -28.895 1.00164.70 C

ANISOU 2514 C ASP B 115 24461 18496 19621 -115 2373 1062 C

ATOM 2515 O ASP B 115 24.702 148.526 -28.308 1.00159.19 O

ANISOU 2515 O ASP B 115 23879- 17720 18887 -173 2603 1102 O

ATOM 2516 N ALA B 116 25.534 146.960 -29.686 1.00174.98 N

ANISOU 2516 N ALA B 116 25748 19894 20841 -110 2241 1009 N

ATOM 2517 CA ALA B 116 26.793 147.660 -29.897 1.00174.01 C

ANISOU 2517 CA ALA B 116 25737 19804 20574 -151 2339 1004 C

ATOM 2518 CB ALA B 116 27.790 147.289 -28.816 1.00168.48 C

ANISOU 2518 CB ALA B 116 25086 19113 19817 -369 2354. 992 C

ATOM 2519 C ALA B 116 27.369 147.368 -31.282 1.00171.23 C

ANISOU 2519 C ALA B 116 25343 19547 20169 -2 2200 .970 C

ATOM 2520 O ALA B 116 * 26.971 146.412 -31.946 1.00175.47 O

ANISOU 2520 O ALA B 116 25773 20128 20771 93 2022 940 O

ATOM 2521 N ALA B 117 28.307 148.200 -31.718 1.00169.08 N

ANISOU 2521 N ALA B 117 25164 19305 19773 8 2286 972 N

ATOM 2522 CA ALA B 117 28.908 148.033 -33.032 1.00170.67 C

ANISOU 2522 CA ALA B 117 25341 19586 19920 147 2175 939 C

ATOM 2523 CB ALA B 117 28.617 149.234 -33.905 1.00179.03 C

ANISOU 2523 CB ALA B 117 26445 20648 20931 285 2282 975 C

ATOM 2524 C ALA B 117 30.405 147.813 -32.906 1.00168.66 C

ANISOU 2524 C ALA B 117 25131 19377 19574 67 2148 916 C

ATOM 2525 O ALA B 117 31.015 148.170 -31.896 1.00167.66 O

ANISOU 2525 O ALA B 117 25077 19232 19394 -95 2247 945 O

ATOM 2526 N PRO B 118 30.998 147.218 -33.942 1.00154.43 N

ANISOU 2526 N PRO B 118 23289 17635 17754 168 2018 873 N

ATOM 2527 CA PRO B 118 32.381 146.734 -33.959 1.00150.32 C

ANISOU 2527 CA PRO B 118 22778 17151 17186 114 1969 864 C

ATOM 2528 CB PRO B 118 32.408 145.819 -35.180 1.00152.78 C

ANISOU 2528 CB PRO B 118 23028 17498 17522 257 1827 802 C

ATOM 2529 CG PRO •B 118 30.963 145.536 -35.481 1.00159.31 C

ANISOU 2529 CG PRO B 118 23788 18317 18424 338 1762 782 C

ATOM 2530 CD PRO B 118 30.242 146.765 -35.114 1.00155.05 C

ANISOU 2530 CD PRO B 118 23301 17743 .17868 330 1907 840 C ATOM 2531 C PRO B 118 33.444 147.818 -34.104 1.00150.16 C

ANISOU 2531 C PRO B 118 22877 17146 17031 87 2098 897 C

ATOM 2532 ' O PRO B 118 33.261 148.781 -34.847 1.00156 .71 O

ANISOO 2532 O PRO B 118 23775 17976 17791 181 2193 899 O

ATOM 2533 N THR B 119 34.554 147.631 -33.396 1.00157 .03 N

ANISOU 2533 N THR B 119 23762 18033 17869 -44 2098 936 N

ATOM 2534 CA THR B 119 35.712 148.520 -33.450 1.00159 .45 C

ANISOU 2534 CA THR B 119 24178 18362 18042 -93 2207 980 C

ATOM 2535 CB THR B 119 36.241 148.800 -32.026 1.00163, 10 C

ANISOU 2535 CB THR B 119 24699 18814 18458 -331 2307 1052 C

ATOM 2536 OGl THR B 119 35.376 149.743 -31.379 1.00163, 23 O

ANISOU 2536 OGl THR B 119 24788 18775 18457 -363 2448 1043 O

ATOM 2537 CG2 THR B 119 37.668 149.351 -32.046 1.00160 16 C

ANISOU 2537 CG2 THR B 119 24420 18483 17951 -420 2378 1117 C

ATOM 2538 C THR B 119 36.802 147.895 -34.324 1.00160. 91 C

ANISOU 2538 C THR B 119 24338 18587 18213 -32 2121 982 C

ATOM 2539 O T 1 HR B 119 37.749 147.271 -33.824 1.00158. 46 O

ANISOU 2539 O THR B 119 23995 18294 17920 -153 2089 1047 O

ATOM 2540 N VAL B 120 36..658 148.082 -35.636 1.00158. 11 N

ANISOU 2540 N VAL B 120 23999 18245 17831 153 2094 922 N

ATOM 2541 CA VAL B 120 37.407 147.300 -36.623 1.00154. 53 C

ANISOU 2541 CA VAL B 120 23513 17807 17396 246 2004 895 C

ATOM 2542 CB VAL B 120 36.568 147.028 -37.896 1.00148. 33 C

ANISOU 2542 CB VAL B 120 22707 17027 16625 422 1934 804 C

ATOM 2543 CGl VAL B 120 35.086 147.120 -37.579 1.00152. 52 C

ANISOU 2543 CGl VAL B 120 23171 17542 17236 423 1889 778 C

ATOM 2544 CG2 VAL B 120 36.923 147.993 -38.976 1.00154. 31 C

ANISOU 2544 CG2 VAL B 120 23557 17811 17262 530 2012 793 C

ATOM 2545 C VAL B 120 38.780 147.858 -37.010 1.00156. 96 C

ANISOU 2545 C VAL B 120 23898 18137 17601 248 2064 942 C

ATOM 2546 O VAL B 120 38.951 149.051 -37.260 1.00157. 69 O

ANISOU 2546 O VAL B 120 24092 18247 17577 278 2164 951 O

ATOM 2547 N SER B 121 39.757 146.963 -37.037 1.00188. 48 N

ANISOU 2547 N SER B 121 27837 22124 21652 215 2009 983 N

ATOM 2548 CA SER B 121 41.108 147.295 -37.436 1.00190. 30 C.

ANISOU 2548 CA SER B 121 28122 22369 21813 230 2049 1042 C

ATOM 2549 CB SER B 121 42.075 147.010 -36.287 1.00181. 35 C

ANISOU 2549 CB SER B 121 26951 21250 20702 37 2064 1186 C

ATOM 2550 OG SER B 121 41.421 147.102 -35.032 1.00178. 51 O

ANISOU 2550 OG SER B 121 26576 20901 20348 -129 2084 1220 O

ATOM 2551 C SER B 121 41.436 146.407 -38.625 1.00190. 01 C

ANISOU 2551 C SER B 121 28052 22302 21841 372 1983 981 C

ATOM 2552 O SER B 121 40.663 145.513 -38.965 1.00185. 46 O

ANISOU 2552 O SER B 121 27421 21703 21344 440 1911 893 O

ATOM 2553 N ILE B 122 42.571 146.660 -39.265 1.00159. 91 N

ANISOU 2553 N ILE B 122 24281 18487 17992 407 2018 1031 N

ATOM 2554 CA ILE B 122 43.064 145.796 -40.334 1.00150. 58 C

ANISOU 2554 CA ILE B 122 23080 17256 16876 521 1986 986 C

ATOM 2555 CB ILE B 122 42.478 146.157 -41.723 1.00145. 68 C

ANISOU 2555 CB ILE B 122 22531 16639 16182 682 1970 845 C

ATOM 2556 CGl ILE B 122 43.062 145.243 -42.799 1.00144. 09 C

ANISOU 2556 CGl ILE B 122 22335 16377 16035 773 1959 794 C

ATOM 2557 CDl ILE B 122 42.256 145.213 -44.049 1.00147. 57 C

ANISOU 2557 CDl ILE B 122 -22821 16822 16426 884 1915 650 C

ATOM 2558 CG2 ILE B 122 42.729 147.620 -42.055 1.00146. 96 C

ANISOU 2558 CG2 ILE B 122 . 22800 16853 16186 734 2036 848 C

ATOM 2559 C ILE B 122 44.573 145.900 -40.356 1.00145. 27 C

ANISOU 2559 C ILE B 122 22434 16575 16186 506 2042 1100 C

ATOM 2560 O ILE B 122 45.137 146.956 -40.067 1.00146. 96 O

ANISOU 2560 O ILE B 122 22726 16835 16279 476 2100 1162 O

ATOM 2561 N PHE B 123 45.232 144.800 -40.677 1.00144. 98 N

ANISOU 2561 N PHE B 123 22331 16475 16279 523 2035 1139 N

ATOM 2562 CA PHE B 123 46.673 144.780 -40.579 1.00150. 90 C

ANISOU 2562 CA PHE B 123 23075 17210 17052 490 2089 1291 C

ATOM 2563 CB PHE B 123 47.086 144.072 -39.311 1.00151. 50 C

ANISOU 2563 CB PHE B 123 23017 17290 17255 319 2076 1463 C

ATOM 2564 CG PHE B 123 46.691 144.815 -38.115 1.00150. 83 C

ANISOU 2564 CG PHE B 123 22933 17286 17091 161 2059 1509 C

ATOM 2565 CDl PHE B 123 45.355 144.948 -37.802 1.00150. 07 C

ANISOσ 2565 CDl PHE B 123 22844 17203 16973 163 2019 1379 C

ATOM 2566 CEl PHE B 123 44.962 145.674 -36.719 1.00153. 27 C

ANISOU 2566 CEl PHE B 123 23266 17664 17307 17 2027 1413 C

ATOM 2567 CZ PHE B 123 45.914 146.293 -35.933' 1.00160. 43 C

ANISOU 2567 CZ PHE B 123 24191 18624 18142 -153 2069 1573 C

ATOM 2568 CE2 PHE B 123 47.261 146.177 -36.252 1.00156. 55 C

ANISOU 2568 CE2 PHE B 123 23686 18136 17661 -164 2092 1715 C

ATOM 2569 CD2 PHE B 123 47.637 145.449 -37.342 1.00149. C ANISOO 2569 CD2 PHE B 123 22816 17224 16906 3 2090 1685 C

ATOM 2570 C PHE B 123 47.375 144.211 -41.777 1.00156 .51 C

ANISOO 2570 C PHE B 123 23805 17835 17825 623 2125 1258 C

ATOM 2571 O PHE B 123 47.090 143.105 -42.211 1.00160 .73 O

ANISOO 2571 O PHE B 123 24277 18293 18500 652 2117 1211 O

ATOM 2572 N PRO B 124 48.313 144.984 -42.312 1.00160 .59 N

ANISOO 2572 N PRO B 124 24420 18359 18238 699 2177 1280 N

ATOM 2573 CA PRO B 124 49.083 144.560 -43.461 1.00160 .53 C

ANISOO 2573 CA PRO B 124 24439 18258 18296 812 2231 1273 C

ATOM 2574 CB PRO B 124 49.811 145.834 -43.879 1.00167, 44 C

ANISOO 2574 CB PRO B 124 25429 19173 19017 877 2274 1302 C

ATOM 2575 CG PRO B 124 49.377 146.915 -42.896 1.00168, 90 C

ANISOO 2575 CG PRO B 124 25662 19469 19042 822 2244 1273 C

ATOM 2576 CD PRO B 124 48.884 146.190 -41.707 1.00167. .80 C

ANISOU 2576 CD PRO B 124 25418 19357 18983 666 2203 1338 C

ATOM 2577 C PRO B 124 50.062 143.571 -42.898 1.00164, 02 C

ANISOO 2577 C PRO B 124 24756 18639 18926 727 2269 1462 C

ATOM 2578 O PRO B 124 50.755 143.893 -41.919 1.00160. 04 O

ANISOO 2578 O PRO B 124 24201 18192 18415 606 2273 1650 O

ATOM 2579 N PRO B 125 50.109 142.379 -43.500 1.00162. 26 N

ANISOO 2579 N PRO B 125 24481 18303 18867 775 2303 1420 N

ATOM 2580 CA PRO B 125 50.875 141.243 -43.009 1.00160. 88 C

ANISOO 2580 CA PRO B 125 24173 18043 18912 720 2365 1598 C

ATOM 2581 CB PRO B 125 51.309 140.560 -44.299 1.00159. 00 C

ANISOO 2581 CB PRO B 125 24000 17662 18750 857 2463 1505 C

ATOM 2582 CG PRO B 125 50.170 140.796 -45.218 1.00155. 51 C

ANISOϋ 2582 CG PRO B 125 23675 17240 18173 931 2406 1237 C

ATOM 2583 CD PRO B 125 49.575 142.129 -44.850 1.00155. 38 C

ANISOϋ 2583 CD PRO B 125 23697 17373 17967 894 2305 1198 C

ATOM 2584 C PRO B 125 52.088 141.699 -42.231 1.00163. 69 C

ANISOϋ 2584 C PRO B 125 24481 18445 19269 638 2393 1851 C

ATOM 2585 O PRO B " 125 52.755 142.671 -42.601 1.00165. 70 O

ANISOO 2585 O PRO B 125 24842 18731 19387 693 2415 1869 O

ATOM 2586 N SER B 126 52.364 141.014 -41.133 1.00174. 99 N

ANISOϋ 2586 N SER B 126 25752 19890 20846 496 2386 2056 N

ATOM 2587 CA SER B 126 53.639 141.225 -40.488 1.00182. 65 C

ANISOO 2587 CA SER B 126 26661 20895 21842 407 2418 2332 C

ATOM 2588 CB SER B 126 54.016 140.025 -39.622 1.00182. 98 C

ANISOϋ 2588 CB SER B 126 26492 20903 22128 285 2440 2570 C

ATOM 2589 OG SER B 126 55.425 139.952 -39.460 1.00184. 82 O

ANISOϋ 2589 OG SER B 126 26662 21096 22465 280" 2520 2831 O

ATOM 2590 C SER B 126 54.622 141.354 -41.626 1.00180. 91 C

ANISOO 2590 C SER B 126 26524 20573 21639 564 2518 2335 C

ATOM 2591 O SER B 126 54.570 140.587 -42.577 1.00182. 37 O

ANISOϋ 2591 O SER B 126 26740 20628 21925 693 2587 2204 O

ATOM 2592 N SER B 127 55.501 142.331 -41.579 1.00150. 54 N

ANISOϋ 2592 N SER B 127 '22725 16780 17692 548 2533 2482 N

ATOM 2593 CA SER B 127 56.520 142.314 -42.592 1.00154. 57 C

ANISOU 2593 CA SER B 127 23277 17175 18277 685 2641 2543 C

ATOM 2594 CB SER B 127 57.255 143.642 -42.665 1.00156. 04 C

ANISOU 2594 CB SER B 127 23563 17438 18287 695 2638 2635 C

ATOM 2595 OG SER B 127 58.325 143.585 -43.584 1.00162. 11 O

ANISOU 2595 OG SER B 127 24289 18106 19199 754 2740 2838 O

ATOM 2596 C SER B 127 57.440 141.121 -42.315 1.00156. 21 C

ANISOU 2596 C SER B 127 23302 17274 18777 643 2730 2792 C

ATOM 2597 O SER B 127 57.608 140.250 -43.166 1.00158. 02 O

ANISOU 2597 O SER B 127 23534 17339 19168 768 2848 2751 O

ATOM 2598 N GLU B 128 57.990 141.046 -41.112 1.00168. 19 N

ANISOϋ 2598 N GLU B 128 24657 18877 20371 459 2686 3052 N

ATOM 2599 CA GLU B 128 58.854 139.926 -40.768 1.00174. 92 C

ANISOU 2599 CA GLU B 128 25308 19633 21521 415 2774 3320 C

ATOM 2600 CB GLO B 128 59.062 139.828 -39.255 1.00182. 85 C

ANISOU 2600 CB GLO B 128 26129 20774 22572 173 2691 3605 C

ATOM 2601 CG GLU B 128 59.905 138.610 -38.834 1.00191. 17 C

ANISOU 2601 CG GLO B 128 26949 21740 23948 122 2787 3942 C

ATOM 2602 CD GLO B 128 59.656 138.154 -37.387 1.00192. 33 C

ANISOU 2602 CD GLO B 128 26887 22008 24180 -118 2698 4167 C

ATOM 2603 OEl GLU B 128 58.769 138.722 -36.713 1.00178. 96 O

ANISOU 2603 OEl GLU B 128 25223 20414 22359 -212 2585 3995 O

ATOM 2604 0E2 GLU B 128 60.351 137.219 -36.925 1.00197. 93 O

ANISOϋ 2604 0E2 GLU B 128 27397 22714 25095 -217 2744 4531 O

ATOM 2605 C GLU B 128 58.297 138.601 -41.265 1.00171. 71 C

ANISOO 2605 C GLU B 128 24847 19071 21325 502 2856 3179 C

ATOM 2606 O GLU B 128 59.060 137.704 -41.625 1.00173. 96 O

ANISOϋ 2606 O GLU B 128 25008 19214 21873 537 2990 3352 O

ATOM 2607 N GLN B 129 56.969 138.474 -41.270 1.00153. 48 N

ANISOU 2607 N GLN B 129 22623 16785 18908 529 2785 2881 N ATOM 2608 CA GLN B 129 56.322 137.186 -41.564 1.00151.61 C

ANISOU 2608 CA GLN B 129 22334 16423 18848 578 2843 2744 C

ATOM 2609 CB GLN B 129 54.810 137.196 -41.277 1.00145 .18 C

ANISOU 2609 CB GLN B 129 21560 15699 17901 535 2712 2498 C

ATOM 2610 CG GLN B 129 54.074 136.025 -41.926 1.00160 .13 C

ANISOU 2610 CG GLN B 129 23477 17461 19906 621 2773 2282 C

ATOM 2611 CD GLN B 129 52.580 136.217 -41.985 1.00154 .06 C

ANISOU 2611 CD GLN B 129 22779 16779 18978 605 2641 2025 C

ATOM 2612 OEl GLN B 129 51.865 135.366 -42.491 1.00150 .09 O

ANISOU 2612 OEl GLN B 129 22287 16198 18543 644 2663 1854 O

ATOM 2613 NE2 GLN B 129 52.099 137.334 -41.463 1.00157 38 N

ANISOU 2613 NE2 GLN B 129 23250 17358 19189 542 2514 2O04 N

ATOM 2614 C GLN B 129 56.525 136.733 -42.992 1.00152. .71 C

ANISOU 2614 C GLN B 129 22598 16376 19048 757 2991 2579 C

ATOM 2615 O GLN B 129 56.907 135.585 -43.232 1.00156. 83 O

ANISOU 2615 O GLN B 129 23039 16737 19812 792 3132 2626 O

ATOM 2616 N LEU B 130 56.250 137.617 -43.945 1.00160. 31 N

ANISOU 2616 N LEU B 130 23762 17357 19793 862 2972 2384 N

ATOM 2617 CA LEU B 130 56.268 137.189 -45.333 1.00162. 37 C

ANISOU 2617 CA LEU B 130 24162 17449 20082 1010 3104 2202 C

ATOM 2618 CB LEU B 130 55.537 138.174 -46.250 1.00157. 33 C

ANISOU 2618 CB LEU B 130 23737 16882 19161 1091 3020 1914 C

ATOM 2619 CG LEU B 130 55.478 139.650 -45.898 1.00149. 27 C

ANISOU 2619 CG LEU B 130 22773 16049 17893 1063 2879 1926 C

ATOM 2620 CDl LEU B 130 56.768 140.307 -46.311 1.00151. 66 C

ANISOU 2620 CDl LEU B 130 23102 16340 18183 1108 2942 2115 C

ATOM 2621 CD2 LEU B 130 54.294 140.259 -46.619 1.00141. 36 C

ANISOU 2621 CD2 LEU B 130 21937 15116 16656 1129 2793 1631 C

ATOM 2622 C LEU B 130 57.685 136.875 -45.797 1.00164. 53 C

ANISOU 2622 C LEU B 130 24416 17578 20521 1080 3278 2412 C

ATOM 2623 O LEU B 130 57.947 135.786 -46.316 1.00165. 47 O

ANISOU 2623 O LEU B 130 24555 17501 20816 1155 3453 2377 O

ATOM 2624 N THR B 131 58.602 137.808 -45.578 1.00158. 52 N

ANISOU 2624 N THR B 131 23612 16907 19710 1046 3240 2643 N

ATOM 2625 CA THR B 131 59.993 137.577 -45.925 1.00159. 96 C

ANISOU 2625 CA THR B 131 23757 16966 20056 1107 3392 2887 C

ATOM 2626 CB THR B 131 . 60.824 138.807 -45.626 1.00168. 66 C

ANISOU 2626 CB THR B 131 24853 18219 21013 1057 3301 3093 C

ATOM 2627 OGl THR B 131 60.349 139.379 -44.402 1.00177. 05 O

ANISOU 2627 OGl THR B 131 25786 19465 22019 875 3149 3221 O

ATOM 2628 CG2 THR B 131 60.696 139.840 -46.762 1.00168. 65 C

ANISOU 2628 CG2 THR B 131 25079 18289 20712 1155 3230 2850 C

ATOM 2629 C THR B 131 60.543 136.406 -45.128 1.00158. 15 C

ANISOU 2629 C THR B 131 23303 16619 20166 1047 3521 3163 C

ATOM 2630 O THR B 131 61.382 136.583 -44.252 1.00159. 27 O

ANISOU 2630 O THR B 131 23311 16756 20450 1006 3573 3499 O

ATOM 2631 N SER B 132 60.072 135.213 -45.467 1.00161. 38 N

ANISOU 2631 N SER B 132 23668 16938 20712 1038 3574 3031 N

ATOM 2632 CA SER B 132 60.373 133.998 -44.740 1.00167. 42 C

ANISOU 2632 CA SER B 132 24214 17586 21813 987 3708 3274 C

ATOM 2633 CB SER B 132 60.968 134.308 -43.374 1.00184. 00 C

ANISOU 2633 CB SER B 132 26089 19839 23985 831 3608 3644 C

ATOM 2634 OG SER B 132 ' 60.102 135.146 -42.625 1.00183. 76 O

ANISOU 2634 OG SER B 132 26078 20041 23700 710 3374 3552 O

ATOM 2635 C SER B 132 59.072 133.241 -44.557 1.00166. 43 C

ANISOU 2635 C SER B 132 24071 17430 21734 956 3693 3053 C

ATOM 2636 O SER B 132 58.821 132.662 -43.498 1.00171. 64 O

ANISOU 2636 O SER B 132 24528 18110 22579 855 3684 3209 O

ATOM 2637 N GLY B 133 58.237 133.267 -45.589 1.00164. 26 N

ANISOU 2637 N GLY B 133 24009 17118 21285 1035 3683 2694 N

ATOM 2638 CA GLY B 133 56.981 132.540 -45.574 1.00168. 25 C

ANISOU 2638 CA GLY B 133 24529 17592 21807 1011 3669 2458 C

ATOM 2639 C GLY B 133 55.952 133.179 -46.479 1.00165. 24 C

ANISOU 2639 C GLY B 133 24382 17276 21127 1061 3560 2098 C

ATOM 2640 O GLY B 133 56.288 133.934 -47.387 1.00165. 82 O

ANISOU 2640 O GLY B 133 24627 17321 21056 1150 3593 2002 O

ATOM 2641 N GLY B 134 54.688 132.860 -46.244 1.00173. 84 N

ANISOU 2641 N GLY B 134 25471 18452 22130 1002 3432 1910 N

ATOM 2642 CA GLY B 134 53.609 133.547 -46.924 1.00169. 36 C

ANISOU 2642 CA GLY B 134 25094 17976 21280 1031 3304 1606 C

ATOM 2643 C GLY B 134 53.237 134.760 -46.096 1.00166. 19 C

ANISOU 2643 C GLY B 134 24673 17802 20668 980 3088 1635 C

ATOM 2644 O GLY B 134 54.035 135.227 -45.289 1.00165. 56 O

ANISOU 2644 O GLY B 134 24500 17797 20610 940 3059 1870 O

ATOM 2645 N ALA B 135 52.023 135.266 -46.274 1.00145. 78 N

ANISOϋ 2645 N ALA B 135 22178 15327 17884 968 2945 1408 N

ATOM 2646 CA ALA B 135 51.582 136.415 -45.498 1.00153. 45 C ANISOU 2646 CA ALA B 135 ' 23143 16496 18664 919 2767 1420 C

ATOM 2647 CB ALA B 135 51.767 137.688 -46.305 1.00142 .99 C

ANISOU 2647 CB ALA B 135 21985 15227 17116 1004 2743 1340 C

ATOM 2648 C ALA B 135 50.138 136.283 -44.989 1.00141 .11 C

ANISOU 2648 C ALA B 135 21564 15032 17020 860 2625 1260 C

ATOM 2649 O ALA B 135 49.265 135.744 -45.679 1.00150 .90 O

ANISOU 2649 O ALA B 135 22880 16224 18230 888 2625 1054 O

ATOM 2650 N SER B 136 49.908 136.773 -43.769 1.00149 .88 N

ANISOU 2650 N SER B 136 22579 16279 18089 766 2509 1365 N

ATOM 2651 CA SER B 136 48.591 136.739 -43.137 1.00148 72 C

ANISOU 2651 CA SER B 136 22398 16227 17882 702 2378 1254 C

ATOM 2652 CB SER B 136 48.651 135.959 -41.816 1.00144. 50 C

ANISOU 2652 CB SER B 136 21666 15701 17535 580 2359 1421 C

ATOM 2653 OG SER B 136 48.850 134.569 -42.017 l. ' θO149, 82 O

ANisoσ 2653 OG SER B 136 22252 16229 18442 594 2478 1468 O

ATOM 2654 C SER B 136 48.026 138.150 -42.895 1.00147. 04 C

ANISOU 2654 C SER B 136 22265 16166 17438 690 2264 1206 C

ATOM 2655 O SER B 136 48.617 138.961 -42.159 1.00143. 30 O

ANISOU 2655 O SER B 136 21768 15770 16909 631 2250 1360 O

ATOM 2656 N VAL B 137 46.876 138.426 -43.512 1.00140. 08 N

ANISOU 2656 N VAL B 137 21475 15326 16424 735 2192 1003 N

ATOM 2657 CA VAL B 137 46.181 139.703 -43.349 1.00139. 92 C

ANISOU 2657 CA VAL B 137 21528 15431 16203 738 2107 949 C

ATOM 2658 CB VAL B 137 45.568 140.180 -44.670 1.00140. 33 C

ANISOU 2658 CB VAL B 137 21727 15490 16101 848 2095 764 C

ATOM 2659 CGl VAL B 137 44.800 141.470 -44.453 1.00140. 38 C .

ANISOO 2659 CGl VAL B 137 21791 15620 15928 858 2025 728 C

ATOM 2660 CG2 VAL B 137 46.650 140.385 -45.696 1.00140. 10 C

ANISOU 2660 CG2 VAL B 137 21789 15383 16060 935 2197 775 C

ATOM 2661 C VAL B 137 45.078 139.654 -42.285 1.00138. 75 C

ANISOU 2661 C VAL B 137 21298 15361 16060 645 2008 937 C

ATOM 2662 O VAL B 137 43.931 139.320 -42.578 1.00138. 93 O

ANISOU 2662 O VAL B 137 21-329 15388 16071 663 1947 797 O

ATOM 2663 N VAL B 138 45.437 140.019 -41.056 1.00144. 64 N

ANISOU 2663 N VAL B 138 21973 16168 16816 535 1996 1091 N

ATOM 2664 CA VAL B 138 44.555 139.905 -39.899 1.00138. 82 C

ANISOU 2664 CA VAL B 138 21148 15491 16107 419 1922 1116 C

ATOM 2665 CB VAL B 138 45.382 139.940 -38.632 1.00143. 25 C

ANISOU 2665 CB VAL B 138 21622 16092 16716 271 1940 1329 C

ATOM 2666 CGl VAL B 138 44.661 139.212 -37.545 1.00136. 09 C

ANISOU 2666 CGl VAL B 138 20614 15229 15866 139 1872 1355 C

ATOM 2667 CG2 VAL B 138 46.746 139.329 -38.889 1.00141. 43 C

ANISOU 2667 CG2 VAL B 138 21302 15783 16651 268 2010 1474 C

ATOM 2668 C VAL B 138 43.559 141.051 -39.793 1.00138. 43 C

ANISOU 2668 C VAL B 138 21179 15524 15893 424 1872 1024 C

ATOM 2669 O VAL B 138 43.897 142.194 -40.079 1.00144. 83 O

ANISOU 2669 O VAL B 138 22095 16377 16557 466 1905 1022 O

ATOM 2670 N CYS B 139 42.340 140.767 -39.348 1.00138. 08 N

ANISOU 2670 N CYS B 139 21083 15501 15882 382 1803 962 N

ATOM 2671 CA CYS B 139 41.338 141.828 -39.242 1.00139. 84 C

ANISOU 2671 CA CYS B 139 21374 15787 15971 394 1776 895 C

ATOM 2672 CB CYS B 139 40.579 141.961 -40.550 1.00139. 76 C

ANISOU 2672 CB CYS B 139 21434 15773 15897 530 1744 741 C

ATOM 2673 SG CYS B 139 39.154 143.063 -40.443 1.00136. 56 S

ANISOU 2673 SG CYS B 139 21096 15439 15350 566 1730 691 S

ATOM 2674 C CYS B 139 40.326 141.673 -38.109 1.00144. 70 C

ANISOU 2674 C CYS B 139 . 21917 16431 16632 284 1729 912 C

ATOM 2675 O CYS B 139 39.335 140.967 -38.261 1.00147. 23 O

ANISOU 2675 O CYS B 139 22190 16738 17012 309 1662 827 O

ATOM 2676 N PHE B 140 40.559 142.374 -37.000 1.00151. 80 N

ANISOU 2676 N PHE B 140 22817 17370 17491 153 1766 1023 N

ATOM 2677 CA PHE B 140 39.705 142.302 -35.817 1.00144. 74 C

ANISOU 2677 CA PHE B 140 21872 16497 16627 28 1740 1046 C

ATOM 2678 CB PHE B 140 40.412 142.957 -34.649 1.00141. 59 C

ANISOU 2678 CB PHE B 140 21492 16139 16166 -149 1800 1187 C

ATOM 2679 CG PHE B 140 41.781 142.429 -34.404 1.00145. 00 C

ANISOU 2679 CG PHE B 140 21855 16573 16665 -223 1807 1329 C

ATOM 2680 CDl PHE B 140 42.871 143.263 -34.440 1.00149. 69 C

ANISOU 2680 CDl PHE B 140 22515 17207 17154 -300 1873 1447 C

ATOM 2681 CEl PHE B 140 44.136 142.782 -34.201 -1.00147. 65 C

ANISOU 2681 CEl PHE B 140 22178 16953 16969 -372 1878 1610 C

ATOM 2682 CZ- PHE B 140 44.321 141.466 -33.931 1.00147. 45 C

ANISOU 2682 CZ PHE B 140 22006 16883 17135 -359 1834 1652 C

ATOM 2683 CE2 PHE B 140 43.245 140.624 -33.898 1.00150. 98 C

ANISOU 2683 CE2 PHE B 140 22397 17285 17684 -280 1778 1517 C

ATOM 2684 CD2 PHE B 140 41.983 141.102 -34.135 1.00146. 22 C

ANISOU 2684 CD2 PHE B 140 21874 16687 16995 -215 1756 1358 C ATOM 2685 C PHE B 140 38.351 142.975 -35.979 1,.00143.66 C

ANISOU 2685 C PHE B 140 21791 16369 16423 91 1733 944 C

ATOM 2686 O PHE B 140 38.144 143.758 -36.885 1.00146 89 O

ANISOU 2686 O PHE B 140 22292 16790 16729 205 1766 885 O

ATOM 2687 N LEU B 141 37.429 142.647 -35.087 1.00146 33 N

ANISOU 2687 N LEU B 141 22063 16702 16835 18 1691 934 N

ATOM 2688 CA LEU B 141 36. 167 143.362 -34.944 1.00150 85 C

ANISOU .2688 CA LEU B 141 22677 17276 17362 49 1706 880 C

ATOM 2689 CB LEU B 141 35.040 142.695 -35.734 1.00147 57 C

ANISOU 2689 CB LEU B 141 22212 16847 17009 174 1612 779 C

ATOM 2690 CG LEU B 141 34.990 142..820 -37.252 1.00144 56 C

ANISOU 2690 CG LEU B 141 21886 16478 16561 331 1594 704 C

ATOM 2691 CDl LEU B 141 35.861 141..759 -37.853 1.00149 .65 C

ANISOU 2691 CDl LEU B 141 22509 17101 17250 348 1572 694 C

ATOM 2692 CD2 LEU B 141 33.578 142..660 -37.752 1.00142. 14 C

ANISOU 2692 CD2 LEU B 141 21544 16177 16284 410 1509 631 C.

ATOM 2693 C LEU B 141 35.825 143..319 -33.465 1.00157. 66 C

ANISOU 2693 C LEU B 141 23507 18134 18264 -121 1727 939 C

ATOM 2694 O LEU B 141 35.215 142..360 -33 ,000 1.00159. 60 O

ANISOU 2694 O LEU B 141° 23664 18360 18615 -143 1656 912 O

ATOM 2695 N ASN B 142 36.221 144..349 -32 ,724 1.00177. 76 N

ANISOU 2695 N ASN B 142 26129 20695 20715 -252 1829 1018 N

ATOM 2696 CA ASN B 142 36.170 144..295 -31.266 1.00178. 29 C

ANISOU 2696 CA ASN B 142 26176 20764 20803 -462 1856 1090 C

ATOM 2697 CB ASN B 142 37.433 144..924 -30 ,680 1.00179. 32 C

ANISOU 2697 CB ASN B 142 26378 20933 20822 -624 1940 1201 C

ATOM 2698 CG ASN B 142 38.684 144..181 -31 072 1.00181. 77 C

ANISOU 2698 CG ASN B 142 26614 21273 21176 -623 1879 1278 C

ATOM 2699 ODl ASN B 142 38.977 143..105 -30 545 1.00179. 02 O

ANISOU 2699 ODl ASN B 142 26132 20915 20972 -604 1782 1286 O

ATOM 2700 ND2 ASN B 142 39.443 144..759 -31 996 1.00185. 91 N

ANISOU 2700 ND2 ASN B 142 27223 21829 21586 -643 1946 1344 N

ATOM 2701 C ASN B 142 34.941 144..912 -30 596 1.00182. 02 C

ANISOU 2701 C ASN B 142 26693 21198 21268 -504 1921 1056 C

ATOM 2702 O ASN B 142 34.542 146..035 -30 903 1.00183. 00 O

ANISOU 2702 O ASN B 142 26925 21303 21303 -441 2030 1030 O

ATOM 2703 N ASN B 143 34.354 144..156 -29 672 1.00168. 10 N

ANISOU 2703 N ASN B 143 24842 19418 19610 -608 1864 1065 N

ATOM 2704 CA ASN B 143 33.347 144..674 -28.749 1.00167. 74 C

ANISOU 2704 CA ASN B 143 24841 19326 19565 -702 1944 1058 C

ATOM 2705 CB ASN B 143 33.893 145.900 -28 017 1.00163. 46 C

ANISOU 2705 CB ASN B 143 24445 18783 18879 -880 2111 1119 C

ATOM 2706 CG ASN B 143 35.267 145.659 -27 415 1.00162. 21 C

ANISOU 2706 CG ASN B 143 24268 18688 18677 -1087 2087 1222 C

ATOM 2707 ODl ASN B 143 35.537 144.596 -26 841 1.00161. 34 O

ANISOU 2707 ODl ASN B 143 24028 18603 18670 -1176 1974 1265 O

ATOM 2708 ND2 ASN B 143 36.145 146.654 -27 537 1.00161. 99 N

ANISOU 2708 ND2 ASN B 143 24361 18689 18500 -1169 2193 1275 N

ATOM 2709 C ASN B 143 32.009 145.014 -29.384 1.00161. 64 C

ANISOU 2709 C ASN B 143 24083 18505 18829 -530 1964 986 C

ATOM 2710 O ASN B 143 31.652 146.180 -29 500 1.00159. 09 O

ANISOU 2710 O ASN B 143 23869 18144 18433 -515 2109 989 O

ATOM 2711 N PHE B 144 31.260 143.998 -29, 777 1.00157. 43 N

ANISOU 2711 N PHE B 144 23435 17970 18412 -410 1825 935 N

ATOM 2712 CA PHE B 144 29.975 144.243 -30 396 1.00160. 29 C

ANISOU 2712 CA PHE B 144 23791 18301 18812 -255 1821 893 C

ATOM 2713 CB PHE B 144 30.022 143.935 -31.888 1.00166. 83 C

ANISOU 2713 CB PHE B 144 24597 19171 19621 -68 1734 844 C

ATOM 2714 CG PHE B 144 30.652. 142.612 -32, 229 1.00167. 56 C

ANISOU 2714 CG PHE B 144 24591 19293 19782 -52 1586 806 C

ATOM 2715 CDl PHE B 144 32.026 142.493 -32, 356 1.00164. 57 C

ANISOU 2715 CDl PHE B 144 24215 18939 19375 -110 1586 831 C

ATOM 2716 CEl PHE B 144 32.606 141.272 -32 696 1.00167. 97 C

ANISOU 2716 CEl PHE B 144 24553 19378 19891 -89 1479 807 C

ATOM 2717 CZ PHE B 144 31.810 140.160 -32.926 1.00170. 47 C

ANISOU 2717 CZ PHE B 144 24783 19682 20304 -18 1368 740 C

ATOM 2718 CE2 PHE B 144 30.439 140.270 -32, 816 1.00174. 76 C

ANISOU 2718 CE2 PHE B 144 25324 20214 20861 34 1347 714 C

ATOM 2719 CD2 PHE B 144 29.864 141.496 -32, 475 1.00174. 06 C

ANISOU 2719 CD2 PHE B 144 25317 20113 20703 22 1458 755 C

ATOM 2720 C PHE B 144 28.882 143.446 -29.737 1.00165. 30 C

ANISOU 2720 " C PHE B 144 24323 18902 19580 -271 1736 877 C

ATOM 2721 O PHE B 144 29.146 142.688 -28.815 1.00170. 12 O

ANISOU 2721 O PHE B 144 24859 19518 20260 -388 1665 884 O

ATOM 2722 N TYR B 145 27.654 143.617 -30, 219 1.00164. 27 N

ANISOU 2722 N TYR B 145 24181 18741 19492 -151 1740 867 N

ATOM 2723 CA TYR B 145 26.502 142.917 -29.662 1.00166. 48 C ANISOU 2723 CA TYR B 145 24370 18984 19900 -153 1665 862 C

ATOM 2724 CB TYR B 145 26.200 143.435 -28.262 1.00170.23 C

ANISOU 2724 CB TYR B 145 24892 19389 20398 -319 1792 903 C

ATOM 2725 CG TYR B 145 25.168 142.600 -27.568 1.00172.10 C

ANISOU 2725 CG TYR B 145 25029 19587 20773 -338 1706 896 C

ATOM 2726 CDl TYR B 145 25.532 141.470 -26.849 1.00173.23 C

ANISOU 2726 CDl TYR B 145 25101 19742 20978 -480 1622 885 C

ATOM 2727 CEl TYR B 145 24.584 140.683 -26.221 1.00172.39 C

ANISOU 2727 CEl TYR B 145 24900 19601 20999 -490 1538 874 C

ATOM 2728 CZ TYR B 145 23.254 141.026 -26.315 1.00171.78 C

ANISOU 2728 CZ TYR B 145 24802 19478 20990 -358 1537 884 C

ATOM 2729 OH TYR B 145 22.296 140.255 -25.702 1.00173.71 O

ANISOU 2729 OH TYR B 145 24952 19686 21362 -362 1451 880 O

ATOM 2730 CE2 TYR B 145 22.873 142.143 -27.027 1.00173.82 C

ANISOU 2730 CE2 TYR B 145 25121 19727 21194 -223 1619 914 C

ATOM 2731 CD2 •TYR B 145 23.828 142.917 -27.654 1.00171.47 C

ANISOU 2731 CD2 TYR B 145 24915 19465 20769 -212 1703 915 C

ATOM 2732 C TYR B 145 25.275 143.096 -30.540 1.00163.37 C

ANISOU 2732 C TYR B 145 23948 18582 19543 13 1641 872 C

ATOM 2733 O TYR B 145 24.950 144.212 -30.896 1.00166.15 O

ANISOU 2733 O TYR B 145 24372 18913 19845 74 1770 917 O

ATOM 2734 N PRO B 146 24.559 142.007 -30.865 1.00174.86 N

ANISOU 2734 N PRO B 146 25292 20055 21090 78 1480 844 N

ATOM 2735 CA PRO B 146 24.646 140.600 -30.444 1.00181.62 C

ANISOU 2735 CA PRO B 146 26045 20927 22036 25 1329 794 C

ATOM 2736. CB PRO B 146 23.485 139.945 -31.208 1.00182.42 C

ANISOU 2736 CB PRO B 146 26064 21046 22203 144 1198 785 C

ATOM 2737 CG PRO B 146 23.291 140.834 -32.396 1.00184.03 C

ANISOU 2737 CG PRO B 146 26322 21280 22320 263 1243 819 C

ATOM 2738 CD PRO B 146 23.441 142.197 -31.802 1.00179.75 C

ANISOU 2738 CD PRO B 146 25879 20684 21732 220 1446 880 C

ATOM 2739. C PRO B 146 25.944 139.907 -30.848 1.00183.44 C

ANISOU 2739 C PRO B 146 26260 21209 22230 4 1257 743 C

ATOM 2740 O PRO B 146 26.889 140.567 -31.273 1.00184.28 O

ANISOU 2740 O PRO B 146 26446 21337 22235 6 1333 750 O

ATOM 2741 N LYS B 147 25.981 138.584 -30.719 1.00170.18 N

ANISOU 2741 N LYS B 147 24477 19542 20640 -10 1124 698 N

ATOM 2742 CA LYS B 147 27.143 137.819 -31.142 1.00169.69 C

ANISOU 2742 CA LYS B 147 24386 19510 20577 -26 1075 661 C

ATOM 2743 CB LYS B 147 27.103 136.410 -30.537 1.00172.10 C

ANISOU 2743 CB LYS B 147 24564 19808 21019 -87 969 637 C

ATOM 2744 CG LYS B 147 28.418 135.610 -30.627 1.00177.11 C

ANISOU 2744 CG LYS B 147 25150 20455 21688 -128 955 633 C

ATOM 2745 CD LYS B 147 28.171 134.079 -30.491 1.00180.00 C

ANISOU 2745 CD LYS B 147 25380 20810 22200 -142 846 594 C

ATOM 2746 CE LYS B 147 29.360 133.234 -31.000 1.00182.54 C

ANISOU 2746 CE LYS B 147 25665 21128 22562 -128 851 579 C

ATOM 2747 NZ LYS B 147 28.976 132.060 -31.868 1.00182.26 N

ANISOU 2747 NZ LYS B 147 25522 21071 22656 -106 767 518 N

ATOM 2748 C LYS B 147 27.152 137.754 -32.662 1.00169.72 C

ANISOU 2748 C LYS B 147 24424 19548 20514 105 1030 606 C

ATOM 2749 O LYS B 147 28.201 137.882 -33.290 1.00166.36 O

ANISOU 2749 O LYS B 147 24045 19138 20028 118 1066 594 O

ATOM 2750 N ASP B 148 25.970 137.570 -33.244 1.00173.63 N

ANISOU 2750 N ASP B 148 24897 20056 21019 191 952 582 N

ATOM 2751 CA ASP B 148 25.836 137.421 -34.684 1.00170.54 C

ANISOU 2751 CA ASP B 148 24535 19706 20558 287 892 529 C

ATOM 2752 CB ASP B 148 24.362 137.377 -35.077 1.00177.57 C

ANISOU 2752 CB ASP B 148 25391 20621 21456 350 805 542 C

ATOM 2753 CG ASP B 148 23.704 136.051 -34.729 1.00191.16 C

ANISOU 2753 CG ASP B 148 27008 22321 23303 310 706 530 C

ATOM 2754 ODl ASP B 148 24.102 135 * .021 -35.320 1.00190.70 O

ANISOU 2754 ODl ASP B 148 26904 22267 23287 292 619 455 O

ATOM 2755 0D2 ASP B 148 22.786 136.032 -33.874 1.00192.51 O

ANISOU 2755 0D2 ASP B 148 27147 22464 23535 299 726 596 O

ATOM 2756 C ASP B 148 26.506 138.585 -35.361 1.00171.84 C

ANISOU 2756 C ASP B 148 24805 19890 20596 331 993 551 C

ATOM 2757 O ASP B 148 26.230 139.726 -35.024 1.00175.40 O

ANISOU 2757 O ASP B 148 25302 20330 21011 331 1091 617 O

ATOM 2758 N ILE B 149 27.401 138.296 -36.300 1.00165.06 N

ANISOU 2758 N ILE B 149 23990 19052 19675 366 984 496 N

ATOM 2759 CA ILE B 149 28.084 139.338 -37.079 1.00165.71 C

ANISOU 2759 CA ILE B 149 24173 19157 19632 420 1068 508 C

ATOM 2760 CB ILE B 149 29.386 139.824 -36.385 1.00155.55 C

ANISOU 2760 CB ILE B 149 22928 17845 18328 356 1183 551 C

ATOM 2761 CGl ILE B 149 29.740 141.242 -36.807 1.00151.78 ' C

ANISOU 2761 CGl ILE B 149 22553 17389 17726 407 1288 589 C ATOM 2762 CDl ILE B 149 30.981 141.728 -36.139 1.00150.45 C

ANISOU 2762 CDl ILE B 149 22435 17204 17524 329 1398 639 C

ATOM 2763 CG2 ILE B 149 30.549 138.907 -36.687 1.00155.49 C

ANISOϋ 2763 CG2 ILE B 149 22906 17819 18356 327 1172 515 C

ATOM 2764 C ILE B 149 28.361 138.820 -38.496 1.00168.18 C

ANISOU 2764 C ILE B 149 24525 19498 19878 477 1012 430 C

ATOM 2765 O ILE B 149 27.848 137.769 -38.880 1.00170.52 O

ANISOU 2765 O ILE B 149 24778 19794 20216 469 916 369 O

ATOM 2766 N ASN B 150 29.155 139.537 -39.282 1.00194.48 N

ANISOU 2766 N ASN B 150 27945 22849 23098 528 1076 428 N

ATOM 2767 CA ASN B 150 29.398 139.078 -40.642 1.00194.03 C

ANISOU 2767 CA ASN B 150 27940 22817 22965 570 1031 351 C

ATOM 2768 CB ASN B 150 28.093 139.105 -41.429 1.00196.37 C

ANISOU 2768 CB ASN B 150 28222 23178 23212 602 ' 937 359 C

ATOM 2769 CG ASN B 150 28.204 138.376 -42.736 1.00202.20 C

ANISOU 2769 CG ASN B 150 29013 23947 23867 603 871 271 C

ATOM 2770 ODl ASN B 150 28.985 137.430 -42.864 1.00202.73 O

ANISOU 2770 ODl ASN B 150 29136 23971 23921 592 914 196 O

ATOM 2771 ND2 ASN B 150 27.425 138.805 -43.722 1.00199.78 N

ANISOU 2771 ND2 ASN B 150 28691 23713 23505 604 774 290 N

ATOM 2772 C ASN B 150 30.459 139.843 -41.424 1.00192.14 C

ANISOU 2772 C ASN B 150 27801 22585 22619 618 1117 346 C

ATOM 2773 O ASN B 150 30.200 140.949 -41.893 1.00193.23 O

ANISOU 2773 O ASN B 150 27984 22771 22665 673 1147 387 O

ATOM 2774 N VAL B 151 31.642 139.244 -41.582 1.00162.81 N

ANISOU 2774 N VAL B 151 24113 18821 18927 600 1163 308 N

ATOM 2775 CA VAL B 151 32.696 139.824 -42.420 1.00158.98 C

ANISOU 2775 CA VAL B 151 23726 18337 18341 652 1236 295 C

ATOM 2776 CB VAL B 151 34.122 139.563 -41.881 1.00147.34 C

ANISOU 2776 CB VAL B 151 22259 16803 16922 624 1327 328 C

ATOM 2777 CGl VAL B 151 34.185 139.811 -40.381 1.00147.49 C

ANISOU 2777 CGl VAL B 151 22213 16817 17009 553 1359 423 C

ATOM 2778 CG2 VAL B 151 34.572 138.150 -42.222 1.00147.34 C

ANISOU 2778 CG2 VAL B 151 22234 16734 17015 597 1322 267 C

ATOM 2779 C VAL B 151 32.627 139.253 -43.821 1.00166.40 C

ANISOU 2779 C VAL B 151 24729 19288 19209 678 1193 199 C

ATOM 2780 O VAL B 151 31.973 138.237 -44.065 1.00168.99 O

ANISOU 2780 O VAL B 151 25028 19617 19565 643 1111 140 O

ATOM 2781 N LYS B 152 33.320 139.917 -44.736 1.00168.74 N

ANISOU 2781 N LYS B 152 25119 19591 19404 729 1252 182 N

ATOM 2782 CA LYS B 152 33.358 139.524 -46.134 1.00169.23 C

ANISOU 2782 CA LYS B 152 25266 19663 19370 743 1229 92 C

ATOM 2783 CB LYS B 152 32.086 140.006 -46.848 1.00171.78 C

ANISOU 2783 CB LYS B 152 25589 20090 19588 755 1136 104 C

ATOM 2784 CG LYS B 152 32.247 140.318 -48.334 1.00178.23 C

ANISOU 2784 CG LYS B 152 26509 20958 20254 778 1130 56 C

ATOM 2785 CD LYS B 152 31.045 141.079 -48.925 1.00176.65 C

ANISOU 2785 CD LYS B 152 26278 20878 19963 779 1032 111 C

ATOM 2786 CE LYS B 152 29.877 140.151 -49.259 1.00181.37 C

ANISOU 2786 CE LYS B 152 26840 21506 20565 687 912 74 C

ATOM 2787 NZ LYS B 152 28.986 140.693 -50.329 1.00176.12 N

ANISOU 2787 NZ LYS B 152 26163 20969 19786 664 810 132 N

ATOM 2788 C LYS B 152 34.589 140.195 -46.709 1.00165.99 C

ANISOU 2788 C LYS B 152 24946 19230 18893 799 1329 96 C

ATOM 2789 O LYS B 152 34.598 141.403 -46.884 1.00168.69 O

ANISOU 2789 O LYS B 152 25311 19626 19159 853 1356 155 O

ATOM 2790 N TRP B 153 35.648 139.439 -46.965 1.00161.04 N

ANISOU 2790 N TRP B 153 24367 18515 18307 789 1397 43 N

ATOM 2791 CA TRP B 153 36.862 140.063 -47.463 1.00162.76 C

ANISOU 2791 CA TRP B 153 24669 18705 18468 848 1492 57 C

ATOM 2792 CB TRP B 153 38.047 139.126 -47.335 1.00158.49 C

ANISOU 2792 CB TRP B 153 24133 18042 18043 831 1590 53 C

ATOM 2793 CG TRP B 153 38.571 139.006 -45.964 1.00155.72 C

ANISOU 2793 CG TRP B 153 23680 17660 17825 800 1624 165 C

ATOM 2794 CDl TRP B 153 38.060 138.243 -44.970 1.00160.32 C

ANISOU 2794 CDl- TRP B 153 24151 18236 18528 734 1577 193 C

ATOM 2795 NEl TRP B 153 38.826 138.363 -43.835 1.00162.27 N

ANISOU 2795 NEl TRP B 153 24322 18463 18870 698 1625 317 N

ATOM 2796 CE2 TRP B 153 39.862 13-9.220 -44.089 1.00157.06 C

ANISOU 2796 CE2 TRP B 153 23728 17797 18150 742 1704 374 C

ATOM 2797 CD2 TRP B 153 39.735 139.645 -45.422 1.00155.70 C

ANISOU 2797 CD2 TRP B 153 23675 17638 17846 816 1707 275 C

ATOM 2798 CE3 TRP B 153 40.679 140.534 -45.933 1.00155.70 C

ANISOU 2798 CE3 TRP B 153 23759 17634 17765 878 1780 307 C

ATOM 2799 CZ3 TRP B 153 41.704 140.966 -45.103 1.00151.79 C

ANISOϋ 2799 CZ3 TRP B 153 23229 17126 17318 860 1844 442 C

ATOM 2800 CH2 TRP B 153 41.800 140.529 -43.783 1.00145.91 C ANISOU 2800 CH2 TRP B 153 22367 16377 16695 769 1835 547 C

ATOM 2801 CZ2 TRP B 153 40.894 139.657 -43.258 1.00150 .89 C

ANISOU 2801 CZ2 TRP B 153 22912 17009 17412 711 1767 513 C

ATOM 2802 C TRP B 153 36.704 140.486 -48.919 1.00175 .65 C

ANISOU 2802 C TRP B 153 26411 20385 19943 885 1477 -15 C

ATOM 2803 O TRP B 153 36.058 139.790 -49.703 1.00182 .10 O

ANISOU 2803 O TRP B 153 27256 21227 20705 839 1409 -95 O

ATOM 2804 N LYS B 154 37.300 141.627 -49.269 1.00177 .99 N

ANisoσ 2804 N LYS B 154 26770 20698 20161 956 1538 19 N

ATOM 2805 CA LYS B 154 37.307 142.141 -50.640 1.00176 .59 C

ANISOO 2805 CA LYS B 154 26695 20570 19833 995 1530 -38 C

ATOM 2806 CB LYS B 154 36.407 143.379 -50.772 1.00179 .08 C

ANISOU 2806 CB LYS B 154 26980 21014 20049 1036 1469 25 C

ATOM 2807 CG LYS B 154 34.978 143.111 -51.271 1.00186 .91 C

ANISOU 2807 CG LYS B 154 27924 22091 21004 981 1348 12 C

ATOM 2808 CD LYS B 154 34.304 144.403 -51.779 1.00195, 34 C

ANISOU 2808 CD LYS B 154 28979 23281 21961 1033 1310 82 C

ATOM 2809 CE LYS B 154 33.058 144.116 -52.623 1.00198 76 C

ANISOU 2809 CE LYS B 154 29372 23810 22336 965 1183 86 C

ATOM 2810 NZ LYS B 154 32.749 145.220 -53.580 1.00187, 28 N

ANISOU 2810 NZ LYS B 154 27921 22475 20760 1004 1152 148 N

ATOM 2811 C LYS B 154 38.726 142.489 -51.092 1.00173. 57 C

ANISOU 2811 C LYS B 154 26399 20122 19426 1056 1640 -39 C

ATOM 2812 O LYS B 154 39.323 143.452 -50.614 1.00170, 77 O

ANISOU 2812 O LYS B 154 26032 19775 19077 . 1110 1694 48 O

ATOM 2813 N ILE B 155 39.261 141.695 -52.010 1.00155. 45 N

ANISOU 2813 N ILE B 155 24202 17759 17104 1038 1681 -136 N

ATOM 2814 CA ILE B 155 40.576 141.954 -52.584 1.00156.. 76 C

ANISOU 2814 CA ILE B 155 24460 17854 17247 1100 1788 -142 C

ATOM 2815 CB ILE B 155 41.356 140.656 -52.785 1.00152, 94 C

ANISOU 2815 CB ILE B 155 24020 17214 16878 1060 1891 -196 C

ATOM 2816 CGl ILE B 155 42.078 140.275 -51.513 1.00147. 79 C

ANISOU 2816 CGl ILE B 155 23255 16490 16410 1052 1943 -87 C

ATOM 2817 CDl ILE B 155 42.835 139.004 -51.657 1.00157. 28 C

ANISOU 2817 CDl ILE B 155 24477 17527 17755 1027 2071 -106 C

ATOM 2818 CG2 ILE B 155 42.394 140.823 -53.867 1.00160. 20 C

ANISOU 2818 CG2 ILE B 155 25062 18056 17752 1117 2001 -226 C

ATOM 2819 C ILE B 155 40.460 142.643 -53.939 1.00162. 31 C

ANISOU 2819 C ILE B 155 25267 18629 17774 1125 1758 -210 C

ATOM 2820 O ILE B 155 39.701 142.200 -54.804 1.00164. 81 O

ANISOU 2820 O ILE B 155 25633 18971 18017 1052 1702 -303 O

ATOM 2821 N ASP B 156 41.228 143.710 -54.134 1.00188. 31 N

ANISOU 2821 N ASP B 156 28592 21962 20995 1216 1791 -160 N

ATOM 2822 CA ASP B 156 41.145 144.463 -55.371 1.00191. 44 C

ANISOU 2822 CA ASP B 156 29075 22435 21228 1246 1762 -211 C

ATOM 2823 CB ASP B 156 C 42.017 143.819 -56.461 1.00195. 53 C

ANISOU 2823 CB ASP B 156 29734 22842 21716 1240 1853 -310 C

ATOM 2824 CG ASP B 156 43.470 144.293 -56.418 1.00188. 90 C

ANISOU 2824 CG ASP B 156 28931 21912 20930 1340 1975 -251 C

ATOM 2825 ODl ASP B 156 43.797 145.174 -55.601 1.00183. 89 O

ANISOU 2825 ODl ASP B 156 28215 21236 20417 1362 2015 -151 O

ATOM 2826 0D2 ASP B 156 44.292 143.789 -57.208 1.00187. 54 O

ANISOU 2826 0D2 ASP B 156 ' 28867 21714 20674 1387 2027 -296 O

ATOM 2827 C ASP B 156 39.675 144.500 -55.788 1.00196. 99 C

ANISOU 2827 C ASP B 156 29741 " 23255 21852 1169 1633 -240 C

ATOM 2828 O ASP B 156 39.258 143.741 -56.662 1.00202. 83 O

ANISOU 2828 O ASP B 156 30549 23983 22534 1077 1602 -338 O

ATOM 2829 N GLY B 157 38.888 145.352 -55.129 1.00180. 22 N

ANISOU .2829 N GLY B 157 27509 21236 19730 1195 1567 -144 N

ATOM 2830 CA GLY B 157 37.469 145.506 -55.429 1.00183. 40 C

ANISOU 2830 CA GLY B 157 ' 27847 21755 20081 1131 1445 -125 C

ATOM 2831 C GLY B 157 36.605 144.244 -55.492 1.00181. 57 C

ANISOU 2831 C GLY B 157 27613 21496 19878 1005 1379 -199 C

ATOM 2832 O GLY B 157 35.414 144.318 -55.797 1.00180. 56 O

ANISOU 2832 O GLY B 157 27460 21471 19675 929 1270 -194 O

ATOM 2833 N SER B 158 37.180 143.086 -55.188 1.00206. 28 N

ANISOU 2833 N SER B 158 30762 24492 23124 975 1448 -253 N

ATOM 2834 CA SER B 158 36.452 141.830 -55.340 1.00214. 65 C

ANISOU 2834 CA SER B 158 31839 25505 24213 854 ' 1413 -340 C

ATOM 2835 CB SER B 158 37.074 141.011 -56.468 1.00219. 18 C

ANISOU 2835 CB SER B 158 32566 25968 24746 805 1509 -468 C

ATOM 2836 OG SER B 158 36.648 139.663 -56.408 1.00227. 36 O

ANISOU 2836 OG SER B 158 33630 26931 25825 685 1513 -558 O

ATOM 2837 C SER B 158 36.407 140.990 -54.064 1.00215. 97 C

ANISOU 2837 C SER B 158 31907 25597 24554 835 1424 -313 C

ATOM 2838 O SER B 158 37.361 140.969 -53.296 1.00209. 47 O

ANISOU 2838 O SER B 158 31055 24685 23849 892 1516 -270 O ATOM 2839 N GLU B 159 35.301 140.286 -53.850 1.00188.30 N

ANISOU 2839 N GLU B 159 28347 22135 21065 746 1327 -328 N

ATOM 2840 CA GLU B 159 35.182 139.410 -52.692 1.00185 .79 C

ANISOU 2840 CA GLU B 159 27935 21747 20908 719 1329 -313 C

ATOM 2841 CB GLU B 159 33.721 139.026 -52.441 1.00188 .74 C

ANISOU 2841 CB GLU B 159 28229 22211 21271 642 1190 -297 C

ATOM 2842 CG GLU B 159 33.579 137.916 -51.390 1.00200 .81 C

ANISOU 2842 CG GLU B 159 29670 23664 22963 602 1189 -303 C

ATOM 2843 CD GLU B 159 32.134 137.526 -51.084 1.00207 07 C

ANISOU 2843 CD GLU B 159 30374 24545 23757 539 1049 -272 C

ATOM 2844 OEl GLU B 159 31.218 138.061 -51.752 1.00209 82 O

ANISOU 2844 OEl GLU B 159 30725 25016 23981 518 950 -234 O

ATOM 2845 0E2 GLU B 159 31.923 136.682 -50.171 1.00205, 00 O

ANISOU 2845 0E2 GLU ' B 159 30032 24231 23627 511 1036 -273 O

ATOM 2846 C GLU B 159 36.014 138.137 -52.831 1.00188. 45 C

ANISOU 2846 C GLU B 159 28336 21930 21338 671 1440 -407 C

ATOM 2847 O GLU B 159 36.061 137.532 -53.898 1.00187, 28 O

ANISOU 2847 O GLU B 159 28304 21744 21111 594 1467 -519 O

ATOM 2848 N ARG B 160 36.667 137.740 -51.741 1.00187. 59 N

ANISOU 2848 N ARG B 160 28148 21728 21398 706 1513 -353 N

ATOM 2849 CA ARG B 160 37.294 136.424 -51.635 1.00192. 76 C

ANISOU 2849 CA ARG B 160 28819 22232 22190 662 1624 -408 C

ATOM 2850 CB ARG B 160 38.768 136.552 -51.266 1.00183. 78 C

ANISOϋ 2850 CB ARG B 160 27674 20989 21164 738 1765 -334 C

ATOM 2851 CG ARG B 160 39.505 135.237 -51.201 1.00186. 30 C

ANISOU 2851 CG ARG B 160 28000 21136 21649 704 1911 -362 C

ATOM 2852 CD ARG B 160 40.962 135.447 -51.531 1.00187. 18 C

ANISOU 2852 CD ARG B 160 28162 21143 21813 775 2063 -307 C

ATOM 2853 NE ARG B 160 41.740 134.228 -51.361 1.00196. 70 N

ANISOU 2853 NE ARG B 160 29373 22168 23195 750 2232 -316 N

ATOM 2854 CZ ARG B 160 42.734 133.861 -52.164 1.00200. 02 C

ANISOU 2854 CZ ARG B 160 29905 22455 23638 777 2397 -342 C

ATOM 2855 NHl ARG B 160 43.058 134.617 -53.209 1.00190. 32 N

ANISOU 2855 NHl ARG B 160 28797 21264 22252 828 2398 -374 N

ATOM 2856 NH2 ARG B 160 43.392 132.727 -51.932 -1.00204. .08 N

ANISOU 2856 NH2 ARG B 160 30410 22791 24340 755 2571 -333 N

ATOM 2857 C ARG B 160 36.549 135.616 -50.577 1.00199. 34 C

ANISOU 2857 C ARG B 160 29523 23065 23151 611 1559 -384 C

ATOM 2858 O ARG B 160 36.068 136.178 -49.590 1.00191. 55 O

ANISOU 2858 O ARG B 160 28426 22160 22196 639 1476 -291 O

ATOM 2859 N GLN B 161 36.441 134.305 -50.784 1.00220. 66 N

ANISOU 2859 N GLN B 161 32245 25671 25924 533 1608 -472 N

ATOM 2860 CA GLN B 161 35.626 133.466 -49.908 1.00219. 65 C

ANISOU 2860 CA GLN B 161 32001 25540 25915 479 1545 -465 C

ATOM 2861 CB GLN B 161 34.418 132.919 -50.662 1.00223. 36 C

ANISOU 2861 CB GLN B 161 32522 26078 26266 378 1436 -565 C

ATOM 2862 CG GLN B 161 33.220 133.836 -50.658 1.00226. 09 C

ANISOU 2862 CG GLN B 161 32826 26595 26482 384 1264 -508 C

ATOM 2863 CD GLN B 161 32.105 133.329 -51.548 1.00240. 09 C

ANISOU 2863 CD GLN B 161 34647 28443 28133 265 1152 -584 C

ATOM 2864 OEl GLN B 161 32.320 132.479 -52.414 1.00239. .06 O

ANISOU 2864 OEl GLN B 161 34613 28236 27983 166 1211 -702 O

ATOM 2865 NE2 GLN B 161 30.905 133.852 -51.342 1.00246. 57 N

ANISOU 2865 NE2 GLN B 161 35403 29410 28873 265 1000 -506 N

ATOM 2866 C GLN B 161 36.401 132.313 -49.298 1.00220. 58 C

ANISOU 2866 C GLN B 161 32077 25498 26234 462 1687 -469 C

ATOM 2867 O GLN B 161 35.870 131.553 -48.490 1.00229. 42 O

ANISOU 2867 O GLN B 161 33137 26584 27447 400 1669 -505 O

ATOM 2868 N ASN B 162 37.659 132.180 -49.686 1.00211. 20 N

ANISOU 2868 N ASN B 162 30914 24210 25123 518 1834 -419 N

ATOM 2869 CA ASN B 162 38.485 131.113 -49.161 1.00210. 54 C

ANISOU 2869 CA ASN B 162 30777 23966 25253 508 1991 -390 C

ATOM 2870 CB ASN B 162 38.800 130.124 -50.267 1.00219. 90 C

ANISOU 2870 CB ASN B 162 32112 25018 26421 447 2131 -535 C

ATOM 2871 CG ASN B 162 39.637 130.744 -51.351 1.00224. 78 C

ANISOU 2871 CG ASN B 162 32903 25621 26883 472 2197 -594 C

ATOM 2872 ODl ASN B 162 39.374 131.874 -51.769 1.00221. 52 O

ANISOU 2872 ODl ASN B 162 32537 25348 26284 494 2070 -601 O

ATOM 2873 ND2 ASN B 162 40.667 130.028 -51.799 1.00226. 29 N

ANISOU 2873 ND2 ASN B 162 33186 25636 27157 472 2408 -628 N

ATOM 2874 C ASN B 162 39.789 131.672 --48.632 1.00204. 86 . C

ANISOU 2874 C ASN B 162 30007 23193 24638 586 2095 -244 C

ATOM 2875 O ASN B 162 40.387 132.555 -49.245 1.00207. 87 O

ANISOU 2875 O ASN B 162 30482 23588 24911 642 2126 -235 O

ATOM 2876 N GLY B 163 40.239 131.146 -47.503 1.00177. 91 N

ANISOU 2876 N GLY B 163 26441 19723 21435 582 2145 -120 N

ATOM 2877 CA GLY B 163 41.501 131.567 -46.931 1.00174. 40 C ANISOU 2877 CA GLY B 163 25925 19245 21093 633 2227 53 C

ATOM 2878 C GLY B 163 41.213 132.291 -45.646 1 00165.13 C

ANISOU 2878 C GLY B 163 24626 18210 19904 624 2085 171 C

ATOM 2879 O GLY B 163 42.114 132.820 -44.994 1 00156.16 ' O

ANISOU 2879 O GLY B 163 23421 17090 18821 639 2112 330 O

ATOM 2880 N VAL B 164 39.934 132.293 -45.287 1 00186.96 N

ANISOU 2880 N VAL B 164 27368 21071 22596 588 1940 94 N

ATOM 2881 CA VAL B 164 39.451 133.026 -44.127 1 00182.64 C

ANISOσ 2881 CA VAL B '164 26727 20651 22016 570 1808 176 C

ATOM 2882 CB VAL B 164 38.164 133.814 -44.468 1 00180.10 C

ANISOU 2882 CB VAL B 164 26480 20446 21503 580 1672 73 C

ATOM 2883 CGl VAL B 164 37.334 134.084 -43.225 1 00180.91 C

ANISOU 2883 CGl VAL B 164 26470 20639 21630 541 1551 126 C

ATOM 2884 CG2 VAL B 164 38.520 135.109 -45.145 1 00173.30 C

ANISOU 2884 ,CG2 VAL B 164 25731 19644 20472 645 1679 79 C

ATOM 2885 C VAL B 164 39.224 132.131 -42..907 1.00182..41 C

ANISOU 2885 C VAL B 164 26526 20612 22168 503 1777 256 C

ATOM 2886 O VAL B 164 38.813 130.970 -43..028 1, 00179..81 O

ANISOU 2886 O VAL B 164 26159 20232 21929 469 1773 181 O

ATOM 2887 N LEU B 165 39.506 132.691 -41..734 1, 00171..13 N

ANISOU 2887 N LEU B 165 25001 19236 20784 474 1756 409 N

ATOM 2888 CA LEU B 165 39.319 131.997 -40..468 1.00170..55 C

ANISOU 2888 CA LEU B 165 24757 19163 20882 396 1730 512 C

ATOM 2889 CB LEU B 165 40.646 131. 403 -39..993 1.00169..72 C

ANISOU 2889 CB LEU B 165 24557 18972 20958 373 1858 674 C

ATOM 2890 CG LEU B 165 41.571 130. 741 -41..008 1.00169..78 C

ANISOU 2890 CG LEU B 165 24573 18828 21106 408 2005 637 C

ATOM 2891 CDl LEU B 165 42.883 130.372 -40..332 1.00169..27 C

ANISOU 2891 CDl LEU B 165 24349 18696 21271 367 2113 850 C

ATOM 2892 CD2 LEU B 165 40.896 129.522 -41..600 1.00170..52 C

ANISOU 2892 CD2 LEU B 165 24666 18883 21241 395 1975 479 C

ATOM 2893 C LEU B 165 38.758 132.936 -39..387 1.00166..62 C

ANISOU 2893 C LEU B 165 24206 18782 20319 341 1622 585 C

ATOM 2894 O LEU B 165 39.333 133.986 -39..082 1.00163..41 O

ANISOU 2894 O LEU B 165 23831 18428 19831 331 1637 680 O

ATOM 2895 N ASN B 166 37.642 132.540 -38..794 1.00168..36 N

ANISOU 2895 N ASN B 166 24352 19036 20581 298 1526 542 N

ATOM 2896 CA ASN B 166 37.004 133.362 -37..785 1.00165..03 C

ANISOU 2896 CA ASN B 166 23892 18706 20105 240 1438 594 C

ATOM 2897 CB ASN B 166 35.641 133.830 -38..302 1.00164..12 C

ANISOU 2897 CB ASN B 166 23856 18643 19859 289 1346 466 C

ATOM 2898 CG ASN B 166 35.756 134.606 -39.607 1.00163..87 C

ANISOU 2898 CG ASN B 166 23977 18627 19661 377 1374 394 C

ATOM 2899 ODl ASN B 166 36.772 135.251 -39.858 1.00162..83 O

ANISOU 2899 ODl ASN B 166 23902 18498 19468 398 1446 456 O

ATOM 2900 ND2 ASN B 166 34.720 134.546 -40.443 1.00161..19 N

ANISOU 2900 ND2 ASN B 166 23697 18303 19243 421 1312 272 N

ATOM 2901 C ASN B 166 36.876 132.633 -36.447 1.00169.78 C

ANISOU 2901 C ASN B 166 24329 19311 20867 137 1399 683 C

ATOM 2902 O ASN B 166 36.736 131.408 -36.412 1.00173.66 O

ANISOU 2902 O ASN B 166 24731 19745 21505 129 1401 657 O

ATOM 2903 N SER B 167 36.958 133.392 -35.353 1.00185.90 N

ANISOU 2903 N SER B 167 26338 21420 22876 50 1372 786 N

ATOM 2904 CA SER B 167 36.654 132.900 -34.005 1.00182.12 C

ANISOU 2904 CA SER B 167 25719 20967 22513 -69 1318 866 C

ATOM 2905 CB SER B 167 37.866 132.205 -33.378 1.00174.73 C

ANISOU 2905 CB SER B 167 24643 20008 21739 -160 1375 1037 C

ATOM 2906 OG SER B 167 38.902 133.127 -33.082 1.00169.51 O

ANISOU 2906 OG SER B 167 24026 19375 21006 -203 1443 1168 O

ATOM 2907 C SER B 167 36.261 134.097 -33.158 1.00175.24 C

ANISOU 2907 C SER B 167 24898 20170 21516 -144 1288 904 C

ATOM 2908 O SER B 167 36.937 135.118 -33.208 1.00176.81 O

ANISOU 2908 O SER B 167 25191 20398 21591 -154 1344 955 O

ATOM 2909 N TRP B 168 35.171 133.997 -32.403 1.00165.34 N

ANISOU 2909 N TRP B 168 23591 18936 20294 -197 1214 876 N

ATOM 2910 CA TRP B 168 34.786 135.082 -31.495 1.00166.57 C

ANISOU 2910 CA TRP B 168 23797 19141 20351 -286 1215 917 C

ATOM 2911 CB TRP B 168 33.276 135.129 -31.284 1.00168.59 C

ANISOU 2911 CB TRP B 168 24063 19396 20597 -248 1Ϊ45 819 C

ATOM 2912 CG TRP B 168 32.478 135.449 -32.498 1.00174.26 C

ANISOU 2912 CG TRP B 168 24869 20104 21236 -92 1123 698 C

ATOM 2913 CDl TRP B 168 31.539 136.434 -32.625 1.00175.17 C

ANISOU 2913 CDl TRP 168 25071 20237 21250 -38 1121 656 C

ATOM 2914 NEl TRP B 168 31.007 136.414 -33.889 1.00182.90 N

ANISOU 2914 NEl TRP B 168 26099 21216 22178 90 1085 565 N

ATOM 2915 CE2 TRP B 168 31.599 135. 404 -34. 603 1.00183.92 C

ANISOU 2915 CE2 TRP B 168 26196 21318 22368 115 1075 527 C ATOM 2916 CD2 TRP B 168 32.531 134.,775 -33.,756 1,.00177.78 C

ANISOU 2916 CD2 TRP B 168 25326 20522 21700 14 1106 614 C

ATOM 2917 CE3 TRP B 168 33.274 133.702 -34.250 1,.00173 .45 C

ANISOU 2917 CE3 TRP B 168 24719 19929 21255 24 1127 611 C

ATOM 2918 CZ3 TRP B 168 33.075 133.303 -35.549 1.,00177 .01 C

ANISOU 2918 CZ3 TRP B 168 25228 20347 21679 123 1127 503 C

ATOM 2919 CH2 TRP B 168 32.147 133.949 -36.371 1.,00180 .77 C

ANISOU 2919 CH2 TRP B 168 25807 20854 22023 203 1083 410 C

ATOM 2920 CZ2 TRP B 168 31.398 134.998 -35.918 1.00184. 51 C

ANISOU 2920 CZ2 TRP B 168 26317 21379 22410 206 1053 431 C

ATOM 2921 C TRP B 168 35.441 134.846 -30.149 1.00166. 33 C

ANISOU 2921 C TRP B 168 23655 19138 20406 -470 1216 1063 C

ATOM 2922 O TRP B 168 35.952 133.765 -29.906 1.00169. 40 O

ANISOU 2922 O TRP B 168 23906 19510 20949 -507 1197 1125 O

ATOM 2923 N THR B 169 35.439 135.839 -29.268 1.00143. 80 N

ANISOU 2923 N THR B 169 20858 16325 17454 -598 1248 1128 N

ATOM 2924 CA THR B 169 35.868 135.571 -27.908 1.00145. 70 C

ANISOU 2924 CA THR B 169 20994 16603 17761 -805 1237 1266 C

ATOM 2925 CB THR B 169 36.524 136.792 -27.204 1.00148. 98 C

ANISOU 2925 CB THR B 169 21504 17070 18033 -962 1317 1383 C

ATOM 2926 OGl THR B 169 35.697 137.962 -27.320 1.00150. 75 O

ANISOU 2926 OGl THR B 169 21890 17285 18103 -936 1372 1296 O

ATOM 2927 CG2 THR B 169 37. 886 137. 065 -27. 791 1.00146. 49 C

ANISOU 2927 CG2 THR B 169 21212 16763 17685 -915 1371 1461 C

ATOM 2928 C THR B 169 34.622 135. 138 -27. 173 1.00154. 83 C

ANISOU 2928 C THR B 169 22106 17752 18971 -856 1174 1209 C

ATOM 2929 O THR B 169 33.553 135.027 -27. 779 1.00155. 35 O

ANISOU 2929 O THR B 169 22227 17785 19014 -729 1147 1079 O

ATOM 2930 N ASP B 170 34.755 134.871 -25.880 1.00186. 09 N

ANISOU 2930 N ASP B 170 25955 21745 23006 ■ -1046 1145 1317 N

ATOM 2931 CA ASP B 170 33.585 134.670 -25.046 1.00188. 13 C

ANISOU 2931 CA ASP B 170 26181 21996 23305 -1123 1095 1275 C

ATOM 2932 CB ASP B 170 33.929 133.870 -23.787 1.00189. 44 C

ANISOU 2932 CB ASP B 170 26189 22208 23582 -1336 1049 1414 C

ATOM 2933 CG ASP B 170 35.083 132.909 -23.999 1.00194. 22 C

ANISOU 2933 CG ASP B 170 26619 22819 24355 -1300 1010 1495 C

ATOM 2934 ODl ASP B 170 34.831 131.684 -24.099 1.00200. 07 O

ANISOU 2934 ODl ASP B 170 27300 23510 25208 -1129 966 1392 O

ATOM 2935 0D2 ASP B 170 36.241 133.383 -24.061 1.00194. 19 O

ANISOU 2935 0D2 ASP B 170 26539 22869 24375 -1453 1032 1672 O

ATOM 2936 C ASP B -170 33.067 136.049 -24.658 1.00192. 20 C

ANISOU 2936 C ASP B 170 26865 22505 23657 -1189 1176 1246 C

ATOM 2937 O ASP B 170 33.851 136.988 -24.479 1.00197. 59 O

ANISOU 2937 O ASP B 170 27640 23221 24213 -1320 1261 1331 O

ATOM 2938 N GLN B 171 31.749 136.178 -24.554 1.00166. 71 N

ANISOU 2938 N GLN B 171 23679 19228 20434 -1099 1160 1134 N

ATOM 2939 CA GLN B 171 31.168 137.385 -24.003 1.00167. 59 C 1

ANISOU 2939 CA GLN B 171 23934 19313 20431 -1173 1258 1118 C

ATOM 2940 CB GLN B 171 29.806 137.075 -23.399 1.00167. 47 C

ANISOU 2940 CB GLN B 171 23881 .19248 20502 -1155 1214 1052 C

ATOM 2941 CG GLN B 171 28.913 138.277 -23.235 1.00169. 24 C

ANISOU 2941 CG GLN B 171 24257 19414 20634 -1163 1337 1021 C

ATOM 2942 CD GLN B 171 27.454 137.892 -23.191 1.00172. 15 C

ANISOU 2942 CD GLN B 171 24585 19721 21102 -1066 1288 953 C

ATOM 2943 OEl GLN B 171 27.114 136.752 -22.882 1.00171. 84 O

ANISOU 2943 OEl GLN B 171 24405 19691 21195 -1050 1-158 933 O.

ATOM 2944 NE2 GLN B 171 26.580 138.839 -23.508 1.00172. 14 N

ANISOU 2944 NE2 GLN B 171 24700 19656 21051 -995 1396 928 N

ATOM 2945 C GLN B 171 32.132 137.870 -22.932 1.00174. 12 C

ANISOU 2945 C GLN B 171 24801 20184 21174 -1441 1331 1240 C

ATOM 2946 O GLN B 171 32.566 137.105 -22.074 1.00175. 67 O

ANISOU 2946 O GLN B 171 24874 20424 21448 -1608 1270 1332 O

ATOM 2947 N ASP B 172 32.506 139.133 -22.998 1.00178. 79 N

ANISOU 2947 N ASP B 172 25561 20767 21603 -1494 1465 1252 N

ATOM 2948 CA ASP B 172 33.596 139.588 -22.165 1.00178. 00 C

ANISOU 2948 CA ASP B 172 25516 20723 21393 -1751 1535 1375 C

ATOM 2949 CB ASP B 172 34 . 092 140 .943 -22.627 .1.00182. 32 C

ANISOU 2949 CB ASP B 172 26253 21262 21760 -1736 1680 1369 C

ATOM 2950 CG ASP B 172 35.588 141. 066 -22.517 1.00189. 28 C

ANISOO 2950 CG ASP B 172 27148 22224 22545 -1900 1702 1505 C

ATOM 2951 ODl ASP B 172 36.046 141. 967 -21.767 1.00184. 87 O

ANISOU 2951 ODl ASP B 172 26738 21678 21825 -2092 1826 1552 O

ATOM 2952 0D2 ASP B 172 36.289 140.244 -23. 174 1.00192. 12 O

ANISOU 2952 0D2 ASP B 172 27369 22630 22996 -1840 1602 1571 O

ATOM 2953 C ASP B 172 33.208 139.661 -20.707 1.00177. 71 C

ANISOU 2953 C ASP B 172 25494 20682 21347 -2009 1566 1414 C

ATOM 2954 O ASP B 172 32.046 139.877 -20.377 1.00176. 53 O ANISOU 2954 O ASP B 172 25407 20457 21211 -1986 1616 1330 O

ATOM 2955 N SER B 173 34.199 139.492 -19.839 1.00193 .19 N

ANISOU 2955 N SER B 173 27392 22724 23286 -2265 1539 1556 N

ATOM 2956 CA SER B 173 33.980 139.521 -18.398 1.00193 .45 C

ANISOU 2956 CA SER B 173 27457 22769 23276 -2567 1576 1610 C

ATOM 2957 CB SER B 173 35.271 139.187 -17.638 1.00183 .91 C

ANISOU 2957 CB SER B 173 26198 21679 22002 -2865 1553 1801 C

ATOM 2958 OG SER B 173 35.601 137.813 -17.729 1.00175 .21 O

ANISOU 2958 OG SER B 173 24860 20644 21069 -2826 1401 1903 O

ATOM 2959 C SER B 173 33.454 140.866 -17.911 1.00195 28 C

ANISOU 2959 C SER B 173 27924 22918 23355 -2635 1763 1531 C

ATOM 2960 O SER B 173 33.111 140.999 -16.741 1.00193 58 O

ANISOU 2960 O SER B 173 27754 22640 23158 -2737 1813 1483 O

ATOM 2961 N LYS B 174 33.390 141.862 -18.790 1.00192. 80 N

ANISOU 2961 N LYS B 174 27760 22595 22899 -2571 1880 1520 N

ATOM 2962 CA LYS B 174 33.049 143.211 -18.340 1.00188. 75 C

ANISOU 2962 CA LYS B 174 27479 22009 22228 -2677 2092 1474 C

ATOM 2963 CB LYS B 174 34.309 144.077 -18.261 1.00187, 80 C

ANISOU 2963 CB LYS B 174 27489 21954 21912 -2833 2190 1561 C

ATOM 2964 CG LYS B 174 35.173 143.705 -17.062 1.00193, 50 C

ANISOU 2964 CG LYS B 174 28169 22788 22566 -3195 2140 1720 C

ATOM 2965 CD LYS B 174 36.550 144.347 -17.081 1.00201. 29 C

ANISOU 2965 CD LYS B 174 29202 23874 23404 -3304 2157 1847 C

ATOM 2966 CE LYS B 174 37.307 144.007 -15.796 1.00204. 19 C

ANISOU 2966 CE LYS B 174 29514 24363 23705 -3696 2100 2033 C

ATOM 2967 NZ LYS B 174 38.675 144.598 -15.748 1.00203. 36 N

ANISOU 2967 NZ LYS B 174 29426 24369 23471 -3817 2094 2194 N

ATOM 2968 C LYS B 174 31.925 ' 143.909 -19.110 1.00190. 09 C

ANISOU 2968 C LYS B 174 27731 22057 22436 -2407 2188 1339 C

ATOM 2969 O LYS B 174 30.829 144.088 -18.587 1.00190. 60 O

ANISOU 2969 O LYS B 174 27831 22031 22559 -2425 ' 2252 1281 O

ATOM 2970 N ASP B 175 32.195 144.309 -20.345 l.OOiβl. 72 N

ANISOU 2970 N ASP B 175 26696 20997 21351 -2163 2200 1302 N

ATOM 2971 CA ASP B 175 31.184 144.980 -21.164 1.00180. 80 C

ANISOU 2971 CA ASP B 175 26655 20780 21260 -1926 2299 1206 C

ATOM 2972 CB ASP B 175 31.837 145.688 -22.355 1.00179. 52 C

ANISOU 2972 CB ASP B 175 26568 20638 21003 -1751 2355 1195 C

ATOM 2973 CG ASP B 175 32.948 144.860 -22.993 1.00179. 47 C

ANISOU 2973 CG ASP B 175 26446 20737 21008 -1677 2192 1237 C

ATOM 2974 ODl ASP B 175 33.163 143.702 -22.563 1.00176. 09 O

ANISOU 2974 ODl ASP B 175 25852 20351 20703 -1679 2026 1258 O

ATOM 2975 0D2 ASP B 175 33.612 145.373 -23.923 1.00179. 53 O

ANISOU 2975 0D2 ASP B 175 26529 20777 20909 -1613 2244 1253 O

ATOM 2976 C ASP B 175 30.130 144.005 -21.663 1.00175. .85 C

ANISOU 2976 C ASP B 175 25876 20121 20817 -1702 2156 1142 C

ATOM 2977 O ASP B 175 29.093 144.413 -22.189 1.00172. 07 O

ANISOU 2977 O ASP B 175 25432 19563 20385 -1524 2220 1085 O

ATOM 2978 N SER B 176 30.414 142.716 -21.496 1.00194. 32 N

ANISOU 2978 N SER B 176 28044 22525 23262 -1721 1968 1164 N

ATOM 2979 CA SER B 176 29.541 141.652 -21.977 1.00197. 27 C

ANISOU 2979 CA SER B 176 28262 22886 23806 -1526 1811 1106 C

ATOM 2980 CB SER B 176 28.215 141.669 -21.218 1.00196. 07 C

ANISOU 2980 CB SER B 176 28111 22647 23738 -1572 1846 1072 C

ATOM 2981 OG SER B 176 28.451 141.629 -19.821 1.00190. 26 O

ANISOU 2981 OG SER B 176 27382 21926 22984 -1861 1867 1127 O

ATOM 2982 C SER B 176 ' 29.322 141.765 -23.487 1.00194. 87 C

ANISOU 2982 C SER B 176 27940 22579 23521 -1231 1765 1044 C

ATOM 2983 O SER B 176 28.185 141.851 -23.962 1.00185. 97 O

ANISOU 2983 O SER B 176 26801 21396 22463 -1065 1756 989 O

ATOM 2984 N THR B 177 30.431 141.763 -24.228 1.00181. 49 N

ANISOU 2984 N THR B 177 26242 20950 21766 -1180 1733 1066 N

ATOM 2985 CA THR B 177 30.415 141.919 -25.682 1.00175. 46 C

ANISOU 2985 CA THR B 177 25489 20194 20985 -938 1706 1014 C

ATOM 2986 CB THR B 177 30.781 143.348 -26.102 1.00175. 05 C

ANISOU 2986 CB THR B 177 25601 20127 20782 -918 1871 1024 C

ATOM 2987 OGl THR B ' 177 32.207 143.466 -26.211 1.00169. 61 O

ANISOU 2987 OGl THR B 177 24953 19499 19993. -1044 1899 1090' O

ATOM 2988 CG2 THR 1 B 177 30.246 144.352 -25.089 1.00180. 34 C

ANISOU 2988 CG2 THR ' B 111 26385 20718 21417 -1028 2039 1032 C

ATOM 2989 C THR B 177 31.381 140.976 -26.397 1.00173. 91 C

ANISOU 2989 C THR B 177 25201 20063 20814 -882 1593 1029 C

ATOM 2990 O THR B 177 32.515 140..752 -25.963 1.00168. 54 O

ANISOU 2990 O THR B 177 24522 19431 20086 -1018 1610 1110 O

ATOM 2991 N TYR B 178 30.924 140.445 -27.519 1.00179. 32 N

ANISOU 2991 N TYR B 178 25813 20746 21574 -688 1489 959 N

ATOM 2992 CA TYR B 178 31.736 139.544 -28.303 1.00176. 63 C

ANISOU 2992 CA TYR B 178 25399 20442 21272 -612 1406 956 C ATOM 2993 CB TYR B 178 30.823 138.635 -29.115 1.00173.92 C

ANISOU 2993 CB TYR B 17.8 24970 20082 21029 -448 1289 865 C

ATOM 2994 CG TYR B 178 29.713 138.047 -28.276 1.00174 .61 C

ANISOU 2994 CG TYR B 178 24982 20142 21221 -487 1228 844 C

ATOM 2995 CDl TYR B 178 28.408 138.480 -28.422 1.00176 .12 C

ANISOU 2995 CDl TYR B 178 25211 20300 21407 -392 1233' 800 C

ATOM 2996 CEl TYR B 178 27.386 137.944 -27.654 1.00185 .54 C

ANISOU 2996 CEl TYR B 178 26333 21460 22702 -423 1179 789 C

ATOM 2997 CZ TYR B 178 27.667 136.974 -26.712 1.00186 15 C

ANISOU 2997 CZ TYR B 178 26305 21543 22882 -555 1117 812 C

ATOM 2998 OH TYR B 178 26.646 136.448 -25.945 1.00180 47 O

ANISOU 2998 OH TYR B 178 25517 20789 22264 -581 1062 798 O

ATOM 2999 CE2 TYR B 178 28.965 136.537 -26.539 1.00180, 64 C

ANISOU 2999 CE2 TYR B 178 25559 20884 22192 -658 1112 864 C

ATOM 3000 CD2 TYR B 178 29.978 137.077 -27.316 1.00176. 27 C

ANISOU 3000 CD2 TYR B 178 25074 20358 21541 -624 1170 887 C

ATOM 3001 C TYR B 178 32.687 140.331 -29.198 1.00174, 88 C

ANISOU 3001 C TYR B 178 25282 20242 20922 -546 1482 969 C

ATOM 3002 O TYR B 178 32.352 141.419 -29.663 1.00174. 44 O

ANISOU 3002 O TYR B 178 25340 20174 20766 -465 1563 939 O

ATOM 3003 N SER B 179 33.879 139.786 -29.410 1.00180. 88 N

ANISOU 3003 N SER B 179 25997 21033 21696 -583 1464 1029 N

ATOM 3004- CA SER B 179 34.869 140.393 -30.290 1.00178. 55 C

ANISOU 3004 CA SER B 179 25785 20755 21299 -509 1522 1044 C

ATOM 3005 CB SER B 179 35.960 141.065 -29.459 1.00175. 73 C

ANISOU 3005 CB SER B 179 25478 20437 20855 -692 1603 1170 C

ATOM 3006 OG SER B 179 35.420 141.623 -28.272 1.00173. 42 O

ANISOU 3006 OG SER B 179 25244 20143 20505 -857 1669 1198 O

ATOM 3007 C SER B 179 35.471 139.271 -31.114 1.00172. 96 C

ANISOU 3007 C SER B 179 24986 20039 20692 -406 1449 1024 C

ATOM 3008 O SER B 179 35.809 138.238 -30.553 1.00176. 66 O

ANISOU 3008 O SER B 179 25324 20503 21294 -474 1389 1068 O

ATOM 3009 N MET B 180 35.604 139.452 -32.427 1.00148. 40 N'

ANISOU 3009 N MET B 180 21943 16919 17524 -248 1463 960 N

ATOM 3010 CA MET B 180 36.067 138.358 -33.289 1.00149. 45 C

ANISOU 3010 CA MET B 180 ' 22011 17024 17750 -153 1417 923 C

ATOM 3011 CB MET B 180 34.913 137.806 -34.122 1.00152. 42 C

ANISOU 3011 CB MET B 180 22382 17377 18152 -25 13.44 788 C

ATOM 3012 CG MET B 180 34.523 138.697 -35.285 1.00154. 43 C

ANISOU 3012 CG MET B 180 22761 17644 18272 111 1369 712 C

ATOM 3013 SD MET B 180 34.010 137.775 -36.749 1.00149. 49 S

ANISOU 3013 SD MET B 180 22132 16994 17673 240 1295 580 S

ATOM 3014 CE MET B 180 35.532 136.958 -37.178 1.00151. 04 C

ANISOU 3014 CE MET B 180 22302 17138 17948 236 1349 609 C

ATOM 3015 C MET B 180 37.194 138.736 -34.234 1.00148. 42 C

ANISOU 3015 C MET B 180 21957 16889 17545 -75 1480 939 C

ATOM 3016 O MET B 180 37.131 139.769 -34.880 1.00151. 47 O

ANISOU 3016 O MET B 180 22463 Ϊ7296 17792 -19 1531 915 O

ATOM 3017 N SER B 181 38.213 137.888 -34.335 1.00147. 78 N

ANISOU 3017 N SER B 181 21807 16774 17568 -65 1487 981 N

ATOM 3018 CA SER B 181 39.284 138.116 -35.298 1.00146. 55 C

ANISOU 3018 CA SER B 181 21724 16599 17360 17 1554 996 C

ATOM 3019 CB SER B 181 40.623 137.613 -34.758 1.00144. 02 C

ANISOU 3019 CB SER B 181 21325 16274 17122 -84 1605 1172 C

ATOM 3020 OG SER B 181 40.853 136.254 -35.101 1.00151. 07 O

ANISOU 3020 OG SER ' B 181 22098 17101 18200 -66 1606 1194 O

ATOM 3021 C SER B 181 38.945 137.413 -36.606 1.00152. 63 C

ANISOU 3021 C SER B 181 22516 17310 18166 158 1543 866 C

ATOM 3022 O SER B 181 38.112 136.514 -36.622 1.00156. 01 O

ANISOU 3022 O SER B 181 22874 17708 18696 167 1488 797 O

ATOM 3023 N SER B 182 39.589 137.815 -37.700 1.00149. 42 N

ANISOU 3023 N SER B 182 22215 16887 17671 256 1598 832 N

ATOM 3024 CA SER B 182 39.331 137.219 -39.015 1.00147. 37 C

ANISOU 3024 CA SER B 182 22009 16573 17410 368 1600 701 C

ATOM 3025 CB SER B 182 38.143 137.904 -39.673 1.00141. 46 C

ANISOU 3025 CB SER B 182 21354 15876 16517 440 1542 578 C

ATOM 3026 OG SER B 182 38.017 137.479 -41.009 1.00143. 74 O-

ANISOU 3026 OG SER B 182 21706 16126 16782 519 1538 458 O

ATOM- 3027 C SER B 182 40.551 137.282 -39.939 1.00146. 74 C

ANISOQ 3027 C SER B 182 21996 16443 17317 429 1695 731 C

ATOM 3028 O SER B 182 40.924 138.350 -40.415 1.00145. 34 O

ANISOU 3028 O SER B 182 21918 16301 17002 475 1727 740 O

ATOM 3029 N THR B 183 41.154 136.129 -40.205 1.00145. 41 N

ANISOU 3029 N THR B 183 21770 16182 17298 432 1753 749 N

ATOM 3030 CA THR B 183 .42.483 136.089 -40.801 1.00144. 45 C

ANISOU 3030 CA THR B 183 21682 15994 17210 473 1865 824 C

ATOM 3031 CB THR B 183 43.442 135.258 -39.948 1.00144. 74 C ANISOU 3031 CB THR B 183 21567 15985 17441 390 1923 1013 C

ATOM 3032 OGl THR B 183 43.381 135.687 -38.581 1.00144.61 O

ANISOU 3032 OGl THR B 183 21458 16060 17427 269 1852 1127 O

ATOM 3033 CG2 THR B 183 44.859 135.393 -40.473 1.00141.04 C

ANISOU 3033 CG2 THR B 183 21131 15473 16985 423 2031 1140 C

ATOM 3034 C THR B 183 42.537 135.488 -42.191 1.00151.62 C

ANISOU 3034 C THR B 183 22679 16803 18127 563 1932 694 C

ATOM 3035 O THR B 183 42.412 134.270 -42.355 1.00152.07 O

ANISOU 3035 O THR B 183 22681 16770 18328 551 1973 656 O

ATOM 3036 N LEU B 184 42.769 136.349.-43.179 1.00149.72 N

ANISOU 3036 N LEU B 184 22580 16576 17730 644 1955 626 N

ATOM 3037 CA LEU B 184 42.996 135.936 -44.564 1.00150.36 C

ANISOU 3037 CA LEU B 184 22777 16567 17787 716 2032 506 C

ATOM 3038 CB LEU B 184 42.651 137.079 -45.517 1.00142.56 C

ANISOU 3038 CB LEU B 184 21937 15651 16580 786 1992 405 C

ATOM 3039 CG LEU B 184 42.850 136.825 -47.008 1.00143.74 C

ANISOU 3039 CG LEU B 184 22222 15729 16663 835 2048 256 C

ATOM 3040 CDl LEU B 184 41.526 136.584 -47.690 1.00147.30 C

ANISOU 3040 CDl LEU B 184 22718 16245 17003 813 1939 105 C

ATOM 3041 CD2 LEU B 184 43.522 138.021 -47.624 1.00144.68 C

ANISOU 3041 CD2 LEU B 184 22456 15864 16650 913 2093 264 C

ATOM 3042 C LEU B 184 44.454 135.533 -44.765 1.00150.12 C

ANISOU 3042 C LEU B 184 22734 16418 17886 739 2182 618 C

ATOM 3043 O LEU B 184 45.354 136.367 -44.656 1.00142.40 O

ANISOU 3043 O LEU B 184 21777 15464 16865 764 2217 733 O

ATOM 3044 N THR B 185 44.684 134.255 -45.049 1.00164.60 N

ANISOU 3044 N THR B 185 24535 18119 19885 730 2282 595 N

ATOM 3045 CA THR B 185 46.040 133.740 -45.225 1.00165.40 C

ANISOU 3045 CA THR B 185 24612 18084 20147 756 2451 720 C

ATOM 3046 CB THR B 185 46.233 132.382 -44.500 1.00168.43 C

ANISOU 3046 CB THR B 185 24830 18366 20798 698 2534 826 C

ATOM 3047 OGl THR B 185 46.185 132.574 -43.075 1.00165.71 O

ANISOU 3047 OGl THR B 185 24317 18121 20525 620 2448 1009 O

ATOM 3048 CG2 THR B 185 47.567 131.741 -44.892 1.00161.35 C

ANISOU 3048 CG2 THR B 185 23927 17295 20084 740 2745 936 C

ATOM 3049 C THR B 185 46.354 133.578 -46.709 1.00166.98 C

ANISOU 3049 C THR B 185 24984 18172 20288 828 2569 584 C

ATOM 3050 O THR B 185 45.544 133.028 -47.458 1.00167.66 O

ANISOU 3050 O THR B 185 25163 18225 20314 818 2565 395 O

ATOM 3051 N LEU B 186 47.519 134.065 -47.134 1.00163.92 N

ANISOU 3051 N LEU B 186 24643 17729 19911 888 2673 685 N

ATOM 3052 CA LEU B 186 47.934 133.955 -48.534 1.00165.55 C

ANISOU 3052 CA LEU B 186 25018 17816 20067 954 2802 570 C

ATOM 3053 CB LEU B 186 47.601 135.235 -49.302 1.00163.43 C

ANISOU 3053 CB LEU B 186 24903 17663 1953.0 1005 2702 449 C

ATOM 3054 CG LEU B 186 46.195 135.828 -49.228 1.00168.32 C

ANISOU 3054 CG LEU B 186 25558 18437 19960 973 2520 299 C

ATOM 3055 CDl LEU B 186 46.144 137.073 -50.086 1.00162.27 C

ANISOU 3055 CDl LEU B 186 24916 17772 18967 1037 2455 240 C

ATOM 3056 CD2 LEU B 186 45.132 134.834 -49.663 1.00174.48 C

ANISOU 3056 CD2 LEU B 186 26396 19162 20736 917 2524 118 C

ATOM 3057 C LEU B 186 49.431 133.677 -48.656 1.00162.94 C

ANISOU 3057 C LEU B 186 24663 17338 19907 1002 2991 743 C

ATOM 3058 O LEU B 186 50.174 133.868 -47.696 1.00158.43 O

ANISOU 3058 O LEU B 186 23971 16808 19417 998 2983 964 O

ATOM 3059 N THR B 187 49.864 133.227 -49.837 1.00164.88 _N

ANISOU 3059 N THR B 187 25030 17411 20204 1036 3165 645 N

ATOM 3060 CA THR B 187 51.285 133.039 -50.135 1.00163.59 C

ANISOU 3060 CA THR B 187 24885 17087 20186 1100 3367 784 C

ATOM 3061 CB THR B 187 51.498 132.584 -51.580 1.00168.41 C

ANISOU 3061 CB THR B 187 25694 17523 20772 1123 3540 592 C

ATOM 3062 OGl THR B 187 50.414 131.745 -52.009 1.00162.12 O

ANISOU 3062 OGl THR B 187 25003 16791 19805 1059 3438 340 O

ATOM 3063 CG2 THR B 187 52.850 131.881 -51.730 1.00173.89 C

ANISOU 3063 CG2 THR B 187 26330 17975 21765 1121 3804 694 C

ATOM 3064 C THR B 187 51.947 134.390 -50.078 1.00163.34 C

ANISOU 3064 C THR B 187 24896 17160 20004 1165 3293 870 C

ATOM 3065 O THR B 187 51.258 135.406 -50.116 1.00166.31 O

ANISOU 3065 O THR B 187 25358 17693 20141 1175 3131 747 O

ATOM 3066 N LYS B 188 53.272 134.442 -50.032 1.00164.11 N

ANISOU 3066 N LYS B 188 24939 17172 20242 1213 3417 ] L086 N

ATOM 3067 CA LYS B 188 53.890 135.751 -50.198 1.00163.13 C

ANISOU 3067 CA LYS B 188 24877 17146 19959 1276 3351 : L154 C

ATOM 3068 CB LYS B 188 55.40l ' l35.710 -49.979 1.00162.27 C

ANISOU 3068 CB LYS B 188 24689 16935 20033 1318 3494 : L427 C

ATOM 3069 CG LYS B 188 56.074 137.077 -50.163 1.00156.92 C

ANISOU 3069 CG LYS B 188 24118 16323 19182 1398 3458 ] L456 C ATOM 3070 CD LYS B 188 57.583 137.009 -49.947 1.00161.83 C

ANISOU 3070 CD LYS B 188 24633 16883 19972 1422 3560 1769 C

ATOM 3071 CE LYS B 188 58.291 138.281 -50.397 1.00163 .01 C

ANISOU 3071 CE LYS B 188 24910 17082 19946 1511 3538 1775 C

ATOM 3072 . NZ LYS B 188 59.757 138.035 -50.534 1.00167 .01 N

ANISOU 3072 NZ LYS B 188 25307 17548 20601 1525 3618 2101 N

ATOM 3073 C LYS B 188 53.566 136.236 -51.607 1.00163 .96 C

ANISOU 3073 C LYS B 188 • 25208 17246 19844 1342 3348 913 C

ATOM 3074 O LYS B 188 52.837 137.207 -51.801 1.00161 .05 O

ANISOU 3074 O LYS B 188 24906 17043 19244 1355 3188 817 O

ATOM 3075 N ASP B 189 54.093 135.515 -52.587 1.00178. 30 N

ANISOU 3075 N ASP B 189 27140 18866 21738 1372 3537 818 N

ATOM 3076 CA ASP B 189 53.907 135.840 -53.990 1.00178 15 C

ANISOU 3076 CA ASP B 189 27341 18826 21521 1419 3556 607 C

ATOM 3077 CB ASP B 189 54.388 134.680 -54.851 1.00183. 86 C

ANISOU 3077 CB ASP B 189 28179 19290 22388 1447 3822 572 C

ATOM 3078 CG ASP B 189 55.766 134.199 -54.447 1.00184. 47 C

ANISOU 3078 CG ASP B 189 28112 19206 22774 1479 4009 845 C

ATOM 3079 ODl ASP B 189 56.645 135.054 -54.207 1.00180. .75 O

ANISOU 3079 ODl ASP B 189 27620 18717 22340 1559 4053 1024 O

ATOM 3080 OD2 ASP B 189 55.968 132.970 -54.362 1.00186. 76 O

ANISOU 3080 OD2 ASP B 189 28303 19383 23276 1423 4119 891 O

ATOM 3081 C ASP B 189 52.468 136.203 -54.326 1.00176. 09 C

ANISOU 3081 C ASP B 189 27174 18689 21043 1356 3404 355 C

ATOM 3082 O ASP B 189 52.240 137.160 -55.053 1.00181. 58 O

ANISOU 3082 O ASP B 189 28024 19440 21530 1383 3355 205 O

ATOM 3083 N GLU B 190 51.498 135.460 -53.803 1.00164. 26 N

ANISOU 3083 N GLU B 190 25579 17236 19595 1271 3329 318 N

ATOM 3084 CA GLU B 190 50.107 135.808 -54.067 1.00164. 59 C

ANISOU 3084 CA GLU B 190 25682 17424 19430 1212 3156 123 C

ATOM 3085 CB GLU B 190 49.120 134.722 -53.625 1.00172. 32 C

ANISOU 3085 CB GLU B 190 26573 18392 20509 1114 3130 72 C

ATOM 3086 CG GLU B 190 47.661 135.234 -53.589 1.00185. 11 C

ANISOU 3086 CG GLU B 190 28182 20214 21939 1059 2900 -43 C

ATOM 3087 CD GLU B 190 46.594 134.160 -53.861 1.00195. 80 C

ANISOU 3087 CD GLU B 190 29650 21548 23198 964 2888 -259 C

ATOM 3088 OEl GLU B 190 45.631 134.473 -54.616 1.00187. 55 O

ANIΞOU 3088 OEl GLU B 190 28734 20599 21928 946 2797 -394 O

ATOM 3089 OE2 GLU B 190 46.711 133.025 -53.320 1.00201. 50 O

ANISOU 3089 OE2 GLU B 190 30324 22170 24067 895 2962 -283 O

ATOM 3090 C GLU B 190 49.736 137.131 -53.422 1.00164. 30 C

ANISOU 3090 C GLU B 190 25581 17605 19241 1244 2957 188 C

ATOM 3091 O GLU B 190 49.189 138.012 -54.076 1.00167. 12 O

ANISOU 3091 O GLU B 190 26030" 18086 19381 1255 2839 67 O

ATOM 3092 N TYR B 191 50.023 137.279 -52.138 1/00166. 36 N

ANISOU 3092 N TYR B 191 25681 17909 19619 1247 2927 389 N

ATOM 3093 CA TYR B 191 49.699 138.528 -51.460 1.00168. 62 C

ANISOU 3093 CA TYR B 191 25914 18385 19770 1259 2766 459 C

ATOM 3094 CB TYR B 191 50.317 138.563 -50.065 1.00166. 84 C

ANISOU 3094 CB TYR B 191 25524 18175 19691 1234 2775 704 C

ATOM 3095 CG TYR B 191 50.334 139.927 -49.419 1.00160. 28 C

ANISOU 3095 CG TYR B 191 24669 17516 18714 1237 2652 787 C

ATOM 3096 CDl TYR B 191 49.164 140.644 -49.237 1.00157. 31 C

ANISOU 3096 CDl TYR B 191 24313 17286 18171 1217 2508 675 C

ATOM 3097 CEl TYR B 191 49.174 141.882 -48.638 1.00157. 92 C

ANIΞOU 3097 CEl TYR B 191 24379 17501 18123 1213 2428 747 C

ATOM 3098 CZ TYR B 191 50.364 142.419 -48.207 1.00165. 16 C

ANISOU 3098 CZ TYR B 191 25268 18424 19060 1217 2475 929 C

ATOM 3099 OH TYR B 191 50.385 143.663 -47.609 1.00165. 93 O

ANISOU 3099 OH TYR B 191 25372 18655 19020 1196 2411 992 O '

ATOM 3100 CE2 TYR B 191 51.541 141.719 -48.371 1.00163. 90 C

ANISOU 3100 CE2 TYR B 191 25078 18134 19061 1235 2597 1058 C

ATOM 3101 CD2 TYR B 191 51.519 140.482 -48.967 1.00158. 40 C

ANISOU 3101 CD2 TYR B 191 24388 17288 18510 1252 2692 990 C

ATOM 3102 C TYR B 191 50.189 139.710 -52.284 1.00169. 71 C

ANISOU 3102 C TYR B 191 26184 18570 19727 1347 2759 418 C

ATOM 3103 O TYR B 191 49.484 140.707 -52:435 1.00170. 62 O

ANISOU 3103 O TYR B 191 26347 18832 19649 1360 2631 331 O

ATOM 3104 N GLU B 192 51.392 139.574 -52.835 1.00180. 15 N

ANISOU 3104 N GLU B 192 27559 19762 21126 1410 2905 491 N

ATOM 3105 CA GLU B 192 52.025 140.655 -53.579 1.00178. 97 C

ANISOU 3105 CA GLU B 192 27527 19643 20830 1503 2914 477 C

ATOM 3106 CB GLU B 192 53.519 140.367 -53.805 1.00173. 57 C

ANISOU 3106 CB GLU B 192 26860 18791 20297 1565 3093 615 C

ATOM 3107 CG GLU B 192 54.419 140.765 -52.625 1.00176. 62 C

ANISOU 3107 CG GLU B 192 27084 19190 20832 1552 3106 888 C

ATOM 3108 CD GLU B 192 55.896 140.474 -52.863 1.00177. 23 C ANISOU 3108 CD GLU B 192 27192 19164 20985 1635 3237 1046 C

ATOM 3109 OEl GLU B 192 56.228 139.969 -53.949 1.00190 .48 O

ANISOU 3109 OEl GLU B 192 29024 20778 22571 1714 3300 923 O

ATOM 3110 0E2 GLU B 192 56.729 140.745 -51.970 1.00168 .38 O

ANISOU 3110 0E2 GLU B 192 25938 18027 20011 1615 3276 1299 O

ATOM 3111 C GLU B 192 51.318 140.987 -54.898 1.00182 .34 C

ANISOU 3111 C GLU B 192 28118 20105 21059 1519 2872 247 C

ATOM 3112 O GLU B 192 51.315 142.141 -55.326 1.00182 .86 O

ANISOU 3112 O GLU B 192 28257 20269 20954 1582 2811 215 O

ATOM 3113 N ARG B 193 50.702 139'.994 -55.533 1.00161 24 N

ANISOU 3113 N ARG B 193 25500 17360 18403 1449 2904 96 N

ATOM 3114 CA ARG B 193 50.083 140.216 -56.841 1.00158, 73 C

ANISOU 3114 CA ARG B 193 25343 17070 17898 1432 2874 -108 C

ATOM 3115 CB ARG B 193 49.718 138.891 -57.529 1.00164. 79 C

ANISOU 3115 CB ARG B 193 26190 17696 18726 1334 2977 -250 C

ATOM 3116 CG ARG B 193 50.908 137.931 -57.730 1.00173. 90 C

ANISOU 3116 CG ARG B 193 27393 18603 20077 1355 3221 -203 C

ATOM 3117 CD ARG B 193 50.679 136.947 -58.878 1.00179. 14 C

ANISOU 3117 CD ARG B 193 28210 19121 20733 1254 3351 -392 C

ATOM 3118 NE ARG B 193 51.096 135.581 -58.547 1.00180. 42 N

ANISOU 3118 NE ARG B 193 28323 19075 21155 1221 3549 -333 N

ATOM 3119 CZ ARG B 193 50.277 134.636 -58.074 1.00177. 01 C

ANISOU 311 * 9 CZ ARG B 193 27852 18612 20791 1115 3555 -403 C

ATOM 3120 NHl ARG B 193 48.988 134.894 -57.870 1.00166. 83 N

ANISOU 3120 NHl ARG B 193 26572 17489 19326 1028 3367 -531 N

ATOM 3121 NH2 ARG B 193 50.742 133.423 -57.805 1.00180. .28 N

ANISOU 3121 NH2 ARG B 193 28212 18827 21459 1098 3757 -333 N

ATOM 3122 C ARG B 193 48.879 141.155 -56.776 1.00157. 41 C

ANISOU 3122 C ARG B 193 25158 17120 17532 1415 2674 -173 C

ATOM 3123 O ARG B 193 48.337 141.556 -57.802 1.00162. 89 O

ANISOU 3123 O ARG B 193 25964 17872 18053 1399 2624 -309 O

ATOM 3124 N HIS B 194 48.478 141.527 -55.569 1.00163. 70 N

ANISOU 3124 N HIS B 194 25812 18031 18355 1410 2567 -67 N

ATOM 3125 CA HIS B 194 47.333 142.408 -55.399 1.00168. 04 C

ANISOU 3125 CA HIS B 194 26336 18774 18739 1409 2403 -100 C

ATOM 3126 CB HIS B 194 46.283 141.719 -54.536 1.00168. 84 C

ANIΞOU 3126 CB HIS B 194 26338 18935 18878 1317 2303 -123 C

ATOM 3127 CG HIS B 194 45.695 140.498 -55.161 1.00167. .52 C

ANISOU 3127 CG HIS B 194 26209 18657 18785 1228 2355 -231 C

ATOM 3128 NDl HIS B 194 44.613 140.548 -56.012 1.00166. 47 N

ANISOU 3128 NDl HIS B 194 26144 18578 18530 1149 2280 -374 N

ATOM 3129 CEl HIS B 194 44.307 139.324 -56.401 1.00174. 81 C

ANISOU 3129 CEl HIS B 194 27232 19506 19681 1066 2362 -450 C

ATOM 3130 NE2 HIS B 194 45.153 138.483 -55.836 1.00176. 06 N

ANISOU 3130 NE2 HIS B 194 27335 19525 20036 1100 2494 -353 N

ATOM 3131 CD2 HIS B 194 46.031 139.193 -55.053 1.00169. 72 C

ANISOU 3131 CD2 HIS B 194 26464 18771 19249 1195 2483 -208 C

ATOM 313.2 C HIS B 194 47.713 143.744 -54.761 1.00168. 43 C

ANISOU 3132 C HIS B 194 26330 18928 18738 1485 2362 31 C

ATOM 3133 O HIS B 194 48.834 143.916 -54.269 1.00163. 86 O

ANISOU 3133 O HIS B 194 25725 18289 18247 1527 2441 161 O

ATOM 3134 N ASN B 195 46.772 144.686 -54.757 1.00149. 95 N

ANISOU 3134 N ASN B 195 23971 16745 16260 1491 2244 N

ATOM 3135 CA ASN B 195 47.003 145.960 -54.086 1.00148. 77 C

ANISOU 3135 CA ASN B 195 23786 16698 16043 1552 2218 111 C

ATOM 3136 CB ASN B 195 47.014 147.126 -55.079 1.00149. 60 C

ANISOU 3136 CB ASN B 195 23980 16892 15970 1626 2187 * 44 C

ATOM 3137 CG ASN B 195 47.688 146.773 -56.380 1.00144. 88 C

ANISOU 3137 CG ASN B 195 23508 16196 15344 1677 2271 -20 C

ATOM 3138 ODl ASN B 195 48.840 147.143 -56.619 1.00140. 28 O

ANISOU 3138 ODl ASN B 195 22951 15543 14805 1740 2358 60 O

ATOM 3139 ND2 ASN B 195 46.975 146.033 -57.231 1.00145. 49 N

ANISOU 3139 ND2 ASN B 195 23668 16269 15344 1641 2247 -158 N

ATOM 3140 C ASN B 195 46.032 146.261 -52.953 1.00145. 31 C

ANISOU 3140 C ASN B 195 23231 16357 15622 1499 2139 176 C

ATOM 3141 O ASN B 195 46.442 146.765 -51.920 1.00144. 80 O

ANISOU 3141 O ASN B 195 23109 16306 15602 1490 2163 299 O

ATOM 3142 N SER B 196 ' 44.750 145.970 -53.133 1.00162. 27 N

ANISOU 3142 N SER B 196 25351 18573 17733 1453 2049 100 N

ATOM 3143 CA SER B 196 43.765 146.415 -52.146 1.00165. 22 C

ANISOU 3143 CA SER B 196 25624 19036 18116 1413 1981 156 C

ATOM 3144 CB SER B 196 42.670 147.284 -52.799 1.00169. 00 C

ANISOU 3144 CB SER B 196 26108 196-38 18467 1435 1900 109 C

ATOM 3145 OG SER B 196 41.694 146.520 -53.491 1.00163. 27 O

ANISOU 3145 OG SER B 196 25385 18921 17730 1376 1825 14 O

ATOM 3146 C SER B 196 43.157 145.286 -51.321 1.00163. 79 C

ANISOU 3146 C SER B 196 25353 18807 18072 1320 1951 161 C ATOM 3147 O SER B 196 42.656 144.312 -51.864 1.00166.61 O

ANISOU 3147 O SER B 196 25728 19098 18477 1278 1946 77 O

ATOM 3148 N TYR B 197 43.205 145.430 -50.002 1.00162.04 N

ANISOU 3148 N TYR B 197 25042 18613 17912 1278 1943 259 N

ATOM 3149 CA TYR B 197 42.624 144.442 -49.107 1.00159.32 C

ANISOU 3149 CA TYR B 197 24600 18234 17700 1189 1909 275 C

ATOM 3150 CB TYR B 197 43.727 143.776 -48.284 1.00162.99 C

ANISOU 3150 CB TYR B 197 25019 18610 18301 1149 1984 377 C

ATOM 3151 CG TYR B 197 44.653 142.872 -49.090 1.00167.60 C

ANISOU 3151 CG TYR B 197 25648 19068 18964 1171 2062 345 C

ATOM 3152 CDl TYR B 197 45~914 143.300 -49.480 1.00164.35 C

ANISOU 3152 CDl TYR B 197 25277 18600 18568 1217 2156 428 C

ATOM 3153 CEl TYR B 197 46.756 142.474 -50.213 1.00163.61 C

ANISOU 3153 CEl TYR B 197 25224 18372 18567 1241 2252 410 . C

ATOM 3154 CZ TYR B 197 46.343 141.205 -50.560 1.00165.47 C

ANISOU 3154 CZ TYR B 197 25471 18527 18873 1206 2265 297 C

ATOM 3155 OH TYR B 197 47.172 140.379 -51.288 1.00162.07 O

ANISOU 3155 OH TYR B 197 25094 17944 18543 1222 2392 275 O

ATOM 3156 CE2 TYR B 197 45.099 140.760 -50.182 1.00164.93 C

ANISOU 3156 CE2 TYR B 197 25367 18525 18775 1150 2162 209 C

ATOM 3157 CD2 TYR B 197 44.264 141.587 -49.451 1.00167.05 C

ANISOU 3157 CD2 TYR B 197 25583 18929 18960 1138 2057 240 C

ATOM 3158 C TYR B 197 41.578 145.095 -48.206 1.00154.10 C

ANISOU 3158 C TYR B 197 23866 17662 17024 1152 1851 321 C

ATOM 3159 O TYR B 197 41.699 146.273 -47.894 1.00154.85 O

ANISOU 3159 O TYR B 197 23976 17813 17048 1177 1883 386 O

ATOM 3160 N THR B 198 40.570 144.332 -47.776 1.00160.19 N

ANISOU 3160 N THR B 198 24563 18436 17866 1091 1782 290 N

ATOM 3161 CA THR B 198 39.379 144.904 -47.115 1.00165.36 C

ANISOU 3161 CA THR B 198 25158 19168 18502 1068 1725 318 C

ATOM 3162 CB THR B 198 38.350 145.295 -48.189 1.00164.55 C

ANISOU 3162 CB THR B 198 25084 19139 18299 1113 1656 249 C

ATOM 3163 OGl THR B 198 38.929 146.269 -49.056 1.00163.89 O

ANISOU 3163 OGl THR B 198 25095 19072 18102 1188 1694 219 O

ATOM 3164 CG2 THR B 198 37.083 145.855 -47.570 1.00163.31 C

ANISOU 3164 CG2 THR B 198 24870 19061 18119 1118 1628 309 C

ATOM 3165 C THR B 198 38.645 144.012 -46.083 1.00163.83 C

ANISOU 3165 C THR B 198 24859 18951 18437 979 1675 334 C

ATOM 3166 O THR B 198 38.690 142.784 -46.174 1.00166.15 O

ANISOU 3166 O THR B 198 25125 19185 18818 942 1650 284 O

ATOM 3167 N CYS B 199 37.968 144.632 -45.110 1.00141.76 N

ANISOU 3167 N CYS B 199 22011 16195 15657 943 1674 403 N

ATOM 3168 CA CYS B 199 36.970 143.930 -44.297 1.00137.76 C

ANISOU 3168 CA CYS B 199 21408 15679 15254 870 1611 407 C

ATOM 3169 CB CYS B 199 37.306 143.982 -42.812 1.00137.23 C

ANISOU 3169 CB CYS B 199 21286 15587 15269 779 1655 499 C

ATOM 3170 SG CYS B 199 39.032 143.838 -42.342 1.00156.03 S

ANISOU 3170 SG CYS B 199 23691 17925 17667 740 1743 584 S

ATOM 3171 C CYS B 199 35.617 144.595 -44.439 1.00142.25 C

ANISOU 3171 C CYS B 199 21955 16313 15779 894 1572 416 C

ATOM 3172 O CYS B 199 35.460 145.719 -44.013 1.00146.55 O

ANISOU 3172 O CYS B 199 22509 16882 16292 896 1635 484 O

ATOM 3173 N GLU B 200 34.628 143.926 -45.012 1.00175.34 N

ANISOU 3173 N GLU B 200 26120 20531 19971 903 1478 360 N

ATOM 3174 CA GLU B 200 33.276 144.485 -44.976 1.00185.47 C

ANISOU 3174 CA GLU B 200 27356 21874 21240 919 1438 402 C

ATOM 3175 CB GLU B 200 32.588 144.447 -46.356 1.00191.16 C

ANISOU 3175 CB GLU B 200 28097 22664 21871 961 1360 364 C

ATOM 3176 CG GLU B 200 32.950 145.627 -47.284 1.00195.16 C

ANISOU 3176 CG GLU B 200 28677 23221 22255 1041 1415 381 C

ATOM 3177 CD GLU B 200 32.349 145.516 -48.694 1.00208.62 C

ANISOU 3177 CD GLU B 200 30396 25005 23865 1055 1326 351 C

ATOM 3178 OEl GLU B 200 32.950 146.057 -49.650 1.00207.75 O

ANISOU 3178 OEl GLU B 200 30360 24924 23650 1104 1354 327 O

ATOM 3179 0E2 GLU B 200 31.278 144.893 -48.854 1.00210.41 O

ANISOU 3179 0E2 GLU B 200 30561 25269 24117 1007 1224 356 O

ATOM 3180 C GLU B 200 32.449 143.777 -43.895 1.00189.61 C

ANISOU 3180 C GLU B 200 27784 22376 21884 850 1383 422 C

ATOM 3181 O GLU B 200 31.896 142.700 -44.130 1.00189.29 O

ANISOU 3181 O GLU B 200 27701 22343 21877 825 1282 374 O

ATOM 3182 N ALA B 201 32.387 144.394 -42.710 1.00176.07 N

ANISOU 3182 N ALA B 201 26043 20633 20223 809 1453 491 N

ATOM 3183 CA ALA B 201 31.696 143.842 -41.537 1.00170.29 C

ANISOU 3183 CA ALA B 201 25224 19872 19607 737 1416 515 C

ATOM 3184 CB ALA B 201 32.426 144.245 -40.269 1.00161.44 C

ANISOU 3184 CB ALA B 201 24106 18708 18526 655 1508 571 C

ATOM 3185 C ALA B 201 30.234 144.271 -41.447 1.00170.08 C ANISOO 3185 C ALA B 201 25146 19878 19600 762 1386 566 C

ATOM 3186 O ALA B 201 29.932 145.347 -40.954 1.00169 .76 O

ANISOU 3186 O ALA B 201 25119 19835 19547 776 1483 640 O

ATOM 3187 N THR B 202 29.327 143.424 -41.910 1.00154 .13 N

ANISOU 3187 N THR B 202 23066 17881 17616 761 1265 535 N

ATOM 3188 CA THR B 202 27.915 143.761 -41.895 1.00154 .63 C

ANISOU 3188 CA THR B 202 23066 17979 17706 786 1227 608 C

ATOM 3189 CB THR B 202 27.182 143.075 -43.043 1.00157 .16 C

ANISOU 3189 CB THR B 202 23362 18367 17983 800 1091 579 C

ATOM 3190 OGl THR B 202 27.939 143. ' 224 -44.251 1.00158. 59 O

ANISOU 3190 OGl THR B 202 23626 18587 18043 833 1095 525 O

ATOM 3191 CG2 THR B 202 25.800 143.682 -43.217 1.00159, 90 C

ANISOU 3191 CG2 THR B 202 23639 18767 18348 834 1063 698 C

ATOM 3192 C THR B 202 27.259 143.313 -40.598 1.00164 32 C

ANISOU 3192 C THR B 202 24216 19158 19060 727 1212 640 C

ATOM 3193 O THR B 202 26.901 142.141 -40.460 1.00169. 90 O

ANISOU 3193 O THR B 202 24864 19864 19828 690 1099 595 O

ATOM 3194 N HIS B 203 27.097 144.242 -39.656 1.00186. 36 N

ANISOU 3194 N ' HIS B 203 27013 21907 21887 712 1334 713 N

ATOM 3195 CA HIS B 203 26.436 143.959 -38.380 1.00191. 60 C

ANISOU 3195 CA HIS B 203 27614 22517 22670 649 1341 750 C

ATOM 3196 CB HIS B 203 27.182 144.654 -37.231 1.00187. 43 C

ANISOU 3196 CB HIS B 203 27143 21927 22145 576 1494 778 C

ATOM 3197 CG HIS B 203 26.849 144.123 -35.867 1.00191. 66 C

ANISOU 3197 CG HIS B 203 27628 22405 22789 473 1493 787 C

ATOM 3198 NDl HIS B 203 25.558 144.025 -35.394 1.00194. 42 N

ANISOU 3198 NDl HIS B 203 27900 22732 23240 479 1447 825 N

ATOM 3199 CEl HIS B 203 25.572 143.533 -34.168 1.00190. 00 C

ANISOU 3199 CEl HIS B 203 27314 22119 22758 373 1459 820 C

ATOM 3200 NE2 HIS B 203 26.829 143.322 -33.820 1.00185. 06 N

ANISOU 3200 NE2 HIS B 203 26741 21489 22085 287 1510 793 N

ATOM 3201 CD2 HIS B 203 27.646 143.686 -34.862 1.00187. 32 C

ANISOU 3201 CD2 HIS B 203 27092 21819 22262 353 1533 774 C

ATOM 3202 C HIS B 203 24.968 144.416 -38.416 1.00198. 99 C

ANISOU 3202 C HIS B 203 28486 23464 23659 701 1334 848 C

ATOM 3203 O HIS B 203 24.593 145.265 -39.228 1.00200. 57 O

ANISOU 3203 O HIS B 203 28693 23711 23803 778 1358 910 O

ATOM 3204 N LYS B 204 24.143 143.832 -37.547 1.00182. 12 N

ANISOU 3204 N LYS B 204 26277 21283 21637 658 1303 876 N

ATOM 3205 CA LYS B 204 22.752 144.258 -37.350 1.00184. 74 C

ANISOU 3205 CA LYS B 204 26541 21604 22049 701 1319 994 C

ATOM 3206 CB LYS B 204 22.054 143.303 -36.365 1.00189. 19 C

ANISOU 3206 CB LYS B 204 27018 22131 22733 649 1221 987 C

ATOM 3207 CG LYS B 204 20.923 143.913 -35.535 1.00187. 99 C

ANISOU 3207 CG LYS B 204 26821 21907 22701 656 1317 1107 C

ATOM 3208 CD LYS B 204 20.566 143.019 -34.350 1.00180. 22 C

ANISOU 3208 CD LYS B 204 25794 20856 21824 569 1278 1066 C

ATOM 3209 CE LYS B 204 19.857 143.809 -33.259" 1.00170. 41 C

ANISOU 3209 CE LYS B 204 24548 19509 20690 552 1435 1167 C

ATOM 3210 NZ LYS B 204 19.705 143.032 -31.994 1.00163. 44' N

ANISOU 3210 NZ LYS B 204 23660 18558 19882 439 1436 1109 N

ATOM 3211 C LYS B 204 22.724 145.692 -36.826 1.00175. 79 C

ANISOU 3211 C LYS B 204 25459 20400 20934 709 1536 1084 C

ATOM 3212 O LYS B 204 21.741 146.424 -36.976 1.00169. 80 O

ANISOU 3212 O LYS B 204 24658 19624 20235 767 1607 1209 O

ATOM 3213 N THR B 205 23.836 14 " 6.071 -36.214 1.00163. 46 N

ANISOU 3213 N THR B 205 23990 18796 19322 641 1650 1030 N

ATOM 3214 CA THR B 205 24.035 147.395 -35.667 1.00162. 75 C

ANISOU 3214 CA THR B 205 23982 18637 19218 622 1875 1091 C

ATOM 3215 CB THR B 205 25.474 147.544 -35.142 1.00157. 92 C

ANISOU 3215 CB THR B 205 23477 18012 18514 523 1951 1017 C

ATOM 3216' OGl THR B 205 25.514 148.544 -34.123 1.00157. 45 O

ANISOU 3216 OGl THR B 205 23505 17869 18451 452 2174 1067 O

ATOM 3217 CG2 THR B 205 26.420 147.936 -36.265 1.00161. 04 C

ANISOU 3217 CG2 THR B 205 23923. 18481 18784 588 1924 976 C

ATOM 3218 C THR B 205 23.774 148.473 -36.712 1.00171. 49 C

ANISOU 3218 C THR B 205 25094 19779 20285 741 1955 1180 C

ATOM 3219 O THR B 205 23.600 149.640 -36.367 1.00174. 10 O

ANISOU 3219 O THR B 205 25416 20049 20685 773 2110 1291 O

ATOM 3220 N SER B 206 23.750 148.082 -37.986 1.00189. 64 N

ANISOU 3220 N SER B 206 27401 22171 22481 804 1857 1138 N

ATOM 3221 CA SER B 206 23.513 149.024 -39.086 1.00192. 84 C

ANISOU 3221 CA SER B 206 27800 22630 22841 912 1908 1223 C

ATOM 3222 CB SER B 206 ' 24.714 149.960 -39.268 1.00190. 90 C

ANISOU 3222 CB SER B 206 27668 22395 22470 923 2021 1176 C

ATOM 3223 OG SER B 206 24.445 150.958 -40.241 1.00192. 72 O

ANISOU 3223 OG SER B 206 27885 22686 22655 1030 2060 1254 O ATOM 3224 C SER B 206 23.204 148.325 -40.411 1.00191.97 C

ANISOU 3224 C SER B 206 27608 22630 22700 968 1702 1227 C

ATOM 3225 O SER B 206 23.291 147.100 -40.521 1.00191 .60 O

ANISOU 3225 O SER B 206 27523 22610 22668 924 1534 1155 O

ATOM 3226 N THR B 207 22.824 149.117 -41.409 1.00190 .19 N

ANISOU 3226 N THR B 207 27359 22473 22430 1052 1722 1316 N

ATOM 3227 CA THR B 207 22.721 148.633 -42.781 1.00194 .79 C

ANISOU 3227 CA THR B 207 27895 23177 22940 1077 1536 1311 C

ATOM 3228 CB THR B 207 21.464 149.178 -43.490 1.00193 .69 C

ANISOU 3228 CB THR B 207 27637 23099 22857 1136 1520 1502 C

ATOM 3229 OGl THR B 207 20.817 150.135 -42.641 1.00191 .82 O

ANISOU 3229 OGl THR B 207 27385 22779 22720 1187 1742 1635 O

ATOM 3230 CG2 THR B 207 20.490 148.046 -43.815 1.00184 22 C

ANISOU 3230 CG2 THR B 207 26332 21926 21737 1093 1355 1551 C

ATOM 3231 C THR B 207 23.975 149.049 -43.547 1.00188 58 C

ANISOU 3231 C THR B 207 27203 22441 22006 1104 1546 1223 C

ATOM 3232 O THR B 207 24.382 148.399 -44.514 1.00179 87 O

ANISOU 3232 O THR B 207 26114 21418 20812 1093 1400 1150 O

ATOM 3233 N SER B 208 24.583 150.142 -43.098 1.00200, 43 N

ANISOU 3233 N SER B 208 28780 23890 23484 1134 1730 1230 N

ATOM 3234 CA SER B 208 25.829 150.624 -43.675 1.00200. 49 C

ANISOU 3234 CA SER B 208 28885 23932 23361 1164 1762 1152 C

ATOM 3235 CB SER B 208 25.999 152.122 -43.404 1.00208. 88 C

ANISOU 3235 CB SER B 208 29988 24963 24414 1224 1976 1236 C

ATOM 3236 OG SER B 208 25.702 152.438 -42.051 1.00209, 97 O

ANISOU 3236 OG SER B 208 30150 24989 24640 1177 2140 1270 O

ATOM 3237 C SER B 208 26.980 149.847 -43.066 1.00195, 11 C

ANISOU 3237 C SER B 208 28291 23201 22641 1092 1743 1007 C

ATOM 3238 O SER B 208 27.258 149.988 -41.879 1.00195. 91 O

ANISOU 3238 O SER B 208 28439 23222 22774 1041 1863 998 O

ATOM 3239 N PRO B 209 27.643 149.013 -43.879 1.00184. 16 N

ANISOU 3239 N PRO B 209 26925 21860 21189 1077 1600 903 N

ATOM 3240 CA PRO B 209 28.712 148.095 -43.458 1.00178. 72 C

ANISOU 3240 CA PRO B 209 26292 21127 20488 1012 'l564 784 C

ATOM 3241 CB PRO B 209 28.894 147.191 -44.687 1.00179. 27 C

ANISOU 3241 CB PRO B 209 26374 21255 20485 1021 1423 700 C

ATOM 3242 CG PRO B 209 27.673 147.407 -45.533 1.00183. 70 C

ANISOU 3242 CG PRO B 209 26857 21894 21045 1045 1336 777 C

ATOM 3243 CD PRO B 209 27.281 148.820 -45.290 1.00183. 46 C

ANISOU 3243 CD PRO B 209 26798 21870 21040 1109 1465 911 C

ATOM 3244 C PRO B 209 30.036 148.794 -43.145 1.00171. 99 C

ANISOU 3244 C PRO B 209 25537 20236 19574 1010 1695 760 C

ATOM 3245 O PRO B 209 30.643 149.325 -44.068 1.00175. 23 O

ANISOU 3245 O PRO B 209 26009 20685 19887 1064 1700 728 O

ATOM 3246 N ILE B 210 30.478 148.782 -41.884 1.00178. 93 N

ANISOU 3246 N ILE B 210 26437 21047 20500 938 1795 780 N

ATOM 3247 CA ILE B 210 31.771 149.371 -41.498 1.00183. 14 C

ANISOU 3247 CA ILE B 210 27065 21554 20965 906 1906 768 C

ATOM 3248 CB ILE B 210 32.114 149.153 -39.994 1.00186. 68 C

ANISOU 3248 CB ILE B 210 27523 21937 21468 772 1970 785 C

ATOM 3249 CGl ILE B 210 31.605 150.311 -39.125 1.00191. 39 C

ANISOU 3249 CGl ILE B 210 28165 22493 22063 736 2149 860 C

ATOM 3250 CDl ILE B 210 31.956 150.180 -37.637 .1.00176. 46 C

ANISOU 3250 CDl ILE B 210 26319 20547 20180 572 2233 876 C

ATOM 3251 CG2 ILE B 210 33.617 149.015 -39.807 1.00172. 55 C

ANISOU 3251 CG2 ILE B 210 25792 20141 19627 711 1980 759 C

ATOM 3252 C ILE B 210 32.878 148.724 -42.301 1.00181. 21 C

ANISOU 3252 C ILE B 210 26858 21332 20661 927 1826 690 C

ATOM 3253 O ILE B 210 32.923 147.499 -42.405 1.00179. 66 O

ANISOU 3253 O ILE B 210 26619 21130 20514 900 1709 632 O

ATOM 3254 N VAL B 211 33.773 149.536 -42.862 1.00180. 65 N

ANISOU 3254 N VAL B 211 26870 21279 20489 975 1901 689 N

ATOM 3255 CA VAL B 211 34.866 149.006 -43.679 1.00174. 91 C

ANISOU 3255 CA VAL B 211 26188 20558 19710 1001 1849 624 C

ATOM 3256 CB VAL B 211 34.633 149.247 -45.185 1.00169. 70 C

ANISOU 3256 CB VAL B 211 25550 19960 18970 1107 1796 586 C

ATOM 3257 CGl VAL B 211 35.700 148.557 -45.989 1.00172. 69 C

ANISOU 3257 CGl VAL B 211 25962 20322 19332 1110 1723 499 C

ATOM 3258 CG2 VAL B 211 33.276 148.727 -45.596 1.00171. 17 C

ANISOU 3258 CG2 VAL B 211 25656 20191 19191 1126 1716 606 C

ATOM 3259 C VAL B 211 36.232 149.556 -43.273 1.00167. 03 C

ANISOU 3259 C VAL B 211 25272 19539 18653 973 1951 650 C

ATOM 3260 O VAL B 211 36.328 150.548 -42.555 1.00169. 30 O

ANISOU 3260 O VAL B 211 25600 19821 18906 940 2069 709 O

ATOM 3261 N LYS B 212 37.281 148.877 -43.722 1.00148. 54 N

ANISOU 3261 N LYS B 212 22956 17179 16302 977 1914 611 N

ATOM 3262 CA LYS B 212 38.651 149.293 -43.492 1.00152. 58 C ANISOU 3262 CA LYS B 212 23538 17679 16758 960 1992 649 C

ATOM 3263 CB LYS B 212 39.121 148.942 -42.082 1.00156 .53 C

ANISOU 3263 CB LYS B 212 24010 18144 17319 816 2025 721 C

ATOM 3264 CG LYS B 212 38.568 149.824 -40.981 1.00159 .14 C

ANISOU 3264 CG LYS B 212 24358 18481 17628 732 2117 780 C

ATOM 3265 CD LYS B 212 39.583 150.815 -40.421 1.00162 .29 C

ANISOU 3265 CD LYS B 212 24849 18890 17925 669 2235 850 C

ATOM 3266 CE LYS B 212 39.098 151.348 -39.068 1.00163 .30 C

ANISOU 3266 CE LYS B 212 25006 19005 18036 540 2343 903 C

ATOM 3267 NZ LYS B 212 39.775 152.589 -38.616 1.00173 .92 N

ANISOU 3267 NZ LYS B 212 26465 20364 19251 481 2480 958 N

ATOM 3268 C LYS B 212 39.514 148.562 -44.492 1.00157 11 C

ANISOU 3268 C LYS B 212 24135 18232 17329 1017 1941 594 C

ATOM 3269 O LYS B 212 39.479 147.333 -44.576 1.00153 83 O

ANISOU 3269 O LYS B 212 23668 17774 17006 983 1876 560 O

ATOM 3270 N SER B 213 40.292 149.331 -45.244 1.00174, 82 N

ANISOU 3270 N SER B 213 26457 20496 19469 1103 1986 584 N

ATOM 3271 CA SER B 213 41.176 148.783 -46.257 1.00169. 92 C

ANISOU 3271 CA SER B 213 25880 19844 18837 1161 1964 532 C

ATOM 3272 CB SER B 213 40.681 149.165 -47.650 1.00170, 24 C

ANISOU 3272 CB SER B 213 25962 19933 18789 1264 1926 453 C

ATOM 3273 OG SER B 213 39.355 148.723 -47.858 1.00166. 28 O

ANISOU 3273 OG SER B 213 25397 19466 18315 1250 1846 418 O

ATOM 3274 C SER B 213 42.591 149.296 -46.089 1.00162. 64 C

ANISOU 3274 C SER B 213 25021 18903 17873 1166 2045 598 C

ATOM 3275 O SER B 213 42.950 149.915 -45.084 1.00159. 60 O

ANISOU 3275 O SER B 213 24639 18528* 17474 1093 2106 688 O

ATOM 3276 N PHE B 214 43.386 149.028 -47.107 1.00144. 95 N

ANISOU 3276 N PHE B 214 22835 16632 15606 1242 2048 554 N

ATOM 3277 CA PHE B 214 44.732 149.528 -47.183 1.00153. 02 C

ANISOU 3277 CA PHE B 214 23921 17637 16584 1270 2119 617 C

ATOM 3278 CB PHE B 214 45.550 149.063 -45.995 1.00149. 74 C

ANISOU 3278 CB PHE B 214 23455 17184 16254 1156 2151 742 C

ATOM 3279 CG PHE B 214 45.914 147.611 -46.048 1.00149. 48 C

ANISOU 3279 CG PHE B 214 23362 17065 16367 1124 2131 750 C

ATOM 3280 CDl PHE B 214 47.226 147.221 -46.249 1.00147. 83 C

ANISOU 3280 CDl PHE B 214 23159 16796 16214 1125 2185 842 C

ATOM 3281 CEl PHE B 214 47.565 145.880 -46.284 1.00150. 49 C

ANISOU 3281 CEl PHE B 214 23433 17039 16709 1100 2193 863 C

ATOM 3282 CZ PHE B 214 46.590 144.918 -46.125 1.00148. 73 C

ANISOU 3282 CZ PHE B 214 - 23149 16786 16574 1071 2141 777 C

ATOM 3283 CE2 PHE B 214 45.279 145.293 -45.928 1.00146. 11 C

ANISOU 3283 CE2 PHE B 214 22816 16524 16175 1067 2071 682 C

ATOM 3284 CD2 PHE B 214 44.944 146.631 -45.895 1.00148. 44 C

ANISOU 3284 CD2 PHE B 214 23166 16908 16328 1096 2068 676 C

ATOM > 3285 C PHE B 214 45.310 148.926 -48.422 1.00158. 41 C

ANISOU 3285 C PHE B 214 24653 18260 17274. 1349 2115 548 C

ATOM 3286 O PHE B 214 45.273 147.714 -48.608 1.00158. 58 O

ANISOU 3286 O PHE B 214 24646 18223 17383 1330 2079 487 O

ATOM 3287 N ASN B 215 45.821 149.771 -49.293 1.00185. 40 N

ANISOU 3287 N ASN B 215 28156 21690 20599 1433 2163 555 N

ATOM 3288 CA ASN B 215 46.557 149.261 -50.413 1.00188. 88 C

ANISOU 3288 CA ASN B 215 28663 22065 21038 1508 2181 494 C

ATOM 3289 CB ASN B 215 46.644 150.324 -51.485 1.00194. 43 C

ANISOU 3289 CB ASN B 215 29451 22831 21592 1615 2186 435 C

ATOM 3290 CG ASN B 215 45.307 150.983 -51.724 1.00196. 43 C

ANISOU 3290 CG ASN B 215 29675 23186 21772 1622 2132 391 C

ATOM 3291 ODl ASN B 215 44.268 150.320 -51.697 1.00186. 24 O

ANISOU 3291 ODl ASN B 215 28342 21906 20513 1586 2063 326 O

ATOM 3292 ND2 ASN B 215 45.317 152.294 -51.934 1.00206. 62 N

ANISOU 3292 ND2 ASN B 215 30985 24550 22971 1663 2173 440 N

ATOM 3293 C ASN B 215 47.908 148.834 -49.876 1.00194. 31 C

ANISOU 3293 C ASN B 215 29351 22671 21807 1492 2252 606 C

ATOM 3294 O ASN B 215 48.267 149.181 -48.744 1.00198. 53 O

ANISOU 3294 O ASN B 215 29873 23238 22320 1453 2286 729 O

ATOM 3295 N ARG B 216 48.636 148.051 -50.665 1.00184. 45 N-

ANISOU 3295 N ARG B 216 28117 21314 20653 1509 2283 574 N

ATOM 3296 CA ARG B 216 49.859 147.411 -50.189 1.00184. 74 C

ANISOU 3296 CA ARG B 216 28129 21253 20810 1493 2361 704 C

ATOM 3297 CB " ARG B 216 50.097 146.092 -50.924 1.00178. 78 C

ANISOU 3297 CB ARG B 216 27397 20361 20171 1514 2413 632 C

ATOM 3298 CG ARG B 216 51.218 145.249 -50.350 1.00174. 88 C

ANISOU 3298 CG ARG B 216 26831 19746 19868 1475 2500 778 C

ATOM 3299 CD ARG B 216 51.405 144.032 -51.217 ϊ.00172. 88 C

ANISOU 3299 CD ARG B 216 26625 19348 19713 1501 2576 672 C

ATOM 3300 NE ARG B 216 51.348 144.398 -52.624 1.00168. 39 N

ANISOU 3300 NE ARG B 216 26203 18773 19003 1592 2592 532 N ATOM 3301 CZ ARG B 216 52.413 144.737 -53.335 1.00170.88I C

ANISOU 3301 CZ ARG B 216 26594 19030 19303 1676 2675 582 C

ATOM 3302 NHl ARG B 216 53.613 144.744 -52.769 1.00169.90 I N

ANISOU 3302 NHl ARG B 216 26408 18850 19298 1678 2747 780 N

ATOM 3303 NH2 ARG B 216 52.281 145.067 -54.607 1.00170.02 N

ANISOU 3303 NH2 ARG B 216 26617 18923 19058 1751 2681 447 N

ATOM 3304 C ARG B 216 51.051 148.332 -50.367 1.00191.40 C

ANISOU 3304 C ARG B 216 29045 22114 21565 1565 2413 783 C

ATOM 3305 O ' ARG B 216 51.952 148.368 -49.528 1.00193.38 O

ANISOU 3305 O ARG B 216 29261 22330 21883 1533 2464 946 O

ATOM 3306 N ASN B 217 51.047 149.073 -51.467 1.00213.99 N

ANISOU 3306 N ASN B 217 31998 25035 24272 1657 2396 677 N

ATOM 3307 CA ASN B 217 52.082 150.051 -51.736 1.00217.97 C

ANISOU 3307 CA ASN B 217 32584 25554 24679 1746 2443 720 C

ATOM 3308 C ASN B 217 52.032 151.205 -50.733 1.00229.24 C

ANISOU 3308 C ASN B 217 34019 27105 25978 1733 2432 783 ' C

ATOM 3309 O ASN B 217 53.071 151.674 -50.261 1.00240.77 O

ANISOU 3309 O ASN B 217 35554 28601 27328 1814 2462 794 O

ATOM 3310 CB ASN B 217 51.929 150.563 -53.165 1.00209.53 C

ANISOU 3310 CB ASN B 217 31618 24471 23522 1855 2441 566 C

ATOM 3311 CG ASN B 217 50.478 150.624 -53.608 1.00213.26 C

ANISOU 3311 CG ASN B 217 32084 25027 23917 1845 2359 429 C

ATOM 3312 ODl ASN B 217 49.745 149.636 -53.515 1.00207.92 O

ANISOU 3312 ODl ASN B 217 31369 24318 23315 1781 2324 , 364 O

ATOM 3313 .ND2 ASN B 217 50.057 151.788 -54.101 1.00216.07 N

ANISOU 3313 ND2 ASN B 217 32472 25494 24129 1905 2331 397 N

ATOM 3314 N GLU B 218 50.815 151.632 -50.396 1.00232.32 N

ANISOU 33i4 N GLU B 218 34338 27554 26379 1628 2400 820 N

ATOM 3315 CA GLU B 218 50.588 152.785 -49.516 1.00239.85 C

ANISOU 3315 CA GLU B 218 35311 28609 27212 1597 2417 869 C

ATOM 3316 CB GLU B 218 49.134 152.829 -49.008 1.00233\26 C

ANISOU 3316 CB GLU B 218 34423 27832 26373 1532 2379 816 C

ATOM 3317 CG GLU B 218 48.068 152.995 -50.101 1.00223.97 C

ANISOU 3317 CG GLU B 218 33257 26688 25154 1623 ' 2332 671 C

ATOM 3318 CD GLU B 218 48.019 154.394 -50.709 1.00231.02 C

ANISOU 3318 CD GLU B 218 34230 27637 25909 1746 2361 628 C

ATOM 3319 OEl GLU B 218 48.460 155.359 -50.055 1.00239.10 O

ANISOU 3319 OEl GLU B 218 35300 28696 26852 1752 2427 700 O

ATOM 3320 0E2 GLU B 218 47.525 154.531 -51.847 1.00227.56 O

ANISOU 3320 OE2 GLU B 218 33809 27214 25438 1826 2318 524 O

ATOM 3321 C GLU B 218 51.572 152.896 -48.343 1.00249.92 C

ANISOU 3321 C GLU B 218 36574 29889 28494 1496 2463 1049 C

ATOM 3322 o GLU B 218 51.556 152.089 -47.399 1.00242.59 • O

ANISOU 3322 O GLU B 218 35565 28922 27685 1383 2453 1151 O

ATOM 3323 N CYS B 219 ' 52.423 153.916 -48.432 1.00291.93 N

ANISOU 3323 N CYS B 219 41973 35262 33684 1530 2510 1095 N

ATOM 3324 CA CYS B 219 53.362 154.270 -47.374 1.00303.61 C

ANISOU 3324 CA CYS B 219 ' 43461 36765 35132 1421 2552 1274 C

ATOM 3325 CB CYS B 219 54.294 153.095 -47.054 1.00307.81 C

ANISOU 3325 CB CYS B 219 43942 37210 35800 1410 2553 1404 C

ATOM 3326 SG CYS B 219 55.076 153.206 -45.426 1.00300.88 S

ANISOU 3326 SG CYS B 219 42994 36365 34962 1190 2565 1671 S

ATOM 3327 C CYS B 219 54.172 155.516 -47.764 1.00296.63 C

ANISOU 3327 C CYS B 219 42683 35946 34076 1480 2608 1285 C

ATOM 3328 O ^ CYS B 219 53.614 156.552 -48.144 1.00285.82 O

ANISOU 3328 O CYS B 219 41373 34602 32625 1615 2617 1157 O

ATOM 3329 N GLN C 1 -42.214 59.626 47.739 1.00191.72 N

ANISOU 3329 N GLN C 1 22967 25392 24485 1124 340 -213 N

ATOM 3330 CA GLN C 1 -42.539 60.372 48.942 1.00193.30 C

ANISOU 3330 CA GLN C 1 23352 25698 24395 980 597 -209 C

ATOM 3331 CB GLN C 1 -41.529 60.057 50.035 1.00198.96 C

ANISOU 3331 CB GLN C 1 24313 26384 24900 899 394 -171 C

ATOM 3332 CG GLN C 1 -41.396 58.581 50.329 1.00217.67 C

ANISOU 3332 CG GLN C 1 26788 28639 27276 734 112 16 C

ATOM 3333 CD GLN C 1 -40.113 58.253 51.072 1.00243.38 C

ANISOU 3333 CD GLN C 1 30267 31826 30382 698 -164 14 C

ATOM 3334 OEl GLN C 1 -39.130 58.993 50.99^ 1.00251.64 O

ANISOU 3334 OEl GLN C 1 31397 32920 31295 782 -108 -117 O

ATOM 3335 NE2 GLN C 1 -40.114 57.137 51.797 1.00247.64 N

ANISOU 3335 NE2 GLN C 1 30904 32238 30950 570 -482 ' 156 N

ATOM 3336 C GLN C 1 -42.546 61.865 48.656 1.00183.22 C

ANISOU 3336 C GLN C 1 22009 24524 23083 1113 866 -395 C

ATOM 3337 O GLN C 1 -42.543 62.681 49.571 1.00182.64 O

ANISOU 3337 O GLN C 1 ■ 22016 24554 22825 1019 1135 -417 O

ATOM 3338 N VAL C 2 -42.556 62.216 47.376 1.00159.73 N

ANISOU 3338 N VAL C 2 18886 21523 20282 1327 780 ' -531 N

ATOM 3339 CA VAL C 2 -42.565 63.610 46.960 1.00150.49 C ANISOU 3339 CA VAL C 2 17655 20426 19097 1454 984 -704 C

ATOM 3340 CB VAL C 2 -41.282 63.972 46.228 1.00142.27 C

ANISOU 3340 CB VAL C 2 16650 19387 18021 1591 817 -814 C

ATOM 3341 CGl VAL C 2 -40.879 65.388 46.584 1.00140.18 C

ANISOU 3341 CGl VAL C 2 16463 19212 17588 1616 1021 -934 C

ATOM 3342 CG2 VAL •c 2 -40.168 62.956 46.541 1.00149.07 C

ANISOU 3342 CG2 VAL C 2 17662 20201 18776 1523 550 -734 C

ATOM 3343 C VAL C 2 -43.688 63.848 45.973 1.00152.40 C

ANISOU 3343 C VAL C 2 17667 20637 19602 1580 1073 -779 C

ATOM 3344 O VAL C 2 -43.492 63.734 44.764 1.00152.56 O

ANISOU 3344 O VAL C 2 17560 20594 19812 1737 899 -832 O

ATOM 3345 N GLN C 3 -44.866 64.180 46.476 1.00170.55 N

ANISOU 3345 N- GLN C 3 19908 22983 21909 1514 1342 -800 N

ATOM 3346 CA GLN C 3 -46.026 64.294 45.612 1.00171.47 C

ANISOU 3346 CA GLN C 3 19811 23051 22289 1625 1432 -881 C

ATOM 3347 CB GLN C en 3 -47.035 63.206 45.959 1.00174.28 C

ANISOU 3347 CB GLN C 3 20081 23358 22781 1511 1444 -739 C

ATOM 3348 CG GLN C 3 -46.525 61.798 45.682 1.00181.52 C

ANISOU 3348 CG GLN C 3 21049 24192 23727 1456 1142 -561 C

ATOM 3349 CD GLN C 3 -46.667 60.859 46.879 1.00188.85 C

ANISOO 3349 CD GLN •C 3 22102 25151 24500 1197 1183 -371 c

ATOM 3350 OEl GLN C 3 -46.516 61.274 48.032 1.00193.52 O

ANISOU 3350 OEl GLN C 3 22808 25859 24862 1049 1420 -372 O

ATOM 3351 NE2 GLN C 3 -46.938 59.583 46.606 1.00188.50 N

ANISOU 3351 NE2 GLN C 3 22041 25005 24574 1138 936 -207 N

ATOM 3352 C GLN C 3 -46.660 65.650 45.782 1.00170.04 C

ANISOU 3352 C GLN C 3 19599 22949 22060 1648 1710 -1048 C

ATOM 3353 O GLN C 3 -46.736 66.165 46.892 1.00171.19 O

ANISOU 3353 O GLN C 3 19841 23202 22000 1511 1905 -1048 O

ATOM 3354 N LEU C 4 -47.103 66.237 44.678 1.00157.52 N

ANISOU 3354 N LEU C 4 17883 21309 20658 1823 1712 -1201 N

ATOM 3355 CA LEU .C 4 -47.863 67.475 44.749 1.00156.93 C

ANISOU 3355 CA LEU C 4 17763 21285 20579 1856 1934 -1381 C

ATOM 3356 CB LEU C 4 -47.328 68.528 43.779 1.00144.53 C

ANISOU 3356 CB LEU C 4 16191 19682 19043 .2022 1849 -1533 C

ATOM 3357 CG LEU C 4 -46.098 69.251 44.323 1.00142.27 C

ANISOU 3357 CG LEU C 4 16090 19482 18483 1986 1809 -1529 C

ATOM 3358 CDl LEU C 4 -46.049 70.682 43.836 1.00143.23 C

ANISOU 3358 CDl LEU C 4 16221 19619 18580 2080 1853 -1710 C

ATOM 3359 ' CD2 LEU C 4 -46.124 69.227 45.829 1.00147.46 C

ANISOU 3359 CD2 LEU C 4 16872 20247 18908 1810 1953 -1446 C

ATOM 3360 C LEU C 4 -49.337 67.202 44.497 1.00168.71 C

ANISOU 3360 C LEU C 4 19072 22730 22302 1860 2078 -1434 C

ATOM 3361 O LEU C 4 -49.727 66.815 43.394 1.00167.96 O

ANISOU 3361 O LEU C 4 18838 22508 22472 1987 1971 -1455 O

ATOM 3362 N GLN C 5 -50.146 67.397 45.537 1.00186.32 N

ANISOU 3362 N GLN C 5 21301 25068 24426 1720 2321 -1463 N

ATOM 3363 CA GLN C 5 -51.572 67.115 45.477 1.00185.22 C

ANISOU 3363 CA GLN C 5 20985 24912 24480 1683 2488 -1513 C

ATOM 3364 CB GLN C 5 -52.067 66.564 46.815 1.00187.64 ' C

ANISOU 3364 CB GLN C 5 21336 25356 24604 1439 2674 -1393 C

ATOM 3365 CG GLN C 5 -53.431 65.899 46.747 1.00193.01 C

ANISOU 3365 CG GLN C 5 2-1834 26006 25496 1368 2791 -1369 C

ATOM 3366 CD GLN C 5 -53.559 64.955 45.561 1.00198.01 C

ANISOU 3366 CD GLN C 5 22338 26437 26460 1522 2576 -1315 C

ATOM 3367 OEl GLN C 5 -53.576 63.731 45.721 1.00206.51 O

ANISOU 3367 OEl GLN C 5 23416 27453 27596 1449 2436 -1106 O

ATOM 3368 NE2 GLN C 5 -53.642 65.523 44.358 1.00190.08 N

ANISOU 3368 NE2 GLN C 21226 25322 25672 1737 2531 -1506 N

ATOM 3369 C GLN C 5 -52.313 68.383 45.148 1.00178.95 C

ANISOU 3369 C GLN C 5 20078 24114 23801 1794 2630 -1781 C

ATOM 3370 O GLN C 5 -52.258 69.339 45.901 1.00176.03 O

ANISOU 3370 O GLN C 5 19748 23875 23260 1736 2803 -1907 O

ATOM 3371 N GLN C 6 -52.992 68.404 44.014 1.00172.51 N

ANI'SOU 3371 N GLN C 6 19123 23139 23283 1962 2535 -1876 N

ATOM 3372 CA GLN C 6 -53.705 69.604 43.631 1.00176.58 C

ANISOU 3372 CA GLN C 6 19540 23613 23939 2080 2617 -2143 C

ATOM 3373 CB GLN C 6 -53.505 69.915 42.148 1.00173.73 C

ANISOU 3373 CB GLN C 6 19139 23065 23807 2289 2400 -2214 C

ATOM 3374 CG GLN C 6 -52.131 70.516 41.839 1.00171.78 C

ANISOU 3374 CG GLN C 6 19052 22834 23384 2351 2230 -2194 C

ATOM 3375 CD GLN C 6 -51.873 70.719 40.345 1.00169.16 C

ANISOU 3375 CD GLN C 6 18685 22342 23246 2535 2041 -2294 C

ATOM 3376 OEl GLN C 6 -50.790 70.403 39.833 1.00162.47 O

ANISOU 3376 OEl GLN C 6 17897 21463 22371 2593 1848 -2189 O

ATOM 3377 NE2 GLN C 6 -52.868 71.252 39.641 1.00169.49 N

ANISOU 3377 NE2 GLN C . 6 18632 22286 23481 2621 2088 -2509 N ATOM 3378 GLN 6 -55.170 69.459 43.988 1.00183.04 C

ANISOU 3378 GLN 6 20183 24451 24912 2015 2836 -2253 C

ATOM 3379 GLN 6 -55.617 68.372 44.337 1 ,00182.55 O

ANISOU 3379 GLN 6 20063 24407 24891 1896 2896 -2098 O

ATOM 3380 SER 7 -55.906 70.563 43.924 1 ,00180.68 N

ANISOU 3380 SER 7 19800 24154 24697 2086 2943 -2528 N

ATOM 3381 CA SER 7 -57.313 70.575 44.300 1 ,00181.01 C

ANISOU 3381 CA SER 7 19656 24233 24886 2033 3163 -2699 C

ATOM 3382 CB SER 7 -57.859 72..002 44.260 1 00182.24 C

ANISOU 3382 CB SER 7 19757 24400 25086 2128 3223 -3038 C

ATOM 3383 OG SER 7 -57.894 72..503 42.936 1 00174.85 O

ANISOU 3383 OG SER 7 18827 23254 24354 2333 3003 -3156 O

ATOM 3384 C SER 7 -58.126 69..688 43.375 I 00184.90 C

ANISOU 3384 C SER 7 19981 24543 25729 2105 3113 -2674 C

ATOM 3385 O SER 7 -57.571 68..882 42.634 1 00187..37 O

ANISOU 3385 O SER 7 20325 24735 26131 2160 2926 -2473 O

ATOM 3386 N GLY -59.446 69..844 43.417 1 00207..96 N

ANISOU 3386 N GLY 22715 27446 28856 2114 3272 -2893 N

ATOM 3387 CA GLY -60..338 69..076 42.562 1 00212..11 C

ANISOU 3387 CA GLY 23066 27788 29739 2190 3240 -2899 C

ATOM 3388 GLY -60.904 69..911 41.428 1 00211..38 C

ANISOU 3388 GLY 22885 27478 29952 2416 3127 -3176 C

ATOM 3389 GLY -60.894 71..141 41.504 1 00209..00 O

ANISOU 3389 GLY 22606 27206 29598 2470 3147 -3423 O

ATOM 3390 PRO 9 -61.406 69..248 40.370 1 00186..61 N

ANISOU 3390 N PRO 9 19652 24112 27141 2553 2989 -3141 N

ATOM 3391 CA PRO 9 -61.922 69..965 39.197 1, 00182..05 C

ANISOU 3391 CA PRO 9 19023 23291 26857 2777 2836 -3382 C

ATOM 3392 CB PRO 9 -62.802 68..910 38.500 1 00180..47 C

ANISOU 3392 CB PRO 9 18666 22889 27014 2864 2780 -3320 C

ATOM 3393 CG PRO 9 -62.879 67..735 39.484 1 00186..68 C

ANISOU 3393 CG PRO 9 19395 23843 27690 2653 2947 -3084 C

ATOM 3394 CD PRO 9 -61.593 67..796 40.229 1, 00184..04 C

ANISOU 3394 CD PRO 9 19254 23729 26945 2506 2958 -2891 C

ATOM 3395 C PPRROO 9 -62.736 71.193 39.604 1.00184..45 C

ANISOU 3395 C PPRROO 9 19238 23628 27217 2786 2975 -3745 C

ATOM 3396 O PPRROO 9 -63.427 71.160 40.622 1, 00189..21 O

ANISOU 3396 O PPRROO 9 19718 24392 27781 .2645 3221 -3836 O

ATOM 3397 N GGLLUU 10 -62.638 72.271 38.832 1 00221..90 N

ANISOU 3397 N. GGLLUU 10 24043 28229 32039 2940 2810 -3956 N

ATOM 3398 CA GLU 10 -63.282 73.526 39.212 1, 00229..16 C

ANISOU 3398 CA GLU 10 24895 29179 32996 2957 2890 -431.9 C

ATOM 3399 CB GLU 10 -62.241 74.633 39.416 1, 00230..00 C

ANISOU 3399 CB GLU 10 25184 29382 32824 2955 2791 -4365 C

ATOM 3400 CG GLU 10 -61.459 74.514 40.718 1, 00233..47 C

ANISOU 3400 CG GLU 10 25735 30115 32857 2774 2933 -4149 C

ATOM 3401 CD GLU 10 -62.340 74.647 41.947 1, 00236..38 C

ANISOU 3401 CD GLU 10 25979 30730 33103 2615 3228 -4283 C

ATOM 3402 OEl GLU 10 -62.790 75.773 42.24.2 1.00239.68 O

ANISOU 3402 OEl GLU 10 26325 31193 33551 2648 3273 -4611 O

ATOM 3403 OE2 GLU 10 -62.574 73.626 42.625 1.00233.06 O

ANISOU 3403 OE2 GLU 10 25538 30470 32546 2451 3402 -4062 O

ATOM 3404 C GLU 10 -64.365 73.978 38.235 1.00233.74 C

ANISOU 3404 C GLU 10 25359 29470 33981 3142 2765 -4611 C

ATOM 3405 O GLU 10 -64.254 73.778 37.022 1.00227.35 O

ANISOU 3405 O GLU 10 24615 28417 33351 3296 2531 -4555 O

ATOM 3406 N LEU 11 -65.411 74.590 38.790 1.00188.93 N

ANISOU 3406 N LEU 11 19510 23829 28446 3124 2919 -4935 N

ATOM 3407 CA LEU 11 -66.548 75.080 38.018 1.00184.77 C

ANISOU 3407 CA LEU 11 18865 23034 28307 3293 2806 r 5281 C

ATOM 3408 CB LEU 11 -67.794 74.244 38.336 1, 00178.41 C

ANISOU 3408 CB LEU 11 17812 22201 27776 3263 3001 -5371 C

ATOM 3409 CG LEU 11 -68.688 73.788 37.178 1.00172.82 C

ANISOU 3409 CG LEU 11 17007 21129 27526 3461 2838 -5519 C

ATOM 3410 CDl LEU 11 -67.867 73.514 35,.930 1.00173.20 C

ANISOU 3410 CDl LEU 11 17248 20948 27613 3608 2540 -5298 C

ATOM 3411 CD2 LEU 11 -69.491 72.556 37..571 1.00173.03 C

ANISOU 3411 CD2 LEU 11 16822 21159 27762 3401 3031 -5448 C

ATOM 3412 C LEU 11 -66.764 76.541 38.391 1.00182.88 C

ANISOU 3412 C LEU 11 18622 22865 27998 3302 2792 -5640 C

ATOM 3413 0 LEU 11 -66.943 76.867 39..559 1.00181.75 O

ANISOU 3413 O LEU 11 18403 23002 27652 3161 3017 -5731 O

ATOM 3414 N VAL 12 -66.728 77.427 37,.405 1.00234.08 N

ANISOU 3414 N VAL 12 25196 29103 34639 3462 2513 -5841 N

ATOM 3415 CA VAL 12 -66.731 78.846 37,.718 1.00245.47 C

ANISOU 3415 CA VAL 12 26656 30596 36015 3480 2438 -6170 C

ATOM 3416 CB VAL 12 -65.305 79.409 37,.721 1.00247.64 C ANISOU 3416 CB VAL C 12 27165 31014 35914 3425 2329 -5975 C

ATOM 3417 CGl VAL C 12 -64.536 78.880 38.922 1.00242.21 C

ANISOO 3417 CGl 'VAL C 12 26496 30673 34861 3237 2597 -5684 C

ATOM 3418 CG2 VAL C 12 -64.595 79.059 36.417 1.00243.23 C

ANISOU 3418 CG2 VAL C 12 26815 30224 35378 3522 2039 -5751 C

ATOM 3419 C VAL C 12 -67.580 79.689 36.785 1.00252.60 C

ANISOU 3419 C VAL C 12 27543 31161 37274 3663 2164 -6533 C

ATOM 3420 O VAL C 12 -67.455 79.610 35.562 1.00249.34 O

ANISOO 3420 O VAL C 12 27250 30463 37024 3784 1918 -6442 O

ATOM 3421 N LYS C 13 -68.445 80.501 37.383 1.00251.80 N

ANISOU 3421 N LYS C 13 27292 31096 37285 3679 2197 -6957 N

ATOM 3422 CA LYS C 13 -69.206 81.492 36.646 1.00245.72 C

ANISOU 3422 CA LYS C 13 26506 30012 36843 3842 1913 -7357 C

ATOM 3423 CB LYS C 13 -70.195 82.200 37.578 1.00249.69 C

ANISOO 3423 CB LYS C 13 . 26779 30641 37452 3832 2026 -7838 C

ATOM 3424 CG LYS C 13 -70.658 81.379 38.787 1.00247.63 C

ANISOU 3424 CG LYS C 13 26285 30742 37060 3670 2459 -7824 C

ATOM 3425 CD LYS C 13 -71.856 80.498 38.469 1.00240.84 C

ANISOU 3425 CD LYS C 13 25184 29763 36561 3698 2618 -7965 C

ATOM 3426 CE LYS C 13 -72.463 79.936 39.740 1.00227.70 C

ANISOO 3426 CE LYS C 13 23279 28473 34763 3515 3035 -8006 C

ATOM 3427 NZ LYS C 13 -73.775 79.298 39.480 1.00212.93 N

ANISOU 3427 NZ LYS C , 13 21172 26491 33239 3527 3191 -8117 N

ATOM 3428 C LYS C ' 13 -68.200 82.502 36.108 1.00240.68 C

ANISOU 3428 C LYS C 13 26133 29260 36056 3889 1579 -7300 C

ATOM 3429 O LYS C 13 -67.281 82.894 36.828 1.00241.12 O

ANISOU 3429 O LYS C 13 26289 29556 35768 3794 1613 -7180 O

ATOM 3430 N PRO C 14 -68.353 82.913 34.838 1.00216.89 N

ANISOU 3430 N PRO C 14 23238 25875 33294 4029 1250 -7377 N

ATOM 3431 CA PRO C 14 -67.478 83.942 34.264 1.00217.42 _C

ANISOU 3431 CA PRO C 14 23552 25807 33250 4062 902 -7362 ' c

ATOM 3432 CB PRO C 14 -68.199 84.316 32.969 1.00211.92 C

ANISOU 3432 CB PRO C 14 22873 ' 24681 32966 4223 586 -7664 C

ATOM 3433 CG PRO C 14 -68.862 83.048 32.559 1.00215.85 C

ANISOU 3433 CG PRO C 14 23246 25068 33698 4277 751 -7544 C

ATOM 3434 CD PRO C 14 -69.288 82.371 33.838 1.00220.98 C

ANISOU 3434 CD PRO C 14 23661 26067 34236 4164 1170 -7526 C

ATOM 3435 C PRO C 14 -67.318 85.164 35.180 1.00221.68 C

ANISOU 3435 C PRO C 14 24095 26561 33574 4000 878 -7562 C

ATOM 3436 O PRO C 14 -68.307 85.695 35.698 1.00219.77 O

ANISOU 3436 O PRO C 14 23651 26386 33464 4018 963 -7942 O

ATOM 3437 N GLY C 15 -66.072 85.594 35.375 1.00242.44 N

ANISOU 3437 N GLY C 15 26934 29303 35880 3932 766 -7320 N

ATOM 3438 CA GLY C 15 -65.762 86.696 36.270 1.00234.36 C

ANISOU 3438 CA GLY C 15 25930 28464 34652 3889 708 -7488 C

ATOM 3439 C GLY C 15 -65.422 86.194 37.658 1.00234.27 C

ANISOO 3439 C GLY C 15 25820 28866 34326 3761 1078 -7344 C

ATOM 3440 O GLY C 15 -64.436 86.621 38.260 1.00222.62 O

ANISOU 3440 O GLY C 15 24464 27585 32536 3691 1064 -7205 O

ATOM 3441 N ALA C 16 -66.248 85.276 38.154 1.00270.37 N

ANISOU 3441 N ALA C 16 30179 33561 38987 3725 1402 -7372 N

ATOM 3442 CA ALA C 16 -66.068 84.684 39.475 1.00274.52 C

ANISOU 3442 CA ALA C 16 30599 34473 39233 3583 1779 -7236 C

ATOM 3443 CB ALA C 16 -67.087 83.578 39.703 1.00266.10 C

ANISOU 3443 CB ALA C 16 29304 33459 38341 3543 2085 -7258 C

ATOM 3444 C ALA C 16 -64.661 84.141 39.648 1.00274.47 C

ANISOU 3444 C ALA C 16 30797 34633 38856 3477 1842 -6762 C

ATOM 3445 O ALA C 16 -64.335 83.067 39.143 1.00272.53 O

ANISOU 3445 O ALA C 16 30603 34352 38593 3443 1924 -6427 O

ATOM 3446 N LEU C 17 -63.831 84.889 40.367 1.00236.15 " N

ANISOU 3446 N LEU C 17 26050 29956 33719 3434 1790 -6750 N

ATOM 3447 CA LEU C 17 -62.455 84.474 40.600 1.00232t43 C

ANISOU 3447 CA LEU C 17 25773 29643 32898 3337 1837 -6334 C

ATOM 3448 CB LEU C 17 -61.693 85.518 41.426 1.00233.99 C

ANISOU 3448 CB LEU C 17 26069 30008 32827 3315 1749 -6397 C

ATOM 3449 CG LEU C 17 -62.274 86.011 42.753 1.00235.38 C

ANISOU 3449 CG LEU C 17 26077 30436 32919 3290 1916 -6709 C

ATOM 3450 CDl LEU C 17 -62.087 84.975 43.850 1.00235.05 C

ANISOU 3450 CDl LEU C 17 25967 30716 32626 3140 2309 -6508 C

ATOM 3451 CD2 LEU C 17 -61.629 87.332 43.151 1.00231.94 C

ANISOU 3451 CD2 LEU C 17 25762 30045 32320 3330 1684 -6820 C

ATOM 3452 C LEU C 17 -62.411 83.101 41.259 1.00224.86 C

ANISOU 3452 C LEU C 17 24740 28907 31788 3208 2190 -6068 C

ATOM 3453 O LEU C 17 -63.293 82.745 42.039 1.00218.06 O

ANISOU 3453 O LEU C 17 23683 28214 30957 3149 2447 -6229 O

ATOM 3454 N VAL C 18 -61.381 82.334 40.921 1.00202.31 N

ANISOU 3454 N VAL C 18 22040 26051 28779 3157 2184 -5667 N ATOM 3455 CA VAL C 18 -61.228 80.966 41.399 1.00197.59 C

ANISOU 3455 CA VAL C 18 21404 25625 28047 3033 2455 -5379 C

ATOM 3456 CB VAL C 18 -61.423 79.961 40.234 1.00190.39 C

ANISOU 3456 CB VAL C 18 20456 24501 27384 3082 2419 -5215 C

ATOM 3457 CGl VAL C 18 -60.900 80.546 38.921 1.00187.15 C

ANISOU 3457 CGl VAL C 18 20205 23829 27073 3201 2095 -5138 C

ATOM 3458 CG2 VAL C 18 -60.771 78.624 40.544 1.00184.75 C

ANISOU 3458 CG2 VAL C 18 19750 23944 26504 2953 2621 -4860 C

ATOM 3459 C VAL C 18 -59.850 80.797 42.044 1.00186.91 C

ANISOU 3459 C VAL C 18 20242 24457 26317 2933 2479 -5059 C

ATOM 3460 O VAL C 18 -58.896 81.466 41.645 1.00185.63 O

ANISOU 3460 O VAL C 18 20255 24217 26059 2978 2254 -4969 O

ATOM 3461 N LYS C 19 -59.745 79.928 43.050 1.00178.52 N

ANISOU 3461 N LYS C 19 19149 23639 25043 2789 2745 -4899 N

ATOM 3462 CA LYS C 19 -58.464 79.703 43.723 1.00178.05 C

ANISOU 3462 CA LYS C 19 19269 23747 24633 2689 2775 -4604 C

ATOM 3463 CB LYS C 19 -58.471 80.346 45.115 1.00185.97 C

ANISOU 3463 CB LYS C 19 20263 25018 25378 2606 2938 -4734 C

ATOM 3464 CG LYS C 19 -57.133 80.943 45.553 1.00184.97 C

ANISOU 3464 CG LYS C 19 20351 24986 24944 2587 2834 -4581 C

ATOM 3465 CD LYS C 19 -57.202 81.512 46.974 1.00187.62 C

ANISOU 3465 CD LYS C 19 20668 25592 25026 2513 3008 -4715 C

ATOM 3466 CE LYS C 19 -55.833 81'.961 47.501 1.00181.65 C

ANISOU 3466 CE LYS C 19 20130 24924 23965 2495 2913 -4541 C

ATOM 3467 NZ LYS C 19 -55.413 83.329 47.062 1.00174.50 N

ANISOU 3467 NZ LYS C 19 19295 23908 23098 2628 2641 -4711 N

ATOM 3468 C LYS C 19 -58.138 78.207 43.826 1.00182.01 C

ANISOU 3468 C LYS C 19 19785 24292 25080 2582 2903 -4269 C

ATOM 3469 O LYS C 19 -58.890 77.457 44.450 1.00180.56 O

ANISOU 3469 O LYS C 19 19452 24182 24972 2500 3113 -4281 O

ATOM 3470 N ILE C 20 -57.016 77.789 43.222 1.00183.80 N

ANISOU 3470 N ILE C 20 20182 24470 25185 2581 2759 -3981 N

ATOM 3471 CA ILE C 20 -56.601 76.379 43.177 1.00170.46 C

ANISOU 3471 CA ILE C 20 18517 22788 23461 2502 2806 -3666 C

ATOM 3472 CB ILE C 20 -56.130 75.986 41.797 1.00162.07 C

ANISOU 3472 CB ILE C 20 17510 21511 22559 2614 2567 -3524 C

ATOM 3473 CGl ILE C 20 -56.665 76.965 40.764 1.00167.90 C

ANISOU 3473 CGl ILE C 20 18195 22031 ' 23568 2773 2398 -3769 C

ATOM 3474 CDl ILE C 20 -56.078 76.766 39.402 1.00165.85 C

ANISOU 3474 CDl ILE C 20 17985 21570 23461 2880 2171 -3643 C

ATOM 3475 CG2 ILE C 20 -56.548 74.577 41.503 1.00157.74 C

ANISOU 3475 CG2 ILE C 20 16882 20919 22133 2576 2617 -3323 C

ATOM 3476 C ILE C 20 -55.438 76.055 44.100 1.00164.78 C

ANISOU 3476 C ILE C 20 17953 22263 22392 2364 2875 -3424 C

ATOM 3477 O ILE C 20 -54.569 76.896 44.343 1.00159.34 O

ANISOU 3477 O ILE C 20 17400 21650 21493 2368 2810 -3438 O

ATOM 3478 N SER C 21 -55.400 74.808 44.563 1.00169.93 N

ANISOU 3478 N SER C 21 18593 22977 22994 2244 2983 -3199 N

ATOM 3479 CA SER C 21 -54.477 74.405 45.621 1.00171.37 C

ANISOU 3479 CA SER C 21 18925 23333 22855 2096 3050 -2978 C

ATOM 3480 CB SER C 21 -55.258 73.795 46.777 1.00175.90 C

ANISOU 3480 CB SER C 21 19418 24079 23338 1914 3313 -2943 C

ATOM 3481 OG ' SER C 21 -55.775 72.534 46.398 1.00173.28 O

ANISOU 3481 OG SER C 21 19004 23663 23173 1865 3316 -2772 O

ATOM 3482 C SER C 21 -53.412 73.405 45.184 1.00172.40 C

ANISOU 3482 C SER C 21 19175 23385 22946 2091 2875 -2689 C

ATOM 3483 O SER C 21 -53.506 72.796 44.116 1.00169.72 O

ANISOU 3483 O SER C 21 18769 22882 22836 2179 2743 -2629 O

ATOM 3484 N CYS C 22 -52.404 73.238 46.041 1.00166.65 N

ANISOU 3484 N CYS C 22 18620 22773 21927 1995 2864 -2527 N

ATOM 3485 CA CYS C 22 -51.320 72.280 45.831 1.00163.24 C

ANISOU 3485 CA CYS C 22 18300 22298 21426 1963 2708 -2266 C

ATOM 3486 CB CYS C 22 -50.196 72.929 45.022 1.00160.30 C

ANISOU 3486 CB CYS C 22 18035 21847 21026 2087 2482 -2263 C

ATOM 3487 SG CYS C 22 -49.200 71.792 44.042 1.00163.39 S

ANISOU 3487 SG CYS C 22 18442 22115 21523 2136 2240 -2049 S

ATOM 3488 C CYS C 22 -50.797 71.860 47.200 1.00159.98 C

ANISOU 3488 C CYS C 22 18025 22045 20714 1782 2812 -2112 C

ATOM 3489 O CYS C 22 -50.423 72.714 47.998 1.00159.81 O

ANISOU 3489 O CYS C 22 18116 22136 20468 1755 2867 -2175 O

ATOM 3490 N LYS C 23 -50.785 70.560 47.490 1.00161.18 N

ANISOU 3490 N LYS C 23 18175 22200 20866 1657 2825 -1912 N

ATOM 3491 CA LYS C 23 -50.396 70.115 48.826 1.00170.95 C

ANISOU 3491 CA LYS C 23 19551 23581 21820 1460 2929 -1767 C

ATOM 3492 CB LYS C 23 -51.476 69.250 49.484 1.00183.15 C

ANISOU 3492 CB LYS C 23 20998 25188 23403 1286 3101 -1682 C

ATOM 3493 CG LYS C 23 -51.359 69.174 51.011 1.00189.85 C ANISOU 3493 CG LYS C 23 21959 26242 23933 1069 3306 -1632 C

ATOM 3494 CD LYS C 23 -52.725 68.981 51.675 1.00202.4 , 9 C

ANISOU 3494 CD LYS C 23 23399 27950 25588 914 3555 -1663 C

ATOM 3495 CE LYS C 23 -52.671 69.279 53.172 1.00208.95 C

ANISOU 3495 CE LYS C 23 24244 29012 26134 781 3823 -1790 C

ATOM 3496 NZ LYS C 23 -54.024 69.499 53.767 1.00213.09 N

ANISOU 3496 NZ LYS C 23 24540 29649 26776 700 4082 -1947 N

ATOM 3497 C LYS C 23 -49.085 69.379 48.790 1.00166.55 C

ANISOU 3497 C LYS C 23 19172 22973 21135 1435 2712 -1559 C

ATOM 3498 O LYS C 23 -49.004 68.236 48.369 1.00165.41 O

ANISOU 3498 O LYS C 23 19005 22725 21118 1430 2554 -1405 O

ATOM 3499 N ALA C 24 -48.047 70.050 49.243 1.00179.90 N

ANISOU 3499 N ALA C 24 21036 24735 22583 1427 2688 -1570 N

ATOM 3500 CA ALA C 24 -46.738 69.459 49.197 1.00178.88 C

ANISOU 3500 CA ALA C 24 21078 24556 22333 1408 ,2476 -1405 C

ATOM 3501 CB ALA C 24 -45.696 70.520 49.362 1.00178.59 C

ANISOU 3501 CB ALA C 24 21202 24582 22072 1442 2461 -1473 C

ATOM 3502 C ALA C 24 -46.621 68.422 50.290 1.00181.51 C

ANISOU 3502 C ALA- C 24 21504 24921 22542 1203 2489 -1196 C

ATOM 3503 O ALA C 24 -46.933 68.*687 51.445 1.00191.01 O

ANISOU 3503 O ALA C 24 22723 26247 23605 1050 2701 -1188 O

ATOM 3504 N SER C 25 -46.168 67.237 49.916 1.00159.91 N

ANISOU 3504 N SER C 25 18824 22077 19858 1193 2250 -1034 N

ATOM 3505 CA SER C 25 -45.943 66.181 50.882 1.00162.85 C

ANISOU 3505 CA SER C 25 19336 22458 20083 990 2198 -827 C

ATOM 3506 CB SER C 25 -46.929 65.049 50.635 1.00163.29 C

ANISOU 3506 CB . SER C 25 19252 22462 20328 901 2199 -708 • C

ATOM 3507 OG SER C 25 -46.919 64.678 49.271 1.00160.41 O

ANISOU 3507 OG SER C 25 18740 21958 20252 1071 2000 -723 O

ATOM 3508 C SER C 25 -44.517 65.649 50.792 1.00168.17 C

ANISOU 3508 C SER C 25 20169 23039 20690 1018 1902 -732 C

ATOM 3509 O SER C 25 -43.910 65.651 49.721 1.00167.20 O

ANISOU 3509 O SER C 25 20004 22850 20676 1194 1742 -817 O

ATOM 3510 N GLY C 26 -43.981 ' 65.205 51.924 1.00188.68 N

ANISOU 3510 N GLY C 26 22954 25637 23099 835 1829 -568 N

ATOM 3511 CA GLY C 26 -42.710 64.498 51.954 1.00187.65 C

ANISOU 3511 CA GLY C 26 22977 25401 22921 839 1520 -480 C

ATOM 3512 C GLY C 26 -41.459 65.233 51.495 1.00175.53 C

ANISOU 3512 C GLY C 26 21516 23848 21331 998 1398 -603 C

ATOM 3513 O GLY C 26 -40.388 64.641. 51.392 1.00173.47 O

ANISOU 3513 O GLY C 26 21332 23493 21084 1028 1122 -566 O

ATOM 3514 N TYR C 27 -41.578 66.522 51.221 1.00151.49 N

ANISOU 3514 N TYR C 27 18443 20889 18227 1094 1584 -758 N

ATOM 3515 CA TYR C 27 -40.418 67.297 50.840 1.00145.24 C

ANISOU 3515 CA TYR C 27 17731 20086 17367 1222 1476 -861 C

ATOM 3516 CB TYR C 27 -40.493 67.604 49.344 1.00140.58 C

ANISOU 3516 CB TYR C 27 16953 19452 17010 1412 1377 -973 C

ATOM 3517 CG TYR C 27 ' -41.195 68.888 48.967 1.00139.02 C

ANISOU 3517 CG TYR C 27 16632 19315 16874 1519 1570 -1129 C

ATOM 3518 CDl TYR C 27 -40.694 70.113 49.375 1.00144.92 C

ANISOU 3518 CDl TYR C 27 17471 20125 17468 1564 1648 -1235 C

ATOM 3519 CEl TYR C 27 -41.295 71.300 49.034 1.00141.89 C

ANISOU 3519 CEl TYR C 27 16983 19780 17149 1661 1779 -1386 C

ATOM 3520 CZ TYR C 27 -42.400 71.289 48.251 1.00139.53 C

ANISOU 3520 CZ TYR C 27 16491 19452 17073 1719 1838 -1442 C

ATOM 3521 OH TYR C 27 -42.960 72.505 47.938 1.00139.97 O

ANISOU 3521 OH TYR C 27 16460 19527 17195 1814 1934 -1607 O

ATOM 3522 CE2 TYR C 27 -42.921 70.087 47.803 1.00137.11 C

ANISOU 3522 CE2 TYR C 27 16085 19082 16928 1686 1778 -1340 C

ATOM 3523 CD2 TYR C 27 -42.312 68.889 48.162 1.00135.02 C

ANISOU 3523 CD2 TYR C 27 15921 18785 16596 1586 1639 -1179 C

ATOM 3524 C TYR C 27 -40.419 68.561 51.694 1.00152.87 C

ANISOU 3524 C TYR C 27 18791 21163 18131 1217 1692 -958 C

ATOM 3525 O TYR C 27 -41.454 69.199 51.807 1.00161.08 O

ANISOU 3525 O TYR C 27 19737 22292 19175 1197 1927 -1022 O

ATOM 3526 N THR C 28 -39.292 68.923 52.312 1.00162.21 N

ANISOU 3526 N THR C 28 20150 22339 19145 1241 1602 -983 N

ATOM 3527 CA THR C 28 -39.266 70.059 53.259 1.00162.73 C

ANISOU 3527 CA THR C 28 20323 22502 19005 1241 1777 -1067 C

ATOM 3528 CB THR C 28 -37.860 70.299 53.825 1.00160.65 C

ANISOU 3528 CB THR C 28 20281 22193 18567 1255. 1623 -1057 C

ATOM 3529 OGl THR C 28 -37.029 69.156 53.574 1.00158.56 O

ANISOU 3529 OGl THR C 28 20122 21817 18305 1175 1394 -930 O

ATOM 3530 CG2 THR C 28 -37.935 70.584 55.319 1.00159.66 ' C

ANISOU 3530 CG2 THR C 28 20324 22158 18182 1179 1792 -1066 C

ATOM 3531 C THR C 28 -39.741 71.372 52.635 1.00161.15 C

ANISOU 3531 C THR C 28 19974 22359 18895 1391 1897 -1246 C ATOM 3532 O THR C 28 -38.983 72.021 51.936 1.00162.62 O

ANISOU 3532 O THR C 28 20171 22513 19106 1515 1781 -1326 O

ATOM 3533 N PHE C 29 -40.972 71.780 52.929 1.00161.52 N

ANISOU 3533 N PHE C 29 19893 22493 18986 1368 2117 -1313 N

ATOM 3534 CA PHE C 29 -41.694 72.775 52.122 1.00163.18 C

ANISOU 3534 CA PHE C 29 19928 22726 19346 1505 2198 -1490 C

ATOM 3535 CB PHE C 29 -42.979 73.205 52.838 1.00170.13 C

ANISOU 3535 CB PHE C 29 20721 23734 20185 1444 2464 -1585 C

ATOM 3536 CG PHE C 29 -44.067 73.721 51.917 1.00173.42 C

ANISOU 3536 CG PHE C 29 20914 24142 20837 1553 2536 -1753 C

ATOM 3537 CDl PHE C 29 -45.101 72.896 51.516 1.00174.04 C

ANISOU 3537 CDl PHE C 29 20829 24177 21120 1525 2579 -1723 C

ATOM 3538 CEl PHE C 29 -46.106 73.373 50.690 1.00173.37 C

ANISOU 3538 CEl PHE C 29 20550 24063 21258 1629 2633 -1889 C

ATOM 3539 CZ PHE C 29 -46.097 74.687 50.269 1.00171.58 C

ANISOU 3539 CZ PHE C 29 20296 23850 21048 1752 2630 -2086 C

ATOM 3540 CE2 PHE C 29 -45.090 75.518 50.667 1.00169.95 C

ANISOU 3540 CE2 PHE C 29 20242 23693 20637 1776 2582 -2110 C

ATOM 3541 CD2 PHE C 29 -44.076 75.039 51.488 1.00173.89 C

ANISOU 3541 CD2 PHE C 29 20932 24223 20916 1681 2544 -1944 C

ATOM 3542 C PHE C 29 -40.901 74.008 51.686 1.00164.27 C

ANISOU 3542 C PHE C 29 20109 22850 19458 1647 2102 -1610 C

ATOM 3543 O PHE C 29 -41.351 74.745 50.806 1.00165.78 O

ANISOU 3543 O PHE C 29 20168 23033 19789 1757 2116 -1749 O

ATOM 3544 N THR C 30 -39.727 74.231 52.275 1.00150.52 N

ANISOU 3544 N THR C 30 18553 21091 17548 1642 1988 -1560 N

ATOM 3545 CA THR C 30 -38.943 75.433 51.949 1.00149.92 C

ANISOU 3545 CA THR C 30 18525 21006 17432 1762 1900 -1663 C

ATOM 3546 CB THR C 30 -39.313 76.550 52.913 1.00144.35 C

ANISOU 3546 CB THR C 30 17894 20401 16552 1762 2049 -1756 C

ATOM 3547 OGl THR C 30 -39.462 75.996 54.226 1.00144.67 O

ANISOU 3547 OGl THR C 30 18061 20499 16407 1622 2158 -1655 O

ATOM 3548 CG2 THR C 30 -40.640 77.095 52.497 1.00138.54 . C

ANISOU 3548 CG2 THR C 30 16975 19728 15936 1806 2199 -1905 C

ATOM 3549 C THR C 30 -37.397 75.293 51.698 1.0O145.18 C

ANISOU 3549 C THR C 30 18042 20325 16795 1797 1673 -1605 C

ATOM 3550 O THR C 30 -36.683 74.497 52.344 1.00138.75 O

ANISOU 3550 O THR C 30 17362 19473 15885 1719 1588 -1495 O

ATOM 3551 N ASN C 31 -36.906 76.112 50.767 1.00155.25 N

ANISOU 3551 N ASN C 31 19266 21575 18146 1906 1568 -1691 N

ATOM 3552 CA ASN C 31 -35.714 75.801 49.971 1.00160.42 C

ANISOU 3552 CA ASN C 31 19939 22169 -18844 1942 1358 -1661 C

ATOM 3553 CB ASN C 31 -34.521 75.221 50.806 1.00164.61 C

ANISOU 3553 CB ASN C 31 20661 22663 19221 1887 1247 -1582 C

ATOM 3554 CG ASN C 31 -33.101 75.405 50.120 1.00151.74 C

ANISOU 3554 CG ASN C 31 19056 20993 17606 1945 1038 -1612 C

ATOM 3555 ODl ASN C 31 -32.710 76.500 49.706 1.00144.26 O

ANISOU 3555 ODl ASN C 31 18113 20061 16639 2012 1009 -1686 O

ATOM 3556 ND2 ASN C 31 -32.335 74.325 50.063 1.00133.79 N

ANISOU 3556 ND2 ASN C 31 16801 18670 15362 1909 885 -1561 N

ATOM 3557 C ASN C 31 -36.217 74.828 48.889 1.00161.00 C

ANISOU 3557 C ASN C 31 19847 22207 19118 1946 1300 -1630 C

ATOM 3558 O ASN C 31 -35.565 73.838 48.580 1.00166.23 O

ANISOU 3558 O ASN C 31 20512 22831 19818 1936 1143 -1576 O

ATOM 3559 N TYR C 32 -37.398 75.099 48.337 1.00163.79 N

ANISOU 3559 N TYR C 32 20053 22572 19608 1970 1416. -1678 N

ATOM 3560 CA TYR C 32 -37.865 74.402 47.138 1.00158.75 C

ANISOU 3560 CA TYR C 32 19245 21889 19182 2002 1358 -1667 C

ATOM 3561 CB TYR C 32 -38.356 72.994 47.466 1.00154.95 C

ANISOU 3561. CB TYR C 32 18739 21387 18749 1922 1382 -1556 C

ATOM 3562 CG TYR C 32 -37.266 71.969 47.712 1.00157.86 C

ANISOU 3562 CG TYR C 32 19217 21724 19040 1865 1218 -1454 C

ATOM 3563 CDl TYR C 32 -36.534 71.424 46.667 1.00158.30 C

ANISOU 3563 CDl TYR C 32 19190 21737 19220 1908 1021 -1437 C

ATOM 3564 CEl TYR C 32 -35.529 70.460 46.906 1.00166.06 C

ANISOU 3564 CEl TYR C 32 20266 22683 20147 1860 837 -1371 C

ATOM 3565 CZ TYR C 32 -35.265 70.032 48.202 1.00171.15 C

ANISOU 3565 CZ TYR C 32 21107 23315 20607 1761 851 -1306 C

ATOM 3566 OH TYR C 32 -34.284 69.090 48.471 1.00167.37 O

ANISOU 3566 OH TYR C 32 20734 22776 20084 1713 642 -1255 O

ATOM 3567 CE2 TYR C 32 -35.988 70.559 49.246 1.00175.82 C

ANISOU 3567 CE2 TYR C 32 21791 23955 21057 1713 1062 -1306 C

ATOM 3568 CD2 TYR C 32 -36.985 71.520 48.998 1.00168.62 C

ANISOU 3568 CD2 TYR C 32 20764 23098 20206 1769 1245 -1387 C

ATOM 3569 C TYR C 32 -38.984 75.208 46.486 1.00161.61 C

ANISOU 3569 C TYR C 32 ■19465 22245 19694 2068 1453 -1777 C

ATOM 3570 O TYR C 32 -39.979 75.511 47.142 1.00165.04 O ANISOU 3570 O TYR C 32 19861 22706 20142 2040 1621 -1813 O

ATOM 3571 N ASP C 33 -38.828 75.546 45.203 1.00149.58 N

ANISOU 3571 N ASP C 33 17862 20687 18286 2146 1339 -1836 N

ATOM 3572 CA ASP C 33 -39.781 76.409 44.497 1.00145.22 C

ANISOU 3572 CA ASP C 33 17196 20099 17883 2212 1384 -1952 C

ATOM 3573 CB ASP C 33 -39.080 77.122 43.367 1.00141.32 C

ANISOU 3573 CB ASP C 33 16686 19578 17433 2268 1223 -1996 C

ATOM 3574 CG ASP C 33 -38.114 78.116 43.855 1.00145.22 C

ANISOU 3574 CG ASP C 33 17313 20114 17751 2256 1154 -2006 C

ATOM 3575 ODl ASP C 33 -38.376 78.694 44.918 1.00148.29 O

ANISOU 3575 ODl ASP C 33 17798 20538 18007 2234 1243 -2019 O

ATOM 3576 OD2 ASP C 33 -37.092 78.317 43.186 1.00144.92 O

ANISOU 3576 OD2 ASP C 33 17281 20078 17704 2267 1012 -2002 O

ATOM 3577 C ASP C 33 -40.984 75.710 43.896 1.00146.03 C

ANISOϋ 3577 C ASP C 33 17145 20149 18192 2229 1447 -1954 C

ATOM 3578 O ASP C 33 -40.877 74.602 43.378 1.00140.32 O

ANISOU 3578 O ASP C 33 16368 19400 17548 2221 1379 -1863 O

ATOM 3579 N ILE C 34 -42.128 76.380 43.935 1.00149.64 N

ANISOU 3579 N ILE C 34 17523 20583 18749 2260 1559 -2072 N

ATOM 3580 CA ILE C 34 -43.293 75.899 43.214 1.00150.25 C

ANISOU 3580 CA ILE C 34 17443 20584 19061 2301 1596 -2108 C

ATOM 3581 CB ILE C 34 -44.535 75.853 44.107 1.00147.84 C

ANISOU 3581 CB ILE C 34 17070 20309 18795 2256 1806 -2162 C

ATOM 3582 CGl ILE C 34 -44.232 75.112 45.394 1.00148.55 C

ANISOU 3582 CGl ILE C 34 17267 20505 18670 2138 1916 -2055 C

ATOM 3583 CDl ILE C 34 -44.639 73.679 45.332 1.00148.38 C

ANISOU 3583 CDl ILE C 34 17224 20468 18684 2066 1908 -1891 C

ATOM 3584 CG2 ILE C 34 -45.645 75.096 43.424 1.00144.93 C

ANISOU 3584 CG2 ILE C 34 16545 19859 18661 2277 1832 -2139 C

ATOM 3585 C ILE C 34 -43.539 76.822 42.022 1.00152.49 C

ANISOU 3585 C ILE C 34 17666 20780 19492 2395 1490 -2232 C

ATOM 3586 O ILE C 34 -43.649 78.039 42.197 1.00147.51 O

ANISOU 3586 O ILE C 34 17078 20149 18821 2418 1484 -2352 O

ATOM 3587 N HIS C 35 -43.582 76.233 40.820 1.00148.06 N

ANISOU 3587 N HIS C 35 17016 20142 19097 2448 1385 -2198 N

ATOM 3588 CA HIS C 35 -43.929 76.916 39.572 1.00140.73 C

ANISOU 3588 CA HIS C 35 16033 19114 18325 2529 1267 -2292 C

ATOM 3589 CB HIS C 35 -43.045 76.409 38.443 1.00137.53 C

ANISOU 3589 CB HIS C 35 15622 18712 17922 2550 1099 -2203 C

ATOM 3590 CG HIS C 35 -41.704 77.058 38.348 1.00137.56 C

ANISOU 3590 CG HIS C 35 15739 18784 17743 2515 983 -2186 C

ATOM 3591 NDl HIS C 35 -40.673 76.777 39.212 1.00138.72 N

ANISOU 3591 NDl HIS C 35 15987 19036 ' 17686 2449 989 -2108 N

ATOM 3592 CEl HIS C 35 -39.598 77.464 38.864 1.00138.88 C

ANISOU 3592 CEl HIS C 35 16080 19096 17591 2429 872 -2113 C

ATOM 3593 NE2 HIS C 35 -39.894 78.164 37.782 1.00137.61 N

ANISOU 3593 NE2 HIS C 35 15878 18867 17540 2465 785 -2179 N

ATOM 3594 CD2 HIS C 35 -41.194 77.918 37.430 1.00137.21 C

ANISOU 3594 CD2 HIS C 35 15724 18718 17693 2526 847 -2229 C

ATOM 3595 C HIS C 35 -45.354 76.530 39.190 1.00143.14 C

ANISOU 3595 C HIS C 35 16195 19309 18884 2589 1333 -2368 C

ATOM 3596 O HIS C 35 -45.811 75.445 39.536 1.00139.50 O

ANISOU 3596 0 HIS C 35 15656 18848 18501 2577 1404 -2288 O

ATOM 3597 N TRP C 36 -46.043 77.380 38.435 1.00142.95 N

ANISOU 3597 N TRP C 36 16137 19179 18999 2653 1288 -2521 N

ATOM 3598 CA TRP C 36 -47.388 77.052 37.978 1.00144.33 C

ANISOU 3598 CA TRP C 36 16176 19226 19437 2722 1336 -2622 C

ATOM 3599 CB TRP C 36 -48.391 77.986 38.641 1.00154.70 C

ANISOU 3599 CB TRP C 36 17466 20516 20796 2728 1435 -2819 C

ATOM 3600 CG TRP C 36 -48.543 77.804 40.136 1.00161.23 C

ANISOU 3600 CG TRP C 36 18290 21485 21485 2644 1643 -2808 C

ATOM 3601 CDl TRP C 36 -47.868 78.469 41.125 1.00164.15 C

ANISOU 3601 CDl TRP C 36 18766 21983 21621 2583 1693 -2814 C

ATOM 3602 NEl TRP C 36 -48.291 78.042 42.360 1.00164.54 N

ANISOU 3602 NEl TRP C 36 18782 22147 21587 2506 1899 -2797 N

ATOM 3603 CE2 TRP C 36 -49.258 77.088 42.185 1.00165.31 C

ANISOU 3603 CE2 TRP C 36 18747 22192 21871 2507 1985 -2772 C

ATOM 3604 CD2 TRP C 36 -49.449 76.919 40.803 1.00158.43 C

ANISOU 3604 CD2 TRP C 36 17824 21161 21211 2605 1824 -2783 C

ATOM 3605 CE3 TRP C 36 -50.398 75.997 40.363 1.00158.86 C

ANISOU 3605 CE3 TRP C 36 17742 21122 21495 2640 1860 -2764 C

ATOM 3606 CZ3 TRP C 36 -51.110 75.285 41.294 1.00162.47 C

ANISOU 3606 CZ3 TRP C 36 18117 21651 21964 2561 2053 -2727 C

ATOM 3607 CH2 TRP C 36 -50.897 75.468 42.654 1.00170.03 C

ANISOU 3607 CH2 TRP C 36 19133 22780 22692 2442 2217 -2709 C

ATOM 3608 CZ2 TRP C 36 -49.978 76.366 43.122 1.00174.10 C

ANISOU 3608 CZ2 TRP C 36 19785 23386 22979 2421 2187 -2736 C ATOM 3609 C TRP C 36 -47.517 77.187 36.465 1.00142.69 C

ANISOU 3609 C TRP C 36 15934 18875 19408 2812 1161 -2660 C

ATOM 3610 O TRP C 36 -47.112 78.199 35.908 1.00140.42 O

ANISOU 3610 O TRP C 36 15726 18543 19085 2821 1026 -2729 O

ATOM 3611 N VAL C 37 -48.093 76.187 35.797 1.00124.80 N

ANISOO 3611 N VAL C 37 13555 16530 17332 2874 1150 -2614 N

ATOM 3612 CA VAL C 37 -48.276 76.255 34.336 1.00128.32 C

ANISOU 3612 CA VAL C 37 13968 16835 17952 2969 985 -2654 C

ATOM 3613 CB VAL C 37 -47.493 75.171 33.614 1.00123.27 C

ANISOU 3613 CB VAL C 37 13293 16239 17306 2996 885 -2504 C

ATOM 3614 CGl VAL C 37 -46.014 75.357 33.794 1.00120.11 C

ANISOU 3614 CGl VAL C 37 12993 16012 16632 2910 840 -2390. C

ATOM 3615 CG2 VAL C 37 -47.922 73.839 34.119 1.00125.53 C

ANISOU 3615 CG2 VAL C 37 13454 16509 17733 3024 975 -2431 C

ATOM 3616 C VAL C 37 -49.730 76.136 33.837 1.00135.65 C

ANISOO 3616 C VAL C 37 14775 17581 19183 3065 1013 -2784 C

ATOM 3617 O VAL C 37 -50.556 75.452 34.435 1.00138.98 O

ANISOU 3617 o- VAL C 37 15098 18000 19709 3063 1166 -2797 O

ATOM 3618 N LYS C 38 -50.014 76.780' 32.708 1.00161.69 N

ANISOU 3618 N LYS C 38 18087 20725 22623 3144 855 -2876 N

ATOM 3619 CA LYS C 38 -51.363 76.879 32.161 1.00166.90 C

ANISOU 3619 CA LYS C 38 18668 21176 23572 3239 844 -3053 C

ATOM 3620 CB LYS C 38 -51.697 78.348 31.943 1.00177.77 C

ANISOU ' 3620 CB LYS C 38 ' 20148 22461 24936 3228 733 -3228 C

ATOM 3621 CG LYS C 38 -52.466 78.658 30.668 1.00180.11 C

ANISOU 3621 CG LYS C 38 20445 22506 25483 3330 559 -3375 C

ATOM 3622 CD LYS C 38 -53.901 79.020 30.989 1.00187.81 C

ANISOO 3622 CD LYS C 38 21299 23327 26733 3405 646 -3587 C

ATOM 3623 CE LYS C 38 -54.307 80.305 30.286 1.00192.69 C

ANISOU 3623 CE LYS C 38 21982 23711 27520 3461 449 -3811 C

ATOM 3624 NZ LYS C 38 -55.301 81.070 31.088 1.00201.13 N

ANISOO 3624 NZ LYS C 38 22927 24666 28828 3519 544 -4058 N

ATOM 3625 C LYS C 38 -51.435 76.177 30.831 1.00167.37 C

ANISOU 3625 C LYS 38 18671 21093 23829 3352 708 -3022 C

ATOM 3626 O LYS C 38 -50.597 76.400 29.969 1.00170.55 O

ANISOO 3626 O LYS C 38 19157 21475 24168 3362 537 -2990 O

ATOM 3627 N GLN C 39 -52.442 75.342 30.641 1.00158.57 N

ANISOU 3627 N GLN C 39 17413 19882 22955 3435 778 -3034 N

ATOM ' 3628 CA GLN C 39 -52.521 74.591 29.400 1.00162.21 C

ANISOU 3628 CA GLN C 39 17814 20209 23610 * ■ 3560 640 -2999 C

ATOM 3629 CB GLN C 39 -52.185 73.123 29.650 1.00163.61 C

ANISOU 3629 CB GLN C 39 17879 20478 23809 3581 687 -2821 C

ATOM 3630 CG GLN C 39 -51.897 72.305 ' 28.394 1.00158.80 C

ANISOU 3630 CG GLN C 39 17239 19832 23266 3688 501 -2739 C

ATOM 3631 CD GLN C 39 -51.648 70.823 28.689 1.00154.30 C

ANISOO 3631 CD GLN C 39 16560 19364 22702 3708 502 -2570 C

ATOM 3632 OEl GLN C 39 -50.931 70.142 27.949 1.00149.62 O

ANISOU 3632 ' OEl GLN C 39 15927 18785 22138 3793 347 -2506 O

ATOM 3633 NE2 GLN C 39 -52.245 70.320 29.770 1.00147.98 N

ANISOO 3633 NE2 GLN C 39 15713 18641 21873 3624 661 -2504 N

ATOM 3634 C GLN C 39 -53.890 74.689 28.773 1.00166.25 C

ANISOU 3634 C GLN C 39 18258 20458 24452 3683 599 -3183 C

ATOM 3635 O GLN C 39 -54.807 73.987 29.185 1.00167.85 O

ANISOU 3635 O GLN C 39 18327 20593 24854 3723 725 -3235 O

ATOM 3636 N ARG C 40 -54.032 75.561 27.780 1.00182.99 N

ANISOU 3636 N ARG C 40 20472 22424 26630 3734 414 -3285 N

ATOM 3637 CA ARG C 40 -55.242 75.579 26.970 1.00192.44 C

ANISOO 3637 CA ARG C 40 21614 23341 28162 3876 323 -3443 C

ATOM 3638 CB ARG C 40 -55.133 76.618 25.865 1.00191.43 C

ANISOU 3638 CB ARG C 40 21636 23061 28038 3902 86 -3523 C

ATOM 3639 CG ARG C 40 -54.678 77.952 26.327 1.00197.29 . C

ANISOU 3639 CG ARG C 40 22536 23869 28558 3774 29 -3577 C

ATOM 3640 CD ARG C 40 -54.998 78.970 25.281 1.00200.02 C

ANISOU 3640 CD ARG C 40 22977 23938 29082 3825 -173 -3779 C

ATOM 3641 NE ARG C 40 -55.590 80.152 25.890 1.00211.90 N

ANISOU 3641 NE ARG C 40 24530 25423 30560 3755 -161 -3954 N

ATOM 3642 CZ ARG C 40 -56.899 80.319 26.044 1.00220.20 C

ANISOU 3642 CZ ARG C 40 25624 26220 31822 3805 -308 -4198 C

ATOM 3643 NHl ARG C 40 -57.727 79.371 25.619 1.00223.18 N

ANISOO 3643 NHl ARG C 40 26019 26330 32451 3922 -472 -4283 N

ATOM 3644 NH2 ARG C 40 -57.382 81.424 26.614 .1.00220.57 N

ANISOU 3644 NH2 ARG C 40 25698 26275 31835 3747 -308 -4368 N

ATOM 3645 C ARG C 40 -55.372 74.206 26.330 1.00200.85 C

ANISOU 3645 C ARG C 40 22553 24378 29381 3990 308 -3316 C

ATOM 3646 O ARG C ' 40 -54.558 73.852 25.475 1.00203.15 O

ANISOU 3646 O ARG C 40 22875 24780 29534 3994 210 -3164 O

ATOM 3647 N PRO C 41 -56.404 73.435 26.718 1.00197.68 N ANISOU 3647 N PRO C 41 22002 23833 29276 4086 391 -3388 N

ATOM 3648 CA PRO C 41 -56.512 72.019 26.344 1.00193.41 C

ANISOU 3648 CA PRO C 41 21325 23252 28909 4203 362 -3264 C

ATOM 3649 CB PRO C 41 -57.985 71.699 26.622 1.00192.-76 C

ANISOU 3649 CB PRO C 41 21105 22951 29184 4298 442 -3420 C

ATOM 3650 CG PRO C 41 -58.657 73.039 26.668 1.00198.67 C

ANISOU 3650 CG PRO C 41 21944 23558 29982 4279 418 -3668 C

ATOM 3651 CD PRO C 41 -57.649 73.904 27.340 1.00197.01 C

ANISOα 3651 CD PRO C 41 21856 23590 29408 4105 484 -3613 C

ATOM 3652 C PRO C 41 -56.182 71.769 24.877 1.00192.23 C

ANISOU 3652 C PRO C 41 21227 23012 28801 4322 132 -3226 C

ATOM 3653 O PRO C 41 -56.330 72.650 24.031 1.00186.96 O

ANISOU 3653 O PRO C 41 20686 22216- 28136 4342 -8 -3340 O

ATOM 3654 N GLY C 42 -55.722 70.563 24.579 1.00194.68 N

ANISOU 3654 N GLY C 42 21440 23395 29133 4396 79 -3068 N

ATOM 3655 CA GLY C 42 -55.344 70.235 23.220 1.00191.32 C

ANISOU 3655 CA GLY C 42 21038 22920. 28736 4516 -131 -3036 C

ATOM 3656 C GLY C 42 -54.033 70.881 22.812 1.00185.38 C

ANISOU 3656 C GLY C 42 20430 22366 27639 4403 -214 -2973 C

ATOM 3657 O GLY C 42 -53.288 70.334 21.991 1.00185.41 O

ANISOU 3657 O GLY C 42 20415 22475 27558 4453 -339 -2885 O

ATOM 3658 N GLN C 43 -53.738 72.038 23.395 1.00171.52 N

ANISOU 3658 N GLN C 43 18810 20672 25687 4251 -149 -3027 N

ATOM 3659 CA GLN C 43 -52.517 72.752 23.055 1.00177.85 C

ANISOU 3659 CA GLN C 43 19755 21651 26168 4128 -227 -2972 C

ATOM 3660 CB GLN C 43 -52.840 74.214 22.800 1.00179.08 C

ANISOU 3660 CB GLN C 43 20079 21672 26291 4055 -290 -3112 C

ATOM 3661 CG GLN C 43 -53.881 74.400 21.735 1.00174.62 C

ANISOU 3661 CG GLN C 43 19549 20806 25993 4189 -451 -3250 C

ATOM 3662 CD GLN C 43 -54.242 75.854 21.557 1.00195.34 C

ANISOU 3662 CD GLN C 43 22277 23221 28722 4153 -481 -3442 C

ATOM 3663 OEl GLN C 43 -54.458 76.577 22.534 ' 1.00197.84 O

ANISOU 3663 OEl GLN C 43 22561 23574 29034 4089 -333 -3505 O

ATOM 3664 NE2 GLN C 43 -54.311 76.298 20.308 1.00207.24 N

ANISOU 3664. NE2 GLN C 43 23909 24504 30327 4194 -686 -3548 N

ATOM 3665 C GLN C 43 -51.375 72.598 24.076 1.00170.05 C

ANISOU 3665 C GLN C 43 18769 20960 24884 3984 -112 -2834 C

ATOM 3666 O GLN C 43 -51.412 71.726 24.945 1.00159.42 O

ANISOU 3666 O GLN C 43 17308 19692 23573 3988 3 -2754 O

ATOM 3667 N GLY C 44 -50.361 73.452 23.956 1.00191.07 N

ANISOU 3667 N GLY C 44 21567 23772 27259 3850 -157 -2805 N

ATOM 3668 CA GLY C 44 -49.132 73.299 24.715 1.00183.52 C

ANISOU 3668 CA GLY C 44 20626 23088 26015 3723 -86 -2683 C

ATOM 3669 C GLY C 44 -49.136. 73.797 26.151 1.00184.20 C

ANISOU 3669 C GLY C 44 . 20737 23247 26003 3614 ' 93 -2675 C

ATOM 3670 O GLY C 44 -50.189 74.078 26.731 1.00181.82 O

ANISOU 3670 O GLY C 44 20385 22818 25882 3648 203 -2748 O

ATOM 3671 N LEU C- 45 -47.936 73.891 26.725 1.00150.69 N

ANISOU 3671 N LEU C 45 16565 19220 21470 3484 . 123 -2591 N

ATOM 3672 CA LEU C 45 -47.751 74.392 28.080 1.00139.30 C

ANISOU 3672 CA LEU C 45 15176 17870 19883 3371 274 -2579 C

ATOM 3673 CB LEU C 45 -46.713 73.550 28.833 1.00130.93 C

ANISOU 3673 CB LEU C 45 14087 17025 18635 3307 322 -2439 C

ATOM 3674 CG LEU C 45 -46.791 72.026 28.931 1.00130.26 C

ANISOU 3674 CG LEU C 45 13857 16962 18673 3389 310 -2351 C

ATOM 3675 CDl LEU C 45 -45.643 71.541 29.754 1.00124.07 C

ANISOU 3675 CDl LEU C 45 13087 16360 17695 3293 367 -2240 C

ATOM 3676 CD2 LEU C 45 -48.075 71.577 29.566 1.00141.32 ' C

ANΪSOU 3676 CD2 LEU C 45 15161 18189 20345 3469 397 -2394 C

ATOM 3677 C LEU C 45 -47.295 75.851 28.036 1.00143.00 C

ANISOU 3677 C LEU C 45 15804 18359 20170 3264 225 -2636 C

ATOM 3678 O LEU C 45 -46.720 76.304 27.046 1.00141.11 O

ANISOU 3678 O LEU C 45 15636 18138 19841 3240 79' -2629 O

ATOM 3679 N GLU C 46 -47.547 76.577 29.118 1.00154.58 N

ANISOU 3679 N GLU C 46 17326 19830 21579 3197 336 -2691 N

ATOM 3680 CA GLU C 46 -47.171 77.980 29.220 1.00158.22 C

ANISOU 3680 CA GLU C 46 17934 20307 21874 3099 273 -2745 C

ATOM 3681 CB GLU C 46 -48.353 78.862 28.801 1.00169.21 C

ANISOU 3681 CB GLU C 46 19367 21466 23459 3147 179 -2920 C

ATOM 3682 CG GLU C 46 -47.996 80.240 28.238 1.00172.68 C

ANISOU 3682 CG GLU C 46 19970 21870 23770 3062 -12 -2952 C

ATOM 3683 CD GLU C 46 -49.231 81.065 27.885 1.00177.07 C

ANISOU 3683 CD GLU C 46 20576 22165 24537 3111 -147 -3139 C

ATOM 3684 OEl GLU C 46 -50.364 80.526 27.924 1.00178.65 O

ANISOU 3684 OEl GLU C 46 20676 22199 25004 3229 -108 -3248 O

ATOM 3685 0E2 GLU C 46 -49.061 82.260 27.570 1.00173.29 O

ANISOU 3685 0E2 GLU C 46 20240 21639 23963 3028 -310 -3181 O ATOM 3686 C GLU C 46 -46.824 78.220 30.679 1.00153.07 C

ANISOU 3686 C GLU C 46 17319 19790 21052 3013 418 -2724 C

ATOM 3687 O GLU C 46 -47.388 77.571 31.557 1.00152.09 O

ANISOU 3687 O GLU C 46 17113 19674 " 21001 3034 576 -2735 O

ATOM 3688 N TRP C 47 -45.905 79.139 30.956 1.00132.62 N

ANISOU 3688 N TRP C 47 14853 17305 18233 2912 361 -2693 N

ATOM 3689 CA TRP C 47 -45.471 79.336 32.341 1.00134.13 C

ANISOU 3689 CA TRP C 47 15089 17630 18244 2839 485 -2664 C

ATOM 3690 CB TRP C 47 -43.946 79.320 32.442 1.00131.11 C

ANISOU 3690 CB TRP C 47 14781 17429 17605 2750 439 -2531 C

ATOM 3691 CG TRP C 47 -43.479 79.643 33.821 1.00127.42 C

ANISOU 3691 CG TRP C 47 14379 17076 16959 2683 543 -2505 C

ATOM 3692 CDl TRP C 47 -43.588 78.855 34.929 1.00123.61 C

ANISOU 3692 CDl TRP C 47 13857 16670 16441 2679 702 -2456 C

ATOM 3693 NEl TRP C 47 -43.060 79.501 36.018 1.00130.53 N

ANISOU 3693 NEl TRP C 47 14830 17637 17129 2614 , 752 -2449 N

ATOM 3694 CE2 TRP C 47 -42.595 80.731 35.627 1.00129.59 C

ANISOU 3694 CE2 TRP C 47 14808 17499 16931 2579 617 -2492 C

ATOM 3695 CD2 TRP C 47 -42.841 80.854 34.246 1.00127.34 C

ANISOU 3695 CD2 TRP C 47 14495 17111 16776 2610 482 -2523 C

ATOM 3696 CE3 TRP C 47 -42.443 82.025 33.588 1.00125.73 C

ANIΞOU 3696 CE3 TRP C 47 14389 16865 16516 2561 311 -2555 C

ATOM 3697 CZ3 TRP C 47 -41.835 83.015 34.321 1.00127.41 C

ANISOU 3697 CZ3 TRP C 47 14711 17136 16564 2496 277 -2557 C

ATOM 3698 CH2 TRP C 47 -41-.612 82.869 35.698 1.00127.12 C

ANISOU 3698 CH2 TRP C 47 14690 17198 16411 2488 416 -2536 C

ATOM 3699 CZ2 TRP C 47 -41.979 81.739 36.367 1.00125.16 C

ANISOU 3699 CZ2 TRP C 47 14361 16997 16197 2523 589 -2503 C

ATOM 3700 C TRP C 47 -46.025 80.575 33.056 1.00135.93 C

ANISOU 3700 C TRP C 47 15388 17796 18464 2815 487 -2802 C

ATOM 3701 O TRP C 47 -45.838 81.700 32.606 1.00133.32 O

ANISOU 3701 O TRP C 47 15164 17426 18067 ' 2772 333 -2844 O

ATOM 3702 N ILE C 48 -46.670 80.356 34.197 1.00134.28 N

ANISOU 3702 N ILE C 48 15114 17592 18314 2837 654 -2874 N

ATOM 3703 CA ILE C 48 -47.307 81.435 34.953 1.00139.55 C

ANISOU 3703 CA ILE C 48 15810 18216 18998 2836 671 -3042 C

ATOM 3704 CB ILE C 48 -48.506 80.895 35.736 1.00141.90 C

ANISOU 3704 CB ILE C 48 15975 18496 19446 2881 868 -3147 C

ATOM 3705 CGl ILE C 48 -49.533 80.300 34.775 1.00140.26 C

ANIΞOU 3705 CGl ILE C 48 15651 l 18123 19520 2972 852 -3199 C

ATOM 3706 CDl ILE C 48 -50.738 79.723 35.469 1.00143.28 C

ANISOU 3706 CDl ILE C 48 15889 18479 20073 3008 1040 -3317 C

ATOM 3707 CG2 ILE C 48 -49.125 81.987 36.583 1.00150.14 C

ANISOU 3707 CG2 ILE C 48 17022 19518 20507 2887 885 -3356 C

ATOM 3708 C ILE C 48 -46.377 82.174 35.929 1.00137.91 C

ANISOU 3708 C ILE C 48 15714 18155 18529 2755 678 -2995 C

ATOM 3709 O ILE C 48 -46.132 83.372 35.794 1.00133.65 O

ANISOU 3709 O ILE C 48 15275 17579 17926 2728 521 -3052 O

ATOM 3710 N GLY C 49 -45.878 81.459 36.929 1.00148.73 N

ANISOU 3710 N GLY C 49 17075 19680 19756 2715 844 -2888 N

ATOM 3711 CA GLY C 49 -44.911 82.028 37.850 1.00146.35 C

ANISOU 3711 CA GLY C 49 16886 19517 19205 2646 850 -2819 C

ATOM 3712 C GLY C 49 -44.305 81.002 38.794 1.00143.58 C

ANISOU 3712 C GLY C 49 16535 19312 18708 2600 1013 -2680 C

ATOM 3713 O GLY C 49 -44.547 79.791 38.686 1.00134.59 O

ANISOU 3713 O GLY C 49 15309 "18177 17653 2610 1103 -2608 O

ATOM 3714 N TRP C 50 -43.498 81.486 39.726 1.00148.35 N

ANISOU 3714 N TRP C 50 17244 20023 1909 ' 9 2550 1028 -2641 N

ATOM 3715 CA TRP C 50 -43.041 80.625 40.792 1.00148.54 C

ANISOU 3715 CA TRP C 50 17299 20171 18970 2498 1169 -2529 C

ATOM 3716 CB TRP C 50 -41.624 80.105 40.548 1.00150.36 C

ANISOU 3716 CB TRP C 50 17605 20469 19056 2454 1077 -2373 C

ATOM 3717 CG TRP C 50 -40.537 81.152 40.442 1.00156.24 C

ANISOU 3717 CG TRP C 50 18468 21242 19655 2428 938 -2372 C

ATOM 3718 CDl TRP C 50 -39.794 81.458 39.328 1.00155.27 C

ANISOU 3718 CDl TRP C 50 18364 21094 19539 2417 767 -2352 C

ATOM 3719 NEl TRP C 50 -38.885 82.447 39.620 1.00156.38 N

ANISOU 3719 NEl TRP C 50 18619 21275 19525 2378 676 -2345 N

ATOM 3720 ' CE2 TRP C 50 -39.021 82.795 40.938 1.00152.09 C

ANISOU 3720 CE2 TRP C 50 18133 20777 18876 2383 781 -2366 C

ATOM 3721 CD2 TRP C 50 -40.045 81.996 41.489 1.00152.68 C

ANISOU 3721 CD2 TRP C 50 18130 20854 19027 2405 953 -2383 C

ATOM 3722 CE3 TRP C 50 -40.372 82.157 42.833 1.00149.87 C

ANISOU 3722 CE3 TRP C 50 17818 20560 18567 2398 1093 -2404 C

ATOM 3723 CZ3 TRP C 50 -39.688 83.088 43.567 1.00150.74 C

ANISOU 3723 CZ3 TRP C 50 18045 20714 18516 2392 1048 -2416 C

ATOM 3724 CH2 TRP C 50 -38.678 83.864 42.995 1.00150.91 C ANISOU 3724 CH2 TRP C 50 18137 20716 18485 2383 865 -2398 C

ATOM 3725 CZ2 TRP C 50 -38.331 83.732 41.685 1.00146.87 C

ANISOU 3725 CZ2 TRP C 50 17586 20157 18060 2367 735 -2370 C

ATOM 3726 C TRP C 50 -43.143 81.324 42.118 1.00152.87 C

ANISOU 3726 C TRP C 50 17916 20795 19373 2479 1260 -2597 C

ATOM 3727 O TRP C 50 -43.090 82.549 42.199 1.00147.99 O

ANISOU 3727 O TRP C 50 17361 20162 18707 2498 1159 -2686 O

ATOM 3728 N ILE C 51 -43.308 80.520 43.157 1.00154.36 N

ANISOU- 3728 N ILE C 51 18094 21067 19488 2438 1438 -2551 N

ATOM 3729 CA ILE C 51 -43.352 81.024 44.513 1.00159.69 C '

ANISOU 3729 CA ILE C 51 18846 21843 19987 2411 1539 -2595 C

ATOM 3730 CB ILE C 51 -44.764 80.971 45.065 1.00158.07 C

ANISOU 3730 CB ILE C 51 18537 21671 19852 2416 1717 -2741 C

'ATOM 3731 CGl ILE C 51 -44.836 81.727 46.388 1.00155.29 C

ANISOU 3731 CGl ILE C 51 18258 21424 19322 2414 1777 -2834 C

ATOM 3732 CDl ILE C 51 -44.731 83.224 46.212 1.00165.33 C

ANISOU 3732 CDl ILE C 51 19435 22678 20706 2485 1774 -3085 C

ATOM 3733 CG2 ILE C 51 -45.214 79.534 45.195 1.00154.74 C

ANISOU 3733 CG2 ILE C 51 18059 21296 19441 2345 1885 -2631 C

ATOM 3734 C ILE C 51 -42.449 80.177 45.397 1.00157.50 C

ANISOU 3734 C ILE C 51 18673 21658 19513 2335 1605 -2430 C

ATOM 3735 O ILE C 51 -42.421 78.950 45.271 1.00152.83 O

ANISOU 3735 O ILE C 51 18051 21065 18951 2290 1644 -2309 O

ATOM 3736 N TYR C 52 -41.704 80.848 46.271 1.00160.53 N

ANISOU 3736 N TYR C 52 19183 22106 19706 2326 1593 -2435 N

ATOM 3737 CA TYR C 52 -40.741 80.206 47.154 1.00157.10 C

ANISOU 3737 CA TYR C 52 18879 21740 19070 2260 1627 -2301 C

ATOM 3738 CB TYR C 52 -39.371 80.893 47.034 1.00156.97 C

ANISOU 3738 CB TYR C 52 18991 21715 18934 2283 1461 -2268 , c

ATOM 3739 CG TYR C 52 -38.302 80.440 48.029 1.00165.68 C

ANISOU 3739 CG TYR C 52 20246 22861 19842 2229 1461 -2148 C

ATOM 3740 CDl TYR C 52 -37.328 81.327 48.486 1.00160.57 C

ANISOU 3740 CDl TYR C 52 19730 22223 19055 2254 1364 -2151 C

ATOM 3741 CEl TYR C 52 -36.352 80.918 49.385 1.00160.99 C

ANISOU 3741 CEl TYR C 52 19930 22295 18945 2212 1351 -2056 C

ATOM 3742 CZ TYR C .52 -36.341 79.613 49.841 1.00161.37 C

ANISOU 3742 CZ TYR C 52 20004 22350 18961 2136 1418 -1953 C

ATOM 3743 OH TYR C 52 -35.380 79.209 50.732 1.00165.02 O

ANISOU 3743 OH TYR C 52 20624 22806 19269 2092 1376 -1869 O

ATOM 3744 CE2 TYR C 52 -37.289 78.715 49.411 1.00160.06 C

ANISOU 3744 CE2 TYR C 52 19708 22182 18926 2101 1506 -1934 C

ATOM 3745 CD2 TYR C 52 -38.264 79.128 48.508 1.00166.89 C

ANISOU 3745 CD2 TYR C 52 20419 23032 19961 2153 1535 -2032 C

ATOM 3746 C TYR C 52 -41.266 80.332 48.560 1.00162.41 C

ANISOU 3746 C TYR C 52 19584 22512 19612 2222 1812 -2350 C

ATOM 3747 O TYR C 52 -40.939 81.275 49.259 1.00166.01 O

ANISOU 3747 O TYR C 52 20118 23015 19942 2254 1805 -2426 O

ATOM ^ 3748 N PRO C 53 -42.098 79.384 48.979 1.00152.58 N

ANISOU 3748 N PRO C 53 18273 21306 iδ396 2151 1973 -2310 N

ATOM 3749 CA PRO C 53 -42.757 79.447 50.278 1.00156.53 C

ANISOU 3749 CA PRO C 53 18794 21926 18755 2081 2174 -2342 C

ATOM 3750 CB PRO C 53 -43.227 78.018 50.479 1.00155.12 C

ANISOU 3750 CB " PRO C 53 18593 21749 18596 1969 2258 -2187 C

ATOM 3751 CG PRO C 53 -43.510 77.555 49.121 1.00157.65 C

ANISOU 3751 CG PRO C 53 18766 21960 19173 2027 2175 -2199 C

ATOM 3752 CD PRO C 53 -42.466 78.169 48.245 1.00154.91 C

ANISOU 3752 CD PRO C 53 18452 21534 18871 2131 1972 -2238 C

ATOM 3753 C PRO C 53 -41.841 79.882 51.421 1.00160.59 C

ANISOU 3753 C PRO C 53 19488 22512 19018 2064 2172 -2314 C

ATOM 3754 O PRO C 53 -42.321 80.516 52.361 1.00166.00 O

ANISOU 3754 O PRO C 53 20174 23301 19599 2070 2291 -2435 O

ATOM 3755 N GLY C 54 -40.553 79.571 51.348 1.00180.88 N

ANISOU 3755 N GLY C 54 22201 25030 21495 2052 2033 -2177 N

ATOM 3756 CA GLY C 54 ' -39.636 79.916 52.428 1.00187.24 C

ANISOU 3756 CA GLY C 54 23188 25876 22077 2048 2011 -2151 C

ATOM 3757 C GLY C 54 -39.751 81.323 53.003 1.00187.83 C

ANISOU 3757 C GLY C 54 23271 26003 22093 2144_ 2010 -2319 C

ATOM 3758 O GLY C 54 -39.560 81.551 54.201 ϊ.00187.24 O

ANISOU 3758 O GLY C 54 23328 25988 21826 2144 2040 -2324 O

ATOM ~ 3759 N ASP C 55 -40.062 82.273 52.135 1.00169.53 N

ANISOU 3759 N ASP C 55 20814 23652 19946 2229 1955 -2462 N

ATOM 3760 CA ASP C 55 -40.064 83.672 52.501 1.00172.39 C

ANISOU 3760 CA ASP C 55 21177 24038 20284 2331 1889 -2628 C

ATOM 3761 CB ASP C 55 -38.661 84.278 52.329 1.00176.70 C

ANISOU 3761 CB ASP C 55 21870 24518 20750 2384 1687 -2564 C

ATOM 3762 CG ASP C 55 -38.191 84.306 50.864 1.00176.14 C

ANISOU 3762 CG ASP c 55 21778 24331 20817 2387 1508 -2480 C ATOM 3763 ODl ASP C 55 -38.916 83.802 49.984 1.00173.44 O

ANISOU 3763 ODl ASP C 55 21317 23950 20631 2359 1532 -2465 O

ATOM 3764 0D2 ASP C 55 -37.091 84.838 50.592 1.00175.03 O

ANISOU 3764 0D2 ASP C 55 21737 24143 20625 2416. 1344 -2433 O

ATOM 3765 C ASP C 55 -41.073 84.383 51.621 1.00168.87 C

ANISOU 3765 C ASP C 55' 20561 23547 20056 2402 1839 ■ -2801 C

ATOM 3766 O ASP C 55 -40.965 85.578 51.368 1.00174.81 O

ANISOU 3766 O ASP C 55 21308 24263 20848 2494 1691 -2926 O

ATOM 3767 N GLY C 56 -42.053 83.636 51.143 1.00132.34 N

ANISOU 3767 N GLY C 56 15799 18905 15578 2360 1941 -2809 N

ATOM 3768 CA GLY C 56 -43.071 84.213 50.300 1.00138.80 C

ANISOU 3768 CA GLY C 56 16463 19656 16620 2428 1881 -2980 C

ATOM 3769 C GLY C 56 -42.586 84.990 49.081 1.00142.14 C

ANISOU 3769 C GLY C 56 16912 19942 17151 2494 1626 -2980 C

ATOM 3770 O GLY C 56 -43.365 85.742 48.503 1.00142.05 O

ANISOU 3770 O GLY C 56 16803 19853 17316 2555 1528 -3136 O

ATOM 3771 N SER C 57 -41.332 84.828 48.662 1.00146.46 N

ANISOU 3771 N SER C 57 17591 20457 17600 2473 1505 -2815 N

ATOM 3772 CA SER C 57 -40.897 85.497 47.424 1.00145.78 C

ANISOU 3772 CA SER C 57 17520 , 20259 17609 2505 1275 -2802 C

ATOM 3773 CB SER C 57 -39.356 85.503 47.245 1.00144.43 C

ANISOU 3773 CB SER C 57 17493 20084 17299 2474 1154 -2640 C

ATOM 3774 OG SER C 57 -38.711 84.338 47.736 1.00143.01 O

ANISOU 3774 OG SER C 57 17356 19942 17041 2406 1249 -2481 O

ATOM 3775 C SER C 57 -41.658 85.029 46.151 1.00145.29 C

ANISOU 3775 C SER C 57 17337 20107 17759 2498 1253 -2807 C

ATOM 3776 O SER C 57 -42.008 83.858 46.000 1.00139.79 O

ANISOU 3776 O SER C 57 16586 19421 17106 2454 1374 -2718 O

ATOM 3777 N THR C 58 -41.907 85.965 45.240 1.00171.86 N

ANISOU 3777 N THR C 58 20666 23371 21261 2545 1081 -2916 N

ATOM 3778 CA THR C 58 -42.824 85.736 44.129 1.00170.23 C

ANISOU 3778 CA THR C 58 20343 23064 21273 2558 1060 -2971 C

ATOM 3779 CB THR C 58 -44.223 86.296 44.486 1.00170.74 C

ANISOU 3779 CB THR C 58 20282 23124 21469 2611 1163 -3191 C

ATOM 3780 OGl THR C 58 -45.217 85.675 43.672 1.00174.78 O

ANISOU 3780 OGl THR C 58 20673 23580 22156 2606 1259 -3192 O

ATOM 3781 ' CG2 THR C 58 -44.285 87.820 44.313 1.00169.08 C

ANISOU 3781 CG2 THR C 58 20063 22818 21361 2681 955 -3395 C

ATOM 3782 C THR C 58 -42.331 86.334 42.797 1.00172.56 C

ANISOU 3782 C THR C 58 20665 23235 21664 2562 816 -2963 C

ATOM 3783 O THR C 58 -41.887 87.486 42.734 1.00169.90 O

ANISOU 3783 O THR C 58 20388 22849 21318 2584 633 -3043 O

ATOM 3784 N LYS C 59 -42.398 85.541 41.732 1.00159.71 N

ANISOU 3784 N LYS C 59 18999 21562 20121 2535 803 -2860 N

ATOM 3785 CA LYS C 59 -42.002 86.019 40.410 1.00155.43 C

ANISOU 3785 CA LYS C 59 18482 20917 19657 2520 591 -2839 C

ATOM 3786 CB LYS C 59 -40.562 85.622 40.090 1.00150.22 C

ANISOU 3786 CB LYS C 59 17905 20327 18846 2449 522 -2656 C

ATOM 3787 CG LYS C 59 -40.070 86.174 38.754 1.00149.60 C

ANISOU 3787 CG LYS C 59 17861 20174 18805 2406 307 -2628 C

ATOM 3788 CD LYS C 59 -38.596 85.841 38.483 1.00148.64 C

ANISOU 3788 CD LYS C 59 17797 20156 18523 2327 260 -2468 C

ATOM 3789 CE LYS C 59 -38.032 86.646 37.296 1.00146.98 C

ANISOU 3789 CE LYS C 59 17645 19906 18296 2252 41 -2438 C

ATOM 3790 NZ LYS C 59 -36.575 86.391 37.076 1.00140.74 N

ANISOU 3790 NZ LYS C 59 16891 19241 17341 2168 11 -2305 N

ATOM 3791 C LYS C 59 -42.928 85.479 39.329 1.00152.86 C

ANISOU 3791 C LYS C 59 18049 20481 19551 2551 593 -2887 C

ATOM 3792 O LYS C 59 -42.906 84.282 39.025 1.00144.32 O

ANISOU 3792 O LYS C 59 16897 19428 18511 2549 713 -2799 O

ATOM 3793 N TYR C 60 -43.730 86.365 38.743 1.00148.21 N

ANISOU 3793 N TYR C 60 17453 19752 19107 2584 433 -3032 N

ATOM 3794 CA TYR C 60 -44.728 85.960 37.755 1.00146.33 C

ANISOU 3794 CA TYR C 60 17125 19371 19101 2630 402 -3119 C

ATOM 3795 CB TYR C 60 -46.048 86.707 37.993 1.00142.55 C

ANISOU 3795 CB TYR C 60 16590 18779 18794 2701 358 -3372 C

ATOM 3796 CG TYR C 60 -46.610 86.558 39.391 1.00143.94 C

ANISOU 3796 CG TYR C 60 16686 19065 18941 2735 575 -3477 C

ATOM 3797 CDl TYR C 60 -46.385 87.523 40.352 1.00150.25 C

ANISOU 3797 CDl TYR C 60 17549 19977 19564 2724 583 -3501 C

ATOM 3798 CEl TYR C 60 -46.886 87.395 41.635 1.00154.10 C

ANISOU 3798 CEl TYR C 60 17965 20586 19999 2746 788 -3599 C

ATOM 3799 CZ TYR C 60 -47.632 86.291 41.973 1.00156.52 C

ANISOU 3799 CZ TYR C 60 18131 20908 20432 2763 994 -3669 C

ATOM 3800 OH TYR C 60 -48.125 86.168 43.260 1.00155.67 O

ANISOU 3800 OH TYR C 60 17953 20946 20250 2760 1209 -3764, O

ATOM 3801 CE2 TYR C 60 -47.876 85.315 41.029 1.00153.75 C ANISOU 3801 CE2 TYR C 60 17711 20433 20274 2777 984 -3642 C

ATOM 3802 CD2 TYR C 60 -47.363 85.451 39.749 1.00148.04 C

ANISOU 3802 CD2 TYR C 60 17063 19584 19602 2771 773 -3550 C

ATOM 3803 C TYR C 60 -44.249 86.187 36.320 1.00144.56 C

ANISOU 3803 C TYR C 60 16967 19056 18905 2588 188 -3045 C

ATOM 3804 O TYR C 60 -43.222 86.811 36.083 1.00141.13 O

ANISOU 3804 O TYR C 60 16642 18666 18315 2514 51 -2950 O

ATOM 3805 N ASN C 61 -44.999 85.670 35.360 1.00167.41 N

ANISOU 3805 N ASN C 61 19791 21823 21996 2632 161 -3093 N

ATOM 3806 CA ASN C 61 -44.713 85.919 33.958 1.00171.12 C

ANISOU 3806 CA ASN C 61 20314 22200 22502 2595 -29 -3035 C

ATOM 3807 CB ASN C 61 -45.227 84.753 33.119 1.00174.08 C

ANISOU 3807 CB ASN C 61 20580 22544 23020 2651 67 -2991 C

ATOM 3808 CG ASN C 61 -44.811 84.846 31.667 1.00178.67 ' C

ANISOU 3808 CG ASN C 61 . 21204 23036 23646 2625 -115 -2943 C

ATOM 3809 ODl ASN C 61 -45.134 83.971 30.861 1.00171.63 O

ANISOU 3809 ODl ASN C 61 20228 22097 22887 2686 -78 -2922 O

ATOM 3810 ND2 ASN C 61 -44.083 85.902 31.323 1.00183.00 N

ANISOU 3810 ND2 ASN C 61 21886 23564 24081 2531 -320 -2920 N

ATOM 3811 C ASN C 61 -45.387 87.210 33.515 1.00182.06 C

ANISOU 3811 C ASN C 61 21759 23385 24031 2608 -259 -3203 C

ATOM 3812 O ASN C 61 -46.507 87.499 33.930 1.00189.34 O

ANISOU 3812 O ASN C 61 22611 24193 25138 2691 -237 -3395 O

ATOM 3813 N GLU C 62 -44.712 87.989 32.677 1.00185.54 N

ANISOU 3813 N GLU C 62 22327 23781 24390 2518 -490 -3140 N

ATOM 3814 CA GLU C 62 -45.282 89.242 32.184 1.00196.44 C

ANISOU 3814 CA GLU C 62 23792 24952 25895 2510 -762 -3287 C

ATOM 3815 CB GLU C 62 -44.465 89.787 31.012 1.00201.74 C

ANISOU 3815 CB GLU C 62 . 24601 25588 26463 2381 -995 -3157 C

ATOM 3816 CG GLU C 62 -43.138 90.417 31.411 1.00213.81 C

ANISOU 3816 CG GLU C 62 26241 27253 27743 2255 -1085 -3025 C

ATOM 3817 CD GLU C 62 -43.305 91.765 32.092 1.00217.73 C

ANISOU 3817 CD GLU C 62 26800 27669 28260 2268 -1247 -3161 C

ATOM 3818 OEl GLU C 62 -44.462 92.220 32.241 1.00214.10 O

ANISOU 3818 OEl GLU C 62 26329 27013 28006 2341 -1379 -3364 O

ATOM 3819 0E2 GLU C 62 -42.275 92.365 32.475 1.00222.26 O

ANISOU 3819 0E2 GLU C 62 27427 28369 28651 2213 -1256 -3077 O

ATOM 3820 C GLU C 62 -46.739 89.079 31.766 1.00192.89 C

ANISOU 3820 C GLU C 62 23257 24296 25735 2622 -775 -3484 C

ATOM 3821 O GLU C 62 -47.601 89.852 32.185 1.00194.07 O

ANISOU 3821 O GLU C 62 23388 24325 26024 2683 -857 -3699 O

ATOM 3822 N LYS C 63 -47.005 88.064 30.948 1.00176.58 N

ANISOU 3822 N LYS C 63 21130 22193 23768 2658 -703 -3426 N

ATOM 3823 CA LYS C 63 -48.343 87.845 30.414 1.00177.58 C

ANISOU 3823 CA LYS C 63 21183 22105 24185 2767 -730 -3603 C

ATOM 3824 CB LYS C 63 -48.388 86.604 29.505 1.00179.90 C

ANISOU 3824 CB LYS C 63 21422 22382 24549 2802 -666 -3490 C

ATOM 3825 CG LYS C 63 -49.613 86.554 28.569 1.00187.21 C

ANISOU 3825 CG LYS C 63 22309 23038 25783 2908 -766 -3662 C

ATOM 3826 CD LYS C 63 -49.745 85.222 27.816 1.00184.57 C

ANISOU 3826 CD LYS C 63 21875 22706 25547 2983 -649 -3566 C

ATOM 3827 CE LYS C 63 -50.774 85.290 26.672 1.00190.83 C

ANISOU 3827 CE LYS C 63 22645 23206 26654 3095 -773 -3739 C

ATOM 3828 NZ LYS C 63 -52.199 85.411 27.110 1.00195.73 N

ANISOU 3828 NZ LYS C 63 23159 23698 27511 3194 -703 -3986 N

ATOM 3829 C LYS C 63 -49.387 87.724 31.519 1.00179.86 C

ANISOU 3829 C LYS C 63 21322 22399 24616 2873 -534 -3783 C

ATOM 3830 O LYS C 63 -50.573 87.944 31.276 1.00188.14 O

ANISOU 3830 O LYS C 63 22294 23267 25922 2967 -556 -3974 O

ATOM 3831 N PHE C 64 -48.952 87.389 32.731 1.00174.61 N

ANISOU 3831 N PHE C 64 20617 21942 23784 2852 -344 -3731 N

ATOM 3832 CA PHE C 64 -49.894 87.066 33.805 1.00178.86 C

ANISOU 3832 CA PHE C 64 21009 22528 24423 2929 -127 -3884 C

ATOM 3833 CB PHE C 64 -49.670 85.637 34.312 1.00168.20 C

ANISOU 3833 CB PHE C 64 19559 21353 22995 2928 163 -3715 C

ATOM 3834 CG PHE C 64 -50.047 84.570 33.320 1.00166.47 C

ANISOU 3834 CG PHE C 64 19260 21037 22954 2984 201 -3662 C

ATOM 3835 CDl PHE C 64 -50.677 83.411 33.734 1.00168.76 C

ANISOU 3835 CDl PHE C 64 19392 21316 23413 3052 400 -3731 C

ATOM 3836 CEl PHE C 64 -51.026 82.426 32.821 1.00164.40 C

ANISOU 3836 CEl PHE C 64 18762 20662 23042 3117 418 -3682 C

ATOM 3837 CZ PHE C 64 -50.752 82.597 31.484 1.00163.89 C

ANISOU 3837 CZ PHE C 64 18776 20517 22979 3118 242 -3574 C

ATOM 3838 CE2 PHE C 64 -50.125 83.749 31.057 1.00165.89 C

ANISOU 3838 CE2 PHE C 64 19187 20799 23045 3034 57 -3506 C

ATOM 3839 CD2 PHE C 64 -49.775 84.727 31.972 1.00165.88 C

ANISOU 3839 CD2 PHE C 64 19264 20887 22876 2965 34 -3546 C ATOM 3840 C PHE C 64 -49.875 88.029 34.985 1.00188.66 C

ANISOU 3840 C PHE C 64 22263 23851 25568 2922 -132 -4018 C

ATOM 3841 O PHE C 64 -50.648 87.851 35.923 1.00191.73 O

ANISOU 3841 O PHE C 64 22531 24329 25988 2967 71 -4135 O

ATOM 3842 N LYS C 65 -49.004 89.037 34.934 1.00212.11 N

ANISOU 3842 N LYS C 65 25376 26797 28421 2864 -370 -4002 N

ATOM 3843 CA LYS C 65 -48.844 89.998 36.034 1.00215.86 C

ANISOU 3843 CA LYS C 65 25872 27346 28798 2867 -419 -4121 C

ATOM 3844 CB LYS C 65 -48.495 91.394 35.492 1.00218.46 C

ANISOU 3844 CB LYS C 65 26336 27506 29161 2837 -795 '-4212 C

ATOM 3845 CG LYS C 65 -47.008 91.785 35.595 1.00229.88 C

ANISOU 3845 CG LYS C 65 27941 29045 30357 2724 -926 -3989 C

ATOM 3846 CD LYS C 65 -46.809 93.311 35.476 1.00246.38 C

ANISOU 3846 CD LYS C 65 30141 31002 32470 2704 -1284 -4117 C

ATOM 3847 CE LYS C 65 -45.408 93.758 35.911 1.00246.95 C

ANISOU 3847 CE LYS C 65 30334 31209 32288 2613 -1363 -3932 C

ATOM 3848 NZ LYS C 65 -45.210 95.232 35.767 1.00236.83 N

ANISOU 3848 NZ LYS C 65 29146 29797 31041 2604 -1725 -4065 N

ATOM 3849 C LYS C 65 -50.055 90.085 36.974 1.00220.13 C

ANISOU 3849 C LYS C 65 26254 27925 29459 2959 -251 -4373 C

ATOM 3850 O LYS C 65 -49.913 90.026 38.205 1.00218.92 O

ANISOU 3850 O LYS C 65 26054 27973 29154 2955 -41 -4351 O

ATOM 3851 N GLY C 66 -51.240 90.227 36.382 1.00156.66 N

ANISOU 3851 N GLY C 66 18136 19696 21693 3035 -350 -4622 N

ATOM 3852 CA GLY C 66 -52.472 90.315 37.143 1.00155.73 C

ANISOU 3852 CA GLY C 66 17846 19611 21714 3118 -206 -4902 C

ATOM 3853 C GLY C 66 -53.462 89.222 36.802 1.00155.45 C

ANISOU 3853 C GLY C 66 17665 19514 21886 3166 -12 -4950 C

ATOM 3854 O GLY C 66 -54.364 88.921 37.583 1.00160.78 O

ANISOU 3854 O GLY C 66 18174 20274 22642 3208 203 -5120 O

ATOM 3855 N LYS C 67 -53.300 88.632 35.627 1.00192.84 N

ANISOU 3855 N LYS C 67 22459 24106 26707 3157 -92 -4802 N

ATOM 3856 CA LYS C 67 -54.152 87.533 35.204 1.00197.30 C

ANISOU 3856 CA LYS C 67 22896 24594 27476 3211 67 -4815 C

ATOM 3857 CB LYS C 67 -53.588 86.905 33.930 1.00192.23 C

ANISOU 3857 CB LYS C 67 22352 23851 26837 3188 -31 -4580 C

ATOM 3858 CG LYS C 67 -53.703 87.767 32.665 1.00191.82 C

ANISOU 3858 CG LYS C 67 22438 23547 26897 3194 -390 -4662 C

ATOM 3859 CD LYS C 67 -54.545 87.070 31.592 1.00195.22 C

ANISOU 3859 CD LYS C 67 22818 23740 27616 3279 -448 -4745 C

ATOM 3860 CE LYS C 67 -53.956 87.262 30.190 1.00198.79 C

ANISOU 3860 CE LYS C 67 23445 24042 28043 3235 -712 -4604 C

ATOM 3861 NZ LYS C 67 -54.495 86.295 29.179 1.00195.27 N

ANISOU 3861 NZ LYS C 67 22949 23455 27789 3309 -684 -4559 N

ATOM 3862 C LYS C 67 -54.271 86.488 36.322 1.00199.03 C

ANISOU 3862 C LYS C 67 22978 25046 27597 3189 433 -4728 C

ATOM 3863 O LYS C 67 -55.280 85.787 36.426 1.00204.36 O

ANISOU 3863 O LYS C 67 23497 25692 28459 3236 602 -4827 O

ATOM 3864 N ALA C 68 -53.234 86.396 37.153 1.00197.77 N

ANISOU 3864 N ALA C 68 22885 25110 27147 3111 545 -4539 N

ATOM 3865 CA ALA C 68 -53.260 85.552 38.350 1.00201.40 C

ANISOU 3865 CA ALA C 68 23245 25796 27480 3070 864 -4472 C

ATOM 3866 CB ALA C 68 -52.925 84.112 37.999 1.00192.93 C

ANISOU 3866 CB ALA C 68 22146 24765 26394 3038 1021 -4212 C

ATOM 3867 C ALA C 68 -52.303 86.086 39.424 1.00198.11 C

ANISOU 3867 C ALA C 68 22919 25585 26768 3008 905 -4396. C

ATOM 3868 O ALA C 68 -51.656 87.117 39.226 1.00194.60 O

ANISOU 3868 O ALA C 68 22603 25105 26233 3003 683 -4401 O

ATOM 3869 N THR C 69 -52.238 85.392 40.561 1.00185.30 N

ANISOU 3869 N THR C 69 21236 24169 25001 2957 1180 -4322 N

ATOM 3870 CA THR C 69 -51.286 85.695 41.642 1.00180.03 C

ANISOU 3870 CA THR C 69 20657 23699 24048 2901 1246 -4237 C

ATOM 3871 CB THR C 69 -51.602 87.038 42.402 1.00187.70 C

ANISOU 3871 CB THR C 69 21592 24716 25009 2950 1182 -4524 C

ATOM 3872 OGl THR C 69 , -53.012 87.174 42.625 1.00199.05 O

ANISOU 3872 OGl THR C 69 22845 26107 26677 3006 1259 -4812 O

ATOM 3873' CG2 THR C 69 -51.082 88.270 41.632 1.00182.67 C

ANISOU 3873 CG2 THR C 69 21081 23932 24394 2992 834 -4587 C

ATOM 3874 C THR C 69 -51.220 84.509 42.622 1.00176.57 C

ANISOU 3874 C THR C 69 20177 23449 23462 2820 1543 '-4067 C

ATOM 3875 O THR C 69 -52.233 83.850 42.863 1.00177.51 O

ANISOU 3875 O THR C 69 20154 23585 23707 2812 1727 -4127 O

ATOM 3876 N LEU C 70 -50.035 84.230 43.176 1.00160.54 N

ANISOU 3876 N LEU C 70 18279 21548 21171 2754 1573 -3852 N

ATOM 3877 CA LEU C 70 -49.835 83.011 43.979 1.00163.21 C

ANISOU 3877 CA LEU C 70 18621 22031 21359 2663 1797 -3645 C

ATOM 3878 CB LEU C 70 -48.776 82.078 43.363 1.00157.73 C ANISOU 3878 CB LEU C 70 18044 21309 20579 2625 1708 -3363 C

ATOM 3879 CG LEU C 70 -48.151 82.297 41.989 1.00151.05 C

ANISOU 3879 CG LEU C 70 17229 20296 19866 2672 1486 -3303 C

ATOM 3880 CDl LEU C 70 -46.906 81.444 41.886 1.00141.65 C

ANISOU 3880 CDl LEU C 70 16163 19163 18496 2619 1421 -3060 C

ATOM 3881 CD2 LEU C 70 -49.122 81.983 40.876 1.00153.88 C

ANISOU 3881 CD2 LEU C 70 17458 20526 20484 2716 1506 -3328 C

ATOM 3882 C LEU C 70 -49.450 83.224 45.444 1.00161.22 C

ANISOU 3882 C LEU C 70 18419 21981 20856 2607 1944 -3652 C

ATOM 3883 O LEU C 70 -48.893 84.262 45.818 1.00152.46 O

ANISOU 3883 O LEU C 70 17391 20905 19631 2641 1834 -3733 O

ATOM 3884 N THR C 71 -49.722 82.189 46.243 1.00198.64 N

ANISOU 3884 N THR C 71 23114 26848 25512 2518 2182 -3559 N

ATOM 3885 CA THR C 71 -49.348 82.136 47.652 1.00204.87 C

ANISOU 3885 CA THR C 71 23971 27836 26033 2439 2342 -3517 C

ATOM 1 3886 CB THR C 71 -50.462 82.668 48.558 1.00213.37 C

ANISOU 3886 CB THR C 71 24915 29046 27109 2445 2503 -3791 C

ATOM 3887 OGl THR C 71 -51.739 82.321 48.006 1.00208.89 O

ANISOU 3887 OGl THR C 71 24155 28424 26789 2453 2600 -3932 O

ATOM 3888 CG2 THR C 71 -50.356 84.166 48.693 1.00221.26 C

ANISOU 3888 CG2 THR C 71 25932 30025 28112 2557 2324 -4020 C

ATOM 3889 C THR C 71 -49.051 80.726 48.136 1.00200.94 C

ANISOU 3889 C THR C 71 23512 27421 25414 2312 2507 -3273 C

ATOM 3890 O THR C 71 -49.097 79.756 47.375 1.00195.28 O

ANISOU 3890 O THR C 71 22743 26617 24838 2289 2508 -3149 O

ATOM 3891 N ALA C 72 -48.757 80.645 49.429 1.00181.28 N

ANISOU 3891 N ALA C 72 21121 25095 22664 2231 2626 -3209 N

ATOM 3892 CA ALA C 72 -48.557 79.389 50.136 1.00189.13 C

ANISOU 3892 CA ALA C 72 22172 26180 23509 2086 2780 -2995 C

ATOM 3893 CB ALA c ' 72 -47.251 78.726 49.712 1.00180.93 C

ANISOU 3893 CB ALA C 72 21288 25055 22404 2067 2623 -2738 C

ATOM 3894 C ALA C 72 -48.541 79.698 51.629 1.00202.93 C

ANISOU 3894 C ALA C 72 23987 28126 24990 2014 2939 -3044 C

ATOM 3895 O ALA C 72 -48.078 80.762 52.042 1.00196.93 O

ANISOU 3895 O ALA C 72 23295 27405 24125 2090 2864 -3159 O

ATOM 3896 N ASP C 73 -49.070 78.784 52.435 1.00223.72 N

ANISOU 3896 N ASP C 73 26601 30886 27516 1863 3152 -2958 N

ATOM 3897 CA ASP C 73 -49.017 78.925 53.885 1.00223.19 C

ANISOU 3897 CA ASP C 73 26610 31024 27167 1767 3322 -2982 C

ATOM 3898 CB ASP C 73 -50.396 78.752 54.521 1.00229.62 C

ANISOU 3898 CB ASP C 73 27236 32010 27999 1688 3580 -3167 C

ATOM 3899 CG ASP C 73 -51.034 80.073 54.892 1.00245.01 C

ANISOU 3899 CG ASP C 73 29074 34058 29960 1809- 3599 -3503 C

ATOM 3900 ODl ASP C 73 -50.315 81.097 54.913 1.00238.82 O

ANISOU 3900 ODl ASP C 73 28358 33182 29200 1958 3390 -3581 O

ATOM 3901 OD2 ASP C 73 -52.251 80.087 55.170 1.00260.83 O

ANISOU 3901 OD2 ASP C 73 30915 36235 31952 1749 3812 -3695 O

ATOM 3902 C ASP C 73 -48.058 77.901 54.442 1.00213.97 C

ANISOU 3902 C ASP C 73 25636 29873 25788 1622 3333 -2689 C

ATOM 3903 O ASP C 73 -48.308 76.703 54.371 1.00208.86 O

ANISOU 3903 O ASP C 73 24967 29207 25183 1498 3397 -2525 O

ATOM 3904 N LYS C 74 -46.951 78.383 54.987 1:00197.68 , N

ANISOU 3904 N LYS C 74 23767 27831 23511 1644 3246 -2631 N

ATOM 3905 CA LYS C 74 -45.916 77.503 55.496 1.00197.19 C

ANISOU 3905 CA LYS C 74 23919 27746 23259 1530 3195 -2370 C

ATOM 3906 CB LYS C 74 -44.856 78.311 56.240 1.00187.04 C

ANISOU 3906 CB LYS C 74 22826 26484 21755 1591 3105 -2378 C

ATOM 3907 CG LYS C 74 -44.305 79.457 55.423 1.00177.65 C

ANISOU 3907 CG LYS C 74 21610 25188 20700 1785 2908 -2507 C

ATOM 3908 CD LYS C 74 -43.125 80.095 56.102 1.00177.61 C

ANISOU 3908 CD LYS C 74 21795 25186 20501 1849 2796 -2497 C

ATOM 3909 CE LYS C 74 -42.637 81.286 55.307 1.00177.46 C

ANISOU 3909 CE LYS C 74 21728 25078 20619 2026 2607 -2642 C

ATOM 3910 NZ LYS C 74 -41.675 82.119 56.083 1.00180.95 N

ANISOU 3 ' 910 NZ LYS C 74 22316 25548 20888 2106 2518 -2687 N

ATOM 3911 C LYS C 74 -46.502 76.420 56.391 1.00204.27 C

ANISOU 3911 C LYS C 74 24834 28764 24015 1315 3396 -2242 C

ATOM 3912 O LYS C 74 -46.158 75.246 56.256 1.00203.46 O

ANISOU 3912 O LYS C 74 24782 28576 23949 1210 3341 -2029 O

ATOM 3913 N SER C 75 -47.398 -76.823 57.289 1.00188.78 N

ANISOU 3913 N SER C 75 22826 27007 21893 1245 3618 -2378 N

ATOM 3914 CA SER C 75 -48.046 75.907, 58.227 1.00189.75 C

ANISOU 3914 CA SER C 75 22956 27285 21856 1014 3838 -2275 C

ATOM 3915 CB SER C 75 -48.924 76.692 59.190 1.00196.70 C

ANISOU 3915 CB SER C 75 23704 28413 22619 987 4088 -2522 C

ATOM 3916 OG SER C 75 -50.146 77.044 58.556 1.00195.38 O

ANISOU 3916 OG SER C 75 23267 28242 22726 1097 4137 -2763 O ATOM 3917 C SER C 75 -48.942 74.929 57.493 1.00188.29 C

ANISOU 3917 C SER C 75 22614 27021 21906 941 3866 -2191 C

ATOM 3918 O SER C 75 -49.119 73.784 57.909 1.00180.57 O

ANISOU 3918 O SER C 75 21711 26029 20869 759 3885 -1962 O

ATOM 3919 N SER C 76 -49.518 75.404 56.398 1.00239.91 N

ANISOU 3919 N SER C 76 28937 33495 28722 1092 3848 -2386 N

ATOM 3920 CA SER C 76 -50.506 74.640 55.665 1.00242.54 C

ANISOU 3920 CA SER C 76 29078 33752 29325 1069 3884 -2377 C

ATOM 3921 CB SER C 76 -51.422 75.602 54.900 1.00239.77 C

ANISOU 3921 CB SER C 76 28508 33361 29234 1257 3878 -2680 C

ATOM 3922 OG SER C 76 -52.743 75.104 54.798 1.00247.68 O

ANISOU 3922 OG SER C 76 29286 34373 30448 1208 4019 -2762 O

ATOM 3923 C SER C 76 -49.844 73.639 54.712 1.00238.55 C

ANISOU 3923 C SER C 76 28649 33029 28959 1079 3661 -2130 C

ATOM 3924 O SER C 76 -50.506 72.738 54.198 1.00240.26 O

ANISOU 3924 O SER C 76 28765 33190 29334 1000 3683 -2024 O

ATOM 3925 N SER C 77 -48.536 73.784 54.502 1.00203.17 N

ANISOU 3925 N SER C 77 24339 28437 24418 1175 3442 -2046 N

ATOM 3926 CA SER C 77 -47.823 73.020 53.470 1.00196.06 C

ANISOU 3926 CA SER C 77 23473 27337 23682 1238 3200 -1885 C

ATOM 3927 CB SER C 77 -47.274 71.695 54.013 1.00195.17 C

ANISOU 3927 CB SER C 77 23542 27194 23420 1076 3114 -1611 C

ATOM 3928 OG SER C 77 -47.819 71.403 55.287 1.00204.04 O

ANISOU 3928 OG SER C 77 24589 28347 24590 908 3223 -1492 O

ATOM 3929 C SER C 77 -48.684 72.824 52.219 1.00190.40 - C

ANISOU 3929 C SER C 77 22532 26514 23299 1318 3185 -1952 C

ATOM 3930 O SER C 77 -48.899 71.707 51.741 1.00180.17 O

ANISOU 3930 O SER C 77 21183 25147 22125 1244 3154 -1800 O

ATOM 3931 N THR C 78 -49.154 73.955 51.702 1.00185.32 N

ANISOU 3931 N THR C 78 21762 25850 22803 1475 3190 -2188 N

ATOM 3932 CA THR C 78 -50.065 74.017 50.572 1.00180.25 C

ANISOU 3932 CA THR C 78 20907 25103 22475. 1570 ^ 3186 -2309 C

ATOM 3933 CB THR C 78 -51.544 74.100 51.040 1.00187.80 C

ANISOU 3933 CB THR C 78 21685 26183 23488 1474 3448 -2442 C

ATOM 3934 OGl THR C 78 -51.873 72.966 51.856 1.00187.29 O

ANISOU 3934 OGl THR C 78 21655 26192 23314 1269 3558 -2227 O

ATOM 3935 CG2 THR C 78 -52.491 74.151 49. ' 856 1.00180.59 C

ANISOU 3935 CG2 THR C 78 20554 25138 22923 1596 3428 -2602 C

ATOM 3936 C THR C 78 -49.730 75.263 49.753 1.00171.37 C

ANISOU 3936 C THR C 78 19749 23890 21473 1765 3050 -2510 C

ATOM 3937 O THR C 78 -49.252 76.266 50.290 1.00168.57 O

ANISOU 3937 O THR C 78 19455 23616 20978 1807 3063 -2646 O

ATOM 3938 N ALA C 79 -49.977 75.184 48.450 1.00150.79 N

ANISOU 3938 N ALA C 79 17053 21112 19127 1878 2903 -2521 N

ATOM 3939 CA ALA C 79 -49.672 76.272 47.524 1.00148.92 C

ANISOU 3939 CA ALA C 79 16814 20764 19006 2041 2729 -2662 C

ATOM 3940 CB ALA C 79 -48.629 75.829 46.530 1.00144.84 C

ANISOU 3940 CB ALA C 79 16378 20123 18533 2094 2508 -2494 C

ATOM 3941 C ALA C 79 -50.928 76.670 46.787 1.00150.22 C

ANISOU 3941 C ALA C 79 16786 20837 19454 2131 2755 -2874 C

ATOM 3942 O ALA C 79 -51.539 75.847 46.119 1.00147.12 O

ANISOU 3942 O ALA C 79 16283 20349 19266 2137 2759 -2822 O

ATOM 3943 N TYR C 80 -51.325 77.927 46.905 1.00185.35 N

ANISOU 3943 N TYR C 80 21197 25300 23927 2210 2750 -3122 N

ATOM 3944 CA TYR C 80 -52.570 78.344 46.289 1.00187.41 C

ANISOU 3944 CA TYR C 80 21276 25472 24460 2296 2768 -3372 C

ATOM 3945 CB TYR C 80 -53.440 79.129 47.289 1.00198.52 C

ANISOU 3945 CB TYR C 80 22583 27039 25807 2269 2950 -3631 C

ATOM 3946 CG TYR C 80 -53.840 78.331 48.521 1.00198.18 C

ANISOU 3946 CG TYR C 80 22509 27213 25579 2097 3226 -3556 C

ATOM 3947 CDl TYR C 80 -53.572 78.799 49.800 1.00197.43 C

ANISOU 3947 CDl TYR C 80 22513 27320 25182 2021 3330 -3559 C

ATOM 3948 CEl TYR C 80 -53.932 78.064 50.924 1.00203.54 C

ANISOU 3948 CEl TYR C 80 23274 28299 25764 1845 3580 -3483 C

ATOM 3949 CZ TYR C 80 -54.557 76.843 50.771 1.00204.82 C

ANISOU 3949 CZ TYR C 80 23316 28463 26042 1735 3725 -3396 C

ATOM 3950 OH TYR C 80 -54.913 76.099 51.870 1.00202.01 O

ANISOU 3950 OH TYR C 80 22957 28314 25485 1533 3965 -3304 O

ATOM 3951 CE2 TYR C 80 -54.830 76.359 49.515 1.00202.46 C

ANISOU 3951 CE2 TYR C 80 22906 27959 26060 1821 3622 -3394 C

ATOM 3952 CD2 TYR C 80 -54.471 77.100 48.399 1.00198.99 C

ANISOU 3952 CD2 TYR C 80 22485 27316 25806 2006 3376 -3479 C

ATOM 3953 C TYR C 80 -52.261 79.165 45.055 1.00180.38 C

ANISOU 3953 C TYR C 80 20417 24399 23722 2443 2513 -3475 C

ATOM 3954 O TYR C 80 -51.153 79.679 44.918 1.00176.37 O

ANISOU 3954 O TYR C 80 20051 23897 23066 2471 2370 -3439 O

ATOM 3955 N MET C 81 -53.227 79.254 44.147 1.00177.15 N ANISOU 3955 N MET C 81 19882 23821 23606 2530 2448 -3595 N

ATOM 3956 CA MET C 81 -53.130 80.173 43.021 1.00183.90 C

ANISOU 3956 CA MET C 81 20766 24493 24614 2655 2202 -3719 C

ATOM 3957 CB MET C 81 -52.696 79.451 41.749 1.00181.49 C

ANISOU 3957 CB MET C 81 20491 24025 24441 2702 2047 -3543 C

ATOM 3958 CG MET C 81 -52.422 80.429 40.618 1.00187.81 C

ANISOU 3958 CG MET C 81 21348 24643 25370 2807 1784 -3650 C

ATOM 3959 SD MET C 81 -51.796 79.679 39.116 1.00176.76 S

ANISOO 3959 SD MET C 81 19989 23082 24091 2860 1596 -3457 S

ATOM 3960 CE MET C 81 -53.261 78.822 38.559 1.00183.43 C

ANISOU 3960 CE MET C 81 20636 23806 25252 2914 1710 -3521 C

ATOM 3961 C MET C 81 -54.441 80.908 42.757 1.00195.55 C

ANISOU 3961 C MET C 81 22089 25873 26339 2737 2200 -4044 C

ATOM 3962 O MET C 81 -55.471 80.280 42.536 1.00197.29 O

ANISOU 3962 O MET C 81 22167 26006 26788 2759 2275 -4102 , O

ATOM 3963 N HIS C 82 -54.388 82.237 42.759 1.00262.19 N

ANISOU 3963 N HIS C 82 30555 34316 34748 2789 2094 -4264 N

ATOM 3964 CA HIS C 82 -55.565 83.067 42.510 1.00272.30 C

ANISOU 3964 CA HIS C 82 31693 35497 36270 2876 2046 -4616 C

ATOM 3965 CB HIS C 82 -55.412 84.406 43.240 1.00282.10 C

ANISOU 3965 CB HIS C 82 32954 36854 37377 2895 2000 -4836 C

ATOM 3966 CG HIS C 82 -56.699 84.979 43.754 1.00299.03 C

ANISOU 3966 CG HIS C 82 34907 38998 39713 2954 2043 -5228 C

ATOM 3967 NDl HIS C 82 -56.991 85.062 45.099 1.00309.73 N

ANISOU 3967 NDl HIS C 82 36135 40596 40954 2896 2291 -5380 N

ATOM 3968 CEl HIS C 82 -58.182 85.614 45.257 1.00315.37 C

ANISOU 3968 CEl HIS C 82 36672 41263 41891 2973 2264 -5761 .. C

ATOM 3969 NE2 HIS C 82 -58.671 85.895 44.063 1.00316.34 N

ANISOU 3969 NE2 HIS C 82 36820 41099 42275 3079 1991 -5855 N

ATOM 3970 CD2 HIS C 82 -57.763 85.511 43.105 1.00305.08 C

ANISOU 3970 CD2 HIS C 82 35586 39554 40776 3065 1855 -5519 C

ATOM 3971 C HIS C 82 -55.735 83.311 41.007 1.00273.20 C

ANISOU 3971 C HIS C 82 31837 35328 36637 2984 1773 -4677 C

ATOM 3972 O HIS C 82 -54.756 83.316 40.260 1.00268.02 O

ANISOU 3972 O HIS C 82 31343 34594 35900 2995 1565 -4529 O

ATOM 3973 N LEU C 83 -56.975 83.510 40.566 1.00215.92 N

ANISOU 3973 N LEU C 83 24432 27922 29686 3055 1771 -4896 N

ATOM 3974 CA LEU C 83 -57.251 83.813 39.160 1.00220.05 C

ANISOU 3974 CA LEU C 83 24988 28155 30465 3159 1505 -4976 C

ATOM 3975 CB LEU C 83 -57.691 82.555 38.405 1.00220.86 ,C

ANISOU 3975 CB LEU C 83 25008 28131 30779 3187 1573 -4858 C

ATOM 3976 CG LEU C 83 -56.551 81.666 37.898 1.00212.68 C

ANISOU 3976 CG LEU C 83 24100 27094 29614 3154 1523 -4496 C

ATOM 3977 CDl LEU C 83 -57.056 80.292 37.490 1.00199.62 C

ANISOU 3977 CDl LEU C 83 22340 25336 28169 3190 1595 -4385 C

ATOM 3978 CD2 LEU C 83 -55.832v 82.341 36.740 1.00210.22 C

ANISOU 3978 CD2 LEU C 83 23962 26640 29272 3194 1219 -4459 C

ATOM 3979 C LEU C 83 -58.282 84.937 39.010 1.00230.25 C

ANISOU 3979 C LEU C 83 26205 29306 31973 3252 1343 -5375 C

ATOM 3980 O ' LEU C 83 -59.477 84.682 38.852 1.00231.05 O

ANISOU 3980 O LEU C 83 26134 29321 32333 3305 1413 -5612 O

ATOM 3981 N SER C 84 -57.787 86.176 39.041 1.00236.91 N

ANISOU 3981 N SER C 84 27178 30117 32720 3270 1104 -5451 N

ATOM 3982 CA SER C 84 -58.608 87.393 39.123 1.00242.90 C

ANISOU 3982 CA SER C 84 27883 30768 33640 3350 907 -5837 C

ATOM 3983 CB SER C 84 -57.705 88.630 39.210 1.00233.66 C

ANISOU 3983 CB SER C 84 26890 29603 32286 3340 647 -5811 C

ATOM 3984 OG SER ' C 84 -56.571 88.391 40.024 1.00222.45 O

ANISOU 3984 OG SER C 84 25513 28462 30544 3262 827 -5639 O

ATOM 3985 C SER C 84 -59.559 87.584 37.951 1.00240.97 C

ANISOU 3985 C SER C 84 27593 30205 33761 3452 697 -6059 C

ATOM 3986 O SER C 84 -60.784 87.553 38.103 1.00237.91 O

ANISOU 3986 O SER C 84 27020 29767 33608 3513 764 -6372 O

ATOM 3987 N SER C 85 -58.969 87.823 36.786 1.00262.13 N

ANISOU 3987 N SER C 85 30443 32671 36482 3467 436 -5908 N

ATOM 3988 CA SER C 85 -59.722 88.006 35.558 1.00274.34 C

ANISOU 3988 CA SER C 85 31990 33888 38359 3560 202 -6087 C

ATOM 3989 CB SER C 85 -58.856 88.729 34.519 1.00267.48 C

ANISOU 3989 CB SER C 85 31351 32824 37455 3552 -187 -6026 C

ATOM 3990- OG SER C 85 -59.516 88.837 33.268 1.00261.84 O

ANISOU 3990 OG SER C 85 30677 31782 37027 3626 -417 -6132 . O

ATOM 3991 C SER C 85 -60.187 86.656 35.015 1.00279.65 C

ANISOU 3991 C SER C 85 32600 34478 39177 .3584 356 -5918 C

ATOM 3992 o SER C 85 -59.754 85.601 35.485 1.00274.90 O

ANISOU 3992 O SER C 85 31967 34074 38409 3520 616 -5645 O

ATOM 3993 N LEU C 86 -61.080 86.701 34.033 1.00242.91 N

ANISOU 3993 N LEU C 86 27929 29522 34845 3682 174 -6094 N ATOM 3994 CA LEU C 86 -61.488 85.512 33.302 1.00239.71 C

ANISOϋ 3994 CA LEU C 86 27490 28981 34609 3730 239 -5942 C

ATOM 3995 CB LEU C 86 -62.542 84.723 34.087 1.00235.33 C

ANISOϋ 3995 CB LEU C 86 26694 28539 34182 3745 577 -6004 C

ATOM 3996 CG LEU C 86 -61.997 83.898 35.259 1.00236.64 C

ANISOϋ 3996 CG LEU C 86 26803 29054 34055 3628 911 -5744 C

ATOM 3997 CDl LEU C 86 -63.111 83.307 36.089 1.00226.17 C

ANISOϋ 3997 CDl LEU C 86 25236 27837 32863 3618 1220 -5858 C

ATOM 3998 CD2 LEU C 86 -61.072 82.805 34.760 1.00241.04 C

ANISOU 3998 CD2 LEU C 86 27485 29660 34439 3585 919 -5335 C

ATOM 3999 C LEU C 86 -61.983 85.925 31.911 1.00242.14 C

ANISOU 3999 C LEU C 86 27877 28906 35218 3834 -93 -6123 C

ATOM 4000 O LEU C 86 -62.655 86.952 31.767 1.00239.70 O

ANISOϋ 4000 O LEU C 86 27512 28424 35140 3904 -248 -6488 O

ATOM 4001 N THR C 87 -61.622 85.139 30.892 1.00249.52 N

ANISOU 4001 N THR C 87 28947 29713 36145 3843 -215 -5879 ( N

ATOM 4002 CA THR C 87 -61.956 85.448 29.495 1.00242.86 C

ANISOU 4002 CA THR C 87 28220 28507 35548 3927 -545 -6003 C

ATOM 4003 CB THR C 87 -60.953 86.474 28.879 1.00236.41 C

ANISOϋ 4003 CB THR C 87 27666 27652 34508 3843 -814 -5781 C

ATOM 4004 OGl THR C 87 -60.942 87.682 29.653 1.00233.55 O

ANISOU 4004 OGl THR C 87 27396 27387 33957 3758 -946 -5856 O

ATOM 4005 CG2 THR C 87 -61.329 86.804 27.442 1.00224.84 C

ANISOU 4005 CG2 THR C 87 26335 25814 33280 3914 -1146 -5884 C

ATOM 4006 C THR C 87 -62.028 84.196 28.599 1.00232.94 C

ANISOϋ 4006 C ' THR C 87 26876 27073 34556 4037 -480 -5963 C

ATOM 4007 O THR C 87 -62.244 83.071 29.068 1.00222.57 O

ANISOU 4007 O THR C 87 25434 25927 33206 4036 -200 -5776 O

ATOM 4008 N SER C 91 -60.791 78.758 29.238 1.00198.34 N

ANISOU 4008 N SER C 91 22079 23449 29832 3991 544 -4702 N

ATOM 4009 CA SER C 91 -61.499 77.619 29.823 1.00207.85 ^ C

ANISOU 4009 CA SER C 91 23074 24727 31172 3997 799 -4701 C

ATOM 4010 CB SER C 91 -62.810 77.400 29.068 1.00201.60 C

ANISOU 4010 CB SER C 91 22159 23631 30807 4150 742 -4932 C

ATOM 4011 OG SER C 91 -63.399 78.653 28.751 1.00195.28 O

ANISOU 4011 OG SER C 91 21424 22621 30152 4201 555 -5246 O

ATOM 4012 C SER C 91 -60.648 76.332 29.848 1.00200.37 C

ANISOU 4012 C SER C 91 22096 23957 30077 3958 911 -4359 C

ATOM 4013 O SER C 91 -60.972 75.356 29.168 1.00192.05 O

ANISOϋ 4013 O SER C 91 20962 22777 29233 4061 880 -4278 O

ATOM 4014 N ALA C 92 -59.594 76.330 30.673 1.00183.35 N

ANISOU 4014 N ALA C 92 19999 22085 27580 3817 1026 -4176 N

ATOM 4015 CA ALA C 92 -58.504 75.342 30.589 1.00169.73 C

ANISOU 4015 CA ALA C 92 18304 20513 25672 3779 1037 -3859 C

ATOM 4016 CB ALA C 92 -57.257 76.012 30.012 1.00163.68 C

ANISOϋ 4016 CB ALA C 92 17729 19802 24660 3748 852 -3753 C

ATOM 4017 C ALA C 92 -58.134 74.575 31.882 1.00162.36 C

ANISOU 4017 C ALA C 92 17308 19843 24538 3644 1269 -3681 C

ATOM 4018 O ALA C 92 -58.936 74.477 32.817 1.00158.43 O

ANISOU 4018 O ALA C 92 16685 19395 24117 3595 1465 -3767 O

ATOM 4019 N VAL C 93 -56.908 74.031 31.897 1.00180.36 N

ANISOU 4019 N VAL C 93 19680 22289 26561 3580 1231 -3438 N

ATOM 4020 CA VAL C 93 -56.357 73.230 33.005 1.00175.75 C

ANISOU 4020 CA VAL C 93 19078 21937 25761 3449 1392 -3238 C

ATOM 4021 CB VAL C 93 -55.967 71.802 32.555 1.00170.46 C

ANISOU 4021 CB VAL C 93 18343 21263 25162 3491 1330 -3013 C

ATOM 4022 CGl VAL C 93 -54.759 71.847 31.646 1.00165.93 C

ANISOU 4022 CGl VAL C 93 17865 20670 24509 3563 1104 -2917 C

ATOM 4023 CG2 VAL C 93 -55.663 70.927 33.747 1.00166.90 C

ANISOU 4023 CG2 VAL C 93 17885 21022 24507 3344 1469 -2818 C

ATOM 4024 C VAL C 93 -55.092 73.877 33.556 1.00174.36 C

ANISOϋ 4024 C VAL C 93 19066 21953 25228 3340 1372 -3148 C

ATOM 4025 O VAL C 93 -54.446 74.670 32.864 1.00171.85 O

ANISOU 4025 O VAL C 93 18867 21600 24828 3372 1203 -3168 O

ATOM 4026 N TYR C 94 -54.728 73.528 34.790 1.00178.06 N

ANISOU 4026 N TYR C 94 19547 22625 25484 3205 1539 -3044 N

ATOM 4027 CA TYR C 94 -53.561 74.126 35.438 1.00176.27 C

ANISOU 4027 CA TYR C 94 19472 22574 24930 3104 ' 1537 -2978 C

ATOM 4028 CB TYR C 94 -53.990 75.236 36.400 1.00180.51 C

ANISOU 4028 CB TYR C 94 20031 23168 25385 3049 1654 -3176 C

ATOM 4029 CG TYR C 94 -54.581 76.453 35.726 1.00182.25 C

ANISOU 4029 CG TYR C 94 20263 23213 25771 3147 1521 -3419 C

ATOM 4030 CDl TYR C 94 -53.788 77.318 34.993 1.00179.61 C

ANISOU 4030 CDl TYR C 94 20078 22869 25298 3150 1349 -3444 C

ATOM 4031 CEl TYR C 94 -54.331 78.434 34.380 1.00190.01 C

ANISOϋ 4031 CEl TYR C 94 21422 24008 26764 3224 1192 -3660 C

ATOM 4032 CZ TYR C 94 -55.677 78.701 34.502 1.00191.81 C ANISOU 4032 CZ TYR C 94 21526 24060 27294 3311 1208 -3875 C

ATOM 4033 OH TYR C 94 -56.216 79.812 33.897 1.00193.57 O

ANISOU 4033 OH TYR C 94 21791 24084 27671 3383 1018 -4102 O

ATOM 4034 CE2 TYR C 94 -56.482 77.860 35.228 1.00191.45 C

ANISOU 4034 CE2 TYR C 94 21318 24028 27397 3318 1397 -3867 C

ATOM 4035 CD2 TYR C 94 -55.933 76.745 35.838 1.00188.88 C

ANISOU 4035 CD2 TYR C 94 20969 23888 26909 3229 1553 -3629 C

ATOM 4036 C TYR C 94 -52.683 73.108 36.171 1.00170.18 C

ANISOU 4036 C TYR C 94 18738 21980 23943 2995 1596 -2737 C

ATOM 4037 O TYR C 94 -53.188 72.206 36.832 1.00167.75 O

ANISOU 4037 O TYR C 94 18347 21721 23671 2932 1732 -2658 O

ATOM 4038 N PHE C 95 -51.367 73.276 36.050 1.00160.81 N

ANISOU 4038 N PHE C 95 17680 20882 22539 2969 1478 -2627 N

ATOM 4039 CA PHE C 95 -50.396 72.408 36.700 1.00151.91 C

ANISOU 4039 CA PHE C 95 16607 1989Θ 21215 2882 1473 -2419 C

ATOM 4040 CB PHE C 95 -49.522 71.732 35.659 1.00148.23 C

ANISOU 4040 CB PHE C 95 16141 19400 20781 2959 1265 -2312 C

ATOM 4041 CG PHE C 95 -50.220 70.717 34.833 1.00148.17 C

ANISOU 4041 CG PHE C 95 15989 19261 21048 3064 1197 , -2280 C

ATOM 4042 CDl PHE C 95 -50.961 69.713 35.423 1.00153.80 C

ANISOU 4042 CDl PHE C 95 16610 19975 21852 3023 1283 -2184 C

ATOM 4043 CEl PHE C 95 -51.589 68.757 34.650 1.00157.97 C

ANISOU 4043 CEl PHE C 95 17001 20373 22646 3129 1197 -2148 C

ATOM 4044 CZ PHE C 95 -51.461 68.793 33.271 1.00157.94 C

ANISOU 4044 CZ PHE C 95 16956 20242 22813 3287 1029 -2215 C

ATOM 4045 CE2 PHE C 95 -50.706 69.779 32.676 1.00149.45 C

ANISOU 4045 CE2 PHE C 95 15983 19175 21627 3316 950 -2308 C

ATOM 4046 CD2 PHE C 95 -50.087 70.729 33.458 1.00144.95 C

ANISOU 4046 CD2 PHE C 95 15546 18732 20798 3200 1029 -2335 C

ATOM 4047 C PHE C 95 -49.452 73.172 37.623 1.00147.45 C

ANISOU 4047 C PHE C 95 16195 19487 20343 2781 1507 -2397 C

ATOM 4048 O PHE C 95 -49.090 74.321 37.357 1.00137.25 O

ANISOU 4048 O PHE C 95 14987 18190 18971 2802 1435 -2491 O

ATOM 4049 N CYS C 96 .-49.022 72.508 38.690 1.00152.85 N

ANISOU 4049 N CYS C 96 16920 20297 20858 2669 1597 -2262 N

ATOM 4050 CA CYS C 96 -47.990 73.048 39.567 1.00157.35 C

ANISOU 4050 CA CYS C 96 17643 21008 21135 2576 1615 -2213 C

ATOM 4051 CB CYS C 96 -48.572 73.420 40.929 1.00168.46 C

ANISOU 4051 CB CYS C 96 19072 22515 22419 2468 1831 -2250 C

ATOM 4052 SG CYS C 96 -48.874 72.022 42.048 1.00185.62 S

ANISOU 4052 SG CYS C 96 21213 24753 24560 2335 1945 -2060 S

ATOM 4053 C CYS C 96 -46.919 71.996 39.760 1.00154.44 C

ANISOU 4053 C CYS C 96 17327 20701 20654 2529 1512 -2023 C

ATOM 4054 O CYS C 96 -47.237 70.812 39.840 1.00152.39 O

ANISOU 4054 O CYS C 96 16987 20409 20507 2519 1498 -1919 O

ATOM 4055 N ALA C 97 -45.659 72.420 39.838 1.00131.71 N

ANISOU 4055 N ALA C 97 14577 17903 17563 2498 1427 -1986 N

ATOM 4056 CA ALA C 97 -44.556 71.484 40.050 1.00126.12 C

ANISOU 4056 CA ALA C 97 13928 17257 16736 2447 1321 -1836 C

ATOM 4057 CB ALA C 97 -43.997 71.022 38.731 1.00124.20 C

ANISOU 4057 CB ALA C 97 13610 16968 16612 2544 1117 -1813 C

ATOM 4058 C ALA C 97 -43.448 72.064 40.922 1.00126.54 C

ANISOU 4058 C ALA C 97 14147 17414 16517 2373 1320 -1818 C

ATOM 4059 O ALA C 97 -43.245 73.277 40.944 1.00124.34 O

ANISOU 4059 O ALA C 97 13928 17155 16161 2392 1339 -1917 O

ATOM 4060 N ARG C 98 -42.749 71.188 41.647 1.00142.21 N

ANISOU 4060 N ARG C 98 16211 19452 18371 2290 1282 -1694 N

ATOM 4061 CA ARG C 98 -41.588 71.575 42.456 1.00144.97 C

ANISOU 4061 CA ARG C 98 16725 19882 18474 2227 1251 -1668 C

ATOM 4062 CB ARG C 98 -41.413 70.639 43.674 1.00140.59 C

ANISOU 4062 CB ARG C 98 16268 19358 17790 2107 1270 -1538 C

ATOM 4063 CG ARG C 98 -39.969 70.214 43.955 1.00145.89 C

ANISOU 4063 CG ARG C 98 17078 200-66 18289 2075 1116 -1491 C

ATOM 4064 CD ARG C 98 -39.544 70.437 45.397 1.00154.23 C

ANISOU 4064 CD ARG C 98 18305 21157 19140 1948 1184 -1410 C

ATOM 4065 NE ARG C 98 -39.319 69.211 46.167 1.00162.29 N

ANISOU 4065 NE ARG C 98 19351 22137 20174 1863 1084 -1277 N

ATOM 4066 CZ ARG C 98 -38.298 68.377 45.989 1.00159.86 C

ANISOU 4066 CZ ARG C 98 19133 21806 19799 1838 8.78 -1225 C

ATOM 4067 NHl ARG C 98 -37.419 68.601 45.030 1.00161.62 N

ANISOU 4067 NHl ARG C 98 19414 22054 19940 1893 771 -1299 N

ATOM 4068 NH2 ARG C 98 -38.165 67.305 46.755 1.00160.24 N

ANISOU 4068 NH2 ARG C 98 19210 21801 19871 1753 763 -1107 N

ATOM 4069 C ARG C 98 -40.304 71.668 41.604 1.00144.27 C

ANISOU 4069 C ARG C 98 16648 19809 18358 2284 1053 -1681 C

ATOM 4070 O ARG C 98 -39.687 70.661 41.245 1.00138.39 O

ANISOU 4070 O ARG C 98 15873 19062 17645 2291 898 -1618 O ATOM 4071 N GLU C 99 -39.920 72.893 41.266 1.00150.66 N

ANISOU 4071 N GLU C 99 17494 20641 19110 2319 1045 -1772 N

ATOM 4072 CA GLU C 99 -38.740 73.120 40.447 1.00144.05 C

ANISOU 4072 CA GLU C 99 16661 19841 18232 2353 877 -1793 C

ATOM 4073 CB GLU C 99 -37.467 72.919 41.274 1.00150.23 C

ANISOU 4073 CB GLU C 99 17576 20692 18814 2289 810 -1747 C

ATOM 4074 CG GLU C 99 -37.272 73.938 42.398 1.00151.43 C

ANISOU 4074 CG GLU C 99 17879 20874 18783 2240 909 -1769 C

ATOM 4075 CD GLU C 99 -36.183 73.523 43.377 1.00151.77 C

ANISOU 4075 CD GLU C 99 18058 20951 18657 2176 857 -1709 C

ATOM 4076 OEl GLU C 99 -35.632 72.408 43.216 1.00148.45 O

ANISOU 4076 OEl GLU C 99 17614 20518 18273 2159 754 -1649 O

ATOM 4077 OE2 GLU C 99 -35.884 74.308 44.305 1.00151.81 O

ANISOU 4077 OE2 GLU C 99 18196 20982 18504 2149 899 -1727 O

ATOM 4078 C GLU C 99 -38.716 72.220 39.215 1.00139.13 C

ANISOU 4078 C GLU C 99 15892 19192 17778 2421 738 -1778 C

ATOM 4079 O GLU C 99 -37.661 71.771 38.796 1.00143.50 O

ANISOU 4079 O GLU C 99 16'436 19797 18292 2422 591 -1756 O

ATOM 4080 N TRP C 100 -39.879 71.947 38.645 1.00122.77 N

ANISOU 4080 N TRP C 100 13702 17040 15904 2485 777 -1803 N

ATOM 4081 CA TRP C 100 ' -39.970 71.258 37.360 1.00124.22 C

ANISOU 4081 CA TRP C 100 13744 17195 16259 2574 '638 -1810 C

ATOM 4082 CB TRP C 100 -39.077 .71.926 36.322 1.00121.41 C

ANISOU 4082 CB TRP C 100 13389 16908 15833 2598 517 -1872 C

ATOM 4083 CG TRP C 100 -39.396 73.327 36.107 1.00121.60 C

ANISOU 4083 CG TRP C 100 13477 ' 16908 15819 2587 586 -1941 C

ATOM 4084 CDl TRP C 100 -38.629 74.400 36.424 1.00116.52 C

ANISOU 4084 CDl TRP C 100 12954 16328 14992 2523 591 -1964 C

ATOM 4085 NEl TRP C 100 -39.266 75.563 36.072 1.00118.21 N

ANISOU 4085 NEl TRP C 100 13197 16477 15242 2532 627 -2035 N

ATOM 4086 CE2 TRP C 100 -40.476 75.245 35.525 1.00121.33 C

ANISOU 4086 CE2 TRP C 100 13491 16759 15849 2606 655 -2070 C

ATOM 4087 CD2 TRP C 100 -40.587 73.836 35.534 1.00118.92 C

ANISOU 4087 CD2 TRP C 100 13087 16456 15642 2643 639 -2006 C

ATOM 4088 CE3 TRP C 100 -41.749 73.239 35.028 1.00117.42 C

ANISOU 4088 CE3 TRP C 100 12777 16152 15685 2726 658 -2022 C

ATOM 4089 CZ3 TRP C 100 -42.752 74.052 34.530 1.00119.02 C

ANIΞOU 4089 CZ3 TRP C 100 12966 16241 16017 2771 695 -2115 C

ATOM 4090 CH2 TRP C 100 -42.612 75.460 34.539 1.00128.18 C

ANIΞOU 4090 CH2 TRP C 100 14231 17397 17075 2729 696 -2189 C

ATOM 4091 CZ2 TRP C 100 -41.482 76.071 35.034 1.00124.19 C

ANISOU 4091 CZ2 TRP C 100 13841 17006 16339 2646 674 -2161 C

ATOM 4092 C TRP C 100 -39.614 69.790 37.392 1.00124.29 C

ANISOU 4092 C TRP C 100 13690 17210 16326 2582 519 -1730 c-

ATOM 4093 O TRP C 100 -39.369 69.219 36.347 1.00118.14 O

ANISOU 4093 O TRP C 100 12793 16432 15664 2664 370 -1747 O

ATOM 4094 N ALA C 101 -39.578 69.164 38.560 1.00118.60 N

ANISOU 4094 N ALA. C 101 13048 16491 15525 2496 564 -1646 N

ATOM 4095 CA ALA C 101 -39.160 67.765 38.614 1.00119.65 C

ANIΞOU 4095 1 CA ALA C 101 13140 16618 15705 2492 399 -1571 C

ATOM 4096 CB ALA C 101 -37.976 67.613 39.495 1.00129.25 C

ANISOU 4096 CB ALA C 101 14500 17893 16715 2401 337 -1541 C

ATOM 4097 C ALA C 101 -40.250 66.813 39.053 1.00122.07 C

ANISOU 4097 C ALA C 101 13389 16835 16157 2470 444 -1476 C

ATOM 4098 O ALA C 101 ' -40.375 65.725 38.513 1.00120.17 O

ANISOU 4098 O ALA C 101 13034- 16549 16078 2528 285 -1440 O

ATOM 4099 N TYR C 102 -41.008 67.211 40.065 1.00127.10 N

ANISOU 4099 N TYR C 102 14102 17457 16733 2380 652 -1440 N

ATOM 4100 CA TYR C 102 -42.196 66.474 40.467 1.00128.83 C

ANISOU 4100 CA TYR C 102 14254 17605 17090 2341 741 -1361 C

ATOM 4101 CB TYR C 102 -42.140 66.119 41.947 1.00128.14 C

ANISOU 4101 CB TYR C 102 14306 17547 16834 2174 823 -1249 C

ATOM 4102 CG TYR C 102 -40.861 65.456 42.364 1.00129.96 C

ANISOU 4102 CG TYR C 102 14649 17799 16931 2118 .621 -1180 C

ATOM 4103 CDl TYR C 102 -40.569 64.163 41.973 1.00133.27 C

ANISOU 4103 ' CDl TYR C 102 15020 18157 17458 2106 407 -1084 C

ATOM 4104 CEl TYR C 102 -39.387 63.545 42.352 1.00138.33 C

ANISOU 4104 CEl TYR C 102 15767 18802 17991 2056 189 -1045 C

ATOM 4105 CZ TYR C 102 -38.481 64.225 43.144 1.00146.57 C

ANISOU 4105 CZ TYR C 102 16965 19911 18815 2020 204 -1100 C

ATOM 4106 OH TYR C 102 -37.293 63.625 43.544 1.00157.05 O

ANISOU 4106 OH TYR C 102 18402 21226 20043 1975 -20 -1084 O

ATOM 4107 CE2 TYR C 102 -38.760 65.518 43.543 1.00143.44 C

ANIΞOU 4107 CE2 TYR C 102 16614 19579 18307 2033 424 -1181 C

ATOM 4108 CD2 ' TYR C 102 -39.945 66.122 43.151' 1.00134.46 C

ANISOU 4108 CD2 TYR C 102 15371 18438 17278 2080 622 -1221 C

ATOM 4109 C TYR C 102 -43.408 67.345 40.200 1.00126.81 C ANISOU 4109 C TYR C 102 13931 17315 16937 2383 942 -1453 C

ATOM 4110 O TYR C 102 -43.467 68.490 40.648 1.00125.64 O

ANISOU 4110 O TYR C 102 13865 17214 16657 2356 1083 -1533 O

ATOM 4111 N TRP C 103 -44.377 66.804 39.472 1.00132.82 N

ANISOU 4111 N TRP C 103 14538 17981 17945 2460 935 -1456 N

ATOM 4112 CA TRP C 103 -45.549 67.583 39.074 1.00140.38 ■ C

ANISOU 4112 CA TRP C 103 15415 18878 19044 2520 1091 -1571 C

ATOM 4113 CB TRP C 103 -45.748 67.502 37.546 1.00138.15 C

ANISOO 4113 CB TRP C 103 14998 18499 18992 2688 949 -1640 C

ATOM 4114 CG TRP C 103 -44.652 68.127 36.717 1.00123.69 C

ANISOU 4114 CG TRP C 103 13215 16722 17061 2749 812 -1701 C

ATOM 4115 CDl TRP C 103 -43.381 67.689 36.609 1.00119.51 C

ANISOU 4115 CDl TRP C 103 12732 16278 16399 2734 652 -1652 C

ATOM 4116 NEl TRP C 103 -42.678 68.503 35.764 1.00121.13 N

ANISOσ 4116 NEl TRP C 103 12960 16532 16533 2784 578 -1738 N

ATOM 4117 CE2 TRP C 103 -43.505 69.489 35.295 1.00119.55 C

ANISOU 4117 CE2 TRP C 103 12744 16260 16420 2831 672 -1836 C

ATOM 4118 CD2 TRP C 103 -44.754 69.283 35.866 1.00118.61 C

ANISOU 4118 CD2 TRP C 103 12576 16051 16439 2821 816 -1830 C

ATOM 4119 CE3 TRP C 103 -45.778 70.165 35.547 1.00122.05 C

ANISOU 4119 CE3 TRP C 103 12982 16391 16999 2870 913 -1947 C

ATOM 4120 CZ3 TRP C 103 -45.515 71.207 34.679 1.00118.98 C

ANISOU 4120 CZ3 TRP C 103 12632 15986 16589 2919 845 -2047 C

ATOM 4121 CH2 TRP C 103 -44.269 71.386 34.133 1.00123.21 C

ANISOU 412l " CH2 TRP C 103 13225 16618 16971 2911 709 -2027 C

ATOM 4122 CZ2 TRP C 103 -43.247 70.542 34.425 1.00119.32 C

ANISOU 4122 CZ2 TRP C 103 12744 16235 16359 2871 629 -1932 .C

ATOM 4123 C TRP C 103 -46.844 67.151 39.788 1.00148.96 C

ANISOU 4123 C TRP C 103 16444 19933 20222 2438 1270 -1531 C

ATOM 4124 O TRP C 103 -47.015 65.976 40.115 1.00151.66 O

ANISOU 4124 O TRP C 103 16766 20262 20594 2366 1222 -1392 O

ATOM 4125 N GLY C 104 -47.747 68.107 40.020 1.00153.61 N

ANISOU 4125 N GLY C 104 17006 20513 20846 2439 1464 -1658 N

ATOM 4126 CA GLY C 104 -49.101 67.804 40.446 1.00161.75 C

ANISOU 4126 CA GLY C 104 17933 21510 22013 2385 1637 -1665 C

ATOM 4127 C GLY C 104 -49.829 67.064 39.335 1.00170.97 C

ANISOU 4127 C GLY C 104 18930 22525 23504 2519 1533 -1674 C

ATOM 4128 O GLY C 104 -49.227 66.748 38.311 1.00168.96 O

ANISOU 4128 O GLY C 104 18650 22207 23340 2650 1336 -1682 O

ATOM 4129 N GLN C 105 -51.114 66.774 39.519 1.00182.07 N

ANISOU 4129 N GLN C 105 20215 23876 25087 2489 1660 -1678 N

ATOM 4130 CA GLN C 105 -51.850 66.009 38.514 1.00177.97 C

ANISOU 4130 CA GLN C 105 19532 23195 24894 2623 1552 -1677 C

ATOM 4131 CB GLN C 105 -52.733 64.937 39.160 1.00181.59 C

ANISOU 4131 CB GLN C 105 19892 23631 25472 2519 1628 -1552 C

ATOM 4132 CG GLN C 105 -53.991 65.468 39.830 1.00190.15 C

ANISOU 4132 CG GLN C 105 20882 24718 26648 2456 1892 -1679 C

ATOM 4133 CD GLN C 105 -53.746 65.984 41.235 1.00194.05 C

ANISOU 4133 CD GLN C 105 ■■ 21485 25401 26845 2266 2121 -1704 C

ATOM 4134 OEl GLN C 105 -52.758 65.630 41.877 1.00190.87 O

ANISOU 4134 OEl GLN C 105 21238 25115 26169 2156 2085 -1581 O

ATOM 4135 NE2 GLN C 105 -54.654 66.821 41.723 1.00195.36 N

ANISOU 4135 NE2 GLN C 105 21563 25596 27067 2233 2349 -1879 N

ATOM 4136 C GLN C 105 -52.688 66.937 37.663 1.00171.72 C

ANISOU 4136 C GLN C 105 18657 22287 24301 2765 1601 -1892 C

ATOM 4137 O GLN C 105 -53.294 66.530 36.674 1.00171.70 O

ANISOU 4137 O GLN C 105 18524 22130 24586 2897 1523 -1929 O

ATOM 4138 N GLY C 106 -52.714 68.197 38.062 1.00155.79 N

ANISOU 4138 N GLY C 106 16724 20334 22137 2742 1709 -2040 N

ATOM 4139 CA GLY C 106 -53.492 69.193 37.358 1.00161.03 C

ANISOU 4139 CA GLY C 106 17333 20880 22972 2862 1729 -2262 C

ATOM 4140 C GLY C 106 -54.883 69.451 37.922 1.00172.55 C

ANISOU 4140 C GLY C 106 18678 22317 24567 2819 1945 -2404 C

ATOM 4141 O GLY C 106 -55.428 68.656 38.698 1.00173.75 O

ANISOU 4141 O. GLY C 106 18765 22532 24719 2702 2077 -2306 O

ATOM 4142 N THR C 107 -55.462 70.579 37.520 1.00182.73 N

ANISOU 4142 N THR C 107 19940 23519 25970 2904 1970 -2642 N

ATOM 4143 CA THR C 107 -56.810 70.938 37.924 1.00181.94 C

ANISOU 4143 CA THR C 107 19710 23391 26027 2885 2158 -2839 C

ATOM 4144 CB THR C 107 -56.779 71.881 39.117 1.00188.02 C

ANISOU 4144 CB THR C 107 20538 24354 26548 2752 2345 -2945 C

ATOM 4145 OGl THR C 107 -56.341 71.161 40.274 1.00193.88 O

ANISOU 4145 OGl THR C 107 21314 25280 27072 2574 2481 -2744 O

ATOM 4146 CG2 THR C 107 -58.158 72.439 39.375 1.00195.48 C

ANISOU 4146 CG2 THR C 107 21337 25261 27674 2769 2499 -3228 C

ATOM 4147 C THR C 107 -57.519 71.612 36.763 1.00182.82 C

ANISOU 4147 c THR C 107 19755 23284 26424 3056 2057 -3077 C ATOM 4148 O THR C 107 -56.973 72.527 36.153 1.00180.08 O

ANISOU 4148 O THR C 107 19511 22888 26024 3125 1928 -3185 O

ATOM 4149 N LEU C 108 -58.730 71.153 36.456 1.00190.22 N

ANISOU 4149 N LEU C 108 20526 24081 27668 3118 2106 -3157 N

ATOM 4150 CA LEU C 108 -59.468 71.645 35.296 1.00193.08 C

ANISOU 4150 CA LEU C 108 20823 24193 28346 3296 1982 -3373 C

ATOM 4151 CB LEU C 108 -60.185 70.488 34.607 1.00191.26 C

ANISOU 4151 CB LEU C 108 20438 23797 28436 3385 1955 -3310 C

ATOM 4152 CG LEU C 108 -61.033 70.835 33.386 1.00193.69 C

ANISOU 4152 CG LEU C 108 20677 23809 29106 3588 1804 -3504 C

ATOM 4153 CDl LEU C 108 -60.409 71.967 32.592 1.00191.90 C

ANISOU 4153 CDl LEU C 108 20611 23492 28809 3683 1589 -3580 C

ATOM 4154 CD2 LEU C 108 -61.229 69.604 32.511 1.00188.66 C

ANISOU 4154 CD2 LEU C 108 19932 23023 28727 3695 1706 -3353 C

ATOM 4155 C LEU C 108 -60.466 72.745 35.652 1.00203.44 C

ANISOU 4155 C LEU C 108 22077 25480 29741 3297 2091 -3698 C

ATOM 4156 O LEU C 108 -61.499 72.479 36.263 1.00212.60 O

ANISOU 4156 O LEU C 108 23093 26702 30982 3224 2298 -3802 O

ATOM 4157 N VAL C 109 -60.157 73.976 35.256 1.00195.96 N

ANISOU 4157 N VAL C 109 21235 24443 28776 3374 1939 -3865 N

ATOM 4158 CA VAL C 109 -61.016 75.126 35.536 1.00200.51 C

ANISOU 4158 CA VAL C 109 21765 24979 29442 3392 1981 -4201 C

ATOM 4159 CB VAL C 109 -60.167. 76.375 35.874 1.00197.02 C

ANISOU 4159 CB VAL C 109 21483 24654 28720 3341 1913 -4261 C

ATOM 4160 CGl VAL C 109 -60.807 77.657 35.349 1.00197.68 C

ANISOU 4160 CGl VAL C 109 21593 24535 28980 3453 1727 -4575 C

ATOM 4161 CG2 VAL C 109 -59.929 76.454 37.369 1.00193.02 C

ANISOU 4161 CG2 VAL C 109 20949 24432 27959 3183 2157 -4264 C

ATOM 4162 C VAL C 109 -61.970 75.416 34.373 1.00209.48 C

ANISOU 4162 C VAL C 109 22833 25803 30957 3565 1822 -4435 C

ATOM 4163 O VAL C 109 -61.578 76.052 33.391 1.00204.89 O

ANISOU 4163 O VAL C 109 22375 25048 30427 3669 1577 -4455 O

ATOM 4164 N THR C 110 -63.214 74.932 34.481 1.00209.94 N

ANISOU 4164 N THR C 110 18895 23820 37052 4049 -2682 -2664 N

ATOM 4165 CA THR C 110 -64.222 75.115 33.425 1.00211.75 C

ANISOU 4165 CA THR C 110 18960 24503 36992 4078 -2672 -3175 C

ATOM 4166 CB THR C 110 -65.105 73.850 33.187 1.00203.95 C

ANISOU 4166 CB THR C 110 17797 23555 36138 3832 -2319 -3608 C

ATOM 4167 OGl THR C 110 -64.589 72.724 33.911 1.00193.76 O

ANISOU 4167 OGl THR C 110 16540 21838 35241 3636 -2095 -3411 O

ATOM 4168 CG2 THR C 110 -65.174 73.517 31.699 1.00201.03 C

ANISOU 4168 CG2 THR C 110 17277 23366 35740 3841 -2162 -3964 C

ATOM 4169 C THR C 110 -65.130 76.308 33.723 1.00206.71 C

ANISOU 4169 C THR C 110 18367 24244 35928 4230 -3007 -3270 C

ATOM 4170 O THR C 110 -65.930 76.284 34.655 1.00199.83 O

ANISOU 4170 O THR C 110 17521 23430 34976 4172 -3055 -3291 O

ATOM 4171 N VAL C 111 -64.995 77.356 32.926 1.00201.27 N

ANISOU 4171 N VAL C 111 17694 23818 34961 4424 -3261 -3323 N

ATOM 4172 CA VAL C 111 -65.787 78.549 33.130 1.00205.30 C

ANISOU 4172 CA VAL C 111 18257 24703 35044 4586 -3626 -3434 C

ATOM 4173 CB VAL C 111 -64.947 79.817 32.921 1.00202.43 C

ANISOU 4173 CB VAL C 111 18070 24375 34471 4830 -4048 -3068 C

ATOM 4174 CGl VAL C 111 -64.712 80.068 31.432 1.00203.49 C

ANISOU 4174 CGI VAL C 111 18122 24772 34422 4899 -4144 -3342 C

ATOM 4175 CG2 VAL C 111 -65.622 81.008 33.572 1.00199.46 C

ANISOU 4175 CG2 VAL C 111 17837 24187 33760 4991 -4447 -2932 ' C

ATOM 4176 C VAL C 111 -66.933 78.523 32.142 1.00214.39 C

ANISOU 4176 C VAL C 111 19233 26244 35980 4545 -3551 -4023 C

ATOM 4177 O VAL C 111 -66.741 78.145 30.991 1.00208.69 O

ANISOU 4177 O VAL C 111 18417 25557 35319 4522 -3421 -4217 O

ATOM 4178 N SER C 112 -68.123 78.908 32.597 1.00239.54 N

ANISOU 4178 N SER C 112 22376 29709 38930 4526 -3617 -4302 N

ATOM 4179 CA SER C 112 -69.325' 78.874 31.760 1.00246.92 C

ANISOU 4179 CA SER C 112 23155 31012 39652 4472 -3540 -4870 C

ATOM 4180 CB SER C 112 -69.678 77.431 31.376 1.00248.80 C

ANISOU 4180 CB SER C 112 23232 31126 40174 4227 -3070 -5126 C

ATOM 4181 OG SER C 112 -70.868 77.370 30.603 1.00249.62 O

ANISOU 4181 OG SER C 112 23200 31559 40086 4167 -2975 -5650 O

ATOM 4182 C SER C 112 -70.525 79.535 32.440 1.00250.30 C

ANISOU 4182 C SER C 112 23590 31789 39725 4535 -3773 -5075 C

ATOM 4183 O SER C 112 ' -70.492 79.832 33.635 1.00244.75 O

ANISOU 4183 O SER C 112 22950 31009 39035 4522 -3824 -4860 O

ATOM 4184 N ALA C 113 -71.589 79.743 31.667 1.00234.36 N

ANISOU 4184 N ALA C 113 21505 30147 37394 4597 -3913 -5503 N

ATOM 4185 CA ALA C 113 -72.793 80.408 32.158 1.00231.94 C

ANISOϋ 4185 CA ALA C 113 21185 30217 36726 4659 -4129 -5776 C

ATOM 4186 CB ALA C 113 -73.330 81.366 31.100 1.00219.19 C ANISOU 4186 CB ALA C 113 19554 28960 34768 4774 -4393 -6166 C

ATOM 4187 C ALA C 113 -73.888 79.426 32.582 1.00236.50 C

ANISOO 4187 C ALA C 113 21611 30872 37376 4446 -3788 -6062 C

ATOM 4188 O ALA C 113 -74.162 79.266 33.774 1.00231.15 O

ANISOU 4188 O ALA C 113 20952 30214 36662 4417 -3821 -5944 O

ATOM 4189 N ALA C 114 -74.487 78.768 31.591 1.00256.94 N

ANISOU 4189 N ALA C 114 24060 33498 40068 4292 -3472 -6420 N

ATOM 4190 CA ALA C 114 -75.723 77.987 31.742 1.00258.03 C

ANISOU 4190 CA ALA C 114 24051 33774 40216 4086 -3165 -6763 C

ATOM 4191 CB ALA C 114 -75.927 77.066 30.528 1.00260.72 C

ANISOU 4191 CB ALA C 114 24294 33927 40841 3914 -2773 -6912 C

ATOM 4192 C ALA C 114 -75.938 77.203 33.046 1.00255.74 C

ANISOU 4192 C ALA C 114 23740 33451 39978 3953 -3070 -6634 C

ATOM 4193 O ALA C 114 -75.068 77.132 33.920 1.00246.52 O

ANISOU 4193 O ALA C 114 22681 32097 38890 4006 -3213 -6238 O

ATOM 4194 N LYS C 115 -77.123 76.605 33.138 1.00244.19 N

ANISOU 4194 N LYS C 115 22141 32166 38474 3764 -2823 -6977 N

ATOM 4195 CA LYS C 115 -77.587 75.907 34.333 1.00243.65 C

ANISOU 4195 CA LYS C 115 22017 32161 38396 3594 -2726 -6970 C

ATOM 4196 CB LYS C 115 -79.012 76.378 34.682 1.00249.85 C

ANISOU 4196 CB LYS C 115 22733 33445 38754 3658 -2904 -7335 C

ATOM 4197 CG LYS C 115 -79.870 76.758 33.457 1.00248.60 C

ANISOU 4197 CG LYS C 115 22509 33563 38384 3719 -2898 -7785 C

ATOM 4198 CD LYS C 115 -81.366 76.931 33.777 1.00243.45 C

ANISOU 4198 CD LYS C 115 21776 33405 37318 3753 -3040 -8185 C

ATOM 4199 CE LYS C 115 -82.184 77.110 32.489 1.00228.00 C

ANISOU 4199 CE LYS C 115 19749 31658 35224 3737 -2941 -8650 C

ATOM 4200 NZ LYS C 115 -83.667 77.121 32.680 1.00205.56 N

ANISOU 4200 NZ LYS C 115 16818 29285 31999 3738 -3029 -9064 N

ATOM 4201 C LYS C 115 -77.558 74.385 34.148 1.00240.26 C

ANISOU 4201 C LYS C 115 21487 315 ^ 79 38221 3309 -2323 -7081 C

ATOM 4202 O LYS C 115 -77.566 73.896 33.018 1.00238.42 O

ANISOU 4202 O LYS C 4 115 21193 31360 38034 3266 -2135 -7323 O

ATOM 4203 N THR C 116 -77.520 73.648 35.260 1.00225.47 N

ANISOU 4203 N THR C 116 19606 29557 36504 3109 -2212 -6907 N

ATOM 4204 CA THR C 116 -77.569 72.181 35.238 1.00232.90 C

ANISOU 4204 CA THR C 116 20475 30337 37681 2824 -1880 -6978 C

ATOM 4205 CB THR C 116 -77.807 71.606 36.657 1.00228.60 C

ANISOU 4205 CB THR C 116 19912 29757 37188 2583 -1845 -6863 C

ATOM 4206 OGl THR C 116 -76.830 72.131 37.565 1.00226.57 O

ANISOU 4206 OGl THR C 116 19784 29153 37150 2626 -1977 -6425 O

ATOM 4207 CG2 THR C 116 -77.751 70.075 36.652 1.00224.56 C

ANISOU 4207 CG2 THR C 116 19338 29098 36885 2274 -1549 -6950 C

ATOM 4208 C THR C 116 -78.673 71.659 34.312 1.00236.36 C

ANISOU 4208 C THR C 116 20795 31062 37950 2753 -1703 -7421 C

ATOM 4209 O THR C 116 -79.806 72.128 34.369 1.00240.51 O

ANISOU 4209 O THR C 116 21269 31977 38136 2854 -1826 -7716 O

ATOM 4210 N THR C 117 -78.347 70.689 33.463 1.00248.40 N

ANISOU 4210 N THR C 117 22290 32382 39709 2587 -1426 -7463 N

ATOM 4211 CA THR C 117 -79.335 70.106 32.553 1.00249.16 C

ANISOU 4211 CA THR C 117 22296 32701 39674 2501 -1238 -7841 C

ATOM 4212 CB THR C 117 -79.117 70.-584 31.095 1.00244.22 C

ANISOU 4212 CB THR C 117 21685 32045 39064 2684 -1216 -7979 C

ATOM 4213 OGl THR C 117 -78.961 72.008 31.078 1.00237.34 O

ANISOU 4213 OGl THR C 117 20870 31278 38032 2935 -1511 -7924 O

ATOM 4214 CG2 THR C 117 -80.293 70.208 30.203 1.00242.04 C

ANISOU 4214 CG2 THR C 117 21330 32053 38580 2627 -1078 -8397 C

ATOM 4215 C THR C 117 -79.278 68.580 32.635 1.00253.15 C

ANISOU 4215 C THR C 117 22772 33024 40388 2220 -977 -7824 C

ATOM 4216 O THR C 117 -78.557 68.030 33.468 1.00256.18 O

ANISOU 4216 O THR C 117 23198 33141 40996 2077 -962 -7556 O

ATOM 4217 N ALA C 118 -80.044 67.901 31.786 1.00241.25 N

ANISOU 4217 N ALA C 118 21207 31657 38799 2134 -792 -8110 N

ATOM 4218 CA ALA C 118 -80.036 66.443 31.747 1.00243.92 C

ANISOU 4218 CA ALA C 118 21533 31853 39293 1879 -574 -8109 C

ATOM 4219 CB ALA C 118 -81.161 65.881 32.587 1.00245.27 C

ANISOU 4219 CB ALA C 118 21632 32365 39194 1661 -566 -8294 C

ATOM 4220 C ALA C 118 -80.127 65.930 30.317 1.00249.14 C

ANISOU 4220 C ALA C 118 22195 32417 40048 1920 -377 -8262 C

ATOM 4221 O ALA C 118 -80.688 66.589 29.446 1.00247.45 O

ANISOU 4221 O ALA C 118 21963 32371 39684 2082 -389 -8478 O

ATOM 4222 N PRO C 119 -79.571 64.741 30.077 1.00286.81 N

ANISOU 4222 N PRO C 119 26996 36908 45071 1'767 -20.9 -8155 N

ATOM 4223 CA PRO C 119 -79.453 64.169 28.733 1.00289.87 C

ANISOU 4223 CA PRO C 119 27400 37127 45610 1811 -21 -8235 C

ATOM 4224 CB PRO C 119 -78.671 62.872 28.975 1.00296.73 C

ANISOU 4224 CB PRO C 119 28318 37646 46781 1638 69 -8012 C ATOM 4225 CG PRO C 119 -77.994 63.064 30.297 1.00289.76 C

ANISOU 4225 CG PRO C 119 27457 36679 45960 1546 -87 -7780 C

ATOM 4226 CD PRO C 119 -78.942 63,.889 31..098 1.00286.04 C

ANISOU 4226 CD PRO C 119 26929 36610 45144 1538 -216 -7935 C

ATOM 4227 C PRO C 119 -80.795 63,.848 28..080 1.00286.28 C

ANISOU 4227 C PRO C 119 26908 36944 44920 1741 111 -8555 C

ATOM 4228 O PRO C 119 -81.752 63..482 28..760 1 .00287.16 O

ANISOU 4228 O PRO C 119 26993 37273 44841 1546 123 -8647 O

ATOM 4229 N SER C 120 -80.847 63..989 26..760 1 .00250.51 N

ANISOU 4229 N SER C 120 22383 32394 40404 1890 203 -8712 N

ATOM 4230 CA SER C 120 -81.992 63..552 25..976 1..00247.11 C

ANISOU 4230 CA SER C 120 21941 32155 39793 1837 347 -8996 C

ATOM 4231 CB SER C 120 -82.572 64..716 25..179 1..00244.96 C

ANISOU 4231 CB SER C 120 21653 32051 39369 2029 291 -9237 C

ATOM 4232 OG SER C 120 -83.015 65..737 26..049 1..00245..82 O

ANISOU 4232 OG SER C 120 21739 32315 39346 2152 51 -9206 O

ATOM 4233 C S * ER C 120 -81.572 62..430 25..036 1..00246..62 C

ANISOU 4233 C SER C 120 21929 31818 39957 1775 558 -8952 C

ATOM 4234 O SER C 120 -80.774 62..634 24..128 1..00245..53 O

ANISOU 4234 O SER C 120 21813 31478 40001 1918 634 -8955 O

ATOM 4235 N VAL C 121 -82.130 61..249 25..254 1..00248..69 N

ANISOU 4235 N VAL C 121 22214 32089 40188 1557 631 -8914 N

ATOM 4236 CA VAL C 121 -81.743 60..050 24..520 1..00249..80 C

ANISOU 4236 CA VAL C 121 22419 31969 40524 1484 791 -8840 C

ATOM 4237 CB = VAL C 121 -81.778 58.851 25..480 1..00247..76 C

ANISOU 4237 CB VAL C 121 22190 31700 40248 1222 747 -8704 C

ATOM 4238 CGl VAL C 121 -81.282 57.591 24..794 1..00248..99 C

ANISOU 4238 CGl VAL C 121 22429 31613 40564 1141 869 -8632 C

ATOM 4239 CG2 VAL C 121 -80.960 59.172 26.727 1..00242..88 C

ANISOU 4239 CG2 VAL C 121 21558 30938 39788 1190 592 -8477 C

ATOM 4240 C VAL C 121 -82.615 59.763 23.272 1..00252..78 C

ANISOU 4240 C VAL C 121 22829 32412 40804 1514 964 -9058 C

ATOM 4241 O VAL C 121 -83.818 59.522 23.389 1..00254..58 O

ANISOU 4241 O VAL C 121 23047 32936 40746 1428 981 -9246 O

ATOM 4242 N TYR C 122 -82.007 59.787 22.082 1. 00281..09 N

ANISOU 4242 N TYR C 122 26455 35718 44630 1633 1091 -9028 N

ATOM 4243 CA TYR C 122 -82.738 59.515 20.837 1. 00276..92 C

ANISOU 4243 CA TYR C 122 25973 35190 44054 1668 1262 -9214 C

ATOM 4244 CB TYR C 122 -82.642 60.696 19.865 1. 00276..81 C

ANISOU 4244 CB TYR C 122 25929 35160 44088 1869 1272 -9373 C

ATOM 4245 CG TYR C 122 -82.903 62.065 20.452 1.00280..28 C

ANISOU 4245 CG TYR C 122 26300 35861 44334 1942 1090 -9488 C

ATOM 4246 CDl TYR C 122 -81.944 63.067 20.362 1.00278..61 C

ANISOU 4246 CDl TYR C 122 26056 35563 44241 2117 972 -9448 C

ATOM 4247 CEl TYR C 122 -82.171 64.324 20.886 1.00279..95 C

ANISOU 4247 CEl TYR C 122 26182 35973 44215 2196 769 -9542 C

ATOM 4248 CZ TYR C 122 -83.369 64.596 21.507 1.00282..17 C

ANISOU 4248 CZ TYR C 122 26437 36588 44186 2107 698 -9693 C

ATOM 4249 OH TYR C 122 -83.589 65.849 22.028 1. 00284..28 O

ANISOU 4249 OH TYR C 122 26666 37102 44246 2203 475 -9791 O

ATOM 4250 CE2 TYR C 122 -84.343 63.622 21.605 1. 00282..51 C

ANISOU 4250 CE2 TYR C 122 26498 36736 44108 1925 829 -9743 C

ATOM 4251 CD2 TYR C 122 -84.108 62.365 21.076 .1. 00281..97 C

ANISOU 4251 CD2 TYR C 122 26487 36421 44228 1840 1017 -9632 C

ATOM 4252 C TYR C 122 -82.228 58.273 20.108 1. 00274..65 C

ANISOU 4252 C TYR C 122 25768 34604 43982 1646 1409 -9098 C

ATOM 4253 O TYR C 122 -81.736 58.383 18.986 1. 00270..76 O

ANISOU 4253 P TYR C 122 25298 33925 43655 1782 1528 -9148 O

ATOM 4254 N PRO C 123 -82.368 57.090 20.727 1. 00224..16 N

ANISOU 4254 N PRO C 123 19426 28171 37574 1469 1385 -8954 N

ATOM 4255 CA PRO C 123 -81.838 55.825 20.207 1. 00221.99 C

ANISOU 4255 CA PRO C 123 19240 27609 37496 1451 1470 -8818 C

ATOM 4256 CB PRO C 123 -82.852 54.807 20.722 1. 00220.65 C

ANISOU 4256 CB PRO C 123 19142 27599 37097 1208 1423 -8790 C

ATOM 4257 CG PRO C 123 -83.260 55.362 22.047 1. 00224.13 C

ANISOU 4257 CG PRO C 123 19503 28299 37356 1082 1263 -8797 C

ATOM 4258 CD PRQ C 123 -83.195 56.871 21.927 1. 00223.96 C

ANISOU 4258 CD PRO C 123 19385 28411 37298 1257 1260 -8941 C

ATOM 4259 C PRO C 123 -81.749 55.767 18.680 1. 00223.97 C

ANISOU 4259 C PRO C 123 19540 27706 37851 1595 1654 -8917 C

ATOM 4260 O PRO C 123 -80.859 55.105 18.134 1. 00221.76 O

ANISOU 4260 O PRO C 123 19337 27180 37743 1613 1725 -8806 O

ATOM 4261 N MET C 135 -72.554 42.998 7.936 1. 00262.52 N

ANISOU 4261 N MET C 135 25370 29118 45257 3214 1964 -7590 N

ATOM 4262 CA MET C 135 -72.698 43.789 9.154 1. 00265.96 C

ANISOU 4262 CA MET C 135 25695 29727 45631 3038 1898 -7629 C

ATOM 4263 CB MET C 135 -71.507 43.557 10.099 1. 00273.64 C ANISOU 4263 CB MET C 135 26616 30618 46736 3026 1688 -7556 C

ATOM 4264 CG MET C 135 -70.145 43.990 9.542 1.00278.36 C

ANISOU 4264 CG MET C 135 27081 31057 47626 3267 1747 -7555 C

ATOM 4265 SD MET C 135 -68.685 43.355 10.429 1.00284.62 S

ANISOU 4265 SD MET C 135 27843 31713 48587 3262 1493 -7467 S

ATOM 4266 CE MET C 135 -68.730 44.298 11.953 1.00270.44 C

ANISOU 4266 CE MET C 135 25914 30062 46780 3078 1478 -7475 C

ATOM 4267 C MET C 135 -72.855 45.275 8.844 1.00263.96 C

ANISOU 4267 C MET C 135 25258 29572 45462 3089 2105 -7756 C

ATOM 4268 O MET C 135 -72.508 45.725 7.753 1.00261.62 O

ANISOU 4268 O MET C 135 24849 29181 45375 3276 2230 -7796 O

ATOM 4269 N VAL C 136 -73.395 46.022 9.806 1.00264.61 N

ANISOU 4269 N VAL C 136 25314 29861 45365 2918 2121 -7825 N

ATOM 4270 CA VAL C 136 -73.538 47.480 9.703 1.00263.61 C

ANISOU 4270 CA VAL C 136 25023 29852 45285 2947 2252 -7947 C

ATOM 4271 CB VAL C 136 -74.773 47.895 8.843 1.00252.81 C

ANISOU 4271 CB VAL C 136 23689 28538 43829 2959 2456 -8087 C

ATOM 4272 CGl VAL C 136 -74.786 49.397 8.597 1.00242.81 C

ANISOU 4272 CGl VAL C 136 22255 27360 42642 3016 2558 -8228 C

ATOM 4273 CG2 VAL C 136 -74.795 47.148 7.508 1.00246.47 C

ANISOU 4273 CG2 VAL C 136 , 22990 27522 43136 3104 2568 -8058 C

ATOM 4274 C VAL C 136 -73.587 48.144 11.103 1.00261.73 C

ANISOU 4274 C VAL C 136 24714 29799 44934 2780 2123 -7944 C

ATOM 4275 O VAL C 136 -73.818 47.473 12.113 1.00254.06 O

ANISOU 4275 O VAL C 136 23822 28864 43846 2620 1953 -7861 O

ATOM 4276 N THR C 137 -73.373 49.461 11.141 1.00301.09 N

ANISOU 4276 N THR C 137 29555 34894 49950 2815 2187 -8032 N

ATOM 4277 CA THR C 137 -73.170 50.231 12.381 1.00301.79 C

ANISOU 4277 CA THR C 137 29558 35126 49984 2712 2066 -8009 C

ATOM 4278 CB THR C 137 -72.600 51.640 12.055 1.00294.30 C

ANISOU 4278 CB THR C 137 28462 34269 49091 2815 2137 -8103 C

ATOM 4279 OGl THR C 137 -71.920 51.608 10.793 1.00282.10 O

ANISOU 4279 OGl THR C 137 26869 32589 47726 2996 2267 -8147 O

ATOM 4280 CG2 THR C 137 -71.635 52.106 13.138 1.00291.86 C

ANISOU 4280 CG2 THR C 137 28057 33973 48865 2815 1998 -7990 C

ATOM 4281 C THR C 137 -74.422 50.379 13.279 1.00300.72 C

ANISOU 4281 C THR C 137 29492 35199 49570 2485 1980 -8035 C

ATOM 4282 O THR C 137 -75.349 49.571 13.185 1.00294.14 O

ANISOU 4282 O THR C 137 28792 34367 48601 2368 1931 -8000 O

ATOM 4283 N LEU C 138 -74.428 51.400 14.151 1.00268.00 N

ANISOU 4283 N' LEU C 138 25258 31239 45331 2426 1940 -8087 N

ATOM 4284 CA LEU C 138 -75.558 51.700 15.061 1.00261.53 C

ANISOU 4284 CA LEU C 138 24470 30666 44233 2228 1872 -8144 C

ATOM 4285 CB LEU C 138 -75.636 50.675 16.207 1.00263.55 C

ANISOU 4285 CB LEU C 138 24795 30912 44430 2037 1687 -8012 C

ATOM 4286 CG LEU C 138 -77.020 50.241 16.724 1.00261.72 C

ANISOU 4286 CG LEU C 138 24672 30871 43900 1817 1630 -8047 C

ATOM 4287 CDl LEU C 138 -77.750 49.360 15.708 1.00262.77 C

ANISOU 4287 CDl LEU C 138 24954 30873 44015 1820 1651 -8000 C

ATOM 4288 CD2 LEU C 138 -76.930 49.527 18.074 1.00260.82 C

ANISOU 4288 CD2 LEU C 138 24565 30848 43688 1590 1424 -7965 C

ATOM 4289 C LEU C 138 -75.528 53.146 15.624 1.00255.50 C

ANISOU 4289 C LEU C 138 23587 30090 43403 2247 1850 -8226 C

ATOM 4290 O LEU C 138 -75.179 54.088 14.911 1.00250.20 O

ANISOU 4290 O LEU C 138 22853 29445 42767 2377 1947 -8342 O

ATOM 4291 N GLY C 139 -75.907 53.326 16.891 1.00259.41 N

ANISOU 4291 N GLY C 139 24059 30712 43794 2111 1703 -8168 N

ATOM 4292 CA GLY C 139 -75.896 54.656 17.497 1.00254.74 C

ANISOU 4292 CA GLY C 139 23368 30282 43140 2146 1644 -8212 C

ATOM 4293 C GLY C 139 -76.917 54.978 18.591 1.00253.98 C

ANISOU 4293 C GLY C 139 23267 30483 42751 1990 1567 -8303 C

ATOM 4294 O GLY C 139 -77.948 54.322 18.713 1.00261.13 O

ANISOU 4294 O GLY C 139 24226 31547 43446 1895 1627 -8430 O

ATOM 4295 N CYS C 140 -76.638 56.015 19.379 1.00260.14 N

ANISOU 4295 N CYS C 140 23985 31341 43514 1970 1431 -8232 N

ATOM 4296 CA CYS C 140 -77.500 56.398 20.502 1.00253.99 C

ANISOU 4296 CA CYS C 140 23187 30852 42464 1833 1333 -8306 C

ATOM 4297 CB CYS C 140 ' -77.282 55.445 21.692 1.00250.71 C

ANISOU 4297 CB CYS C 140 22821 30419 42019 1608 1214 -8172 C

ATOM 4298 SG CYS C 140 -78.051 55.880 23.306 1.00231.43 S

ANISOU 4298 SG CYS C 140 20327 28222 39383 1465 1036 -8149 S

ATOM 4299 C CYS C 140 -77.260 57.850 20.935 1.00252.71 C

ANISOU 4299 C CYS C 140 22942 30805 42270 1944 1230 -8309 C

ATOM 4300 O CYS C 140 -76.806 58.096 22.051 1.00253.83 O

ANISOU 4300 O CYS C 140 23068 30890 42485 1914 1099 -8143 O

ATOM 4301 N LEU C 141 -77.583 58.805 20.062 1.00222.47 N

ANISOU '4301 N LEU C 141 19076 27126 38327 2065 1273 " -8496 N ATOM 4302 CA' LEU C 141 -77.267 60..219 20.301 1.00219.94 C

ANISOU 4302 CA LEU C 141 18693 26917 37958 2193 1143 -8508 C

ATOM 4303 CB LEU C 141 -77.825 61. 106 19.178 1 00214.75 C

ANISOU 4303 CB LEU C 141 18015 26391 37190 2307 1194 -8758 C

ATOM 4304 CG LEU C 141 -77.432 62. 592 19.252 1 00215.71 C

ANISOU 4304 CG LEU C 141 18088 26639 37232 2449 1027 -8807 C

ATOM 4305 CDl LEU C 141 -76.102 62.847 18.561 1 00213.77 C

ANISOU 4305 CDl LEU C 141 17820 26169 37234 2601 999 -8653 C

ATOM 4306 CD2 LEU C 141 -78.505 63.515 18..689 1 00226..43 C

ANISOU 4306 CD2 LEU C 141 19444 28206 38384 2474 1043 -9120 C

ATOM 4307 C LEU C 141 -77.705 60.770 21..669 1 00225..77 C

ANISOU 4307 C LEU C 141 19411 27876 38495 2100 974 -8475 C

ATOM 4308 O LEU C 141 -78.505 60.162 22..380 1 00227..00 O

ANISOU 4308 O LEU C 141 19585 28171 38492 1921 972 -8513 O

ATOM 4309 N VAL C 142 -77.148 61.932 22..011 1 00240..70 N

ANISOU 4309 N VAL C 142 21268 29797 40391 2221 818 -8390 N

ATOM 4310 CA VAL C 142 -77.442 62.668 23..241 1. 00242..27 C

ANISOU 4310 CA VAL C 142 21450 30192 40409 2175 636 -8342 C

ATOM 4311 CB VAL C 142 -76.511 62.231 24..409 1, 00238..21 C

ANISOU 4311 CB VAL C 142 20963 29463 40082 2084 555 -8042 C

ATOM 4312 CGl VAL C 142 -76.372 63.331 25..444 1, 00235..35 C

ANISOU 4312 CGl VAL C 142 20591 29263 39570 2078 354 -7958 C

ATOM 4313 CG2 VAL C 142 -77.009 60.938 25..055 1. 00236..62 C

ANISOU 4313 CG2 VAL C 142 20797 29183 39923 1857 647 -8022 C

ATOM 4314 C VAL C 142 -77.273 64.169 22..953 1.00243..74 C

ANISOU 4314 C VAL C 142 21610 30510 40491 2368 478 -8393 C

ATOM 4315 O VAL C 142 -76.445 64.553 22..127 1.00241.62 O

ANISOU 4315 O VAL C 142 21340 30083 40380 2517 467 -8324 O

ATOM 4316 N LYS C 143 -78.071 65.010 23.612 1. 00250.22 N

ANISOU 4316 N LYS C 143 22410 31634 41028 2363 336 -8520 N

ATOM 4317 CA LYS C 143 -77.998 66.467 23.425 1, 00248.72 C

ANISOU 4317 ' CA LYS C 143 22210 31605 40687 2542 142 -8601 C

ATOM 4318 CB LYS C 143 -78.637 66.885 22.088 1.00243.63 C

ANISOU 4318 CB LYS C 143 21555 31080 39933 2599 215 -8922 C

ATOM 4319 CG LYS C 143 -78.541 68.383 21.759 1.00240.50 C

ANISOU 4319 CG LYS C 143 21160 30845 39374 2766 -16 -9043 C

ATOM 4320 CD LYS C 143 -77.292 68.734 20.9'43 1.00241.18 C

ANISOU 4320 CD LYS c- 143 21262, 30700 39676 2905 -77 -8870 C

ATOM 4321 CE LYS C 143 -77.286 70.214 20.555 1.00239.46 C

ANISOU 4321 CE LYS G 143 21058 30656 39269 3050 -342 -9009 C

ATOM 4322 NZ LYS C 143 -76.037 70.630 19.859 1. 00235.28 N

ANISOU 4322 NZ LYS C 143 20545 29939 38911 3176 -453 -8793 N

ATOM 4323 C LYS C 143 -78.623 67.251 24.592 1. 00245.57 C

ANISOU 4323 C LYS C 143 21800 31486 40019 2539 -72 -8616 C

ATOM 4324 O LYS C 143 -79.733 66.955 25.041 1.00243.94 O

ANISOU 4324 O LYS C 143 21570 31468 39647 2391 -38 -8713 O

ATOM 4325 N GLY C 144 -77.888 " 68.245 25.081 1. 00272.13 N

ANISOU 4325 N GLY C 144 25184 34883 43330 2706 -309 -8508 N

ATOM 4326 CA GLY C 144 -78.368 69.110 26.141 1. 00273.58 C

ANISOU 4326 CA GLY C 144 25368 35325 43255 2746 -546 -8508 C

ATOM • 4327 C GLY C 144 -78.202 68.568 27.550 1. 00279.45 C

ANISOU 4327 C GLY C 144 26120 36000 44057 2623 -576 -8256 C

ATOM 4328 O GLY C 144 -79.173 68. 107 28. 152 1.00279.07 O

ANISOU 4328 O GLY C 144 26034 36185 43814 2493 -574 -8380 O

ATOM 4329 N TYR C 145 -76.974 68. 616 28. 071 1.00226.91 N

ANISOU 4329 N TYR C 145 19518 29025 37672 * 2651 -607 -7907 N

ATOM 4330 CA TYR C 145 -76.704 68.350 29. 490 1.00219.83 C

ANISOU 4330 CA TYR C 145 18656 28019 36852 2558 -692 -7630 C

ATOM 4331 CB TYR C 145 -76.386 66.878 29.736 1. 00217.54 C

ANISOU 4331 CB TYR C 145 18374 27441 36841 2338 -489 -7495 C

ATOM 4332 CG TYR C 145 -75.138 66.380 29.054 1. 00221.70 C

ANISOU 4332 CG TYR C 145 18938 27594 37703 2393 -377 -7311 C

ATOM 4333 CDl TYR C 145 -73.908 66.450 29.686 1. 00219.72 C

ANISOU 4333 CDl TYR C 145 18757 27010 37715 2404 -439 -6955 C

ATOM 4334 CEl TYR C 145 -72.761 65.985 29. 072 1.00217.33 C

ANISOU 4334 CEl TYR C 145 18481 26387 37708 2460 -341 -6796 C

ATOM 4335 CZ TYR C 145 -72.836 65.435 27. 815 1. 00217.07 C

ANISOU 4335 CZ TYR C 145 18402 26364 37712 2507 -179 -6992 C

ATOM 4336 OH TYR C 145 -71.694 64.976 27.214 1. 00217.52 O

ANISOU 4336 OH TYR C 145 18473 26125 38050 2570 -87 -6844 O

ATOM 4337 CE2 TYR C 145 -74.044 65.346 27.162 1. 00220.19 C

ANISOU 4337 CE2 TYR C 145 18738 27059 ' 37866 2491 -110 -7334 C

ATOM 4338 CD2 TYR C 145 -75.190 65.816 27.785 1. 00225.51 C

ANISOU 4338 CD2 TYR C 145 19389 28050 38243 2432 -208 -7492 C

ATOM 4339 C TYR C 145 -75.547 69.237 29.917 1. 00214.57 C

ANISOU 4339 C TYR C 145 18069 27182 36276 2747 -909 -7312 C

ATOM 4340 O TYR C 145 -74.906 69.826 29.050 1. 00213.24 O ANISOU 4340 O TYR C 145 17920 26977 36124 2924 -974 -7308 O

ATOM 4341 N PHE C 146 -75.280 69.359 31.222 1.00230.58 N

ANISOϋ 4341 N PHE C 146 20150 29107 38353 2705 -1033 -7040 N

ATOM 4342 CA PHE C 146 -74.217 70.283 31.661 1.00232.39 C

ANISOϋ 4342 CA PHE C 146 20478 29174 38646 2893 -1261 -6702 C

ATOM 4343 CB PHE C 146 -74.772 71.651 32.064 1.00228.07 C

ANISOU 4343 CB PHE C 146 19954 28952 37751 3058 -1559 -6757 C

ATOM 4344 CG PHE C 146 -73.760 72.761 31.957 1.00226.07 C

ANISOU 4344 CG PHE C 146 19817 28571 37507 3288 -1826 -6435 C

ATOM 4345 CDl PHE C 146 -73.611 73.472 30.777 1.00224.27 C

ANISOU 4345 CDl PHE C 146 19606 28397 37211 3470 -1930 -6495 C

ATOM 4346 CEl PHE C 146 -72.678 74.490 30.675 1.00217.37 C

ANISOU 4346 CEl PHE C 146 18846 27430 36313 3671 -2204 -6186 C

ATOM 4347 CZ PHE C 146 -71.883 74.805 31.754 1.00211.87 C

ANISOU 4347 CZ PHE C 146 18262 26562 35677 3707 -2362 -5796 C

ATOM 4348 CE2 PHE C 146 -72.019 74.104 32.932 1.00215.15 C

ANISOU 4348 CE2 PHE C 146 18663 26897 36187 3525 -2243 -5737 C

ATOM 4349 CD2 PHE C 146 -72.949 73.085 33.030 1.00220.92 C

ANISOU 4349 CD2 PHE C 146 19268 27744 36927 3309 -1984 -6063 C

ATOM 4350 C PHE C 146 -73.156 69.806 32.678 1.00236.19 C

ANISOU 4350 C PHE C 146 21049 29252 39440 2812 -1259 -6285 C

ATOM 4351 O PHE C 146 -71.983 69.670 32.319 1.00239.04 O

ANISOU 4351 O PHE C 146 21465 29311 40048 2888 -1231 -6050 O

ATOM 4352 N PRO C 147 -73.535 69.586 33.948 1.00268.50 N

ANISOU 4352 N PRO C 147 25159 33333 43524 2656 -1298 -6191 N

ATOM 4353 CA PRO C 147 -72.454 69.168 34.855 1.00269.87 C

ANISOU 4353 CA PRO C 147 25436 33075 44026 2571 -1301 -5792 C

ATOM 4354 CB PRO C 147 -73.183 68.879 36.166 1.00268.17 C

ANISOU 4354 CB PRO C 147 25216 32929 43748 2356 -1337 -5791 C

ATOM 4355 CG PRO C 147 -74.508 69.589 36.036 1.00267.83 C

ANISOU 4355 CG PRO C 147 25082 33395 43287 2425 -1436 -6120 C

ATOM 4356 CD PRO C 147 -74.857 69.511 34.586 1.00265.95 C

ANISOU 4356 CD PRO C 147 24763 33340 42945 2513 -1314 -6430 C

ATOM 4357 C PRO C 147 -71.836 67.905 34.276 1.00272.19 C

ANISOU 4357 C PRO C 147 25718 33053 44648 2435 -1058 -5774 C

ATOM 4358 O PRO C 147 -72.554 66.929 34.082 1.00277.41 O

ANISOU 4358 O PRO C 147 26298 33816 45291 2257 -884 -6039 O

ATOM 4359 N GLU C 148 -70.534 67.920 34.011 1.00252.35 N

ANISOU 4359 N GLU C 148 23290 30175 42415 2520 -1061 -5463 N

ATOM 4360 CA GLU C 148 -70.010 67.161 32.875 1.00252.30 C

ANISOU 4360 CA GLU C 148 23256 29953 42653 2496 -862 -5497 C

ATOM 4361 CB GLU C 148 -69.036 68.045 32.089 1.00252.02 C

ANISOU 4361 CB GLU C 148 23269 29786 42702 2747 -942 -5280 C

ATOM 4362 CG GLU C 148 -69.178 67.948 30.577 1.00251.05 C

ANISOU 4362 CG GLU C 148 23054 29890 42445 2886 -874 -5554 C

ATOM 4363 CD GLU C 148 -69.214 66.515 30.076 1.00254.42 C

ANISOU 4363 CD GLU C 148 23405 30219 43045 2751 -609 -5759 C

ATOM 4364 OEl GLU C 148 -70.205 65.809 30.353 1.00253.41 O

ANISOU 4364 OEl GLU C 148 23237 30165 42881 2549 -497 -5954 O

ATOM 4365 0E2 GLU C 148 -68.257 66.095 29.393 1.00254.43 O

ANISOU 4365 0E2 GLU C 148 23389 30079 43203 2848 -527 -5719 O

ATOM 4366 C " GLU C 148 -69.394 65.763 33.072 1.00249.73 C

ANISOU 4366 C GLU C 148 22957 29272 42658 2249 -702 -5413 C

ATOM 4367 O GLU C 148 -68.232 65.550 32.739 1.00255.44 O

ANISOU 4367 O GLU C 148 23746 29635 43673 2278 -671 -5163 O

ATOM 4368 N PRO C 149 -70.163 64.807 33.608 1.00229.06 N

ANISOU 4368 N PRO C 149 20292 26761 39980 2000 -621 -5623 N

ATOM 4369 CA PRO C 149 -69.777 63.420 33.319 1.00230.26 C

ANISOU 4369 CA PRO C 149 20444 26664 40380 1798 -458 -5669 C

ATOM 4370 CB PRO C 149 -70.016 62.697 34.650 1.00235.24 C

ANISOU 4370 CB PRO C 149 21117 27209 41056 1494 -511 -5626 C

ATOM 4371 CG PRO C 149 -70.306 63.789 35.662 1.00235.26 C

ANISOU 4371 CG PRO C 149 21154 27340 40895 1571 -693 -5481 C

ATOM 4372 CD PRO C 149 -70.897 64.905 34.875 1.00234.81 C

ANISOU 4372 CD PRO C 149 21026 27654 40539 1849 -733 -5643 C

ATOM 4373 C PRO C 149 -70.655 62.818 32.214 1.00235.39 C

ANISOU 4373 C PRO C 149 20992 27567 40877 1785 -303 -6023 C

ATOM 4374 O PRO C 149 -70.581 63.289 31.083 1.00233.70 O

ANISOU 4374 O PRO C 149 20728 27508 40558 2001 -265 -6136 O

ATOM 4375 N VAL C 150 -71.475 61.822 32.561 1.00229.24 N

ANISOU 4375 N VAL C 150 20197 26823 40081 1521 -233 -6183 N

ATOM 4376 CA VAL C 150 -72.340 61.048 31.640 1.00230.02 C

ANISOU 4376 CA VAL C 150 20227 27127 40042 1459 -91 -6486 C

ATOM 4377 CB VAL C 150 -72.641 61.762 30.289 1.00226.50 C

ANISOU 4377 CB VAL C 150 19712 26923 39424 1719 -19 -6672 C

ATOM 4378 CGl VAL C 150 -73.346 60.824 29.321 1.00225.06 C

ANISOU 4378 CGl VAL C 150 19491 26838 39185 1653 146 -6924 C ATOM 4379 CG2 VAL C 150 -73.490 62.993 30.517 1.00229.57 C

ANISOU 4379 CG2 VAL C 150 20055 27687 39483 1811 -133 -6794 C

ATOM 4380 C VAL C 150 -71.734 59.662 31.416 1.00231.93 C

ANISOU 4380 C VAL C 150 20516 27045 40563 1319 2 -6442 C

ATOM 4381 O VAL C 150 -70.568 59.439 31.744 1.00232.23 O

ANISOU 4381 O VAL C 150 20621 26718 40896 1332 -26 -6203 O

ATOM 4382 N THR C 151 -72.515 58.724 30.888 1.00248.82 N

ANISOU 4382 N THR C 151 22631 29308 42601 1182 93 -6662 N

ATOM 4383 CA THR C 151 -71.994 57.377 30.684 1.00254.70 C

ANISOU 4383 CA THR C 151 23434 29760 43580 1044 139 -6630 C

ATOM 4384 CB THR C 151 -71.695 56.691 32.033 1.00257.73 C

ANISOU 4384 CB THR C 151 23901 29910 44115 740 7 -6488 C

ATOM 4385 OGl THR C 151 -71.477 55.293 31.821 1.00260.81 O

ANISOU 4385 OGl THR C 151 24347 30128 44621 553 15 -6548 O

ATOM 4386 CG2 THR C 151 -72.851 56.871 32.992 1.00257.04 C

ANISOU 4386 CG2 THR C 151 23787 30115 43761' 539 -90 -6573 C

ATOM 4387 C THR C 151 -72.871 56.455 29.835 1.00255.22 C

ANISOU 4387 C THR C 151 23483 29980 43508 977 243 -6865 ' C

ATOM 4388 O THR C 151 -73.709 55.731 30.366 1.00259.06 O

ANISOU 4388 O THR C 151 23996 30564 43871 715 192 -6956 O

ATOM 4389 N VAL C 152 -72.659 56.476 28.520 1.00225.18 N

ANISOU 4389 N VAL C 152 19644 26189 39727 1203 377 -6947 N

ATOM 4390 CA VAL C 152 -73.310 55.532 27.612 1.00228.38 C

ANISOU 4390 CA VAL C 152 20056 26674 40043 1165 482 -7129 C

ATOM 4391 CB VAL C 152 -73.035 55.881 26.130 1.00219.68 C

ANISOU 4391 CB VAL ■c 152 18906 25591 38971 1444 634 -7215 C

ATOM 4392 CGl VAL C 152 -73.732 54.896 25.201 1.00217.42 C

ANISOU 4392 CGl VAL C 152 18650 25353 38606 1398 739 -7375 C

ATOM 4393 CG2 VAL C 152 -73.466 57.309 25.825 1.00213.59 C

ANISOU 4393 CG2 VAL C 152 18061 25105 37989 1604 648 -7319 C

ATOM 4394 C VAL C 152 -72.813 54.117 27.904 1.00232.26 C

ANISOU 4394 C VAL C 152 20636 26879 40733 986 433 -7056 C

ATOM 4395 O VAL C 152 -71.698 53.938 28.388 1.00232.03 O

ANISOU 4395 O VAL C 152 20647 26525 40988 ' 1002 383 -6878 O

ATOM 4396 N THR C 153 -73.641 53.116 27.621 1.00274.79 N

ANISOU 4396 N THR C 153 26064 32387 45957 812 429 -7191 N

ATOM 4397 CA THR C 153 -73.274 51.729 27.884 1.00281.14 C

ANISOU 4397 CA THR C 153 26969 32961 46890 597 320 -7140 C

ATOM 4398 CB THR C 153 -73.369 51.398 29.383 1.00280.03 C

ANISOU 4398 CB THR C 153 26872 32791 46734 278 130 -7068 C

ATOM 4399 OGl THR C 153 -73.278 52.602 30.152 1.00274.51 O

ANISOU 4399 , OGl THR C 153 26118 32101- 46083 352 118 -6959 O

ATOM 4400 CG2 THR C 153 -72.254 50.454 29.794 1.00283.06 C

ANISOU 4400 CG2 THR C 153 27365 32800 47386 106 -7 -6959 C

ATOM 4401 C THR C 153 -74.204 50.786 27.139 1.00286.92 C

ANISOU 4401 C THR C 153 27749 33854 47412 511 344 -7292 C

ATOM 4402 O THR C 153 -75.279 50.457 27.636 1.00291.94 O

ANISOU 4402 O THR C 153 28415 34704 47806 260 247 -7365 O

ATOM 4403 N TRP C 154 -73.792 50.344 25.956 1.00303.79 N

ANISOU 4403 N TRP C 154 29900 35892 49635 713 464 -7327 N

ATOM 4404 CA TRP C 154 -74.652 49.499 25.135 1.00304.99 C

ANISOU 4404 CA TRP C 154 30110 36191 49583 678 507 -7450 C

ATOM 4405 CB TRP C 154 -74.032 49.230 23.770 1.00302.28 C

ANISOU 4405 CB TRP C 154 29779 35669 49403 936 642 -7455 C

ATOM 4406 CG TRP C 154 -74.547 50.176 22.770 1.00300.11 C

ANISOU 4406 CG TRP C 154 29421 35571 49036 1164 845 -7565 C

ATOM 4407 CDl TRP C 154 -75.677 50.042 22.026 1.00299.51 C

ANISOU 4407 CDl TRP C 154 29366 35716 48718 1172 947 -7703 C

ATOM 4408 NEl TRP C 154 -75.843 51.137 21.220 1.00293.29 N

ANISOU 4408 NEl TRP C 154 28490 35018 47929 1392 1113 -7794 . N

ATOM 4409 CE2 TRP C 154 -74.813 52.009 21.446 1.00292.35 C

ANISOU 4409 CE2 TRP C 154 28290 34759 48029 1533 1106 -7705 C

ATOM 4410 CD2 TRP C 154 -73.982 51.437 22.424 1.00295.36 C

ANISOU 4410 CD2 TRP C 154 28713 34938 48572 1400 951 -7550 C

ATOM 4411 CE3 TRP C 154 -72.848 52.134 22.839 1.00289.85 C

ANISOU 4411 CE3 TRP C 154 27962 34056 48112 1505 915 -7413 . C

ATOM 4412 CZ3 TRP C 154 -72.583 53.357 22.271 1.00286.45 C

ANISOU 4412 CZ3 TRP C 154 27439 33674 47726 1734 1014 -7427 C

ATOM 4413 CH2 TRP C 154 -73.427 53.901 21.298 1.00285.29 C

ANISOU 4413 CH2 TRP C 154 27249 33740 47407 1850 1147 -7601 C

ATOM 4414 CZ2 TRP C 154 -74.545 53.243 20.874 1.00287.92 C

ANISOU 4414 CZ2 TRP C 154 27635 34232 47531 1752. 1204 -7744 C

ATOM 4415 C TRP C 154 -75.066 48.198 25.804 * 1.00310.39 C

ANISOU 4415 C TRP C 154 30911 36892 50130 360 311 -7451 ' C

ATOM 4416 O TRP C 154 -74.227 47.349 .26.115 1.00308.52

ANISOU 4416 O TRP C 154 30764 36387 50073 269 172 -7371 O

ATOM 4417 N ASN C 155 -76.375 48.062 26.006 ' 1.00297.56 N ANISOU 4417 N ASN C 155 29289 35602 48169 191 286 -7550 N

ATOM 4418 CA ASN C 155 -76.955 46.898 26.660 1.00298.86 C

ANISOCI 4418 CA ASN C 155 29555 >35870 48127 -149 74 -7558 C

ATOM 4419 CB ASN C 155 -76.632 45.632 25.860 1.00299.65 C

ANISOO 4419 CB ASN C 155 29797 35802 48255 -152 O -7533 C

ATOM 4420 CG ASN C 155 -77.739 44.599 25.920 1.00297.23 C

ANISOU 4420 CG ASN C 155 29593 35760 47581 -391 -128 -7584 C

ATOM 4421 ODl ASN C 155 -77.703 43.598 25.207 1.00290.42 O

ANISOU 4421 ODl ASN C 155 28835 34872 46638 -316 -118 -7581 O

ATOM 4422 ND2 ASN C 155 -78.733 44.839 26.765 1.00302.18 N

ANISOU 4422 ND2 ASN C 155 30193 36650 47971 -676 -255 -7619 N

ATOM 4423 C ASN C 155 -76.406 46.799 28.077 1.00296.67 C

ANISOU 4423 C ASN C 155 29286 35466 47969 -408 -129 -7474 C

ATOM 4424 O ASN C 155 -76.136 45.707 28.574 1.00299.86 O

ANISOU 4424 O ASN C 155 29799 35765 48368 -679 -353 -7442 O

ATOM 4425 N SER C 156 -76.251 47.954 28.720 1.00267.06 N

ANISOU 4425 N SER C 156 25430 31718 44322 -327 -65 -7437 N

ATOM 4426 CA SER C 156 -75.530 48.047 29.983 1.00264.28 C

ANISOU 4426 CA SER C 156 25089 31166 44160 -518 -222 -7325 C

ATOM 4427 CB SER C 156 -76.265 47.290 31.089 1.00264.87 C

ANISOU 4427 CB SER C 156 25199 31449 43990 -920 -431 -7370 C

ATOM 4428 OG SER C 156 -75.772 47.650 32.365 1.00264.55 O

ANISOU 4428 OG SER C 156 25161 31223 44132 -1108 -564 -7268 O

ATOM 4429 C SER C 156 -74.107 47.515 29.792 1.00264.11 C

ANISOU 4429 C SER C 156 25159 30701 44488 -503 -304 -7215 C

ATOM 4430 O SER C 156 -73.329 48.078 29.024 1.00262.52 O

ANISOU 4430 O SER C 156 24929 30299 44518 -208 -166 -7159 O

ATOM 4431 N GLY C 157 -73.772 46.420 30.466 1.00281.77 N

ANISOU 4431 N GLY C 157 27509 32797 46753 -827 -545 -7197 N

ATOM 4432 CA GLY C 157 -72.444 45.840 30.347 1.00285.06 C

ANISOU 4432 CA GLY C 157 28026 32791 47493 -846 -661 -7115 C

ATOM 4433 C GLY C 157 -72.362 44.637 29.423 1.00282.88 C

ANISOU 4433 C GLY C 157 27848 32455 47179 -780 -710 -7170 C

ATOM 4434 O GLY C 157 -71.669 43.664 29.723 1.00277.98 O

ANISOU 4434 O GLY C 157 27360 31674 46586 -1020 -958 -7176 O

ATOM 4435 N SER C 158 -73.060 44.705 28.293 1.00296.45 N

ANISOU 4435 N SER C 158 29511 34294 48834 -458 -489 -7210 N

ATOM 4436 CA SER C 158 -73.099 43.598 27.339 1.00297.98 C

ANISOU 4436 CA SER C 158 29798 34440 48979 -357 -513 -7250 C

ATOM 4437 CB SER C 158 -74.529 43.352 26.852 1.00302.85 C

ANISOU 4437 CB SER C 158 30422 35427 49220 -359 -438 -7342 C

ATOM 4438 OG SER C 158 -75.407 43.071 27.929 1.00298.76 O

ANISOU 4438 OG SER C 158 29946 35153 48415 -719 -626 -7380 O

ATOM 4439 C SER C 158 -72.185 43.846 26.144 1.00293.44 C

ANISOU 4439 C SER C 158 29175 33642 48676 22 -326 -7210 C

ATOM 4440 O SER C 158 -71.123 43.233 26.028 1.00291.89 O

ANISOU 4440 O SER C 158 29018 33120 48767 58 -411 -7144 O

ATOM 4441 N LEU C 159 -72.611 44.731 25.247 1.00272.06 N

ANISOU 4441 N LEU C 159 26384 31112 45873 292 -81 -7261 N

ATOM 4442 CA LEU C 159 -71.777 45.119 24.120 1.00270.44 C

ANISOU 4442 CA LEU C 159 26115 30740 45901 644 107 -7235 C

ATOM 4443 CB LEU C 159 -72.540 46.012 23.149 1.00267.11 C

ANISOU 4443 CB LEU C 159 25589 30561 45339 872 367 -7313 C

ATOM 4444 CG LEU C 159 -73.163 45.262 21.976 1.00269.13 C

ANISOU 4444 CG LEU C 159 25909 30934 45413 963 450 -7393 C

ATOM 4445 CDl LEU C 159 -73.938 46.226 21.112 1.00272.37 C

ANISOU 4445 CDl LEU C 159 26224 31601 45662 1101 678 -7490 C

ATOM 4446 CD2 LEU C 159 -72.094 44.545 21.164 1.00265.76 C

ANISOU 4446 CD2 LEU C 159 25519 30251 45205 1192 486 -7361 C

ATOM 4447 C LEU C 159 -70.545 45.843 24.626 1.00274.20 C

ANISOU 4447 C LEU C 159 26523 30975 46686 709 110 -7126 C

ATOM 4448 O LEU C 159 -70.648 46.769 25.430 1.00273.42 O

ANISOU 4448 O LEU C 159 26364 30950 46575 617 112 -7085 O

ATOM 4449 N SER C 160 -69.381 45.409 24.148 1.00276.73 N

ANISOU 4449 N SER C 160 26860 31009 47275 870 101 -7070 N

ATOM 4450 CA SER C 160 -68.103 45.959 24.585 1.00269.56 C

ANISOU 4450 CA SER C 160 25891 29860 46669 972 123 -6947 C

ATOM 4451 CB SER C 160 -67.268 44.877 25.280 1.00263.19 C

ANISOU 4451 CB SER C 160 25200 28728 46073 770 -116 -6883 C

ATOM 4452 OG SER C 160 -67.280 43.660 24.547 1.00259.78 O

ANISOU 4452 OG SER C 160 24881 28212 45612 733 -257 -6957 O

ATOM 4453 C SER C 160 -67.320 46.563 23.423 1.00266.58 C

ANISOU 4453 C SER C 160 25415 29425 46449 1339 323 -6929 C

ATOM 4454 O SER C 160 -66.831 47.694 23.518 1.00260.27 O

ANISOU 4454 O SER C 160 24521 28579 45792 1487 420 -6835 O

ATOM 4455 N SER C 161 -67.215 45.806 22.329 1.00295.87 N

ANISOU 4455 N SER C 161 29152 33150 50114 1479 372 -7011 N ATOM 4456 CCAA SER C 161 -66.402 46.204 21.179 1.00296.57 C

ANISOU 4456 CCAA SER C 161 29154 33164 50365 1807 536 -7004 C

ATOM 4457 CCBB SER C 161 -65.500 45.050 20 ,721 1.00300.56 C

ANISOO 4457 CCBB SER C 161 29744 33440 51017 1870 421 -7010 C

ATOM 4458 OOGG SER C 161 -64.418 45.523 19.932 1.00305.65 O

ANISOU 4458 OOGG SER C 161 30286 33987 51860 2171 558 -6982 O

ATOM 4459 CC SER C 161 -67.231 46.727 20 ,005 1, .00291.85 C

ANISOU 4459 CC SER C 161 28480 32806 49604 1993 755 -7103 C

ATOM 4460 OO SER C 161 -68.443 46..518 19 939 1..00291.03 O

ANISOU 4460 OO SER C 161 28418 32912 49248 1882 776 -7191 O

ATOM 4461 NN GLY C 162 -66.555 47..398 19 077 1..00237.98 N

ANISOU 4461 NN GLY C 162 21548 25943 42929 2266 910 -7091 N

ATOM 4462 CCAA GLY C 162 -67.209 48..111 17 997 1..00231.22 C

ANISOU 4462 CCAA GLY C 162 20610 25281 41963 2436 1114 -7187 C

ATOM 4463 CC GLY C 162 -67.651 49..465 18, 504 1..00226..59 C

ANISOU 4463 CC GLY C 162 19950 24895 41250 2379 1160 -7191 C

ATOM 4464 OO GLY C 162 -68.115 50..309 17, 745 1..00226..81 O

ANISOU 4464 OO GLY C 162 19903 25093 41183 2497 1304 -7278 O

ATOM 4465 NN VAL C 163 -67.464 49..669 19.803 1. .00254..64 N

ANISOU 4465 NN VAL C 163 23532 28413 44808 2193 1020 -7099 N

ATOM 4466 CCAA VAL C 163 -68.043 50..793 20.527 1. .00254..62 C

ANISOU 4466 CCAA VAL C 163 23484 28604 44656 2107 1016 -7094 C

ATOM 4467 CCBB VAL C 163 -68.283 50..406 21.992 1. .00254..93 C

ANISOU 4467 CCBB VAL C 163 23607 28615 44640 1816 836 -7036 C

ATOM 4468 CGl VAL C 163 -69.074 51..493 22.706 1. .00250..07 C

ANISOU 4468 CGl VAL C 163 22942 28212 43862 1744 827 -7030 C

ATOM 4469 CG2 VAL C 163 -69.000 49..070 22.063 1..00263..29 C

ANISOU 4469 CG2 VAL C 163 24776- 29733 45531 1626 763 -7135 C

ATOM 4470 C VAL C 163 -67.204 52..070 20.519 1..00253..77 C

ANISOU 4470 C VAL C 163 23275 28467 44678 2271 1047 -6980 C

ATOM 4471 O VAL C 163 -66.462 52..333 21.462 1..00256..86 . O

ANISOU 4471 O VAL C 163 23682 28698 45216 2213 940 -6819 O

ATOM 4472 N HIS 1 C 164 -67.337 52..874 19.471 1. .00266..53 N

ANISOU 4472 N HIS C 164 24801 30235 46233 2461 1176 -7058 N

ATOM 4473 CA HIS C 164 -66.636 54..149 19.417 1. ,00259..81 C

ANISOU 4473 CA HIS C 164 23861 29397 45457 2617 1177 -6952 C

ATOM 4474 CB HIS C 164 -66.283 54.502 17.974 1. .00259..24 C

ANISOU 4474 CB HIS C 164 23702 29355 45444 2846 1308 -7026 C

ATOM 4475 CG HIS C 164 -65.270 53.583 17.367 1. .00271..34 C

ANISOU 4475 CG HIS C 164 25236 30667 47192 2942 1345 -6990 C

ATOM 4476 NDl HIS C 164 -63.914 53.821 17.434 1. .00275..89 N '

ANISOU 4476 NDl HIS C 164 25803 31028 47995 2996 1272 -6809 N

ATOM 4477 CEl HIS' C 164 -63.268 52.842 16.822 1. ,00272..19 C

ANISOU 4477 CEl HIS C 164 25335 30414 47671 3088 1313 -6836 C

ATOM 4478 NE2 HIS C 164 -64.156 51.978 16.367 1. .00274..26 N

ANISOU 4478 NE2 HIS C 164 25614 ' 30780 47812 3099 1413 -7013 N

ATOM 4479 CD2 HIS C 164 -65.417 52.415 16.695 1. ,00271..92 C

ANISOU 4479 CD2 HIS C 164 25326 30702 47290 3004 1441 -7108 C

ATOM 4480 CC HIS C 164 -67.487 55.245 20.033 1. ,00255..48 C

ANISOU 4480 CC HIS C 164 23290 29086 44695 2567 1133 -6979 C

ATOM 4481 OO HIS C 164 -68.153 55.975 19.318 1. ,00254..58 O

ANISOU 4481 OO HIS C 164 23119 29174 44434 2664 1203 -7113 O

ATOM 4482 NN THR C 165 -67.457 55.352 21.359 1. 00257.41 N

ANISOU 4482 NN THR C 165 23583 29296 44924 2413 1004 -6858 N

ATOM 4483 CCAA THR C 165 -68.270 56.326 22.101 1.00255.02 C

ANISOU 4483 CCAA THR C 165 23268 29223 44406 2357 935 -6878 C

ATOM 4484 CCBB THR C 165 -68.481 55.858 23.550 1.,00253.11 C

ANISOU 4484 CCBB THR C 165 23100 28917 44152 2119 804 -6779 C

ATOM 4485 OGl THR C 165 -69.063 54.549 23.554 1. 00258.91 O

ANISOU 4485 OGl THR C 165 23900 29593 44880 1935 810 -6868 O

ATOM 4486 CG2 THR C 165 -69.382 56.821 24.295 1.00248.46 C

ANISOU 4486 CG2 THR C 165 22494 28608 43301 2054 739 -6840 C

ATOM 4487 CC THR C 165 -67.654 57.732 22.136 1.00254.51 C

ANISOU 4487 CC THR C 165 23148 29205 44351 2536 880 -6756 C

ATOM 4488 OO THR C 165 -66.787 58.015 22.960 1.00257.94 O

ANISOU 4488 OO THR C 165 23611 29477 44919 2537 774 -6525 O

ATOM 4489 NN PHE C 166 -68.133 58.620 21.271 1.00236.16 N

ANISOU 4489 N PHE C 166 20759 27096 41876 2672 932 -6905 N

ATOM 4490 CA PHE 166 -67.437 59.880 20.985 1.00232.12 C

ANISOU 4490 CA PHE 166 20198 26645 41351 2850 853 -6806 C

ATOM 4491 CB PHE 166 -68.037 60.540 19.745 1.00230.52 C

ANISOU 4491 CB PHE 166 19934 26680 40973 2952 914 -7046 C

ATOM 4492 CG PHE 166 -67.656 59.853 18.468 1. 00237.52 C

ANISOU 4492 CG PHE 166 20783 27479 41984 3019 1082 -7170 C

ATOM 4493 CDl PHE C 166 -67.097 60.559 17.423 1. 00237.14 C

ANISOU 4493 CDl PHE C 166 20665 27444 41992 3182 1101 -7188 C

ATOM 4494 CEl PHE C 166 -66.738 59.913 16.250 1.00238.04 C ANISOU 4494 CEl PHE C 166 20743 27472 42231 3243 1257 -7298 C

ATOM 4495 CZ PHE C 166 -66.920 58.548 16.120 1.00241.65 C

ANISOU 4495 CZ PHE C 166 21246 27820 4274~9 3159 1383 -7374 C

ATOM 4496 CE2 PHE C 166 -67.461 57.832 17.161 1.00244.06 C

ANISOU 4496 CE2 PHE C 166 • 21629 28117 42984 2993 1345 -7350 C

ATOM 4497 CD2 PHE C 166 -67.824 58.485 18.329 1.00241.79 C

ANISOU 4497 CD2 PHE C 166 21365 27923 42582 2916 1201 -7255 C

ATOM 4498 C PHE C 166 -67.308 60.873 22.140 1.00234.38 C

ANISOU 4498 C PHE C 166 20524 26974 41556 2826 672 -6622 C

ATOM 4499 O PHE C 166 -68.031 60.785 23.126 1.00240.44 O

ANISOU 4499 O PHE C 166 21339 27778 42239 2664 621 -6622 O

ATOM 4500 N PRO C 167 -66.362 61.819 22.020 1.00207.76 N

ANISOU 4500 N PRO C 167 17137 23597 38204 2984 561 -6451 N

ATOM 4501 CA PRO C 167 -66.039 62.737 23.110 1.00208.26 C

ANISOU 4501 CA PRO C 167 17258 23666 38204 2986 372 -6227 C

ATOM 4502 CB PRO C 167 -64.624 63.227 22.758 1.00206.70 C

ANISOU 4502 CB PRO C 167 17063 23299 ' 38175 3147 301 -5955 C

ATOM 4503 CG PRO C 167 -64.188 62.421 21.573 1.00209.22 C

ANISOU 4503 CG PRO C 167 17299 23585 38609 3235 454 -6088 C

ATOM 4504 CD PRO C 167 -65.450 62.012 20.887 1.00209.41 C

ANISOU 4504 CD PRO C 167 17283 23785 38497 3163 589 -6429 C

ATOM 4505 C PRO C 167 -66.978 63.912 23.112 1.00215.58 C

ANISOU 4505 C PRO C 167 18171 24924 38814 3037 251 -6373 C

ATOM 4506 O PRO C 167 -67.333 64.416 22.052 1.00216.04 O

ANISOU 4506 O PRO C 167 18171 25169 38744 3126 280 -6585 O

ATOM 4507 N ALA C 168 -67.357 64.348 24.303 1.00228.61 N

ANISOU 4507 N ALA C 168 19880 26635 40348 2979 103 -6262 N

ATOM 4508 CA ALA C 168 -68.242 65.489 24.465 1.00228.98 C

ANISOU 4508 CA ALA C 168 19921 27005 40075 3017 -38 -6408 C

ATOM 4509 CB ALA C 168 -68.597 65.651 25.931 1.00228.50 C

ANISOU 4509 CB ALA C 168 19926 26948 39944 2914 -166 -6264 C

ATOM 4510 C ALA C 168 -67.664 66.797 23.914 1.00226.57 C

ANISOU 4510 C ALA C 168 19609 26848 39628 3220 -214 -6374 C

ATOM 4511 O ALA C 168 -66.626 67.275 24.369 1.00225.01 O

ANISOU 4511 O ALA C 168 19474 26576 39443 3316 -400 -6084 O

ATOM 4512 N VAL C 169 -68.346 67.372 22.932 1.00243.21 N

ANISOU 4512 N VAL C 169 21655 29162 41592 3272 -174 -6667 N

ATOM 4513 CA VAL C 169 -68.049 68.726 22.492 1.00247.11 C

ANISOU 4513 CA VAL C 169 22148 29848 41896 3426 -381 -6702 C

ATOM 4514 CB VAL C 169 -67.528 68.758 21.050 1.00250.81 C

ANISOU 4514 CB VAL C 169 22544 30320 42432 3480 -269 -6883 C

ATOM 4515 CGl VAL C 169 -68.548 68.14? 20.116 1.00256.47 C

ANISOU 4515 CGl VAL C 169 23211 31118 43118 3370 -44 -7242 C

ATOM 4516 CG2 VAL C 169 -67.195 70.187 20.631 1.00252.74 C

ANISOU 4516 CG2 VAL C 169 22794 30764 42471 3611 -524 -6923 C

ATOM 4517 C VAL C 169 -69.333 69.533 22.603 1.00256.61 C

ANISOU 4517 C VAL C 169 23361 31372 42768 3415 -526 -6943 C

ATOM 4518 O VAL C 169 -70.427 68.992 22.444 1.00261.32 O

ANISOU 4518 O VAL C 169 23929 32074 43285 3293 -389 -7185 O

ATOM 4519 N LEU C 170 -69.206 70.823 22.889 1.00234.85 N

ANISOU 4519 N LEU C 170 20650 28782 39800 3544 -820 -6877 N

ATOM 4520 CA LEU C 170 -70.378 71.656 23.141 1.00237.54 C

ANISOU 4520 CA LEU C no 21009 29434 39810 3554 -1003 -7094 C

ATOM 4521 CB LEU C 170 -70.292 72.323 24.527 1.00233.54 C

ANISOU 4521 CB LEU C 170 20584 28931 39220 3579 -1200 -6821 ' C

ATOM 4522 CG LEU C 170 -69.142 73.278 24.903 1.00225.71 C

ANISOU 4522 CG LEU C 170 19689 27881 38188 3744 -1506 -6457 C

ATOM 4523 CDl LEU C 170 -69.085 74.515 24.020 1.00224.62 C

ANISOU 4523 CDl LEU Ci 170 19584 28045 37716 3881 -1833 -6610 C

ATOM 4524 CD2 LEU C 170 -69.233 73.692 26.371 1.00217.94 . C

ANISOU 4524 CD2 LEU C 170 18792 26787 37230 3731 -1606 -6140 C

ATOM 4525 C LEU C 170 -70.608 72.719 22.073 1.00243.35 C

ANISOU 4525 C LEU C 170 21752 30399 40310 3672 -1246 -7276 C

ATOM 4526 O LEU C 170 -69.685 73.098 21.346 1.00242.38 O

ANISOU 4526 O LEU C 170 21643 30203 40247 3767 -1358 -7128 O

ATOM 4527 N GLN C 171 -71.855 73.177 21.983 1.00302.60 N

ANISOU 4527 N GLN C 171 29249 38186 47538 3654 -1339 -7607 N

ATOM 4528 CA GLN C 171 -72.191 74.422 21.300 1.00302.91 C

ANISOU 4528 CA GLN C 171 29331 38473 47289 3767 -1681 -7752 C

ATOM 4529 CB GLN C 171 -72.561 74.201 19.834 1.00300.75 C

ANISOU 4529 CB GLN C 171 29012 38229 47029 3748 -1635 -8039 C

ATOM 4530 CG GLN C 171 -73.118 75.463 19.185 1.00297.46 C

ANISOU 4530 CG GLN C 171 28657 38046 46318 3850 -2049 -8156 C

ATOM 4531 CD GLN C 171 -72.718 75.609 17.733 1.00297.46 C

ANISOU 4531 CD GLN C 171 28622 38037 46361 3819 -2049 -8377 C

ATOM 4532 OEl GLN C 171 -72.933 74.706 16.923 1.00297.91 O

ANISOU 4532 OEl GLN C 171 28607 37976 46610 3712 -1722 -8577 O ATOM 4533 NE2 GLN C 171 -72.134 76.756 17.393 1.00290.55 N

ANISOU 4533 NE2 GLN C 171 27808 37288 45298 3905 -2435 -8336 N

ATOM 4534 C GLN C 171 -73.341 75.105 22.022 1.00301.69 C

ANISOU 4534 C GLN C 171 29200 38619 46811 3771 -1857 -7979 C

ATOM 4535 O GLN C 171 -74.355 74.476 22.320 1.00301.16 O

ANISOU 4535 O GLN C 171 29082 38628 46718 3655 -1649 -8202 O

ATOM 4536 N SER C 172 -73.176 76.393 22.301 1.00274.48 N

ANISOU 4536 N SER C 172 25834 35354 43100 3910 -2260 -7915 N

ATOM 4537 CA SER C 172 -74.175 77.154 23.037 1.00272.82 C

ANISOU 4537 CA SER C 172 25656 35436 42566 3950 -2484 -8080 C

ATOM 4538 CB SER C 172 -75.454 77.328 22.205 1.00273.17 C

ANISOU 4538 CB SER C 172 25656 35729 42407 3892 -2481 -8600 C

ATOM 4539 OG SER C 172 -76.277. 76.172 22.240 1.00272.56 O

ANISOU 4539 OG SER C 172 25491 35606 42464 3729 -2083 -8811 O

ATOM 4540 C SER C 172 -74.499 76.493 24.374 1.00277.47 C

ANISOU 4540 C SER C 172 26221 35983 43223 3870 -2302 -7950 C

ATOM 4541 O SER C 172 -75.646 76.508 24.816 1.00284.77 O

ANISOU 4541 O SER C 172 27091 37097 44013 3782 -2196 -8236 O

ATOM 4542 N ASP C 173 -73.484 75.911 25.008 1.00250.45 N

ANISOU 4542 N ASP C 173 22841 32306 40013 3885 -2268 -7519 N

ATOM 4543 CA ASP C 173 -73.632 75.246 26.308 1.00249.74 C

ANISOU 4543 CA ASP C 173 22748 32140 40000 3797 -2150 -7341 C

ATOM 4544 CB ASP C 173 -74.312 76.163 27.333 1.00248.49 C

ANISOU 4544 CB ASP C 173 22633 32276 39505 3879 -2446 -7394 C

ATOM 4545 CG ASP C 173 -73.558 77.460 27.545 1.00247.08 C

ANISOU 4545 CG ASP C 173 22573 32196 39109 4099 -2889 -7223 C

ATOM 4546 ODl ASP C 173 -73.741 78.091 28.607 1.00240.83 O

ANISOU 4546 ODl ASP C 173 21858 31500 38146 4195 -3142 -7044 O

ATOM 4547 0D2 ASP C 173 -72.781 77.848 26.648 1.00245.33 O

ANISOU 4547 0D2 ASP C 173 22376 31964 38876 4174 -3002 -7264 O

ATOM 4548 C ASP C 173 -74.354 73.893 26.239 1.00249.27 C

ANISOU 4548 C ASP C 173 22590 32010 40110 3584 -1755 -7525 C

ATOM 4549 O ASP C 173 -74.421 73.171 27.237 1.00237.33 O

ANISOU 4549 O ASP C 173 21074 30392 38709 3471 -1638 -7367 O

ATOM 4550 N LEU C 174 -74.894 73.558 25.067 1.00259.15 N

ANISOU 4550 N LEU C 174 23775 33316 41376 3524 -1571 -7851 N

ATOM 4551 CA LEU C 174 -75.536 72.261 24.855 1.00258.99 C

ANISOU 4551 CA LEU C 174 23679 33226 41500 3336 -1214 -8019 C

ATOM 4552 CB LEU C 174 -76.511 72.308 23.662 1.00258.50 C

ANISOU 4552 CB LEU C 174 23568 33327 41324 3304 -1106 -8441 C

ATOM 4553 CG LEU C 174 -77.915 72.923 23.786 1.00252.83 C

ANISOU 4553 CG LEU C 174 22837 32977 40248 3326 -1259 -8815 C

ATOM 4554 CDl LEU C 174 -78.542 73.147 22.417 1.00246.24 C

ANISOU 4554 CDl LEU C 174 21984 32172 39403 3308 -1161 -9157 C

ATOM 4555 CD2 LEU C 174 -78.830 72.067 24.645 1.00247.36 C

ANISOU 4555 CD2 LEU C 174 22100 32468 39418 3192 -1147 -8937 C

ATOM 4556 C LEU C 174 -74.466 71.203 24.606 1.00254.15 C

ANISOU 4556 C LEU C 174 23065 32240 41262 3281 -991 -7762 * C

ATOM 4557 O LEU C 174 -74.046 71.003 23.464 1.00254.11 O

ANISOU 4557 O LEU C 174 23052 32110 41388 3341 -941 -7768 O

ATOM 4558 N TYR C 175 -74.008 70.541 25.668 1.00257.46 N

ANISOU 4558 N TYR C 175 23491 32482 41850 3159 -870 -7550 N

ATOM 4559 CA TYR C 175 -73.052 69.448 25.506 1.00258.83 C

ANISOU 4559 CA TYR C 175 23663 32306 42373 3091 -657 -7351 C

ATOM 4560 CB TYR C 175 -72.607 68.874 26.853 1.00258.19 C

ANISOU 4560 CB TYR C 175 ' 23627 32011 42462 2982 -646 -7047 C

ATOM 4561 CG TYR C 175 -71.501 69.659 27.526 1.00257.35 C

ANISOU 4561 CG TYR C 175 23606 31725 42452 3113 -852 -6664 C

ATOM 4562 CDl TYR C 175 -71.713 70.289 28.744 1.00258.25 C

ANISOU 4562 CDl TYR C 175 23781 31916 42427 3138 -1068 -6499 C

ATOM 4563 CEl TYR C 175 -70.709 71.010 29.367 1.00250.93 C

ANISOU 4563 CEl TYR C 175 22954 30804 41584 3263 -1262 -6116 C

ATOM 4564 CZ TYR C 175 ' -69.479 71.110 28.774 1.00245.15 C

ANISOU 4564 CZ TYR C 175 22252 29827 41066 3357 -1242 -5903 C

ATOM 4565 OH TYR C 175 -68.488 71.829 29.397 1.00235.84 O

ANISOU 4565 OH TYR C 175 21185 28465 39957 3480 -1441 -5499 O

ATOM 4566 CE2 TYR C 175 -69.239 70.494 27.564 1.00250.74 C

ANISOU 4566 CE2 TYR C 175 22882 30477 41910 3333 -1029 -6081 C

ATOM 4567 CD2 TYR C 175 -70.248 69.773 26.946 1.00253.23 C

ANISOU 4567 CD2 TYR C 175 23107 30958 42150 3214 -836 -6456 C

ATOM 4568 C TYR C 175 -73.713 68.369 24.674 1.00259.38 C

ANISOU 4568 C TYR C 175 23673 32366 42514 2964 -374 -7616 C

ATOM 4569 O TYR C 175 -74.934 68.350 24.547 1.00265.07 O

ANISOU 4569 O TYR C 175 24361 33312 43043 2866 -312 -7879 O

ATOM 4570 N THR C 176 -72.925 67.464 24.111 1.00244.21 N

ANISOU 4570 N THR C 176 21742 30187 40859 2971 -210 -7535 N

ATOM 4571 CA THR C 176 -73.495 66.526 23.166 1.00245.34 C ANISOU 4571 CA THR C 176 21846 30292 41081 2872 47 -7754 C

ATOM 4572 CB THR C 176 -74.043 67.295 21.940 1.00250.34 C

ANISOU 4572 CB THR C 176 22448 31084 41586 2958 64 -8053 C

ATOM 4573 OGl THR C 176 -74.973 66.479 21.216 1.00252.36 O

ANISOU 4573 OGl THR C 176 22685 31348 41852 2843 302 -8286 O

ATOM 4574 CG2 THR C 176 -72.910 67.759 21.033 1.00247.60 C

ANISOU 4574 CG2 THR C 176 22094 30576 41408 3099 29 -7940 C

ATOM 4575 C THR C 176 -72.510 65.428 22.754 1.00241.66 C

ANISOU 4575 C THR C 176 21385 29485 40948 2839 215 -7564 C

ATOM 4576 O THR C 176 -71.366 65.700 22.392 1.00241.76 O

ANISOU 4576 O THR C 176 21401 29326 41132 2959 175 -7381 O

ATOM 4577 N LEU C 177 -72.972 64.184 22.818 1.00244.25 N

ANISOU 4577 N LEU C 111 21717 29734 41352 2675 384 -7613 N

ATOM 4578 CA LEU C 111 -72.127 63.027 22.569 1.00242.01 C

ANISOO 4578 CA LEU C 111 21447 29141 41364 2635 524 -7467 C

ATOM 4579 CB LEU C 111 -72.080 62.148 23.814 1.00244.58 C

ANISOU 4579 CB LEU C 177 21818 29343 41769 2444 514 -7318 C

ATOM 4580 CG LEU C 177 -71.638 62.747 25.144 1.00251.10 C

ANISOU 4580. CG LEU C 177 22685 30085 42636 2417 339 -7056 C

ATOM 4581 CDl LEU C 177 -72.342 62.030 26.289 1.00251.27 C

ANISOU 4581 CDl LEU C 111 22742 30082 42647 2169 337 -7035 C

ATOM 4582 CD2 LEU C 111 -70.121 62.678 25.293 1.00248.81 C

ANISOU 4582 CD2 LEU C 111 22426 29477 42634 2524 306 -6764 C

ATOM 4583 C LEU C 111 -72.669 62.168 21.446 1.00240.22 C

ANISOU 4583 C LEU C 111 21202 28906 41164 2607 729 -7686 C

ATOM 4584 O LEU C 111 -73.734 61.581 21.580 1.00247.21 O

ANISOU 4584 O LEU C 111 22095 29954 41880 2490 800 -7881 O

ATOM 4585 N SER C 178 -71.932 62.059 20.351 1.00255.24 N

ANISOU ' 4585 N SER C 178 23086 30621 43274 2715 822 -7646 N

ATOM 4586 CA SER C 178 -72.257 61.052 19.351 1.00255.98 C

ANISOU 4586 CA SER C 178 23182 30640 43440 2685 1020 -7797 C

ATOM 4587 CB SER C 178 -71.345 61.209 18.139 1.00253.36 C

ANISOU 4587 CB SER C 178 22805 30185 43274 2848 1089 -7803 C

ATOM 4588 OG SER C 178 -71.279 62.575 17.751 1.00244.95 O

ANISOU 4588 OG SER C 178 21703 29300 42067 2952 992 -7917 O

ATOM 4589 C SER C 178 -72.117 59.669 20.007 1.00255.15 C

ANISOU 4589 C SER C 178 23128 30342 43477 2543 1073 -7671 C

ATOM 4590 O SER C 178 -72.117 59.579 21.232 1.00253.54 O

ANISOU 4590 O SER C 178 22953 30107 43274 2437 962 -7523 O

ATOM 4591 N SER C 179 -72.006 58.603 19.214 1.00255.86 N

ANISOU 4591 N SER C 179 23239 30297 43680 2532 1219 -7729 N

ATOM 4592 CA SER C 179 -71.869 57.247 19.765 '1.00260.88 C

ANISOU 4592 CA SER C 179 23939 30748 44436 2396 1229 -7622 C

ATOM 4593 CB SER C 179 -72.654 57.125 21.073 1.00256.07 C

ANISOU 4593 CB SER C 179 23370 30256 43670 2188 1113 -7591 C

ATOM 4594 OG SER C 179 -72.094 56.145 21.921 1.00260.65 O

ANISOU 4594 OG SER C 179 24004 30605 44425 2068 1038 -7412 O

ATOM 4595 C SER C 179 -72.341 56.156 18.797 1.00269.52 C

ANISOU 4595 C SER C 179 25081 31786 45539 2368 1371 -7743 C

ATOM 4596 O SER C 179 -73.390 56.291 18.175 1.00275.08 O

ANISOU 4596 O SER C 179 25814 32667 46035 2285 1429 -7908 O

ATOM 4597 N SER C 180 -71.580 55.070 18.677 1.00276.86 N

ANISOU 4597 N SER C 180 26025 32469 46700 2440 1415 -7650 N

ATOM 4598 CA SER C 180 -71.983 53.955 17.814 1.00278.39 C

ANISOU 4598 CA SER C 180 26281 32584 46909 2432 1525 -7732 C

ATOM 4599 CB SER C 180 -71.543 54.194" 16.366 1.00275.24 C

ANISOU 4599 CB SER C 180 25830 32085 46664 2643 1658 -7782 C

ATOM 4600 OG SER C 180 -70.132 54.243 16.249 1.00275.12 O

ANISOU 4600 OG SER C 180 25760 31885 46888 2766 1615 -7626 O

ATOM 4601 C SER C 180 -71.456 52.602 18.282 1.00284.59 C

ANISOU 4601 C SER C 180 27153 33171 47808 2318 1439 -7607 C

ATOM 4602 O SER C 180 -70.518 52.528 19.074 1.00287.12 O

ANISOU 4602 O SER C 180 27466 33336 48290 2298 1331 -7451 O

ATOM 4603 N VAL C 181 -72.075 51.535 17.783 1.00253.70 N

ANISOU 4603 N VAL C 181 23335 29258 43803 2236 1470 -7672 N

ATOM 4604 CA VAL C 181 -71.590 50.173 17.997 1.00259.63 C

ANISOU 4604 CA VAL C 181 24182 29805 44660 2158 1371 -7575 C

ATOM 4605 CB VAL C 181 -72.307 49.482 19.180 1.00256.26 C

ANISOU 4605 CB VAL C 181 23850 29464 44053 1872 1206 -7554 C

ATOM 4606 CGl VAL C 181 -73.759 49.896 19.237 1.00254.54 C

ANISOU 4606 CGl VAL C 181 23654 29532 43526 1768 1263 -7687 C

ATOM 4607 CG2 VAL C 181 -72.172 47.970 19.083 1.00255.24 C

ANISOU 4607 CG2 VAL C 181 23848 29144 43988 1785 1079 -7490 C

ATOM 4608 C VAL C 181 -71.780 49.371 16.711 1.00264.13 C

ANISOU 4608 C VAL C 181 24812 30291 45253 ' 2275 1479 -7634 C

ATOM 4609 O VAL C 181 -72.713 49.621 15.957 1.00263.58 O

ANISOU 4609 O VAL C 181 24744 30349 45056 2327 1619 -7755 O ATOM 4610 N THR C 182 -70.891 48.420 16.446 1.00280.83 N

ANISOU 4610 N THR C 182 26986 32181 47537 2321 1409 -7551 N

ATOM 4611 CA THR C 182 -70.963 47.674 15.195 1.00283.10 C

ANISOU 4611 CA THR C 182 27334 32370 47861 2460 1499 -7587 C

ATOM 4612 CB THR C 182 -69.827 48.080 14.232 1.00281.59 C

ANISOU 4612 CB THR C 182 27031 32044 47916 2723 1623 -7582 C

ATOM 4613 OGl THR C 182 -69.997 49.448 13.840 1.00272.94 O

ANISOU 4613 OGl THR C 182 25811 31094 46798 2796 1751 -7658 O

ATOM 4614 CG2 THR C 182 -69.842 47.207 12.994 1.00283.65 C

ANISOU 4614 CG2 THR C 182 27358 32200 48215 2867 1717 -7619 C

ATOM 4615 C THR C 182 -70.978 46.159 15.403 1.00288.80 C

ANISOU 4615 C THR C 182 28208 32953 48570 2365 1326 -7518 C

ATOM 4616 O THR C 182 -70.015 45.571 15.900 1.00286.15 O

ANISOU 4616 O THR C 182 27885 32442 48398 2351 1177 -7432 O

ATOM 4617 N VAL C 183 -72.087 45.538 15.014 1.00301.10 N

ANISOU 4617 N VAL C 183 29895 34591 49920 2294 1330 -7555 N

ATOM 4618 CA VAL C 183 -72.265 44.099 15.159 1.00305.26 C

ANISOU 4618 CA VAL C 183 30593 35014 50378 2202 1135 -7488 C

ATOM 4619 CB VAL C 183 -73.130 43.773 16.395 1.00300.09 C

ANISOU 4619 CB VAL C 183 30029 34496 49495 1879 918 -7463 C

ATOM 4620 CGl VAL C 183 -72.470 44.312 17.662 1.00286.02 C

ANISOU 4620 CGl VAL C 183 28141 32704 47831 1763 835 -7437 C

ATOM 4621 CG2 VAL C 183 -74.531 44.344 16.232 1.00299.15 C

ANISOU 4621 CG2 VAL C 183 29946 34644 49075 1759 1007 -7530 C

ATOM 4622 C VAL C 183 -72.913 43.529 13.894 1.00305.80 C

ANISOU 4622 C VAL C 183 30770 35069 50350 2324 1246 -7508 C

ATOM 4623 O VAL C 183 -73.574 44.265 13.157 1.00299.10 O

ANISOU 4623 O VAL C 183 29869 34312 49465 2419 1470 -7588 O

ATOM 4624 N PRO C 184 -72.719 42.221 13.631 1.00309.91 N

ANISOU 4624 N PRO C 184 31456 35460 50837 2324 1075 -7432 N

ATOM 4625 CA PRO C 184 -73.273 41.573 12.433 1.00309.53 C

ANISOU 4625 CA PRO C 184 31538 35357 50711 2457 1156 -7413 C

ATOM 4626 CB PRO C 184 -72.883 40.100 12.618 1.00307.09 C

ANISOU 4626 CB PRO C 184 31389 34876 50417 2466 880 -7315 C

ATOM 4627 CG PRO C 184 -71.717 40.124 13.531 1.00304.87 C

ANISOU 4627 CG PRO C 184 31012 34502 50324 2413 725 -7313 C

ATOM 4628 CD PRO C 184 -71.953 41.274 14.460 1.00307.90 C

ANISOU 4628 CD PRO C 184 31279 35069 50639 2218 781 -7360 C

ATOM 4629 C PRO C 184 -74.795 41.702 12.354 1.00314.30 C

ANISOU 4629 C PRO C 184 32257 36161 51000 2296 1197 -7424 C

ATOM 4630 O PRO C 184 -75.444 41.880 13.387 1.00315.95 O

ANISOU 4630 O PRO C 184 32492 36550 51003 2042 1061 -7423 O

ATOM 4631 N SER C 185 -75.355 41.615 11.146 1.00320.83 N

ANISOU 4631 N SER C 185 33155 36952 51795 2435 1382 -7431 N

ATOM 4632 CA SER C 185 -76.808 41.668 10.971 1.00322.45 C

ANISOU 4632 CA SER C 185 33475 37327 51715 2305 1452 -7437 C

ATOM 4633 CB SER C 185 -77.186 42.016 9.526 1.00316.36 C

ANISOU 4633 CB SER C 185 32746 36446 51011 2501 1716 -7464 C

ATOM 4634 OG SER C 185 -76.955 40.929 8.649 1.00314.60 O

ANISOU 4634 OG SER C 185 32703 36021 50811 2634 1638 -7334 O

ATOM 4635 C SER C 185 -77.446 40.347 11.399 1.00323.24 C

ANISOU 4635 C SER C 185 33797 37497 51523 2105 1174 -7309 C

ATOM 4636 O SER C 185 -78.653 40.145 11.255 1.00325.80 O

ANISOU 4636 O SER C 185 34219 38004 51565 1949 1183 -7297 O

ATOM 4637 N SER C 186 -76.611 39.451 11.920 1.00297.47 N

ANISOU 4637 N SER C 186 30617 34095 48312 2102 906 -7218 N

ATOM 4638 CA SER C 186. -77.067 38.206 12.523 1.00293.85 C

ANISOU 4638 CA SER C 186 30373 33710 47567 1883 576 -7102 C

ATOM 4639 CB SER C 186 -76.087 37.071 12.209 1.00289.33 C

ANISOU 4639 CB SER C 186 29935 32905 47093 1996 319 -7003 C

ATOM 4640 OG SER C 186 -76.642 35.804 12.514 1.00285.85 O

ANISOU 4640 OG SER C 186 29746 32527 46338 1822 1 -6875 O

ATOM 4641 C SER C 186 -77.189 38.410 14.033 1.00297.72 C

ANISOU 4641 C SER C 186 30794 34407 47919 1572 398 -7146 C

ATOM 4642 O SER C 186 -77.072 37.465 14.812 1.00298.18 O

ANISOU 4642 O SER C 186 30998 34529 47768 1344 75 -7073 O

ATOM 4643 N THR C 187 -77.412 39.662 14.429 1.00297.38 N

ANISOU 4643 N THR C 187 30535 34465 47991 1560 595 -7266 N

ATOM 4644 CA THR C 187 -77.618 40.030 15.829 1.00295.72 C

ANISOU 4644 CA THR C 187 30242 34459 47658 1282 473 -7313 C

ATOM 4645 CB THR C 187 -76.307 39.967 16.651 1.00293.19 C

ANISOU 4645 CB THR C 187 29827 33982 47588 1244 316 -7317 C

ATOM 4646 OGl THR C 187 -75.182 40.143 15.781 1.00288.42 O

ANISOU 4646 OGl THR C 187 29109 33152 47324 1545 496 -7339 O

ATOM 4647 CG2 THR C 187 -76.179 38.619 17.348 1.00289.67 C

ANISOU 4647 CG2 THR C 187 29564 33432 47064 1077 -62 -7229 C

ATOM 4648 C THR C 187 -78.281 41.410 15.960 1.00296.54 C ANISOU 4648 C THR C 187 30187 34786 47697 1269 732 -7432 C

ATOM 4649 O THR C 187 -78.082 42.114 16.953 1.00295.96 O

ANISOO 4649 O THR C 187 29978 34829 47643 1141 707 -7492 O

ATOM 4650 N TRP C 188 -79.055 41.777 14.936 1.00278.83 N

ANISOU 4650 N TRP C 188 27971 32585 45385 1405 968 -7468 N

ATOM 4651 CA TRP C 188 -79.946 42.947 14.955 1.00280.81 C

ANISOU 4651 CA TRP C 188 28118 33072 45504 1370 1178 -7594 C

ATOM 4652 CB TRP C 188 -79.199 44.226 15.343 1.00280.19 C

ANISOU 4652 CB TRP C 188 27810 33009 45639 1449 1299 -7709 C

ATOM 4653 CG TRP C 188 -80.114 45.402 15.619 1.00276.59 C

ANISOU 4653 CG TRP C 188 27255 32832 45006 1378 1437 -7849 C

ATOM 4654 CDl TRP C 188 -80.553 45.832 16.839 1.00270.03 C

ANISOU 4654 CDl TRP C 188 26344 32253 44001 1174 1332 -7896 C

ATOM 4655 NEl TRP C 188 -81.366 46.927 1-6.689 1.00268.54 N

ANISOU 4655 NEl TRP C 188 26079 32284 43670 1188 1495 -8042 N

ATOM 4656 CE2 TRP C 188 -81.470 47.225 15.357 1.00272.68 C

ANISOU 4656 CE2 TRP C 188 26641 32681 44285 1383 1710 -8096 C

ATOM 4657 CD2 TRP C 188 -80.696 46.286 14.652 1.00276.17 C

ANISOU 4657 CD2 TRP C 188 27178 32827 44928 1508 1687 -7970 C

ATOM 4658 CE3 TRP C 188 -80.636 46.372 13.258 1.00275.10 C

ANISOU 4658 CE3 TRP C 188 27097 32503 44927 1711 1886 -7991 C

ATOM 4659 CZ3 TRP C 188 -81.338 47.378 12.626 1.00271.36 C

ANISOU 4659 CZ3 TRP C 188 26589 32122 44395 1762 2095 -8143 C

ATOM 4660 CH2 TRP C 188 -82.094 48.298 13.354 1.00269.91 C

ANISOU 4660 CH2 TRP C 188 26314 32234 44005 1634 2100 -8280 C

ATOM 4661 CZ2 TRP C 188 -82.175 48.237 14.717 1.00271.89 C

ANISOU 4661 CZ2 TRP C 188 26502 32693 44109 1454 1911 -8255 C

ATOM 4662 C TRP C 188 -80.647 43.137 13.601 1.00281.31 C

ANISOU 4662 C TRP C 188 28258 33087 45539 1535 1421 -7620 C

ATOM 4663 O TRP C 188 -80.013 43.007 12.550 1.00277.43 O

ANISOU 4663 O TRP C 188 27773 32348 45288 1769 1548 -7605 O

ATOM 4664 N PRO C 189 -81.954 43.469 13.622 1.00315.28 N

ANISOU 4664 N PRO C 189 32616 37622 49555 1408 1491 -7666 N

ATOM 4665 CA PRO C 189 -82.781 43.726 14.812 1.00312.95 C

ANISOU 4665 CA PRO C 189 32289 37664 48953 1139 1371 -7709 C

ATOM 4666 CB PRO C 189 -84.011 44.456 14.238 1.00303.18 C

ANISOU 4666 CB PRO C 189 31108 36589 47498 1132 1565 -7785 C

ATOM 4667 CG PRO C 189 -83.645 44.835 12.835 1.00302.11 C

ANISOU 4667 CG PRO C 189 30964 36194 47631 1401 1826 -7839 C

ATOM 4668 CD PRO C 189 -82.677 43.797 12.382 1.00306.26 C

ANISOU 4668 CD PRO C 189 31553 36411 48399 1545 1736 -7701 C

ATOM 4669 C PRO C 189 -83.250 42.485 15.591 1.00315.49 C

ANISOU 4669 C PRO C 189 32751 38090 49031 883 1044 -7568 C

ATOM 4670 O PRO C 189 -84.146 42.633 16.422 1.00315.89 O

ANISOU 4670 O PRO C 189 32737 38404 48884 649 913 -7610 O

ATOM 4671 N SER C 190 -82.672 41.308 15.347 1.00307.94 N

ANISOU 4671 N SER C 190 31984 36942 48077 919 894 -7411 N

ATOM 4672 CA SER C 190 -83.122 40.084 16.028 1.00306.47 C

ANISOU 4672 CA SER C 190 31967 36867 47609 661 545 -7276 C

ATOM 4673 CB SER C 190 -82.597 38.819 15.328 1.00301.03 C

ANISOU 4673 CB SER C 190 31483 35905 46988 773 372 -7111 C

ATOM 4674 OG SER C 190 -81.274 38.986 14.855 1.00299.01 O

ANISOU 4674 OG SER C 190 31140 35343 47128 1054 506 -7143 O

ATOM 4675 C SER C 190 -82.825 40.057 17.537 1.00304.42 C

ANISOU 4675 C SER C 190 31604 36757 47304 398 307 -7317 C

ATOM 4676 O SER C 190 -83.709 39.765 18.343 1.00301.21 O

ANISOU 4676 O SER C 190 31234 36641 46570 114 139 -7307 O

ATOM 4677 N GLU C 191 -81.586 40.357 17.915 1.00286.61 N

ANISOU 4677 N GLU C 191 29222 34300 45375 482 289 -7355 N

ATOM 4678 CA GLU C 191 -81.237 40.509 19.326 1.00284.58 C

ANISOU 4678 CA GLU C 191 28861 34139 45129 247 104 -7396 C

ATOM 4679 CB GLU C 191 -79.797 40.063 19.589 1.00286.41 C

ANISOU 4679 CB GLU C 191 29093 34057 45673 296 -62 -7351 C

ATOM 4680 CG GLU C 191 ' -79.643 38.586 19.926 1.00285.77 C

ANISOU 4680 CG GLU C 191 29228 33893 45458 119 -437 -7237 C

ATOM 4681 CD GLU C 191 -79.540 37.703 18.698 1.00281.97 C

ANISOU 4681 CD GLU C 191 28922 33233 44981 343 -433 -7138 C

ATOM 4682 OEl GLU C 191 -79.808 38.193 17.582 1.00285.78 O

ANISOU 4682 OEl GLU C 191 29365 33670 45549 608 -122 -7157 O

ATOM 4683 OE2 GLU C 191 -79.186 36.515 18.852 1.00272.87 O

ANISOU 4683 0E2 GLU C 191 27956 31978 43746 249 -757 -7044 O

ATOM 4684 C GLU C 191 -81.417 41.961 19.748 1.00283.96 C

ANISOU 4684 C GLU C 191 28559 34221 45111 285 336 -7537 . C

ATOM 4685 O GLU C 191 -81.071 42.875 19.001 1.00284.41 O

ANISOU 4685 O GLU C 191 28510 34172 45382 550 605 -7606 O

ATOM 4686 N THR C 192 -81.949 42.171 20.950 1.00285.11 N

ANISOU 4686 N THR C 192 28640 34632 45056 15 210 -7581 N ATOM 4687 CA THR C 192 -82.292 43.518 21.415 1.00284.26 C

ANISOU 4687 CA THR C 192 28342 34732 44932 37 393 -7713 C

ATOM 4688 CB THR C 192 -83.528 43.492 22.363 1.00277.59 C

ANISOU 4688 CB THR C 192 27488 34292 43690 -266 273 -7758 C

ATOM 4689 OGl THR C 192 -84.534 42.619 21.829 1.00274.29 O

ANISOU 4689 OGl THR C 192 27232 34027 42960 -335 247 -7710 O

ATOM 4690 CG2 THR C 192 -84.116 44.889 22.531 1.00269.46 C

ANISOU 4690 CG2 THR C 192 26273 33494 42617 -197 469 -7910 C

ATOM 4691 C THR C 192 -81.117 44.258 22.085 1.00281.76 C

ANISOU 4691 C THR C 192 27870 34257 44930 97 399 -7734 C

ATOM 4692 O THR C 192 -80.977 44.248 23.310 1.00276.54 O

ANISOU 4692 O THR C 192 27178 33646 44250 -134 204 -7714 O

ATOM 4693 N VAL C 193 -80.281 44.903 21.272 1.00291.70 N

ANISOU 4693 N VAL C 193 29039 35322 46473 398 617 -7767 N

ATOM 4694 CA VAL C 193 -79.152 45.678 21.783 1.00289.21 C

ANISOU 4694 CA VAL C 193 28584 34857 46445 485 637 -7764 C

ATOM 4695 CB VAL C 193 -77.961 45.663 20.806 1.00288.28 C

ANISOU 4695 CB VAL C 193 28440 34425 46669 793 781 -7733 C

ATOM 4696 CGl VAL C 193 -77.406 44.252 20.663 1.00287.03 C

ANISOU 4696 CGl VAL C 193 28411 33995 46653 774 610 -7620 C

ATOM 4697 CG2 VAL C 193 -78.374 46.223 19.452 1.00287.84 C

ANISOU 4697 CG2 VAL C 193 28381 34415 46571 1013 1030 -7819 C

ATOM 4698 C VAL C 193 -79.561 47.122 22.060 1.00289.11 C

ANISOU 4698 C VAL C 193 28417 35087 46343 504 752 -7873 C

ATOM 4699 O VAL C 193 -79.877 47.874 21.137 1.00286.42 O

ANISOU 4699 O VAL C 193 28019 34839 45970 689 958 -7976 O

ATOM 4700 N THR C 194 -79.546 47.503 23.335 1.00304.77 N

ANISOU 4700 N THR C 194 30343 37168 48289 305 601 -7854 N

ATOM 4701 CA THR C 194 -80.020 48.823 23.755 1.00300.85 C

ANISOU 4701 CA THR C 194 29706 36902 47700 317 662 -7942 C

ATOM 4702 CB THR C 194 -81.046 48.718 24.916 1.00295.95 C

ANISOU 4702 CB THR C 194 29080 36559 46810 -10 475 -7955 C

ATOM 4703 OGl THR C 194 -81.827 47.524 24.771 1.00299.07 O

ANISOU 4703 OGl THR C 194 29606 37063 46965 -223 356 -7939 O

ATOM 4704 CG2 THR C 194 -81.973 49.933 24.939 1.00288.59 C

ANISOU 4704 CG2 THR C 194 28027 35981 45642 16 562 -8095 C

ATOM 4705 C THR C 194 -78.876 49.759 24.173 1.00295.42 C

ANISOU 4705 C THR C 194 28922 35995 47328 474 683 -7876 C

ATOM 4706 O THR C 194 -77.700 49.437 24.017 1.00292.95 O

ANISOU 4706 O THR C 194 28639 35365 47305 592 685 -7779 O

ATOM 4707 N CYS C 195 -79.247 50.922 24.695 1.00294.32 N

ANISOU 4707 N CYS C 195 28673 36040 47115 481 688 -7924 N

ATOM 4708 CA CYS C 195 -78.312 51.935 25.160 1.00294.30 C

ANISOU 4708 CA CYS C 195 28596 35864 47359 580 657 -7826 C

ATOM 4709 CB CYS C 195 -78.667 53.282 24.518 1.00281.04 C

ANISOU 4709 CB CYS C 195 26825 34215 45744 884 818 -7893 C

ATOM 4710 SG CYS C 195 -77.696 54.744 25.003 1.00249.77 S

ANISOU 4710 SG CYS C 195 22749 30467 41684 938 760 -7914 S

ATOM 4711 C CYS C 195 -78.464 51.986 26.675 1.00294.56 C

ANISOU 4711 C CYS C 195 28596 36060 47264 344 495 -7799 C

ATOM 4712 O CYS C 195 -79.171 51.153 27.248 1.00295.29 O

ANISOU 4712 O CYS C 195 28729 36348 47121 81 387 -7842 O

ATOM 4713 N ASN C 196 -77.817 52.947 27.327 1.00284.54 N

ANISOU 4713 N ASN C 196 27259 34714 46138 433 466 -7718 N

ATOM 4714 CA ASN C 196 -77.943 53.076 28.774 1.00281.45 C

ANISOU 4714 CA ASN C 196 26842 34421 45674 223 310 -7664 C

ATOM 4715 CB ASN C 196 -77.464 51.793 29.462 1.00283.41 C

ANISOU 4715 CB ASN C 196 27188 34436 46060 -65 142 -7548 C

ATOM 4716 CG ASN C 196 -78.097 51.583 30.828 1.00288.08 C

ANISOU 4716 CG ASN C 196 27765 35189 46503 -368 -30 -7536 C

ATOM 4717 ODl ASN C 196 -78.655 52.508 31.424 1.00289.63 O

ANISOU 4717 ODl ASN C 196 27880 35549 46618 -316 -35 -7538. O

ATOM 4718 ND2 ASN C 196 -78.010 50.356 31.331 1.00287.08 N

ANISOU 4718 ND2 ASN C 196 27722 35022 46332 -692 -192 -7525 N

ATOM 4719 C ASN C 196 -77.189 54.275 29.328 1.00281.49 C

ANISOU 4719 C ASN C 196 26785 34329 45840 408 305 -7558 C

ATOM 4720 O ASN C 196 -76.203 54.111 30.040 1.00287.26 O

ANISOU 4720 O ASN C 196 27552 34719 46873 437 259 -7379 O

ATOM 4721 N VAL C 197 -77.654 55.479 29.004 1.00254.56 N

ANISOU 4721 N VAL C 197 23290 31212 42219 538 338 -7663 N

ATOM 4722 CA VAL C 197 -77.037 56.700 29.523 1.00252.42 C

ANISOU 4722 CA VAL C 197 22974 30889 42045 718 292 -7555 C

ATOM 4723 CB VAL C 197 -77.619 57.969 28.840 1.00243.79 C

ANISOU 4723 CB VAL C 197 21805 30069 40755 974 365 -7717 C

ATOM 4724 CGl VAL C 197 -76.910 59.221 29.317 1.00237.33 C

ANISOU 4724 CGl VAL C 197 20964 29169 40040 1178 282 -7576 C

ATOM 4725 CG2 VAL C 197 -77.503 57.857 27.332 1.00241.61 C ANISOU 4725 CG2 VAL C 197 21537 29734 40529 1136 533 -7829 C

ATOM 4726 C VAL C 197 -77.201 56.770 31.047 1.00251.28 C

ANISOϋ 4726 C VAL C 197 22825 30809 41841 511 126 -7463 * C

ATOM 4727 O VAL C 197 -77.989 56.022 31.625 1.00254.02 O

ANISOU 4727 O VAL C 197 23167 31370 41978 254 61 -7554 O

ATOM 4728 N ALA C 198 -76.433 57.646 31.690 1.00249.62 N

ANISOU 4728 N ALA C 198 22624 30405 41816 616 51 -7269 N

ATOM 4729 CA ALA C 198 -76.529 57.871 33.129 1.00249.71 C

ANISOU 4729 CA ALA C 198 22643 30426 41809 441 -105 -7151 C

ATOM 4730 CB ALA C 198 -76.008 56.671 33.900 1.00248.62 C

ANISOU 4730 CB ALA C 198 22592 29971 41900 139 -183 -7018 C

ATOM 4731 C ALA C 198 -75.738 59.125 33.478 1.00249.04 C

ANISOU 4731 C ALA C 198 22561 30233 41831 671 -172 -6965 C

ATOM 4732 O ALA C 198 -74.581 59.258 33.092 1.00251.76 O

ANISOO 4732 O ALA C 198 22969 30203 42484 758 -178 -6742 O

ATOM 4733 N HIS C 199 -76.365 60.043 34.204 1.00234.26 N

ANISOU 4733 N HIS C 199 20625 28698 39685 771 -240 -7053 N

ATOM 4734 CA HIS C 199 -75.805 61".379 34.390 1.00229.38 C

ANISOU 4734 CA HIS C 199 20018 28044 39092 1019 -339 -6893 C

ATOM 4735 CB HIS C 199 -76.492 62.349 33.417 1.00224.53 C

ANISOU 4735 CB HIS C 199 19332 27781 38200 1279 -319 -7110 C

ATOM 4736 CG HIS C 199 -76.024 63.770 33.519 1.00221.12 C

ANISOU 4736 CG HIS C 199 18914 27386 37714 1536. -469 -6980 C

ATOM 4737 NDl HIS C 199 -76.894 64.827 33.675 1.00224.67 N

ANISOU 4737 NDl HIS C 199 19317 28208 37841 1612 -604 -7107 N

ATOM 4738 CEl HIS C 199 -76.210 65.957 33.724 1.00221.40 C

ANISOU 4738 CEl HIS C 199 18948 27742 37433 1855 -756 -6939 C

ATOM 4739 NE2 HIS C 199 -74.928 65.671 33.604 1.00217.02 N

ANISOU 4739 NE2 HIS C 199 18463 26801 37192 1931 -712 -6701 N

ATOM 4740 CD2 HIS C 199 -74.785 64.310 33.471 1.00220.16 C

ANISOU 4740 CD2 HIS C 199 18858 26995 37797 1741 .-528 -6734 C

ATOM 4741 C HIS C 199 -75.938 61.854 35.840 1.00229.41 C

ANISOU 4741 C HIS C 199 20038 28091 39038 884 -505 -6762 C

ATOM 4742 O HIS C 199 -76.950 62.449 36.205 1.00233.73 O

ANISOU 4742 O HIS C 199 20515 29022 39269 876 -576 -6921 O

ATOM 4743 N PRO C 200 -74.909 61.584 36.668 1.00244.10 N

ANISOU 4743 N PRO C 200 21993 29546 41207 779 -569 -6474 N

ATOM 4744 CA PRO C 200 -74.795 61.907 38.100 1.00242.77 C

ANISOU 4744 CA PRO C 200 21865 29314 41063 601 -718 -6310 C

ATOM 4745 CB PRO C 200 -73.293 61.774 38.355 1.00242.73 C

ANISOU 4745 CB PRO C 200 21990 28752 41486 575 -735 -5977 C

ATOM 4746 CG PRO C 200 -72.884 60.674 37.446 1.00245.34 C

ANISOU 4746 CG PRO C 200 22329 28893 41996 591 -592 -6035 C

ATOM 4747 CD PRO C 200 -73.750 60.798 36.206 1.00248.09 C

ANISOU 4747 CD PRO C 200 22579 29601 42083 822 -495 -6285 C

ATOM 4748 C PRO C 200 -75.279 63.300 38.524 1.00242.51 C

ANISOU 4748 C PRO C 200 21805 29551 40788 803 -860 -6277 C

ATOM 4749 O PRO C 200 -75.753 63.461 39.651 1.00235.55 O

ANISOU 4749 O PRO C 200 20929 28733 39837 652 -982 -6212 O

ATOM 4750 N ALA C 201 -75.155 64.289 37.647 1.00258.56 N

ANISOU 4750 N ALA C 201 23813 31739 42689 1134 -864 -6328 N

ATOM 4751 CA ALA C 201 -75.597 65.649 37.956 1.00257.94 C

ANISOU. 4751 CA ALA C 201 23724 31924 42358 1358 -1037 -6308 C

ATOM 4752 CB ALA C 201 -75.300 66.562 36.791 1.00256.38 C

ANISOU 4752 CB ALA C 201 23535 31769 42108 1703 -1057 -6315 C

ATOM 4753 C ALA C 201 -77.082 65.705 38.280 1.00253.01 C

ANISOU 4753 C ALA C 201 22983 31810 41339 1268 -1076 -6620 C

ATOM 4754 O ALA C 201 -77.481 65.788 39.439 1.00245.45 O

ANISOU 4754 O ALA C 201 22017 30966 40278 1145 -1198 -6572 O

ATOM 4755 N SER C 202 -77.890 65.674 37.230 1.00236.56 N

ANISOU 4755 N SER C 202 20812 30030 39041 1329 -970 -6936 N

ATOM 4756 CA SER C 202 -79.335 65.684 37.352 1.00233.75 C

ANISOU 4756 CA SER C 202 20343 30165 38308 1235 -979 -7255 C

ATOM 4757 CB SER C 202 -79.964 65.945 35.984 1.00234.60 C

ANISOU 4757 CB SER C 202 20389 30536 38212 1408 -883 -7556 C

ATOM 4758 OG SER C 202 -79.613 64.927 35.060 1.00235.03 O

ANISOU 4758 OG SER C 202 20471 30337 38494 1363 -691 -7563 O

ATOM 4759 C SER C 202 -79.861 64.365 37.910 1.00234.72 C

ANISOU 4759 C SER C 202 20432 30305 38446 853 -895 -7324 C

ATOM 4760 O SER C 202 -81.025 64.268 38.290 1.00235.04 O

ANISOU 4760 O SER C 202 20379 30749 38177 721 -901 -7565 O

ATOM 4761 N SER C 203 -78.999 63.354 37.951 1.00254.31 N

ANISOU 4761 N SER C 203 22994 32356 41276 • 671 -838 -7114 N

ATOM 4762 CA SER C 203 -79.382 62.022 38.421 1.00256.47 C

ANISOU 4762 CA SER C 203 23261 32598 41587 287 -797 -7163 C

ATOM 4763 CB SER C 203 -80.040 62.092 39.803 1.00257.68 C

ANISOU 4763 CB SER C 203 23367 32982 41557 60 -943 -7174 C ATOM 4764 OG SER C 203 -79.156 62.641 40.765 1.00260.95 O

ANISOU 4764 OG SER C 203 23869 33064 42217 53 -1064 -6870 O

ATOM 4765 C SER C 203 -80.307 61.317 37.434 1.00254.93 C

ANISOU 4765 C SER C 203 23008 32641 41212 204 -655 -7441 C

ATOM 4766 O SER C 203 -81.421 60.935 37.783 1.00253.41 O

ANISOU 4766 O SER C 203 22773 32671 40841 -82 -666 -7576 O

ATOM 4767 N THR C 204 -79.830 61.135 36.206 1.00254.08 N

ANISOU 4767 N THR C 204 22909 32477 41152 448 -531 -7509 N

ATOM 4768 CA THR C 204 -80.628 60.520 35.150 1.00259.08 C

ANISOU 4768 CA THR C 204 23509 33296 41635 413 -385 -7750 C

ATOM 4769 CB THR C 204 -80.585 61.364 33.847 1.00255.49 C

ANISOU 4769 CB THR C 204 23044 32866 41165 755 ' -284 -7855 C

ATOM 4770 OGl THR C 204 -80.741 62.755 34.156 1.00248.04 O

ANISOU 4770 OGl THR C 204 22052 32180 40012 974 -399 -7922 O

ATOM 4771 CG2 THR C 204 -81.682 60.932 32.879 1.00254.91 C

ANISOU 4771 CG2 THR C 204 22942 32998 40913 723 -132 -8111 C

ATOM 4772 C THR C 204 -80.173 59.094 34.821 1.00262.56 C

ANISOU 4772 C THR C 204 24019 33447 42294 180 -308 -7683 C

ATOM 4773 O THR C 204 -78.987 58.770 34.908 1.00259.97 O

ANISOU 4773 O THR C 204 23772 32697 42306 144 -327 -7459 O

ATOM 4774 N LYS C 205 -81.133 58.248 34.461 1.00256.60 N

ANISOU 4774 N LYS C 205 23242 32927 41327 22 -240 -7877 N

ATOM 4775 CA LYS C 205 -80.860 56.959 33.828 1.00256.67 C

ANISOU 4775 CA LYS C 205 23327 32710 41486 -111 -160 -7858 C

ATOM 4776 CB LYS C 205 -80.726 55.833 34.855 1.00256.00 C

ANISOU 4776 CB LYS C 205 23300 32478 41490 -487 -290 -7750 C

ATOM 4777 CG LYS C 205 -79.295 55.352 35.053 1.00257.07 C

ANISOU 4777 CG LYS C 205 23531 32089 42056 -497 -329 -7505 C

ATOM 4778 CD LYS C 205 -79.244 53.880 35.434 1.00253.85 C

ANISOU 4778 CD LYS C 205 23212 31477 41761 -847 -428 -7455 C

ATOM 4779 CE LYS C 205 -77.820 53.359 35.401 1.00249.09 C

ANISOU 4779 CE LYS C 205 22708 30338 41597 -831 -458 -7233 C

ATOM 4780 NZ LYS C 205 -76.888 54.250 36.148 1.00251.21 N

ANISOU 4780 NZ LYS C 205 22972 30456 42022 -785 -528 -7057 N

ATOM 4781 C LYS C 205 -81.971 56.648 32.834 1.00254.67 C

ANISOU 4781 C LYS C 205 23049 32762 40953 -94 -42 -8091 C

ATOM 4782 O LYS C 205 -83.147 56.805 33.150 1.00259.60 O

ANISOU 4782 O LYS C 205 23607 33796 41232 -201 -74 -8257 O

ATOM 4783 N VAL C 206 -81.600 56.216 31.633 1.00247.37 N

ANISOU 4783 N VAL C 206 22179 31631 40178 43 95 -8098 N

ATOM 4784 CA VAL C 206 -82.575 56.013 30.566 1.00249.35 C

ANISOU 4784 CA VAL C 206 22425 32108 40207 103 228 -8296 C

ATOM 4785 CB VAL C 206 -82.778 57.300 29.744 1.00249.21 C

ANISOU 4785 CB VAL C 206 22347 32227 40116 420 322 -8436 C

ATOM 4786 CGl VAL C 206 -83.951 58.096 30.286 1.00253.46 C

ANISOU 4786 CGl VAL C 206 22792 33212 40299 398 244 -8605 C

ATOM 4787 CG2 VAL C 206 -81.515 58.141 29.753 1.00247.32 C

ANISOU 4787 CG2 VAL C 206 22111 31682 40179 649 302 -8277 C

ATOM 4788 C VAL C 206 -82.177 54.878 29.636 1.00253.20 C

ANISOU 4788 C VAL C 206 23014 32304 40886 96 321 -8236 C

ATOM 4789 O VAL C 206 -81.113 54.287 29.802 1.00256.85 O

ANISOU 4789 O VAL C 206 23530 32389 41674 129 304 -8066 O

ATOM 4790 N ASP C 207 -83.042 54.582 28.665 1.00260.14 N

ANISOU 4790 N ASP C 207 23925 33356 41560 59 412 -8370 N

ATOM 4791 CA ASP C 207 -82.819 53.495 27.709 1.00259.88 C

ANISOU 4791 CA ASP C 207 24000 33073 41669 53 482 -8311 C

ATOM 4792 CB ASP C 207 -83.246 52.151 28.309 1.00259 ' .76 C

ANISOU 4792 CB ASP C 207 24066 33107 41523 -291 333 -8252 C

ATOM 4793 CG ASP C 207 -82.567 51.853 29.637 1.00258.63 C

ANISOU 4793 CG ASP C 207 23921 32824 41521 -508 138 -8113 C

ATOM 4794 ODl ASP C 207 -81.319 51.857 29.690 1.00263.53 O

ANISOU 4794 ODl ASP C 207 24553 33093 42484 -392 135 -7980 O

ATOM 4795 0D2 ASP C 207 -83.284 51.602 30.628 1.00255.91 O

ANISOU 4795 0D2 ASP C 207 23569 32719 40948 -806 -13 -8136 O

ATOM 4796 C ASP C 207 -83.580 53.725 26.401 1.00246.76 C

ANISOU 4796 C ASP C 207 22356 31503 39899 237 670 -8460 C

ATOM 4797 O ASP C 207 -83.163 54.504 25.545 1.00226.85 O

ANISOU 4797 O ASP C 207 19776 28984 37431 485 776 -8548 O

ATOM 4798 N ASP D 1 -35.892 87.361 25.938 1.00177.76 N

ANISOU 4798 N ASP D 1 23578 20156 23806 337 1890 -111 N

ATOM 4799 CA ASP D 1 -37.023 86.461 26.152 1.00180.03 C

ANISOU 4799 CA ASP D 1 23714 20643 24046 607 1683 -161 C

ATOM 4800 CB ASP, D 1 -38.345 87.207 25.966 1.00184.59 C

ANISOU 4800 CB ASP D 1 24420 20920 24797 879 1523 -93 C

ATOM 4801 CG ASP D 1 -39.433 86.699 26.891 1.00185.26 C

ANISOU 4801 CG ASP D 1 24261 21175 24955 1069 1378 -316 C

ATOM 4802 ODl ASP D 1 -39.569 85.464 27.008 1.00179.99 O ANISOU 4802 ODl ASP D 1 23491 20779 24117 1195 1255 -282 O

ATOM 4803 0D2 ASP D 1 -40.143 87.531 27.505 1.00189.89 O

ANISOU 4803 0D2 ASP D 1 24748 21633 25769 1075 1398 -542 O

ATOM 4804 C ASP D 1 -36.952 85.234 25.237 1.00181.96 C

ANISOU 4804 C ASP D 1 23948 21184 24005 670 1604 -3 C

ATOM 4805 O ASP D 1 -37.619 85.166 24.204 1.00183.32 O

ANISOU 4805 O ASP D 1 24307 21279 24066 805 1512 240 O

ATOM 4806 N ILE D 2 -36.132 84.271 25.652 1.00176.78 N

ANISOU 4806 N ILE D 2 23063 20873 23234 580 1633 -156 N

ATOM 4807 CA ILE D 2 -35.818 83.053 24.902 1.00168.13 C

ANISOU 4807 CA ILE D 2 21924 20066 21890 581 1600 -70 C

ATOM 4808 CB ILE D 2 -35.049 82.105 25.800 1.00161.34 C

ANISOU 4808 CB ILE D 2 20819 19509 20975 442 1671 -277 _ C

ATOM 4809 CGl ILE D 2 -33.714 82.718 26.200 1.00164.89 C

ANISOU 4809 CGl ILE D 2 21283 19955. 21411 165 1882 -335 C

ATOM 4810 CDl ILE D 2 -32.942 81.870 27.174 1.00161.64 C

ANISOU 4810 CDl ILE D 2 20620 19767 21027 32 1961 -597 C

ATOM 4811 CG2 ILE D 2 -34.891 80.758 25.127 1.00159.37 C

ANISOU 4811 CG2 ILE D 2 20475 19546 20533 530 1573 -243 C

ATOM 4812 C ILE D 2 -37.015 82.239 24.447 1.00164.51 C

ANISOU 4812 C ILE D 2 21434 19715 21356 838 1396 -4 C

ATOM 4813 O ILE D 2 -37.877 81.918 25.258 1.00167.26 O

ANISOU 4813 O ILE D 2 21634 20119 21799 957 1297 -140 O

ATOM 4814 N GLN D 3 -37.052 81.844 23.177 1.00145.09 N

ANISOO 4814 N GLN D 3 19094 17318 18714 908 1340 184 N

ATOM 4815 CA GLN D 3 -38.199 81.081 22.696 1.00145.21 C

ANISOU 4815 CA GLN D 3 19074 17435 18666 1149 1147 223 C

ATOM 4816 CB GLN D 3 - -39.044 81.919 21.738 1.00163.41 C

ANISOU 4816 CB GLN D 3 21597 19517 20975 1330 1047 423 C

ATOM 4817 CG GLN D 3 -38.605 81.827 20.284 1.00178.00 C

ANISOU 4817 CG GLN D 3 23655 21364 22614 1282 1090 672 C

ATOM 4818 CD GLN D 3 -39.408 82.737 19.363 1.00198.67 C

ANISOU 4818 CD GLN D 3 26513 23729 25243 1472 985 902 C

ATOM 4819 OEl GLN D 3 -40.060 83.684 19.819 1.00207.24 O

ANISOU 4819 OEl GLN D 3 27654 24541 26548 1577 940 877 O

ATOM 4820 NE2 GLN D 3 -39.357 82.456 18.056 1.00195.48 N

ANISOU 4820 NE2 GLN D 3 26248 23429 24597 1530 938 1120 N

ATOM 4821 C GLN D 3 -37.814 79.772 22.036 1.00136.30 C

ANISOU 4821 C GLN D 3 17853 16602 17331 1157 1105 225 C

ATOM 4822 O GLN D 3 -37.000 79.744 21.124 1.00135.93 O

ANISOU .4822 O GLN D 3 17887 16643 17116 1059 1178 326 O

ATOM 4823 N MET D 4 -38.431 78.689 22.486 1.00145.47 N

ANISOU 4823 N MET D 4 18843 17916 18514 1273 987 102 N

ATOM 4824 CA MET D 4 -38.114 77.357 21.979 1.00145.13 C

ANISOU 4824 CA MET D 4 18'690 18126 18327 1289 937 60 C

ATOM 4825 CB MET D 4 -38.318 76.323 23.085 1.00139.78 C

ANISOU 4825 CB MET D 4 17804 17566 17739 1296 891 -113 C

ATOM 4826 CG MET D 4 -37.306 76.394 24.208 1.00137.97 C

ANISOU 4826 CG MET D 4 17473 17389 17562 1124 1013 -221 C

ATOM 4827 SD MET D ' 4 -35.649 76.029 23.622 1.00130.98 S

ANISOU 4827 SD MET D 4 16585 16662 16518 969 1135 -220 S

ATOM 4828 CE MET D 4 -34.901 77.657 23.563 1.00140.97 C

ANISOU 4828 CE MET D 4 18009 17739 17816 800 1306 -149 C

ATOM 4829 C MET D 4 -38.929 76.936 20.751 1.00150.49 C

ANISOU 4829 C MET D 4 19425 18875 18880 1467 798- 152 C

ATOM 4830 O MET D 4 -40.150 76.771 20.827 1.00152.69 O

ANISOU 4830 O MET D 4 19664 19127 19223 1634 665 121 O

ATOM 4831 N THR D 5 -38.253 76.732 19.627 1.00149.07 N

ANISOU 4831 N THR D 5 19307 18827 18507 1423 832 . 235 N

ATOM 4832 CA THR D 5 -38.923 76.238 18.427 1.00149.88 C

ANISOU 4832 CA THR D 5 19441 19059 18447 1575 710 302 C

ATOM 4833 CB THR D 5 -38.510 77.047 17.180 1.00151.01 C

ANISOU 4833 CB THR D 5 19767 19228 18383 1506 787 498 C

ATOM 4834 OGl THR D 5 -37.106 77.320 17.239 1.00148.64 O

ANISOU 4834 OGl THR D 5 19570 18765 18142 1306 960 562 O

ATOM 4835 CG2 THR D 5 -39.278 78.372 17.115 1.00152.96 C

ANISOU 4835 CG2 THR D 5 20173 19396 18548 1700 663 683 C

ATOM 4836 C THR D 5 -38.662 74.737 18.223 1.00142.95 C

ANISOU 4836 C THR D 5 18377 18422 17517 1595 652 136 C

ATOM 4837 O THR D 5 -37.623 74.332 17.691 1.00139.06 O

ANISOU 4837 O THR D 5 17846 18092 16898 1495 722 100 O

ATOM 4838 N GLN D 6 -39.609 73.911 18.654 1.00141.92 N

ANISOU 4838 N GLN D 6 18122 18309 17492 1716 529 18 N

ATOM 4839 CA GLN D 6 -39.386 72.473 18.633 1.00142.05 C

ANISOU 4839 CA GLN D 6 17971 18487 17515 1714 486 -147 C

ATOM 4840 CB GLN D 6 -39.733 71.817 19.976 1.00140.29 C

ANISOU 4840 CB GLN D 6 17619 18193 17490 1687 469 -267 C ATOM 4841 CG GLN D 6 -41.065 71.076 20.012 1.00134.81 C

ANISOU 4841 CG GLN D 6 16813 17541 16868 1795 339 -378 C

ATOM 4842 CD GLN D 6 -41.273 70.322 21.310 1.00130.08 C

ANISOU 4842 CD GLN D 6 16097 16897 16432 1723 347 -473 C

ATOM 4843 OEl GLN D 6 -42.207 69.538 21.437 1.00130.95 O

ANISOU 4843 OEl GLN D 6 16112 17026 16617 1763 268 -565 O

ATOM 4844 NE2 GLN D 6 -40.401 70.557 22.280 1.00122.48 N

ANISOU 4844 NE2 GLN D 6 15136 15890 15511 1606 447 -449 N

ATOM 4845 C GLN D 6 -40.168 71.819 17.532 1.00144.06 C

ANISOU 4845 C GLN D 6 18180 18894 17662 1856 357 -195 C

ATOM 4846 O GLN D 6 -41.373 72.017 17.402 1.00141.86 O

ANISOU 4846 O GLN D 6 17893 18590 17419 1991 247 -202 O

ATOM 4847 N SER D 7 -39.456 71.021 16.753 1.00162.55 N

ANISOU 4847 N SER D 7 20470 21419 19874 1826 371 -262 N

ATOM 4848 CA SER D 7 -40.012 70.339 15.605 1.00166.58 C

ANISOU 4848 CA SER D 7 20911 22121 20260 1942 262 -349 C

ATOM 4849 CB SER D 7 -39.401 70.937 14.347 1.00171.51 C

ANISOU 4849 CB SER D 7 21652 22894 20619 1943 296 -212 C

ATOM 4850 OG SER D 7 -38.097 71.422 14.627 1.00170.61 O

ANISOU 4850 OG SER D 7 21574 22804 20447 1774 446 -178 O

ATOM 4851 C. SER D 7 -39.642 68.876 15.710 1.00162.45 C

ANISOU 4851 C SER D 7 20224 21708 19791 1907 252 -560 C

ATOM 4852 O SER D 7 -38.618 68.549 16.286 1.00157.95 O

ANISOU 4852 O SER D 7 19625 21114 19276 1799 339 -596 O

ATOM 4853 N PRO D 8 -40.453 67.983 15.137 1.00163.52 N

ANISOU 4853 N PRO D 8 20246 21967 19918 2006 140 -716 N

ATOM 4854 CA PRO D 8 -41.679 68.152 14.363 1.00164.66 C

ANISOU 4854 CA PRO D 8 20381 22202 19980 2148 22 -724 C

ATOM 4855 CB PRO D 8 -41.778 66.820 13.638 1.00168.93 C

ANISOU 4855 CB PRO D 8 20750 22921 20514 2188 -51 -975 C

ATOM 4856 CG PRO D 8 -41.241 65.887 14.626 1.00161.89 C

ANISOU 4856 CG PRO D 8 19783 21895 19834 2088 -2 -1090 C

ATOM 4857 CD PRO D 8 -40.017 66.583 15.101 1.00164.68 C

ANISOU 4857 CD PRO D 8 20244 22199 20129 1986 123 -934 C

ATOM 4858 C PRO D 8 -42.869 68.263 15.281 1.00162.83 C

ANISOU 4858 C PRO D 8 20132 21802 19934 2195 -37 -725 C

ATOM 4859 O PRO D 8 -42.788 67.791 16.411 1.00163.26 O

ANISOU 4859 O PRO D 8 20149 21699 20183 2105 8 -761 O

ATOM 4860 N SER D 9 -43.959 68.840 14.783 1.00150.23 N

ANISOU 4860 N SER D 9 18550 20266 18263 2338 -140 -695 N

ATOM 4861 CA SER D 9 -45.150 69.122 15.585 1.00150.50 C

ANISOU 4861 CA SER D 9 18547 20183 18455 2397 -201 -724 C

ATOM 4862 CB SER D 9 -46.071 70.056 14.809 1.00152.65 C

ANISOU 4862 CB SER D 9 18878 20537 18585 2589 -313 -638 C

ATOM 4863 OG SER D 9 -46.229 69.580 13.486 1.00155.88 O

ANISOU 4863 OG SER D 9 19236 21206 18784 2682 -392 -702 O

ATOM 4864 C SER D 9 -45.920 67.864 15.974 1.00148.76 C

ANISOU 4864 C SER D 9 18137 19993 18393 2370 -254 -964 C

ATOM 4865 O SER D 9 -46.400 67.735 17.111 1.00143.95 O

ANISOU 4865 O SER D ' 9 17472 19258 17963 2315 -243 -1011 O

ATOM 4866 N SER D 10 -46.066 66.966 15.001 1.00151.79 N

ANISOU 4866 N SER D 10 18417 20555 18702 2397 -305 -1125 N

ATOM 4867 CA SER D 10 -46.584 65.621 15.226 1.00157.54 C

ANISOU 4867 CA SER D 10 18974 21294 19591 2344 -340 -1368 C

ATOM 4868 CB SER D 10 -47.963 65.428 14.591 1.00165.68 C

ANISOU 4868 CB SER D 10 19874 22489 20586 2464 -463 -1530 C

ATOM 4869 OG SER D 10 -47.911 65.560 13.185 1.00174.53 O

ANISOU 4869 OG SER D 10 20997 23861 21457 2608 -541 -1535 O

ATOM 4870 C SER D 10 -45.581 64.683 14.599 1.00159.00 C

ANISOU 4870 C SER D 10 19108 21575 19729 2307 -323 -1487 C

ATOM 4871 O SER D 10 -44.611 65.143 14.006 1.00158.35 O

ANISOU 4871 O SER D 10 19102 21608 19456 2335 -294 -1394 O

ATOM 4872 N LEU D 11 -45.796 63.378 14.719 1.00152.19 N

ANISOU 4872 N LEU D 11 18115 20669 19043 2240 -338 -1703 N

ATOM 4873 CA LEU D 11 -44.812 62.430 14.212 1.00151.06 C

ANISOU 4873 CA LEU D 11 17917 20567 18912 2208 -320 -1841 C

ATOM 4874 CB LEU D 11 -43.501 62.583 14.974 1.00146.90 C

ANISOU 4874 CB LEU D 11 17498 19884 18434 2125 -222 -1686 C

ATOM 4875 CG LEU D 11 -42.448 61.516 14.694 1.00147.18 C

ANISOU 4875 CG LECJ D 11 17475 19898 18548 2093 -202 -1827 C

ATOM 4876 CDl LEU D 11 -42.332 61.221 13.192 1.00153.48 C

ANISOU 4876 CDl LEU D 11 18190 20981 19143 2169 -233 -1990 C

ATOM 4877 CD2 LEU D 11 -41.123 61.971 15.271 1.00140.62 C

ANISOU 4877 CD2 LEU D 11 16751 18947 17732 2029 -110 -1645 C

ATOM 4878 C LEU D 11 -45.259 61.004 14.369 1.00150.40 C

ANISOU 4878 C LEU D 11 17692 20396 19057 2148 -355 -2094 C

ATOM 4879 O LEU D 11 -45.332 60.508 15.489 1.00145.83 O ANISOU 4879 O LEU D 11 17130 19579 18701 2041 -318 -2064 O

ATOM 4880 N SER D 12 -45.530 60.335 13.252 1.00140.89 N

ANISOU 4880 N SER D 12 16349 19388 17795 2207 -423 -2344 N

ATOM 4881 CA SER D 12 -45.844 58.916 13.303 1.00141.55 C

ANISOU 4881 CA SER D 12 16298 19366 18120 2137 -448 -2614 C

ATOM 4882 CB SER D 12 -46.917 58.508 12.281 1.00149.07 C

ANISOU 4882 CB SER D 12 17067 20567 19005 2199 -536 -2903 C

ATOM 4883 OG SER D 12 -47.225 59.550 11.369 1.00147.49 O

ANisoσ 4883 OG SER D 12 16868 20688 18484 2343 -591 -2836 O

ATOM 4884 C SER D 12 -44.600 58.070 13.164 1.00136.22 C

ANISOU 4884 C SER D 12 15619 18599 17538 2117 -420 -2701 C

ATOM 4885 O SER D 12 -43.753 58.288 12.296 1.00137.23 O

ANISOU 4885 O SER D 12 15750 18917 17474 2187 -412 -2704 O

ATOM 4886 N ALA D 13 -44.489 ' 57.114 14.061 1.00161.88 N

ANISOU 4886 N ALA D 13 18866 21557 21083 2021 -403 -2761 N

ATOM 4887 CA ALA D 13 -43.436 56.138 13.976 1.00167.98 C

ANISOU 4887 CA ALA D ' 13 19617 22204 22002 2027 -403 -2887 C

ATOM 4888 CB ALA D 13 -42.345 56.449 14.964 1.00161.73 C

ANISOU 4888 CB ALA D 13 18967 21279 21205 2021 -344 -2632 C

ATOM 4889 C ALA D 13 -44.102 54.828 14.301 1.00170.19 C

ANISOU 4889 C ALA D 13 19845 22201 22617 1932 -423 -3055 C

ATOM 4890 O ALA D 13 -45.276 54.810 14.668 1.00171.89 O

ANISOU 4890 O ALA D 13 20081 22290 22940 1826 -405 -2987 O

ATOM 4891 N SER D 14 -43.369 53.733 14.154 1.00151.60 N

ANISOU 4891 N SER D 14 17422 19744 20436 1962 -455 -3284 N

ATOM 4892 CA SER D 14 -43.936 52.426 14.409 1.00148.51 C

ANISOU 4892 CA SER D 14 16986 19059 20383 1867 -475 -3469 C

ATOM 4893 CB SER D 14 -43.830 51.563 ,13.161 1.00152.00 C

ANISOU 4893 CB SER D 14 17242 19625 20887 1932 -534 -3886 C

ATOM 4894 OG SER D 14 -44.177 52.318 12.016 1.00150.28 O

ANISOU 4894 OG SER D 14 16912 19856 20331 2026 -554 -3988 O

ATOM 4895 C SER D 14 -43.216 51.787 15.579 1.00144.83 C

ANISOU 4895 C SER D 14 16662 18203 20163 1831 -460 -3289 C

ATOM 4896 O SER D 14 -42.174 52.270 16.009 1.00144.02 O

ANISOU 4896 O SER D 14 16648 18111 19963 1907 -448 -3100 O

ATOM 4897 N LEU D 15 ,-43.782 50.708 16.100 1.00144.06 N

ANISOU 4897 N LEU D 15 16588 17773 20377 1708 -461 -3344 N

ATOM 4898 CA LEU D 15 -43.225 50.057 17.271 1.00149.42 C

ANISOU 4898 CA LEU D 15 17425 18059 21290 1668 -456 -3130 C

ATOM 4899 CB LEU D 15 -44.053 48.833 17.633 1.00152.53 C

ANISOU 4899 CB ' LEU D 15 17834 18089 22031 1507 -452 -3234 C

ATOM 4900 CG LEU D 15 -45.167 49.075 18.644 1.00157.64 C

ANISOU 4900 CG LEU D 15 18570 18597 22728 1284 -375 -3007 C

ATOM 4901 CDl LEU D 15 -45.658 47.742 19.178 1.00165.69 C

ANISOU 4901 CDl LEU D 15 19737 19136 24082 1171 -371 -2881 C

ATOM 4902 CD2 LEU D 15 -44.685 49.959 19.787 1.00155.23 C

ANISOU 4902 CD2 LEU D 15 18355 18473 22153 1291 -328 -2668 C

ATOM 4903 C LEU D 15 -41.770 49.654 17.084 1.00151.10 C

ANIΞOU 4903 C LEU D 15. 17659 18197 21556 1841 -513 -3164 C

ATOM 4904 O LEU D 15 -41.469 48.769 16.292 1.00154.67 O

ANISOU 4904 O LEU D 15 18016 18565 22186 1917 -573 -3464 O

ATOM 4905 N GLY D 16 -40.876 50.305 17.824 1.00154.34 N

ANISOU 4905 N GLY D 16 18175 18646 21821 1903 -496 -2884 N

ATOM 4906 CA GLY D 16 -39.466 49.954 17.822 1.00154.60 C

ANISOU 4906 CA GLY D 16 18220 18614 21906 2067 -552 -2905 C

ATOM 4907 C GLY D 16 -38.581 50.873 16.995 1.00153.83 C

ANISOU 4907 C GLY D 16 18030 18915 21505 2188 -539 -2982 C

ATOM 4908 O GLY D 16 -37.351 50.785 17.030 1.00152.74 O

ANISOU 4908 O GLY D 16 17880 18806 21347 2317 -569 -2994 O

ATOM 4909 N GLU D 17 -39.210 51.759 16.240 1.00161.36 N

ANISOU 4909 N GLU D 17 18912 20186 22210 2145 -494 -3034 N

ATOM 4910 CA GLU D 17 -38.482 52.648 15.356 1.00162.01 C

ANISOU 4910 CA GLU D 17 18919 20653 21986 2228 -468 -3092 C

ATOM 4911 CB GLU D 17 -39.466 53.296 14.391 1.00164.11 C

ANISOU 4911 CB GLU D 17 19107 21217 22032 2189 -447 -3182 C

ATOM 4912 CG GLU D 17 -38.916 54.455 13.608 1.00161.85 C

ANISOU 4912 CG GLU D 17 18801 21311 21383 2233 -400 -3122 C

ATOM 4913 CD GLU D 17 -39.951 55.033 12.678 1.00167.63 C

ANISOU 4913 CD GLU D 17 19464 22331 21897 2225 -404 -3202 C

ATOM 4914 OEl GLU D 17 -39.768 56.187 12.249 1.00174.14 O

ANISOU 4914 OEl GLU D 17 20319 23433 22413 2240 -361 -3071 O

ATOM r 4915 0E2 GLU D 17 -40.949 54.335 12.382 1.00167.65 O

ANISOU 4915 0E2 GLU D 17 19382 22280 22037 2201 -452 -3390 O

ATOM 4916 C GLU D 17 -37.794 53.715 16.180 1.00159.92 C

ANISOU 4916 C GLU D 17 18771 20447 21543 2216 -404 -2774 C

ATOM 4917 O GLU D 17 -38.437 54.345 17.007 1.00158.86 O

ANISOU 4917 O GLU D 17 18743 20253 21362 2119 -357 -2522 O ATOM 4918 N ARG D 18 -36.494 53.919 15.978 1.00152.26 N

ANIΞOU 4918 N ARG D 18 17764 19610 20477 2308 -400 -2814 N

ATOM 4919 CA ARG D 18 -35.803 54.995 16.690 1.00143.90 C

ANISOU 4919 CA ARG D 18 16791 18659 19226 2279 -325 -2555 C

ATOM 4920 CB ARG D 18 -34.284 54.962 16.489 1.00145.64 C

ANISOU 4920 CB ARG D 18 16929 19040 19366 2378 -323 -2671 C

ATOM 4921 CG ARG D 18 -33.757 56.061 15.576 1.00142.69 C

ANISOU 4921 CG ARG D 18 16488 19070 18657 2349 -239 -2729 C

ATOM 4922 CD ARG D 18 -32.247 56.019 15.438 1.00139.25 C

ANISOU 4922 CD ARG D 18 15970 18817 18121 2403 -208 -2817 C

ATOM 4923 NE ARG D 18 -31.561 55.721 16.697 1.00148.47 N

ANISOU 4923 NE ARG D 18 17188 19757 19466 2457 -247 -2701 N

ATOM 4924 CZ ARG D 18 -30.946 56.623 17.461 1.00147.82 C

ANISOU 4924 CZ ARG D 18 17156 19741 19267 2408 -176 -2514 C

ATOM 4925 NHl ARG D 18 -30.938 57.903 17.104 1.00139.53 N

ANISOU 4925 NHl ARG D 18 16130 18941 17945 2285 -51 -2416 N

ATOM 4926 NH2 ARG D 18 -30.333 56.244 18.586 1.00141.04 N

ANISOU 4926 NH2 ARG D 18 16326 18698 18564 2480 -234 -2428 N

ATOM 4927 C ARG D 18 -36.360 56.285 16.150 1.00138.88 C

ANISOU 4927 C ARG D 18 16179 18283 18305 2202 -248 -2450 C

ATOM 4928 O ARG D 18 -36.910 56.321 15.051 1.00138.44 O

ANISOU 4928 O ARG D 18 16038 18442 18121 2219 -257 -2619 O

ATOM 4929 N VAL D 19 -36.219 57.351 16.915 1.00134.07 N

ANISOU 4929 N VAL D 19 15686 17659 17595 2127 -178 -2173 N

ATOM 4930 CA VAL D 19 -36.855 58.589 16.533 1.00134.46 C

ANISOU 4930 CA VAL D 19 15786 17890 17412 2068 -116 -2045 C

ATOM 4931 CB VAL D / 19 -38.376 58.475 16.730 ~1.00137.67 C

ANISOU 4931 CB VAL D 19 16221 18182 17907 2025 -150 -2006 C

ATOM 4932 CGl VAL D 19 -38.717 58.197 18.195 1.00130.08 C

ANISOU 4932 CGl VAL D 19 15354 16971 17100 1946 -131 -1799 C

ATOM 4933 CG2 VAL D 19 -39.066 59.718 16.231 1.00143.59 C

ANISOU 4933 CG2 VAL D 19 16989 19157 18413 2026 -126 -1948 C

ATOM 4934 C VAL D 19 -36.289 59.764 17.317 1.00127.00 C

ANISOU 4934 C VAL D 19 14942 16978 16334 2004 -22 -1803 C

ATOM 4935 O VAL D 19 -35.759 59.591 18.416 1.00124.03 O

ANISOU 4935 O VAL D 19 14597 16465 16062 1990 -10- -1711 O

ATOM 4936 N SER D 20 -36.387 60.962 16.754 1.00117.82 N

ANISOU 4936 N .SER D 20 13830 15994 14941 1967 43 -1703 N

ATOM 4937 CA SER D 20 -35.811 62.116 17.427 1.00120.14 C

ANISOU 4937 CA SER D 20 14218 16297 15133 1890 141 -1499 C

ATOM 4938 CB SER D 20 -34.371 62.300 16.984 1.00118.95 C

ANISOU 4938 CB SER D 20 14015 16335 14844 1876 208 -1574 C

ATOM 4939 OG SER D 20 -33.562 61.362 17.649 1.00118.11 O

ANISOU 4939 OG SER D 20 13839 16143 14895 1920 173 -1666 O

ATOM 4940 C SER D 20 -36.563 63.443 17.327 1.00127.07 C

ANIΞOU 4940 C SER D 20 15209 17200 15873 1842 191 -1312 C

ATOM 4941 O SER D 20 -36.719 64.002 16.247 1.00135.49 O

ANISOU 4941 O SER D 20 16294 18439 16747 1860 201 -1308 O

ATOM 4942 N LEU D 21 -37.008 63.942 18.477 1.00122.81 N

ANISOU 4942 N LEU D 21 14741 16492 15431 1792 214 -1158 N

ATOM 4943 CA LEU D 21 -37.491 65.302 18.608 1.00117.61 C

ANISOU 4943 CA LEU D 21 14191 15818 14676 1750 272 -982 C

ATOM 4944 CB LEU D 21 -38.290 65.446 19.891 1.00113.74 C

ANISOU 4944 CB LEU D 21 13726 15150 14339 1720 259 -898 C

ATOM 4945 CG LEU D 21 -39.237 64.282 20.111 1.00115.34 C

ANISOU 4945 CG LEU D 21 13851 15259 14713 1746 170 -1000 C

ATOM 4946 CDl LEU D 21 -40.098 64.502 21.341 1.00112.55 C

ANISOU 4946 CDl LEU D 21 13511 14769 14482 1682 181 -913 C

ATOM 4947 CD2 LEU D 21 -40.073 64.106 18.863 1.00118.91 C

ANIΞOU 4947 CD2 LEU D 21 14262 15798 15122 1823 92 -1109 C

ATOM 4948 C LEU D 21 -36.287 66.212 18.684 1.00118.97 C

ANISOU 4948 C LEU D 21 14412 16049 14741 1664 389 -903 C

ATOM 4949 O LEU D 21 -35.293 65.881 19.324 1.00116.61 O

ANISOU 4949 O LEU D 21 14064 15736 14506 1626 422 -941 O

ATOM 4950 N THR D 22 -36.375 67.359 18.028 1.00137.87 N

ANISOU 4950 N THR D 22 16906 18511 16969 1633 451 -791 N

ATOM 4951 CA THR D 22 -35.336 68.369 18.105 1.00140.04 C

ANISOU 4951 CA THR D 22 17244 18823 17142 1515 585 -706 C

ATOM 4952 CB THR D 22 -34.781 68.662 16.724 1.00144.18 C

ANISOU 4952 CB THR D 22 17793 19555 17435 1486 636 -709 C

ATOM 4953 OGl THR D 22 -35.568 69.697 16.127 1.00150.90 O

ANISOU 4953 OGl THR D 22 18808 20355 18172 1461 677 -510 O

ATOM 4954 CG2 THR D 22 -34.825 67.400 15.832 1.00138.93 C

ANISOU 4954 CG2 THR D 22 17024 19043 16720 1602 526 -867 C

ATOM 4955 C THR D 22 -35.963 69.643 18.683 1.00142.32 C

ANISOU 4955 C THR D 22 17664 18946 17464 1472 632 -531 C

ATOM 4956 O THR D 22 -37.180 69.787 18.710 1.00144.60 O ANISOU 4956 O THR D 22 17988 19136 17816 1556 552 -483 O

ATOM 4957 N CYS D 23 -35.148 70.577 19.142 1.00136 .89 N

ANISOU 4957 N CYS D 23 17036 18232 16744 1344 761 -461 N

ATOM 4958 CA CYS D 23 -35.683 71.718 19.858 1.00137 .21 C

ANISOU 4958 CA CYS D 23 17187 18087 16858 1302 808 -333 C

ATOM 4959 CB CYS D 23 -35.875 71.313 21.314 1.00134 .31 C

ANISOU 4959 CB CYS D 23 16731 17627 16672 1289 794 -396 C

ATOM 4960 SG CYS D 23 -36.975 72.335 22.333 1.00160. 82 S

ANISOU 4960 SG CYS D 23 20150 20779 20176 1321 770 -324 S

ATOM 4961 C CYS D 23 -34.666 72.837 19.760 1.00143 92 C

ANISOU 4961 C CYS D 23 18126 18942 17616 1141 968 -261 C

ATOM 4962 O CYS D 23 -33.745 72.885 20.560 1.00142. 97 O

ANISOU 4962 O CYS D 23 17926 18876 17519 1026 1059 -347 O

ATOM 4963 N ARG D 24 -34.802 73.720 18.771 1.00154 79 N

ANISOD 4963 N ARG D 24 19665 20268 18880 1127 1003 -104 N

ATOM 4964 CA ARG D 24 -33.749 74.715 18.525 1.00160, 61 C

ANISOU 4964 CA ARG D 24 20508 20993 19525 939 1173 -19 C

ATOM 4965 CB ARG D 24 -33.703 75.194 17.064 1.00173. 93 C

ANISOU 4965 CB ARG D 24 22358 22725 21001 934 1191 158 C

ATOM 4966 CG ARG D 24 -32.342 75.817 16.658 1.00184, 26 C

ANISOU 4966 CG ARG D 24 23617 24297 22095 785 1306 105 C

ATOM 4967 CD ARG D 24 -32.247 76.135 15.167 1.00193, 51" C

ANISOU 4967 CD ARG D 24 24975 25519 23032 738 1352 319 C

ATOM 4968 NE ARG D 24 -32.839 75.081 14.354 1.00209. 26 N

ANISOU 4968 NE ARG D 24 26867 27830 24813 807 1287 236 N

ATOM 4969 CZ ARG D 24 -33.393 75.286 13.165 1.00227. 56 C

ANISOU 4969 CZ ARG D 24 29303 30266 26895 850 1256 398 C

ATOM 4970 NHl ARG D 24 -33.427 76.509 12.652 1.00228. 42 N

ANISOU 4970 NHl ARG D 24 29659 30172 26957 842 1275 686 N

ATOM 4971 NH2 ARG D 24 -33.919 74.270 12.493 1.00236. 56 N

ANISOU 4971 NH2 ARG D 24 30310 31729' 27843 910 1198 270 N

ATOM 4972 C ARG D 24 -33.898 75.893 19.448 1.00154. 98 C

ANISOU 4972 C ARG D 24 19878 20033 18974 861 1248 37 C

ATOM 4973 O ARG D 24 -35.009 76.300 19.757 1.00155. 49 O

ANISOU 4973 O ARG D 24 19996 19920 19164 982 1159 91 O

ATOM 4974 N ALA D 25 -32.763 76.437 19.871 1.00146. 43 N

ANISOU 4974 N ALA D 25 18787 18957 17893 656 1414 -6 N

ATOM 4975 CA ALA D 25 -32.726 77.445 20.923 1.00145. 23 C

ANISOU 4975 CA ALA D 25 18678 18587 17915 561 1499 -10 C

ATOM 4976 CB ALA D 25 -31.292 77.882 21.197 1.00144. 70 C

ANISOU 4976 CB ALA D 25 18550 18603 17825 316 1689 -114 C

ATOM 4977 C ALA D 25 -33.571 78.646 20.572 1.00150. 07 C

ANISOU 4977 C ALA D 25 19524 18927 18569 597 1496 195 C

ATOM 4978 O ALA D 25 -34.791 78.555 20.440 1.00154. 26 O

ANISOU 4978 O ALA D 25 20121 19383 19107 796 1348 291 O

ATOM 4979 N SER D 26 -32.893 79.774 20.415 1.00136. 26 N

ANISOU 4979 N SER D 26 17895 17026 16852 402 1660 253 N

ATOM 4980 CA SER D 26 -33-.509 81.057 20.122 1.00142. 71 C

ANISOU 4980 CA SER D 26 18958 17528 17739 418 1674 457 C

ATOM 4981 CB SER D 26 -34.598 81.374 21.153 1.00146. 15 C

ANISOU 4981 CB SER D 26 19369 17732 18428 550 1589 384 C

ATOM 4982 OG SER D 26 -35.412 82.468 20.776 1.00149. 90 O

ANISOU 4982 OG SER D 26 20061 17924 18970 698 1506 578 O

ATOM 4983 C SER D 26 -32.330 81.978 20.305 1.00147. 67 C

ANISOU 4983 C SER D 26 19635 18108 18364 117 1903 439 C

ATOM 4984 O SER D 26 -31.291 81.537 20.800 1.00145. 12 O

ANISOU 4984 O SER D 26 19124 18018 17998 -30 1997 245 O

ATOM 4985 N GLN D 27 -32.453 83.236 19.897 1.00203. 67 N

ANISOU 4985 N GLN D 27 26977 24905 25504 20 1994 631 N

ATOM 4986 CA GLN D 27 -31.440 84.207 20.286 1.00216. 78 C

ANISOU 4986 CA GLN D 27 28667 26461 27239 -291 2225 565 C

ATOM 4987 CB GLN D 27 -31.840 85.641 19.904 1.00228. 16 C

ANISOU 4987 CB GLN D 27 30405 27453 28831 -351 2293 775 C

ATOM 4988 CG GLN D 27 -31.569 86.019 18.448 1.00234. 77 C

ANISOU 4988 CG GLN D 27 31530 28207 29464 -392 2323 1122 C

ATOM 4989 CD GLN D 27 -32.056 87.419 18.113 1.00258. 48 C

ANISOU 4989 CD GLN D 27 34853 30709 32650 -383 2342 1362 C

ATOM 4990 OEl GLN D 27 -32.358 88.213 19.005 1.00263. 16 O

ANISOU 4990 OEl GLN D 27 35440 31007 33541 -395 2369 1230 O

ATOM 4991 NE2 GLN D 27 -32.135 87.727 16.821 1.00267. 47 N

ANISOU 4991 NE2 GLN D 27 36271 31749 33607 -352 2320 1715 N

ATOM 4992 C GLN D 27 -31.264 84.053 21.800 1.00209. 14 C

ANISOU 4992 C GLN D 27 27442 25569 26453 -296 2225 258 C

ATOM 4993 O GLN D 27 -32.064 84.568 22.588 1.00202. 87 O

ANISOU 4993 O GLN D 27 26602 24653 25827 -99 2089 201 O

ATOM 4994 N ASP D 28 -30.221 83.313 22.175 1.00201. 17 N

ANISOU 4994 N ASP D 28 26249 24802 25384 -513 2370 54 N ATOM 4995 CA ASP D 28 -29.940 82.900 23.547 1.00194.91 C

ANISOU 4995 CA ASP D 28 25184 24176 24697 -517 2364 -237 C

ATOM 4996 CB ASP D 28 -31.120 83.157 24.492 1.00192.45 C

ANISOU 4996 CB ASP D 28 24856 • 23645 24623 -358 2258 -297 C

ATOM 4997 CG ASP D 28 -31.181 84.598 24.996 1.00200.76 •C

ANISOU 4997 CG ASP D 28 26126 24277 25876 -439 2344 -209 C

ATOM 4998 ODl ASP D 28 -30.120 85.239 25.143 1.00211.69 O

ANISOU 4998 ODl ASP D 28 27583 25557 27294 -710 2546 -232 O

ATOM 4999 OD2 ASP D 28 -32.302 85.088 25.252 1.00194.08 O

ANISOU 4999 OD2 ASP D 28 25372 23198 25170 -230 2209 -132 O

ATOM 5000 C ASP D 28 -29.613 81.414 23.518 1.00176.21 C

ANISOU 5000 C ASP D 28 22605 22180 22168 -381 2244 -335 C

ATOM 5001 O ASP D 28 -30.390 80.605 23.015 1.00171.59 O

ANISOU 5001 O ASP D 28 22051 21630 21515 -161 2076 -222 O

ATOM 5002 N ILE D 29 -28.450 81.057 24.035 1.00146.94 N

ANISOU 5002 N ILE D 29 18679 18745 18405 -512 2329 -556 N

ATOM 5003 CA ILE D 29 -28.113 79.656 24.163 1.00144.73 C

ANISOU 5003 CA ILE D 29 18196 18784 18009 -371 2209 -666 C

ATOM 5004 CB ILE D 29 -26.565 79.432 24.063 1.00149.14 C

ANISOU 5004 CB ILE D 29 18576 19660 18431 -558 2343 -861 C

ATOM 5005 CGl ILE D ' 29 -26.094 78.277 24.944 1.00148.23 C

ANISOU 5005 CGl ILE D 29 18190 19821 18309 -437 2242 -1073 C

ATOM 5006 CDl ILE D 29 -24.595 78.068 24.875 1.00149.18 C

ANISOU 5006 CDl ILE D 29 18103 20275 18305 -594 2360 -1304 C

ATOM 5007 CG2 ILE D 29 -25.790 80.711 24.389 1.00143.77 C

ANISOU 5007 CG2 ILE D 29 17929 18891 17806- -864 2576 -940 C

ATOM 5008 C ILE D 29 -28.744 79.134 25.456 1.00136.47 C

ANISOU 5008 C ILE D 29 17013 17741 17097 -203 2073 -764 C

ATOM 5009 O ILE D 29 -28.446 79.639 26.536 1.00137.30 O

ANISOU 5009 O ILE D 29 17038 17808 17322 -294 2141 -898 O

ATOM 5010 N GLY D 30 -29.669 78.180 25.339 1.00133.09 N

ANISOU 5010 N GLY D 30 16566 17355 16649 26 1888 -697 N

ATOM 5011 CA GLY D 30 -30.200 77.518 26.509 1.00123.69 C

ANISOU 5011 CA GLY D 30 15241 16205 15550 163 1767 -775 C

ATOM 5012 C GLY D 30 -29.053 77.304 27.500 1.00133.88 C

ANISOU 5012 C GLY D 30 16314 17737 16817 67 1830 -983 . C

ATOM 5013 O GLY D 30 -29.071 77.853 28.608 1.00133.91 O

ANISOU 5013 O GLY D 30 16233 17732 16915 19 1861 -1088 O

ATOM 5014 N GLY D 31 -28.027 76.551 27.084 1.00133.14 N

ANISOU 5014 N GLY. D 31 16116 17884 16589 43 1847 -1064 N

ATOM 5015 CA GLY D 31 -26.979 76.054 27.972 1:00120.62 C

ANISOU 5015 CA GLY D 31 14300 16573 14956 24 1852 -1261 C

ATOM 5016 c- GLY D 31 -27.394 74.705 28.544 1.00119.57 C

ANISOU 5016 C GLY D 31 14081 16518 14832 249 1658 -1233 C

ATOM 5017 O GLY D 31 -26.684 73.718 28.396 1.00116.97 O

ANISOU 5017 O GLY D 31 13652 16369 14424 349 1579 -1286 O

ATOM 5018 N ASN D 32 -28.588 74.686 29.150 1.00136.52 N

ANISOU 5018 N ASN D 32 16276 18514 17083 323 1584 -1149 N

ATOM 5019 CA ASN D 32 -29.149 73.573 29.926 1.00127.38 C

ANISOU 5019 CA ASN D 32 15048 17404 15945 489 1424 -1105 C

ATOM 5020 CB ASN D 32 -28.708 73.683 31.406 1.00135.26 C

ANISOU 5020 CB ASN D 32 15880 18574 16938 443 1443 -1224 C

ATOM 5021 CG ASN D 32 -28.688 75.153 31.946 1.00133.83 C

ANISOU 5021 CG ASN D 32 15682 18353 16813 250 1610 -1346 C

ATOM 5022 ODl ASN D 32 -27.753 75.563 32.667 1.00126.27 O

ANISOU 5022 ODl ASN D 32 14576 17595 15805 137 1702 -1522 O

ATOM 5023 ND2 ASN D 32 -29.722 75.927 31.606 1.00128.77 N

ANISOU 5023 ND2 ASN D 32 15185 17454 16287 222 1641 -1271 N

ATOM 5024 C ASN D 32 -30.683 73.525 29.855 1.00123.20 C

ANISOU 5024 C ASN D 32 14649 16652 15509 581 1337 -958 C

ATOM 5025 O ASN D 32 -31.352 74.421 30.360 1.00123.83 O

ANISOU 5025 O ASN D 32 14776 16601 15674 525 1386 -954 O

ATOM 5026 ' N LEU D 33 -31.243 72.475 29.257 1.00117.58 N

ANISOU 5026 N LEU D 33 13977 15906 14793 724 1207 -866 N

ATOM 5027 CA LEU D 33 -32.707 72.383 29.031 1.00115.21 C

ANISOU 5027 CA LEU D 33 13782 15424 14570 810 1124 -754 C

ATOM 5028 CB LEU D 33 -33.023 72.766 27.575 1.00114.57 C

ANISOU 5028 CB LEU D 33 13838 15237 14458 837 1128 -684 C

ATOM 5029 CG LEU D 33 -33.941 71.912 26.697 1.00118.02 C

ANISOU 5029 CG LEU D 33 14347 15578 14919 972 1005 -600 C

ATOM 5030 CDl LEU D 33 -35.340 72.470 26.668 1.00123.69 C

ANISOU 5030 CDl LEU D 33 15179 16123 15696 992 1005 -528 C

ATOM 5031 CD2 LEU D 33 -33.396 71.871 25.292 1.00121.10 C

ANISOU 5031 CD2 LEU D 33 14767 16037 15210 1015 986 -601 C

ATOM 5032 C LEU D 33 -33.378 71.025 29.418 1.00117.20 C

ANISOU 5032 C LEU D 33 13987 15692 14850 929 982 -703 C

ATOM 5033 O LEU' D 33 -32.736 69.982 29.408 1.00116.85 O ANISOU 5033 O LEU D 33 13870 15758 14768 983 925 -723 O

ATOM 5034 N TYR D 34 -34.663 71.047 29.776 1.00127.61 N

ANISOU 5034 N TYR D 34 15347 16896 16244 967 925 -644 N

ATOM 5035 CA TYR D 34 -35.378 69.842 30.236 1.00124.21 C

ANISOU 5035 CA TYR D 34 14879 16464 15850 1034 815 -592 C

ATOM 5036 CB TYR D 34 -36.394 70.192 31.311 1.00125.72 C

ANISOU 5036 CB TYR D 34 15025 16653 16088 984 820 .-588 C

ATOM 5037 CG TYR D 34 -35.884 70.844 32.556 1.00124.50 C

ANISOU 5037 CG TYR D 34 14770 16635 15899 887 899 -652 C

ATOM 5038 CDl TYR D 34 -35.141 70.147 33.466 1.00126.32 C

ANISOU 5038 CDl TYR D 34 14907 17025 16063 874 872 -631 C

ATOM 5039 CEl TYR D 34 -34.711 70.737 34.620 1.00124.53 C

ANISOU 5039 CEl TYR D 34 14568 16968 15780 788 939 -708 C

ATOM 5040 CZ TYR D 34 -35.039 72.022 34.880 1.00125.70 C

ANISOU 5040 CZ TYR D 34 14695 17097 15968 706 1040 -826 C

ATOM 5041 OH TYR D 34 -34.613 72.608 36.035 1.00131.52 O

ANISOU 5041 OH TYR D 34 15298 18019 16654 614 1111 -941 O

ATOM 5042 CE2 TYR D 34 -35.787 72.728 34.003 1.00125.05 C

ANISOU 5042 CE2 TYR D 34 14724 16812 15979 723 1066 -835 C

ATOM 5043 CD2 TYR D 34 -36.213 72.139 32.854 1.00122.66 C

ANISOU 5043 CD2 TYR D 34 14534 16369 15701 817 992 -737 C

ATOM 5044 C TYR D 34 -36.197 69.185 29.137 1.00121.24 C

ANISOU 5044 C TYR D 34 14576 15975 15514 1126 728 -552 C

ATOM 5045 O TYR D 34 -36.541 69.818 28.146 1.00121.60 O

ANISOU 5045 O TYR D 34 14701 15948 15554 1150 741 -548 r o

ATOM 5046 N TRP ' D 35 -36.568 67.927 29.343 1.00123.21 > N

ANISOU 5046 N TRP D 35 14799 16209 15806 1172 637 -519 N

ATOM 5047 CA TRP D 35 -37.473 67.250 28.420 1.00126.00 C

ANISOU 5047 CA TRP D 35 15194 16466 16215 1242 555 -515 C

ATOM 5048 CB TRP D 35 -36.734 66.200 27.581 1.00127.27 C

ANISOU 5048 CB TRP D 35 15356 16627 16374 1324 492 .-548 C

ATOM 5049 CG TRP D 35 -35.971 66.792 26.416 1.00128.24 C

ANISOU 5049 CG TRP D 35 15510 16813 16404 1346 539 -601 C

ATOM 5050 CDl TRP D 35 -34.631 67.028 26.343 1.00130.86 C

ANISOU 5050 CDl TRP D 35 15810 17255 16657 1322 600 -643 C

ATOM 5051 NEl TRP D 35 -34.306 67.584 25.131 1.00126.19 N

ANISOU 5051 NEl TRP D 35 15265 16709 15974 1315 651 -673 N

ATOM 5052 CE2 TRP D 35 -35.451 67.717 24.399 1.00127.35 C

ANISOU 5052 CE2 TRP D 35 15480 16776 16133 1359 608 -638 C

ATOM 5053 CD2 TRP D 35 -36.515 67.229 25.175 1.00125.29 C

ANISOU 5053 CD2 TRP D 35 15199 16421 15984 1381 538 -611 C

ATOM 5054 CE3 TRP D 35 -37.801 67.265 24.647 1.00128.01 C

ANISOU 5054 CE3 TRP D 35 15577 16702 16359 1429 481 -604 C

ATOM 5055 CZ3 TRP D 35 -37.983 67.769 23.384 1.00131.68 C

ANISOU 5055 CZ3 TRP D 35 16102 17197 16732 1476 481 -603 C

ATOM 5056 CH2 TRP D 35 -36.910 68.243 22.638 1.00137.01 C

ANISOU 5056 CH2 TRP D 35 16816 17958 17284 1448 553 -597 C

ATOM 5057 CZ2 TRP D 35 -35.636 68.225 23.130 1.00136.95 C

ANISOU 5057 CZ2 TRP D 35 16766 18015 17253 1377 625 -624 C

ATOM 5058 C TRP D 35 -.38.624 66.632 29.195 1.00126.03 C

ANISOU 5058 C TRP D 35 15164 16428 16292 1205 513 -480 C

ATOM 5059 O TRP D 35 -38.413 65.982 30.212 1.00126.75 O

ANISOU 5059 O TRP D 35 15217 16551 16391 1163 501 -427 O

ATOM 5060 N LEU D 36 -39.841 66.850 ,28.706 1.00110.76 . N

ANISOU 5060 N LEU D 36 13242 14443 14399 1218 492 -510 N

ATOM 5061 CA LEU D 36 -41.057 66.495 29.440 1.00111.26 C

ANISOU 5061 CA LEU D 36 13253 14499 14523 1157 471 -508 C

ATOM 5062 CB LEU D 36 -41.791 67.765 29.876 1.00110.17 C

ANISOU 5062 CB LEU D 36 13078 14403 14380 1123 522 -555 C

ATOM 5063 CG LEU D 36 -41.202 68.701 30.923 1.00103.20 C

ANISOU 5063 CG LEU D 36 12163 13597 13452 1058 608 -558 C

ATOM 5064 CDl LEU D 36 -41.825 70.093 30.818 1.00102.38 C

ANISOU 5064 CDl LEU D 36 12056 13466 13378 1083 640 -638 C

ATOM 5065 CD2 LEU D 36 -41.409 68.091 32.282 1.00104.41 C

ANISOU 5065 CD2 LEU. D 36 12231 13858 13581 948 629 -523 C

ATOM 5066 C LEU D 36 -42.041 65.625 28.649 1.00113.72 C

ANISOU 5066 C LEU D 36 13564 14741 14902 1196 395 -556 C

ATOM 5067 O LEU D 36 -42.545 66.029 27.585 1.00113.32 O

ANISOU 5067 O LEU D 36 13535 14681 14841 1280 364 -619 O

ATOM ' 5068 N GLN D 37 -42.326 64.444 29.194 1.00115.12 N

ANISOU 5068 N GLN D 37 13720 14874 15147 1131 366 -524 N

ATOM 5069 CA GLN D 37 -43.348 63.552 28.658 1.00119.58 C

ANISOU 5069 CA GLN D 37 14264 15370 15800 1128 308 -595 C

ATOM 5070 CB GLN D 37 -42.972 62.089 28.963 1.00119.51 C

ANISOU 5070 CB GLN D 37 14287 15242 15881 1096 269 -539 C

ATOM 5071 CG GLN D 37 -44.098 61.036 28.991 1.00124.32 C

ANISOU 5071 CG GLN D 37 14870 15764 16603 971 258 -547 C ATOM 5072 CD GLN D 37 -43.556 59.593 28.934 1.00128.43 C

ANISOU 5072 CD GLN D 37 15447 16098 17252 978 201 -518 C

ATOM 5073 . OEl GLN D 37 -43.258 59.076 27.858 1.00126.23 O

ANISOU 5073 OEl GLN D 37 15169 15760 17031 1080 145 -637 O

ATOM 5074 NE2 GLN D 37 -43.427 58.947 30.094 1.00135.12 N

ANISOU 5074 NE2 GLN D 37 16342 16855 18144 875 212 -361 N

ATOM 5075 C GLN D 37 -44.671 63.937 29.299 1.00127.32 C

ANISOU 5075 C GLN D 37 15166 16410 16799 1029 335 -639 C

ATOM 5076 O GLN D 37 -44.734 64.117 30.518 1.00127.55 O

ANISOU 5076 O GLN D 37 15164 16493 16807 914 389 -570 O

ATOM 5077 N GLN D 38 -45.710 64.115 28.478 1.00131.13 N

ANISOU 5077 N GLN D 38 15601 16919 17305 1077 298 -768 ( N

ATOM 5078 CA GLN D 38 -47.064 64.331 28.994 1.00133.21 C

ANISOU 5078 CA GLN D 38 15758 17264 17592 988 317 -854 C

ATOM 5079 CB GLN D 38 -47.901 65.216 28.067 1.00128.54 C

ANISOU 5079 CB GLN D 38 15114 16746 16980 1118 266 -996 C

ATOM 5080 CG GLN D 38 -49.276 65.526 28.632 1.00134.52 C

ANISOU 5080 CG GLN D 38 15733 17622 17757 1045 284 -1119 C

ATOM 5081 CD GLN D 38 -49.646 66.997 28.574 1.00140.33 C

ANISOU 5081 CD GLN D 38 16441 18426 18453 1181 266 -1186 C

ATOM 5082 OEl GLN D 38 -49.944 67.607 29.604 1.00139.68 O

ANISOU 5082 OEl GLN D 38 16285 18420 18367 1117 319 -1221 O

ATOM 5083 NE2 GLN D 38 -49.637 67.574 27.373 1.00141.32 N

ANISOU 5083 NE2 GLN D 38 16627 18523 18547 1371 189 -1204 N

ATOM 5084 C GLN D 38 -47.775 63.001 29.261 1.00145.03 C

ANISOU 5084 C GLN D 38 17211 18714 19181 839 319 -877 C

ATOM 5085 O GLN D 38 -47.301 ?2.161 30.040 1.00148.60 O

ANISOU 5085 O GLN D 38 17708 19095 19660 718 353 -747 O

ATOM 5086 N GLY D 39 -48.913 62.795 28.620 1.00154.03 N

ANISOU 5086 N GLY D 39 18264 19892 20368 845 280 -1043 N

ATOM 5087 CA GLY D 39 -49.634 61.563 28.839 1.00160.05 C

ANISOU 5087 CA GLY D 39 18976 20602 21234 679 295 -1098 C

ATOM 5088 C GLY D 39 -50.988 61.606 28.191 1.00166.74 C

ANISOU 5088 C GLY D 39 19675 21578 22101 682 266 -1329 C

ATOM 5089 O GLY D 39 -51.465 62.660 27.771 1.00165.01 O

ANISOU 5089 O GLY D 39 19397 21490 21810 831 225 -1425 O

ATOM 5090 N PRO D 40 -51.619 60.446 28.083 1.00173.90 N

ANISOU 5090 N PRO D 40 20519 22443 23113 523 284 -1425 N

ATOM 5091 CA PRO D 40 -53.012 60.568 27.686 1.00177.86 C

ANISOU 5091 CA PRO D 40 20839 23117 23621 494 270 -1672 C

ATOM 5092 CB PRO D 40 -53.468 59.106 27.597 1.00185.36 C

ANISOU 5092 CB PRO D 40 21758 23952 24717 308 294 -1766 C

ATOM 5093 CG PRO D 40 -52.201 58.252 27.764 1.00175.77 C

ANISOU 5093 CG PRO D 40 20735 22468 23582 289 298 -1551 C

ATOM 5094 CD PRO D 40 -51.272 59.095 28.549 1.00169.60 C

ANISOU 5094 CD PRO D 40 20056 21697 22689 345 324 -1319 C

ATOM 5095 C PRO D 40 -53.642 61.242 28.888 1.00180.31 C

ANISOU 5095 C PRO D 40 21062 23575 23874 354 355 -1656 C

ATOM 5096 O PRO D 40 -54.158 62.362 28.853 1.00176.63 O

ANISOU 5096 O PRO D 40 20487 23288 23336 463 331 -1776 O

ATOM 5097 N ASP D 41 -53.528 60.500 29.978 1.00184.91 N

ANISOU 5097 N ASP D 41 21697 24074 24486 118 449 -1500 N

ATOM 5098 CA ASP D 41 -53.844 60.903 31.332 1.00178.20 C

ANISOU 5098 CA ASP D 41 20792 " 23363 23554 -51 546 -1427 C

ATOM 5099 CB ASP D 41 -52.859 60.200 32.255 1.00181.81 C

ANISOU 5099 CB ASP D 41 21412 23657 24010 -192 603 -1136 C

ATOM 5100 CG ASP D 41 -53.288 60.242 33.686 1.00191.37 C

ANISOU 5100 CG ASP D 41 22559 25027 25124 -434 717 -1053 C

ATOM 5101 ODl ASP D 41 -54.473 60.557 33.916 1.00197.72 O

ANISOU 5101 ODl ASP D 41 - 23175 26066 25882 -510 760 -1255 O

ATOM 5102 OD2 ASP D 41 -52.450 59.959 34.575 1.00197.18 O

ANISOU 5102 OD2 ASP D 41 23422 25680 25818 -539 758 -795 O

ATOM 5103 C ASP D 41 -53.827 62.398 31.643 1.00169.35 C

ANISOU 5103 C ASP D 41 19615 22408 22321 112 531 -1465 C

ATOM 5104 O ASP D 41 -54.726 62.909 32.281 1.00168.04 O

ANISOU 5104 O ASP D 41 19300 22448 22101 20 586 -1578 O

ATOM 5105 N GLY D 42 -52.791 63.100 31.232 1.00143.72 N

ANISOU 5105 N GLY D 42 16484 19073 19049 343 463 -1385 N

ATOM 5106 CA GLY D 42 -52.669 64.487 31.614 1.00138.47 C

ANISOU 5106 CA GLY D 42 15790 18511 18310 486 454 -1414 C

ATOM 5107 C GLY D 42 -51.409 64.735 32.421 1.00139.81 C

ANISOU 5107 C GLY D 42 16064 18643 18416 451, 511 -1211 C

ATOM 5108 O GLY D 42 -50.700 65.716 32.188 1.00139.32 O

ANISOU 5108 O GLY D .42 16055 18562 18319 605 492 -1185 O

ATOM 5109 N THR ' D 43 -51.118 63.850 33.367 1.00164.47 N

ANISOU 5109 N THR D 43 19215 21758 21517 244 583 -1065 N

ATOM 5110 CA THR D 43 -49.920 63.978 34.198 1.00164.24 C ANISOU 5110 CA THR D 43 19278 21715 21409 217 623 -865 C

ATOM 5111 CB THR D 43 -49.643 62.682 34.946 1.00173.18 C

ANISOU 5111 CB THR D 43 20475 22794 22530 7 670 -667 C

ATOM 5112 OGl THR D 43 -49.930 61.577 34.078 1.00172.63 O

ANISOU 5112 OGl THR D 43 20474 22530 22589 -12 626 -662 O

ATOM 5113 CG2 THR D 43 -50.495 62.590 36.211 1.00179.63 C

ANISOU 5113 CG2 THR D 43 21157 23829 23266 -237 769 -697 C

ATOM 5114 C THR D 43 -48.702 64.236 33.341 1.00159.64 C

ANISOU 5114 C THR D 43 18839 20975 20843 420 558 -781 C

ATOM 5115 O THR D 43 -48.684 63.851 32.182 1.00163.02 O

ANISOU 5115 O THR D 43 19317 21283 21341 537 489 -830. O

ATOM 5116 N ILE D 44 -47.673 64.868 33.895 1.00147.97 N

ANISOU 5116 N ILE D 44 17409 19524 19289 454 585 -676 N

ATOM 5117 CA ILE D 44 -46.436 65.019 33.132 1.00143.07 C

ANISOU 5117 CA ILE D 44 16909 18778 18674 616 539 -609 C

ATOM 5118 CB ILE D 44 -46.344 66.402 32.451 1.00134.34 C

ANISOU 5118 CB ILE D 44 15799 17683 17560 771 528 -721 C

ATOM 5119 CGl ILE D 44 -45.894 67.479 33.419 1.00129.71 C

ANISOU 5119 CGl ILE D 44 15161 17212 16909 741 598 -740 C

ATOM 5120 CDl ILE D 44 -46.078 68.839 32.844 1.00125.13 C

ANISOU 5120 CDl ILE D 44 14586 16598 16358 876 589 -853 C

ATOM 5121 CG2 ILE D 44 -47.686 66.806 31.876 1.00139.73 C

ANISOU 5121 CG2 ILE D 44 16404 18392 18294 827 488 -886 C

ATOM 5122 C ILE D 44 -45.162 64.658 33.921 1.00148.29 C

ANISOU 5122 C ILE D 44 17636 19443 19266 589 560 -439 C

ATOM 5123 O ILE D 44 -45.074 64.913 35.124 1.00147.55 O

ANISOU 5123 O ILE D 44 17481 19500 .19081 506 619 -410 O

ATOM 5124 N LYS D 45 -44.200 64.035 33.233 1.00156.18 N

ANISOU 5124 N LYS D 45 18738 20299 20304 670 504 -352 N

ATOM 5125 CA LYS D 45 -42.921 63.604 33.815 1.00151.71 C

ANISOU 5125 CA LYS D 45 18227 19736 19679 690 497 -209 C

ATOM 5126 CB LYS D 45 -42.611 62.173 33.404 1.00151.43 C

ANISOU 5126 CB LYS D 45 18283 19523 19731 712 426 -104 C

ATOM 5127 CG LYS D 45 -43.214 61.064 34.233 1.00165.21 C

ANISOU 5127 CG LYS D 45 20038 21183 21553 564 428 -44 C

ATOM 5128 CD LYS D 45 -43.~099 59.758 33.442 1.00176.29 C

ANISOU 5128 CD LYS D 45 21548 22349 23087 625 346 28 C

ATOM 5129 CE LYS D 45 -42.309 58.679 34.175 1.00188.67 C

ANISOU 5129 CE LYS D 45 23188 23823 24676 496 343 241 C

ATOM 5130 NZ LYS D 45 -41.801 57.657 33.207 1.00184.90 N

ANISOU 5130 NZ LYS D 45 22825 23135 24294 625 246 351 N

ATOM 5131 C LYS D 45 -41.780 64.457 33.286 1.00146.99 C

ANISOU 5131 C LYS D 45 17653 19156 19041 824 497 -258 C

ATOM 5132 O LYS D 45 -41.855 64.967 32.164 1.00141.53 O

ANISOU 5132 O LYS D 45 16987 18401 18388 918 479 -354 O

ATOM 5133 N ARG D 46 -40.712 64.594 34.071 1.00136.32 N

ANISOU 5133 N ARG D 46 16290 17908 17599 825 520 -193 N

ATOM 5134 CA ARG D 46 -39.527 65.321 33.605 1.00132.94 C

ANISOU 5134 CA ARG D 46 15873 17509 17130 921 534 -249 C

ATOM 5135 CB ARG D 46 -38.848 66.107 34.732 1.00127.68 C

ANISOU 5135 CB ARG D 46 15128 17032 16351 868 602 -262 C

ATOM 5136 CG ARG D 46 -37.871 67.203 34.277 1.00118.46 . C

ANISOU 5136 CG ARG D 46 13955 15901 15155 914 656 -366 C

ATOM 5137 CD ARG D 46 -36.383 66.885 34.538 1.00122.75 C

ANISOU 5137 CD ARG D 46 14476 16540 15624 967 638 -345 C

ATOM 5138 NE ARG D 46 -35.986 66.653 35.942 1.00125.35 N

ANISOU 5138 NE ARG D 46 14727 17050 15852 926 631 -279 N

ATOM 5139 CZ ARG D 46 -35.584 67.581 36.820 1.00121.97 C

ANISOU 5139 CZ ARG D 46 14192 16826 15326 853 705 -355 C

ATOM 5140 NHl ARG D 46 -35.547 68.868 36.512. 1.00117.49 N

ANISOU 5140 NHl ARG D 46 13589 16271 14779 799 802 -506 N

ATOM 5141 NH2 ARG D 46 -35.229 67.221 38.041 1.00122.65 N

ANISOU 5141 NH2 ARG D 46 14204 17106 15292 833 681 -282 N

ATOM 5142 C ARG D 46 -38.575 64.284 33.085 1.00134.34 C

ANISOU 5142 C ARG D 46 16108 17599 17335 1021 457 -191 C

ATOM 5143 O ARG D 46 -37.815 63.703 33.859 1.00136.31 O

ANISOU 5143 O ARG D 46 16355 17889 17546 1028 422 -86 O

ATOM 5144 N LEU D 47 -38.623 64.048 31.776 1.00128.80 N

ANISOU 5144 N LEU D 47 15452 16790 16696 1109 424 -266 N

ATOM 5145 CA LEU D 47 -37.906 62.934 31.170 1.00124.57 C

ANISOU 5145 CA LEU D 47 14956 16155 16220 1211 341 -255 C

ATOM 5146 CB LEU D 47 -38.268 62.817 29.707 1.00115.66 C

ANISOU 5146 CB LEU D 47 13856 14932 15158 1276 309 -364 C

ATOM 5147 CG LEU D 47 -38.569 61.361 29.440 1.00115.16 C

ANISOU 5147 CG LEU D 47 13824 14702 15230 1298 224 -346 C

ATOM 5148 CDl LEU D 47 -39.069 60.731 30.709 1.00116.15 C

ANISOU 5148 CDl LEU D 47 13963 14781 15389 1181 227 -206 C ATOM 5149 CD2 LEU D 47 -39.585 61.251 28.335 1.00121.04 c

ANISOU 5149 CD2 LEU D 47 14568 15383 16040 1316 201 -467 C

ATOM 5150 C LEU D 47 -36.397 63.026 31.358 1.00128.78 C

ANISOU 5150 C LEU D 47 15460 16793 16677 1287 336 -266 C

ATOM 5151 O LEU D 47 -35.788 62.117 31.928 1.00130.81 O

ANISOU 5151 O LEU D 47 15721 17028 16952 1349 265 -195 O

ATOM 5152 N ILE D 48 -35.799 64.124 30.898 1.00117.91 N

ANISOU 5152 N ILE D 48 14053 15530 15219 1281 411 -357 N

ATOM 5153 CA ILE D 48 -34.394 64.393 31.189 1.00113.05 C

ANISOU 5153 CA ILE D 48 13379 15056 14519 1323 427 -401 C

ATOM 5154 CB ILE D 48 -33.534 63.936 30.048 1.00104.88 C

ANISOU 5154 CB ILE D 48 12346 14005 13500 1429 389 -501 C

ATOM 5155 CGl ILE D 48 -33.847 64.768 28.836 1.00107.50 C

ANISOU 5155 CGl ILE D 48 12722 14303 13821 1400 446 -572 C

ATOM 5156 CDl ILE D 48 -32.729 64.760 27.873 1.00110.86 C

ANISOU 5156 CDl ILE D 48 13114 14838 14170 1433 482 -687 C

ATOM 5157 CG2 ILE D 48 -33.832 62.513 29.707 1.00107.08 C

ANISOU 5157 CG2 ILE D 48 12658 14131 13896 1532 266 -470 C

ATOM 5158 C ILE D 48 -34.121 65.883 31.477 1.00113.05 C

ANISOU 5158 C ILE D 48 13338 15184 14431 . 1227 549 -465 C

ATOM 5159 O ILE D 48 -34.934 66.753 31.150 1.00111.63 O

ANISOU 5159 O ILE D 48 13199 14944 14271 1170 607 -488 O

ATOM 5160 N TYR D 49 -32.985 66.169 32.110 1.00121.86 N

ANISOU 5160 N TYR D 49 14369 16473 15460 1215 581 -504 N

ATOM 5161 CA TYR D 49 -32.584 67.552 32.383 1.00120.89 C

ANISOU 5161 CA TYR D 49 14193 16469 15270 1109 708 -602 C

ATOM 5162 CB TYR D 49 -32.601 67.848 33.875 1.00121.43 C

ANISOU 5162 CB TYR D 49 14165 16700 15271 1040 737 -595 C

ATOM 5163 CG TYR D 49 -31.760 66.927 34.703 1.00120.83 C

ANISOU 5163 CG TYR D 49 14015 ' 16774 15122 1125 648 -548 C

ATOM 5164 CDl TYR D 49 -32.156 65.631 34.930 1.00123.24 C

ANISOU 5164 CDl TYR D 49 14380 16977 15470 1219 524 -399 C

ATOM 5165 ' CEl TYR D 49 -31.407 64.789 35.686 1.00124.74 C

ANISOU 5165 CEl TYR D 49 14524 17273 15598 1321 426 -327 C

ATOM 5166 CZ TYR D 49 -30.254 65.231 36.235 1.00120.93 C

ANISOU 5166 CZ TYR D 49 13910 17047 14991 1340 446 -425 C

ATOM 5167 OH TYR D 49 -29.522 64.371 36.992 1.00119.69 O

ANISOU 5167 OH TYR D 49 13707 17007 14762 1475 325 -343 O

ATOM 5168 CE2 TYR D 49 -29.837 66.512 36.035 1.00120.85 C

ANISOU 5168 CE2 TYR D 49 13816 17168 14935 1227 582 -606 C

ATOM 5169 CD2 TYR D 49 -30.589 67.356 35.276 1.00118.15 C

ANISOU 5169 CD2 TYR D 49 13544 16674 14672 1115 685 -655 C

ATOM 5170 C TYR D 49 -31.207 67.869 31.833 1.00123.02 C

ANISOU 5170 • C TYR D 49 14411 16855 15475 1120 756 -726 C

ATOM 5171 O TYR D 49 -30.742 67.213 30.917 1.00125.89 O

ANISOU 5171 O TYR D 49 14784 17201 15846 1217 695 -752 O

ATOM 5172 N ALA D 50 -30.549 68.870 32.404 1.00117.59 N

ANISOU 5172 N ALA D 50 13652 16301 14727 1009 872 -828 N

ATOM 5173 CA ALA D 50 -29.267 69.339 31.880 1.00121.59 C

ANISOU 5173 CA ALA D 50 14085 16953 15161 981 942 -970 C

ATOM 5174 CB ALA D 50 -28.159 69.016 32.840 1.00125.14 C

ANISOU 5174 CB ALA D 50 14377 17643 15526 1039 893 -1041 C

ATOM 5175 C ALA D 50 -28.950 68.796 30.479 1.00120.81 C

ANISOU 5175 C ALA D 50 14044 16792 15068 1056 907 -985 C

ATOM 5176 O ALA D 50 -27.970 68.079 30.269 1.00120.07 O

ANISOU 5i76 O ALA D 50 13868 16816 14938 1158 841 -1058 O

ATOM 5177 N THR D 51 -29.825 69.138 29.540 1.00129.57 N

ANISOU 5177 N THR D 51 15282 17730 16219 1020 941 -925 N

ATOM 5178 CA THR D 51 -29.674 68.863 28.107 1.00132.31 C

ANISOU 5178 CA THR D 51 15686 18043 16542 1063 930 -945 C

ATOM 5179 CB THR D 51 -28.600 69.773 27.466 1.00132.89 C

ANISOU 5179 CB THR D 51 15726 18255 16511 936 1073 -1059 C

ATOM 5180 OGl THR D 51 -27.367 69.059 27.357 1.00137.01 O

ANISOU 5180 OGl THR D 51 16101 18986 16970 999 1040 -1203 O

ATOM 5181 CG2 THR D 51 -28.410 71.073 28.291 1.00123.88 C

ANISOU 5181 CG2 THR D 51 14574 ' 17126 15368 767 1212 -1085 C

ATOM 5182 C THR D 51 -29.479 67.406 27.666 1.00128.87 C

ANISOU 5182 C THR D 51 15217 17612 16137 1231 786 -966 C

ATOM 5183 O THR D 51 -29.886 67.051 26.553 1.00125.59 O

ANISOU 5183 O THR D 51 14866 17119 15735 1281 749 -959 O

ATOM 5184 N SER D 52 -28.890 66.580 28.539 1.00131.41 N

ANISOU 5184 N SER D 52 15440 18015 16473 1326 700 -993 N

ATOM 5185 CA SER D 52 -28.474 65.207 28.199 1.00134.45 C

ANISOU 5185 CA SER D 52 15782 18394 16908 1499 562 -1042 C

ATOM 5186 CB SER D 52 -26.967 65.133 27.986 1.00145.48 C

ANISOU 5186 CB SER D 52 17034 20026 18216 1538 583 -1233 C

ATOM 5187 OG SER D 52 -26.357 64.466 29.090 1.00150.50 O ANISOU 5187 OG SER D 52 17564 20772 18846 1638 501 -1248 O

ATOM 5188 C SER D 52 -28.744 64.153 29.252 1.00131.02 C

ANISOU 5188 C SER D 52 - 15343 17881 16556 1617 427 -939 C

ATOM 5189 O SER D 52 -29.031 63.008 28.910 1.00128.48 O

ANISOU 5189 O SER D 52 15057 17419 16340 1742 308 -917 O

ATOM 5190 N SER D 53 -28.558 64.529 30.519 1.00127.16 N

ANISOU 5190 N SER D 53 14803 17499 16012 1574 448 -889 N

ATOM 5191 CA SER D 53 -28.711 63.625 31.663 1.00130.68 C

ANIΞOU 5191 CA SER D 53 15240 17923 16488 1676 326 -765 C

ATOM 5192 CB SER D 53 -27.973 64.176 '32.887 1.00131.47 C

ANISOU 5192 CB SER D 53 15222 18270 16460 1637 365 -792 C

ATOM 5193 OG SER D 53 -28.800 65.045 33.649 1.00128.61 O

ANISOU 5193 OG SER D 53 14886 17916 16065 1471 468 -727 O

ATOM 5194 C SER D 53 -30.181 63.294 32.006 1.00125.71 C

ANIΞOU 5194 C SER D 53 14735 17082 15946 1626 297 -579 C

ATOM 5195 O SER D 53 -31.103 64.061 31.748 1.00125.15 O

ANISOU 5195 O SER D 53 14723 16940 15890 1502 - 383 -561 O

ATOM 5196 N LEU D 54 -30.384 62.154 32.637 1.00117.74 N

ANISOU 5196 N LEU D 54 13765 15976 14996 1720 174 -440 N

ATOM 5197 CA LEU D 54 -31.639 61.456 32.490 1.00119.35 C

ANISOU 5197 CA LEU D 54 14087 15939 15320 1683 137 -306 C

ATOM 5198 CB LEU D 54 -31.311 60.195 31.707 1.00117.49 C

ANISOU 5198 CB LEU D 54 13894 15520 15227 1835 19 -346 C

ATOM 5199 CG LEU D 54 -32.373 59.364 31.020 1.00124.12 C

ANISOU 5199 CG LEU D 54 14841 16089 16231 1815 -28 -279 C

ATOM 5200 CDl LEU D 54 -31.846 58.852 29.688 1.00127.33 C

ANISOU 5200 CDl LEU D 54 15234 16396 16748 1943 -92 -452 C

ATOM 5201 CD2 LEU D 54 -32.744 58.225 31.948 1.00131.61 C

ANISOU 5201 CD2 LEU D 54 15864 16900 17241 1838 -119 -69 C

ATOM 5202 C LEU D 54 -32.298 61.115 33.826 1.00127.63 C

ANISOU 5202 C LEU D 54 15173 16982 16340 1624 110 -103 C

ATOM 5203 O LEU D 54 -31.792 60.275 34.566 1.00131.04 O

ANISOU 5203 O LEU D 54 15597 -17450 16743 1726 14 1 Q

ATOM 5204 N ASP D 55 -33.432 61.748 34.127 1.00145.87 N

ANISOU 5204 N ASP D 55 17515 19263 18646 1465 191 -47 N

ATOM 5205 CA ASP D 55 -34.034 61.631 35.459 1.00151.86 C

ANISOU 5205 CA ASP D 55 18281 20083 19337 1367 198 ' 122 C

ATOM 5206 CB ASP D 55 " " -35.356 62.416 35.546 1.00150.89 C

ANISOU 5206 CB AΞP D 55 18151 19969 19210 1193 307 96 C

ATOM 5207 CG ASP D 55 -35.400 63.399 36.746 1.00162.19 C

ANIΞOU 5207 CG ASP D 55 19484 21657 20484 1079 387 104 C

ATOM 5208 ODl ASP D 55 -35.950 63.060 37.830 1.00163.25 O

ANISOU 5208 ODl ASP D 55 19619 21861 20549 1003 375 255 O

ATOM 5209 OD2 ASP D 55 -34.882 64.528 36.595 1.00157.96 O

ANISOU 5209 OD2 AΞP D 55 18867 21257 19894 1053 470 -52 O

ATOM 5210 C ASP D 55 -34.224 60.166 35.877 1.00153.71 C

ANISOU 5210 C ASP D 55 18620 20123 19660 1421 82 317 C

ATOM 5211 O ASP D 55 -34.426 59.301 35.028 1.00148.77 O

ANIΞOU 5211 O ASP D 55 18069 19260 19195 1486 23 294 O

ATOM 5212 N PRO D 56 -34.154 59.889 37.197 1.00176.69 N

ANISOU 5212 N PRO D 56 21537 23136 22462 1391 51 509 N

ATOM 5213 CA PRO D 56 -34.215 58.512 37.696 1.00175.13 C

ANISOU 5213 CA PRO D 56 21463 22749 22328 1430 -57 751 C

ATOM 5214 CB PRO D 56 -34.126 58.671 39.218 1.00182.24 C

ANISOU 5214 CB PRO D 56 22329 23899 23015 1351 -44 935 C

ATOM 5215 CG PRO D 56 -33.741 60.097 39.467 1.00186.82 C

ANISOU 5215 CG PRO D 56 22739 24813 23430 1331 43 746 C

ATOM 5216 CD PRO D 56 -34.215 60.873 38.293 1.00178.30 C

ANISOU 5216 CD PRO D 56 21627 23655 22463 1294 132 504 C

ATOM 5217 C PRO D 56 -35.567 57.974 37.363 1.00168.06 C

ANISOU 5217 C PRO D 56 20669 21603 21'584 1286 -24 808 C

ATOM 5218 O PRO D 56 -36.547 58.640 37.631 1.00170.97 O

ANISOU 5218 O PRO D 56 20996 22057 21909 1108 87 763 O

ATOM 5219 N GLY D 57 -35.635 56.791- 36.789 1.00136.16 N

ANISOU 5219 N GLY D 57 16748 17258 17728 1361 -119 885 N

ATOM 5220 CA GLY D 57 -36.918 56.260 36.376 1.00133.75 C

ANISOU 5220 CA GLY D 57 16519 16718 17581 1212 -80 893 C

ATOM 5221 C GLY D 57 -36.877 55.983 34.893 1.00130.64 C

ANIΞOU 5221 C GLY D 57 16116 16154 17368 1319 -110 661 C

ATOM 5222 O GLY D 57 -36.852 54.840 34.461 1.00135.05 O

ANISOU 5222 O GLY D 57 16762 16426 18124 1363 -182 671 O

ATOM 5223 N VAL D 58 -36.855 57.046 34.111 1.00116.55 N

ANISOU 5223 N VAL D 58 14224 14549 15510 1356 -54 451 N

ATOM 5224 CA VAL D 58 -36.688 56.943 32.677 1.00113.10 C

ANISOU 5224 CA VAL D 58 13765 14016 15193 1449 -74 231 C

ATOM 5225 CB VAL D 58 -36.066 58.217 32.161 1.00111.36 C

ANISOU 5225 CB VAL D 58 13442 14031 14838 1495 -12 63 C ATOM 5226 CGl VAL D 58 -36.013 58.158 30.660 1.00115.50 C

ANISOU 5226 CGl VAL D 58 13947 14489 15450 1560 -21 -142 C

ATOM 5227 CG2 VAL D 58 -36.827 59.456 32.668 1.00109.04 C

ANISOU 5227 CG2 VAL D 58 13099 13923 14407 1339 106 79 C

ATOM 5228 C VAL D 58 -35.726 55.827 32.314 1.00116.66 C

ANISOU 5228 C VAL D 58 14259 14281 15784 1640 -205 215 C

ATOM 5229 O VAL D 58 -34.718 55.666 32.994 1.00119.25. O

ANISOU 5229 O VAL D 58 14579 14684 16046 1769 -272 291 O

ATOM 5230 N PRO D 59 -36.026 55.067 31.238 1.00122.13 N

ANISOU 5230 N PRO D 59 14985 14745 16675 1672 -249 91 N

ATOM 5231 CA PRO D 59 -35.274 53.873 30.786 1.00132.61 C

ANISOU 5231 CA PRO D 59 16345 15860 18179 1865 -381 31 C

ATOM 5232 CB PRO D 59 -36.319 53.071 29.987 1.00127.05 C

ANISOU 5232 CB PRO D 59 15685 14890 17700 1792 -388 -76 C

ATOM 5233 CG PRO D 59 -37.630 53.796 30.182 1.00122.59 C

ANISOU 5233 CG PRO D 59 15117 14399 17062 1559 -268 -29 C

ATOM 5234 CD PRO D 59 -37.290 55.208 30.508 1.00118.61 C

ANISOU 5234 CD PRO D 59 14536 14224 16308 1525 -183 -9 C

ATOM 5235 C PRO D 59 -34.059 54.161 29.889 1.00134.50 C

ANISOU 5235 C PRO D 59 16468 16271 18365 2046 -411 -204 C

ATOM 5236 O PRO D 59 -33.961 55.269 29.36Z 1.00128.68 O

ANISOU 5236 O PRO D 59 15643 15784 17464 1995 -317 -315 O

ATOM 5237 N LYS D 60 -33.160 53.191 29.711 1.00177.49 N

ANISOU 5237 N LYS D 60 21912 21576 23950 2250 -540 -283 N

ATOM 5238 CA LYS D 60 -32.011 53.404 28.830 1.00189.03 C

ANISOU 5238 CA LYS D 60 . 23238 23222 25361 2417 -567 -540 C

ATOM 5239 CB LYS D 60 -31.133 52.151 28.733 1.00207.33 C

ANISOU 5239 CB LYS D 60 25552 25367 27858 2670 -734 -616 C

ATOM 5240 CG LYS D 60 -31.632 51.097 27.729 1.00217.30 C

ANISOU 5240 CG LYS D 60 26834 26334 29395 2736 -808 -803 C

ATOM 5241 CD LYS D 60 -30.587 ' 50.745 26.642 1.00216.38 C

ANISOU 5241 CD LYS D 60 26560 26340 29316 2949 -877 -1143 C

ATOM 5242 CE LYS D 60 -30.698 51.681 25.420 1.00206.25 C

ANISOU 5242 CE LYS D 60 25139 25410 27818 2846 -743 -1354 C

ATOM 5243 NZ LYS D 60 -29.897 51.224 24.250 1.00200.42 N

ANISOU 5243 NZ LYS D 60 24239 24803 27107 2996 -785 -1711 N

ATOM 5244 C LYS D 60 -32.492 53.802 27.434 1.00188.39 C

ANISOU 5244 C LYS D 60 23085 23222 25273 2349 -490 -785 C

ATOM 5245 O LYS D 60 -31.793 54.484 26.676 1.00186.03 O

ANISOU 5245 O LYS D 60 .22676 23189 24818 2370 -432 -947 O

ATOM 5246 N ARG D 61 -33.692 53.336 27.109 1.00148.17 N

ANISOU 5246 N ARG D 61 18050 17907 20341 2261 -491 -808 N

ATOM 5247 CA ARG D 61 -34.404 53.674 25.878 1.00140.72 C

ANISOU 5247 CA ARG D 61 17049 17053 19367 2172 -419 -992 C

ATOM 5248 CB ARG D 61 -35.860 53.178 26.025 1.00136.35 C

ANISOU 5248 CB ARG D 61 16579 16311 18915 1993 -382 -879 C

ATOM 5249 CG ARG D 61 -36.858 53.667 24.989 1.00135.10 C

ANISOU 5249 CG ARG D ' 61 16365 16172 18793 1922 -349 -1081 C

ATOM 5250 CD ARG D 61 -38.267 53.680 25.557 1.00129.83 C

ANISOU 5250 CD ARG D 61 15757 15389 18182 1725 -294 -961 C

ATOM 5251 NE ARG D 61 -38.567 52.499 26.357 1.00131.73 N

ANISOU 5251 NE ARG D 61 16112 15337 18601 1669 -334 -774 N

ATOM 5252 CZ ARG D 61 -39.673 52.372 27.080 1.00138.54 C

ANISOU 5252 CZ ARG D 61 17035 16098 19505 1471 -276 -631 C

ATOM 5253 NHl ARG D 61 -40.553 53.357 27.085 1.00143.81 N

ANISOU 5253 NHl ARG D 61 • 17639 16943 20059 1340 -190 -685 N

ATOM 5254 NH2 ARG D 61 -39.907 51.279 27.798 1.00143.22 N

ANISOU 5254 NH2 ARG D 61 17750 16421 20245 1405 -306 -433 N

ATOM 5255 C ARG D 61 -34.336 55.186 25.534 1.00134.50 C

ANISOU 5255 C ARG D 61 16192 16601 18312 2113 -307 -1019 C

ATOM 5256 O ARG D 61 • -34.178 55.587 24.374 1.00126.89 O

ANISOU 5256 O ARG D 61 15138 15817 17256 2161 -284 -1217 O

ATOM 5257 N PHE D 62 -34.446 56.028 26.549 1.00139.20 N

ANISOU 5257 N PHE D 62 16831 17276 18781 2000 -235 -816 N

ATOM 5258 CA PHE D 62 -34.410 57.451 26.318 1.00131.96 C

ANISOU 5258 CA PHE D 62 15872 16615 17651 1926 -125 -824 C

ATOM 5259 CB PHE D 62 -35.245 58.147 27.351 1.00125.92 C

ANISOU 5259 CB PHE D 62 15161 15860 16822 1773 -51 -636 C

ATOM 5260 CG PHE D 62 -36.691 57.938 27.163 1.00128.22 C

ANISOU 5260 CG PHE D 62 15494 16011 17213 1671 -46 -619 C

ATOM 5261 CDl PHE D 62 ' -37.290 56.779 27.604 1.00132.25 C

ANISOU 5261 CDl PHE D 62 16062 16288 17899 1648 -109 -546 C

ATOM 5262 CEl PHE D 62 -38.634 56.580 27.429 1.00135.57 C

ANISOU 5262 1 CEl PHE D 62 16502 16594 18416 1528 -92 -558 C

ATOM 5263 CZ PHE D 62 -39.395 57.551 26.804 1.00135.96 C

ANISOU 5263 CZ PHE D 62 16502 16778 18377 1464. -30 -651 C

ATOM 5264 CE2 PHE D 62 -38.798 58.718 26.351 1.00128.63 C ANISOU 5264 CE2 PHE D 62 15535 16063 17275 1515 17 -700 C

ATOM 5265 CD2 PHE D 62 • -37.459 58.899 26.530 1.00126.04 C

ANISOU 5265 CD2 PHE D 62 15199 15832 16860 1600 19 -681 C

ATOM 5266 C PHE D 62 -33.000 57.960 26.396 1.00138.62 C

ANISOU 5266 C PHE D 62 16646 17655 18369 2008 -114 -868 C

ATOM 5267 O PHE D 62 -32.085 57.212 26.722 1.00149.41 O

ANISOU 5267 O PHE D 62 18000 18986 19784 2117 -192 -832 O

ATOM 5268 N SER D 63 -32.838 59.246 26.116 1.00138.30 N

ANISOU 5268 N SER D 63 16560 17826 18161 1951 -14 -941 N

ATOM 5269 CA SER D 63 -31.534 59.882 26.061 1.00134.38 C

ANISOU 5269 CA SER D 63 15979 17553 17527 1984 31 -1019 C

ATOM 5270 CB SER D 63 -30.608 59.099 25.158 1.00142.49 C

ANISOU 5270 .CB SER D 63 16912 18648 18578 2118 -28 -1244 C

ATOM 5271 OG SER D 63 -31.125 59.116 23.838 1.00141.46 O

ANISOU 5271 OG SER D 63 16790 18522 18436 2084 -2 -1346 O

ATOM 5272 C SER D 63 -31.798 61.180 25.379 1.00130.34 C

ANISOU 5272 C SER D 63 15483 17179 16863 1849 164 ' -1017 C

ATOM 5273 O SER D 63 -32.929 61.467 25.005 1.00131.77 O

ANISOU 5273 O SER D 63 15738 17279 17051 1756 202 -911 O

ATOM 5274 N GLY D 64 -30.754 61.958 25.177 1.00143.40 N

ANISOU 5274 N GLY D 64 17066 19034 18384 1839 233 -1141 N

ATOM 5275 CA GLY D 64 -30.910 63.185 24.437 1.00145.83 C

ANISOU 5275 CA GLY D 64 17415 19441 18553 1709 359 -1122 C

ATOM 5276 C GLY D 64 -29.613 63.920 24.526 1.00148.86 C

ANISOU 5276 C GLY D 64 17730 20026 18805 1639 463 -1175 C

ATOM 5277 O GLY D 64 -28.943 63.859 25.560 1.00146.47 O

ANISOU 5277 O GLY D 64 17375 19763 18514 1649 453 -1153 O

ATOM 5278 N SER D 65 -29.245 64.586 23.441 1.00141.89 N

ANISOU 5278 N SER D 65 16840 19288 17785 1561 562 -1251 N

ATOM 5279 CA SER D 65 -27.996 65.312 23.419 1.00144.45 C

ANISOU 5279 CA SER D 65 17088 19818 17980 1460 682 -1333 C

ATOM 5280 CB SER D 65 -26.856 64.403 23.000 1.00147.83 C

ANISOU 5280 CB SER D 65 17351 20430 18387 1567 630 -1545 C

ATOM 5281 OG SER D 65 -25.650 64.834 23.601 1.00157.73 O

ANISOU 5281 OG SER D 65 18512 21920 19499 1442 764 -1654 O

ATOM 5282 C SER D 65 -28.095 66.485 22.480 1.00145.95 C

ANISOU 5282 C SER D 65 17352 20077 18027 1313 818 -1307 C

ATOM 5283 O SER D 65 -29.017 66.558 21.678 1.00144.30 O

ANISOU 5283 O SER D 65 17234 19792 17801 1330 794 -1244 O

ATOM 5284 ARG D 66 -27.139 67.401 22.573 1.00151.07 N

ANISOU 5284 N ARG D 66 17960 20877 18564 1165 961 -1355 N

ATOM 5285 CA ARG D 66 -27.248 68.647 21.842 1.00154.51 C

ANISOU 5285 CA ARG D- 66 18503 21332 18871 992 1109 -1279 C

ATOM 5286 CB ARG D 66 -27.100 69.836 22.781 1.00157.12 C

ANISOU 5286 CB ARG D 66 18880 21601 19216 ' 827 1238 -1207 C

ATOM 5287 CG ARG D 66 -25.680 70.329 22.953 1.00162.32 C

ANISOU 5287 CG ARG D 66 19400 22488 19786 688 1368 -1374 C

ATOM 5288 CD ARG D 66 -25.618 71.812 22.611 1.00168.03 C

ANISOU 5288 CD ARG D 66 20236 23176 20433 444 1564 -1301 C

ATOM 5289 NE ARG D 66 -25.023 72.626 23.667 1.00176.67 N

ANISOU 5289 NE ARG D 66 21234 24352 21539 288 1689 -1410 N

ATOM 529θ ' CZ ARG D 66 -25.062 73.958 23.695 1.00182.08 C

ANISOU 5290 CZ ARG D 66 22021 24937 22226 67 1859 -1352 C

ATOM 5291 NHl ARG D 66 -25.663 74.631 22.718 1.00179.15 N

ANISOU 5291 NHl ARG D 66 21867 24363 21838 -2 1912 -1156 N

ATOM 5292 NH2 ARG D 66 -24.500 74.620 24.701 1.00183.28 N

ANISOU 5292 NH2 ARG D 66 22055 25185 22399 -77 1971 -1496 N

ATOM 5293 C ARG D 66 -26.234 68.769 20.734 1.00161.72 C

ANISOU 5293 C ARG D 66 19331 22505 19609 910 1201 -1427 C

ATOM 5294 O ARG D 66 -25.208 68.096 20.729 1.00163.83 O

ANISOU 5294 O ARG D 66 19421 22978 19850 940 1196 -1629 O

ATOM 5295 N SER D 67 -26.548 69.647 19.793 1.00157.08 N

ANISOU 5295 N SER D 67 18868 21926 18891 810 1282 -1326 N

ATOM 5296 CA SER D 67 -25.627 70.040 18.743 1.00162.54 C

ANISOU 5296 CA SER D 67 19505 22878 19374 659 1419 -1425 C

ATOM 5297 CB SER D 67 -26.054 69.439 17.411 1.00166.40 C

ANISOU 5297 CB SER D 67 19998 23488 19738 739 1358 -1452 C

ATOM 5298 OG SER D 67 -25.444 70.129 16.334 1.00173.86 O

ANISOU 5298 OG SER D 67 20963 24654 20441 542 1522 -1452 O

ATOM 5299 C SER D 67 -25.603 71.563 18.637 1.00161.87 C

ANISOU 5299 C SER D 67 19584 22712 19206 421 1603 -1252 C

ATOM 5300 O SER D 67 -26.130 72.129 17.684 1.00162.95 O

ANISOU 5300 O SER D 67 1986-9 22835 19211 348 1657 -1103 O

ATOM 5301 N GLY D 68 -25.007 72.218 19.631 1.00167.16 N

ANISOU 5301 N GLY D 68 20230 23324 19959 304 1693 -1273 N

ATOM 5302 CA GLY" D 68 -24.896 73.667 19.653 1.00173.87 C

ANISOU 5302 CA GLY D 68 21228 24064 20770 61 1879 -1140 C ATOM 5303 C GLY D 68 -26.120 74.398 19.131 1.00178.27 C

ANISOU 5303 C GLY D 68 2204:i 24352 21340 84 1854 -861 C

ATOM 5304 O GLY D 68 -26. 244 74.645 17.932 1.00178.71 O

ANISOU 5304 O GLY D 68 2219:i 24470 21238 83 1856 -758 O

ATOM 5305 N SER D 69 -27. 023 74.750 20.039 1.00202.13 N

ANISOU 5305 N SER D 69 25164 I 27098 24540 117 1824 -750 N

ATOM 5306 CA SER D 69 -28. 248 75.469 19.690 1.00203.03 C

ANISOU 5306 CA SER D 69 2550E I 26940 24694 171 1782 -505 C

ATOM 5307 CB SER D 69 -27. 945 76.639 18.739 1.00210.03 C

ANISOU 5307 CB SER D 69 26581 . 27797 25425 -27 1940 -340 C

ATOM 5308 OG SER D 69 -28. 692 77.798 19.076 1.00209.22 O

ANISOU 5308 OG SER D 69 2670S I 27418 25367 54 1884 -93 O

ATOM 5309 C SER D 69 -29. 320 74.531 19.108 1.00193.43 C

ANISOU 5309 C SER D 69 2429S I 25716 23478 421 1581 -457 C

ATOM 5310 O SER D 69 -30. 471 74.925 18.936 1.00189.83 O

ANISOU 5310 O SER D 69 23977 25050 23098 531 1494 -304 O

ATOM 5311 N ASP D 70 -28. 936 73.292 18.817 1.00167.61 N

ANISOU 5311 N ASP D 70 20871 22679 20136 512 1506 -613 . N

ATOM 5312 CA ASP D 70 -29. 874 72.272 18.356 1.00164.43 C

ANISOU 5312 CA ASP D 70 20440i 22267 19768 734 1321 -622 C

ATOM 5313 CB ASP D 70 -29. 408 71.672 17.027 1.00176.37 C

ANISOU 5313 CB ASP D 70 21887 24039 21086 763 1303 -709 C

ATOM 5314 CG ASP D 70 -29. 931 72.428 15.813 1.00191.60 C

ANISOU 5314 CG ASP D 70 23994 25987 22820 706 1351 -515 C

ATOM 5315 ODl ASP D 70 -30. 982 73.100 15.911 1.00189.96 O

ANISOU 5315 ODl ASP D 70 23939 25573 22664 794 1280 -331 O

ATOM 5316 0D2 ASP D 70 -29. 287 72.329 14.744 1.00199.14 O

ANISOU 5316 0D2 ASP D 70 24928 27182 23554 580 1456 -546 O

ATOM 5317 C ASP D 70 -29. 980 71.145 19.373 1.00160.19 C

ANISOU 5317 C ASP D 70 19750 21705 19410 858 1208 -763 C

ATOM 5318 O ASP D 70 -29. 278 70.140 19.268 1.00161.02 O

ANISOU 5318 O ASP D 70 19695 21985 19500 902 1176 -942 O

ATOM 5319 N TYR D 71 -30. 853 71.296 20.358 1.00143.63 N

ANISOU 5319 N TYR D 71 17700 19395 17477 918 1146 -683 N

ATOM 5320 CA TYR D 71 -31. 037 70.240 21.346 1.00136.08 C

ANISOU 5320 CA TYR D 71 16625 18411 16670 1030 1035 -773 C

ATOM 5321 CB TYR D 71 -31. 574 70.822 22.648 1.00131.53 C

ANISOU 5321 CB TYR D 71 16072 17676 16228 994 1051 -709 C

ATOM 5322 CG TYR D 71 -30. 612 71.799 23.248 1.00131.51 C

ANISOU 5322 CG TYR D 71 16055 17718 16193 821 1207 -741 C

ATOM 5323 CDl TYR D 71 -29. 855 71.470 24.350 1.00131.60 C

ANISOD 5323 CDl TYR D 71 15931 17821 16250 790 1225 -850 C

ATOM 5324 CEl TYR D 71 -28. 956 72.359 24.880 1.00131.69 C

ANISOU 5324 CEl TYR D 71 15905 17900 16231 621 1374 -918 C

ATOM 5325 CZ TYR D 71 -28. 799 73.587 24.294 1.00137.26 C

ANISOU 5325 CZ TYR D 71 16732 18544 16877 464 1516 -858 C

ATOM 5326 OH TYR D 71 -27. 905 74.496 24.798 1.00146.57 O

ANISOU 5326 OH TYR D 71 17876 19770 18043 266 1680 -941 O

ATOM 5327 CE2 TYR D 71 -29. 526 73.925 23.196 1.00140.11 C

ANISOU 5327 CE2 TYR D 71 17253 18796 17186 498 1496 -713 C

ATOM 5328 CD2 TYR D 71 -30. 418 73.033 22.675 1.00137.53 C

ANISOU 5328 CD2 TYR D 71 16940 18442 16872 684 1337 -664 C

ATOM . 5329 C TYR D 71 -31. 975 69.179 20.804 1.00134.07 C

ANISOU 5329 C TYR D 71 16366 18117 16457 1193 883 -779 C

ATOM 5330 O TYR D 71 -32. 664 69.411 19.811 1.00133.38 O

ANISOU 5330 O TYR D 71 16372 18008 16300 1227 859. -701 O

ATOM 5331 N SER D 72 -32. 013 68.014 21.446 1.00142.21 N

ANISOU 5331 N SER D 72 17289 19145 17601 1293 780 -875 N

ATOM 5332 CA SER D 72 -32. 876 66.944 20.958 1.00138.94 C

ANISOU 5332 CA SER D 72 16855 18682 17252 1426 646 -917 C

ATOM 5333 CB SER D 72 -32. 317 66.395 19.661 1.00141.58 C

ANISOU ' 5333 CB SER D 72 17135 19199 17460 1466 634 -1045 C

ATOM 5334 OG SER D 72 -30. 990 65.968 19.875 1.00152.21 O

ANISOU 5334 OG SER D 72 18358 20696 18779 1459 663 -1195 O

ATOM 5335 C SER D 72 -33. 070 65.791 21.930 1.00136.46 C

ANISOU 5335 C SER D 72 16466 18274 17110 1507 544 -965 C

ATOM 5336 O SER D 72 -32. 134 65.385 22.623 1.00136.11 O

ANISOU 5336 O SER D 72 16338 18288 17091 1521 542 -1035 O

ATOM 5337 N LEU D 73 -34. 302 65.282 21.961 1.00133.31 N

ANISOU 5337 N LEU D 73 16099 17732 16820 1560 458 -923 N

ATOM 5338 CA LEU D 73 -34. 655 64.052 22.658 1.00131.85 . C

ANISOU 5338 CA LEU D 73 15872 17422 16802 1618 362 -939 C

ATOM 5339 CB LEU D 73 -36. 104 64.117 23.139 1.00127.35 C

ANISOU 5339 CB LEU D 73 15357 16714 16318 1580 343 -831 C

ATOM 5340 CG LEU D 73 -36. 534 63.015 24.106 1.00130.99 C

ANISOU 5340 CG LEU D 73 15793 17031 16945 1608 253 -833 C

ATOM 5341 CDl LEU D 73 -36. 050 63.359 25.483 1.00129.34 C ANISOU 5341 CDl LEU D 73 15566 16795 16781 1591 253 -762 C

ATOM 5342 CD2 LEU D 73 -38.048 62.798 24.115 1.00133.77 C

ANISOϋ 5342 CD2 LEU D 73 16173 17298 17356 1562 239 -783 C

ATOM 5343 C LEU D 73 -34.494 62.925 21.645 1.00134.73 C

ANISOϋ 5343 C LEU D 73 16181 17792 17218 1718 269 -1088 C

ATOM 5344 O LEU D 73 -34.571 63.177 20.445 1.00136.82 O

ANISOU 5344 O LEU D 73 16454 18129 17402 1736 264 -1141 O

ATOM 5345 N THK D 74 -34.259 61.695 22.104 1.00130.29 N

ANISOU 5345 N THR D 74 15561 17156 16786 1793 191 -1163 N

ATOM 5346 CA THR D 74 -34.026 60.572 21.186 1.00131.67 C

ANISOU 5346 CA THR D 74 15665 17328 17035 1896 105 -1352 C

ATOM 5347 CB THR D 74 -32.545 60.409 20.838 1.00137.78 C

ANISOU 5347 CB THR D 74 16339 18274 17738 1964 111 -1511 C

ATOM 5348 OGl THR D 74 -31.865 61.672 20.903 1.00134.28 O

ANISOU 5348 OGl THR D 74 15902 18023 17095 1871 234 -1458 O

ATOM 5349 CG2 THR p 74 -32.404 59.777 19.459 1.00136.18 C

ANISOU 5349 CG2 THR D 74 16049 18162 17531 2044 58 -1742 C

ATOM- 5350 C THR D 74 -34.442 59.227 21.753 1.00130.87 C

ANISOU 5350 C THR D 74 15561 16994 17169 1957 -4 -1376 C

ATOM 5351 O THR D 74 -33.735 58.637 22.575 1.00131.87 O

ANISOU 5351 O THR D 74 15673 17034 17396 2021 -55 -1364 O

ATOM 5352 N ILE D 75 -35.571 58.721 21.291 1.00115.01 N

ANISOU 5352 N ILE D 75 13568 14882 15249 1940 -43 -1413 N

ATOM 5353 CA ILE D 75 -36.041 57.434 21.768 1.00120.07 C

ANISOU 5353 CA ILE D 75 14216 15277 16128 1965 -130 -1441 C

ATOM 5354 CB ILE D 75 -37.551 57.368 21.723 1.00113.42 C

ANISOU 5354 CB ILE D 75 13405 14329 15360 1873 ' -131 -1412 C

ATOM 5355 CGl ILE D 75 -38.114 58.526 22.521 1.00109.62 C

ANISOU 5355 CGl ILE D 75 12987 13891 14772 1765 -54 -1206 C

ATOM 5356 CDl ILE D 75 -39.566 58.654 22.396 1.00120.29 C

ANISOU 5356 CDl ILE D 75 14339 15213 16154 1685 -48 -1209 C

ATOM 5357 CG2 ILE D 75 -38.021 56.077 22.316 1.00118.25 C

ANISOU 5357 CG2 ILE D 75 14044 14662 16223 1857 -198 -1411 C

ATOM 5358 C ILE D 75 -35.454 56.317 20.925 1.00130.72 C

ANISOU 5358 C ILE D 75 15476 16609 17581 2089 -211 -1688 C

ATOM 5359 O ILE D 75 -35.699 56.243 19.721 1.00132.53 O

ANISOU 5359 O ILE D 75 15633 16959 17762 2111 -219 -1879 O

ATOM 5360 N SER D 76 -34.668 55.449 21.547 1.00156.68 N

ANISOU 5360 N SER D 76 18761 19767 .21004 2183 -277 -1694 N

ATOM 5361 CA SER D 76 -33.937 54.447 20.784 1.00159.34 C

ANISOU 5361 CA SER D 76 19002 20070 21470 2329 -365 -1953 C

ATOM 5362 CB SER D 76 -32.551 54.186 21.396 1.00171.19 C

ANISOU 5362 CB SER D 76 20468 21596 22982 2463 -413 -1955 C

ATOM 5363 OG SER D 76 -32.472 54.-577 22.763 1.00169.95 O

ANISOU 5363 OG SER D 76 20414 21315 22844 2434 -415 -1680 O

ATOM 5364 C SER D 76 -34.721 53.162 20.635 1.00153.56 C

ANISOU 5364 C SER D 76 18304 19018 21022 2332 -447 -2013 C

ATOM 5365 O SER D 76 -34.298 52.120 21.095 1.00159.70 O

ANISOU 5365 O SER D 76 19162 19523 21992 2366 -511 -1892 O

ATOM 5366 N SER D 77 -35.851 53.260 19.953 1.00135.29 N

ANISOU 5366 N SER D 77 15931 16745 18729 2288 -442 -2197 N

ATOM 5367 CA SER D 77 -36.848 52.193 19.851 1.00142.80 C

ANISOU 5367 CA SER D 77 16914 17409 19933 2224 -485 -2250 C

ATOM 5368 CB SER D 77 -36.340 50.849 20.373 1.00150.71 C

ANISOU 5368 CB SER D 77 17968 18054 21242 2317 -585 -2264 C

ATOM 5369 OG SER D 77 -37.382 50.164 21.064 1.00143.48 O

ANISOU 5369 OG SER D 77 17177 16815 20524 2181 -583 -2087 O

ATOM 5370 C SER D 77 -38.042 52.594 20.674 1.00138.28 C

ANISOU 5370 C SER D 77 16444 16756 19339 2047 -420 -2006 C

ATOM 5371 O SER D 77 -37.918 52.752 21.875 1.00136.18 O

ANISOU 5371 O SER D 77 16287 16366 19090 2000 -404 -1745 O

ATOM 5372 N LEU D 78 -39.195 52.759 20.041 1.00146.13 N

ANISOU 5372 N LEU D 78 17387 17847 20289 1955 -387 -2109 N

ATOM 5373 CA LEU D 78 -40.377 53.162 20.780 1.00144.47 C

ANISOU 5373 CA LEU D 78 17240 17580 20072 1791 -330 -1934 C

ATOM 5374 CB LEU D 78 -41.365 53.867 19.868 1.00140.04 C

ANISOU 5374 CB LEU D 78 16588 17262 19357 1751 -301 -2066 C

ATOM 5375 CG LEU D 78 -40.855 55.182 19.296 1.00142.21 C

ANISOU 5375 CG LEU D 78 16847 17854 19334 1828 -266 -2017 C

ATOM 5376 CDl LEU D 78 -41.820 55.672 18.251 1.00148.70 C

ANISOU 5376 CDl LEU D 78 17572 18919 20009 1847 -275 -2188 C

ATOM 5377 CD2 LEU D 78 -40.676 56.217 20.377 1.00134.40 C

ANISOU 5377 CD2 LEU D 78 15957 16888 18220 1764 -197 -1728 C

ATOM 5378 C LEU D 78 -41.036 51.967 21.445 1.00153.78 C

ANISOU 5378 C LEU D 78 18476 18411 21542 1687 -354 -1919 C

ATOM 5379 O LEU D 78 -40.837 50.821 21.035 1.00160.27 O

ANISOU 5379 O LEU D 78 19257 19056 22581 1727 -414 -2131 O ATOM 5380 N LYS D 79 -41.803 52.247 22.491 1.00160.00 N

ANISOU 5380 N LYS D 79 19358 19101 22333 1542 -301 -1669 N

ATOM 5381 CA LYS D 79 -42.611 51.239 23.152 1.00163.52 C

ANISOU 5381 CA LYS D 79 19866 19251 23013 1378 -290 -1618 C

ATOM 5382 CB LYS D 79 -42.097 50.992 24.571 1.00160.52 C

ANISOU 5382 CB LYS D 79 19639 18688 22664 1325 -280 -1283 C

ATOM 5383 CG LYS D 79 -40.830 50.138 24.655 1.00160.44 C

ANISOU 5383 CG LYS D 79 ' 19712 18414 22833 1475 -377 -1239 C

ATOM 5384 CD LYS D 79 -41.198 48.692 24.884 1.00174.72 C

ANISOU 5384 CD LYS D 79 21602 19822 24962 1366 -401 -1256 C

ATOM 5385 CE LYS D 79 -42.413 48.622 25.811 1.00182.84 C

ANISOU 5385 CE LYS D 79 22683 20807 25979 1085 -297 -1081 C

ATOM 5386 NZ LYS D 79 -43.092 47.290 25.868 1.00186.14 N

ANISOU 5386 NZ LYS D 79 23141 20894 26690 897 -276 -1168 N

ATOM 5387 C LYS D 79 -44.026 51.789 23.164 1.00164.78 C

ANISOU 5387 C LYS D 79 19950 19561 23096 1212 -219 -1680 C

ATOM 5388 O LYS D 79 -44.214 52.996 23.248 1.00164.05 O

ANISOU 5388 O LYS D 79 19809 19755 22769 1235 -183 -1652 O

ATOM 5389 N SER D 80 -45.018 50.916 23.048 1.00157.36 N

ANISOU 5389 N SER D 80 18995 18431 22362 1049 -200 -1783 N

ATOM 5390 CA SER D 80 -46.411 51.349 22.978 1.00157.70 C

ANISOU 5390 CA SER D 80 18931 18638 22349 894 -140 -1899 C

ATOM 5391 CB SER D 80 -47.338 50.243 23.491 1.00168.60 C

ANISOU 5391 CB SER D 80 20341 19737 23984 654 -93 -1920 C

ATOM 5392 OG SER D 80 -46.985- 49.838 24.808 1.00170.34 O

ANISOU 5392 OG SER D 80 20725 19754 24244 537 -50 -1583 O

ATOM 5393 C SER D 80 -46.675 52.632 23.760 1.00155.56 C

ANISOU 5393 C SER D 80 18670 18597 21839 848 -77 -1695 C

ATOM 5394 O SER D 80 -47.226 53.594 23.226 1.00150.13 O

ANISOU 5394 O SER D 80 17873 18183 20988 877 -67 -1809 O

ATOM 5395 N GLU D 81 -46.261 52.632 25.026 1.00158.23 N

ANISOU 5395 N GLU D 81 19137 18824 22161 791 -43 -1399 N

ATOM 5396 CA GLU D 81 -46.594 53.689 25.979 1.00153.13 C

ANISOU 5396 CA GLU D 81 18496 18351 21336 697 30 -1214 C

ATOM 5397 CB GLU D 81 -46.107 53.285 27.361 1.00148.21 C

ANISOU 5397 CB GLU D 81 18012 17548 20753 589 62 -915 C

ATOM 5398 CG GLU D 81 -45.975 51.794 27.494 1.00159.45 C

ANISOU 5398 CG GLU D 81 19541 18611 22433 555 20 -883 C

ATOM 5399 CD GLU D 81 -44.725 51.394 28.223 1.00173.90 C

ANISOU 5399 CD GLU D 81 21521 20296 24257 632 -19 -597 C

ATOM 5400 OEl GLU D 81 -44.118 50.377 27.834 1.00178.72 O

ANISOU 5400 OEl GLU D 81 22216 20632 25057 730 -99 -592 O

ATOM 5401 OE2 GLU D 81 -44.342 52.100 29.177 1.00181.05 O

ANISOU 5401 OE2 GLU D 81 22449 21373 24969 607 23 -393 O

ATOM 5402 C GLU D 81 -45.958 55.011 25.617 1.00148.24 C

ANISOU 5402 C GLU D 81 17851 17993 20481 868 19 -1185 C

ATOM 5403 O GLU D 81 -46.314 56.049 26.161 1.00145.88 O

ANISOU 5403 O GLU D 81 17527 " 17866 20034 821 72 -1098 O

ATOM 5404 N ASP D 82 -45.016 54.964 24.687 1.00146.42 N

ANISOU 5404 N ASP D 82 17620 17790 20222 1056 -44 -1271 N

ATOM 5405 CA ASP D 82 -44.157 56.103 24.411 1.00142.38 C

ANISOU 5405 CA ASP D 82 17112 17486 19500 1199 -43 -1215 C

ATOM 5406 CB ASP D 82 -42.804 55.627 23.889 1.00139.11 C

ANISOU 5406 CB ASP D 82 16732 17019 19105 1354 -99 -1238 C

ATOM 5407 CG ASP D 82 -41.937 55.052 24.983 1.00141.61 C

ANISOU 5407 CG ASP D 82 17149 17150 19507 1344 -109 -1041 C

ATOM 5408 ODl ASP D 82 -42.153 55.406 26.168 1.00141.99 O

ANISOU 5408 ODl ASP D 82 17249 17183 19518 1227 -58 -839 O

ATOM 5409 OD2 ASP D 82 -41.038 54.251 24.656 1.00138.40 O

ANISOU 5409 OD2 ASP D 82 16758 16635 19192 1467 -175 -1097 O

ATOM 5410 C ASP D 82 -44.759 57.117 23.456 1.00138.41 C

ANISOU 5410 C ASP D 82 16520 17224 18847 1269 -48 -1362 C

ATOM 5411 O ASP D 82 -44.238 58.223 23.313 1.00131.57 O

ANISOU 5411 O ASP D 82 15670 16516 17806 1366 -36 -1305 O

ATOM 5412 N PHE D 83 -45.845 56.751 22.791 1.00134.21 N

ANISOU 5412 N PHE D 83 15893 16721 18381 1221 -67 -1553 N

ATOM 5413 CA PHE D 83 -46.501 57.712 21.922 1.00135.79 C

ANISOU 5413 CA PHE D 83 16007 17165 18421 1305 -88 -1672 C

ATOM 5414 CB PHE D 83 -47.364 57.017 20.882 1.00143.66 C

ANISOU 5414 CB PHE D 83 16876 18219 19489 1310 -140 -1952 C

ATOM 5415 CG PHE D 83 -46.604 56.059 20.029 1.00141.30 C

ANISOU 5415 CG PHE D 83 16564 17858 19267 1392 -191 -2102 C

ATOM 5416 CDl PHE D 83 -46.331 54.779 20.485 1.00140.11 C

ANISOU 5416 CDl PHE D 83 16454 17430 19352 1312 -191 -2119 C

ATOM 5417 CEl PHE D 83 -45.619 53.891 19.708 1.00139.46 C

ANISOU 5417 CEl PHE D 83 16342 17284 19362 1405 -245 -2292 C

ATOM 5418 CZ PHE D 83 -45.165 54.279 18.460 1.00140.27 C ANISOU 5418 CZ PHE D 83 16364 17642 19292 1559 -289 -2450 C

ATOM 5419 CE2 PHE D 83 -45.434 55.551 17.993 1.00140.47 C

ANISOU 5419 CE2 PHE D 83 16364 17952 19058 1624 -285 -2400 C

ATOM 5420 CD2 PHE D 83 -46.148 56.436 18.779 1.00138.96 C

ANISOU 5420 CD2 PHE D 83 16213 17781 18804 1551 -242 -2225 C

ATOM 5421 C PHE D 83 -47.327 58.633 22.793 1.00134.63 C

ANISOU 5421 C PHE D 83 15849 17101 18204 1227 -37 -1569 C

ATOM 5422 O PHE D 83 -48.436 58.293 23.201 1.00132.84 O

ANISOU 5422 O PHE D 83 15554 16854 18065 1085 -11 -1632 O

ATOM 5423 N VAL D 84 -46.755 59.791 23.101 1.00140.97 N

ANISOU 5423 N VAL D 84 16712 17996 18853 1310 -17 -1424 N

ATOM 5424 CA VAL D 84 -47.402 60.779 23.950 1.00136.37 C

ANISOU 5424 CA VAL D 84 16119 17493 18204 1264 28 -1339 C

ATOM 5425 CB VAL D 84 -46.893 60.679 ,25.374 1.00128.39 C

ANISOU 5425 CB VAL D 84 15175 16378 17230 1139 101 -1148 C

ATOM 5426 CGl VAL D 84 -47.737 61.541 26.271 1.00131.16 C

ANISOU 5426 CGl VAL D 84 15481 1 " 6837 17515 1084 150 -1111 C

ATOM 5427 CG2 VAL D 84 -46.903 59.231 25.836 1.00129.13 C

ANISOU 5427 CG2 VAL D 84 15275 16302 17486 985 115 -1136 C

ATOM 5428 C VAL D 84 -47.097 62.175 23.433 1.00136.34 C

ANISOU 5428 C VAL D 84 16154 17619 18031 1422 12 -1291 C

ATOM 5429 O VAL D 84 -46.713 62.348 22.279 1.00138.71 O

ANISOU 5429 O VAL D 84 16461 17996 18246 1551 -40 -1354 O

ATOM 5430 N ASP D 85 -47.277 63.178 24.278 i:00150.50 N

ANISOU 5430 N ASP D 85 17972 19438 19775 1402 60 -1184 N

ATOM 5431 CA ASP D 85 -46.818 64.505 23.934 1.00154.93 C

ANISOU 5431 CA ASP D 85 18605 20054 20207 1523 64 -1101 C

ATOM 5432 CB ASP D 85 -47.808 65.568 24.418 1.00162.53 C

ANISOU 5432 CB ASP D 85 19524 21085 21144 1560 62 -1124 C

ATOM 5433 CG ASP D 85 -49.191 65.413 23.798 1.00169.62 C

ANISOU 5433 CG ASP D 85 20285 22083 22081 1576 -3 -1306 C

ATOM 5434 ODl ASP D 85 -49.460 64.345 23.208 -1.00177.39 O

ANISOU 5434 ODl ASP D 85 21192 23049 23159 1453 4 -1397 O

ATOM 5435 0D2 ASP D 85 -50.010 66.358 23.903 1.00165.19 O

ANISOU 5435 0D2 ASP D 85 19687 21613 21463 1709 -61 -1365 O

ATOM 5436 C ASP D 85 -45.450 64.696 24.579 1.00148.92 C

ANISOU 5436 C ASP D 85 17932 19218 19431 1470 137 -949 C

ATOM 5437 O ASP D 85 -45.202 64.204 25.680 1.00145.92 O

ANISOU 5437 O ASP D 85 17543 18780 19120 1349 182 -890 O

ATOM 5438 N TYR D 86 -44.552 65.391 23.892. 1.00129.04 N

ANISOU 5438 N TYR D 86 15496 16723 16811 1554 149 -887 N

ATOM 5439 CA TYR D 86 -43.254 65.694 24.466 1.00121.45 C

ANISOU 5439 CA TYR D 86 14596 15730 15821 1506 222 -776 C

ATOM 5440 CB TYR D 86 -42.1"7O 64.905 23.757 1.00119.33 C

ANISOU 5440 CB TYR D 86 14348 15460 15533 1535 209 -792 C

ATOM 5441 CG TYR D 86 -42.232 63.467 24.130 1.00119.53 C

ANISOU 5441 CG TYR D 86 14325 15403 15687 1494 165 -845 C

ATOM 5442 CDl TYR D 86 -42.113 62.477 23.184 1.00124.09 C

ANISOU 5442 CDl TYR D 86 14863 15977 16308 1547 97 -976 C

ATOM 5443 CEl TYR D 86 -42.190 61.159 23.540 1.00124.98 C

ANISOU 5443 CEl TYR D 86 14945 15969 16573 1500 62 -1029 C

ATOM 5444 CZ TYR D 86 -42.396 60.827 24.851 1.00121.96 C

ANISOU 5444 CZ TYR D 86 14587 15474 16278 1402 90 -912 C

ATOM 5445 OH TYR D 86 -42.483 59.519 25.222 1.00124.90 O

ANISOU 5445 OH TYR D 86 14959 15687 16812 1348 56 -930 O

ATOM 5446 CE2 TYR D 86 -42.527 61.790 25.802 1.00119.34 C

ANISOU 5446 CE2 TYR D 86 14284 15189 15871 1352 154 -776 C

ATOM 5447 CD2 TYR D 86 -42.455 63.098 25.440 1.00119.76 C

ANISOU 5447 CD2 TYR D 86 14351 15356 15796 1396 192 -762 C

ATOM 5448 C TYR D 86 -42.965 67.169 24.384 1.00120.82 C

ANISOU 5448 C TYR D 86 14584 15671 15650 1548 267 -711 C

ATOM 5449 O TYR D 86 -42.853 67.724 23.294 1.00123.23 O

ANISOU 5449 O TYR D 86 14945 16013 15863 1641 242 -705 O

ATOM 5450 N TYR D 87 -42.859 67.815 25.536 1.00124.69 N

ANISOU 5450 N TYR D 87 15073 16139 16165 1475 334 -662 N

ATOM 5451 CA TYR D 87 -42.579 69.238 25.533 1.00131.14 C

ANISOU 5451 CA TYR D 87 15963 16934 16932 1498 388 -610 C

ATOM " 5452 CB TYR D 87 -43.631 70.030 26.345 1.00139.81 C

ANISOU 5452 CB TYR D 87 17017 18010 18094 1498 393 -649 C

ATOM 5453 CG TYR D 87 -45.087 69.940 25.855 1.00141.24 C

ANISOU 5453 CG TYR D 87 17137 18220 18308 1590 298 -738 C

ATOM 5454 CDl TYR D 87 -45.514 70.604 24.706 1.00141.65 C

ANISOU 5454 CDl TYR D 87 17249 18257 18314 1743 230 -733 C

ATOM 5455 CEl TYR D 87 -46.837 70.513 24.276 1.00148.74 C

ANISOU 5455 CEl TYR D 87 18063 19218 19232 1844 132 -840 C

ATOM 5456 CZ TYR D 87 -47.746 69.765 25.010 1.00150.66 C

ANISOU 5456 CZ TYR D 87 18158 19534 19551 1757 122 -963 C ATOM 5457 OH TYR D 87 -49.064 69.651 24.623 1.00154.37 O

ANISOU 5457 OH TYR D 87 18514 20097 20042 1835 35 -1107 O

ATOM 5458 CE2 TYR D 87 -47.346 69.119 26.150 1.00140.08 C

ANISOU 5458 CE2 TYR D 87 16780 18187 18257 1584 202 -942 C

ATOM 5459 CD2 TYR D 87 -46.033 69.211 26.569 1.00135.94 C

ANISOU 5459 CD2 TYR D 87 16341 17605 17704 1518 279 -825 C

ATOM 5460 C TYR D 87 -41.158 69.483 26.042 1.00123.95 C

ANISOU 5460 C TYR D 87 15078 16029 15989 1411 481 -558 C

ATOM 5461 O TYR D 87 -40.679 68.776 26.922 1.00117.36 O

ANISOU 5461 O TYR D 87 14182 15224 15186 1333 502 -558 O

ATOM 5462 N CYS D 88 -40.488 70.475 25.458 1.00131.33 N

ANISOU 5462 N CYS D 88 16103 16945 16852 1421 535 -510 N

ATOM 5463 CA CYS D 88 -39.132 70.843 25.846 1.00132.15 C

ANISOU 5463 CA CYS D 88 16217 17075 16918 1325 638 -491 C

ATOM 5464 CB CYS D 88 -38.254 70.987 24.613 1.00137.46 C

ANISOU 5464 CB CYS D 88 16965 17785 17477 1334 670 -460 C

ATOM 5465 SG CYS D 88 -38.162 72.676 23.967 1.00157.47 S

ANISOU 5465 SG CYS D 88 19657 20219 19956 1326 741 -365 S

ATOM 5466 C CYS D 88 -39.147 72.177 26.563 1.00132.27 C

ANISOU 5466 C CYS D 88 16257 17022 16976 1266 718 -489 C

ATOM 5467 O CYS D 88 -39.810 73.111 26.111 1.00135.77 O

ANISOU 5467 O CYS D 88 16771 17368 17447 1327 702 -465 O

ATOM 5468 N LEU D 89 -38.389 72.276 .27.654 1.00114.40 N

ANISOU 5468 N LEU D 89 13931 14815 14721 1159 800 -525 N

ATOM 5469 CA LEU D 89 -38.459 73.435 28.551 1.00114.56 C

ANISOU 5469 CA LEU D 89 13933 14788 14805 1091 877 -572 C

ATOM 5470 CB LEU D 89 -39.230 73.043 29.814 1.00112.71 C

ANISOU 5470 CB LEU D 89 13572 14628 14625 1070 844 -633 C

ATOM 5471 CG LEU D 89 -39.090 73.826 31.112 1.00112.38 C

ANISOU 5471 CG LEU D 89 13433 14645 14620 971 924 -729 C

ATOM 5472 CDl LEU D 89 -39.153 75.321 30.915 1.00115.54 C

ANISOU 5472 CDl LEU D 89 13893 14899 15107 970 984 -786 C

ATOM 5473 CD2 LEU D 89 -40.188 73.376 32.022 1.00112.69 C

ANISOU 5473 CD2 LEU D 89 13356 14781 14680 964 872 -766 C

ATOM 5474 C LEU D 89 ' -37.090 74.019 28.911 1.00112.55 C

ANISOU 5474 C LEU D 89 13667 14581 14516 967 1000 -610 C

ATOM 5475 O LEU D 89 -36.327 73.419 29.653 1.00112.20 . O

ANISOU 5475 O LEU D 89 13524 14682 14426 913 1018 -650 O

ATOM 5476 N GLN D 90 -36.779 75.197 28.394 1.00115.91 N

ANISOU 5476 N GLN D 90 14193 14884 14965 921 1084 -599 N

ATOM 5477 CA GLN D 90 -35.463 75.780 28.617 1.00120.26 C

ANISOU 5477 CA GLN D 90 14728 15487 15479 778 1216 -653 C

ATOM 5478 CB GLN D 90 -35.156 76.764 27.490 1.00129.06 C

ANISOU 5478 CB GLN D 90 16013 16454 16571 736 1291 -568 C

ATOM 5479 CG GLN D 90 -34.214 77.877 27.874 1.00130.57 C

ANISOU 5479 CG GLN D 90 16213 16607 16792 553 1457 -643 C

ATOM 5480 CD GLN D 90 -34.922 78.921 28.674 1.00130.40 C

ANISOU 5480 CD GLN D 90 16229 16382 16935 538 1491 -691 C

ATOM 5481 OEl GLN D 90 -36.132 79.095 28.531 1.00131.50 O

ANISOU 5481 OEl GLN D 90 16440 16376 17149 679 1393 -629 O

ATOM 5482 NE2 GLN D 90 -34.189 79.613 29.539 1.00132.14 N

ANISOU 5482 NE2 GLN D 90 16383 16604 17221 376 1625 -832 N

ATOM 5483 C GLN D 90 -35.387 76.482 29.962 1.00119.80 C

ANISOU 5483 C GLN D 90 14565 15454 15501 675 1297 -787 C

ATOM 5484 O GLN D 90 -36.261 77.271 30.266 1.00124.03 O

ANISOU 5484 O GLN D 90 15143 15833 16150 681 1316 -818 O

ATOM 5485 N TYR D 91 -34.357 76.222 30.768 1.00125.46 N

ANISOU 5485 N TYR D 91 15136 16376 16157 594 1339 -881 N

ATOM 5486 CA TYR D 91 -34.310 76.840 32.099 1.00126.58 C

ANISOU 5486 CA TYR D .91 15151 16593 16351 493 1415 -1035 C

ATOM 5487 C TYR D 91 -33.128 77.727 32.396 1.00125.46 C

ANISOU 5487 C TYR D 91 14975 16485 16208 328 1568 -1159 C

ATOM 5488 O TYR D 91 -32.644 77.750 33.523 1.00127..08 O

ANISOU 5488 O TYR D 91 15016 16884 16386 245 1618 ' -1308 O

ATOM 5489 CB TYR D 91 -34.453 75.808 33.211 1.00127.20 C

ANISOU 5489 CB TYR D 91 15060 16910 16361 516 1348 -1073 C

ATOM 5490 CG TYR D 91 -33.350 74.795 33.313 1.00126.66 C

ANISOU 5490 CG TYR D 91 14916 17047 16162 524 1321 -105& C

ATOM 5491 CDl TYR D 91 -33.236 73.763 32.392 1.00124.29 C

ANISOU 5491 CDl TYR D 91 14684 16722 15817 631 1226 -933 C

ATOM 5492 CD2 TYR D 91 -32.450 74.837 34.359 1.00128.32 C

ANISOU 5492 CD2 .TYR D 91 14969 17488 16299 442 1379 -1183 C

ATOM 5493 CEl TYR D 91 -32.235 72.815 32.500 1.00126.53 C

ANISOU 5493 CEl TYR D 91 14894 17178 16005 669 1184 -935 C

ATOM 5494 CE2 TYR D 91 -31.442 73.888 34.471 1.00128.62 C

ANISOU 5494 CE2 TYR D 91 14928 17722 16219 486 1331 -1175 C

ATOM 5495 CZ TYR D 91 -31.337 72.879 33.539 1.00126.79 C ANISOU 5495 CZ TYR D 91 14778 17434 15964 606 1231 -1049 C

ATOM 5496 OH TYR D 91 -30.329 71.941 33.657 1.00126.98 O

ANISOU 5496 OH TYR D 91 14719 17634 15894 677 1169 -1059 O

ATOM 5497 N SER D 92 -32.693 78.471 31.388 1.00116.65 N

ANISOU 5497 N SER D 92 14010 15195 15115 267 1648 -1104 N

ATOM 5498 CA SER D 92 -31.652 79.473 31.558 1.00124.80 C

ANISOU 5498 CA SER D 92 15015 16242 16161 72 1817 -1234 C

ATOM 5499 C SER D 92 -32.214 80.821 32.009 1.00131.89 C

ANISOU 5499 C SER D 92 15942 16933 17238 -20 1911 -1344 C

ATOM 5500 O SER D 92 -32.079 81.206 33.171 1.00141.07 O

ANISOU 5500 O SER D 92 16946 18222 18434 -141 1998 -1551 O

ATOM 5501 CB SER D 92 -30.869 79.667 30.265 1.00127.48 C

ANISOU 5501 CB SER D 92 15494 16517 16426 -5 1893 -1134 C

ATOM 5502 OG SER D 92 -30.063 80.828 30.347 1.00128.04 O

ANISOU 5502 OG SER D 92 15566 16537 16545 -227 2078 -1255 O

ATOM 5503 N SER D 93 -32.857 81.529 31.087 1.00124.67 N

ANISOU 5503 N SER D 93 15220 15706 16442 50 1885 -1222 N

ATOM 5504 CA SER D 93 -33.268 82.910 31.329 1.00130.17 C

ANISOU 5504 CA SER D 93 15981 16139 17337 -40 1985 -1322 C

ATOM 5505 C SER D 93 -34.641 83.146 31.960 1.00135.00 C

ANISOU 5505 C SER D 93 16613 16573 18108 119 1882 -1343 C

ATOM 5506 O SER D 93 -35.641 82.560 31.549 1.00132 12 O

ANISOU 5506 O SER D 93 16367 16096 17738 301 1751 -1174 O

ATOM 5507 CB SER D 93 -33.200 83.708 30.028 1.00137.51 C

ANISOU 5507 CB SER D 93 17151 16797 18299 -145 2091 -1177 C

ATOM 5508 OG SER D 93 -34.199 84.722 30.005 1.00150.95 O

ANISOU 5508 OG SER D 93 19020 18122 20213 -103 2096 -1142 O

ATOM 5509 N SER D 94 -34.651 84.052 32.937 1.00146.84 N

ANISOU 5509 N SER D 94 17972 18076 19744 47 1944 -1583 N

ATOM 5510 CA SER D 94 -35.857 84.664 33.505 1.00149.61 C

ANISOU 5510 CA SER D 94 18323 18230 20291 164 1884 -1680 C

ATOM 5511 C SER D 94 -37.215 84.027 33.160 1.00147.94 C

ANISOU 5511 C SER D 94 18160 17988 20064 407 1700 -1542 C

ATOM 5512 O SER D 94 -37.786 83.363 34.014 1.00145.26 O

ANISOU 5512 O SER D 94 17637 17884 19673 469 1624 -1640 O

ATOM 5513 CB SER D 94 -35.878 86.179 33.244 1.00156.52 C

ANISOU 5513 CB SER D 94 19368 18700 21403 90 1989 -1721 C

ATOM 5514 OG SER D 94 -36.845 86.835 34.055 1.00154.96 O

ANISOU 5514 OG SER D 94 19098 18359 21420 180 1951 -1917 O

ATOM 5515 N PRO D 95 -37.757 84.239 31.938 1.00139.95 N

ANISOU 5515 N PRO D 95 17384 16703 19086 537 1631 -1323 N

ATOM 5516 CA PRO D 95 -39.083 83.640 31.706 1.00129.36 C

ANISOU 5516 CA PRO D 95 16037 15387 17727 765 1454 -1251 C

ATOM 5517 C PRO D 95 -38.937 82.238 31.148 1.00124.62 C

ANISOU 5517 C PRO D 95 15417 15029 16903 797 1383 -1095 C

ATOM 5518 O PRO D 95 -38.308 82.024 30.113 1.00124.76 O

ANISOU 5518 O PRO D 95 15590 14994 16820 783 1396 -909 O

ATOM 5519 CB PRO D 95 -39.715 84.558 30.654 1.00136.32 C

ANISOU 5519 CB PRO D 95 17177 15896 18723 909 1397 -1083 C

ATOM 5520 CG PRO D 95 -38.620 85.567 30.264 1.00142.79 C

ANISOU 5520 CG PRO D 95 18162 16475 19615 726 1560 -1033 C

ATOM 5521 CD PRO D 95 -37.318 85.026 30.776 1.00141.08 C

ANISOU 5521 CD PRO D 95 17794 16543 19267 494 1695 -1134 C

ATOM 5522 N TRP D 96 -39.495 81.272 31.851 1.00143.31 N

ANISOU 5522 N TRP D 96 17596 17661 19196 828 1316 -1176 N

ATOM 5523 CA TRP D 96 -39.305 79.892 31.460 1.00144.05 C

ANISOU 5523 CA TRP D 96 17664 17958 19109 853 1248 -1048 C

ATOM 5524 C TRP D 96 -40.180 79.687 30.241 1.00145.98 C

ANISOU 5524 C TRP D 96 18053 18068 19345 1035 1122 -890 C

ATOM 5525 O TRP D 96 -41.369 79.980 30.281 1.00151.95 O

ANISOU 5525 O TRP D 96 18799 18736 20200 1170 1036 -940 O

ATOM 5526 CB TRP D 96 -39.688 78.945 32.614 1.00139.52 C

ANISOU 5526 CB TRP D 96 16873 17667 18472 830 1209 -1153 C

ATOM 5527 CG TRP D 96 -38.978 79.250 33.928 1.00143.25 C

ANISOU 5527 CG TRP D 96 17175 18316 18939 674 1317 -1332 C

ATOM 5528 CDl TRP D 96 -39.154 80.347 34.753 1.00152.14 C

ANISOU 5528 CDl TRP D 96 18222 19388 20195 613 1394 -1533 C

ATOM 5529 CD2 TRP D 96 -37.993 78.453 34.550 1.00137.31 C

ANISOU 5529 CD2 TRP D 96 16299 17831 18040 577 1346 -1339 C

ATOM 5530 NEl TRP D 96 -38.318 80.273 35.850 1.00137.95 N

ANISOU 5530 NEl TRP D 96 16247 17843 18323 469 1478 -1676 N

ATOM 5531 CE2 TRP D 96 -37.595 79.119 35.746 1.00141.21 C

ANISOU 5531 CE2 TRP D 96 16636 18460 18558, 453 1444 -1546 C

ATOM 5532 CE3 TRP D 96 -37.392 77.244 34.214 1.00135.71 C

ANISOU 5532 CE3 TRP D 96 16101 17769 17695 594 1292 -1202 C

ATOM 5533 CZ2 TRP D 96 -36.633 78.609 36.592 1.00149.18 C

ANISOU 5533 CZ2 TRP D 96 17493 19763 19426 358 1481 -1601 C ATOM 5534 CZ3 TRP D 96 -36.432 76.736 35.057 1.00144.48 C

ANISOU 5534 CZ3 TRP D 96 17075 19134 ,18688 512 1323 -1246 C

ATOM 5535 CH2 TRP D 96 -36.056 77.416 36.232 1.00150.73 C

ANISOϋ 5535 CH2 TRP D 96 17711 20081 19478 398 1413 -1435 C

ATOM 5536 N THR D 97 -39.598 79.221 29.146 1.00138.21 N

ANISOU 5536 N THR D 97 17186 17091 18235 1047 1107 -724 N

ATOM 5537 CA THR D 97 -40.376 78.976 27.937 1.00138.86 C

ANISOU 5537 CA THR D 97 17392 17094 18276 1218 985 -583 C

ATOM 5538 C THR D 97 -40.449 77.500 27.571 1.00137.06 C

ANISOU 5538 C THR D 97 17097 17066 17913 1257 904 -537 C

ATOM 5539 O THR D 97 -39.734 76.679 28.131 1.00135.93 O

ANISOU 5539 O THR D 97 16869 17082 17697- 1151 951 -562 O

ATOM 5540 CB THR D 97 . -39.787 79.730 26.768 1.00139.25 C

ANISOU 5540 CB THR D 97 17662 16957 18288 1212 1033 -418 C

ATOM 5541 OGl THR D 97 -38.392 79.924 27.013 1.00141.84 O

ANISOU 5541 OGl THR D 97 17994 17321 18576 1006 1189 -435 O

ATOM 5542 CG2 THR D 97 -40.461 81.077 26.633 1.00142.84 C

ANISOU 5542 CG2 THR D 97 18242 17129 18902 1306 1015 -402 C

ATOM 5543 N PHE D 98 -41.312 77.164 26.619 1.00142.21 N

ANISOU 5543 N PHE D 98 17785 17709 18539 1418 776 -483 N

ATOM 5544 CA PHE D 98 -41.452 75.781 26.178 1.00140.09 C

ANISOU 5544 CA PHE D 98 17457 17603 18169 1453 699 -463 C

ATOM 5545 C PHE D 98 -41.397 75.663 24.653 1.00141.34 C

ANISOU 5545 C PHE D 98 17746 17750 18208 1549 642 -335 C

ATOM 5546 O PHE D 98 -41.167 76.645 23.951 1.00139.56 O

ANISOU 5546 O PHE D 98 17678 17401 17949 1564 678 -223 O

ATOM 5547 CB PHE D 98 ' -42.777 75.200 26.664 1.00137.96 C

ANISOU 5547 CB PHE D 98 17050 17410 17957 1530 ' 599 -566 C

ATOM 5548 CG PHE D 98 -42.893 75.063 28.163 1.00135.22 C

ANISOU 5548 CG PHE D 98 16548 17155 17676 1415 651 -685 C

ATOM 5549 CDl PHE D 98 -42.786 73.813 28.771 1.00136.26 C

ANISOU 5549 CDl PHE D 98 16570 17436 17768 1342 638 -704 C

ATOM . 5550 CD2 PHE D 98 -43.165 76.161 28.958 1.00133.33 C-

ANISOU 5550 CD2 PHE D 98 16271 16854 17534 1383 709 -778 C

ATOM 5551 CEl PHE D 98 . -42.921 73.662 30.143 1.00130.62 C

ANISOU 5551 CEl PHE D 98 15720 16832 17078 1232 683 -784 C

ATOM 5552 CE2 PHE D 98 -43.304 76.013 30.325 1.00134.06 C

ANISOU 5552 CE2 PHE D 98 16203 17082 17653 1274 756 -897 C

ATOM 5553 CZ PHE D 98 -43.181 74.756 30.917 1.00127.57 C

ANISOU 5553 CZ PHE D 98 15281 16433 16758 1196 743 -885 C

ATOM 5554 N GLY D 99 -41.617 74.451 24.153 1.00125.01 N

ANISOU 5554 N GLY D 99 15611 15815 16073 1606 556 -356 N

ATOM 5555 ' CA GLY D 99 -41.751 74.222 22.729 1.00127.45 C

ANISOU 5555 CA GLY D 99 16004 16167 16254 1708 487 -275 C

ATOM 5556 C GLY D 99 -43.181 73.887 22.338 1.00135.28 C

ANISOU 5556 C GLY D 99 16939 17205 17257 1873 342 -330 C

ATOM 5557 O GLY D 99 -43.998 73.537 23.186 1.00129.81 O

ANISOU 5557 O GLY D 99 16114 16540 16667 1877 302 -450. O

ATOM 5558 N GLY D 100 -43.482 73.981 21.045 1.00174.09 N

ANISOU 5558 N GLY D 100 21943 22157 22047 1999 266 -249 N

ATOM 5559 CA GLY D 100 -44.833 73.776 20.541 1.00176.01 C

ANISOU 5559 CA GLY D 100 22126 22479 22269 2178 117 -310 C

ATOM 5560 C GLY D 100 -45.444 72.430 20.877 1.00170.65 C

ANISOU 5560 C GLY D 100 21260 21934 21646 2148 68 -486 C

ATOM 5561 O GLY D 100 -46.662 72.286 20.968 1.00170.93 O

ANISOU 5561 O GLY D 100 21187 22020 21739 2239 -24 -603 O

ATOM 5562 N GLY D 101 -44.589 71.435 21.058 1.00148.73 N

ANISOU 5562 N GLY D 101 18443 19210 18858 2018 131 -513 N

ATOM 5563 CA GLY D 101 -45.049 70.102 21.386 1.00148.41 C

ANISOU 5563 CA GLY D 101 18254 19246 18888 1967 98 -655 " ' C

ATOM 5564 C GLY D 101 -45.025. 69.133 20.216 1.00149.56 C

ANISOU 5564 C GLY D 101 18369 19519 18937 2015 38 -715 C

ATOM 5565 O GLY D 101 -45.662 69.361 19.181 1.00150.19 O

ANISOU 5565 O GLY D 101 18504 19685 18877 2134 -21 -677 O

ATOM 5566 N THR D 102 -44.279 68.045 20.383 1.00137.32 N

ANISOU 5566 N THR D 102 16731 17983 17460 1926 50 -810 N

ATOM 5567 CA THR D 102 -44.304 66.935 19.441 1.00138.17 C

ANISOU 5567 CA THR D 102 16779 18202 17519 1966 -10 -924 C

ATOM 5568 C THR D 102 -45.328 65.912 19.928 1.00138.37 C

ANISOU 5568 C THR D 102 16670 18208 17695 1919 -55 -1079 C

ATOM 5569 O THR D 102 -45.414 65.649 21.126 1.00136.78 O

ANISOU 5569 O THR D 102 ' 16446 17900 17625 1804 -6 -1062 O

ATOM 5570 CB THR D 102 -42.932 66.252 19.351 1.00130.89 C

ANISOU 5570 CB THR D 102 15881 17283 16570 1900 51 -912 C

ATOM 5571 OGl THR D 102 -41.'957 67.171 18.843 1.00125.74 O

ANISOU 5571 OGl THR D 102 15343 16665 15767 1906 115. -779 O

ATOM 5572 CG2 THR D 102 -43.014 65.067 18.437 1.00136.72 C ANISOU 5572 CG2 THR D 102 16531 18132 17286 1944 -13 -1076 C

ATOM 5573 N LYS D 103 -46.108 65.339 19.017 1.00148.44 N

ANISOU 5573 N LYS D 103 17853 19601 18945 1994 -144 -1231 N

ATOM 5574 CA LYS D 103 -47.130 64.373 19.416 1.00151.89 C

ANISOU 5574 CA LYS D 103 18157 20018 19535 1919 -172 -1400 C

ATOM 5575 C LYS D 103 -47.072 63.084 18.600 1.00153.35 C

ANISOU 5575 C LYS D 103 18264 20251 19750 1916 -213 -1574 c

ATOM 5576 O LYS D 103 -47.583 63.000 17.488 1.00154.38 O

ANISOU 5576 O LYS D 103 18345 20555 19756 2028 -283 -1681 O

ATOM 5577 CB LYS D 103 -48.529 64.999 19.363 1.00160.47 C

ANISOU 5577 CB LYS D 103 19154 21205 20613 1987 -238 -1492 C

ATOM 5578 CG LYS D 103 -48.862 65.976 20.523 1.00167.36 C

ANISOU 5578 CG LYS D 103 20054 22007 21530 1959 -195 -1393 C

ATOM 5579 CD LYS D 103 -48.942 67.480 20.116 1.00169.11 C

ANISOU 5579 CD LYS D 103 20404 22225 21626 2099 -205 -1231 C

ATOM 5580 CE LYS D 103 ' -49.737 68.315 21.164 1.00168.84 C

ANISOU 5580 CE LYS D 103 20340 22151 21660 2113 -198 -1228 C

ATOM 5581 NZ LYS D 103 -49.814 69.795 20.913 1.00159.50 N

ANISOU 5581 NZ LYS D 103 19279 20923 20402 2265 -223 -1097 N

ATOM 5582 N LEU D 104 -46.440 62.077 19.179 1.00151.13 N

ANISOU 5582 N LEU D 104 17970 19816 19636 1793 -174 -1604 N

ATOM 5583 CA LEU D 104 -46.188 60.817 18.494 1.00156-.29 C

ANISOU 5583 CA LEU D 104 18559 20460 20364 1790 -208 -1779 C

ATOM 5584 C LEU D 104 -47.460 59.998 18.293 1.00160.42 C

ANISOU 5584 C LEU D 104 18940 21010 21004 1741 -255 -2007 C

ATOM 5585 O LEU D 104 -48.143 59.693 19.271 1.00159.66 O

ANISOU 5585 O LEU D 104 18815 20809 21040 1614 -223 -2002 O

ATOM 5586 CB LEU D 104 -45.179 59.987 19.299 1.00152.38 C

ANISOU 5586 CB LEU D 104 18125 19753 20020 1701 -159 -1705 C

ATOM 5587 CG LEU D 104 -43.679 60.217 19.072 1.00148.49 C

ANISOU 5587 CG LEU D 104 17709 19281 19428 1764 -132 -1610 C

ATOM 5588 CDl LEU D 104 -43.351 61.691 18.908 1.00143.45 C

ANISOU 5588 CDl LEU D 104 17156 18757 18590 1811 -89 -1437 C

ATOM 5589 CD2 LEU D 104 -42.857 59.594 20.190 1.00136.40 C

ANISOU 5589 CD2 LEU D 104 16228 17546 18050 1696 -101 -1526 C

ATOM 5590 N GLU D 105 -47.760 59.644 17.033 1.00155.46 N

ANISOU 5590 N GLU D 105 18209 20547 20313 1826 -324 -2222 N

ATOM 5591 CA GLU D 105 -48.853 58.713 16.675 1.00158.76 C

ANISOU 5591 CA GLU D 105 18465 21006 20851 1768 -365 -2493 C

ATOM 5592 C GLU D 105 ' -48.352 57.389 16.072 1.00158.32 C

ANISOU 5592 C GLU D 105 18338 20886 20932 1741 -385 -2719 C

ATOM 5593 O GLU D 105 -47.393 57.367 15.289 1.00153.78 O

ANISOU 5593 O GLU D 105 17764 20426 20239 1852 -414 -2767 O

ATOM 5594 CB GLU D 105 -49.867 59.361 15.715 1.00161.02 C

ANISOU 5594 CB GLU D 105 18636 21585 20960 1890 -445. -2616 C

ATOM 5595 CG GLU D 105 -49.389 59.526 14.272 1.00168.89 C

ANISOU 5595 CG GLU D 105 19610 22860 21702 2080 -522 -2669 C

ATOM 5596 CD GLU D 105 -50.408 59.019 13.244 1.00178.31 C

ANISOU 5596 CD GLU D 105 20596 24276 22877 2118 -602 -3017 C

ATOM 5597 OEl GLU D 105 -50.396 59.485 12.075 1.00177.25 O

ANISOU 5597 OEl GLU D 105 20396 24450 22500 2284 -692 -3071 O

ATOM 5598 OE2 GLU D 105 -51.219 58.142 13.613 1.00180.28 O

ANΪSOU 5598 OE2 GLU D 105 20751 24391 23355 1984 -578 -3234 O

ATOM 5599 N ILE D 106 -49.001 56.284 16.430 1.00161.87 N

ANISOU 5599 N ILE D 106 18726 21143 21635 1584 -362 -2862 N

ATOM 5600 CA ILE D 106 -48.614 54.990 15.875 1.00165.03 C

ANISOU 5600 CA ILE D 106 19051 21435 22218 1552 -384 -3113 C

ATOM 5601 C ILE D 106 -48.804 55.040 14.376 1.00171.13 C

ANISOU 5601 C ILE D 106 19662 22535 22825 1688 -463 -3395 C

ATOM 5602 O ILE D 106 -49.822 55.539 13.913 1.00182.44 O

ANISOU 5602 O ILE D 106 20958 24180 24179 1695 -500 -3553 O

ATOM 5603 CB ILE D 106 -49.474 53.838 16.429 1.00166.78 C

ANISOU 5603 CB ILE D 106 19210 21426 22732 ~ 1340 -347 -3263 C

ATOM 5604 CGl ILE D 106 -49.248 53.680 17.937 1.00167.43 C

ANISOU 5604 CGl ILE D 106 19460 21187 22970 1191 -268 -2972 C

ATOM 5605 CG2 ILE D 106 -49.170 52.547 15.674 1.00166.99 C

ANISOU 5605 CG2 ILE D 106 19144 21344 22960 1325 -379 -3572 C

ATOM 5606 CDl ILE D 106 -49.906 52.461 18.556 1.00169.81 C

ANISOU 5606 CDl ILE D 106 19765 21161 23595 974 -223 -3063 C

ATOM 5607 N LYS D 107 -47.840 54.553 13.603 1.00169.77 N

ANISOU 5607 N LYS D 107 21317 22751 20437 4152 -1271 -1879 N

ATOM 5608 CA LYS D 107 -48.073 54.508 12.167 1.00177.72 C

ANISOU 5608 CA LYS D 107 22287 23914 21325 4388 -1574 -2119 C

ATOM 5609 C LYS D 107 -48.808 53.238 11.772 1.00188.83 C

ANISOU 5609 C LYS D 107 23812 25046 22887 4302 -1464 -2614 C

ATOM 5610 O LYS D 107 -48.535 52.152 12.282 1.00183.75 O

ANISOU 5610 O LYS D 107 23408 24137 22273 4220 -1112 -2628 O ATOM 5611 CB LYS D 107 -46.802 54.684 11 343 1,.00167.11 C ANISOU 5611 CB LYS D 107 21082 22880 19532 4792 -1718 -1702 C ATOM 5612 CG LYS D 107 -47.096 54.748 9 852 1.00170.70 C ANISOU 5612 CG LYS D 107 21533 23453 19871 5030 -1997 -1980 C ATOM 5613 CD LYS D 107 -45.832 54.938 9 022 1, 00175.96 C ANISOU 5613 CD LYS D 107 22267 24457 20132 5441 -2209 -1568 C ATOM 5614 CE LYS D 107 -45.647 56.386 8 571 1.00182.86 C ANISOU 5614 CE LYS D 107 22831 25644 21002 5536 -2560 -1497 C ATOM 5615 NZ LYS D 107 -44.434 56.571 7 708 1.00181.72 N ANISOU 5615 NZ LYS D 107 22744 25832 20471 5943 -2752 -1054 N ATOM 5616 N ARG D 108 -49.767 53.409 10 874 1.00197.59 N ANISOU 5616 N ARG D 108 24741 26230 24105 4307 -1756 -3026 N ATOM 5617 CA ARG D 108 -50.615 52..335 10 402 1.00205..67 C ANISOU 5617 CA ARG D 108 25818 27020 25309 4168 -1701 -3563 C ATOM 5618 C ARG D 108 -50.408 52..268 8-, 921 1.00212..88 C ANISOU 5618 C ARG D 108 26781 28146 25957 4449 -1972 -3684 C ATOM 5619 O ARG D 108 -49.761 53..139 8, 341 1.00206..04 O ANISOU 5619 O ARG D 108 25837 27606 ' 24841 4729 -2239 -3400 O ATOM 5620 CB ARG D 108 -52.088 52..703 10.596 1.00214..72 C ANISOU 5620 CB ARG D 108 26636 28083 26866 3859 -1838 -4001 C ATOM 5621 CG ARG D 108 -52.810 52..085 11.775 1.00216..48 C ANISOU 5621 CG ARG D 108 26839 27954 27459 3503 -1530 -4132 C ATOM 5622 CD ARG D 108 -54.325 52..163 11. 565 1.00217..99 C ANISOU 5622 CD ARG D 108 26804 28001 28021 3232 -1635 -4707 C ATOM 5623 NE ARG D 108 -54.892 50..901 11. 081 1.00226..87 N ANISOU 5623 NE ARG D 108 28122 28930 29148 3189 -1514 -5105 N ATOM 5624 CZ ARG D 108 -54.997 50..553 9. 800 1.00230..99 C ANISOU 5624 CZ ARG D 108 28610 29611 29543 3292 -1766 -5404 C ATOM 5625 NHl ARG D 108 -54.570 51..367 8. 846 1.00233..19 N ANISOU 5625 NHl ARG D 108 28645 30261 29695 3465 -2162 -5350 N ATOM 5626 NH2 ARG D 108 -55.531 49..384 9.470 1.00230..25 N ANISOU 5626 NH2 ARG D 108 28729 29307 29450 ' 3217 -1606 -5765 N ATOM 5627 N ALA D 109 -50.993 51..250 8.303 1.00213..69 N ANISOU 5627 N ALA D 109 27013 28059 26119 4366 -1900 -4118 N ATOM 5628 CA ALA D 109 -51.262 51..301 6.880 1.00217..76 C ANISOU 5628 CA ALA D 109 27475 28768 26495 4522 -2217 -4403 C ATOM 5629 C ALA D 109 -52.336 52..361 6.727 1.00217..79 C ANISOU 5629 C ALA D 109 27043 28969 26740 4389 -2559 -4650 C ATOM 5630 O ALA D 109 -52.662 53..056 7.687 1.00219..48 O ANISOU 5630 O ALA D 109 27059 29083 27252 4142 -2486 -4664 O ATOM 5631 CB ALA D 109 -51.772 49..969 6.398 1.00218..72 C ANISOU 5631 CB ALA D 109 27813 28617 26675 4375 -2035 -4865 C ATOM 5632 N ASP D 110 -52.889 52..502 5.531 1.00222.50 N ANISOU 5632 N ASP D 110 27487 29850 27202 4564 -2919 -4822 N ATOM 5633 CA ASP D 110 -54.074 53..332 5.372 1.00227.75 C ANISOU 5633 CA ASP D 110 27733 30696 28106 4423 -3212 -5116 C ATOM 5634 C ASP D 110 -55.308 52..471 5.697 1.00235.45 C ANISOU 5634 C ASP D 110 28635 31392 29435 4022 -3090 -5663 C ATOM 5635 O ASP D 110 -55J.73 51.291 6.044 1.00231.48 O ANISOU 5635 O ASP D 110 28417 30560 28975 3876 -2781 -5817 O ATOM 5636 CB ASP D 110 -54.152 53.934 3.960 1.00226.96 C ANISOU 5636 CB ASP D 110 27487 30980 27766 4714 -3611 -5187 C ATOM 5637 CG ASP D 110 -53.074 54.984 3.699 1.00223.10 C ANISOU 5637 CG ASP D 110 26912 30811 27046 5060 -3790 -4688 C ATOM 5638 ODl ASP D 110 -52.197 55.194 4. 566 1.00219.40 O ANISOU 5638 ODl ASP D 110 26459 30286 26618 5036 -3627 -4309 O ATOM 5639 0D2 ASP D 110 -53.107 55.600 2. 615 1.00228.19 O ANISOU 5639 0D2 ASP D 110 27471 31767 27465 5353 -4091 -4683 O ATOM 5640 N ALA D 111 -56.496 53.071 5.607 1.00246.57 N ANISOU 5640 N ALA D 111 29658 32935 31094 3853 -3316 -5937 N ATOM 5641 CA ALA D 111 -57.770 52.375 5.822 1.00253.14 C ANISOU 5641 CA ALA D 111 30355 33554 32272 3472 -3255 -6461 C ATOM 5642 C ALA D 111 -58.920 53.380 5. 801 1.00260.73 C ANISOU 5642 C ALA D 111 30843 34750 33471 3358 -3532 -6607 C ATOM 5643 O ALA D 111 -59.095 54.148 6. 744 1.00256.02 O ANISOU 5643 O ALA D 111 30074 34163 33038 3317 -3497 -6343 O ATOM 5644 CB ALA D 111 -57.762 51.603 7.136 1.00239.23 C ANISOU 5644 CB ALA D 111 28779 31341 30777 3192 -2834 -6468 C ATOM 5645 N ALA D 112 -59.697 53.377 4.721 1.00253.86 N ANISOU 5645 N ALA D 112 29767 34082 32608 3306 -3794 -7013 N ATOM 5646 CA ALA D 112 -60.753 54.369 4.533 1.00249.45 C ANISOU 5646 CA ALA D 112 28741 33798 32241 3232 -4063 -7134 C ATOM 5647 C ALA D 112 -61.867 54.211 5.564 1.00251.21 C ANISOU 5647 C ALA D 112 28794 33735 32920 2822 -3888 -7372 C -ATOM 5648 O ALA D 112 -62.063 53.119 6.104 1.00249.09 O ANISOU 5648 O ALA D 112 28738 33091 32815 2568 -3625 -7621 O ATOM 5649 CB ALA D 112 -61.310 54.284 3.124 1.00251.79 C ANISOU 5649 CB ALA D 112 28856 34443 32370 3317 -4406 -7471 C

ATOM 5650 N PRO D 113 -62.604 55.303 5.834 1.00240.86 N

ANISOU 5650 N PRO D 113 27104 32593 31818 2769 -4016 -7285 N

ATOM 5651 CA PRO D 113 -63.662 55.312 6.853 1.00236.29 C

ANISOU 5651 CA PRO D 113 26341 31757 31682 2416 -3856 -7426 C

ATOM 5652 C PRO D 113 -64.735 54.275 6.552 1.00243.17 C

ANISOU 5652 C PRO D 113 27083 32543 32769 2104 -3902 -7988 C

ATOM 5653 O PRO D 113 -64.692 53.637 5.502 1.00249.99 O

ANISOU 5653 O PRO D 113 27902 33652 33430 2169 -4129 -8264 O

ATOM 5654 CB PRO D 113 -64.268 56.717 6.723 1.00235.27 C

ANISOU 5654 CB PRO D 113 25825 31944 31623 2523 -4043 -7178 C

ATOM 5655 CG PRO D 113 -63.240 57.525 6.027 1.00236.99 C

ANISOU 5655 CG PRO D 113 26099 32506 31440 2940 -4219 -6823 C

ATOM 5656 CD PRO D 113 -62.518 56.587 5.118 1.00239.25 C

ANISOU 5656 CD PRO D 113 26625 32850 31429 3072 -4313 -7030 C

ATOM 5657 N THR D 114 -65.677 54.098 7.471 1.00244.05 N

ANISOU 5657 N THR D 114 27142 32307 33280 1765 -3684 -8155 N

ATOM 5658 CA THR D 114 -66.900 53.357 7.173 1.00247.60 C

ANISOU 5658 CA THR D 114 27407 32683 33988 1437 -3728 -8673 C

ATOM 5659 C THR D 114 -68.098 54.270 7.480 1.00252.80 C

ANISOU 5659 C THR D 114 27615 33469 34968 1289 -3844 -8665 C

ATOM 5660 O THR D 114 -68.921 53.978 8.350 1.00251.91 O

ANISOU 5660 O THR D 114 27460 33015 35239 1013 -3628 -8735 O

ATOM 5661 CB THR D 114 -66.987 52.009 7.933 1.00231.91 C

ANISOU 5661 CB THR D 114 25727 30162 32226 1149 -3361 -8932 C

ATOM 5662 OGl THR D 114 -65.787 51.253 7.721 1.00213.71 O

ANISOU 5662 OGl THR D 114 23828 27766 29607 1288 -3246 -8963 O

ATOM 5663 CG2 THR D 114 -68.169 51.201 7.437 1.00234.31 C

ANISOU 5663 CG2 THR D 114 25821 30386 32819 792 -3401 -9459 C

ATOM 5664 N VAL D 115 -68.161 55.384 6.750 1.00251.71 N

ANISOU 5664 N VAL D 115 27148 33823 34669 1490 -4169 -8564 N

ATOM 5665 CA VAL D 115 -69.174 56.430 6.917 1.00252.80 C

ANISOU 5665 CA VAL D 115 26850 34152 35052 1425 -4276 -8467 C

ATOM 5666 C VAL D 115 -70.603 55.917 7.157 1.00260.26 C

ANISOU 5666 C VAL D 115 27564 34945 36377 1032 -4251 -8881 C

ATOM 5667 O VAL D 115 -71.060 54.973 6.510 1.00261.29 O

ANISOU 5667 O VAL D 115 27733 35058 36486 857 -4314 -9321 O

ATOM 5668 CB VAL D 115 -69.167 57.407 5.707 1.00250.32 C

ANISOU 5668 CB VAL D 115 26214 34442 34455 1738 -4633 -8326 C

ATOM 5669 CGl VAL D 115 -70.276 58.444 5.831 1.00250.05 C

ANISOU 5669 CGl VAL D 115 25744 34599 34663 1700 -4690 -8162 C

ATOM 5670 CG2 VAL D 115 -67.806 58.081 5.573 1.00245.75 C

ANISOU 5670 CG2 VAL D 115 25863 34002 33507 2133 -4656 -7918 C

ATOM 5671 N SER D 116 -71.292 56.556 8.100 1.00272.82 N

ANISOU 5671 N SER D 116 28929 36417 38314 891 -4144 -8729 N

ATOM 5672 CA SER D 116 -72.679 56.245 8.430 1.00275.21 C

ANISOU 5672 CA SER D 116 28990 36564 39014 532 -4104 -9050 C

ATOM 5673 C SER D 116 -73.437 57.538 8.755 1.00279.86 C

ANISOU 5673 C SER D 116 29200 37291 39843 530 -4126 -8772 C

ATOM 5674 O SER D 116 -73.187 58.157 9.790 1.00274.46 O

ANISOU 5674 O SER D 116 28613 36273 39397 474 -3867 -8494 O

ATOM 5675 CB SER D 116 -72.748 55.302 9.638 1.00264.13 C

ANISOU 5675 CB SER D 116 27905 34545 37908 251 -3749 -9213 C

ATOM 5676 OG SER D 116 -71.850 54.215 9.512 1.00254.98 O

ANISOU 5676 OG SER D 116 27135 33220 36525 278 -3658 -9403 O

ATOM 5677 N ILE D 117 -74.354 57.948 7.878 1.00287.88 N

ANISOU 5677 N ILE D 117 29791 38803 40789 593 -4417 -8837 N

ATOM 5678 CA ILE D 117 -75.175 59.137 8.134 1.00287.78 C

ANISOU 5678 CA ILE D 117 29395 38965 40984 612 -4428 -8563 C

ATOM 5679 C ILE D 117 -76.506 58.767 8.798 1.00292.54 C

ANISOU 5679 C ILE D 117 29791 39319 42043 233 -4323 -8801 C

ATOM 5680 O ILE D 117 -77.131 57.763 8.443 1.00287.65 O

ANISOU 5680 O ILE D 117 29109 38687 41499 -10 -4416 -9254 O

ATOM 5681 CB ILE D 117 -75.429 59.979 6.851 1.00285.73 C

ANISOU 5681 CB ILE D 117 28740 39375 40448 881 -4759 -8469 C

ATOM 5682 CGl ILE D 117 -76.091 61.320 7.201 1.00279.76 C

ANISOU 5682 CGl ILE D 117 27686 38773 39838 1001 -4688 -8041 C

ATOM 5683 CG2 ILE D 117 -76.270 59.201 5.861 1.00293.97 C

ANISOU 5683 CG2 ILE D 117 29476 40725 41495 693 -5020 -8927 C

ATOM 5684 CDl ILE D 117 -76.381 62.202 6.007 1.00280.34 C

ANISOU 5684 CDl ILE D 117 27327 39509 39680 1260 -4977 -7945 C

ATOM 5685 N PHE D 118 -76.920 59.580 9.771 1.00329.03 N

ANISOU 5685 N PHE D 118 34319 43733 46966 181 -4117 -8487 N

ATOM 5686 CA PHE D 118 -78.139 59.334 10.542 1.00330.11 C

ANISOU 5686 CA PHE D 118 34286 43570 47569 -155 -3974 -8633 C

ATOM 5687 C PHE D 118 -79.095 60.518 10.513 1.00330.57 C

ANISOU 5687 C PHE D 118 33921 43887 47794 -108 -4002 -8335 C ATOM 5688 O PHE D 118 -78.696 61.656 10.772 1 00323.04 O

ANISOU 5688 O PHE D 118 32985 42972 46782 106 -3889 -7884 O

ATOM 5689 CB PHE D 118 -77.808 58.990 11.996 1 00320.26 C

ANISOU 5689 CB PHE D 118 33425 41649 46612 -328 -3601 -8565 C

ATOM 5690 CG PHE D 118 -77.054 57.709 12.153 1 00318.91 C

ANISOU 5690 CG PHE D 118 33649 41174 46348 -420 -3515 -8883 C

ATOM 5691 CDl PHE D 118 -75.774 57.702 12.678 1 003Ϊ1.58 C

ANISOU 5691 CDl PHE D 118 33136 40027 45224 -257 -3345 -8664 C

ATOM 5692 CD2 PHE D 118 -77.620 56.510 11.762 1 00319.63 C

ANISOU 5692 CD2 PHE D 118 33697 41216 46532 -669 -3592 -9393 C

ATOM 5693 CEl PHE D 118 -75.078 56.519 12.816 1, 00308..62 C

ANISOU 5693 CEl PHE D 118 33124 39385 44754 -323 -3237 -8928 C

ATOM 5694 CE2 PHE D 118 -76.929 55.328 11.897 1, 00315..23 C

ANISOU 5694 CE2 PHE D 118 33518 40372 45882 -746 -3473 -9678 C

ATOM 5695 CZ PHE D 118 -75.656 55.332 12.423 1- 00309..07 C

ANISOU 5695 CZ PHE D 118 3314.8 39373 44910 -562 -3289 -9435 C

ATOM 5696 N PRO D 119 -80.371 60.242 10..211 1, 00320..33 N

ANISOU 5696 N PRO D 119 32244 42761 46706 -318 -4130 -8581 N

ATOM 5697 CA PRO D 119 -81.408 61.274 10..156 1. 00322..61 C

ANISOU 5697 CA PRO D 119 32086 43342 47148 -277 -4162 -8311 C

ATOM 5698 C PRO D 119 -81.756 61.730 11..564 1. 00320..88 C

ANISOU 5698 C PRO D 119 31968 42611 47339 -406 -3807 -8014 C

ATOM 5699 O PRO D 119 -81.873 60.881 12..448 1, 00317..21 O

ANISOU 5699 O PRO D 119 31796 41588 47143 -647 -3594 -8186 O

ATOM 5700 CB PRO D 119 -82.607 ' 60.532 9..544 1. 00325..96 C

ANISOU 5700 CB PRO D 119 32141 44015 47695 -532 -4382 -8732 C

ATOM 5701 CG PRO D 119 -82.072 59.205 9..057 1. 00321..36 C

ANISOU 5701 CG PRO D 119 31823 43343 46938 -663 -4500 -9225 C

ATOM 5702 CD PRO D 119 -80.918 58. 904 9..939 1. 00317..79 C

ANISOU 5702 CD PRO D 119 31906 42333 46505 -631 -4219 -9125 C

ATOM 5703 O PRO D 120 -84.575 62. 620 12..897 1. 00338..06 O

ANISOU 5703 O PRO D 120 33607 44436 50406 -893 -3562 -7972 O

ATOM 5704 CB PRO D 120 -82.849 64.924 12..816 1. 00332..19 C

ANISOU 5704 CB PRO D 120 32837 44166 49213 -201 -3391 -6891 C

ATOM 5705 CG PRO D 120 -81.989 65.387 11..684 1. 00331..14 C

ANISOU 5705 CG PRO D 120 32639 44590 48590 153 -3623 -6793 C

ATOM 5706 CD PRO D 120 -81.707 64.168 10..842 1. 00334..58 C

ANISOU 5706 CD PRO D 120 33172 45153 48802 93 -3903 -7287 C

ATOM 5707 N PRO D 120 -81.907 63.048 11..780 1. 00341..44 N

ANISOU 5707 N PRO D 120 34349 45393 49989 -241 -3721 -7566 N

ATOM 5708 CA PRO D 120 -82.370 63.499 13..095 1. 00336..37 C

ANISOU 5708 CA PRO D 120 33772 44275 49757 -390 -3383 -7292 C

ATOM 5709 C PRO D 120 -83.533 62.617 13..549 1. 00336..34 C

ANISOU 5709 C PRO D 120 33712 43909 50173 -768 -3324 -7650 C

ATOM 5710 N SER D 121 -83.347 61.862 14..631 1. 00326..58 N

ANISOU 5710 N SER D 121 32795 42027 49262 -951 -3011 -7608 N

ATOM 5711 CA SER D 121 -84.345 60.885 15..073 1. 00323..94 C

ANISOU 5711 CA SER D 121 32457 41286 49341 -1297 -2923 -7954 C

ATOM 5712 C SER D 121 -85.714 61.501 15..367 1. 00327..88 C

ANISOU 5712 C SER D 121 32538 41847 50195 -1432 -2892 -7830 C

ATOM 5713 O SER D 121 -85.967 62.661 15..043 1. 00328..69 O

ANISOU 5713 , O SER D 121 32391 42252 50243 -1251 -2882 -7426 O

ATOM 5714 ' CB SER D 121 -83.836 60.096 16..283 1. 00311..39 C

ANISOU 5714 CB SER D 121 31353 38990 47972 -1425 -2593 -7955 C

ATOM 5715 OG SER D 121 -83.037 60.912 17..117 1. 00307..88 O

ANISOU 5715 OG SER D 121 31158 38425 47397 -1225 -2399 -7502 O

ATOM 5716 N SER D 122 -86.594 60.718 15..982 1. 00260..60 N

ANISOU 5716 N SER D 122 23939 33047 42031 -1742 -2865 -8170 N

ATOM 5717 CA SER D 122 -87.985 61.132 16..183 1. 00254..08 C

ANISOU 5717 CA SER D 122 22699 32292 41547 -1892 -2858 -8091 C

ATOM ' 5718 C SER D 122 -.88.196 62.199 17..267 1. 00250..04 C

ANISOU 5718 C SER D 122 22251 31386 41365 -1871 -2515 -7602 C

ATOM 5719 O SER D 122 -88.660 63.306 16..983 1. 00246..52 O

ANISOU 5719 O SER D 122 21477 31241 40950 -1758 -2508 -7242 O

ATOM 5720 CB SER D 122 -88.859 59. 905 16.458 1. 00251.22 C

ANISOU 5720 CB SER D 122 22266 31704 41483 -2242 -2908 -8603 C

ATOM 5721 OG SER D 122 -88.111 58. 880 17.090 1. 00243.51 O

ANISOU 5721 OG SER D 122 21756 30156 40612 -2371 -2722 -8872 O

ATOM 5722 N GLU D 123 -87.855 61.858 18.506 1. 00295.97 N

ANISOU 5722 N GLU D 123 28498 36534 47424 -1978 -2214 -7586 N

ATOM 5723 CA GLU D 123 -88.062 62.752 19.641 1. 00290.54 C

ANISOU 5723 CA GLU D 123 27939 35400 47052 -1984 -1864 -7148 C

ATOM 5724 C GLU D 123 -87.171 63.984 19.590 1. 00289.09 C

ANISOU 5724 C GLU D 123 27952 35318 46570 -1707 -1741 -6682 C

ATOM 5725 O GLU D 123 -87.283 64.869 20.435 1. 00285.71 O

ANISOU 5725 O GLU D 123 27723 34499 46333 -1704 -1426 -6310 O

ATOM 5726 CB GLU D 123 -87.837 62.014 20.961 1. 00287.45 C ANISOU 5726 CB GLU D 123 27926 34253 47039 -2212 -1585 -7322 C

ATOM 5727 CG GLU D 123 -88 ' .8Ol 60.869 21.209 1 00289.16 C

ANISOU 5727 CG GLU D 123 28060 34319 47489 -2481 -1690 -7868 C

ATOM 5728 CD GLU D 123 -88.338 59.570 20.584 1 00294.08 C

ANISOU 5728 CD GLU D 123 28954 34950 47833 -2488 -1806 -8288 C

ATOM 5729 OEl GLU D 123 -87.437 59.606 19.721 1 00296.87 O

ANISOU 5729 OEl GLU D 123 29326 35748 47722 -2276 -2003 -8253 O

ATOM 5730 0E2 GLU D 123 -88.874 58.509 20..962 1, 00296..20 O

ANISOU 5730 0E2 GLU D 123 29425 34767 48349 -2698 -1682 -8645 O

ATOM 5731 N GLN D 124 -86.273 64.033 18..612 1, 00296..55 N

ANISOU 5731 N GLN D 124 28857 36777 47042 -1482 -1985 -6712 N

ATOM 5732 CA GLN D 124 -85.447 -65.217 18..405 1, 00297..60 C

ANISOU 5732 CA GLN D 124 29099 37120 46854 -1197 -1911 -6275 C

ATOM 5733 C GLN D 124 -86.233 66.212 17..560 1, 00302..31 C

ANISOU 5733 C GLN D 124 29217 38330 47316 -1009 -2056 -6025 C

ATOM 5734 O GLN D 124 -86.136 67.424 17..756 1. 00301..84 O

ANISOU 5734 O GLN D 124 29154 38420 47110 -793 -1916 -5577 O

ATOM 5735 CB GLN D 124 -84.116 64.862 17..727 1. 00297..22 C

ANISOU 5735 CB GLN D 124 29322 37240 46367 -1037 -2068 -6432 C

ATOM 5736 CG GLN D 124 -83.023 65.917 17..898 1. 00293..42 C

ANISOU 5736 CG GLN D 124 29033 36890 45562 -765 -1961 -6000 C

ATOM 5737 CD GLN D 124 -81.886 65.754 16..908 1. 00293..59 C

ANISOU 5737 CD GLN D 124 29061 37405 45083 -520 -2253 -6122 C

ATOM 5738 OEl GLN D 124 -80.741 65.528 17..293 1. 00284..45 O

ANISOU 5738 OEl GLN D 124 28269 36096 43713 -461 -2224 -6158 O

ATOM 5739 NE2 GLN D 124 -82.199 65.867 15..625 1. 00298..80 N

ANISOU 5739 NE2 GLN D 124 29311 38666 45555 -373 -2534 -6178 N-

ATOM 5740 N LEU D 125 -87.019 65.689 16..622 1. 00310..94 N

ANISOU 5740 N LEU D 125 29905 39783 48456 -1100 -2321 -6315 N

ATOM 5741 CA LEU D 125 -87.913 66.517 15..826 1. 00313..65 C

ANISOU 5741 CA LEU D 125 29735 40707 48730 -959 -2448 -6093 -C

ATOM 5742 C LEU D 125 -88.889 67.242 16..738 1. 00312..41 C

ANISOU 5742 C LEU D 125 29447 40261 48993 -1059 -2146 -5733 C

ATOM 5743 O LEU D 125 -88.984 68.472 16..720 1. 00309..84 O

ANISOU 5743 O LEU D 125 28901 40212 48611 -862 -2032 -5286 O

ATOM 5744 CB LEU D 125 -88..698 65.661 14..833 1. 00312..40 C

ANISOU 5744 CB LEU D 125 29188 40999 48509 -1075 -2820 -6537 C

ATOM 5745 CG LEU D 125 -87.959 65.149 13..600 1. 00311..83 C

ANISOU 5745 CG LEU D 125 29154 41341 47985 -953 -3155 -6877 C

ATOM 5746 CDl LEU D 125 -88.841 64.179 12..843 1. 00311..28 C

ANISOU 5746 CDl LEU D 125 28873 41420 47981 -1215 -3427 -7422 C

ATOM 5747 CD2 LEU D 125 -87.540 66.303 12..709 1. 00314..89 C

ANISOU 5747 CD2 LEU D 125 29266 42412 47964 -591 -3317 -6588 C

ATOM 5748 N THR D 126 -89.603 66.464 17..546 1. 00263..22 N

ANISOU 5748 N THR D 126 23365 33461 43187 -1356 -2000 -5926 N

ATOM 5749 CA THR D 126 -90.670 66.987 18..390 1. 00256..01 C

ANISOU 5749 CA THR D 126 22360 32194 42719 -1483 -1712 -5628 C

ATOM 5750 C THR D 126 -90.180 67.838 19. 573 1. 00253.07 C

ANISOU 5750 C THR D 126 22360 31372 42423 -1390 -1307 -5146 C

ATOM 5751 O THR D 126 -90.826 67.880 20. 617 1. 00252.32 O

ANISOU 5751 O THR D 126 22250 30941 42681 -1470 -1018 -4834 O

ATOM 5752 CB THR D 126 -91.572 65.844 18. 885 1. 00248.29 C

ANISOU 5752 CB THR D 126 21429 30738 42171 -1826 -1692 -6018 C

ATOM 5753 OGl THR D 126 -90.765 64.693 19. 159 1. 00248.13 O

ANISOU 5753 OGl THR D 126 21885 30261 42132 -1921 -1636 -6317 O

ATOM 5754 CG2 THR D 126 -92.576 65.478 17. 816 1. 00243.59 C

ANISOU 5754 CG2 THR D 126 20394 30622 41536 -1948 -2057 -6429 C

ATOM 5755 N SER D 127. -89.049 68.521 19. 399 1. 00272.72 N

ANISOU 5755 N SER D 127 25187 33862 44574 -1228 -1285 -5082 N

ATOM 5756 CA SER D 127 -88.545 69.452 20. 406 1. 00269.67 C

ANISOU 5756 CA SER D 127 25138 33156 44168 -1127 -927 -4619 C

ATOM 5757 C SER D 127 -88.324 70.828 19. 790 1.00268.82 C

ANISOU 5757 C SER D 127 24808 33601 43732 -815 -922 -4206 C

ATOM 5758 O SER D 127 -88.244 71.836 20. 493 1.00262.29 O

ANISOU 5758 O SER D 127 24187 32603 42869 -714 -610 -3770 O

ATOM 5759 CB SER D 127 -87.237 68.940 21. 013 1.00265.20 C

ANISOU 5759 CB SER D 127 25077 32266 43420 -1142 -880 -4759 C

ATOM 5760 OG SER D 127 -87.433 67.729 21. 721 1.00262.25 O

ANISOU 5760 OG SER D 127 24973 31281 43390 -1413 -762 -5030 O

ATOM 5761 N GLY D 128 -88.235 70.860 18. 467 1.00272.25 N

ANISOU 5761 N GLY D 128 24821 34700 43920 -667 -1257 -4353 N

ATOM 5762 CA GLY D 128 -87.925 72.081 17. 756 1.00274.61 C

ANISOU 5762 CA GLY D 128 24887 35588 43866 -337 -1292 -4019 C

ATOM 5763 C GLY D 128 -86.469 72.090 17. 331 1.00284.64 C

ANISOU 5763 C GLY D 128 26408 37061 44683 -132 -1434 -4094 C

ATOM 5764 O GLY D 128 -85.924 73.142 16. 995 1.00288.37 O

ANISOU 5764 O GLY D 128 26841 37861 44867 149 -1361 -3757 O ATOM 5765 N GLY D 129 -85.842 70.913 17.354 1.00312.32 N

ANISOU 5765 N GLY D 129 30173 40367 48129 -265 -1617 -4524 N

ATOM 5766 CA GLY D 129 -84.456 70.741 16.932 1.00309.52 C

ANISOU 5766 CA GLY D 129 30085 40158 47359 -90 -1758 -4619 C

ATOM 5767 C GLY D 129 -84.306 69.594 15.941 1.00312.61 C

ANISOU 5767 C GLY D 129 30329 40933 47515 -69 -2181 -5103 C

ATOM 5768 O GLY D 129 -85.180 68.733 15.849 1.00311.49 O

ANISOU 5768 O GLY D 129 30000 40775 47577 -281 -2342 -5462 O

ATOM 5769 N ALA D 130 -83.206 69.569 15.194 1.00300.73 N

ANISOU 5769 N ALA D 130 28918 39768 45576 182 -2356 -5113 N

ATOM 5770 CA ALA D 130 -83.053 68.565 14.143 1.00304.50

ANISOU 5770 CA ALA D 130 29248 40664 45785 241 -2756 -5533 C

ATOM 5771 C ALA D 130 -81.622 68^389 13.652 1.00301.09 C

ANISOU 5771 C ALA D 130 29144 40307 44948 443 -2857 -5568 C

ATOM 5772 O ALA D 130 -81.365 68.403 12.445 1.00301.54 O

ANISOU 5772 O ALA D 130 29035 40900 44636 717 -3099 -5567 O

ATOM 5773 CB ALA D 130 -83.970 68.882 12.977 1.00309.88 C

ANISOU 5773 CB ALA D 130 29386 42030 46326 418 -2989 -5490 C

ATOM 5774 N SER D 131 -80.696 68.221 14.587 1.00286.30 N

ANISOU 5774 N SER D 131 27734 37895 43152 308 -2665 -5592 N

ATOM 5775 CA SER D 131 -79.319 67.909 14.236 1.00281.61 C

ANISOU 5775 CA SER D 131 27493 37299 42206 471 -2712 -5586 C

ATOM 5776 C SER D 131 -79.284 66.582 13.481 1.00285.70 C

ANISOU 5776 C SER D 131 28074 37898- 42581 407 -2995 -6081 C

ATOM 5777 O SER D 131 -79.899 65.603 13.908 1.00285.33 O

ANISOU 5777 O SER D 131 28164 37458 42791 126 -2942 -6394 O

ATOM 5778 CB SER D 131 -78.442 67.825 15.494 1.00273.95 C

ANISOU 5778 CB SER D 131 26976 35729 41385 334 -2366 -5384 C

ATOM 5779 OG SER D 131 -78.029 69.106 15.947 1.00264.34 O

ANISOU 5779 OG SER D 131 25991 34612 39835 568 -2296 -5072 O

ATOM 5780 N VAL D 132 -78.587 66.561 12.347 1.00286.13 N

ANISOU 5780 N VAL D 132 28035 38451 42230 673 -3276 -6148 N

ATOM 5781 CA VAL D 132 -78.299 65.317 11.641 1.00285.67 C

ANISOU 5781 CA VAL D 132 28068 38498 41977 645 -3536 -6588 C

ATOM 5782 C VAL D 132 -77.022 64.725 12.237 1.00280.32 C

ANISOU 5782 C VAL D 132 27905 37426 41178 638 -3398 -6593 C

ATOM 5783 O VAL D 132 -76.150 65.467 12.690 1.00277.25 O

ANISOU 5783 O VAL D 132 27741 36902 40698 766 -3206 -6223 O

ATOM 5784 CB VAL D 132 -78.100 65.562 10.138 1.00286.61 C

ANISOU 5784 .CB VAL D 132 27923 39286 41690 953 -3876 -6627 C

ATOM 5785 CGl VAL D 132 -78.149 64.248 9.378 ' 1.00289.44 C

ANISOU 5785 CGl VAL D 132 28306 39764 41903 861 -4149 -7131 C

ATOM 5786 CG2 VAL D 132 -79.159 66.522 9.622 1.00290.17 C

ANISOU 5786 CG2 VAL D 132 27862 40175 42214 1040 -3952 -6463 C

ATOM 5787 N VAL D 133 -76.905 63.400 12.255 1.00278.59 N

ANISOU 5787 N VAL D 133 27874 37025 40951 484 -3475 -7000 N

ATOM 5788 CA VAL D 133 -75.761 62.770 12.923 1.00276.74 C

ANISOU 5788 CA VAL D 133 28123 36397 40629 464 -3305 -6995 C

ATOM 5789 C VAL D 133 -74.959 61.803 12.046 1.00281.21 C

ANISOU 5789 C VAL D 133 28865 37107 40875 550 -3506 -7309 C

ATOM 5790 O VAL D 133 -75.456 60.752 11.649 1.00282.71 O

ANISOU 5790 O VAL D 133 29023 37233 41161 355 -3595 -7741 O

ATOM 5791 CB VAL D 133 -76.177 62.114 14.260 ' 1.00271.67 C

ANISOU 5791 CB VAL D 133 27691 35122 40408 135 -2997 -7084 C

ATOM 5792 CGl VAL D 133 -75.453 60.797 14.476 1.00266.40 C

ANISOU 5792 CGl VAL D 133 27425 34128 39665 53 -2910 -7328 C

ATOM 5793 CG2 VAL D 133 -75.916 63.080 15.406 1.00262.41 C

ANISOU 5793 CG2 VAL D 133 26629 33683 39391 136 -2703 -6627 C

ATOM 5794 N CYS D 134 i -73.708 62.177 11.768 1.00298.75 N

ANISOU 5794 N CYS D 134 31288 39507 42717 840 -3557 -7078 N

ATOM 5795 CA CYS D 134 -72.852 61.468 10.811 1.00293.76 C

ANISOU 5795 CA CYS D 134 30832 39058 41726 991 -3749 -7291 C

ATOM 5796 C CYS D 134 -71.692 60.741 11.479 1.00280.45 C

ANISOU 5796 C CYS D 134 29635 36978 39946 983 -3530 -7223 C

ATOM 5797 O CYS D 134 -71.050 61.269 12.388 1.00273.85 O

ANISOU 5797 O CYS D 134 28988 36018 39045 1090 -3355 -6834 O

ATOM 5798 CB CYS D 134 -72.301 62.446 9.764 1.00292.36 C

ANISOU 5798 CB CYS D 134 30486 39444 41154 1372 -4004 -7075 C

ATOM 5799 SG CYS D 134 -71.387 61.692 8.383 1.00298.44 S

ANISOU 5799 SG CYS D 134 31340 40564 41490 1573 -4325 -7383 S

ATOM 5800 N PHE D 135 -71.423 59.529 11.004 1.00240.61 N

ANISOU 5800 N PHE D 135 24789 31745 34885 850 -3525 -7595 N

ATOM 5801 CA PHE D 135 -70.314 58.726 11.506 1.00237.92 C

ANISOU 5801 CA PHE D 135 24903 31096 34398 885 -3329 -7538 C

ATOM 5802 C PHE D 135 -69.237 58.438 10.454 1.00244.67 C

ANISOU 5802 C PHE D 135 25907 32286 34772 1201 -3530 -7494 C

ATOM 5803 O PHE D 135 -69.527 58.317 9.265 1.00254.84 O ANISOU 5803 O PHE D 135 26981 33969 35877 1314 -3824 -7687 " O

ATOM 5804 CB PHE D 135 -70.825 57.410 12.097 1.00231.24 C

ANISOU 5804 CB PHE D 135 24241 29806 33812 577 -3137 -7934 C

ATOM 5805 CG PHE D 135 -71.270 57.529 13.511 1.00227.32 C

ANISOU 5805 CG PHE D 135 23747 28859 33764 306 -2851 -7890 C

ATOM 5806 CDl PHE D 135 -70.795 58.557 14.306 1.00222.99 C

ANISOU 5806 CDl PHE D 135 23260 28179 33288 355 -2673 -7453 C

ATOM 5807 CD2 PHE D 135 -72.138 56.612 14.057 1.00233.57 C

ANISOU 5807 CD2 PHE D 135 24497 29347 34903 -3 -2749 -8287 C

ATOM 5808 CEl PHE D 135 -71.190 58.678 15.612 1.00216.70 C

ANISOU 5808 CEl PHE D 135 22484 26955 32899 111 -2405 -7407 C

ATOM 5809 CE2 PHE D 135 -72.541 56.732 15.360 1.00231.01 C

ANISOU 5809 CE2 PHE D 135 24181 28591 35000 -234 -2484 -8238 C

ATOM 5810 CZ PHE D 135 -72.060 57.762 16.141 1.00221.00 C

ANISOU 5810 CZ PHE D 135 22981 27193 33797 -172 -2313 -7794 C

ATOM 5811 N LEU D 136 -67.989 58.344 10.907 1.00232.52 N

ANISOU 5811 N LEU D 136 24726 30598 33022 1347 -3372 -7223 N

ATOM 5812 CA LEU D 136 -66.877 57.906 10.074 1.00225.03 C

ANISOU 5812 CA LEU D 136 23982 29884 31637 1634 -3513 -7176 C

ATOM 5813 C LEU D 136 -65.927 57.140 10.992 1.00225.09 C

ANISOU 5813 C LEU D 136 24438 29521 31565 1618 -3225 -7062 C

ATOM 5814 O LEU D 136 -65.116 57.738 11.703 1.00223.20 O

ANISOU 5814 O LEU D 136 24376 29289 31142 1794 -3129 -6651 O

ATOM 5815 CB LEU D 136 -66.163 59.098 9.427 1.00216.20 C

ANISOU 5815 CB LEU D 136 22736 29191 30219 1984 -3703 -6785 C

ATOM 5816 CG LEU D 136 -66.979 60.193 8.731 1.00214.92 C

ANISOU 5816 CG LEU D 136 22124 29446 30088 2075 -3955 -6780 C

ATOM 5817 CDl LEU D 136 -67.494 61.220 9.720 .1.00218.07 C

ANISOU 5817 CDl LEU D 136 22345 29711 30801 1933 -3784 -6545 C

ATOM 5818 CD2 LEU D 136 -66.134 60.880 7.693 1.00221.13 C

ANISOU 5818 CD2 LEU D 136 22867 30677 30474 2479 -4178 -6524 C

ATOM 5819 N ASN D 137 -66.046 55.816 10.997 1.00256.05 N

ANISOU 5819 N ASN D 137 28539 33131 35619 1407 -3075 -7422 N

ATOM 5820 CA ASN D 137 -65.314 54.994 11.959 1.00252.65 C

ANISOU 5820 CA ASN D 137 28514 32307 35176 1358 -2741 -7329 C

ATOM 5821 C ASN D 137 -64.153 54.192 11.369 1.00251.52 C

ANISOU 5821 C ASN D 137 28697 32245 34624 1596 -2742 -7281 C

ATOM 5822 O ASN D 137 -64.263 53.619 10.284 1.00254.67 O

ANISOU 5822 O ASN D 137 29057 32904 34802 1714 -2975 -7503 O

ATOM 5823 CB ASN D 137 -66.275 54.056 12.700 1.00252.67 C

ANISOU 5823 CB ASN D 137 28567 31869 35566 1007 -2500 • -7711 C

ATOM 5824 CG ASN D 137 -67.122 54.780 13.732 1.00253.02 C

ANISOU 5824 CG ASN D 137 28329 31772 36036 770 -2455 -7725 C

ATOM 5825 ODl ASN D 137 -66.605 55.338 14.702 1.00247.51 O

ANISOU 5825 ODl ASN D 137 27722 30797 35522 689 -2212 -7466 O

ATOM 5826 ND2 ASN D 137 -68.435 54.763 13.532 1.00258.37 N

ANISOU 5826 ND2 ASN D 137 28662 32641 36865 655 -2685 -8021 N

ATOM 5827 N ASN D 138 -63.037 54.174 12.097 1.00242.53 N

ANISOU 5827 N ASN D 138 27879 30889 33381 1667 -2470 -6970 N

ATOM 5828 CA ASN D 138 -61.914 53.286 11.803 1.00239.24 C

ANISOU 5828 CA ASN D 138 27833 30419 32649 1835 -2347 -6924 C

ATOM 5829 C ASN D 138 -61.123 53.635 10.540 1.00237.75 C

ANISOU 5829 C ASN D 138 27684 30642 32008 2195 -2622 -6754 C

ATOM 5830 O ASN D 138 -61.177 52.912 9.547 1.00240.07 O

ANISOU 5830 O ASN D 138 28135 30985 32095 2282 -2677 -6977 O

ATOM 5831 CB ASN D 138 -62.405 51.837 11.741 1.00240.29 C

ANISOU 5831 CB ASN D 138 28117 30244 32939 1612 -2168 -7405 C

ATOM 5832 CG ASN D 138 -63.219 51.447 12.960 1.00237.61 C

ANISOU 5832 CG ASN D 138 27741 29483 33058 1276 -1888 -7570 C

ATOM 5833 ODl ASN D 138 -64.294 50.854 12.844 1.00240.85 O

ANISOU 5833 ODl ASN D 138 28039 29736 33736 1025 -1877 -8020 O

ATOM 5834 ND2 ASN D 138 -62.714 51.789 14.138 1.00233.56 N

ANISOU 5834 ND2 ASN D 138 27315 28790 32636 1266 -1664 -7201 N

ATOM 5835 N PHE D 139 -60.373 54.733 10.588 1.00245.77 N

ANISOU 5835 N PHE D 139 28574 31936 32870 2406 -2773 -6347 N

ATOM 5836 CA PHE D 139 -59.594 55.167 9.431 1.00246.82 C

ANISOU 5836 CA PHE D 139 28730 32459 32591 2772 -3030 -6139 C

ATOM 5837 C PHE D 139 -58.197 55.676 9.799 1.00239.78 C

ANISOU 5837 C PHE D 139 28067 31597 31440 2994 -2900 -5600 C

ATOM 5838 O PHE D 139 -57.816 55.679 10.968 1.00235.12 O

ANISOU 5838 O PHE D 139 27573 30770 30992 2853 -2637 -5374 O

ATOM 5839 CB PHE D 139 -60.361 56.223 8.629 1.00251.19 C

ANISOU 5839 CB PHE D 139 28881 33405 33156 2871 -3378 -6162 C

ATOM 5840 CG PHE D 139 -60.694 57.458 9.412 1.00249.29 C

ANISOU 5840 CG PHE D 139 28429 33176 33113 2798 -3329 -5876 C

ATOM 5841 CDl PHE D 139 -61.797 57.490 10.248 1.00246.29 C

ANISOU 5841 CDl PHE D 139 27882 32548 33150 2465 -3196 -6060 C ATOM 5842 CD2 PHE D 139 -59.907 58.592 9..308 1,,00247.42 C

ANISOU 5842 CD2 PHE D 139 28174 33189 32646 3059 -3402 -5421 C

ATOM 5843 CEl PHE D 139 -62.103 58.626 10.968 1, 00245.16 C

ANISOU 5843 CEl PHE D 139 27571 32392 33185 2392 -3127 -5790 C

ATOM 5844 CE2 PHE D 139 -60.209 59.731 iθ, 025 1.00243.39 C

ANISOU 5844 CE2 PHE D 139 27494 32674 32309 2972 -3326 -5164 C

ATOM 5845 CZ PHE D 139 -61.308 59.748 10.856 1.00241.86 C

ANISOU 5845 CZ PHE D 139 27150 32220 32526 2639 -3184 -5345 C

ATOM 5846 N TYR D 140 -57.443 56.105 8.789 1.00238.46 N

ANISOU 5846 N TYR D 140 27982 31733 30888 3340 -3090 -5392 N

ATOM 5847 CA TYR D 140 -56.069 56.558 8.981 1.00232..31 C

ANISOU 5847 CA TYR D 140 27395 31049 29824 3582 -3013 -4866 C

ATOM 5848 C TYR D 140 -55.520 57.107 7. 662 1.00235..97 C

ANISOU 5848 C TYR D 140 27788 31935 29936 3968 -3344 -4723 C

ATOM 5849 O TYR D 140 -55.851 56.585 6. 602 1.00245..12 O

ANISOU 5849 O TYR D 140 28929 33209 30995 4061 -3531 -5029 O

ATOM 5850 CB TYR D 140 -55.201 55.400 9.480 1.00222..36 C

ANISOU 5850 CB TYR D 140 26538 29505 28444 3573 -2690 -4757 C

ATOM 5851 CG TYR D 140 -53.805 55.823 9.824 1.00216..83 C

ANISOU 5851 CG TYR D 140 26026 28916 27443 3803 -2599 -4193 C

ATOM 5852 CDl TYR D 140 -52.828 55.903 8.848 1.00218..26 C

ANISOU 5852 CDl TYR D 140 26309 29388 27231 4176 -2785 -3951 C

ATOM 5853 CD2 TYR D 140 -53.465 56.166 11.122 1.00212..01 C

ANISOU 5853 CD2 TYR D 140 25476 28140 26937 3646 -2340 -3891 C

ATOM 5854 CEl TYR D 140 -51.540 56.305 9.154 1.00216..24 C

ANISOU 5854 CEl TYR D 140 26210 29258 26694 4387 -2714 -3419 C

ATOM 5855 CE2 TYR D 140 -52.181 56.573 11.443 1.00208..13 C

ANISOU 5855 CE2 TYR D 140 25138 27790 26151 3839 -2270 -3363 C

ATOM 5856 CZ TYR D 140 -51.217 56.641 10.454 1.00209..09 C

ANISOU 5856 CZ TYR D 140 25354 28206 25884 4210 -2459 -3126 C

ATOM 5857 OH TYR D 140 -49.929 57.043 10.755 1.00195..62 O

ANISOU 5857 OH TYR D 140 23792 26655 23881 4400 -2394 -2594 O

ATOM 5858 N PRO D 141 -54.696 58.172 7.708 1.00224..27 N

ANISOU 5858 N PRO D 141 26259 30686 28267 4188 -3417 -4272 N

ATOM 5859 CA PRO D 141 -54.254 58.983 8.851 1.00222..11 C

ANISOU 5859 CA PRO D 141 25994 30331 28067 4084 -3224 -3890 C

ATOM 5860 C PRO D 141 -55.431 59.649 9.560 1.00226..49 C

ANISOU 5860 C PRO D 141 26252 30796 29008 3789 -3200 -4049 C

ATOM 5861 O PRO D 141 -56.563 59.521 9.089 1.00229..32 O

ANISOU 5861 O PRO D 141 26398 31148 29587 3658 -3322 -4457 O

ATOM 5862 CB PRO D 141 -53.371 60.054 8.187 1.00216..86 C

ANISOU 5862 CB PRO D 141 25294 30033 27069 4443 -3411 -3471 C

ATOM 5863 CG PRO D 141 -53.808 60.063 6.740 1.00215..63 C

ANISOU 5863 CG PRO D 141 24952 30169 26807 4676 -3746 -3718 C

ATOM 5864 CD PRO D 141 -54.038 58.621 6.469 1.00223..72 C

ANISOU 5864 CD PRO D 141 26154 30999 27852 4590 -3704 -4099 C

ATOM 5865 N LYS D 142 -55.178 60.350 10. 663 1.00236..83 N

ANISOU 5865 N LYS D 142 27551 32042 30392 3677 -3037 -3722 N

ATOM 5866 CA LYS D 142 -56.267 60.992 11. 395 1.00238.22 C

' ANISOU 5866 CA LYS D 142 27473 32117 30924 3410 -2984 -3818 C

ATOM 5867 C LYS D 142 -57.061 61.962 10.509 1.00247.02 C

ANISOU 5867 C LYS D 142 28235 33568 32053 3556 -3270 -3903 C

ATOM 5868 O LYS D 142 -58.241 62.208 10.755 1.00251.53 O

ANISOU 5868 O LYS D 142 28556 34080 32935 3358 -3291 -4154 O

ATOM 5869 CB LYS D 142 -55.762 61.703 12.663 1.00232.17 C

ANISOU 5869 CB LYS D 142 26798 31224 30193 3267 -2741 -3423 C

ATOM - 5870 CG . LYS D 142 -56.903 62.188 13.584 1.00236.73 C

ANISOU 5870 CG LYS D 142 27154 31645 31149 2974 -2640 -3500 C

ATOM 5871 CD LYS D 142 -56.429 62.956 14.828 1.00228.76 C

ANISOU 5871 CD LYS D 142 26300 30408 30210 2755 -2341 -3182 C

ATOM 5872 CE LYS D 142 -57.623 63.504 15.626 1.00223.11 C

ANISOU 5872 CE LYS D 142 25405 29461 29904 2441 -2208 -3298 C

ATOM 5873 NZ LYS D 142 -57.218 64.341 16.796 1.00209.87 N

ANISOU 5873 NZ LYS D 142 23895 27540 28305 2204 -1907 -3012 N

ATOM 5874 N ASP D 143 -56.414 62.491 9.473 1.00238.65 N

ANISOU 5874 N ASP D 143 27153 32866 30658 3915 -3477 -3682 N

ATOM 5875 CA ASP D 143 -57.000 63.530 8.617 1.00236.57 C

ANISOU 5875 CA ASP D 143 26559 32959 30368 4108 -3725 -3694 C

ATOM 5876 C ASP D 143 -58.320 63.144 7.938 1.00245.58 C

ANISOU 5876 C ASP D 143 27438 34170 31702 4035 -3913 -4166 C

ATOM ' 5877 O ASP D 143 -58.521 61.985 7.566 1.00243.92 O

ANISOU 5877 O ASP D 143 27321 33950 31408 4077 -4022 -4452 ' O

ATOM 5878 CB ASP D 143 -551991 63.949 7.549 1.00229.87 C

ANISOU 5878 CB ASP D 143 25763 32467 29112 4541 -3926 -3429 C

ATOM 5879 CG ASP D 143 -54.767 64.609 8.133 1.00218.52 C

ANISOU 5879 CG ASP D 143 24617 30977 27432 4626 -3761 -2981 C

ATOM 5880 ODl ASP D 143 -54.886 65.775 8.563 1.00211.13 O ANISOU 5880 ODl ASP D 143 23615 30183 26422 4699 -3722 -2643 O

ATOM 5881 0D2 ASP D 143 -53.691 63.967 8.149 1, 00216.12 O

ANISOU 5881 0D2 ASP D 143 24608 30502 27004 4620 -3659 -2959 O

ATOM 5882 N ILE D 144 -59.200 64..133 7.757 1, 00230.41 N

ANISOU 5882 N ILE D 144 25191 32327 30026 3921 -3939 -4233 N

ATOM 5883 CA ILE D 144 -60.505 63..918 7.121 1. 00233.52 C

ANISOU 5883 CA ILE D 144 25280 32847 30599 3849 -4127 -4640 C

ATOM 5884 C ILE D 144 -61.411 65..168 7.150 1. 00238.80 C

ANISOU 5884 C ILE D 144 25573 33699 31461 3827 -4151 -4564 C

ATOM 5885 O ILE D 144 -61.412 65..930 8 ,120 1. 00236..41 O

ANISOU 5885 O ILE D 144 25263 33189 31373 3626 -3918 -4378 O

ATOM 5886 CB ILE D 144 -61.246 62..723 7.768 1. 00230..28 C

ANISOU 5886 CB ILE D 144 24953 32067 30476 3485 -4003 -5037 C

ATOM 5887 CGl ILE D 144 -62.170 62..038 6.765 ' l. 00234..39 C

ANISOU 5887 CGl ILE D 144 25251 32777 31031 3476 -4255 -5485 C

ATOM 5888 CG2 ILE D 144 -62.016 63..163 8.999 1. 00231..02 C

ANISOU 5888 CG2 ILE D 144 24959 31858 30961 3144 -3758 -5013 C

ATOM 5889 CDl ILE D 144 -62.766 60..749 7 288 1. 00230..47 C

ANISOU 5889 CDl ILE D 144 24804 31932 30831 3105 -4133 -5897 C

ATOM 5890 N ASN D 145 -62.171 65..370 6 074 1. 00274..74 N

ANISOU 5890 N ASN D 145 29820 38647 35922 4044 -4419 -4693 N

ATOM 5891 CA ASN D 145 -63.135 66..471 5 ,978 1. 00279..17 C

ANISOU 5891 CA ASN D 145 29988 39432 36651 4055 -4450 -4644 C

ATOM 5892 C ASN D 145 -64.539 65..956 5 677 1. 00283..53 C

ANISOU 5892 C ASN D 145 30264 39986 37477 3816 -4548 -5069 C

ATOM 5893 O ASN D 145 -64.706 65. 071 4 848 1. 00281..52 O

ANISOU 5893 O ASN D 145 30067 39722 37176 ' 3760 -4696 -5419 O

ATOM 5894 CB ASN D 145 -62.698 67. 485 4 908 1. 00279..08 C

ANISOU 5894 CB ASN D 145 29796 39906 36337 4497 -4653 -4429 C

ATOM 5895 CG ASN D 145 -63.877 68.184 4 233 1. 00280..34 C

ANISOU 5895 CG ASN D 145 29495 40439 36583 4587 -4838 " -4591 C

ATOM 5896 ODl ASN D 145 -64.646 67.560 3 502 1. 00284..68 O

ANISOU 5896 ODl ASN D 145 29902 41145 37119 4574 -5065 -4950 O

ATOM 5897 ND2 ASN D 145 -64.005 69.489 4 458 1. 00268..81 N

ANISOU 5897 ND2 ASN D 145 27805 39145 35187 4688 -4732 -4313 N

ATOM 5898 N VAL D 146 -65.545 66.512 6 346 1. 00279..67 N

ANISOU 5898 NN VAL D 146 29492 39494 37274 3660 -4447 -5030 N

ATOM 5899 CCAA VAL D 146 -66.928 66.092 6 127 1. 00282..85 C

ANISOU 5899 CCAA VAL D 146 29592 39935 37945 3434 -4539 -5394 C

ATOM 5900 C VAL D 146 -67.817 67.240 5 641 1. 00289..18 C

ANISOU 5900 C VAL D 146 29947 41103 38824 3559 -4599 -5267 C

ATOM 5901 O VAL D 146. -68.206 68.107 6 425 1. 00287..13 O

ANISOU 5901 O VAL D 146 29624 40729 38744 3490 -4367 -4985 O-

ATOM 5902 CB VAL D 146 -67.547 65.474 7 400 1. 00275..34 C

ANISOU 5902 CB VAL D 146 28765 38469 37382 2994 -4289 -5550 C

ATOM 5903 CGl VAL D 146 -69.040 65.260 7 216 1. 00277..88 C

ANISOU 5903 CGl VAL D 146 28753 38855 37973 2767 -4399 -5921 C

ATOM 5904 CG2 VAL D 146 -66.863 64.165 7 736 1. 00269..13 C

ANISOU 5904 CG2 VAL D 146 28404 37325 36529 2875 -4196 -5679 C

ATOM 5905 N LYS D 147. -68.131 67.236 4 346 1. 00266..59 N

ANISOU 5905 N LYS D 147 26786 38689 35818 3743 -4897 -5468 N

ATOM 5906 CA LYS D 147 -69.012 68.244 3 758 1. 00262..79 C

ANISOU 5906 CA LYS D 147 25845 38620 35383 3890 -4971 -5366 C

ATOM 5907 CC LYS D 147 -70.475 67.856 3 871 1. 00267..06 C

ANISOU 5907 CC LYS D 147 26074 39162 36235 3582 -5013 -5675 C

ATOM 5908 OO LYS D 147 -70.936 66. 927 3 210 1. 00269..60 O

ANISOU 5908 OO LYS D 147 26322 39588 36525 3475 -5238 -6072 O

ATOM 5909 CCBB LYS D 147 -68.657 -68. 518 2 289 1. 00258..40 C

ANISOU 5909 CCBB LYS D 147 25105 38614 34461 4317 -5269 -5353 C

ATOM 5910 CG LYS D 147 -67.885 69. 814 2 080 1. 00253..06 C

ANISOU 5910 CG LYS D 147 24471 38114 33567 4690 -5179 -4905 C

ATOM 5911 CD LYS D 147 -67.661 70. 122 0 608 1. 00248..66 C

ANISOU 5911 CD LYS D 147 23625 38139 32717 5115 r 5455 -4890 C

ATOM 5912 CE LYS D 147 -67.075 71. 519 0.434 1. 00242.78 C

ANISOU 5912 CE LYS D 147 22837 37586 31824 5470 -5314 -4433 C

ATOM 5913 NZ LYS D 147 -65.937 71. 797 1 361 1. 00230.41 N

ANISOU 5913 NZ LYS D 147 21715 35671 30158 5482 -5123 -4171 N

ATOM 5914 N TRP D 148 -71.193 68.572 4 728 1. 00285.47 N

ANISOU 5914 N TRP D 148 28235 41367 38862 3430 -4782 -5480 N

ATOM 5915 CA TRP D 148 -72.641 68.473 4 793 1. 00290.38 C

ANISOU 5915 CA TRP D 148 28506 42038 39788 3175 -4804 -5690 C

ATOM 5916 C TRP D 148 -73.219 69.243 3.616 1. 00294.56 C

ANISOU 5916 C TRP D 148 28549 43189 40183 3451 -4999 -5621 C

ATOM 5917 O TRP D 148 -72.653 70.257 3 209 1. 00292.39 O

ANISOU 5917 O TRP D 148 28187 43166 39742 3779 -4934 -5262 O

ATOM 5918 CB TRP D 148 -73.149 69.071 6 101 1. 00287.47 C

ANISOU 5918 CB TRP D 148 28168 41266 39791 2922 -4450 -5464 C ATOM 5919 CG TRP D 148 -73.120 68.111 7.231 1.00285.16 C

ANISOU 5919 CG TRP D 148 28232 40373 39742 2556 -4274 -5637 C

ATOM 5920 CDl TRP D 148 -72.305 68.148 8.323 1.00278.98 C

ANISOU 5920 CDl TRP D 148 27846 39149 39006 2475 -4002 -5414 C

ATOM 5921 CD2 TRP p 148 -73.946 66.9 ' 57 7.381 1.00285.44 C

ANISOU 5921 CD2 TRP D 148 28251 40198 40007 2223 -4341 -6065 C

ATOM 5922 NEl TRP D 148 " -72.577 67.086 9.147 1.00275.94 N

ANISOU 5922 NEl TRP D 148 27688 38289 38868 2130 -3891 -5671 N

ATOM 5923 CE2 TRP D 148 -73.581 66.339 8.589 1.00279.97 C

ANISOU 5923 CE2 TRP D 148 27958 38915 39504 ' 1968 -4089 -6083 C

ATOM 5924 CE3 TRP D 148 -74.963 66.387 6.612 1.00288.61 C

ANISOU 5924 CE3 TRP D 148 28339 40850 40470 2099 -4583 -6447 C

ATOM 5925 CZ2 TRP D 148 -74.197 65.180 9.045 1.00281.22

ANISOU 5925 CZ2 TRP D 148 28217 38719 39916 1626 -4054 -6456 C

ATOM 5926 CZ3 TRP D 148 -75.572 65.236 7.064 1.00290.55 C

ANISOU 5926 CZ3 TRP D 148 28686- 40745 40963 1734 -4557 -6829 C

ATOM 5927 CH2 TRP D 148 -75.188 64.644 8.268 1.00287.24 C

ANISOU 5927 CH2 TRP D 148 28675 39723 40740 1511 -4286 -6832 C

ATOM 5928 N LYS D 149 -74.336 68.772 3.066 1.00295.14 N

ANISOU 5928 N LYS D 149 28299 43519 40323 3317 -5224 -5962 N

ATOM 5929 CA LYS D 149 -74.934 69.431 1.903 1.00300.54 C

ANISOU 5929 CA LYS D 149 28480 44837 40875 3564 -5421 -5915 C

ATOM 5930 C LYS D 149 -76.464 69.445 1.901 1.00307.77 C

ANISOU 5930 C LYS D 149 28979 45863 42095 3294 -5422 -6047 C

ATOM 5931 O LYS D 149 -77.094 68.570 1.303 1.00309.57 O

ANISOU 5931 O LYS D 149 29125 46093 42403 3020 -5607 -6466 O

ATOM 5932 CB LYS D 149 -74.414 68.811 0.600 1.00296.79 C

ANISOU 5932 CB LYS D 149 27957 44782 40026 3787 -5796 -6184 C

ATOM 5933 CG LYS D 149 -72.958 69.125 0.310 1.00292.14 C

ANISOU 5933 CG LYS D 149 27690 44210 39100 4145 -5823 -5989 C

ATOM 5934 CD LYS D 149 -72.559 68.728 -1.095 1.00290.31 C

ANISOU 5934 CD LYS D 149 27388 44406 38509 4380 -6190 -6241 C

ATOM 5935 CE LYS D 149 -71.192 69.292 -1.435 1.00281.48 C

ANISOU 5935 CE LYS D 149 26508 43384 37056 4811 -6213 -5968 C

ATOM 5936 NZ LYS D 149 -70.775 68.899 -2.804 1.00278.34 N

ANISOU 5936 NZ LYS D 149 26064 43383 36309 5054 . -6566 -6204 N

ATOM 5937 N ILE D 150 -77.054 70.443 2.559 1.00322.01 N

ANISOU 5937 N ILE D 150 30528 47756 44066 3369 -5198 -5679 N

ATOM 5938 CA ILE D 150 -78.502 70.637 2.510 1.00323.86 C

ANISOU 5938 CA ILE D 150 30309 48188 44555 3183 -5200 -5727 C

ATOM 5939 C ILE D 150 -78.938 70.679 1.049 1.00322.30 C

ANISOU 5939 C ILE D 150 29645 48720 44093 3406 -5547 -5872 C

ATOM 5940 O ILE D 150 -78.517 71.556 0.292 1.00314.85 O

ANISOU 5940 O ILE D 150 28498 48227 42905 3815 -5576 -5592 O

ATOM 5941 CB ILE D 150 -78.953 71.939 3.223 1.00322.74 C

ANISOU 5941 CB ILE D 150 30025 47947 44654 3222 -4830 -5253 C

ATOM 5942 CGl ILE D 150 -78.651 71.888 4.724 1.00313.96 C

ANISOU 5942 CGl ILE D 150 29386 46126 43777 3011 -4478 -5088 C

ATOM 5943 CG2 ILE D 150 -80.435 72.164 3.024 1.00323.83 C

ANISOU 5943 CG2 ILE D 150 29710 48260 45071 3008 -4830 -5305 C

ATOM 5944 CDl ILE D 150 -79.314 73.008 5.517 1.00299.13 C

ANISOU 5944 CDl ILE D 150 27410 44085 42161 2993 -4089 -4647 C

ATOM 5945 N ASP D 151 -79.774 69.723 0.656 1.00310.42 N

ANISOU 5945 N ASP D 151 27979 47331 42635 3130 -5802 -6316 N

ATOM 5946 CA ASP D 151 -80.171 69.566 -0.742 1.00315.54 C

ANISOU 5946 CA ASP D 151 28218 48659 43014 3278 -6169 -6532 C

ATOM 5947 C ASP D 151 -78.946 69.463 -1.655 1.00308.39 C

ANISOU 5947 C ASP D 151 27499 47999 41676 3657 -6373 -6550 C

ATOM 5948 O ASP D 151 -78.347 68.394 -1.793 1.00302.78 O

ANISOU 5948 O ASP D 151 27169 47036 40838 3562 -6496 -6848 O

ATOM 5949 CB ASP D 151 -81.104 70.702 -1.184 1.00317.88 C

ANISOU 5949 CB ASP D 151 27932 49489 43360 3447 -6128 -6229 C

ATOM 5950 CG ASP D 151 -82.560 70.450 -0.807 1.00316.25 C

ANISOU 5950 CG ASP D 151 27413 49240 43506 3043 -6092 -6366 C

ATOM 5951 ODl ASP D 151 -83.086 69.365 -1.134 1.00317.41 O

ANISOU 5951 ODl ASP D 151 27435 49521 43644 2765 -6365 -6817 O

ATOM 5952 0D2 ASP D 151 -83.183 71.340 -0.192 1.00310.15 O

ANISOU 5952 0D2 ASP D 151 26520 48307 43017 3003 -5785 -6016 O

ATOM 5953 N GLY D 152 -78.575 70.578 -2.271 1.00311.65 N

ANISOU 5953 N GLY D 152 27647 48899 41868 4098 -6389 -6218 N

ATOM 5954 CA GLY D 152 -77.423 70.607 -3.149 1.00308.66 C

ANISOU 5954 CA GLY D 152 27426 48757 41095 4503 -6560 -6180 C

ATOM 5955 C GLY D 152 -76.239 71.308 -2.517 1.00302.99 C

ANISOU 5955 C GLY D 152 27180 47584 40359 4664 -6290 -5865 C

ATOM 5956 O GLY D 152 -75.364 70.661 -1.943 1.00297.56 O

ANISOU 5956 O GLY D 152 .26960 46378 39722 4455 -6235 -6019 O

ATOM 5957 N SER D 153 -76.228 72.635 -2.612 1.00300.84 N ANISOU 5957 N SER D 153 26770 47523 40012 5033 -6106 -5416 N

ATOM 5958 CA SER D 153 -75.096 73.451 -2.174 1.00297.73 C

ANISOU 5958 CA SER D 153 26768 46829 39528 5259 -5874 -5080 C

ATOM 5959 C SER D 153 -74.576 73.071 -0.787 1.00292.74 C

ANISOU 5959 C SER D 153 26620 45465 39141 4901 -5619 -5079 C

ATOM 5960 O SER D 153 -75.318 72.530 0.033 1.00290.84 O

ANISOU 5960 O SER D 153 26375 44916 39215 4490 -5533 -5251 O

ATOM 5961 CB SER D 153 -75.461 74.937 -2.214 1.00293.09 C

ANISOU 5961 CB SER D 153 25923 46505 38933 5595 -5613 -4588 C

ATOM 5962 OG SER D 153 -76.511 75.222 -1.311 1.00290.42 O

ANISOU 5962 OG SER D 153 25463 45933 38950 5333 -5301 -4405 O

ATOM 5963 N GLU D 154 -73.300 73.372 -0.537 1.00304.37 N

ANISOU 5963 N GLU D 154 28499 46682 40464 5071 -5497 -4873 N

ATOM 5964 CA GLU D 154 -72.613 72.987 0.704 1.00299.41 C

ANISOU 5964 CA GLU D 154 28353 45401 40009 4784 -5255 -4831 C

ATOM 5965 C GLU D 154 -72.868 73.933 1.899 1.00298.25 C

ANISOU 5965 C GLU D 154 28214 44982 40124 4684 -4844 -4445 C

ATOM 5966 O GLU D 154 -72.686 75.152 1.801 1.00295.62 O

ANISOU 5966 O GLU D 154 27750 44879 39693 4986 -4685 -4076 O

ATOM 5967 CB GLU D 154 -71.106 72.798 0.447 1.00290.16 C

ANISOU 5967 CB GLU D 154 27602 44112 38535 5006 -5316 -4768 C

ATOM 5968 CG GLU D J.54 -70.319 72.195 1.611 1.00287.14 C

ANISOU 5968 CG GLU D ~ Ϊ54 27711 43119 38271 4773 -5048 -4645 C

ATOM 5969 CD GLU D 154 -69.327 73.168 2.230 1.00281.48 C

ANISOU 5969 CD GLU D 154 27154 42353 37444 5013 -4792 -4177 C

ATOM 5970 OEl GLU D 154 -68.960 74.156 1.560 1.00281.00 O

ANISOU 5970 OEl GLU D 154 26962 42697 37107 5433 -4888 -3995 O

ATOM 5971 0E2 GLU D 154 -68.902 72.935 3.381 1.00275.48 O

ANISOU 5971 0E2 GLU D 154 26656 41146 36869 4778 -4489 -3995 O

ATOM 5972 N ARG D 155 -73.292 73.336 3.016 1.00291.37 N

ANISOU 5972 N ARG D 155 27505 43615 39589 4260 -4658 -4536 N

ATOM 5973 CA ARG D 155 -73.627 74.036 4.261 1.00284.09 C

ANISOU 5973 CA ARG D 155 26606 42392 , 38944 4116 -4263 -4201 C

ATOM 5974 C ARG D 155 -72.397 74.288 5.125 1.00277.97 C

ANISOU 5974 C ARG D 155 26309 41197 38110 4108 -4013 -3949 C

ATOM 5975 O ARG D 155 -71.670- 73.356 5.463 1.00278.55 O

ANISOU 5975 O ARG D 155 26746 40989 38103 3997 -4093 -4121 O

ATOM 5976 CB ARG D 155 -74.651 73.216 5.058 1.00286.53 C

ANISOU 5976 CB ARG D 155 26853 42360 39655 3668 -4177 -4409 C

ATOM 5977 CG ARG D 155 -74.426 73.175 6.571 1.00281.49 C

ANISOU 5977 CG ARG D 155 26672 41039 39242 3328 -3924 -4405 C

ATOM 5978 CD ARG D 155 -74.711 74.511 7.232 1.00277.75 C

ANISOU 5978 CD ARG D 155 26269 40318 38944 3296 -3511 -3965 C

ATOM 5979 NE ARG D 155 -76.080 74.968 7.001 1.00283.62 N

ANISOU 5979 NE ARG D 155 26563 41365 39836 3365 -3425 -3798 N

ATOM 5980 CZ ARG D 155 -77.083 74:805 7.860 1.00285.60 C

ANISOU 5980 CZ ARG D 155 26696 41360 40458 3081 -3224 -3763 C

ATOM 5981 NHl ARG D 155 -76.869 74.190 9.017 1.00285.38 N

ANISOU 5981 NHl ARG D 155 26974 40751 40705 2709 -3085 -3895 N

ATOM 5982 NH2 ARG D 155 -78.301 75.256 7.566 1.00280.89 N

ANISOU 5982 NH2 ARG D 155 25674 41093 39960 3185 -3147 -3576 N

ATOM 5983 N GLN D 156 -72.173 75.547 5.489 1.00283.99 N

ANISOU 5983 N GLN D 156 27074 41926 38905 4218 -3693 -3530 N

ATOM 5984 CA GLN D 156 -71.010 75.908 6.292 1.00278.42 C

ANISOU 5984 CA GLN D 156 26801 40863 38122 4201 -3446 -3268 C

ATOM 5985 C GLN D 156 -71.343 76.113 7.775 1.00282.25 C

ANISOU 5985 C GLN D 156 27508 40782 38954 3799 -3097 -3162 C

ATOM 5986 O GLN D 156 -70.532 75.786 8.645 1.00282.88 O

ANISOU 5986 O GLN D 156 27921 40436 39126 3523 -3082 -3325 O

ATOM 5987 CB GLN D 156 -70.312 77.155 5.729 1.00276.71 C

ANISOU 5987 CB GLN D 156 26519 40959 37658 4595 -3305 -2873 C

ATOM 5988 CG GLN D 156 -69.459 76.919 4.474 1.00280.05 C

ANISOU 5988 CG GLN D 156 26956 41769 37681 4992 -3602 -2921 C

ATOM 5989 CD GLN D 156 -70.165 77.308 3.178 1.00281.48 C

ANISOU 5989 CD GLN D 156 26661 42564 37724 5329 -3855 -3007 C

ATOM 5990 OEl GLN D 156 -71.374 77.543 3.158 1.00286.94 O

ANISOU 5990 OEl GLN D 156 26995 43415 38614 5232 -3868 -3096 O

ATOM 5991 NE2 GLN D 156 -69.403 77.379 2.089 1.00267.59 N

ANISOU 5991 NE2 GLN D 156 24892 41161 35619 5733 -4055 -2968 N

ATOM 5992 N ASN D 157 -72.533 76.639 8.061 1.00290.98 N

ANISOU 5992 N ASN D 157 28426 41882 40251 3775 -2807 -2885 N

ATOM 5993 CA ASN D 157 -72.892 77.024 9.431 1.00289.31 C

ANISOU 5993 CA ASN D 157 28451 41134 40338 3438 -2424 -2703 C

ATOM 5994 C ASN D 157 -74.016 76.199 10.073 1.00291.56 C

ANISOU 5994 C ASN D 157 28648 41112 41019 3063 -2416 -2951 C

ATOM 5995 O ASN D 157 -75.135 76.149 9. ^ 570 1.00294.17 O

ANISOU 5995 O ASN D 157 28582 41692 41497 3076 -2496 -3028 O ATOM 5996 CB ASN D 157 -73.228 78.515 9.488 1.00285.17 C

ANISOU 5996 CB ASN D 157 27828 40696 39827 3583 -2058 -2253 C

ATOM 5997 CG ASN D 157 -72.305 79.351 8.624 1.00285.82 C

ANISOU 5997 CG ASN D 157 27872 41199 39526 4015 -2093 -2032 C

ATOM 5998 ODl ASN D 157 -72.368 79.294 7.397 1.00284.51 O

ANISOU 5998 ODl ASN D 157 27446 41510 39143 4318 -2411 -2178 O

ATOM 5999 ND2 ASN D 157 -71.446 80.137 9.261 1.00286.75 N

ANISOU 5999 ND2 ASN D 157 . 28255 41139 39557 4041 -1756 -1680 N

ATOM 6000 N GLY D 158 -73.708 75.578 11.208 1.00264.32 N

ANISOU 6000 N GLY D 158 25563 37127 37741 2733 -2307 -3061 N

ATOM 6001 CA GLY D 158 -74.617 74.656 11.862 1.00259.86 C

ANISOU 6001 CA GLY D 158 24965 36222 37549 2377 -2304 -3328 C

ATOM 6002 C GLY D 158 -74.049 73.250 11.805 1.00263.36 C

ANISOU 6002 C GLY D 158 25599 36535 37932 2255 -2573 -3742 C

ATOM 6003 O GLY D 158 -74.782 72.290 11.588 1.00263.25 O

ANISOU 6003 O GLY D 158 25389 36578 38056 2130 -2785 -4096 O

ATOM 6004 N VAL D 159 -72.733 73.136 11.985 1.00268.45 N

ANISOU 6004 N VAL D 159 26627 37020 38353 2295 -2553 -3687 N

ATOM 6005 CA VAL D 159 -72.034 71.849 11.934 1.00265.42 C

ANISOU 6005 CA VAL D 159 26485 36482 37882 2200 -2750 -4024 C

ATOM 6006 C VAL D 159 -71.202 71.620 13.208 1.00259.60 C

ANISOU 6006 C VAL D 159 26214 35235 37189 1992 -2494 -3898 C

ATOM 6007 O VAL D 159 -70.493 72.520 13.668 1.00253.49 O

ANISOU 6007 O VAL D 159 25613 34386 36317 2045 -2264 -3533 O

ATOM 6008 CB VAL D 159 -71.128 71.741 10.686 1.00258.69 C

ANISOU 6008 CB VAL D 159 25533 36090 36609 2545 -3076 -4118 C

ATOM 6009 CGl VAL D 159 -70.828 70.289 10.380 1.00257.53 C

ANISOU 6009 CGl VAL D 159 25649 35797 36405 2433 -3273 -4502 C

ATOM 6010 CG2 VAL D 159 -71.795 72.390 9.491 1.00259.19 C

ANISOU 6010 CG2 VAL D 159 25185 36704 36593 2786 -3299 -4169 C

ATOM 6011 N LEU D 160 -71.279 70.403 13.752 1.00263.43 N

ANISOU 6011 N LEU D 160 26898 35384 37811 1756 -2525 -4200 N

ATOM 6012 CA LEU D 160 -70.809 70.101 15.110 1.00259.20 C

ANISOU 6012 CA LEU D 160 26747 34319 37418 1497 -2247 -4111 C

ATOM 6013 C LEU D 160 -69.993 68.795 15.191 1.00257.93 C

ANISOU 6013 C LEU D 160 26871 33983 37148 1433 -2349 -4379 C

ATOM 6014 O LEU D 160 -70.451 67.809 15.774 1.00257.54 O

ANISOU 6014 O LEU D 160 26890 33594 37369 1178 -2297 -4659 O

ATOM 6015 CB LEU D 160 -72.030 70.004 16.035 1.00260.17 C

ANISOU 6015 CB LEU D 160 26793 34052 38009 1179 -2024 -4158 C

ATOM 6016 CG LEU D 160 -72.004 70.491 17.485 1.00257.42 C

ANISOU 6016 CG LEU D 160 26685 33252 37871 959 -1635 -3855 C

ATOM 6017 CDl LEU D 160 -71.412 69.441 18.400 1.00254.66 C

ANISOU 6017 CDl LEU D 160 26673 32400 37686 689 -1497 -4013 C

ATOM 6018 CD2 LEU D 160 -71.266 71.814 17.602 1.00253.09 C

ANISOU 6018 CD2 LEU D 160 26276 32854 37031 1133 -1492 -3428 C

ATOM 6019 N ASN D 161 -68.785 68.799 14.624 1.00252.01 N

ANISOU 6019 N ASN D 161 26291 33455 36005 1674 -2469 -4275 N

ATOM 6020 CA ASN D 161 -67.938 67.600 14.560 1.00244.80 C

ANISOU 6020 CA ASN D 161 25654 32427 34933 1667 -2555 -4479 C

ATOM 6021 C ASN D 161 -67.125 67.334 15.828 1.00239.98 C

ANISOU 6021 C ASN D 161 25433 31370 34377 1465 -2271 -4331 C

ATOM 6022 O ASN D 161 -66.870 68.244 16.616 1.00240.60 O

ANISOU 6022 O ASN D 161 25621 31314 34481 1398 -2040 -3994 O

ATOM 6023 CB ASN D 161 -66.966 67.685 13.377 1.00245.80 C

ANISOU 6023 CB ASN D 161 25806 32981 34607 2029 -2801 -4405 C

ATOM 6024 CG ASN D 161 -67.671 67.787 12.043 1.00249.35 C

ANISOU 6024 CG ASN D 161 25880 33900 34 * 960 2253 -3105 -4573 C

ATOM 6025 ODl ASN D 161 -68.882 67.979 11.982 1.00255.12 O

ANISOU 6025 ODl ASN D 161 26305 34684 35945 2149 -3129 -4704 O

ATOM 6026 ND2 ASN D 161 -66.912 67.664 10.961 1.00245.48 N

ANISOU 6026 ND2 ASN D 161 25411 33766 34096 2570 -3336 -4556 N

ATOM 6027 N SER D 162 -66.700 66.085 16.007 1.00220.68 N

ANISOU 6027 N SER D 162 23203 28712 31934 1371 -2277 -4577 N

ATOM 6028 CA SER D 162 -65.835 65.720 17.126 1.00218.36 C

ANISOU 6028 CA SER D 162 23275 28040 31651 1212 -2019 -4446 C

ATOM 6029 C SER D 162 -64.996 64.498 16.777 1.00220.48 C

ANISOU 6029 C SER D 162 23769 28335 31667 1323 -2114 -4601 C

ATOM 6030 O SER D 162 -65.550 63.458 16.430 1.00226.03 O

ANISOU 6030 O SER D 162 24429 28976 32478 1264 -2211 -4983 O

ATOM 6031 CB SER D 162 -66.669 65.426 18.371 1.00217.33 C

ANISOU 6031 CB SER D 162 23177 27423 31977 864 -1779 -4605 C

ATOM 6032 OG SER D 162 -65.844 65.190 19.497 1.00206.40 O

ANISOU 6032 OG SER D 162 22135 25684 30603 719 -1530 -4504 O

ATOM 6033 N TRP D 163 -63.670 64.624 16.880 1.00244.66 N

ANISOU 6033 N TRP D 163 27076 31491 34392 1476 -2071 -4301 N

ATOM 6034 CA TRP D 163 -62.736 63.539 16.544 1.00243.16 C ANISOO 6034 CA TRP D 163 27129 31321 33941 1601 -2123 -4384 C

ATOM 6035 C TRP D 163 -62.609 62.508 17 ,661 1.00239.72 C

ANISOU 6035 C TRP D 163 26963 30436 33684 1360 -1847 -4472 C

ATOM 6036 O TRP D 163 -62.942 62.780 18 ,812 1.00241.41 O

ANISOU 6036 O TRP D 163 27254 30352 34120 1136 -1596 -4328 O

ATOM 6037 CB TRP D 163 -61.334 64.088 16 261 1 ,00238.37 C

ANISOU 6037 CB TRP D 163 26675 30998 32897 1870 -2179 -3999 C

ATOM 6038 CG TRP D 163 -61.228 64.945 15 052 1.00246..14 C

ANISOU 6038 CG TRP D 163 27438 32442 33642 2176 -2464 -3941 C

ATOM 6039 CDl TRP D 163 -60.385 64..766 13 997 1.00247..99 C

ANISOU 6039 CDl TRP D 163 27709 32983 33534 2480 -2696 -3963 C

ATOM 6040 CD2 TRP D 163 -61.985 66..128 14 769 1.00247..63 C

ANISOU 6040 CD2 TRP D 163 27337 32838 33912 2226 -2531 -3837 C

ATOM 6041 NEl TRP D 163 -60.570 65..765 13 072 1.00251..92 N

ANISOU 6041 NEl TRP D 163 27946 33872 33900 2722 -2916 -3889 N

ATOM 6042 CE2 TRP D 163 -61.549 66..612 13, 523 1.00251..56 C

ANISOU 6042 CE2 TRP D 163 27691 33781 34108 2575 -2810 -3807 C

ATOM 6043 CE3 TRP D 163 -62.989 66..824 15 448 1.00238..45 C

ANISOU 6043 CE3 TRP D 163 26027 31523 33049 2021 -2362 -3751 C

ATOM 6044 CZ2 TRP D 163 -62.085 67..754 12 942 1.00245..96 C

ANISOU 6044 CZ2 TRP D 163 26687 33382 33385 2732 -2918 -3699 C

ATOM 6045 CZ3 TRP D 163 -63.516 67..951 ' 14, 871 1.00241..18 C

ANISOU 6045 CZ3 TRP D 163 26093 32168 33378 2170 -2457 -3634 C

ATOM 6046 CH2 TRP D 163 -63.065 -68..408 13.631 1.00242..48 C

ANISOU 6046 CH2 TRP D 163 26107 32790 33236 2527 -2729 -3609 C

ATOM 6047 N THR D 164 -62.102 61..330 17.319 1.00185.53 N

ANISOU 6047 N THR D 164 20255 23520 26718 1414 -1874 -4703 N

ATOM 6048 CA THR D 164 -61.813 60..317 18.327 1.00181.98 C

ANISOU 6048 CA THR D 164 20085 22681 26379 1241 -1585 -4740 C

ATOM 6049 C THR D 164 -60.309 60..230 18.580 1.00188, 69 C

ANISOU 6049 C THR D 164 21210 23636 26846 1410 -1496 -4358 C

ATOM 6050 O THR D 164 -59.516 60.622 17.721 1.00187.79 O

ANISOU 6050 O THR D 164 21083 23890 26378 1681 -1697 -4163 O

ATOM 6051 CB THR D 164 -62.405 58.943 17.933 1.00185.49 C

ANISOU 6051 CB THR D 164 20571 22957 26949 1177 -1589 -5200 C

ATOM 6052 OGl THR D 164 -63.562 58.698 18.731 1.00190.80 O

ANISOU 6052 OGl THR D 164 21103 23312 28082 890 -1479 -5485 O

ATOM 6053 CG2 THR D 164 -61.424 57.802 18.166 1.00189.55 C