Inhibitors of DHODH, an enzyme of the pyrimidine biosynthesis, and pharmaceutical compositions containing them, are useful, for example, for the treatment of rheumatoid arthritis (RA). Its treatment with usual medications as for example non-steroid anti- inflammatory agents is not satisfactory. In view of the increasing ageing of the population, especially in the developed Western countries or in Japan, the development of new medications for the treatment of RA is urgently required.

The DHODH inhibiting leflunomide (ARAVA) [EP 780128, WO 97/34600] is the first medicament of this class of compounds (leflunomides) for the treatment of RA.

Leflunomide has immunomodulatorial as well as anti-inflammatorial properties [EP 217206, DE 2524929].

In the body, DHODH catalyzes the synthesis of pyrimidines, which are necessary for cell growth. An inhibition of DHODH inhibits the growth of (pathologically) fast proliferating cells, whereas cells which grow at normal speed may obtain their required pyrimidine bases from the normal metabolic cycle. The most important types of cells for the immune response, the lymphocytes, use exclusively the synthesis of pyrimidines for their growth and react particularly sensitively to DHODH inhibition. Substances that inhibit the growth of lymphocytes are important medicaments for the treatment of auto-immune diseases.

WO 99/45926 is a further reference that discloses compounds which act as inhibitors of DHODH. A further object of the present invention is to provide alternative effective agents which can be used for the treatment of diseases which require the inhibition of DHODH.

In Structure, 2000, Vol. 8, No. 1, pages 25-33, the structure of human DHODH in complex with the antiproliferative agents brequinar and leflunomide are described.

In Structure, 2000, Vol. 8, No. 1, pages 1227-1238, crystal structures of DHODH B and its product complex are determined. In Pharmaceutical Reasearch, 1998, Vol. 15, No. 2, pages 286-295, and in Biochemical Pharmacology, 1990, Vol. 40, No. 4, pages 709-714, the structure-activity relationship of leflunomide and quinoline carboxylic acid analogues is analyzed.

In the Journal of Medicinal Chemistry, 1999, Vol. 42, pages 3308-3314, virtual combinatorial syntheses and computational screening of new potential anti-Herpes compounds are described. In Table 3 on page 3313 experimental results regarding ICso and cytotoxicity are presented for 2- (2, 3-difluorophenylcarbamoyl)-l-cyclopentene-l- carboxylic acid, 2- (2, 6-difluorophenylcarbamoyl)-l-cyclopentene-l-carboxylic acid and 2- (2,3, 4-trifluorophenyl-carbamoyl)-1-cyclopentene-1-carboxylic acid.

In one embodiment, the present invention relates to a polypeptide comprising the ligand binding domain of human dihydroorotate dehydrogenase (DHODH), crystalline forms of this polypeptide complexed with a ligand, and the three dimensional structure of the polypeptide, including the three dimensional structure of the ubiquinone binding site of DHODH.

In another embodiment, the present invention provides a method of determining the three dimensional structure of a crystalline polypeptide comprising the ubiquinone binding site of DHODH complexed with the ligands. The method comprises the steps of (1) obtaining a crystal of the polypeptide comprising the ubiquinone binding site of DHODH complexed with a ligand; (2) obtaining x-ray diffraction data for said crystal; and (3) solving the crystal structure of said crystal by using said x-ray diffraction data and the atomic coordinates for the DHODH complex with the ligand.

The invention further relates to a method of identifying a compound which is a potential inhibitor of DHODH. The method comprises the steps of (1) obtaining a crystal of the polypeptide comprising the ubiquinone binding site of DHODH complexed with a

ligand; (2) obtaining the atomic coordinates of the polypeptide in said crystal; (3) using said atomic coordinates to define the ubiquinone binding site of DHODH complexed with a ligand; and (4) identifying a compound which fits the ubiquinone binding site. The method can further include the steps of obtaining or synthesizing the compound to inhibit at least one biological activity of DHODH, such as enzymatic activity.

In another embodiment, the method of identifying a potential inhibitor of DHODH comprises the step of determining the ability of one or more functional groups and/or moieties of the compound, when present in, or bound to, the ubiquinone binding site of DHODH; to interact with one or more subsites of the ubiquinone binding site of DHODH.

Generally, the ubiquinone binding site of DHODH is defined by the atomic coordinates of a polypeptide comprising the ubiquinone binding site of DHODH. If the compound is able to interact with a preselected number or set of subsites, or has a calculated interaction energy with a desired or preselected range, the compound is identified as a potential inhibitor of DHODH.

The human DHODH enzyme is composed of two domains, namely a large C-terminal domain (Met78 to C-terminus) and a small N-terminal domain (Met30 to Leu68), connected by an extended loop. The large C-terminal domain can be described best as an afp-barrel fold with a central barrel of eight parallel B strands surrounded by eight a helices. The redox site, formed by the substrate binding site and the site of the cofactor flavine mononucleotide (FMN), is located on this large C-terminal domain. The small N- terminal domain, on the other hand, consists of two a helices, al and a2, connected by a short loop. This small N-terminal domain contains the binding site for the cofactor ubiquinone. The helices al and a2 span a slot of about 10 x 20 A in the so-called hydrophobic patch, with the short al-a2 loop at the narrow end of that slot. The slot forms the entrance to a tunnel that ends at the FMN cavity nearby the al-a2 loop. This tunnel is narrowing towards the proximal redox site and ends with several charged or polar sidechains (Gln47, His56, Tyr356, Thr360 and Arg36). It is evident that ubiquinone which can easily diffuse into the mitochondrial inner membrane uses this tunnel to approach the FMN cofactor for a redox reaction.

The structural knowledge mentioned above can be used to design potential inhibitors of the human DHODH activity targeting the tunnel mentioned above and

competing with ubiquinone for the ubiquinone binding site. Potential inhibitors were co- crystallized with human DHODH (Met30 to Arg396) and the three dimensional structures were solved by protein X-ray crystallography techniques, ten of the solved structures being three dimensional structures of human DHODH (Met30 to Arg396) in complex with compounds 1,2, 3,4, 5,6, 7,8, 9, and 10. These crystal structures were solved at atomic resolution and the binding modes of the ten compounds were analyzed. The structural formulars of the co-crystallized compounds are given below.

H N HO O Compound 1 Compound 2 Compound 3 Compound 4 Compound 5 Compound 6 Compound 8 Compound 7 F HO F 0 0 F 0 0 F s Han Compound 9 F

Compound 10 Detailed analysis of the three dimensional structure of the DHODH small N- terminal domain as well as the three dimensional structure of DHODH in complex with certain inhibitors designed to target the ubiquinone binding site revealed the presence of a number of subsites. Each subsite includes molecular functional groups or moieties capable of forming stabilizing interactions with complementary functional groups or moieties of an inhibitor.

The found subsites are characterized below according to the properties of functional groups or chemical moieties they are complementary to, or they can interact with in a stabilizing way, for example, groups or moieties capable of hydrogen bond formation or groups or moieties with hydrophobic (= lipophilic) character. A hydrogen bond is formed between a hydrogen atom covalently bond to an electronegative element (proton donor or hydrogen bond donor) and a lonely electron pair of a second electronegative atom (proton acceptor or hydrogen bond acceptor). Hydrogen bonds typically occur when the hydrogen bond donor and the hydrogen bond acceptor are separated by about 2.5 A and 3.5 A.

Stabilizing hydrophobic or lipophilic interactions occur if two groups or moieties with hydrophobic/lipophilic character, for example, aliphatic chains or aromatic systems, are separated by distances close to their van der Waals radii.

The method of identifying a potential inhibitor of DHODH comprises the step of determining the ability of one or more functional groups and/or moieties of the compound, when present in the ubiquinone binding site, to interact with one or more subsites of the ubiquinone binding site. Preferably, the ubiquinone binding site is defined by the atomic coordinates of a polypeptide comprising the ubiquinone binding site of DHODH. If the

compound is able to interact with a preselected number or set of subsites, the compound is identified as a potential inhibitor of DHODH.

A functional group or moiety of the compound is said to"interact"with a subsite of the ubiquinone binding site if it participates in an energetically favourable, or stabilizing, interaction with one or more complementary moieties within the subsite.

Two chemical moieties are"complementary"if they are capable, when suitably positioned, of participating in an attractive, or stabilizing, interaction, such as an electrostatic or an van der Waals interaction. Typically, the attractive interaction is an ion- ion, a salt bridge, ion-dipole, dipole-dipole, hydrogen bond, pi-pi or hydrophobic interaction. An extreme case of attractive interaction is the formation of a covalent bond by a chemical reaction between the test compound and the enzyme. For example, a negatively charged moiety and a positively charged moiety are complementary because, if suitably positioned, they can form a salt bridge. Likewise, a hydrogen bond donor and a hydrogen bond acceptor are complementary if suitably positioned.

Preferably, the groups capable of hydrogen bond formation ("HB") are selected from halogen, such as fluorine, chlorine, bromine and iodine, NO2, haloalkyl, haloalkyloxy, CN, hydroxyl, amino, hydroxylamine, hydroxamic acid, carbonyl, carbonic acid, sulfonamide, amide, sulfone, sulfonic acid, alkylthio, alkoxy, ester, hydroxyalkylamino group, and other groups including a heteroatom having at least one lone pair of electrons, such as groups containing trivalent phosphorous, di-and tetravalent sulfur, oxygen and nitrogen atoms; Preferably, hydrophobic groups ("H") are selected from groups, such as linear, branched or cyclic alkyl groups; linear, branched or cyclic alkenyl groups; linear, branched or cyclic alkynyl groups; aryl groups, such as mono-and polycyclic aromatic hydrocarbyl groups and mono-and polycyclic heteroaryl groups; Preferably, negatively charged groups ("N") are selected from groups, such as carboxylate, sulfonamide, sulfamate, boronate, vanadate, sulfonate, sulfinate and phosphonate groups. A given chemical moiety can contain one or more of these groups.

In the following a detailed description of identified subsites is provided. Residue numbering and atom labeling is identical to the numbering and labeling in Fig. 2,3 and 4.

Subsite 1 : Hydrophobic pocket; interacting chemical moieties: H; Residues involved: Leu 42; Met 43; Leu 46; Ala 55; Ala 59; Phe 98; Met 111; Leu 359; Pro 364; Non-hydrogen atoms which interact with H: Leu 42 CB, CG, CD1, CD2; Met 43 SD, CE; Leu 46 CB, CG, CD1, CD2; Ala 55 CB; Ala 59 CA, CB; Phe 98 CG, CD1, CD2, CE1, CE2; Met 111 SD, CE; Leu 359 CA, CB, CG, CD1, CD2; Pro 364 CB, CD, CG; Preferably for the hydrophobic interacting with subsite 1, the group is selected from aryl groups, such as an aromatic group having five to fifteen carbon atoms, which can optionally be substituted by one or more substituents R'. More preferably the aryl group is a phenyl group, such as-CH2Ph,-C2H4Ph,-CH=CH-Ph,-C=C-Ph,-o-C6H4-R',-m- C6H4-R',-p-C6H4-R',-o-CH2-C6H4-R',-m-CHZ-C6H4-R',-p-CH2-C6H4 -R' ; or a biphenyl group, in which the phenyl rings can optionally be substituted by one or more substituents R', such biphenyl groups are-C6H4-C6H5 ;-C6H4-C6H4-R' ;-C6H3-R'-C6H5 ; -C6H3-R'-C6H4-R'; -C6H3-R'-C6H4-R'; -C6H4-O-C6H5; -C6H3-R'-O-C6H4-R'; -C6H4-O-C6H4-R'; - C6H3-R-OC6H5 R'-O-C6H5; -C6H4-O-CH2-C6H5; -C6H3- ;-C6H3-R-O-CH2-C6H4-R ;-C6H4-O-CH2- C6H4-R ;-C6H3-R-0-CHz-CgHg ; R is independently H, -CO2R'', -CONHR'', -CR''O, -SO2NR'', -NR''-CO-haloalkyl, <BR> <BR> <BR> <BR> - NO2,-NR"-SO2-haloalkyl,-NR"-SO2-alkyl,-SO2-alkyl,-NR"-CO-alk yl,-CN, alkyl, cycloalkyl, aminoalkyl, alkylamino, alkoxy, -OH,-SH, alkylthio, hydroxyalkyl, hydroxyalkylamino, halogen, haloalkyl, haloalkyloxy, aryl, arylalkyl or heteroaryl; R"is independently hydrogen, haloalkyl, hydroxyalkyl, alkyl, cycloalkyl, aryl, heteroaryl or aminoalkyl ; R is preferably F, Cl, Br, I, CF3, OCF3, or OCH3 ; Subsite 2: First anion binding site; interacting with HB, N, HB and N, HB and HB, or N and N ; Residues involved: Gln 47; Arg 136; one conserved water molecule Non-hydrogen atoms which interact with HB and N: Glu 47 OE1, NE2; Arg 136 NE, NH1, NH2 ; conserved water molecule OH2.

preferably for one or two hydrogen bond formations with subsite 2 the group is selected from halogen, such as fluorine, chlorine, bromine and iodine, NOz, haloalkyl, haloalkyloxy, CN, hydroxyl, amino, hydroxylamine, hydroxamic acids, carbonyl, carbonic acid, sulfonamide, amide, sulfone, sulfonic acid, alkylthio, alkoxy, such as methoxy, ester, hydroxyalkylamino, carboxylate, tetrazole, sulfonamide, sulfamate, boronate, vanadate, sulfonate, sulfinate and phosphonate group, more preferably from a carboxylate, sulfonamide, sulfamate, sulfonate, carbonyl or carbonic acid group.

Subsite 3: Second anion binding site; interacting with HB, N, HB and N, HB and HB, or N and N ; Residues involved: His 56; Tyr 356; Tyr 147 (interacting via a conserved water molecule); Non-hydrogen atoms which interact with HB and N: His 56 N, ND1 ; Tyr 356 OH; Tyr 147 OH (interacting via a conserved water molecule); preferably for one or two hydrogen bond formations with subsite 2 the group is selected from halogen, such as fluorine, chlorine, bromine and iodine, NO ?,, haloalkyl, haloalkyloxy, CN, hydroxyl, amino, hydroxylamine, hydroxamic acids, carbonyl, carbonic acid, sulfonamide, amide, sulfone, sulfonic acid, alkylthio, alkoxy, such as methoxy, ester, hydroxyalkylamino, carboxylate, tetrazole, sulfonamide, sulfamate, boronate, vanadate, sulfonate, sulfinate and phosphonate group, more preferably from a carboxylate, sulfonamide, sulfamate, sulfonate, carbonyl or carbonic acid group.

Subsite 4: Remote hydrophobic pocket; interacting chemical moieties: H; Residues involved: Pro 52; Val 134; Arg 136; Val 143; Thr 360; FMN; Non-hydrogen atoms which interact with H: Pro 52 CB, CG, CD; Val 134 CB, CG1, CG2; Val 143 CB, CG1, CG2; Thr 360 CG2; FMN C7M, C8M ; Preferably for the hydrophobic interacting with subsite 4, the group is selected from such as linear, branched or cyclic Cl-C6-alkyl groups; such as methyl, ethyl, propyl, butyl, tert. butyl, linear, branched or cyclic Cl-C6-alkenyl groups; linear, branched or cyclic Cl-C6- alkynyl groups; aryl groups, such as mono-and bi aromatic hydrocarbyl groups, such as- <BR> <BR> <BR> CH2Ph,-C2H4Ph,-CH=CH-Ph,-C=C-Ph,-o-C6H4-R',-m-C6H4-R,-p-C6H4 -R,-o- CH2-C6H4-R,-m-CH2-C6H4-R,-p-CHz-C6H4-R and mono-and bicyclic heteroaryl groups, such as thiazol-2-yl, thiazol-4-yl, thiazol-5-yl, isothiazol-3-yl, isothiazol-4-yl, isothiazol-5-yl, 1, 2,4-oxadiazol-3-yl, 1, 2,4-oxadiazol-5-yl, 1, 2,4-thiadiazol-3-yl, 1,2, 4-

thiadiazol-5-yl, 1, 2,5-oxadiazol-3-yl, 1, 2,5-oxadiazol-4-yl, 1, 2,5-thiadiazol-3-yl, 1-imidazolyl, 2-imidazolyl, 1, 2,5-thiadiazol-4-yl, 4-imidazolyl, 1-pyrrolyl, 2-pyrrolyl, 3- pyrrolyl, 2-furanyl, 3-furanyl, 2-thienyl, 3-thienyl, 2-pyridyl, 3-pyridyl, 4-pyridyl, 2- pyrimidinyl, 4-pyrimidinyl, 5-pyrimidinyl, 3-pyridazinyl, 4-pyridazinyl, 2-pyrazinyl, 1- pyrazolyl, 3-pyrazolyl, 4-pyrazolyl, indolyl, indolinyl, tetrazolyl, benzo- [b]-furanyl, benzo [b] thiophenyl, benzimidazolyl, benzothiazolyl, quinazolinyl, quinoxazolinyl, or preferably isoxazol-3-yl, isoxazol-4-yl, isoxazol-5-yl, quinolinyl, tetrahydroquinolinyl, isoquinolinyl, tetrahydroisoquinolinyl; all this groups can optionally be substituted by one or more substituents R, such as H, amino, alkoxy, OH, SH, alkylthio, hydroxyalkyl, haloalkyl, haloalkyloxy hydroxyalkylamino, halogen; R is preferably F, Cl, Br, I, CF3, OCF3, or OCH3; Core: chemical moiety connecting the different moieties interacting with Subsite 1, Subsite 2, Subsite 3, and Subsite 4; Preferably, the core is selected from cyclic alkyl groups; cyclic alkenyl groups; cyclic alkynyl groups; aryl groups, such as mono-and polycyclic aromatic hydrocarbyl groups and mono-and polycyclic heteroaryl groups; more preferably it is selected from mono-, or bicyclic aromatic or non-aromatic ring systems, most preferably from 5-membered mono-, or bicyclic aromatic or non-aromatic ring systems, such as trans-cyclopentan-1, 2-diyl, trans-cyclohexan-1, 2-diyl, cis-cyclopentan-1, 2-diyl, cis-cyclohexan-1, 2-diyl, 1- cyclopenten-1, 2-diyl, 2-cyclopenten-1, 2-diyl, 3-cyclopenten-1, 2-diyl, 4-cyclopenten-1, 2- diyl, 5-cyclopenten-1, 2-diyl, 1-cyclopenten-1, 3-diyl, 1-cyclopenten-1, 4-diyl, 1- cyclohexen-1, 2-diyl, 1-cyclohepten-1, 2-diyl or 1-cycloocten-1, 2-diyl, 2,5- dihydrothiophene-3,4-diyl, 2,5-dihydro-furan-3, 4-diyl, 2, 5-dihydro-lH-pyrrole-3, 4-diyl, 2, 5-dihydro-1-methyl-pyrrole-3, 4-diyl, 2, 5-dihydro-1-ethyl-pyrrole-3, 4-diyl, 2,5-dihydro- 1-acetyl-pyrrole-3, 4-diyl, 2, 5-dihydro-1-methylsulfonyl-pyrrole-3, 4-diyl, thiazol-2-yl, thiazol-4-yl, thiazol-5-yl, isothiazol-3-yl, isothiazol-4-yl, isothiazol-5-yl, 1,2, 4-oxadiazol- 3-yl, 1, 2,4-oxadiazol-5-yl, 1, 2,4-thiadiazol-3-yl, 1, 2,4-thiadiazol-5-yl, 1, 2,5-oxadiazol-3- yl, 1, 2,5-oxadiazol-4-yl, 1, 2,5-thiadiazol-3-yl, 1-imidazolyl, 2-imidazolyl, 1,2, 5-thiadiazol- 4-yl, 4-imidazolyl, 1-pyrrolyl, 2-pyrrolyl, 3-pyrrolyl, 2-furanyl, 3-furanyl, 2-thienyl, 3-thienyl, 2-pyridyl, 3-pyridyl, 4-pyridyl, 2-pyrimidinyl, 4-pyrimidinyl, 5-pyrimidinyl, 3-pyridazinyl, 4-pyridazinyl, 2-pyrazinyl, 1-pyrazolyl, 3-pyrazolyl, 4-pyrazolyl, indolyl, indolinyl, tetrazolyl, benzo- [b]-furanyl, benzo [b] thiophenyl, benzimidazolyl, benzothiazolyl, quinazolinyl, quinoxazolinyl, or preferably quinolinyl, tetrahydro- quinolinyl, isoquinolinyl, tetrahydroisoquinolinyl or from a group comprising of:

Bridge: chemical moiety connecting the core with Subsite 1; Preferably, the bridge is selected from-NH ;-O ; -CO-NH;-NH-CO ; -NH-CO-NH; alkyl ; <BR> <BR> <BR> -O-CH2 ;-CH2-O ;-O-CH2-CH2 ;-CH2-CH2-O ;-NH-CH2 ;-CH2-NH ;-NH-CH2-CH2 ;-CH2- CH2-NH ;-CH2-CO-NH ;-CH2-NH-CO ; Subsite 5: Solvent anchor; interacting chemical moieties : HB Residues involved: Met 30; Tyr 38; Leu 67; Non-hydrogen atoms which interact with HB: Met 30 O, SD, CE; Tyr 38 OH, CE2, CD2; Leu 67 O ; preferably for the hydrogen bond formation with subsite 5, the group is selected from F, Cl, Br, I, CF3, OCF3, or OCH3 Subsite 6: Solvent anchor; interacting chemical moieties: H; Residues involved: Leu 68; Non-hydrogen atoms which interact with H: Leu 68 CB, CG, CD1, CD2; Preferably for the hydrophobic interacting with subsite 6, the group is selected from such as linear, branched or cyclic Cl-C6-alkyl groups; such as methyl, ethyl, propyl, butyl, tert. butyl, linear, branched or cyclic Cl-C6-alkenyl groups; linear, branched or cyclic Cl-C6- alkynyl groups; aryl groups, such as mono-and bi aromatic hydrocarbyl groups, such as- <BR> <BR> <BR> CH2Ph,-C2H4Ph,-CH=CH-Ph,-C=C-Ph,-o-C6H4-R',-m-C6H4-R,-p-C6H4 -R,-o- CH2-C6H4-R,-m-CH2-C6H4-R,-p-CH2-C6H4-R and mono-and bicyclic heteroaryl groups.

An alkyl group, if not stated otherwise, denotes a linear or branched Cl-C6-alkyl, preferably a linear or branched chain of one to five carbon atoms, a linear or branched Cl-

C6-alkenyl or a linear or branched Cl-C6-alkinyl group, which can optionally be substituted by one or more substituents R', preferably by halogen; the Cl-C6-alkyl, Cl-C6-alkenyl and Cl-C6-alkinyl residue may be selected from the group comprising -CH3, -C2H5, -CH=CH2, -C#CH, -C3H7, -CH (CH3) 2,-CH2-CH=CH2, -C (CH3) =CH2, -CH=CH-CH3, -C#C-CH3, -CH2-C#CH, -C4H9, -CH2-CH (CH3) 2, -CH(CH3)-C2H5, -C (CH3) 3, -C5H11, -C6H13, -C (R) 3, -C2(R')5, -CH2-C(R')3, -C3(R')7, -C2H4-C (R) 3,-C2H4-CH=CH2,-CH=CH-C2H5,-CH=C (CH3) 2,-CH2-CH=CH-CH3, -CH=CH-CH=CH2,-C2H4-C-CH,-C-C-C2H5,-CH2-C-C-CH3,-C-C-CH=CH2, -CH=CH-C#CH, -C#C-C#CH, -C2H4-CH (CH3) 2,-CH (CH3)-C3H7,-CH2-CH (CH3) - C2H5,-CH (CH3) -CH (CH3) 2,-C (CH3) 2-C2H5,-CH2-C (CH3) 3,-C3H6-CH=CH2, <BR> <BR> <BR> <BR> - CH=CH-C3H7,-C2H4-CH=CH-CH3,-CH2-CH=CH-C2H5,-CH2-CH=CH-CH=CH2 , -CH=CH-CH=CH-CH3, -CH=CH-CH2-CH=CH2, -C (CH3) =CH-CH=CH2, -CH=C(CH3)-CH=CH2, -CH=CH-C (CH3) =CH2,-CH2-CH=C (CH3) 2, C (CH3) =C (CH3) 2, <BR> <BR> <BR> <BR> -C3H6-C#CH, -C#C-C3H7, -C2H4-C#C-CH3, -CH2-C#C-C2H5, -CH2-C#C-CH=CH2,<BR> <BR> <BR> <BR> <BR> -CH2-CH=CH-C#CH, -CH2-C#C-C#CH, -C#C-CH=CH-CH3, -CH=CH-C#C-CH3,<BR> <BR> <BR> <BR> <BR> <BR> -C#C-C#C-CH3, -C#C-CH2-CH=CH2, -CH=CH-CH2-C#CH, -C#C-CH2-C#CH, -C (CH3) =CH-CH=CH2,-CH=C (CH3) -CH=CH2, -CH=CH-C (CH3) =CH2,-C (CH3) =CH- C=CH,-CH=C (CH3)-C=CH,-C=C-C (CH3) =CH2, -C3H6-CH (CH3) 2,-C2H4-CH (CH3) - C2H5,-CH (CH3)-C4H9,-CH2-CH (CH3)-C3H7,-CH (CH3)-CH2-CH (CH3) 2,-CH (CH3)- CH (CH3)-C2H5,-CH2-CH (CH3) -CH (CH3) 2,-CH2-C (CH3) 2-C2H5,-C (CH3) 2-C3H7,- C (CH3) 2-CH (CH3) 2,-C2H4-C (CH3) 3, -CH (CH3) -C (CH3) 3, -C4H8-CH=CH2, -CH=CH- <BR> <BR> <BR> <BR> C4H9,-C3H6-CH=CH-CH3,-CH2-CH=CH-C3H7,-C2H4-CH=CH-C2H5,-CH2- C (CH3) =C (CH3) 2,-C2H4-CH=C (CH3) 2, -C4H8-C#CH, -C#C-C4H9, -C3H6-C#C-CH3, -CH2-C#C-C3H7, -C2H4-C#C-C2H5; R is independently H, -CO24'', -CONHR'', -CR''O, -SO2NR'', -NR''-CO-haloalkyl, -NO2, -NR''-SO2-haloalkyl, -NR''-SO2-alkyl, -SO2-alkyl, -NR''-CO-alkyl, -CN, alkyl, cycloalkyl, aminoalkyl, alkylamino, alkoxy, -OH,-SH, alkylthio, hydroxyalkyl, hydroxyalkylamino, halogen, haloalkyl, haloalkyloxy, aryl, arylalkyl or heteroaryl; R"is independently hydrogen, haloalkyl, hydroxyalkyl, alkyl, cycloalkyl, aryl, heteroaryl or aminoalkyl ;

a cycloalkyl group denotes a non-aromatic ring system containing four to eight carbon atoms, preferably four to eight carbon atoms, wherein one or more of the carbon atoms in the ring can be substituted by a group X, X being as defined above; the C4-C8-cycloalkyl residue may be selected from the group comprising-cyclo-C4H7,-cyclo-C5H9, - cyclo-C6H11, -cyclo-C7H13, -cyclo-C8H15; an alkoxy group denotes an 0-alkyl group, the alkyl group being as defined above; the alkoxy group is preferably a methoxy, ethoxy, isopropoxy, t-butoxy or pentoxy group; an alkylthio group denotes an S-alkyl group, the alkyl group being as defined above. an haloalkyl group denotes an alkyl group which is substituted by one to five halogen atoms, the alkyl group being as defined above; the haloalkyl group is preferably a-C (Rl°) 3, -CR10(R10')2, -CR10(R10')R10'', -C2(R10)5, -CH2-C(R10)3, -CH2-CR10(R10')2, -CH2- CR10(R10')R10'', -C3(R10)7 or -C2H4-C(R10)3, wherein Rl°, Rl°'Rl°"repre t F Cl B I, preferably F; a hydroxyalkyl group denotes an HO-alkyl group, the alkyl group being as defined above; an haloalkyloxy group denotes an alkoxy group which is substituted by one to five halogen atoms, the alkyl group being as defined above; the haloalkyloxy group is preferably a -OC(R10)3, -OCR10(R10')2, -OCR10(R10')R10'', -OC2(R10)5, -OCH2-C(R10)3, -OCH2- CR° (R°) 2,-OCH2-CRi° (R°) R°,-OC3 (Rlo) 7 or -OC2H4-C(R10) 3, wherein Rl°, R10', Rl°"represent F, Cl, Br or I, preferably F; a hydroxyalkylamino group denotes an (HO-alkyl) 2-N- group or HO-alkyl-NH-group, the alkyl group being as defined above; an alkylamino group denotes an HN-alkyl or N-dialkyl group, the alkyl group being as defined above; a halogen group is chlorine, bromine, fluorine or iodine, fluorine being preferred;

an aryl group preferably denotes an aromatic group having five to fifteen carbon atoms, which can optionally be substituted by one or more substituents R', where R'is as defined above; the aryl group is preferably a phenyl group,-CH2Ph,-C2H4Ph,-CH=CH-Ph,- <BR> <BR> <BR> <BR> C=C-Ph,-0-C6H4-R',-m-C6H4-R',-p-C6H4-R',-o-CHZ-C6H4-R',-m-CH 2-C6H4-<BR> <BR> <BR> <BR> <BR> <BR> R',-p-CHz-C6H4-R'; a heteroaryl group denotes a 5-or 6-membered heterocyclic group which contains at least one heteroatom like O, N, S. This heterocyclic group can be fused to another ring. For example, this group can be selected from a thiazol-2-yl, thiazol-4-yl, thiazol-5-yl, isothiazol-3-yl, isothiazol-4-yl, isothiazol-5-yl, 1, 2,4-oxadiazol-3-yl, 1, 2,4-oxadiazol-5-yl, 1, 2,4-thiadiazol-3-yl, 1, 2,4-thiadiazol-5-yl, 1, 2,5-oxadiazol-3-yl, 1, 2,5-oxadiazol-4-yl, 1, 2,5-thiadiazol-3-yl, 1-imidazolyl, 2-imidazolyl, 1, 2,5-thiadiazol-4-yl, 4-imidazolyl, 1-pyrrolyl, 2-pyrrolyl, 3-pyrrolyl, 2-furanyl, 3-furanyl, 2-thienyl, 3-thienyl, 2-pyridyl, 3- pyridyl, 4-pyridyl, 2-pyrimidinyl, 4-pyrimidinyl, 5-pyrimidinyl, 3-pyridazinyl, 4- pyridazinyl, 2-pyrazinyl, 1-pyrazolyl, 3-pyrazolyl, 4-pyrazolyl, 1H-tetrazol-2-yl, 1H- tetrazol-3-yl, tetrazolyl, indolyl, indolinyl, benzo- [b]-furanyl, benzo [b] thiophenyl, benzimidazolyl, benzothiazolyl, quinazolinyl, quinoxazolinyl, or preferably quinolinyl, tetrahydroquinolinyl, isoquinolinyl, tetrahydroisoquinolinyl group. This heterocyclic group can optionally be substituted by one or more substituents R', where R'is as defined above.

In another embodiment, the present invention provides DHODH inhibitors, and methods of use thereof, which are capable of binding to the ubiquinone binding site of DHODH, for example, compounds wich are identified as inhibitors of DHODH or which are designed by the methods described above to inhibit DHODH. For example, the invention includes compounds which interact with one or more, preferably two or more, and more preferably, three or more of DHODH subsites 1 to 6.

Preferably an inhibitor of DHODH should have a core-unit and interact with subsite 1,2, 3 and 5 or an inhibitor of DHODH should have a core-unit and interact with subsite 1, 2 and 5, or an inhibitor of DHODH should have a core-unit and interact with subsite 1,3 and 5.

More preferably an inhibitor of DHODH should have a core-unit and interact with subsite 1,2 and 3, or an inhibitor of DHODH should have a core-unit and interact with subsite 1 and 3.

In Fig. 1, the spatial arrangement of the subsites is depicted schematically. subsite 2 subsite 1//\ \ r - ( (core) ST ; z CD m subsite 1 subsite 3

Fig. 1 The three dimensional structure published by Shenpig et al. shows human DHODH (Met30-Arg396) in complex with brequinar and the leflunomide metabolite A771726, respectively. The main interaction in the binding of brequinar to DHODH is the formation of a salt bridge between the carboxy group of brequinar and the sidechain of Argl36. In particular, the salt bridge is formed between the carboxylic group and the atoms NE, NH1 or NH2. More precisely, the above mentioned subsite 2, the first anion binding site, is addressed in this kind of interaction. In the following, this type of interactioned will be termed"brequinar-like binding mode".

Analysis of the three dimensional structures of human DHODH in complex with ligands presented here clearly shows a new binding mode for inhibitors containing a carboxylic acid group. This binding mode differs from the brequinar-like binding mode in interacting not with subsite 2 but with subsite 3, termed the second anion binding site. In particular this is true for inhibitor compounds 1,4, 5,7 and 8 as can be seen from figure 2. This so far unobserved binding mode will be termed"non-brequinar-like"binding mode in the following.

The"non-brequinar-like"binding mode is characterized by a number of hydrogen bonds formed between the ligand and protein residues belonging to subsite 3. In particular this residues are His 56, Tyr 356 and Tyr 147. Non-hydrogen atoms involved in the

formation of hydrogen bonds are N and ND1 of His 56, the oxygen of the hydroxyl group of Tyr 356 and the oxygen of the hydroxyl group of Tyr 147. The latter interaction involves a conserved water molecule bridging the space between the carboxyl function of the ligand molecule and the hydroxyl group of the tyrosine residue 147.

Similar findings can be seen in the three dimensional structure of human DHODH in complex with the compounds 2,6 and 10. As can be seen clearly from the electron density map, the compounds 2,6 and 10 are able to utilize both anion binding sites (subsite 2 and 3) by adopting two alternative conformations. Therefore, both a brequinar-like and a non-brequinar-like binding mode can be utilized. In the brequinar-like binding mode the carboxy group of compounds 2,6 and 10 forms hydrogen bonds to the sidechains of residues Gln 47 and Arg 136. In the non-brequinar-like binding mode the five membered ring of compounds 2,6 and 10 containing the carboxy group is rotated by almost 180 degrees and forms hydrogen bonds to residues His 56 and Tyr 356. Non-hydrogen atoms involved in the formation of hydrogen bonds are N and ND1 of His 56 and the oxygen of the hydroxyl group of Tyr 356.

The compounds 2,3 and 4 are particularly interesting for a structure-activity- relationship (SAR) analysis. These molecules differ only in the degree of ring substitution (see structures above). Clearly, one can observe a correlation between the number of fluorinated positions at the aromatic ring in the middle of the molecules and the corresponding ICso values. The higher the number of ring substituents the lower the IC50.

Interestingly compound 2 and compound 3 display both the brequinar-like and non- brequinar-like binding mode in the crystal structure (see table 27). It is quite reasonable to speculate whether the ring substituents exhibit a steering effect on the five membered ring and by such facilitate the formation of the more favourable brequinar-like binding mode.

Therefore, the presence of both binding modes might explain the increased affinity of this compounds.

Table 27: Relation of inhibitor binding mode and degree of ring substitutions. Structures of the compounds are shown above.

Compound Brequinar-like Non-Brequinar-like

3 x x 2 X X 4 X A similar structure-activity-relationship can be deduced from the crystal structures of humann DHODH in complex with compounds 9 and 10. These compounds carry a sulfur atom at an ortho position with respect to the carboxylic group in the five membered ring. Compound 10 is single substituted with fluorine at the biaryl ring system, whereas compound 9 bears two substituents. Interestingly, compound 9 exhibits a pure brequinar- like binding mode whereas compound 10 shows both alternatives. Additionally, the sulfur atom in the ortho position on the five membered ring can favourably interact with the protein's subsite 4 (remote hydrophobic pocket). The activity data correlate to a very high degree with the presence of a particular binding mode (Table 28). Obviously, not only the degree of ring subsitution but also ring planarity might contribute to the formation of a particular binding mode.

Table 28: Relation of inhibitor binding mode and degree of ring substitutions. Structures of the compounds are shown above.

Compound Brequinar-like Non-Brequinar-like 9 X 10 X X From the discussion above several possibilities for further synthesis of compounds emerge. First, one could try to stabilize the Brequinar-like conformation by a more elaborate variation of substitution patterns at the aromatic ring system. A second way to improve on the affinity might comprise the addition of a second functional group, which is able to form hydrogen bonds or salt bridges to the five membered ring opposite to the position of the carboxy group. Thus the molecule should be able to address both anion subsites and utilize brequinar-like as well as non-brequinar-like binding modes at the same time. This is highly supported by the evidence of structural data. Mobility at the site of Gln47 and Argl36 indicates that the protein should be able to exhibit sufficient conformational flexibility to adopt ligand molecules displaying more demanding sterical requirements.

Another interesting finding is that the DHODH binding pocket is able to selectively discriminate between enantiomeres. Compounds 5 and 6 were synthesized as a racemic mixtures caused by the presence of a stereo centre at the five membered ring (see above).

The racemic mixtures were used for crystallization experiments. In both cases the refined structures unequivocally showed the inhibitor bound in its R-form. It is not possible to fit the S-enantiomer into the electron density.

The invention further provides a method of designing a compound which is a potential inhibitor of DHODH. The method includes the steps of (1) identifying one or more functional groups capable of interacting with one or more subsites of the ubiquinone binding site of DHODH; and (2) identifying a scaffold which presents the functional group or functional groups identified in step 1 in a suitable orientation for interacting with one or more subsites of the ubiquinone binding site of DHODH. The compound which results from attachment of the identified functional groups or moieties to the identified scaffold is a potential inhibitor of DHODH. The DHODH ubiquinone binding site is, generally, defined by the atomic coordinates of a polypeptide comprising the DHODH ubiquinone binding site.

The present invention also provides several advantages. For example, the invention provides a new three dimensional structure of a crystalline polypeptide comprising the ubiquinone binding site of DHODH complexed with the ligands. This structure enables the rational development of inhibitors of DHODH by permitting the design and/or identification of molecular structures having features which facilitate binding to the ubiquinone binding site of DHODH. The methods of use of this structure disclosed herein, thus, permit more rapid discovery of compounds which are potentially useful for the treatment of conditions which are mediated, at least in part, by DHODH activity.

The polypeptide preferably comprises the ubiquinone binding site of a mammalian DHODH. More preferably the polypeptide comprises the ubiquinone binding site of human DHODH. In a preferred embodiment, the polypeptide is a polypeptide of the present invention, as described above.

The polypeptide can be crystallized using methods known in the art, such as the methods described in Structure, 2000, Vol. 8, No. 1, pages 25-33, to afford polypeptide crystals which are suitable for x-ray diffraction studies. A crystalline polypeptide/ligand complex can be produced by co-crystallizing the polypeptide with a solution including the ligand.

The atomic coordinates of the polypeptide and the ligand can be determined, for example, by x-ray crystallography using methods known in the art. The data obtained from the crystallography can be used to generate atomic coordinates, for example, of the polypeptide and ligand, if present. As is known in the art, solution and refinement of the x- ray crystal structure can result in the determination of coordinates for some or all of the non-hydrogen atoms.

The atomic coordinates of the polypeptide can be used, as is known in the art, to generate a three-dimensional structure of the ubiquinone binding site of DHODH. This structure can then be used to assess the ability of any given compound, preferably using computer-based methods, to fit into the ubiquinone binding site.

The atomic coordinates of the polypeptide/ligand complex can be used, as is known in the art, to generate a three-dimensional structure of the ligand in its binding conformation.

This structure can then be used to assess the ability of any given compound, preferably using computer-based methods, to exhibit a similar spatial orientation and electrostatic and/or van der Waals interactions as the ligand and therefore, to fit into the addressed binding site.

A compound fits into the ubiquinone binding site if it is of suitable size and shape to physically reside in the ubiquinone binding site, that is if it has a shape which is complementary to the ubiquinone binding site and can reside in the ubiquinone binding site without significant unfavorable sterical or van der Waals interactions. Preferably, the compound includes one or more functional groups and/or moieties which interact with one or more subsites within the ubiquinone binding site. Computational methods for evaluating the ability of a compound to fit into the ubiquinone binding site, as defined by the atomic coordinates of the polypeptide, are known in the art, and representative examples are provided below.

In another embodiment, the method of identifying a potential inhibitor of DHODH comprises the step of determining the ability of one or more functional groups and/or moieties of the compound, when present in the DHODH ubiquinone binding site, to interact with one or more subsites of the DHODH ubiquinone binding site. Preferably, the DHODH ubiquinone binding site is defined by the atomic coordinates of a polypeptide comprising the DHODH ubiquinone binding site. If the compound is able to interact with a preselected number of subsites, the compound is identified as a potential inhibitor of DHODH.

In yet another embodiment, the method of identifying a potential inhibitor of DHODH comprises the steps of (1) identifying the size and shape of the ligand co-crystallized in the polypeptide/ligand complex and/or identifying functional groups or moieties of the ligand which are capable to form stabilizing interactions with the polypeptide, and (2) by comparison with these, identifying one or more functional groups and/or moieties of any given compound which have similar size and shape as the cocrystallized ligand and/or are capable to form one or more interactions to the polypeptide in a similar manner as the co- crystallized ligand. If a compound exhibits one or more of these features, the compound is identified as a potential inhibitor of DHODH.

A functional group or moiety of the compound is said to"interact"with a subsite of the DHODH ubiquinone binding site if it participates in an energetically favourable, or stabilizing, interaction with one or more complementary moieties within the subsite, as defined above.

A functional group or moiety of the compound is said to interact in a"similar"manner as the co-crystallized ligand if one or more, preferably two or more of its functional groups or moieties capable of forming the attractive interactions mentioned above can be superimposed on those functional groups or moieties of the co-crystallized ligand capable of forming the attractive interactions. The superposition can be performed based on the identity of atoms, and/or the identity or similarity of functional groups, and/or the similarity of molecular shape and/or the identity or similarity of interaction possibilities.

For example, an-OH group of a compound and an-NH group of the cocrystallized ligand may interact in the same way, namely as hydrogen bond donors, with a hydrogen bond acceptor atom suitably positioned in the enzyme. Therefore, the-OH group and the-NH

group are said to have similar interaction properties, and a molecule containing an-OH group may be superimposed onto a molecule carrying an-NH group at the corresponding position.

Typically, the assessment of interactions between (1) the test compound and the DHODH ubiquinone binding site and (2) the superposition of a test compound and the co- crystallized ligand employ computer-based computational methods, such as those known in the art, in which, for the first case, possible interactions of a compound with the protein, as defined by atomic coordinates, are evaluated with respect to interaction strength by calculating the interaction energy upon binding the compound to the protein. For the second case, the superposition of a test compound and the cocrystallized ligand is performed according to the identity of atoms, and/or the identity or similarity of functional groups, and/or the similarity of molecular shape and/or the identity or similarity of interaction possibilities in a process termed alignment. Matching atoms/functional groups /shape/interaction possibilities are evaluated and summarized to an alignment score enabling the ranking of the tested molecules.

Compounds which have calculated interaction energies within a preselected range or which otherwise, in the opinion of the computational chemist employing the method, have the greatest potential as DHODH inhibitors, can then be provided, for example, from a compound library or via synthesis, and assayed for the ability to inhibit DHODH. The interaction energy for a given compound generally depends upon the ability of the compound to interact with one or more subsites within the protein catalytic domain.

In one embodiment, the atomic coordinates used in the method are the atomic coordinates set forth in Figs. 2,3 and 4. It is to be understood that the coordinates set forth in Figs. 2,3 and 4 can be transformed, for example, into a different coordinate system, in ways known to those of skill in the art without substantially changing the three dimensional structure represented thereby.

In certain cases a moiety of the compound can interact with a subsite via two or more individual interactions. A moiety of the compound and a subsite can interact if they have complementary properties and are positioned in sufficient proximity and in a suitable orientation for a stabilizing interaction to occur. The possible range of distances for the

moiety of the compound and the subsite depends upon the distance dependence of the interaction, as known in the art. For example, a hydrogen bond typically occurs when a hydrogen bond donor atom, which bears a hydrogen atom, and a hydrogen bond acceptor atom are separated by about 2.5 Å and about 3.5 Å. Hydrogen bonds are well known in the art. Generally, the overall interaction, or binding, between the compound and the ubiquinone binding site will depend upon the number and strength of these individual interactions.

The ability of a test compound to interact with one or more subsites of the ubiquinone binding site can be determined by computationally evaluating interactions between functional groups, or moieties, of the test compound and one or more amino acid side chains and/or backbone atoms in the ubiquinone binding site. Typically, a compound which is capable of participating in stabilizing interactions with a preselected number of subsites, preferably without simultaneously participating in significant destabilizing interactions, is identified as a potential inhibitor of DHODH. Such a compound will interact with one or more subsites, preferably with two or more subsites and, more preferably, with three or more subsites.

The invention further provides methods of designing a compound which is a potential inhibitor of DHODH.

The first method includes the steps of (1) identifying one or more functional groups capable of interacting with one or more subsites of the DHODH ubiquinone binding site; and (2) identifying a scaffold which presents the functional group or functional groups identified in step 1 in a suitable orientation for interacting with one or more subsites of the DHODH ubiquinone binding site. The compound which results from attachment of the identified functional groups or moieties to the identified scaffold is a potential inhibitor of DHODH. The DHODH ubiquinone binding site is, generally, defined by the atomic coordinates of a polypeptide comprising the DHODH ubiquinone binding site, for example, the atomic coordinates set forth in Figs. 2,3 and 4.

The second method comprises the steps of (1) identifying one or more functional groups or moieties capable of interacting in a similar way as one or more functional groups or moieties of the co-crystallized ligand, and (2) identifying a scaffold which presents the functional group or functional groups identified in step 1 in a suitable orientation for

interacting in a similar way as one or more functional groups or moieties of the co- crystallized ligand. The compound which results from attachment of the identified functional groups or moieties to the identified scaffold is a potential inhibitor of DHODH.

The co-crystallized ligand is, generally, defined by the atomic coordinates of a ligand complexed in the polypeptide comprising the DHODH ubiquinone binding site, for example, the atomic coordinates set forth in Figs. 2,3 and 4.

Suitable methods, as known in the art, can be used to identify chemical moieties, fragments or functional groups which are capable of interacting favorably with a particular subsite or sets of subsites. These methods include, but are not limited to: interactive molecular graphics; molecular mechanics; conformational analysis; energy evaluation; docking; database searching; virtual high-throughput screening (US 422303, DE 10009479, EP 1094415, US 693731, US 885893, US 885517); structural alignment; functional group alignment; interaction-point alignment ; pharmacophore modeling; de novo design; property estimation and descriptor-based database searching. These methods can also be employed to assemble chemical moieties, fragments or functional groups into a single inhibitor molecule. These same methods can also be used to determine whether a given chemical moiety, fragment or functional group is able to interact favorably with a particular subsite or sets of subsites.

In one embodiment, the design of potential DHODH inhibitors begins from the general perspective of three-dimensional shape and electrostatic complementarity for the ubiquinone binding site, and subsequently, interactive molecular modeling techniques can be applied by one skilled in the art to visually inspect the quality of the fit of a candidate molecule into the binding site. Suitable visualization programs include SYBYL (Tripos Inc. , St. Louis, MO), MOLOC (Gerber Molecular Design, Basel), RASMOL (Sayle et al.

Trends Biochem. Sci. 20: 374-376 (1995) ) and MOE (Chemical Computing Group Inc., Montreal).

A further embodiment of the present invention utilizes a database searching program which is capable of scanning a database of small molecules of known three-dimensional structure for candidates which fit into the target protein site. Suitable software programs include 4SCan (US 422303, DE 10009479, EP 1094415, US 693731, US 885893, US 885517),

FLEXX (Rarey et al. , J. Mol. Biol. 261: 470-489 (1996) ), and UNITY (Tripos Inc. , St.

Louis, MO). Especially 4SCan was developed to scan/screen large virtual databases up to several millions of small molecules in a reasonable time-frame.

A further embodiment of the present invention utilizes a database searching program which is capable of scanning a database of small molecules of known three-dimensional structure for candidates which align properly with the co-crystallized ligand, both in shape and interaction properties. Suitable software programs include 4SCan (US 422303, DE 10009479, EP 1094415, US 693731, US 885893, US 885517) and FLEXS (Lemmen et al., J. Med. Chem 41: 4502-4520 (1998) ). Especially 4SCan is capable of aligning large virtual databases up to several millions of small molecules in a reasonable time-frame.

It is not expected that the molecules found in the search will necessarily be leads themselves, since a complete evaluation of all interactions will necessarily be made during the initial search. Rather, it is anticipated that such candidates might act as the framework for further design, providing molecular skeletons to which appropriate atomic replacements can be made. Of course, the chemical complementarity of these molecules can be evaluated, but it is expected that the scaffold, functional groups, linkers and/or monomers may be changed to maximize the electrostatic, hydrogen bonding, and hydrophobic interactions with the enzyme.

Goodford (Goodford J. Med. Chem. 28: 849-857 (1985) ) has produced a computer program, GRID, which seeks to determine regions of high affinity for different chemical groups (termed probes) on the molecular surface of the binding site. GRID hence provides a tool for suggesting modifications to known ligands that might enhance binding.

Consequently, virtual combinatorial libraries covering numerous variations of the addressed scaffold, functional groups, linkers and/or monomers can be build up using suitable software programs including LEGION (Tripos Inc. , St. Louis, MO) or ACCORD FOR EXCEL (Accelrys Inc. , San Diego, CA), followed by scanning or virtual screening or docking of these libraries using suitable software mentioned above.

A range of factors, including electrostatic interactions, hydrogen bonding, hydrophobic interactions, desolvation effects, conformational strain, ligand flexibility and cooperative

motions of ligand and enzyme, all influence the binding effect and should be taken into account in attempts to design bioactive inhibitors.

Yet another embodiment of a computer-assisted molecular design method for identifying inhibitors of DHODH comprises searching for fragments which fit into a binding region subsite and link to a pre-defined scaffold. The scaffold itself may be identified in such a manner. A representative program suitable for the searching of such functional groups and monomers include LUDI (Boehm, J. Comp. Aid. Mol. Des. 6: 61-78 (1992) ) and MCSS (Miranker et al., Proteins 11: 314-328 (1991)).

Yet another embodiment of a computer-assisted molecular design method for identifying inhibitors of DHODH comprises the de novo synthesis of potential inhibitors by algorithmic connection of small molecular fragments that will exhibit the desired structural and electrostatic complementarity with the active site of the enzyme. The methodology employs a large template set of small molecules which are iteratively pierced together in a model of the DHODH ubiquinone binding site. Programs suitable for this task include GROW (Moon et al. Proteins 11: 314-328 (1991) ) and SPROUT (Gillet et al. J. Comp. Aid.

Mol. Des. 7: 127 (1993)).

In yet another embodiment, the suitability of inhibitor candidates can be determined using an empirical scoring function, which can rank the binding affinities for a set of inhibitors.

For examples of such a method see Muegge et al. and references therein (Muegge et al. , J.

Med. Chem. 42: 791-804 (1999) ) and ScoreDock (Tao et al. J Comp. Aid. Mol. Des. 15: 429-446 (2001)).

Other modeling techniques can be used in accordance with this invention, for example, those described by Stahl (Stahl, in: Virtual Screening for Bioactive Molecules, Wiley- VCH, Weinheim, 2000, pp. 229-264), Cohen et al. (J. Med. Chem. 33: 883-894 (1990) ) ; Navia et al. (Current Opinions in Structural Biology 2: 202-210 (1992) ) ; Baldwin et al. (J.

Med. Chem. 32: 2510-2513 (1989) ) ; Appelt et al. (J. Med. Chem. 34: 1925-1934 (1991) ) ; Ealick et al. (Proc. Nat. Acad. Sci. USA 88: 11540-11544 (1991) ) ;

A compound which is identified by one of the foregoing methods as a potential inhibitor of DHODH can then be obtained, for example, by synthesis or from a compound library, and assessed for the ability to inhibit DHODH in vitro. Such an in vitro assay can be performed as is known in the art, for example, by contacting DHODH in solution with the test compound in the presence of the substrate and cofactor of DHODH and ubiquinone. The rate of substrate transformation can be determined in the presence of the test compound and compared with the rate in the absence of the test compound. Suitable assays for DHODH biological activity are described below, the teachings of each of which are hereby incorporated by reference herein in their entity.

An inhibitor identified or designed by a method of the present invention can be a competitive inhibitor, an uncompetitive inhibitor or a noncompetitive inhibitor with respect to ubiquinone.

A screen of thousands of compounds using 4Scan 0 as described above was performed. Hits were ranked according to consensus score.

In table 25 the structures of the highest ranking compounds of the combinatorial library are shown. The consensus score of each molecule is calculated by the summation of the two predicted 4SCan activity scores for the two different structures of the ubiquinone binding site.

The compounds of the present invention can be used for a variety of human and animal diseases, preferably human diseases, where inhibition of the pyrimidine metabolism is beneficial. Such diseases are: - fibrosis, uveitis, rhinitis, asthma or arthropathy, in particular, arthrosis - all forms of rheumatism - acute immunological events and disorders such as sepsis, septic shock, endotoxic shock, Gram-negative sepsis, toxic shock syndrome, acute respiratory distress syndrome, stroke, reperfusion injury, CNS injury, serious forms of allergy, graft versus host and host versus graft reactions, alzheimer's disease or pyresis, restenosis, chronic pulmonary inflammatory disease, silicosis, pulmonary sarcosis, bone resorption disease. These immunological events also include a desired modulation and suppression of the immune system ;

- all types of autoimmune diseases, in particular rheumatoid arthritis, rheumatoid spondylitis, osteoarthritis, gouty arthritis, multiple sclerosis, insulin dependent diabetes mellitus and non-insulin dependent diabetes mellitus, and lupus erythematoidis, ulcerative colitis, Morbus Crohn, inflammatory bowel disease, as well as other chronic inflammations, chronic diarrhea; - dermatological disorders such as psoriasis - progressive retinal atrophy - all kinds of infections including opportunistic infections.

The compounds according to the invention and medicaments prepared therewith are generally useful for the treatment of cell proliferation disorders, for the treatment or prophylaxis, immunological diseases and conditions (as for instance inflammatory diseases, neuroimmunological diseases, autoimmune diseases or other).

The compounds of the present invention are also useful for the development of immunomodulatory and anti-inflammatory medicaments or, more generally, for the treatment of diseases where the inhibition of the pyrimidine biosynthesis is beneficial.

The compounds of the present invention are also useful for the treatment of diseases which are caused by malignant cell proliferation, such as all forms of hematological and solid cancer. Therefore the compounds according to the invention and medicaments prepared therewith are generally useful for regulating cell activation, cell proliferation, cell survival, cell differentiation, cell cycle, cell maturation and cell death or to induce systemic changes in metabolism such as changes in sugar, lipid or protein metabolism. They can also be used to support cell generation poiesis, including blood cell growth and generation (prohematopoietic effect) after depletion or destruction of cells, as caused by, for example, toxic agents, radiation, immunotherapy, growth defects, malnutrition, malabsorption, immune dysregulation, anemia and the like or to provide a therapeutic control of tissue generation and degradation, and therapeutic modification of cell and tissue maintenance and blood cell homeostasis.

These diseases and conditions include but are not limited to cancer as hematological (e. g. leukemia, lymphoma, myeloma) or solid tumors (for example breast, prostate, liver,

bladder, lung, esophageal, stomach, colorectal, genitourinary, gastrointestinal, skin, pancreatic, brain, uterine, colon, head and neck, ovarian, melanoma, astrocytoma, small cell lung cancer, glioma, basal and squameous cell carcinoma, sarcomas as Kaposi's sarcoma and osteosarcoma), treatment of disorders involving T-cells such as aplastic anemia and DiGeorge syndrome, Graves'disease.

Leflunomide was previously found to inhibit HCMV replication in cell culture. Ocular herpes is the most common cause of infectious blindness in the developed world. There are about 50.000 cases per year in the US alone, of which 90% are recurrences of initial infections. Recurrences are treated with antivirals and corticosteroids. Cytomegalovirus, another herpes virus, is a common cause of retinal damage and blindness in patients with aids. The compounds of the present invention can be used alone or in combination with other antiviral compounds such as ganciclovir and foscarnet to treat such diseases.

The compounds of the present invention can further be used for diseases that are caused by protozoal infestations in humans and animals. Such veterinary and human pathogenic protozoas are preferably intracellular active parasites of the phylum Apicomplexa or Sarcomastigophora, especially Trypanosoma, Plasmodia, Leishmania, Babesia and Theileria, Cryptosporidia, Sacrocystida, Amoebia, Coccidia and Trichomonadia. These active substances or corresponding drugs are especially suitable for the treatment of Malaria tropica, caused by Plasmodium falciparum, Malaria tertiana, caused by Plasmodium vivax or Plasmodium ovale and for the treatment of Malaria quartana, caused by Plasmodium malariae. They are also suitable for the treatment of Toxoplasmosis, caused by Toxoplasma gondii, Coccidiosis, caused for instance by Isospora belli, intestinal Sarcosporidiosis, caused by Sarcocystis suihominis, dysentery caused by Entamoeba histolytica, Cryptosporidiosis, caused by Cryptosporidium parvum, Chargas'disease, caused by Trypanosoma cruzi, sleeping sickness, caused by Trypanosoma brucei rhodesiense or gambiense, the cutaneous and visceral as well as other forms of Leishmaniosis. They are also suitable for the treatment of animals infected by veterinary pathogenic protozoa, like Theileria parva, the pathogen causing bovine East coast fever, Trypanosoma congolense congolense or Trypanosoma vivax vivax, Trypanosoma brucei brucei, pathogens causing Nagana cattle disease in Africa, Trypanosoma brucei evansi causing Surra, Babesia bigemina, the pathogen causing Texas fever in cattle and buffalos,

Babesia bovis, the pathogen causing european bovine Babesiosis as well as Babesiosis in dogs, cats and sheep, Sarcocystis ovicanis and ovifelis pathogens causing Sarcocystiosis in sheep, cattle and pigs, Cryptosporidia, pathogens causing Cryptosporidioses in cattle and birds, Eimeria and Isospora species, pathogens causing Coccidiosis in rabbits, cattle, sheep, goats, pigs and birds, especially in chickens and turkeys. The use of the compounds of the present invention is preferred in particular for the treatment of Coccidiosis or Malaria infections, or for the preparation of a drug or feed stuff for the treatment of these diseases.

This treatment can be prophylactic or curative. In the treatment of malaria, the compounds of the present invention may be combined with other anti-malaria agents.

The compounds of the present invention can further be used for viral infections or other infections caused for instance by Pneumocystis carinii.

Examples 1. X-Ray structure determination Expression and Purification The cDNA encoding for an N-terminally truncated human DHODH (Met30- Arg396) was amplified by the polymerase chain reaction (PCR) from a human liver cDNA bank (Invitrogen, Groningen). The following primers were used to amplify the DHODH gene form the cDNA bank: DHODH-V: 5'-GGA ATT CCA TAT GGC CAC GGG AGA TGA GCG-3' DHODH-R: 5'-GCG CGG ATC CTC ACC TCC GAT GAT CTG C-3' The underlined sequence regions encode for the cutting sites of the restriction enzymes NdeI (DHODH-V) and BamHI (DHODH-R), respectively. The primers are designed such that subcloning using the NdeI and BamHI restriction sites into a pET-19b vector is possible. The amplified DNA bands were purified and isolated from an agarose gel (QIAquick PCR purification kit). The band showed the expected length of 1.2 kb. The isolated PCR fragment was subcloned into a TOPO vector (Invitrogen, Groningen) according to the protocol outlined in the TOPT TA Cloning Kit. The TOPO vector including the ligated PCR fragment was digested with the restriction enzymes NdeI and BamHI (New England Biolabs Inc. ) to produce sticky ends. Finally, the fragment was cloned into the NdeI/BamHI sites of a pET-19b vector (Novagen, Madison, WI). This

vector produced the human DHODH (Met30-Arg396) as an N-terminal ten histidine fusion protein (hisl0-hDHODH (Met30-Arg396) ). The vector was transformed into chemical competent E. coli BL21 (DE3) Gold cells (Stratagene, LaJolla, CA). Cells were stored as glycerol stocks at-80°C until further use.

100 ml LB-medium in 250 ml flasks containing 100 tL freshly prepared ampicilline were inoculated with BL21 (DE3) Gold cells hosting the pET-19b/hDHODH (Met30-Arg396) construct. Cells were grown overnight at 25°C and constantly vortexed with 150 rpm.

For the expression cultures four 2 L flasks each were filled with 800 mL rich medium (LB) containing 800 pL ampicilline. The flasks were inoculated with 40 mL of overnight culture and were grown to an optical density O. D. goo of 0.6-0. 8 at 25 °C. The cells were induced with 80 p. L of a 1 M isopropyl-13-D-thiogalactoside (IPTG) stock solution and grown for another 20 h at 25°C.

The cells were harvested by centrifugation for 15 min in a JA-10 Beckmann rotor at 5000 rpm at 4°C. The cell pellet was stored until further use at-20°C.

The pellets of 4 x 800 mL expression were thawed on ice and resuspended in 100 mL lysisbuffer containing 50 mM HEPES at pH 7.7, 300 mM NaCI, 10% glycerol, 10% bugbuster (Novagen, lOx), two tablets of protease-inhibitor mix (Complete Tabletes EDTA-free, Roche) and 1% triton X-100. The cell suspension was incubated under gentle rocking for 20 min at room temperature.

Cell lysis was performed via ultra sonification using a Branson sonotrode. The chosen parameters for sonification were the following: amplitude : 60% duration: 3 x 3 min maximal allowed temperature: 37°C pulse duration : 0. 5 sec duty cycle: 0.1 sec The resulting suspension was centrifuged in a JA-25.50 rotor (Beckmann) at 25.000 rpm for 1 hour at 4°C.

The supernatant was loaded onto a Ni-NTA-column (resin was from Quiagen, column adapter from Pharmacia). The column had a bed volume of 3 mL and was

equilibrated with 5 column volumes (CV) of starting buffer (50 mM HEPES pH 7.7 ; 300 mM NaCI ; 10% glycerol and 10 mM imidazole). The sample was loaded with a flow rate of 1 mL/min at 4°C using a BioRad Econopump. Then the column was mounted on a BioRad BioLogic-LP chromatography system and washed with 5-10 CVs of 50 mM HEPES pH 7.7, 300 mM NaCI, 10% glycerol, 10 mM imidazole and 10 mM N, N- dimethylundecylamin-N-oxide (C11DAO) at a rate of 1 mL/min. Another more stringent washing step was performed by applying step gradients consisting of the above washing buffer containing 20 mM and 50 mM imidazole, respectively. At this point, pure DHODH was eluted with 50 mM HEPES pH 7.7, 300 mM NaCI, 10% glycerol, 200 mM imidazole and 10 mM N, N-dimethylundecylamin-N-oxide. Elution was carried out with a flow rate of 0.5 mL/min and the eluate was collected in 4 mL fractions. Fractions containing hDHODH (Met30-Arg396) are characterized by a bright yellow colour and showed full activity in an in vitro assay (as described above/below).

Fractions containing hDHODH were combined (approx. 10 mL) and dialysed against 3 L of buffer containing 50 mM HEPES pH 7.7, 400 mM NaCI, 30% glycerol, 1 mM EDTA and 10 mM N, N-dimethylundecylamin-N-oxide overnight at 4°C. The dialysed protein sample was concentrated to a final concentration of 20 mg/mL using an Ultrafree 4/YM-30 device from Millipore. During the concentrating procedure the temperature was kept at 4° C. The protein concentration was determined spectrometrically. The His-tag was not removed for further studies.

Finally, aliquots of 50 pL were flash frozen in liquid nitrogen and stored at -80°C until further use.

Crystallization and data collection Human his10-hDHODH (Met30-Arg396) was co-crystallized with compound 1 and compound 2 at 20°C using the hanging-drop vapour diffusion method. Drops were formed by mixing equal amounts of 20 mg/ml protein in 50 mM HEPES pH 7.7, 400 mM NaCI, 30% glycerol, 1 mM EDTA and 10 mM N, N-dimethylundecylamin- N-oxide (C11 DAO) with a precipitant solution of 0.1 M acetate pH 4.6-5. 0,40 mM C11 DAO, 20.8 mM N, N-dimethyldecylamine-N-oxide (DDAO), 2 mM dihydroorotate (DHO), 1.8-2. 4 M ammonium sulfate, 1 mM compound 1 or 2.

The hanging drops were incubated against 0.5 mL reservoir of 0.1 M acetate pH

4.8, 2.4-2. 6 M ammonium sulfate and 30% glycerol. The crystallization conditions were screened by variation of pH versus ammonium sulfate concentration using a small grid screen (see figure 5): [ammonium sulfate]/M 1.8 2.0 2.2 2.4 pH4. 6 A1 A2 A3 A4 pH 4. 0iE E B4 pH 5. ci C2 C3 C4 Figure 5: Minimal grid screen used for crystallization trails.

The same procedure was applied to obtain single crystals of DHODH (Met30- Arg396) in complex with compounds 3,4, 5,6, 7,8, 9 and 10. Compounds 5 and 6 were synthesized as racemic mixtures due to the presence of a stereo center at the five membered ring. The racemic mixtures were used for crystallization experiments..

Crystals usually appeared as small cubes within three days. They usually reached a full size of 0.2 x 0.2 x 0.2 mm within three to four weeks. The protein crystallized in the space group P3221. Crystals were harvested with pre-mounted loops of size 0.5 mm (Hampton Research) and were flash frozen directly in the cryo stream of the measurement device.

Data were collected at the beamline BW6 at the DESY Hamburg on a MAR-CCD camera. A total of 120 frames (0. 5° each) were collected from a human DHODH (Met30- Arg396) crystal co-crystallized with compound 1. For the crystal cocrystallized with compound 2 a total of 85 frames (1° each) was recorded. The crystals were maintained at a temperature of 100 K during data collection. The indexing and integration of the reflection intensities were performed with the program MOSFLM (Collaborative Computational

Project, Number 4 (1994). Acta Cryst. D50,760-763.). Data were scaled and merged with SCALA and reduced to structure factor amplitudes with TRUNCATE, both from the CCP4 program suite (Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50, 760-763. ). At this stage 5% and 10% (the"test set") of unique reflections were flagged for cross validation to calculate the free R-factor (Rfree) during the refinement process later on for compound 1 and compound 2, respectively. The remaining 95% and 90% of the reflections constituted the"working set"for calculation of the R-factor (R), respectively.

The statistics of data collection are shown in table 1 and table 2.

Table 1: Crystal & Data collection statistics for compound 1 A. Crystal data Spacegroup P3221 Cell dimensions (A) a = 90. 69 b = 90.69 c = 123. 22 Molecules/asymmetric unit 1 Matthews'constant (Vm) (A3/Da) 4.1 Maximum resolution (A) 2. 35 B. Data Collection X-Ray source DESY BW6 Wavelength (A) 1.05 Total/unique reflections 91431/24977 Completeness (%) 98.2 (99.0) I/sigma 23.9 (6.5) Rmerge (%) 5.7 (20.2) Table 2: Crystal & Data collection statistics for compound 2 A. Crystal data Spacegroup P3221 Cell dimensions (A) a = 90.65 b = 90.65 c = 123. 07 Molecules/asymmetric unit 1 Matthews'constant (Vm) (A3/Da) 4.1 Maximum resolution (A) 2.4 B. Data Collection X-Ray source DESY BW6

Wavelength (A) 1.05 Total/unique reflections 101935/22253 Completeness (%) 95. 8 (97.1) I/sigma 14.6 (3.8) Rmerge (%) 9.1 (38.1) Datasets for the crystals of human DHODH (Met30-Arg396) co-crystallized with compounds 3,4, 6,7, 8,9 and 10 were also collected at the beamline BW6 at the DESY Hamburg on a MAR-CCD camera. Co-crystals with compound 5 were recorded at an in house generator using CuKa radiation and a MAR-dtb image plate.

A total of 55 frames, 65 frames, 96 frames, 62 frames, 120 frames, 60 frames, 100 frames and 100 frames (1° each) were collected from human DHODH (Met30-Arg396) crystals co-crystallized with compound 3,4, 5,6, 7,8, 9 and 10 respectively. The crystals were maintained at a temperature of 100 K during data collection. The indexing and integration of the reflection intensities were performed with the program MOSFLM (Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50,760-763.). Data were scaled and merged with SCALA and reduced to structure factor amplitudes with TRUNCATE, both from the CCP4 program suite (Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50,760-763.). At this stage 5% or 10% (the"test set") of unique reflections were flagged for cross validation to calculate the free R-factor (Rfree) during the refinement process. The remaining 95% or 90% of the reflections constituted the"working set"for calculation of the R-factor (R), respectively. The statistics of data collection are shown in tables 5 to 12, respectively.

Table 5: Crystal & Data collection statistics for compound 3 A. Crystal data Spacegroup P3221 Cell dimensions (A) a = 90.43 b = 90.43 c = 123. 00 Molecules/asymmetric unit 1 Matthews'constant (Vm) (A3/Da) 4.1 Maximum resolution (A) 1.95 B. Data Collection X-Ray source DESY BW6 Wavelength (A) 1.05 Total/unique reflections 142628/42908 Completeness (%) 99. 8/99.9 I/sigma 12.6/3. 4 Rmerge (%) 8.2/38. 3 Table 6: Crystal & Data collection statistics compound 4 A. Crystal data Spacegroup P3221 Cell dimensions (A) a = 90.65 b = 90.65 c = 123. 21 Molecules/asymmetric unit 1 Matthews'constant (Vm) (A3/Da) 4.1 Maximum resolution (A) 2.15 B. Data Collection X-Ray source DESY BW6 Wavelength (A) 1.05 Total/unique reflections 124056/32175 Completeness (%) 99. 2/99.0 I/sigma 14.7/5. 7 Rmerge (%) 7.1/24. 8 Table 7: Crystal & Data collection statistics for compound 5 A. Crystal data Spacegroup P3221 Cell dimensions (A) a = 90.30 b = 90.30 c = 123. 09 Molecules/asymmetric unit 1 Matthews'constant (Vm) (A3/Da) 4.1 Maximum resolution (A) 2.2 B. Data Collection X-Ray source CuKa Wavelength (A) 1.54 Total/unique reflections 171127/30057 Completeness (%) 99. 9 (99.9) I/sigma 4.0/1. 9 Rmerge (%) 15.4/43. 5

Table 8: Crystal & Data collection statistics for compound 6 A. Crystal data Spacegroup P3221 Cell dimensions (A) a = 90.44 b = 90.44 c = 123. 20 Molecules/asymmetric unit 1 Matthews'constant (Vm) (A3/Da) 4.1 Maximum resolution (A) 1.9 B. Data Collection X-Ray source DESY BW 6 Wavelength (A) 1.05 Total/unique reflections 173775/46257 Completeness (%) 99. 4/99.9 I/sigma 13.8/2. 8 Rmerge (%) 8.5/46. 0 Table 9: Crystal & Data collection statistics for compound 7 A. Crystal data Spacegroup P3z21 Cell dimensions (A) a = 90.74 b = 90.74 c = 122. 88 Molecules/asymmetric unit 1 Matthews'constant (Vm) (A3/Da) 4.1 Maximum resolution (A) 1.9 B. Data Collection X-Ray source DESY BW 6 Wavelength (Å) 1.05 Total/unique reflections 341319/46198 Completeness (%) 98. 6/99.7 I/sigma 23.5/5. 1 Rmerge (%) 8. 2/21. 8

Table 10: Crystal & Data collection statistics for compound 8 A. Crystal data Spacegroup P3221 Cell dimensions (A) a = 90.56 b = 90.56 c = 123. 06 Molecules/asymmetric unit 1 Matthews'constant (Vm) (A3/Da) 4.1 Maximum resolution (A) 1.8 B. Data Collection X-Ray source DESY BW 6 Wavelength (A) 1.05 Total/unique reflections 190208/53993 Completeness (%) 98. 8/96.7 1/sigma 16.7/2. 9 Rmerge (%) 6. 3/38. 3

Table 11: Crystal & Data collection statistics for compound 9 A. Crystal data Spacegroup P3221 Cell dimensions (A) a = 90.29 b = 90.29 c = 122. 69 Molecules/asymmetric unit 1 Matthews'constant (Vm) (A3/Da) 4.1 Maximum resolution (A) 2.0 B. Data Collection X-Ray source DESY BW 6 Wavelength (A) 1.05 Total/unique reflections 103711/39080 Completeness (%) 98. 6/99.0 I/sigma 14.1/3. 9 Rmerge (%) 6.5/24. 8 Table 12: Crystal & Data collection statistics for compound 10 A. Crystal data Spacegroup P3221 Cell dimensions (A) a = 90.75 b = 90.75 c = 122. 71 Molecules/asymmetric unit 1 Matthews'constant (Vm) (A3/Da) 4.1 Maximum resolution (A) 1.8 B. Data Collection X-Ray source DESY BW 6 Wavelength (A) 1.05 Total/unique reflections 326425/54728 Completeness (%) 99.9/100 I/sigma 27.5/6. 0 Rmerge (%) 6.0 30.6

Structure determina

tion and refinement of DHODH/compound 1 complex The structure for the human DHODH (Met30-Arg396) in complex with compound 1 was solved using the method of molecular replacement (MR). The free accessible pdb entry lD3G. pdb was used as a search model. The ligands brequinar and DDQ as well as all of the water molecules were removed prior to the MR search. The search model included the polypeptide chain of hDHODH (Met30-Arg396), one molecule of orotate, one molecule of the cofactor flavinmononucleotide (FMN) and one acetate molecule which was present under the crystallization conditions. A standard rotational and translational molecular replacement search at 3.5 A was performed using the program molrep (Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50,760-763.). Solutions for both the rotational and translational search were well above the next ranking solutions. The MR resulted in an R-factor of 35.6 % and a correlation coefficient of 69.4 % for compound 1 complex.

In a first round of refinement the MR model was subjected to rigid body refinement and a slow cooling simulated annealing protocol using a maximum likelihood target to remove model bias (Accelrys Inc. CNX program suite, CNX2002). Additionally, an individual b-factor refinement was carried out using standard CNX protocols. Finally, SIGMAA weighted 2Fo-Fc and Fo-Fc electron density maps were calculated and displayed together with the protein model in the program O (DatOno AB; Jones, T. A. , Zou, J. Y., Cowan, S. W. & Kjelgaard, M. (1991). Acta Cryst. A47,110-119.). The resulting experimental electron density was so excellent that the conformation of compound 1 could be interpreted unambiguously.

A pdb file for compound 1 was created using the program MOE (Chemical Computing Group Inc. , MOE 2002.02). After energy minimization the compound was built into the electron density manually. Topology and parameter files for compound 1 were created using the program Xplo2d (Uppsala Software Factory; Kleywegt, G. M. (1997) J. Mol. Biol.

273, 371-376). After an additional round of model building and water picking using CNX another complete round of refinement was performed. The final model included the DHODH (Met30-Arg396) protein, the cofactor flavinmononucleotide (FMN), one orotate molecule (ORO), one acetate molecule (ACT), two sulfate ions (S04), one molecule of compound 1 (INH) and 153 water molecules (TIP) (see figure 2). The model is well refined and has very good geometry. The refinement process which included data from

o 12.0-2. 35 A resulted in an R-factor of 18. 5 % and a free R-factor of 21. 7%. With the exception of glycine residues, 92.4 % (278) of the residues are located in the most favoured region of the ramachandran plot and 7.6 % (22) cluster in the additional allowed regions. Table 13 summarizes the refinement statistics for the inhibitor compound 1 in complex with human DHODH. Values in parentheses give the R-factor and Rfree-factors, respectively, for the last resolution bin ranging from 2.50 to 2.35.

The N-terminal His tag could not be detected in the electron density map.

Table 13: Refinement Statistics for DHODH/compound 1 complex R-factor (%) 18.5 (19.6) Rfree 21.7 (24.2) RMS deviation from ideal values bond length (A) 0.006 Bond angle (°) 1.2 Dihedral angles (°) 21. 4 Improper angles (°) 0. 83 Structure determination and refinement of DHODH/compound 2 complex The structure for the human DHODH (Met30-Arg396) in complex with compound 2 was solved using the method of molecular replacement (MR). The free accessible pdb entry lD3G. pdb was used as a search model. The ligands brequinar and DDQ as well as all of the water molecules were removed prior to the MR search. The search model included the polypeptide chain of hDHODH (Met30-Arg396), one molecule of orotate, one molecule of the cofactor flavinmononucleotide (FMN) and one acetate molecule which was present under the crystallization conditions. A standard rotational and translational molecular replacement search at 3.5 A was performed using the program molrep (Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50,760-763.). Solutions for both the rotational and translational search were well above the next ranking solutions. The MR

resulted in an R-factor of 33.8 % and a correlation coefficient of 68.2 % for the DHODH/compound 2 complex.

In a first round of refinement the MR model was subjected to rigid body refinement and a slow cooling simulated annealing protocol using a maximum likelihood target to remove model bias (Accelrys Inc. CNX program suite, CNX2002). Additionally, an individual b-factor refinement was carried out using standard CNX-protocols. Finally a SIGMAA weighted 2Fo-Fc and Fo-Fc electron density maps were calculated and displayed together with the protein model in the program O (DatOno AB ; Jones, T. A. , Zou, J. Y., Cowan, S. W. & Kjelgaard, M. (1991). Acta Cryst. A47,110-119.). The resulting experimental electron density was so excellent that the conformation of the inhibitor compound 2 could be interpreted unambiguously. The electron density around the five- membered ring carrying the carboxy group clearly showed the presence of two alternative conformations of compound 2. In one conformation (conformation A) the carboxy group interacts with residues Gln 47 and Arg 136, whereas in the second conformation (conformation B) the interaction involves residues His 56 and Tyr 356 (see above). For each conformation a separate DHODH/compound 2 complex was subjected to refinement.

Pdb files for the compound 2 in conformation A and B were created using the program MOE (Chemical Computing Group Inc. , MOE 2002.02). Both compounds were energy minimized and built into the electron density manually. Topology and parameter files for compound 2 were created using the program Xplo2d (Uppsala Software Factory; Kleywegt, G. M. (1997) J. Mol. Biol. , 273,371-376). After an additional round of model building and water picking using CNX, another complete round of refinement was performed. The final model included the human DHODH (Met30-Arg396) protein, the cofactor flavinmononucleotide (FMN), one orotate molecule (ORO), one acetate molecule (ACT), four sulfate ions (S04), one molecule of compound 2 (INH) either in conformation A or conformation B and 250 water molecules (TIP) (see figures 3 and 4). The models are well refined and show very good geometry. The refinement process which included data 0 from 12.0-2. 4 A resulted in an R-factor of 17.5 % and a free R-factor of 21.1% for conformation A complex and an R-factor of 17.6 % and a free R-factor of 21.6% for conformation B complex, respectively. With the exception of glycine residues, 91.7 % (276) of the residues are located in the most favoured region of the ramachandran plot and 8.3 % (24) cluster in the additional allowed regions.. Table 14 summarizes the refinement statistics for compound 2 in complex with human DHODH. Values in parentheses give the

R-factor and Rfree-factors, respectively, for the last resolution bin ranging from 2.55 to 2.40.

Table 14: Refinement Statistics for DHODH/compound 2 complex Conformation A Conformation B R-factor (%) 17. 5 (19.6) 17.6 (19.4) Rfree 21.1 (23.6) 21.6 (23.2) RMS deviation from ideal values bond length (A) 0.005 0.005 Bond angle (°) 1.2 1.2 Dihedral angles (°) 21. 3 21.3 Improper angles (°) 0. 81 0. 81 Structure determination and refinement of DHODH/compound 3 complex The structure for the human DHODH (Met30-Arg396) in complex with compound 3 was solved using the method of molecular replacement (MR). The free accessible pdb entry lD3G. pdb was used as a search model. The ligands brequinar and DDQ as well as all of the water molecules were removed prior to the MR search. The search model included the polypeptide chain of hDHODH (Met30-Arg396), one molecule of orotate, one molecule of the cofactor flavinmononucleotide (FMN) and one acetate molecule which was present under the crystallization conditions. A standard rotational and translational molecular replacement search at 3.0 A was performed using the program molrep (Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50,760-763.). Solutions for both the rotational and translational search were well above the next ranking solutions. The MR resulted in an R-factor of 33.9 % and a correlation coefficient of 72.5 for the DHODH/compound 3 complex.

In a first round of refinement the MR model was subjected to rigid body refinement and a slow cooling simulated annealing protocol using a maximum likelihood target to remove model bias (Accelrys Inc. CNX program suite, CNX2002). Additionally, an individual b-factor refinement was carried out using standard CNX-protocols. Finally SIGMAA weighted 2Fo-Fc and Fo-Fc electron density maps were calculated and displayed

together with the protein model in the program O (DatOno AB; Jones, T. A. , Zou, J. Y., Cowan, S. W. & Kjelgaard, M. (1991). Acta Cryst. A47,110-119.). The resulting experimental electron density was so excellent that the conformation of the inhibitor compound 3 could be interpreted unambiguously. The electron density around the five- membered ring carrying the carboxy group clearly showed the presence of two alternative conformations of compound 3. In one conformation (conformation A) the carboxy group interacts with residues Gln 47 and Arg 136, whereas in the second conformation (conformation B) the interaction involves residues His 56 and Tyr 356 (see above). For each conformation a separate DHODH/compound 3 complex was subjected to refinement.

The pdb files for the compound 3 in conformation A and B were created using the program MOE (Chemical Computing Group Inc. , MOE 2002.02). Both compounds were energy minimized and built into the electron density manually. Topology and parameter files for compound 3 were created using the program Xplo2d (Uppsala Software Factory; Kleywegt, G. M. (1997) J. Mol. Biol. , 273,371-376). After an additional round of model building and water picking using CNX, another complete round of refinement was performed. The final model included the human DHODH (Met30-Arg396) protein, the cofactor flavinmononucleotide (FMN), one orotate molecule (ORO), two acetate molecules (ACT), two sulfate ions (S04), one molecule of compound 3 (INH) either in conformation A or conformation B and 263 water molecules (WAT). Residues which are missing the coordinate file due to very poor electron density are listed in the header of the pdb files.

The models are well refined and show very good geometry. The refinement process which included data from 19.9-1. 95 A resulted in an R-factor of 18.5 % and a free R- factor of 20.3% for the complex in conformation A and an R-factor of 18.5 % and a free R- factor of 20.3% for the complex in conformation B, respectively. The almost identical R- factors indicate that non of the conformers A and B represent a preferred conformation.

Except for non-glycine and non-proline residues 91.6% are located in the most favoured region of the ramachandran plot and 8 % cluster in the additional allowed regions. There are no residues in the disallowed region. Table 15 summarizes the refinement statistics for compound 3 in complex with human DHODH. Values in parentheses give the R-factor and Rfree-factors, respectively, for the last resolution bin ranging from 2.07 to 1.95.

Table 15: Refinement Statistics for DHODH/compound 3 complex conformation A conformation B R-factor (%) 18. 5 (20.6) 18.5 (20.6) Rfree 20.3 (23.5) 20.2 (23.6) RMS deviation from ideal values bond length (A) 0.005 0.005 Bond angle (°) 1.2 1.2 Dihedral angles 21. 2 21.2 Improper angles (°) 0. 81 0. 81 Structure determination and refinement of DHODH/compound 4 complex The structure for the human DHODH (Met30-Arg396) in complex with compound 4 was solved using the method of molecular replacement (MR). The free accessible pdb entry lD3G. pdb was used as a search model. The ligands brequinar and DDQ as well as all of the water molecules were removed prior to the MR search. The search model included the polypeptide chain of hDHODH (Met30-Arg396), one molecule of orotate, one molecule of the cofactor flavinmononucleotide (FMN) and one acetate molecule which was present under the crystallization conditions. A standard rotational and translational molecular replacement search at 3.0 A was performed using the program molrep (Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50,760-763.). Solutions for both the rotational and translational search were well above the next ranking solutions. The MR resulted in an R-factor of 34.6 % and a correlation coefficient of 71.1 for the DHODH/compound 4 complex.

In a first round of refinement the MR model was subjected to rigid body refinement and a slow cooling simulated annealing protocol using a maximum likelihood target to remove model bias (Accelrys Inc. CNX program suite, CNX2002). Additionally, an individual b-factor refinement was carried out using standard CNX-protocols. Finally SIGMAA weighted 2Fo-Fc and Fo-Fc electron density maps were calculated and displayed together with the protein model in the program O (DatOno AB; Jones, T. A. , Zou, J. Y., Cowan, S. W. & Kjelgaard, M. (1991). Acta Cryst. A47,110-119.). The resulting experimental electron density was so excellent that the conformation of the inhibitor

compound 4 could be interpreted unambiguously. The electron density around the five- membered ring carrying the carboxy group clearly showed the carboxy group in contact with residues His 56 and Tyr 356 in non-brequinar-like conformation.

A pdb file for compound 4 was created using the program MOE (Chemical Computing Group Inc. , MOE 2002.02). After energy minimization the compound was built into the electron density manually. Topology and parameter files for compound 4 were created using the program Xplo2d (Uppsala Software Factory; Kleywegt, G. M. (1997) J. Mol. Biol. 273,371-376). After an additional round of model building and water picking using CNX another complete round of refinement was performed. The final model included the DHODH (Met30-Arg396) protein, the cofactor flavinmononucleotide (FMN), one orotate molecule (ORO), one acetate molecule (ACT), one sulfate ion (S04), one molecule of compound 4 (INH) and 192 water molecules (TIP).

The model is well refined and shows very good stereochemical geometry. The 0 refinement process which included data from 19.9-2. 15 A resulted in an R-factor of 20.1 % and a free R-factor of 22.1%. Except for non-glycine and non-proline residues 91.6% of the residues are located in the most favoured region of the ramachandran plot and 8 % and 0.3 % cluster in the additional allowed or generously allowed regions, respectively. There are no residues in the disallowed region. Table 16 summarizes the refinement statistics for compound 4 in complex with human DHODH. Values in parentheses give the R-factor and Rfree-factors, respectively, for the last resolution bin ranging from 2.28 to 2.15.

Table 16: Refinement Statistics for DHODH/compound 4 complex R-factor (%) 20.1 (19.1) Rfree 22.1 (20.9) RMS deviation from ideal values bond length (A) 0.005 Bond angle (°) 1.2 Dihedral angles (°) 21. 5 Improper angles (°) 0. 80 Structure determination and refinement of DHODH/compound 5 complex

The structure for the human DHODH (Met30-Arg396) in complex with compound 5 was solved using the method of molecular replacement (MR). The free accessible pdb entry lD3G. pdb was used as a search model. The ligands brequinar and DDQ as well as all of the water molecules were removed prior to the MR search. The search model included the polypeptide chain of hDHODH (Met30-Arg396), one molecule of orotate, one molecule of the cofactor flavinmononucleotide (FMN) and one acetate molecule which was present under the crystallization conditions. A standard rotational and translational molecular replacement search at 3.0 A was performed using the program molrep (Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50,760-763.). Solutions for both the rotational and translational search were well above the next ranking solutions. The MR resulted in an R-factor of 33.8 % and a correlation coefficient of 71.5 for the DHODH/compound 5 complex.

In a first round of refinement the MR model was subjected to rigid body refinement and a slow cooling simulated annealing. protocol using a maximum likelihood target to remove model bias (Accelrys Inc. CNX program suite, CNX2002). Additionally, an individual b-factor refinement was carried out using standard CNX-protocols. Finally SIGMAA weighted 2Fo-Fc and Fo-Fc electron density maps were calculated and displayed together with the protein model in the program O (DatOno AB; Jones, T. A. , Zou, J. Y., Cowan, S. W. & Kjelgaard, M. (1991). Acta Cryst. A47,110-119.). The resulting experimental electron density was so excellent that the conformation of the inhibitor compound 5 could be interpreted unambiguously. The electron density around the five- membered ring carrying the carboxy group clearly showed the carboxy group in contact with residues His 56 and Tyr 356 in non-brequinar-like conformation. Interestingly the protein's active site discriminates between the S-and R-enantiomere. Inspection of the corresponding electron density unequivocally shows the presences of the R-enantiomere only.

A pdb file for compound 5 was created using the program MOE (Chemical Computing Group Inc., MOE 2002.02). After energy minimization the compound was built into the electron density manually. Topology and parameter files for compound 5 were created using the program Xplo2d (Uppsala Software Factory; Kleywegt, G. M. (1997) J. Mol. Biol. 273,371-376). After an additional round of model building and water picking using CNX another complete round of refinement was performed. The final model included the DHODH (Met30-Arg396) protein, the cofactor flavinmononucleotide (FMN),

one orotate molecule (ORO), one acetate molecule (ACT), two sulfate ions (S04), one molecule of compound 5 (INH) and 287 water molecules (TIP).

The model is well refined and shows very good stereochemical geometry. The refinement 0 process which included data from 25.5-2. 2 A resulted in an R-factor of 18.3 % and a free R-factor of 20.9 %. Except for non-glycine and non-proline residues 92.6 % of the residues are located in the most favoured region of the ramachandran plot and 7 % and 0.3 % cluster in the additional allowed or generously allowed regions, respectively. There are no residues in the disallowed region. Table 17 summarizes the refinement statistics for compound 5 in complex with human DHODH. Values in parentheses give the R-factor and Rfree-factors, respectively, for the last resolution bin ranging from 2.34 to 2.2.

Table 17: Refinement Statistics for DHODH/compound 5 complex R-factor (%) 18. 3 (19.4) Rfree 20.9 (22.0) RMS deviation from ideal values bond length (A) 0. 005 Bond angle (°) 1. 2 Dihedral angles (°) 21. 3 Improper angles (°) 0. 83 Structure determination and refinement of DHODH/compound 6 complex The structure for the human DHODH (Met30-Arg396) in complex with compound 6 was solved using the method of molecular replacement (MR). The free accessible pdb entry lD3G. pdb was used as a search model. The ligands brequinar and DDQ as well as all of the water molecules were removed prior to the MR search. The search model included the polypeptide chain of hDHODH (Met30-Arg396), one molecule of orotate, one molecule of the cofactor flavinmononucleotide (FMN) and one acetate molecule which was present under the crystallization conditions. A standard rotational and translational molecular replacement search at 3.0 A was performed using the program molrep (Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50,760-763.). Solutions for both the rotational and translational search were well above the next ranking solutions. The MR

resulted in an R-factor of 32.7 % and a correlation coefficient of 74.5 for the DHODH/compound 6 complex.

In a first round of refinement the MR model was subjected to rigid body refinement and a slow cooling simulated annealing protocol using a maximum likelihood target to remove model bias (Accelrys Inc. CNX program suite, CNX2002). Additionally, an individual b-factor refinement was carried out using standard CNX-protocols. Finally SIGMAA weighted 2Fo-Fc and Fo-Fc electron density maps were calculated and displayed together with the protein model in the program O (DatOno AB; Jones, T. A. , Zou, J. Y., Cowan, S. W. & Kjelgaard, M. (1991). Acta Cryst. A47,110-119.). The resulting experimental electron density was so excellent that the conformation of the inhibitor compound 6 could be interpreted unambiguously. The electron density around the five- membered ring carrying the carboxy group clearly showed that the inhibitor molecule adopts both the brequinar and non-brequinar binding mode. The carboxy group is in contact with both anion binding sites. Interestingly the protein's active site discriminates between the S-and R-enantiomere. Inspection of the corresponding electron density unequivocally shows the presences of the R-enantiomere only.

A pdb file for compound 6 was created using the program MOE (Chemical Computing Group Inc. , MOE 2002.02). After energy minimization the compound was built into the electron density manually. Topology and parameter files for compound 6 were created using the program Xplo2d (Uppsala Software Factory; Kleywegt, G. M. (1997) J. Mol. Biol. 273,371-376). After an additional round of model building and water picking using CNX another complete round of refinement was performed. The final model included the DHODH (Met30-Arg396) protein, the cofactor flavinmononucleotide (FMN), one orotate molecule (ORO), one acetate molecule (ACT), one sulfate ion (S04), one molecule of compound 6 (INH) and 312 water molecules (TIP).

The models are well refined and show very good geometry. The refinement process which 0 included data from 19.3-1. 9 A resulted in an R-factor of 18.5 % and a free R-factor of 20.8% for the complex in conformation A and an R-factor of 18.5 % and a free R-factor of 20.7% for the complex in conformation B, respectively. The almost identical R-factors indicate that non of the conformers A and B represent a preferred conformation. Except for non-glycine and non-proline residues 92.6% are located in the most favoured region of the ramachandran plot and 7.4 % cluster in the additional allowed regions. There are no residues in the disallowed region. Table 18 summarizes the refinement statistics for compound 6 in complex with human DHODH. Values in parentheses give the R-factor and Rfree-factors, respectively, for the last resolution bin ranging from 2.02 to 1.9.

Table 18: Refinement Statistics for DHODH/compound 6 complex conformation A conformation B R-factor (%) 18.5 (21.1) 18.5 (21.2) Rfree 20.8 (21.5) 20.7 (21.6) RMS deviation from ideal values bond length (A) 0.005 0.005 Bond angle (°) 1.2 1.2 Dihedral angles (°) 21.3 21.3 Improper angles (') 0. 79 0. 79 Structure determination and refinement of DHODH/compound 7 complex The structure for the human DHODH (Met30-Arg396) in complex with compound 7 was solved using the method of molecular replacement (MR). The free accessible pdb entry lD3G. pdb was used as a search model. The ligands brequinar and DDQ as well as all of the water molecules were removed prior to the MR search. The search model included the polypeptide chain of hDHODH (Met30-Arg396), one molecule of orotate, one molecule of the cofactor flavinmononucleotide (FMN) and one acetate molecule which was present under the crystallization conditions. A standard rotational and translational molecular replacement search at 3.0 A was performed using the program molrep (Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50,760-763.). Solutions for both the rotational and translational search were well above the next ranking solutions. The MR resulted in an R-factor of 32.7 % and a correlation coefficient of 73.9 for the DHODH/compound 7 complex.

In a first round of refinement the MR model was subjected to rigid body refinement and a slow cooling simulated annealing protocol using a maximum likelihood target to

remove model bias (Accelrys Inc. CNX program suite, CNX2002). Additionally, an individual b-factor refinement was carried out using standard CNX-protocols. Finally SIGMAA weighted 2Fo-Fc and Fo-Fc electron density maps were calculated and displayed together with the protein model in the program O (DatOno AB; Jones, T. A. , Zou, J. Y., Cowan, S. W. & Kjelgaard, M. (1991). Acta Cryst. A47,110-119.). The resulting experimental electron density was so excellent that the conformation of the inhibitor compound 7 could be interpreted unambiguously. The electron density around the five- membered ring carrying the carboxy group clearly showed the carboxy group in contact with residues His 56 and Tyr 356 in non-brequinar-like conformation addressing subsite 3.

In compound 7 a hydroxy group at 3-position at the five membered ring was introduced creating a stereo center at this position. The racemic mixture was used for crystallization experiments. Analysis of the electron density reveals the presence of both enantiomeres.

Interestingly only the R-enantiomere is able to form additional contacts to the side chains of residues Gln47 and Argl36 and to a conserved water molecule. As is clearly shown from experimental data compound 7 is able to form interactions with both subsite 2 and subsite 3 at the same time. This feature clearly discriminates this compound class from, for example, compounds 2,6 and 10 which can address both binding sites utilizing alternative conformations but not at the same time.

A pdb file for compound 7 was created using the program MOE (Chemical Computing Group Inc. , MOE 2002.02). After energy minimization the compound was built into the electron density manually. Topology and parameter files for compound 7 were created using the program Xplo2d (Uppsala Software Factory; Kleywegt, G. M. (1997) J. Mol. Biol. 273,371-376). After an additional round of model building and water picking using CNX another complete round of refinement was performed. The final model included the DHODH (Met30-Arg396) protein, the cofactor flavinmononucleotide (FMN), one orotate molecule (ORO), one acetate molecule (ACT), two sulfate ions (S04), one molecule of compound 7 (INH) and 229 water molecules (TIP).

The model is well refined and shows very good stereochemical geometry. The refinement 0 process which included data from 17.0-2. 0 A resulted in an R-factor of 17.5 % and a free R-factor of 20.4 % for the R-form and S-form. Except for non-glycine and non-proline residues 92.3 % of the residues are located in the most favoured region of the ramachandran plot and 7.7 % cluster in the additional allowed regions. There are no residues in the disallowed region. Table 19 summarizes the refinement statistics for

compound 7 in complex with human DHODH. Values in parentheses give the R-factor and Rfree-factors, respectively, for the last resolution bin ranging from 2.13 to 2.0.

Table 19: Refinement Statistics for DHODH/compound 7 complex R-form S-form R-factor (%) 17. 5 (17.3) 17.5 (17.3) Rf, ee 20.4 (21.4) 20.4 (21.4) RMS deviation from ideal values bond length (A) 0.005 0. 008 Bond angle (°) 1.2 1.2 Dihedral angles 21. 2 21.2 Improper angles (°) 0. 82 0. 81 Structure determination and refinement of DHODH/compound 8 complex The structure for the human DHODH (Met30-Arg396) in complex with compound 8 was solved using the method of molecular replacement (MR). The free accessible pdb entry lD3G. pdb was used as a search model. The ligands brequinar and DDQ as well as all of the water molecules were removed prior to the MR search. The search model included the polypeptide chain of hDHODH (Met30-Arg396), one molecule of orotate, one molecule of the cofactor flavinmononucleotide (FMN) and one acetate molecule which was present under the crystallization conditions. A standard rotational and translational molecular replacement search at 3.0 A was performed using the program molrep (Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50,760-763.). Solutions for both the rotational and translational search were well above the next ranking solutions. The MR resulted in an R-factor of 33.3 % and a correlation coefficient of 73.9 for the DHODH/compound 8 complex.

In a first round of refinement the MR model was subjected to rigid body refinement and a slow cooling simulated annealing protocol using a maximum likelihood target to remove model bias (Accelrys Inc. CNX program suite, CNX2002). Additionally, an individual b-factor refinement was carried out using standard CNX-protocols. Finally SIGMAA weighted 2Fo-Fc and Fo-Fc electron density maps were calculated and displayed

together with the protein model in the program O (DatOno AB; Jones, T. A. , Zou, J. Y., Cowan, S. W. & Kjelgaard, M. (1991). Acta Cryst. A47,110-119.). The resulting experimental electron density was so excellent that the conformation of the inhibitor compound 8 could be interpreted unambiguously. The electron density around the five- membered ring carrying the carboxy group clearly showed the carboxy group in contact with residues His 56 and Tyr 356 in non-brequinar-like conformation addressing subsite 3.

In compound 8 a hydroxy group at 5-position at the five membered ring was introduced creating a stereo center at this position. The racemic mixture was used for crystallization experiments. Analysis of the electron density reveals that both enantiomeres fit into the electron density. The R-enantiomere appears to be positioned in a more favourable position to form interactions with subsite 3 whereas in the S-enantiomere the hydroxy group protrudes into the direction of subsite 4 (remote hydrophobic pocket) in a less favourable manner.

A pdb file for compound 8 was created using the program MOE (Chemical Computing Group Inc. , MOE 2002.02). After energy minimization the compound was built into the electron density manually. Topology and parameter files for compound 8 were created using the program Xplo2d (Uppsala Software Factory; Kleywegt, G. M. (1997) J. Mol. Biol. 273,371-376). After an additional round of model building and water picking using CNX another complete round of refinement was performed. The final model included the DHODH (Met30-Arg396) protein, the cofactor flavinmononucleotide (FMN), one orotate molecule (ORO), one acetate molecule (ACT), five sulfate ions (S04), one molecule of compound 8 (INH) and 218 water molecules (TIP).

The model is well refined and shows very good stereochemical geometry. The refinement 0 process which included data from 19.0-1. 8 A resulted in an R-factor of 18.2 % and a free R-factor of 19.6 % for the R-form and S-form (statistics are given only for R-form).

Except for non-glycine and non-proline residues 91.6 % of the residues are located in the most favoured region of the ramachandran plot and 8.4 % cluster in the additional allowed regions. There are no residues in the disallowed region. Table 20 summarizes the refinement statistics for compound 8 in complex with human DHODH. Values in parentheses give the R-factor and Rfree-factors, respectively, for the last resolution bin ranging from 1.91 to 1.8.

Table 20: Refinement Statistics for DHODH/compound 8 complex R-factor (%) 18. 2 (22.1) Rfree 19.6 (24.6) RMS deviation from ideal values bond length (A) 0.005 Bond angle (°) 1.2 Dihedral angles (°) 21. 2 Improper angles (°) 0. 83 Structure determination and refinement of DHODH/compound 9 complex The structure for the human DHODH (Met30-Arg396) in complex with compound 9 was solved using the method of molecular replacement (MR). The free accessible pdb entry lD3G. pdb was used as a search model. The ligands brequinar and DDQ as well as all of the water molecules were removed prior to the MR search. The search model included the polypeptide chain of hDHODH (Met30-Arg396), one molecule of orotate, one molecule of the cofactor flavinmononucleotide (FMN) and one acetate molecule which was present under the crystallization conditions. A standard rotational and translational molecular replacement search at 3.0 A was performed using the program molrep (Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50,760-763.). Solutions for both the rotational and translational search were well above the next ranking solutions. The MR resulted in an R-factor of 32.8 % and a correlation coefficient of 73.6 for the DHODH/compound 9 complex.

In a first round of refinement the MR model was subjected to rigid body refinement and a slow cooling simulated annealing protocol using a maximum likelihood target to remove model bias (Accelrys Inc. CNX program suite, CNX2002). Additionally, an individual b-factor refinement was carried out using standard CNX-protocols. Finally SIGMAA weighted 2Fo-Fc and Fo-Fc electron density maps were calculated and displayed together with the protein model in the program O (DatOno AB; Jones, T. A. , Zou, J. Y., Cowan, S. W. & Kjelgaard, M. (1991). Acta Cryst. A47,110-119.). The resulting experimental electron density was so excellent that the conformation of the inhibitor compound 9 could be interpreted unambiguously. The electron density around the five-

membered ring carrying the carboxy group clearly showed the carboxy group in contact with residues Gln 47 and Arg 136 and a conserved water molecule in a unique brequinar- like conformation addressing subsite 2 only. In this conformation the sulfur atom of the five membered ring comes into close contact to Val 134 and Val 143 which form in part subsite 4 (remote hydrophobic pocket).

A pdb file for compound 9 was created using the program MOE (Chemical Computing Group Inc. , MOE 2002.02). After energy minimization the compound was built into the electron density manually. Topology and parameter files for compound 9 were created using the program Xplo2d (Uppsala Software Factory; Kleywegt, G. M. (1997) J. Mol. Biol. 273,371-376). After an additional round of model building and water picking using CNX another complete round of refinement was performed. The final model included the DHODH (Met30-Arg396) protein, the cofactor flavinmononucleotide (FMN), one orotate molecule (ORO), one acetate molecule (ACT), five sulfate ions (S04), one molecule of compound 9 (INH) and 291 water molecules (TIP).

The model is well refined and shows very good stereochemical geometry. The refinement 0 process which included data from 17.2-2. 0 A resulted in an R-factor of 18.1 % and a free R-factor of 20.0 %. Except for non-glycine and non-proline residues 92.1 % of the residues are located in the most favoured region of the ramachandran plot and 7.9 % cluster in the additional allowed regions. There are no residues in the disallowed region. Table 21 summarizes the refinement statistics for compound 9 in complex with human DHODH.

Values in parentheses give the R-factor and Rfree-factors, respectively, for the last resolution bin ranging from 2.13 to 2.0.

Table 21: Refinement Statistics for DHODH/compound 9 complex R-factor (%) 18. 1 (19.7) Rfree 20.0 (22.0) RMS deviation from ideal values bond length (A) 0.005 Bond angle (°) 1.2 Dihedral angles (°) 21. 2 Improper angles (°) 0. 80

Structure determination and refinement of DHODH/compound 10 complex The structure for the human DHODH (Met30-Arg396) in complex with compound 10 was solved using the method of molecular replacement (MR). The free accessible pdb entry lD3G. pdb was used as a search model. The ligands brequinar and DDQ as well as all of the water molecules were removed prior to the MR search. The search model included the polypeptide chain of hDHODH (Met30-Arg396), one molecule of orotate, one molecule of the cofactor flavinmononucleotide (FMN) and one acetate molecule which was present under the crystallization conditions. A standard rotational and translational molecular replacement search at 3.0 A was performed using the program molrep (Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50,760-763.). Solutions for both the rotational and translational search were well above the next ranking solutions. The MR resulted in an R-factor of 32.8 % and a correlation coefficient of 74.1 for the DHODH/compound 10 complex.

In a first round of refinement the MR model was subjected to rigid body refinement and a slow cooling simulated annealing protocol using a maximum likelihood target to remove model bias (Accelrys Inc. CNX program suite, CNX2002). Additionally, an individual b-factor refinement was carried out using standard CNX-protocols. Finally SIGMAA weighted 2Fo-Fc and Fo-Fc electron density maps were calculated and displayed together with the protein model in the program O (DatOno AB; Jones, T. A. , Zou, J. Y., Cowan, S. W. & Kjelgaard, M. (1991). Acta Cryst. A47,110-119.). The resulting experimental electron density was so excellent that the conformation of the inhibitor compound 10 could be interpreted unambiguously. The electron density around the five- membered ring carrying the carboxy group clearly showed the presence of two alternative conformations of compound 10. In one conformation (conformation A) the carboxy group interacts with residues Gln 47 and Arg 136, whereas in the second conformation (conformation B) the interaction involves residues His 56 and Tyr 356 (see above). For each conformation a separate DHODH/compound 10 complex was subjected to refinement.

The pdb files for the compound 10 in conformation A and B were created using the program MOE (Chemical Computing Group Inc. , MOE 2002.02). Both compounds were energy minimized and built into the electron density manually. Topology and parameter files for compound 10 were created using the program Xplo2d (Uppsala Software Factory; Kleywegt, G. M. (1997) J. Mol. Biol. , 273,371-376). After an additional round of model

building and water picking using CNX, another complete round of refinement was performed. The final model included the human DHODH (Met30 Arg396) protein, the cofactor flavinmononucleotide (FMN), one orotate molecule (ORO), two acetate molecules (ACT), four sulfate ions (S04), one molecule of compound 10 (INH) either in conformation A or conformation B and 226 water molecules (TIP). Residues which are missing the coordinate file due to very poor electron density are listed in the header of the pdb files.

The models are well refined and show very good geometry. The refinement process which 0 included data from 19.5-1. 8 A resulted in an R-factor of 19.5% and a free R-factor of 20.5% for the complex in conformation A and for the complex in conformation B, respectively. The identical R-factors indicate that non of the conformers A and B represent a preferred conformation. Except for non-glycine and non-proline residues 91.6% are located in the most favoured region of the ramachandran plot and 8.4 % cluster in the additional allowed regions. There are no residues in the disallowed region. Table 22 summarizes the refinement statistics for compound 10 in complex with human DHODH.

Values in parentheses give the R-factor and Rfree-factors, respectively, for the last resolution bin ranging from 1.91 to 1.8.

Table 22: Refinement Statistics for DHODH/compound 10 complex conformation A & B R-factor (%) 19.5 (20.5) Rfree 20.5 (22.7) RMS deviation from ideal values bond length (A) 0.005 Bond angle (°) 1.2 Dihedral angles (°) 21. 9 Improper angles (°) 0. 82 While this invention has been particularly shown and described with references to preferred embodiments thereof, it will be understood by those skilled in the art that various

changes in form and details may be made therein without departing from the scope of the invention encompassed by the appended claims.

The following compounds are preferred: 3- (Biphenyl-4-ylcarbamoyl)-thiophene-2-carboxylic acid ; 3- (2'-Ethoxy-3, 5-difluoro- biphenyl-4-ylcarbamoyl)-thiophene-2-carboxylic acid ; 3- (3'-Ethoxy-3, 5-difluoro-biphenyl- 4-yl-carbamoyl)-thiophene-2-carboxylic acid ; 3- (3, 5-Difluoro-2', 4'-dimethoxy-biphenyl-4- yl-carbamoyl)-thiophene-2-carboxylic acid ; 3- (2, 3,5, 6-Tetrafluoro-2'-methoxy-biphenyl-4- yl-carbamoyl)-thiophene-2-carboxylic acid ; 3- (2'-Chloro-3, 5-difluoro-biphenyl-4- ylcarbamoyl) -thiophene-2-carboxylic acid; 3- (3, 5, 2'-Trifluoro-biphenyl-4-ylcarbamoyl)- thiophene-2-carboxylic acid; 3- (2-Chloro-2'-methoxy-biphenyl-4-ylcarbamoyl)-thiophene- 2-carboxylic acid; 3- (2, 3,5, 6-Tetrafluoro-3'-trifluoromethoxy-biphenyl-4-ylcarbamoyl) - thiophene-2-carboxylic acid ; 3- (3-Fluoro-3'-methoxy-biphenyl-4-ylcarbamoyl)-thiophene- 2-carboxylic acid; 3- (3, 5-Difluoro-3'-trifluoromethoxy-biphenyl-4-ylcarbamoyl)- thiophene-2-carboxylic acid; 3- (Biphenyl-4-ylcarbamoyl)-furan-2-carboxylic acid; 4- (Biphenyl-4-ylcarbamoyl) -thiophene-3-carboxylic acid; 4- (2-Chloro-2'-methoxy-biphenyl- 4-ylcarbamoyl) -thiophene-3-carboxylic acid; 4- (3, 5,2'-Trifluoro-biphenyl-4-ylcarbamoyl)- thiophene-3-carboxylic acid ; 4- (3'-Ethoxy-3, 5-difluoro-biphenyl-4-ylcarbamoyl) - thiophene-3-carboxylic acid ; 4- (2'-Ethoxy-3, 5-difluoro-biphenyl-4-ylcarbamoyl) - thiophene-3-carboxylic acid; 4- (3, 5-Difluoro-3'-trifluoromethoxy-biphenyl-4- ylcarbamoyl) -thiophene-3-carboxylic acid; 4- (3-Fluoro-3'-methoxy-biphenyl-4- ylcarbamoyl)-thiophene-3-carboxylic acid ; 4- (Biphenyl-4-ylcarbamoyl)-furan-3-carboxylic acid; 2- (Biphenyl-4-ylcarbamoyl)-thiophene-3-carboxylic acid; 2- (Bi-phenyl-4- ylcarbamoyl) -furan-3-carboxylic acid; 3- (3-Fluoro-3'-methoxy-biphenyl-4-yl-carbamoyl)- cyclopent-2-ene-1, 2-dicarboxylic acid ; 2- (3-Fluoro-3'-methoxy-biphenyl-4-ylcarbamoyl)- cyclopent-1-ene-1, 3-dicarboxylic acid; 2- (3-Fluoro-3'-methoxy-biphenyl-4-ylcarbamoyl)- cyclopent-1-enecarboxylic acid methyl ester; Cyclopent-1-ene-1, 2-dicarboxylic acid 1- [ (3- fluoro-3'-methoxy-biphenyl-4-yl)-amide] 2-hydroxyamide; 3-Hydroxy-2- (2, 3,5, 6- tetrafluoro-3'-trifluoromethoxy-biphenyl-4-ylcarbamoyl)-cycl opent-1-enecarboxylic acid ; 5-Hydroxy-2- (2,3, 5, 6-tetrafluoro-3'-trifluoromethoxy-biphenyl-4-ylcarbamoyl)-cy clopent- 1-enecarboxylic acid; 2- (3'-Ethoxy-3, 5-difluoro-biphenyl-4-ylcarbamoyl) -3-hydroxy- cyclopent-1-enecarboxylic acid ; 2- (3'-Ethoxy-3, 5-difluoro-biphenyl-4-ylcarbamoyl) -5- hydroxy-cyclo-pent-1-enecarboxylic acid ; 2- (l', 3'di-methoxy-3, 5-difluoro-biphenyl-4- ylcarbamoyl)-3-hydroxy-cyclopent-1-enecarboxylic acid ; 2- (l', 3'di-methoxy-3, 5-difluoro-

biphenyl-4-yl-carbamoyl)-5-hydroxy-cyclopent-1-enecarboxylic acid; 3-Hydroxy-2- (3,5, 2'-trifluoro-biphenyl-4-ylcarbamoyl)-cyclopent-1-enecarboxyl ic acid ; 5-Hydroxy-2- (3,5, 2'-trifluoro-biphenyl-4-ylcarbamoyl)-cyclopent-1-enecarboxyl ic acid ; 2- (2-Chloro-2'- methoxy-biphenyl-4-ylcarbamoyl)-3-hydroxy-cyclopent-1-enecar boxylic acid ; 2- (2- Chloro-2'-methoxy-biphenyl-4-ylcarbamoyl)-5-hydroxy-cyclopen t-1-enecarboxylic acid ; <BR> <BR> <BR> 2-(2'-Chloro-3, 5-difluoro-biphenyl-4-ylcarbamoyl)-3-hydroxy-cyclopent-1-ene carboxylic acid; 2- (2'-Chloro-3, 5-difluoro-biphenyl-4-ylcarbamoyl)-5-hydroxy-cyclopent-l- enecarboxylic acid ; 2- (3-Fluoro-3'-methoxy-biphenyl-4-ylcarbamoyl)-3-hydroxy- cyclopent-1-enecarboxylic acid ; 2- (3-Fluoro-3'-methoxy-biphenyl-4-ylcarbamoyl)-5- hydroxy-cyclopent-1-enecarboxylic acid; trans 2- (3-Fluoro-3'-methoxy-biphenyl-4- ylcarbamoyl)-cyclopentane carboxylic acid; cis-2- (3-Fluoro-3'-methoxy-biphenyl-4- ylcarbamoyl) -cyclopentane carboxylic acid; 2- (2'- Chloro-3, 5-difluoro-biphehyl-4- ylcarbamoyl)-cyclopentane carboxylic acid; 2- (3, 5-Difluoro-2', 4'-dimethoxy-biphenyl-4- ylcarbamoyl)-cyclopentane carboxylic acid; 2- (3'-Ethoxy-3, 5-difluoro-biphenyl-4- ylcarbamoyl) -cyclopentane carboxylic acid; 2- (2'-Ethoxy-3, 5-difluoro-biphenyl-4- ylcarbamoyl)-cyclopentane carboxylic acid; 2- (Biphenyl-4-ylcarbamoyl)-cyclopentane carboxylic acid; 2- (2,3, 5,6-Tetrafluoro-3'-trifluoro-methoxy-biphenyl-4-ylcarbamoyl) - cyclopentane carboxylic acid; 2- (3, 5-Difluoro-3'-trifluoro-methoxy-biphenyl-4-yl- carbamoyl) -cyclopentane carboxylic acid.

Table 25: Structure Con- sensus Score H02C-63, 04 - 0 -N zon p t N

Figure 2

CRYST1 90.651 90.651 123.072 90. 00 90.00 120.00 P 32 2 1 12 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.011031 0.006369 0.000000 0.00000 SCALE2 0.000000 0.012738 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008125 0.00000 ATOM 2779 N1 FMN 398 41.764 36.130 8.647 1.00 13.22 ATOM 2780 C2 FMN 398 42.155 35.485 9.782 1.00 16.74 ATOM 2781 02 FMN 398 41.551 35.587 10.834 1.00 15.99 ATOM 2782 N3 FMN 398 43.334 34.654 9.723 1.00 15.64 ATOM 2783 C4 FMN 398 44.085 34.461 8.625 1.00 15.45 ATOM 2784 04 FMN 398 45.083 33.724 8.672 1.00 15.51 ATOM 2785 C4A FMN 398 43.662 35.157 7.396 1.00 14.11 ATOM 2786 N5 FMN 398 44.352 35.025 6.251 1.00 13.88 ATOM 2787 C5A FMN 398 43.933 35.705 5.122 1.00 11.84 ATOM 2788 C6 FMN 398 44.672 35.590 3.867 1.00 10.31 ATOM 2789 C7 FMN 398 44.292 36.270 2.717 1.00 11.40 ATOM 2790 C7M FMN 398 45.109 36.125 1.414 1.00 9.20 ATOM 2791 C8 FMN 398 43.119 37.130 2.739 1.00 11.94 ATOM 2792 C8M FMN 398 42.649 37.914 1.520 1.00 13.94 ATOM 2793 C9 FMN 398 42.397 37.245 3.923 1.00 11.56 ATOM 2794 C9A FMN 398 42.767 36.561 5.119 1.00 13.59 ATOM 2795 N10 FMN 398 42.048 36.664 6.371 1.00 13.81 ATOM 2796 C10 FMN 398 42.448 36.000 7.512 1.00 14.45 ATOM 2797 C1* FMN 398 40.845 37.508 6.453 1.00 12.64 ATOM 2798 C2* FMN 398 41.112 39.002 6.630 1.00 13.30 ATOM 2799 02* FMN 398 41.776 39.190 7.920 1.00 13.46 ATOM 2800 C3* FMN 398 39.786 39.812 6.672 1.00 12.09 ATOM 2801 03* FMN 398 38.927 39.299 7.749 1.00 12.88 ATOM 2802 C4* FMN 398 38.953 39.699 5.366 1.00 12.40 ATOM 2803 04* FMN 398 39.803 39.461 4.214 1.00 11.71 ATOM 2804 C5* FMN 398 38.115 40.952 5.105 1.00 9.96 ATOM 2805 05* FMN 398 38.918 42.129 4.957 1.00 13.77 ATOM 2806 P FMN 398 39.368 42.735 3.536 1.00 12.98 ATOM 2807 O1P FMN 398 40.420 41.816 2.954 1.00 14.29

ATOM 2808 02P FMN 398 39.893 44.111 3.861 1.00 12.03 ATOM 2809 03P FMN 398 38.119 42.812 2.647 1.00 13.57 ATOM 2810 N1 ORO 399 41.668 32.377 4.927 1.00 16. 79 ATOM 2811 C2 ORO 399 40.653 33.293 5.236 1.00 16.19 ATOM 2812 02 ORO 399 40.042 33.934 4.385 1.00 20.26 ATOM 2813 N3 ORO 399 40.353 33.457 6.587 1.00 14.42 ATOM 2814 C4 ORO 399 40.966 32.794 7.654 1.00 14.86 ATOM 2815 04 ORO 399 40.645 32.999 8.803 1.00 14.43 ATOM 2816 C5 ORO 399 42.023 31.842 7.276 1.00 14.27 ATOM 2817 C6 ORO 399 42.317 31.682 5.968 1.00 16.76 ATOM 2818 C7 ORO 399 43.403 30.705 5.524 1.00 17.77 ATOM 2819 071 ORO 399 44.513 30.665 6.039 1.00 19.80 ATOM 2820 072 ORO 399 42.936 29.994 4.595 1.00 18.75 ATOM 2821 S S04 400 56.428 40.104 34.632 1.00 33.94 ATOM 2822 01 S04 400 56.122 41.420 35.218 1.00 34.17 ATOM 2823 02 S04 400 55.206 39.280 34.611 1.00 35.21 ATOM 2824 03 S04 400 56.931 40.290 33.260 1.00 35.14 ATOM 2825 04 S04 400 57.461 39.431 35.440 1.00 35.91 ATOM 2826 C ACT 401 24.612 49.259 4.963 1.00 34.33 C . ATOM 2827 0 ACT 401 23.428 49.625 4.658 1.00 33.50 ATOM 2828 OXT ACT 401 24.926 48.987 6.156 1.00 35.35 ATOM 2829 CH3 ACT 401 24.980 48.156 3.942 1.00 30.98 ATOM 2830 S S04 402 56.699 36.609 28.290 1.00 39.30 ATOM 2831 01 S04 402 55.391 37.270 28.281 1.00 48.45 ATOM 2832 02 S04 402 56.512 35.164 28.489 1.00 46.40 ATOM 2833 03 S04 402 57.362 36.850 26.997 1.00 48.09 ATOM 2834 04 S04 402 57.515 37.166 29.380 1.00 46.88 ATOM 2835 S S04 403 48.271 43.913 28.816 1.00 92.32 ATOM 2836 01 S04 403 49.281 42.998 28.253 1.00 91.75 ATOM 2837 02 S04 403 47.936 43.487 30.189 1.00 91.47 ATOM 2838 03 S04 403 48.811 45.286 28.848 1.00 91.52 ATOM 2839 04 S04 403 47.056 43.882 27.977 1.00 91.67 ATOM 2840 S S04 404 32.887 23.014 6.481 1.00 79.75 ATOM 2841 01 S04 404 32.953 24.098 7.479 1.00 80.39 ATOM 2842 02 S04 404 32.083 23.456 5.326 1.00 79.78 ATOM 2843 03 S04 404 34.249 22.673 6.029 1.00 79.79

ATOM 2844 04 S04 404 32.257 21. 829 7.091 1.00 79.81 ATOM 2845 OH2 TIP 2 35.590 55.465-5. 472 1.00 26.63 ATOM 2846 OH2 TIP 3 38.348 45.654 5.431 1.00 10.48 ATOM 2847 OH2 TIP 4 26.302 32. 577-2. 704 1.00 19.39 ATOM 2848 OH2 TIP 5 32.739 49.699 5.057 1.00 5.11 ATOM 2849 OH2 TIP 6 40.173 36.489 0.177 1.00 9.37 ATOM 2850 OH2 TIP 7 28.781 46.327 21.174 1.00 10. 19 ATOM 2851 OH2 TIP 8 50.103 40.154 27.008 1.00 11.09 ATOM 2852 OH2 TIP 9 52.699 35.114 39.857 1.00 14.19 ATOM 2853 OH2 TIP 10 32.651 48.949 19.281 1.00 9.20 ATOM 2854 OH2 TIP 11 31.681 31.390 6.490 1. 00 17.24 ATOM 2855 OH2 TIP 12 54.417 36.438 7.903 1.00 15.61 ATOM 2856 OH2 TIP 13 48.745 30.174-4. 588 1.00 19.16 ATOM 2857 OH2 TIP 14 52.941 44.773 24.555 1.00 23.37 ATOM 2858 OH2 TIP 15 56.887 41.485 19.910 1.00 12.52 ATOM 2859 OH2 TIP 16 24.269 48.192 0.627 1.00 11.85 ATOM 2860 OH2 TIP 17 35.611 30.647-11. 558 1.00 19.10 ATOM 2861 OH2 TIP 19 27.016 52.988 8.586 1.00 12.80 ATOM 2862 OH2 TIP 20 33.134 44.858-12. 599 1.00 21.07 ATOM 2863 OH2 TIP 21 41.811 40.231 11.637 1.00 8.18 ATOM 2864 OH2 TIP 22 42.183 27.798 7.499 1.00 16.55 ATOM 2865 OH2 TIP 23 55.491 43.097 24.315 1.00 20.61 ATOM 2866 OH2 TIP 24 22.596 45.819 3.212 1.00 20.68 ATOM 2867 OH2 TIP 25 40.140 46.060 2.081 1.00 12.15 ATOM 2868 OH2 TIP 28 52.896 40.807 35.670 1.00 26.75 ATOM 2869 OH2 TIP 29 39.349 36.839-11. 592 1.00 16.06 ATOM 2870 OH2 TIP 30 29.722 63.391 4.730 1.00 30.50 ATOM 2871 OH2 TIP 31 31.088 52.800 1.900 1.00 16.24 ATOM 2872 OH2 TIP 33 48.477 40.642 9.325 1.00 18.06 ATOM 2873 OH2 TIP 34 48.151 60.664-5. 676 1.00 38.87 ATOM 2874 OH2 TIP 35 33.824 25.066-2. 250 1.00 26.85 ATOM 2875 OH2 TIP 36 27.559 36.164-15. 409 1.00 20.80 ATOM 2876 OH2 TIP 37 36.106 58.318 1.505 1.00 17.98 ATOM 2877 OH2 TIP 38 18.439 32.041 12.105 1.00 33.41 ATOM 2878 OH2 TIP 39 30.083 49.589 4.400 1.00 25.73 ATOM 2879 OH2 TIP 40 22.237 50.945 6.710 1.00 15.44 ATOM 2880 OH2 TIP 41 25.160 53.838 20.665 1.00 38.02

ATOM 2881 OH2 TIP 42 28.378 43.059 0.383 1.00 15.63 ATOM 2882 OH2 TIP 43 48.055 30.902 8.812 1.00 25.12 ATOM 2883 OH2 TIP 44 37.474 35.997 32.369 1.00 32.92 ATOM 2884 OH2 TIP 45 36.065 52.338-1. 345 1.00 20.39 ATOM 2885 OH2 TIP 46 48.124 51.068 24.354 1.00 27.11 ATOM 2886 OH2 TIP 47 31.748 42.518-7. 963 1.00 13.51 ATOM 2887 OH2 TIP 48 60.117 28.753 24.514 1.00 24.03 ATOM 2888 OH2 TIP 49 39.433 48.490-3. 629 1.00 30.32 ATOM 2889 OH2 TIP 50 48.317 58.149 0.954 1.00 30.47 ATOM 2890 OH2 TIP 51 55.691 32.327 25.490 1.00 27.61 ATOM 2891 OH2 TIP 52 64.195 35.380 20.138 1.00 19.56 ATOM 2892 OH2 TIP 53 58.833 49.910 15.155 1.00 27.93 ATOM 2893 OH2 TIP 54 51.798 31.467 11.336 1.00 13.39 ATOM 2894 OH2 TIP 55 39.565 45.795-2. 524 1.00 14.64 ATOM 2895 OH2 TIP 56 24.410 28.634 17.373 1.00 22.71 ATOM 2896 OH2 TIP 57 51.724 20.261 6.842 1.00 27.61 ATOM 2897 OH2 TIP 58 41.381 26.139-9. 718 1.00 20.97 ATOM 2898 OH2 TIP 59 25.055 40.702 6.956 1.00 19.36 ATOM 2899 OH2 TIP 60 23.993 41.143 9.391 1.00 25.03 ATOM 2900 OH2 TIP 61 38.010 29.506-11. 416 1.00 23.41 ATOM 2901 OH2 TIP 62 36.303 47.966-1. 088 1.00 30.41 ATOM 2902 OH2 TIP 63 38.481 26.042 1.645 1.00 31.40 ATOM 2903 OH2 TIP 64 53.281 23.398 20.183 1.00 41.21 ATOM 2904 OH2 TIP 65 59.227 43.487 12.586 1.00 16.75 ATOM 2905 OH2 TIP 66 19.680 42.939 12.681 1.00 37.20 ATOM 2906 OH2 TIP 67 34.545 51.641 22.341 1.00 33.42 ATOM 2907 OH2 TIP 68 47.228 63.064 3.669 1.00 42.40 ATOM 2908 OH2 TIP 69 45.044 42.104-5. 477 1.00 28.59 ATOM 2909 OH2 TIP 70 61.334 39.614 15.105 1.00 33.49 ATOM 2910 OH2 TIP 71 63.480 33.513 24.510 1.00 29.51 ATOM 2911 OH2 TIP 72 56.468 35.136 4.213 1.00 43.21 ATOM 2912 OH2 TIP 73 38.377 59.761 19.196 1.00 29.60 ATOM 2913 OH2 TIP 74 44.178 24.030 9.805 1.00 20.05 ATOM 2914 OH2 TIP 75 59.041 44.570 9.927 1.00 18.74 ATOM 2915 OH2 TIP 76 57.140 34.369 26.067 1.00 16.87 ATOM 2916 OH2 TIP 77 39.600 50.271 27.318 1.00 30.06 ATOM 2917 OH2 TIP 78 18.395 33.040 20.240 1.00 39.24

ATOM 2918 OH2 TIP 80 46.253 28. 328 18.697 1.00 23.12 ATOM 2919 OH2 TIP 81 21.439 37.365 21.789 1.00 23.23 ATOM 2920 OH2 TIP 82 20.542 32.670 21.994 1.00 27.90 ATOM 2921 OH2 TIP 83 24.655 41.169-5. 254 1.00 24.02 ATOM 2922 OH2 TIP 84 55.024 41.551 26.503 1.00 26.29 ATOM 2923 OH2 TIP 85 38.257 32.272 33.898 1.00 23.92 ATOM 2924 OH2 TIP 86 44.348 24. 278-3. 540 1.00 35.59 ATOM 2925 OH2 TIP 87 27.444 36.842 9.754 1.00 30.73 ATOM 2926 OH2 TIP 88 31.179 49.190 21.579 1.00 26.24 ATOM 2927 OH2 TIP 89 47.770 20.871 17.535 1.00 24.51 ATOM 2928 OH2 TIP 91 38.465 53.285-2. 768 1.00 34.79 ATOM 2929 OH2 TIP 92 46.308 60.185 17.231 1.00 28.55 ATOM 2930 OH2 TIP 93 28.701 66. 849 4.531 1.00 40.45 ATOM 2931 OH2 TIP 94 60.902 30.818 9.650 1.00 33.92 ATOM 2932 OH2 TIP 96 19.893 46.306 21.698 1.00 30.29 ATOM 2933 OH2 TIP 97 45.510 23.104 6.071 1.00 28.35 ATOM 2934 OH2 TIP 98 55.196 41.435 21.940 1.00 16.83 ATOM 2935 OH2 TIP 99 47.253 53.876-3. 810 1.00 23.52 ATOM 2936 OH2 TIP 100 39.089 57.043-2. 142 1.00 24.05 ATOM 2937 OH2 TIP 101 42.036 65.124 6.183 1.00 24.43 ATOM 2938 OH2 TIP 102 50.161 38.979 37.857 1.00 34.83 ATOM 2939 OH2 TIP 103 24.826 38.099 6.266 1.00 52.04 ATOM 2940 OH2 TIP 104 37.666 19.146 18.942 1.00 44.29 ATOM 2941 OH2 TIP 105 34.064 23.132 21.675 1.00 37.52 ATOM 2942 OH2 TIP 106 50.935 24.631 25.846 1.00 22.54 ATOM 2943 OH2 TIP 108 43.565 44.627 28.144 1.00 49.40 ATOM 2944 OH2 TIP 109 31.117 28.110 31.273 1.00 32.65 ATOM 2945 OH2 TIP 110 20.805 49.008 19.699 1.00 46.79 ATOM 2946 OH2 TIP 111 52.650 36.241 5.934 1.00 27.82 ATOM 2947 OH2 TIP 112 58.236 26.559 10.967 1.00 36.15 ATOM 2948 OH2 TIP 113 43.031 36.731 36.240 1.00 44.91 ATOM 2949 OH2 TIP 114 24.141 50.228 27.710 1.00 47.63 ATOM 2950 OH2 TIP 115 30.276 30.961-7. 868 1.00 31.47 ATOM 2951 OH2 TIP 116 48.292 22.098 6.628 1.00 25.84 ATOM 2952 OH2 TIP 117 39.234 38.015-14. 279 1.00 31.09 ATOM 2953 OH2 TIP 119 46.519 32.215-8. 891 1.00 39.56 ATOM 2954 OH2 TIP 121 20.107 49.247 17.242 1.00 29.89

ATOM 2955 OH2 TIP 122 35.093 44.434 26.730 1.00 43.37 ATOM 2956 OH2 TIP 124 49.192 64.685 7.996 1.00 51.57 ATOM 2957 OH2 TIP 125 37.926 56.308 22.575 1.00 45. 89 ATOM 2958 OH2 TIP 126 35.206 25.843 8.170 1.00 43.48 ATOM 2959 OH2 TIP 128 53.408 48.397 27.188 1.00 32.97 ATOM 2960 OH2 TIP 130 31.779 41.307 27.403 1.00 51.72 ATOM 2961 OH2 TIP 133 45.206 19.827 20.469 1.00 48.38 ATOM 2962 OH2 TIP 135 62.104 49.309 13.802 1.00 52.21 ATOM 2963 OH2 TIP 136 36.380 24.415 5.240 1.00 39.20 ATOM 2964 OH2 TIP 137 37.147 47.795 25.950 1.00 44.17 ATOM 2965 OH2 TIP 139 33.823 32.635 6.973 1.00 21.67 ATOM 2966 OH2 TIP 140 37.744 20.754 21.527 1.00 35.36 ATOM 2967 OH2 TIP 141 27.926 24.074 16.116 1.00 35.24 ATOM 2968 OH2 TIP 142 28.721 24.539 25.917 1.00 43.93 ATOM 2969 OH2 TIP 143 29.978 30.667 9.311 1.00 26.87 ATOM 2970 OH2 TIP 145 32.683 65.958 1.323 1.00 39.30 ATOM 2971 OH2 TIP 146 43.026 23.254 7.640 1.00 42.61 ATOM 2972 OH2 TIP 149 45.148 45.063 12.836 1.00 30.97 ATOM 2973 OH2 TIP 150 56.809 54.243 24.922 1.00 36.26 ATOM 2974 OH2 TIP 154 28.303 35.710-8. 702 1.00 36.61 ATOM 2975 OH2 TIP 157 49.266 20.617 1.054 1.00 39.92 ATOM 2976 OH2 TIP 161 35.433 24.497 28.823 1.00 31.77 ATOM 2977 OH2 TIP 162 48.071 19.322 10.918 1.00 50.89 ATOM 2978 OH2 TIP 170 52.214 41.890 26.882 1.00 29.94 ATOM 2979 OH2 TIP 171 43.481 68.261 20.226 1.00 50.24 ATOM 2980 OH2 TIP 173 30.552 59.616 2.762 1.00 44.94 ATOM 2981 OH2 TIP 177 49.192 23.653 29.887 1.00 45.14 ATOM 2982 OH2 TIP 179 34.894 68.176 14.392 1.00 41.94 ATOM 2983 OH2 TIP 180 34.153 33.362 32.215 1.00 41.27 ATOM 2984 OH2 TIP 183 23.367 59.922 15.715 1.00 40.54 ATOM 2985 OH2 TIP 184 37.180 22.990-4. 060 1.00 29.83 ATOM 2986 OH2 TIP 186 59.902 32.926 5.795 1.00 48.68 ATOM 2987 OH2 TIP 187 38.635 46.185-0. 225 1.00 14.36 ATOM 2988 OH2 TIP 188 52.924 26.976 2.822 1.00 20.37 ATOM 2989 OH2 TIP 189 56.875 26.651 15.240 1.00 18.86 ATOM 2990 OH2 TIP 190 55.306 25.358 16.983 1.00 13.37 ATOM 2991 OH2 TIP 191 51.595 53.593 12.466 1.00 17.70

ATOM 2992 OH2 TIP 192 27.679 24.004 18.956 1.00 35.95 ATOM 2993 OH2 TIP 193 28.677 32.820-8. 974 1.00 32.62 ATOM 2994 OH2 TIP 194 20.577 38.735 10.813 1.00 31. 02 ATOM 2995 OH2 TIP 195 24.128 43.401 2.958 1.00 26.14 ATOM 2996 OH2 TIP 196 21.872 27.301 26.191 1.00 44.90 ATOM 2997 OH2 TIP 197 63.765 33.808 21.998 1.00 36.70 ATOM 2998 OH2 TIP 198 32.846 49.810 23.746 1.00 37.36 ATOM 2999 OH2 TIP 199 58.905 40.769 13.020 1.00 30.69 ATOM 3000 OH2 TIP 200 22.377 49.968 21.592 1.00 39.90 ATOM 3001 OH2 TIP 201 49.605 32.015-6. 500 1.00 33.85 ATOM 3002 OH2 TIP 202 19.520 32.689 24.514 1.00 40.34 ATOM 3003 OH2 TIP 203 18.186 43.942 25.261 1.00 37.04 ATOM 3004 OH2 TIP 204 31.924 23.419 9.913 1.00 41.07 ATOM 3005 OH2 TIP 205 59.551 39.040 29.664 1.00 48.01 ATOM 3006 OH2 TIP 206 24.747 35.005-2. 252 1.00 38.50 ATOM 3007 OH2 TIP 207 51.726 24.271 23.364 1.00 45.92 ATOM 3008 OH2 TIP 208 41.227 63.077 0.564 1.00 52.88 ATOM 3009 OH2 TIP 209 45.043 24.853-7. 064 1.00 63.99 ATOM 3010 OH2 TIP 210 60.297 33.503 0.872 1.00 44.71 ATOM 3011 OH2 TIP 211 55.354 57.898-5. 181 1.00 67.46 ATOM 3012 OH2 TIP 212 26.342 34.721 3.607 1.00 43.97 ATOM 3013 OH2 TIP 213 57.229 58.636 2.147 1.00 56.52 ATOM 3014 OH2 TIP 214 48.952 19.413 7.794 1.00 36.39 ATOM 3015 OH2 TIP 215 18.698 34.346 22.436 1.00 40.47 ATOM 3016 OH2 TIP 216 50.056 55.688 3.654 1.00 41.15 ATOM 3017 OH2 TIP 217 23.808 39.359-3. 697 1.00 38.56 ATOM 3018 OH2 TIP 219 30.490 25.063 28.451 1.00 52.43 ATOM 3019 OH2 TIP 220 26. 031 30.526 16.823 1.00 35.58 ATOM 3020 OH2 TIP 222 54.897 58.072 2.961 1.00 48.36 ATOM 3021 OH2 TIP 223 59.398 53.141-2. 805 1.00 58.38 ATOM 3022 OH2 TIP 224 51.436 23.394 27.949 1.00 42.69 ATOM 3023 OH2 TIP 225 37.497 39.534 29.612 1.00 29.55 ATOM 3024 OH2 TIP 226 20.525 42.018 22.609 1.00 59.58 ATOM 3025 OH2 TIP 227 38.073 51.947-4. 969 1.00 45.26 ATOM 3026 OH2 TIP 228 52.416 32.620 0.869 1.00 58.50 ATOM 3027 OH2 TIP 229 58.152 50.912 12.884 1.00 32.92 ATOM 3028 OH2 TIP 230 56.059 24.385 3.859 1.00 54.19

ATOM 3029 OH2 TIP 231 51.657 20. 142 23.177 1.00 49. 92 ATOM 3030 OH2 TIP 232 48.247 18.532 16.124 1.00 47.86 ATOM 3031 OH2 TIP 233 49.710 20.786 19.715 1.00 37.69 ATOM 3032 OH2 TIP 234 61.171 40.499 27.294 1.00 41.21 ATOM 3033 OH2 TIP 235 60.229 28.450 9.873 1.00 39.53 ATOM 3034 OH2 TIP 236 39.482 20.654 25.665 1.00 40.24 ATOM 3035 OH2 TIP 237 21.898 39.040 23.981 1.00 49.44 ATOM 3036 OH2 TIP 238 41.482 40.544-15. 377 1.00 41.34 ATOM 3037 OH2 TIP 239 53.795 60.848 4.850 1.00 53.61 ATOM 3038 OH2 TIP 240 34.935 52.929-3. 681 1.00 35.26 ATOM 3039 OH2 TIP 241 55.320 34.524-10. 024 1.00 38.15 ATOM 3040 OH2 TIP 243 26.335 37.508-0. 149 1.00 39.86 ATOM 3041 OH2 TIP 244 50.998 60.568 3.880 1.00 65.48 ATOM 3042 OH2 TIP 246 30.232 56.037 21.276 1.00 50.32 ATOM 3043 OH2 TIP 247 25.549 38.311 8.586 1.00 39.52 ATOM 3044 OH2 TIP 248 56.414 42.750 28.581 1.00 44.10 ATOM 3045 OH2 TIP 249 50.755 57.649 7.886 1.00 35.64 ATOM 3046 OH2 TIP 250 41.230 43.187 29.095 1.00 43.86 ATOM 3047 OH2 TIP 251 44.998 22.901 28.299 1.00 53.89 ATOM 3048 OH2 TIP 252 20.352 42.557 15.132 1.00 52.49 ATOM 3049 OH2 TIP 253 26.184 65.798 8.905 1.00 43.68 ATOM 3050 OH2 TIP 254 45.893 38.490-11. 594 1.00 51.24 ATOM 3051 OH2 TIP 255 42.710 41.577 34.594 1.00 40.69 ATOM 3052 OH2 TIP 256 48.240 52.727 26.492 1.00 43.49 ATOM 3053 OH2 TIP 257 39.554 58.190 23.447 1.00 49.04 ATOM 3054 OH2 TIP 258 37.575 57.178 25.056 1.00 45.47 ATOM 3055 OH2 TIP 259 50.664 56.391 11.881 1.00 31.43 ATOM 3056 OH2 TIP 260 59.974 24.777 12.397 1.00 37.68 ATOM 3057 OH2 TIP 261 23.885 35.887 6.227 1.00 46.04 ATOM 3058 OH2 TIP 262 64.702 52.392 26.765 1.00 59.22 ATOM 3059 OH2 TIP 263 35.576 61.522 20.195 1.00 49.81 ATOM 3060 OH2 TIP 264 43.682 65.275-7. 504 1.00 43.86 ATOM 3061 OH2 TIP 266 60.870 47.912 27.467 1.00 53.93 ATOM 3062 OH2 TIP 268 51.707 34.577 42.346 1.00 45.87 ATOM 3063 OH2 TIP 269 29.465 40.196 30.722 1.00 38.31 ATOM 3064 OH2 TIP 270 22.879 53.243 8.461 1.00 43.09 ATOM 3065 OH2 TIP 272 42.793 30.638 35.734 1.00 54.91

ATOM 3066 OH2 TIP 273 39.878 24.302 0.355 1.00 42.81 ATOM 3067 OH2 TIP 274 45.874 43.477 32.353 1.00 44.64 ATOM 3068 OH2 TIP 276 60.439 26.457 22.587 1.00 58.50 ATOM 3069 OH2 TIP 277 33.501 19.630 7.711 1.00 40.97 ATOM 3070 OH2 TIP 278 31.136 37.255 33.009 1.00 49.32 ATOM 3071 OH2 TIP 279 54.504 24.817 21.938 1.00 49. 97 ATOM 3072 OH2 TIP 280 47.280 60.101 19.796 1.00 43.35 ATOM 3073 OH2 TIP 282 54.430 30.932 0.309 1.00 63.58 ATOM 3074 OH2 TIP 283 61.848 32.266 15.111 1.00 38.33 ATOM 3075 OH2 TIP 284 24.901 34.423-6. 980 1.00 40.77 ATOM 3076 OH2 TIP 285 24.740 32.154 26.786 1.00 43.19 ATOM 3077 OH2 TIP 286 32.495 60.380 1.080 1.00 46. 07 ATOM 3078 OH2 TIP 287 55.139 56.211 24.904 1.00 43.70 ATOM 3079 OH2 TIP 288 43.595 38.488 39.052 1.00 50.51 ATOM 3080 OH2 TIP 292 20.724 36.629 8.924 1.00 43.74 ATOM 3081 OH2 TIP 293 46.686 64.930 9.425 1.00 50.38 ATOM 3082 OH2 TIP 294 17.201 60.221 10.522 1.00 43.72 ATOM 3083 OH2 TIP 295 17.500 28.964 19.499 1.00 38.98 ATOM 3084 OH2 TIP 297 36.397 31.380 32.306 1.00 41.95 ATOM 3085 OH2 TIP 300 46.747 59.180-13. 611 1.00 47.00 ATOM 3086 OH2 TIP 301 29.632 25.523 9.658 1.00 45.27 ATOM 3087 OH2 TIP 302 50.813 58.467 0.387 1.00 40.01 ATOM 3088 OH2 TIP 303 29.510 51.948 22.195 1.00 37.26 ATOM 3089 OH2 TIP 304 34.546 62. 038 23.290 1.00 43.28 ATOM 3090 OH2 TIP 305 28.994 20.945 23.473 1.00 43.57 ATOM 3091 OH2 TIP 306 50.928 49.942 27.992 1.00 49.74 ATOM 3092 OH2 TIP 307 18.603 51.462 16.940 1.00 45.75 ATOM 3093 OH2 TIP 309 42.013 36.897-13. 981 1.00 47.94 ATOM 3094 OH2 TIP 310 45.087 42.847-9. 324 1.00 47.04 ATOM 3095 Cl INH 1 55.236 47.264 0.315 0.00 19.32 ATOM 3096 C2 INH 1 55.731 48.195-0. 664 0.00 19.20 ATOM 3097 C3 INH 1 55.258 48.140-2. 050 0.00 19.12 ATOM 3098 C4 INH 1 54.265 47.124-2. 434 0.00 19.23 ATOM 3099 C5 INH 1 53.756 46.171-1. 432 0.00 19.43 ATOM 3100 C6 INH 1 52.787 45.139-1. 726 0.00 19.40 ATOM 3101 C7 INH 1 54.267 46.267-0. 057 0.00 19.29 ATOM 3102 C8 INH 1 53.065 44.157-2. 777 0.00 19.48

ATOM 3103 C9 INH 1 52.120 43.114-3. 081 0.00 19.61 ATOM 3104 F10 INH 1 52.396 42.242-4. 029 0.00 19.47 ATOM 3105 Cll INH 1 50.854 43.001-2. 347 0.00 19.73 ATOM 3106 N12 INH 1 49.946 41.963-2. 657 0.00 19.81 ATOM 3107 C13 INH 1 50.566 43.971-1. 304 0.00 19.50 ATOM 3108 F14 INH 1 49.438 43.905-0. 620 0.00 19.51 ATOM 3109 C15 INH 1 51.512 45.029-0. 990 0.00 19.42 ATOM 3110 C16 INH 1 49.182 41.562-3. 767 0.00 20.05 ATOM 3111 C17 INH 1 48.294 40.370-3. 753 0.00 20.24 ATOM 3112 018 INH 1 49.255 42.235-4. 804 0.00 20.11 ATOM 3113 C19 INH 1 47.993 39.496-2. 733 0.00 20.33 ATOM 3114 C20 INH 1 47.042 38.465-3. 244 0.00 20.37 ATOM 3115 C21 INH 1 46.405 39.116-4. 465 0.00 20.37 ATOM 3116 C22 INH 1 47.561 39.964-4. 990 0.00 20.30 ATOM 3117 C23 INH 1 48.435 39.426-1. 307 0.00 20.38 ATOM 3118 024 INH 1 49.215 40.225-0. 791 0.00 20.42 ATOM 3119 025 INH 1 47.969 38.433-0. 500 0.00 20.42 ATOM 3120 026 INH 1 55.745 49.052-2. 996 0.00 19.20 ATOM 3121 C27 INH 1 57.043 48.675-3. 568 0.00 19.22 ATOM 3122 F28 INH 1 57.052 47.408-3. 962 0.00 18.96 ATOM 3123 F29 INH 1 57.283 49.439-4. 611 0.00 18.96 ATOM 3124 F30 INH 1 58.012 48.867-2. 686 0.00 18.96 TER 1 INH 1 ATOM 1 CB MET A 30 59.689 55.188-5. 634 1.00 78.93 ATOM 2 CG MET A 30 59.846 54.459-6. 959 1.00 79.24 ATOM 3 SD MET A 30 59.231 52.765-6. 869 1.00 79.21 ATOM 4 CE MET A 30 60.653 51.913-6. 175 1.00 79.18 ATOM 5 C MET A 30 58.206 55.626-3. 674 1.00 77.77 ATOM 6 O MET A 30 57.247 55.273-2. 989 1.00 77.07 ATOM 7 N MET A 30 57.559 56.411-5. 965 1.00 78.11 ATOM 8 CA MET A 30 58.237 55.344-5. 173 1.00 78.21 ATOM 9 N ALA A 31 59.261 56.261-3. 170 1.00 77.18 ATOM 10 CA ALA A 31 59.357 56.584-1. 750 1.00 75.83 ATOM 11 CB ALA A 31 60.804 56.889-1. 382 1.00 76.33 ATOM 12 C ALA A 31 58.466 57.766-1. 386 1.00 74.57 ATOM 13 O ALA A 31 58.120 57.955-0. 220 1.00 74.68 ATOM 14 N THR A 32 58.098 58.559-2. 388 1.00 73.02

ATOM 15 CA THR A 32 57.247 59.724-2. 172 1.00 70.94 ATOM 16 CB THR A 32 57.070 60.531-3. 474 1.00 71.72 ATOM 17 OG1 THR A 32 58.350 60.991-3. 929 1.00 71.26 ATOM 18 CG2 THR A 32 56.155 61.727-3. 242 1.00 71.64 ATOM 19 C THR A 32 55.872 59.303-1. 660 1.00 68.92 ATOM 20 O THR A 32 55.231 60.029-0. 897 1.00 69.22 ATOM 21 N GLY A 33 55.423 58.127-2. 086 1.00 65.85 ATOM 22 CA GLY A 33 54.133 57.627-1. 650 1.00 61.62 ATOM 23 C GLY A 33 52.950 58.306-2. 308 1.00 58.54 ATOM 24 0 GLY A 33 52.111 58.899-1. 630 1.00 59.44 ATOM 25 N ASP A 34 52.875 58.220-3. 631 1.00 53.96 ATOM 26 CA ASP A 34 51.773 58.831-4. 358 1.00 48.74 ATOM 27 CB ASP A 34 52.285 59.470-5. 648 1.00 48.47 ATOM 28 CG ASP A 34 51.171 60.046-6. 488 1.00 48.19 ATOM 29 OD1 ASP A 34 50.675 59.329-7. 383 1.00 47.90 ATOM 30 OD2 ASP A 34 50. 783 61.210-6. 245 1.00 48.88 ATOM 31 C ASP A 34 50.687 57.803-4. 663 1.00 45.54 ATOM 32 O ASP A 34 50.947 56.760-5. 266 1.00 42.96 ATOM 33 N GLU A 35 49.467 58.115-4. 237 1.00 42.40 ATOM 34 CA GLU A 35 48.319 57.236-4. 420 1.00 39.88 ATOM 35 CB GLU A 35 47.072 57.897-3. 824 1.00 39.71 ATOM 36 CG GLU A 35 47.055 57.882-2. 298 1.00 41.04 ATOM 37 CD GLU A 35 46.065 58.866-1. 695 1.00 42.39 ATOM 38 OE1 GLU A 35 44.959 59.028-2. 254 1.00 43.92 ATOM 39 OE2 GLU A 35 46.391 59.468-0. 649 1.00 40.71 ATOM 40 C GLU A 35 48.058 56.800-5. 859 1.00 38.11 ATOM 41 0GLU A 35 47.820 55.618-6. 109 1.00 36.81 ATOM 42 N ARG A 36 48.107 57.738-6. 804 1.00 36.86 ATOM 43 CA ARG A 36 47.867 57.397-8. 205 1.00 36.42 ATOM 44 CB ARG A 36 47.761 58.650-9. 077 1.00 39.87 ATOM 45 CG ARG A 36 46.462 59.421-8. 961 1.00 44.23 ATOM 46 CD ARG A 36 46.287 60.321-10. 176 1.00 46.52 ATOM 47 NE ARG A 36 45.492 61.506-9. 878 1.00 50.65 ATOM 48 CZ ARG A 36 45.852 62.445-9. 008 1.00 52.47 ATOM 49 NH1 ARG A 36 46.997 62.336-8. 346 1.00 52.64 ATOM 50 NH2 ARG A 36 45.073 63.500-8. 804 1.00 53.33 ATOM 51 C ARG A 36 48.950 56.509-8. 791 1.00 34.75

ATOM 52 O ARG A 36 48.657 55.559-9. 513 1.00 34.22 ATOM 53 N PHE A 37 50.204 56.826-8. 488 1.00 33.66 ATOM 54 CA PHE A 37 51.316 56.048-9. 014 1.00 33.12 ATOM 55 CB PHE A 37 52.653 56.602-8. 521 1.00 34.20 ATOM 56 CG PHE A 37 53.836 55.879-9. 088 1.00 36.60 ATOM 57 CD1 PHE A 37 54.115 55.945-10. 444 1.00 36.51 ATOM 58 CD2 PHE A 37 54.647 55.101-8. 277 1.00 38.02 ATOM 59 CE1 PHE A 37 55.180 55.247-10. 980 1.00 38.42 ATOM 60 CE2 PHE A 37 55.714 54.398-8. 808 1.00 38.15 ATOM 61 CZ PHE A 37 55.980 54.471-10. 161 1.00 38.74 ATOM 62 C PHE A 37 51.217 54.577-8. 639 1.00 31.06 ATOM 63 O PHE A 37 51.387 53.702-9. 485 1.00 30.53 ATOM 64 N TYR A 38 50.949 54.304-7. 368 1.00 30.51 ATOM 65 CA TYR A 38 50.833 52.924-6. 919 1.00 31.07 ATOM 66 CB TYR A 38 50.801 52.852-5. 392 1.00 29.44 ATOM 67 CG TYR A 38 52.169 52.881-4. 759 1.00 29.09 ATOM 68 CD1 TYR A 38 52.904 54.060-4. 694 1.00 29.44 ATOM 69 CE1 TYR A 38 54.167 54.082-4. 129 1.00 28.77 ATOM 70 CD2 TYR A 38 52.738 51.721-4. 242 1.00 26.55 ATOM 71 CE2 TYR A 38 53.996 51.731-3. 680 1.00 26.62 ATOM 72 CZ TYR A 38 54.706 52.912-3. 626 1.00 28.87 ATOM 73 OH TYR A 38 55.963 52.921-3. 078 1.00 29.87 ATOM 74 C TYR A 38 49.596 52.252-7. 486 1.00 31.66 ATOM 75 O TYR A 38 49.656 51.117-7. 954 1.00 30.99 ATOM 76 N ALA A 39 48.476 52.965-7. 454 1.00 33.37 ATOM 77 CA ALA A 39 47.215 52.433-7. 952 1.00 35.76 ATOM 78 CB ALA A 39 46.076 53.365-7. 562 1.00 35.92 ATOM 79 C ALA A 39 47.203 52.212-9. 460 1.00 37.51 ATOM 80 O ALA A 39 46.769 51.161-9. 939 1.00 37.40 ATOM 81 N GLU A 40 47.692 53.199-10. 203 1.00 39.90 ATOM 82 CA GLU A 40 47.697 53.129-11. 660 1.00 41.43 ATOM 83 CB GLU A 40 47.505 54.531-12. 247 1.00 43.66 ATOM 84 CG GLU A 40 46.253 55.250-11. 764 1.00 47.51 ATOM 85 CD GLU A 40 46.103 56.633-12. 372 1.00 50.59 ATOM 86 OE1 GLU A 40 46.046 56.728-13. 618 1.00 53.22 ATOM 87 OE2 GLU A 40 46.041 57.623-11. 609 1.00 51.67 ATOM 88 C GLU A 40 48.920 52.493-12. 311 1.00 40.64

ATOM 89 0 GLU A 40 48.804 51.910-13. 387 1.00 41. 18 ATOM 90 N HIS A 41 50.085 52.585-11. 678 1.00 39.76 ATOM 91 CA HIS A 41 51.282 52.028-12. 303 1.00 38.73 ATOM 92 CB HIS A 41 52.275 53.153-12. 616 1.00 40.77 ATOM 93 CG HIS A 41 51.702 54.239-13. 470 1.00 44.26 ATOM 94 CD2 HIS A 41 51.815 54.482-14. 797 1.00 45.53 ATOM 95 ND1 HIS A 41 50.869 55.218-12. 971 1.00 46.11 ATOM 96 CE1 HIS A 41 50.494 56. 018-13. 954 1.00 46.63 ATOM 97 NE2 HIS A 41 51.054 55.593-15. 072 1.00 47.73 ATOM 98 C HIS A 41 52.034 50.903-11. 605 1.00 35.82 ATOM 99 0 HIS A 41 52.166 49.809-12. 153 1.00 36.05 ATOM 100 N LEU A 42 52.537 51.168-10. 407 1.00 33.50 ATOM 101 CA LEU A 42 53.317 50.166-9. 688 1.00 32.13 ATOM 102 CB LEU A 42 53.872 50.770-8. 393 1.00 30.83 ATOM 103 CG LEU A 42 54.988 49.962-7. 723 1.00 33.78 ATOM 104 CD1 LEU A 42 55.923 50.904-6. 983 1.00 32.87 ATOM 105 CD2 LEU A 42 54.391 48.919-6. 784 1.00 33.61 ATOM 106 C LEU A 42 52.589 48.852-9. 394 1.00 30.33 ATOM 107 0 LEU A 42 52.988 47.801-9. 893 1.00 31.41 ATOM 108 N MET A 43 51.530 48.907-8. 593 1.00 28.07 ATOM 109 CA MET A 43 50.781 47.701-8. 243 1.00 28.07 ATOM 110 CB MET A 43 49.559 48.057-7. 389 1.00 24.63 ATOM 111 CG MET A 43 49.917 48.620-6. 024 1.00 24.00 ATOM 112 SD MET A 43 51.097 47.580-5. 115 1.00 25.98 ATOM 113 CE MET A 43 50.029 46.223-4. 620 1.00 22.82 ATOM 114 C MET A 43 50.350 46.873-9. 451 1.00 28.45 ATOM 115 0 MET A 43 50.534 45.657-9. 470 1.00 27.65 ATOM 116 N PRO A 44 49.759 47.517-10. 471 1.00 30.19 ATOM 117 CD PRO A 44 49.318 48.922-10. 520 1.00 28.99 ATOM 118 CA PRO A 44 49.320 46.795-11. 670 1.00 30.48 ATOM 119 CB PRO A 44 48.748 47.903-12. 545 1.00 30.20 ATOM 120 CG PRO A 44 48.214 48.872-11. 543 1.00 30.28 ATOM 121 C PRO A 44 50.481 46.067-12. 352 1.00 32.32 ATOM 122 0 PRO A 44 50.348 44.916-12. 767 1.00 32.75 ATOM 123 N THR A 45 51.616 46.750-12. 468 1.00 33.19 ATOM 124 CA THR A 45 52.796 46.170-13. 099 1.00 34.66 ATOM 125 CB THR A 45 53.930 47.214-13. 231 1.00 35.79

ATOM 126 OG1 THR A 45 53.475 48.321-14. 019 1.00 33.62 ATOM 127 CG2 THR A 45 55.155 46.591-13. 896 1.00 35.42 ATOM 128 C THR A 45 53.301 45.003-12. 261 1.00 36.33 ATOM 129 0 THR A 45 53.666 43.951-12. 787 1.00 36.54 ATOM 130 N LEU A 46 53.317 45.201-10. 949 1.00 37.72 ATOM 131 CA LEU A 46 53.770 44.173-10. 022 1.00 38.02 ATOM 132 CB LEU A 46 53.686 44.700-8. 590 1.00 38.12 ATOM 133 CG LEU A 46 54.340 43.856-7. 500 1.00 39.50 ATOM 134 CD1 LEU A 46 55.808 43.642-7. 839 1.00 41.34 ATOM 135 CD2 LEU A 46 54.202 44.562-6. 161 1.00 38.74 ATOM 136 C LEU A 46 52.912 42.920-10. 164 1.00 38.63 ATOM 137 O LEU A 46 53.430 41.806-10. 244 1.00 38.89 ATOM 138 N GLN A 47 51.596 43.108-10. 203 1.00 38.81 ATOM 139 CA GLN A 47 50.669 41.990-10. 329 1.00 40.49 ATOM 140 CB GLN A 47 49.254 42.446-9. 957 1.00 40.67 ATOM 141 CG GLN A 47 49.138 42.901-8. 503 1.00 42.61 ATOM 142 CD GLN A 47 47.756 43.414-8. 147 1.00 44.18 ATOM 143 OE1 GLN A 47 47.259 44.366-8. 750 1.00 46.67 ATOM 144 NE2 GLN A 47 47.127 42.787-7. 159 1.00 43.17 ATOM 145 C GLN A 47 50.688 41.377-11. 729 1.00 39.96 ATOM 146 0 GLN A 47 50.273 40.234-11. 923 1.00 39.12 ATOM 147 N GLY A 48 51.182 42.137-12. 701 1.00 40.79 ATOM 148 CA GLY A 48 51.260 41.634-14. 061 1.00 39.68 ATOM 149 C GLY A 48 52.515 40.806-14. 283 1.00 39.30 ATOM 150 O GLY A 48 52.687 40.200-15. 339 1.00 40.84 ATOM 151 N LEU A 49 53.391 40.772-13. 283 1.00 37.80 ATOM 152 CA LEU A 49 54.636 40.017-13. 377 1.00 37.34 ATOM 153 CB LEU A 49 55.836 40.947-13. 175 1.00 38.41 ATOM 154 CG LEU A 49 56.089 42.039-14. 217 1.00 38.40 ATOM 155 CD1 LEU A 49 57.229 42.929-13. 751 1.00 38.36 ATOM 156 CD2 LEU A 49 56.414 41.402-15. 558 1.00 38.65 ATOM 157 C LEU A 49 54.717 38.886-12. 359 1.00 36.86 ATOM 158 0 LEU A 49 55.440 37.913-12. 564 1.00 36.92 ATOM 159 N LEU A 50 53.978 39.016-11. 263 1.00 36.23 ATOM 160 CA LEU A 50 53.992 38.009-10. 207 1.00 35.06 ATOM 161 CB LEU A 50 54.594 38.605-8. 929 1.00 35.63 ATOM 162 CG LEU A 50 56.039 39.102-8. 996 1.00 36.84

ATOM 163 CD1 LEU A 50 56.382 39.831-7. 707 1.00 36.77 ATOM-164 CD2 LEU A 50 56.982 37.925-9. 220 1.00 36.09 ATOM 165 C LEU A 50 52.608 37.460-9. 886 1.00 34.37 ATOM 166 O LEU A 50 51.627 38.206-9. 843 1.00 34.32 ATOM 167 N ASP A 51 52.530 36.152-9. 655 1.00 33.01 ATOM 168 CA ASP A 51 51.258 35.534-9. 309 1.00 33.05 ATOM 169 CB ASP A 51 51.365 34.008-9. 370 1.00 34.40 ATOM 170 CG ASP A 51 52.309 33.450-8. 331 1.00 37.10 ATOM 171 OD1 ASP A 51 53.510 33.791-8. 377 1.00 39.23 ATOM 172 OD2 ASP A 51 51.850 32.670-7. 469 1.00 38.47 ATOM 173 C ASP A 51 50.917 35.999-7. 890 1.00 30.99 ATOM 174 0 ASP A 51 51.801 36.411-7. 135 1.00 30.97 ATOM 175 N PRO A 52 49.633 35.935-7. 510 1.00 28.90 ATOM 176 CD PRO A 52 48.538 35.321-8. 280 1.00 27.63 ATOM 177 CA PRO A 52 49.161 36.357-6. 185 1.00 27.61 ATOM 178 CB PRO A 52 47.781 35.715-6. 097 1.00 28.92 ATOM 179 CG PRO A 52 47.313 35.772-7. 514 1.00 27.88 ATOM 180 C PRO A 52 50.054 35.993-4. 996 1.00 25.59 ATOM 181 O PRO A 52 50.463 36.864-4. 237 1.00 25.26 ATOM 182 N GLU A 53 50.363 34.713-4. 836 1.00 24.82 ATOM 183 CA GLU A 53 51.189 34.290-3. 714 1.00 25.88 ATOM 184 CB GLU A 53 51.229 32.761-3. 632 1.00 26.19 ATOM 185 CG GLU A 53 51.892 32.254-2. 366 1.00 27.45 ATOM 186 CD GLU A 53 51.418 30.874-1. 956 1.00 28.77 ATOM 187 OE1 GLU A 53 51.973 30.337-0. 977 1.00 32.06 ATOM 188 OE2 GLU A 53 50.496 30.328-2. 600 1.00 27.91 ATOM 189 C GLU A 53 52.612 34.863-3. 730 1.00 25.94 ATOM 190 0 GLU A 53 53.103 35.326-2. 698 1.00 24.19 ATOM 191 N SER A 54 53.273 34.835-4. 887 1.00 24.50 ATOM 192 CA SER A 54 54.625 35.380-4. 990 1.00 24.72 ATOM 193 CB SER A 54 55.195 35.170-6. 395 1.00 26.25 ATOM 194 OG SER A 54 55.432 33.797-6. 656 1.00 29.09 ATOM 195 C SER A 54 54.610 36.871-4. 676 1.00 25.01 ATOM 196 O SER A 54 55.537 37.395-4. 059 1.00 24.88 ATOM 197 N ALA A 55 53.550 37.549-5. 111 1.00 23.57 ATOM 198 CA ALA A 55 53.404 38.977-4. 876 1.00 22.63 ATOM 199 CB ALA A 55 52.163 39.500-5. 602 1.00 21.92

ATOM 200 C ALA A 55 53.285 39.221-3. 371 1.00 22.63 ATOM 201 0 ALA A 55 53.909 40.127-2. 822 1.00 22.32 ATOM 202 N HIS A 56 52.481 38.402-2. 706 1.00 22.16 ATOM 203 CA HIS A 56 52.304 38.533-1. 267 1.00 23.00 ATOM 204 CB HIS A 56 51.295 37.507-0. 757 1.00 18.21 ATOM 205 CG HIS A 56 51.244 37.422 0.734 1.00 18.62 ATOM 206 CD2 HIS A 56 51.508 36.398 1.580 1.00 16.96 ATOM 207 ND1 HIS A 56 50.926 38.503 1.527 1.00 18.90 ATOM 208 CE1 HIS A 56 50.996 38.149 2.797 1.00 19.09 ATOM 209 NE2 HIS A 56 51.349 36.878 2.857 1.00 18.86 ATOM 210 C HIS A 56 53.620 38.348-0. 508 1.00 24.69 ATOM 211 0 HIS A 56 53.945 39.127 0.394 1.00 24.05 ATOM 212 N ARG A 57 54.368 37.310-0. 873 1.00 25.73 ATOM 213 CA ARG A 57 55.638 37.015-0. 224 1.00 28.93 ATOM 214 CB ARG A 57 56.230 35.724-0. 792 1.00 32.78 ATOM 215 CG ARG A 57 55.243 34.565-0. 760 1.00 40.35 ATOM 216 CD ARG A 57 55.890 33.236-1. 119 1.00 45.50 ATOM 217 NE ARG A 57 56.855 32.813-0. 110 1.00 51.35 ATOM 218 CZ ARG A 57 57.402 31.603-0. 063 1.00 54.26 ATOM 219 NH1 ARG A 57 57.078 30.691-0. 971 1.00 54.88 ATOM 220 NH2 ARG A 57 58.270 31.303 0.896 1.00 56.37 ATOM 221 C ARG A 57 56.625 38.163-0. 382 1.00 27.70 ATOM 222 0 ARG A 57 57.345 38.500 0.554 1.00 28.64 ATOM 223 N LEU A 58 56.653 38.763-1. 567 1.00 26.64 ATOM 224 CA LEU A 58 57.543 39.887-1. 828 1.00 26.14 ATOM 225 CB LEU A 58 57.484 40.268-3. 310 1.00 29.02 ATOM 226 CG LEU A 58 58.480 41.323-3. 798 1.00 31.41 ATOM 227 CD1 LEU A 58 59.896 40.765-3. 693 1.00 32.43 ATOM 228 CD2 LEU A 58 58.167 41.709-5. 237 1.00 32.16 ATOM 229 C LEU A 58 57.086 41.070-0. 971 1.00 25.90 ATOM 230 0 LEU A 58 57.903 41.836-0. 454 1.00 24.40 ATOM 231 N ALA A 59 55.769 41.205-0. 832 1.00 24.36 ATOM 232 CA ALA A 59 55.166 42.275-0. 042 1.00 23.05 ATOM 233 CB ALA A 59 53.641 42.159-0. 074 1.00 20.54 ATOM 234 C ALA A 59 55.651 42.188 1.391 1.00 20.64 ATOM 235 0 ALA A 59 56.037 43.190 1.992 1.00 21.25 ATOM 236 N VAL A 60 55.612 40.982 1.941 1.00 20.09

ATOM 237 CA VAL A 60 56.056 40.766 3.308 1.00 19. 99 ATOM 238 CB VAL A 60 55.817 39.300 3.741 1.00 18.43 ATOM 239 CG1 VAL A 60 56.407 39.054 5.129 1.00 17.76 ATOM 240 CG2 VAL A 60 54.324 39.003 3.742 1.00 14.72 ATOM 241 C VAL A 60 57.541 41.111 3.425 1.00 21.05 ATOM 242 O VAL A 60 57.951 41.785 4.365 1.00 21.13 ATOM 243 N ARG A 61 58.340 40.664 2.459 1.00 23.89 ATOM 244 CA ARG A 61 59.776 40.944 2.471 1.00 27.66 ATOM 245 CB ARG A 61 60.469 40.352 1.239 1.00 29.95 ATOM 246 CG ARG A 61 60.426 38.838 1.122 1.00 38.36 ATOM 247 CD ARG A 61 61.548 38.355 0.196 1.00 44.69 ATOM 248 NE ARG A 61 61.477 36.926-0. 101 1.00 50.18 ATOM 249 CZ ARG A 61 60.671 36.388-1. 014 1.00 51.97 ATOM 250 NH1 ARG A 61 59.863 37.159-1. 729 1.00 51.92 ATOM 251 NH2 ARG A 61 60.674 35.076-1. 212 1.00 53.20 ATOM 252 C ARG A 61 60.065 42.443 2.510 1.00 27.16 ATOM 253 O ARG A 61 60.778 42.925 3.392 1.00 25.78 ATOM 254 N PHE A 62 59.514 43.175 1.546 1.00 26.45 ATOM 255 CA PHE A 62 59.737 44.611 1.470 1.00 28.86 ATOM 256 CB PHE A 62 59.039 45.194 0.239 1.00 31.67 ATOM 257 CG PHE A 62 59.842 45.074-1. 024 1.00 35.37 ATOM 258 CD1 PHE A 62 60.354 43.852-1. 424 1.00 36.62 ATOM 259 CD2 PHE A 62 60.081 46.186-1. 816 1.00 38.91 ATOM 260 CE1 PHE A 62 61.089 43.739-2. 591 1.00 38.37 ATOM 261 CE2 PHE A 62 60.816 46.079-2. 986 1.00 40.05 ATOM 262 CZ PHE A 62 61.320 44.853-3. 373 1.00 39.06 ATOM 263 C PHE A 62 59.277 45.345 2.717 1.00 28.84 ATOM 264 0 PHE A 62 59.950 46.265 3.184 1.00 28.63 ATOM 265 N THR A 63 58.131 44.941 3.252 1.00 28.32 ATOM 266 CA THR A 63 57.598 45.576 4.446 1.00 27.37 ATOM 267 CB THR A 63 56.196 45.023 4.798 1.00 26.41 ATOM 268 OG1 THR A 63 55.298 45.267 3.709 1.00 24.23 ATOM 269 CG2 THR A 63 55.653 45.700 6.044 1.00 25.26 ATOM 270 C THR A 63 58.537 45.351 5.626 1.00 28.52 ATOM 271 0 THR A 63 58.851 46.284 6.369 1.00 27.19 ATOM 272 N SER A 64 58.991 44.112 5.793 1.00 28.48 ATOM 273 CA SER A 64 59. 890 43.790 6.895 1.00 30.95

ATOM 274 CB SER A 64 60.206 42.291 6.909 1.00 30.12 ATOM 275 OG SER A 64 60.986 41.918 5.787 1.00 34.09 ATOM 276 C SER A 64 61.186 44.592 6.791 1.00 31.50 ATOM 277 0 SER A 64 61.789 44.940 7.803 1.00 31.30 ATOM 278 N LEU A 65 61.603 44.893 5.565 1.00 33.16 ATOM 279 CA LEU A 65 62.830 45.654 5.343 1.00 34.16 ATOM 280 CB LEU A 65 63.497 45.212 4.035 1.00 33.74 ATOM 281 CG LEU A 65 63.989 43.762 3.999 1.00 36.53 ATOM 282 CD1 LEU A 65 64.580 43.449 2.636 1.00 34.22 ATOM 283 CD2 LEU A 65 65.026 43.543 5.098 1.00 36.82 ATOM 284 C LEU A 65 62.599 47.165 5.320 1.00 34.01 ATOM 285 O LEU A 65 63.543 47.939 5.177 1.00 34.34 ATOM 286 N GLY A 66 61.345 47.582 5.457 1.00 33. 51 ATOM 287 CA GLY A 66 61.041 49.002 5.463 1.00 34.57 ATOM 288 C GLY A 66 61.063 49.698 4.110 1.00 35.92 ATOM 289 O GLY A 66 61.089 50.930 4.044 1.00 35.49 ATOM 290 N LEU A 67 61.056 48.924 3.030 1.00 36.20 ATOM 291 CA LEU A 67 61.062 49.500 1.689 1.00 37.47 ATOM 292 CB LEU A 67 61.477 48.439 0.665 1.00 39.14 ATOM 293 CG LEU A 67 62.785 47.701 0.982 1.00 41.61 ATOM 294 CD1 LEU A 67 63.070 46.664-0. 092 1.00 41.43 ATOM 295 CD2 LEU A 67 63.931 48.701 1.077 1.00 43.31 ATOM 296 C LEU A 67 59.647 49.992 1.400 1.00 36.88 ATOM 297 O LEU A 67 58.908 49.377 0.635 1.00 36.23 ATOM 298 N LEU A 68 59.281 51.106 2.024 1.00 37.29 ATOM 299 CA LEU A 68 57.947 51.677 1.881 1.00 38.19 ATOM 300 CB LEU A 68 57.206 51.575 3.215 1.00 38.57 ATOM 301 CG LEU A 68 57.206 50.198 3.878 1.00 39.38 ATOM 302 CD1 LEU A 68 56.690 50.310 5.299 1.00 39.44 ATOM 303 CD2 LEU A 68 56.356 49.244 3.059 1.00 40.05 ATOM 304 C LEU A 68 57.983 53.137 1.449 1.00 38.35 ATOM 305 0 LEU A 68 58.922 53.865 1.764 1.00 38.77 ATOM 306 N PRO A 69 56.945 53.583 0.726 1.00 38.45 ATOM 307 CD PRO A 69 55.780 52.778 0.323 1.00 37.87 ATOM 308 CA PRO A 69 56.819 54.956 0.232 1.00 39.07 ATOM 309 CB PRO A 69 55.580 54.885-0. 657 1.00 38.36 ATOM 310 CG PRO A 69 54.754 53.842 0.012 1.00 38.12

ATOM 311 c PRO A 69 56.666 55.976 1.358 1.00 39.55 ATOM 312 O PRO A 69 56.798 55.640 2.535 1.00 40.34 ATOM 313 N PHE A 73 51. 509 61.626 6.239 1.00 57. 41 ATOM 314 CA PHE A 73 50.304 61.905 7.014 1.00 57.56 ATOM 315 CB PHE A 73 49.146 61.013 6.554 1.00 57.94 ATOM 316 CG PHE A 73 47.896 61.178 7.376 1.00 57.97 ATOM 317 CD1 PHE A 73 47.046 62.252 7.167 1.00 58.09 ATOM 318 CD2 PHE A 73 47.592 60.279 8.388 1.00 58.00 ATOM 319 CE1 PHE A 73 45.918 62.427 7.950 1.00 57.86 ATOM 320 CE2 PHE A 73 46.465 60.451 9.175 1.00 56.97 ATOM 321 CZ PHE A 73 45.628 61.525 8.956 1.00 56.70 ATOM 322 C PHE A 73 50.519 61.683 8.506 1.00 56.61 ATOM 323 0 PHE A 73 50.884 60.586 8.932 1.00 56. 50 ATOM 324 N GLN A 74 50.289 62.727 9.295 1.00 55.80 ATOM 325 CA GLN A 74 50.434 62.632 10.743 1.00 54.27 ATOM 326 CB GLN A 74 51.067 63.902 11.316 1.00 55.72 ATOM 327 CG GLN A 74 52.551 64.063 11.029 1.00 58.53 ATOM 328 CD GLN A 74 53.176 65.195 11.835 1.00 60.58 ATOM 329 OE1 GLN A 74 52.868 66.371 11.625 1.00 60.54 ATOM 330 NE2 GLN A 74 54.050 64.839 12.770 1.00 60.75 ATOM 331 C GLN A 74 49.061 62.429 11.366 1.00 51.91 ATOM 332 O GLN A 74 48.107 63.128 11.029 1.00 51.26 ATOM 333 N ASP A 75 48.965 61.464 12.271 1.00 49.71 ATOM 334 CA ASP A 75 47.705 61.173 12.940 1.00 47.29 ATOM 335 CB ASP A 75 47.826 59.868 13.733 1.00 46.43 ATOM 336 CG ASP A 75 48.173 58.681 12.853 1.00 44.45 ATOM 337 OD1 ASP A 75 48.650 57.657 13.391 1.00 41.73 ATOM 338 OD2 ASP A 75 47.960 58.771 11.626 1.00 44.21 ATOM 339 C ASP A 75 47.359 62.319 13.884 1.00 46.48 ATOM 340 0 ASP A 75 48.217 62.803 14.622 1.00 46.43 ATOM 341 N SER A 76 46.106 62.757 13.853 1.00 45.52 ATOM 342 CA SER A 76 45.666 63.839 14.726 1.00 43.83 ATOM 343 CB SER A 76 44.732 64.791 13.976 1.00 43.83 ATOM 344 OG SER A 76 43.519 64.147 13.630 1.00 45.56 ATOM 345 C SER A 76 44.935 63.239 15.916 1.00 42.06 ATOM 346 0 SER A 76 44.492 62.094 15.866 1.00 42.96 ATOM 347 N ASP A 77 44.814 64.014 16.985 1.00 40.79

ATOM 348 CA ASP A 77 44.131 63. 558 18.188 1.00 40.57 ATOM 349 CB ASP A 77 43.969 64.725 19.167 1.00 42.86 ATOM 350 CG ASP A 77 45.303 65.296 19.620 1.00 46.39 ATOM 351 OD1 ASP A 77 45.301 66.339 20.307 1.00 48.20 ATOM 352 OD2 ASP A 77 46.354 64.702 19.294 1.00 47.94 ATOM 353 C ASP A 77 42.761 62.959 17.866 1.00 38.52 ATOM 354 0 ASP A 77 42.285 62.070 18.568 1.00 37.86 ATOM 355 N MET A 78 42.137 63.451 16.799 1.00 37.07 ATOM 356 CA MET A 78 40.819 62.976 16.376 1.00 35.68 ATOM 357 CB MET A 78 40.371 63.700 15.105 1.00 36.68 ATOM 358 CG MET A 78 40.022 65.154 15.279 1.00 38.98 ATOM 359 SD MET A 78 39.373 65.811 13.731 1.00 43.55 ATOM 360 CE MET A 78 37.673 65.195 13.798 1.00 40.05 ATOM 361 C MET A 78 40.758 61.476 16.104 1.00 33.08 ATOM 362 0 MET A 78 39.758 60.823 16.405 1.00 32.55 ATOM 363 N LEU A 79 41.823 60.937 15.521 1.00 29.66 ATOM 364 CA LEU A 79 41.861 59.523 15.186 1.00 28.85 ATOM 365 CB LEU A 79 42.852 59.286 14.043 1.00 26.36 ATOM 366 CG LEU A 79 42.531 60.008 12.728 1.00 27.00 ATOM 367 CD1 LEU A 79 43.494 59.545 11.640 1.00 24.52 ATOM 368 CD2 LEU A 79 41.090 59.723 12.316 1.00 23.83 ATOM 369 C LEU A 79 42.197 58.611 16.359 1.00 28.62 ATOM 370 O LEU A 79 42.120 57.387 16.237 1.00 27.51 ATOM 371 N GLU A 80 42.558 59.199 17.495 1.00 27.92 ATOM 372 CA GLU A 80 42.905 58.408 18.666 1.00 28.74 ATOM 373 CB GLU A 80 43.609 59.272 19.717 1.00 30.72 ATOM 374 CG GLU A 80 43.731 58.592 21.078 1.00 36.88 ATOM 375 CD GLU A 80 44.634 59.344 22.045 1.00 40.61 ATOM 376 OE1 GLU A 80 44.556 59.070 23.262 1.00 40.98 ATOM 377 OE2 GLU A 80 45.427 60. 199 21.591 1.00 43.20 ATOM 378 C GLU A 80 41.686 57.743 19.286 1.00 28.29 ATOM 379 0 GLU A 80 40.633 58.357 19.432 1.00 29.91 ATOM 380 N VAL A 81 41.841 56.478 19.649 1.00 26.82 ATOM 381 CA VAL A 81 40.762 55.717 20.255 1.00 27.29 ATOM 382 CB VAL A 81 40.157 54.697 19.253 1.00 27.96 ATOM 383 CG1 VAL A 81 38.975 53.978 19.891 1.00 26.13 ATOM 384 CG2 VAL A 81 39.736 55.401 17.976 1.00 27.50

ATOM 385 C VAL A 81 41.306 54.939 21.441 1.00 27.37 ATOM 386 0 VAL A 81 42.470 54.529 21.445 1.00 27.61 ATOM 387 N ARG A 82 40.468 54.738 22.450 1.00 27. 98 ATOM 388 CA ARG A 82 40.887 53.977 23.615 1.00 29.54 ATOM 389 CB ARG A 82 40.957 54.860 24.862 1.00 32.27 ATOM 390 CG ARG A 82 42.033 54.387 25.823 1.00 39.97 ATOM 391 CD ARG A 82 41.640 54.494 27.289 1.00 45.20 ATOM 392 NE ARG A 82 42.662 53.886 28.145 1.00 48.67 ATOM 393 CZ ARG A 82 43.059 52.618 28.050 1.00 48.74 ATOM 394 NH1 ARG A 82 42.523 51.816 27.139 1.00 49.38 ATOM 395 NH2 ARG A 82 43.999 52.153 28.859 1.00 50.09 ATOM'396 C ARG A 82 39.912 52.836 23.853 1.00 28.48 ATOM 397 0 ARG A 82 38.738 53.064 24.133 1.00 29.58 ATOM 398 N VAL A 83 40.408 51.609 23.729 1.00 28.50 ATOM 399 CA VAL A 83 39.604 50.406 23.930 1.00 28.91 ATOM 400 CB VAL A 83 38.780 50.041 22.673 1.00 29.46 ATOM 401 CG1 VAL A 83 37.530 50.896 22.597 1.00 31.26 ATOM 402 CG2 VAL A 83 39.633 50.220 21.423 1.00 25.10 ATOM 403 C VAL A 83 40.493 49.216 24.245 1.00 29.96 ATOM 404 0 VAL A 83 41.710 49.284 24.086 1.00 29.44 ATOM 405 N LEU A 84 39.873 48.124 24.688 1.00 31.71 ATOM 406 CA LEU A 84 40.596 46.896 25.005 1.00 32.74 ATOM 407 CB LEU A 84 41.132 46.263 23.712 1.00 31.47 ATOM 408 CG LEU A 84 40.080 46.012 22.622 1.00 31.62 ATOM 409 CD1 LEU A 84 40.753 45.558 21.343 1.00 31.18 ATOM 410 CD2 LEU A 84 39.079 44.976 23.103 1.00 27.96 ATOM 411 C LEU A 84 41.752 47.136 25.973 1.00 33.44 ATOM 412 0 LEU A 84 42.748 46.413 25.946 1.00 35.00 ATOM 413 N GLY A 85 41.613 48.151 26.824 1.00 33.39 ATOM 414 CA GLY A 85 42.654 48.466 27.790 1.00 31.80 ATOM 415 C GLY A 85 43.896 49.059 27.148 1.00 31.85 ATOM 416 0 GLY A 85 44.998 48.962 27.694 1.00 30.17 ATOM 417 N HIS A 86 43.718 49.683 25.988 1.00 31.24 ATOM 418 CA HIS A 86 44.836 50.281 25.271 1.00 31.52 ATOM 419 CB HIS A 86 45.423 49.271 24.275 1.00 33.75 ATOM 420 CG HIS A 86 45.969 48.034 24.915 1.00 36.55 ATOM 421 CD2 HIS A 86 45.508 46.760 24.931 1.00 37.53

ATOM 422 ND1 HIS A 86 47.121 48.033 25.672 1.00 37.68 ATOM 423 CE1 HIS A 86 47.346 46.814 26.128 1.00 37.36 ATOM 424 NE2 HIS A 86 46.381 46.022 25.693 1.00 39.46 ATOM 425 C HIS A 86 44.453 51.546 24.511 1.00 30.30 ATOM 426 0 HIS A 86 43.280 51.835 24.280 1.00 29.95 ATOM 427 N LYS A 87 45.471 52.297 24.122 1.00 29.57 ATOM 428 CA LYS A 87 45.272 53.512 23.357 1.00 28.75 ATOM 429 CB LYS A 87 46.130 54.643 23.928 1.00 31.29 ATOM 430 CG LYS A 87 46.065 55.930 23.131 1.00 36.25 ATOM 431 CD LYS A 87 46.998 56.986 23.704 1.00 39.73 ATOM 432 CE LYS A 87 48.452 56.557 23.603 1.00 41.38 ATOM 433 NZ LYS A 87 49.372 57.604 24.134 1.00 43.32 ATOM 434 C LYS A 87 45.710 53.199 21.931 1.00 26.30 ATOM 435 0 LYS A 87 46.724 52.525 21.724 1.00 24.62 ATOM 436 N PHE A 88 44.928 53.657 20.958 1.00 22.40 ATOM 437 CA PHE A 88 45.251 53.453 19.549 1.00 21.04 ATOM 438 CB PHE A 88 44.151 52.648 18.845 1.00 17.91 ATOM 439 CG PHE A 88 43.990 51.239 19.358 1.00 16.58 ATOM 440 CD1 PHE A 88 43.489 50.995 20.628 1.00 15. 22 ATOM 441 CD2 PHE A 88 44.321 50.157 18.555 1.00 13.45 ATOM 442 CE1 PHE A 88 43.317 49.703 21.087 1.00 15.04 ATOM 443 CE2 PHE A 88 44.153 48.866 19.007 1.00 13.65 ATOM 444 CZ PHE A 88 43.650 48.636 20.275 1.00 15.42 ATOM 445 C PHE A 88 45.350 54.841 18.917 1.00 21.32 ATOM 446 0 PHE A 88 44.363 55.578 18.900 1.00 21.11 ATOM 447 N ARG A 89 46.524 55.203 18.399 1.00 21.70 ATOM 448 CA ARG A 89 46.681 56.526 17.797 1.00 23.91 ATOM 449 CB ARG A 89 48.142 56.803 17.422 1.00 27.51 ATOM 450 CG ARG A 89 48.735 55.905 16.369 1.00 34.45 ATOM 451 CD ARG A 89 50.095 56.441 15.949 1.00 39.63 ATOM 452 NE ARG A 89 50.942 56.726 17.103 1.00 43.01 ATOM 453 CZ ARG A 89 52.223 57.073 17.025 1.00 45.72 ATOM 454 NH1 ARG A 89 52.814 57.180 15.840 1.00 45.78 ATOM 455 NH2 ARG A 89 52.915 57.309 18.133 1.00 46.24 ATOM 456 C ARG A 89 45.764 56.722 16.593 1.00 21.40 ATOM 457 0 ARG A 89 45.350 57.839 16.308 1.00 20.59 ATOM 458 N ASN A 90 45.467 55.643 15.877 1.00 19.60

ATOM 459 CA ASN A 90 44.525 55.708 14.759 1.00 19.44 ATOM 460 CB ASN A 90 45.218 56.045 13.418 1.00 17.27 ATOM 461 CG ASN A 90 45.918 54.870 12.782 1.00 17.47 ATOM 462 OD1 ASN A 90 45.286 53.885 12.404 1.00 18.85 ATOM 463 ND2 ASN A 90 47.236 54. 977 12.635 1.00 17.61 ATOM 464 C ASN A 90 43.814 54.357 14.762 1.00 19.17 ATOM 465 0 ASN A 90 44.377 53.351 15.199 1.00 20.42 ATOM 466 N PRO A 91 42.555 54.325 14.307 1.00 17.95 ATOM 467 CD PRO A 91 41.802 55.495 13.815 1.00 18.80 ATOM 468 CA PRO A 91 41.721 53.123 14.259 1.00 17.08 ATOM 469 CB PRO A 91 40.319 53.708 14.339 1.00 17.82 ATOM 470 CG PRO A 91 40.444 54.896 13.443 1.00 15.11 ATOM 471 C PRO A 91 41.872 52.197 13.059 1.00 17.57 ATOM 472 O PRO A 91 41.071 51.277 12.889 1.00 17.10 ATOM 473 N VAL A 92 42.889 52.425 12.236 1.00 17.30 ATOM 474 CA VAL A 92 43.086 51.607 11.040 1.00 17.64 ATOM 475 CB VAL A 92 43.391 52.504 9.816 1.00 17.72 ATOM 476 CG1 VAL A 92 43.497 51.666 8.555 1.00 14.42 ATOM 477 CG2 VAL A 92 42.310 53.560 9.678 1.00 16. 61 ATOM 478 C VAL A 92 44.206 50.588 11.201 1.00 18.02 ATOM 479 O VAL A 92 45.377 50.948 11.280 1.00 18.29 ATOM 480 N GLY A 93 43.840 49.311 11.242 1.00 17.60 ATOM 481 CA GLY A 93 44.839 48.274 11.394 1.00 16.36 ATOM 482 C GLY A 93 44.907 47.332 10.212 1.00 16.58 ATOM 483 O GLY A 93 44.043 47.352 9.336 1.00 17.37 ATOM 484 N ILE A 94 45.956 46.517 10.174 1.00 16.03 ATOM 485 CA ILE A 94 46.123 45.541 9.106 1.00 14.28 ATOM 486 CB ILE A 94 47.621 45.319 8.772 1.00 15.21 ATOM 487 CG2 ILE A 94 48.409 45.008 10.035 1.00 14.14 ATOM 488 CG1 ILE A 94 47.766 44.197 7.740 1.00 15.27 ATOM 489 CD1 ILE A 94 47.288 44.580 6.347 1.00 15.14 ATOM 490 C ILE A 94 45.494 44.236 9.595 1.00 14.89 ATOM 491 0 ILE A 94 45.868 43.707 10.639 1.00 14.26 ATOM 492 N ALA A 95 44.521 43.729 8.847 1.00 14.41 ATOM 493 CA ALA A 95 43.837 42.501 9.228 1.00 14.87 ATOM 494 CB ALA A 95 42.665 42.244 8.282 1.00 14.00 ATOM 495 C ALA A 95 44.770 41.292 9.248 1.00 14.88

ATOM 496 0 ALA A 95 45.877 41.338 8.715 1.00 13.34 ATOM 497 N ALA A 96 44.314 40.215 9.878 1.00 14.32 ATOM 498 CA ALA A 96 45.092 38.989 9.952 1.00 17.35 ATOM 499 CB ALA A 96 44.392 37.976 10.856 1.00 16.42 ATOM 500 C ALA A 96 45.240 38.419 8.546 1.00 17.48 ATOM 501 O ALA A 96 44.386 38.641 7.686 1.00 19.61 ATOM 502 N GLY A 97 46.326 37.691 8.309 1.00 18.20 ATOM 503 CA GLY A 97 46.534 37.106 6.997 1.00 16.78 ATOM 504 C GLY A 97 47.697 37.681 6.214 1.00 15.75 ATOM 505 0 GLY A 97 48.411 36.937 5.551 1.00 16.02 ATOM 506 N PHE A 98 47.894 38.995 6.266 1.00 15.54 ATOM 507 CA PHE A 98 49.006 39.586 5.533 1.00 16.58 ATOM 508 CB PHE A 98 48.955 41.115 5.550 1.00 16. 83 ATOM 509 CG PHE A 98 50.097 41.747 4.815 1.00 18.26 ATOM 510 CD1 PHE A 98 50.166 41.680 3.429 1.00 19.90 ATOM 511 CD2 PHE A 98 51.139 42.346 5.505 1.00 19.00 ATOM 512 CE1 PHE A 98 51.254 42.193 2.748 1.00 19.02 ATOM 513 CE2 PHE A 98 52.233 42.863 4.831 1.00 18.84 ATOM 514 CZ PHE A 98 52.291 42.786 3.451 1.00 20.99 ATOM 515 C PHE A 98 50.315 39.127 6.164 1.00 15.86 ATOM 516 O PHE A 98 51.200 38.620 5.482 1.00 15.58 ATOM 517 N ASP A 99 50.433 39.322 7.472 1.00 16.10 ATOM 518 CA ASP A 99 51.626 38.905 8.203 1.00 15.76 ATOM 519 CB ASP A 99 52.158 40.070 9.040 1.00 15.13 ATOM 520 CG ASP A 99 53.540 39.802 9.610 1.00 18.19 ATOM 521 OD1 ASP A 99 54.167 38.794 9.224 1.00 17.29 ATOM 522 OD2 ASP A 99 54.006 40.612 10.439 1.00 19.53 ATOM 523 C ASP A 99 51.228 37.729 9.101 1.00 16.25 ATOM 524 0 ASP A 99 50.995 37.894 10.300 1.00 14.46 ATOM 525 N LYS A 100 51.134 36.546 8.499 1.00 16.78 ATOM 526 CA LYS A 100 50.750 35.335 9.215 1.00 17.78 ATOM 527 CB LYS A 100 50.484 34.194 8.222 1.00 19.95 ATOM 528 CG LYS A 100 49.149 34.250 7.478 1.00 21.28 ATOM 529 CD LYS A 100 49.084 33.139 6.426 1.00 24.43 ATOM 530 CE LYS A 100 47.727 33.060 5.714 1.00 25.79 ATOM 531 NZ LYS A 100 46.644 32.486 6.578 1.00 23.81 ATOM 532 C LYS A 100 51.767 34.849 10.247 1.00 18.87

ATOM 533 0 LYS A 100 51.389 34.269 11.267 1.00 19.75 ATOM 534 N HIS A 101 53.050 35.083 9.993 1.00 18.22 ATOM 535 CA HIS A 101 54.088 34.601 10.902 1.00 20.19 ATOM 536 CB HIS A 101 55.109 33.779 10.106 1.00 17.78 ATOM 537 CG HIS A 101 54.507 33.029 8.959 1.00 18.92 ATOM 538 CD2 HIS A 101 54.760 33.081 7.629 1.00 17.74 ATOM 539 ND1 HIS A 101 53.491 32.110 9.120 1.00 18. 19 ATOM 540 CE1 HIS A 101 53.145 31.629 7.938 1.00 17.82 ATOM 541 NE2 HIS A 101 53.899 32.202 7.017 1.00 17.25 ATOM 542 C HIS A 101 54.818 35.677 11.705 1.00 20.40 ATOM 543 0 HIS A 101 55.859 35.403 12.299 1.00 22.15 ATOM 544 N GLY A 102 54.277 36.892 11.718 1.00 21.38 ATOM 545 CA GLY A 102 54.896 37.979 12.460 1.00 21.06 ATOM 546 C GLY A 102 56.275 38.379 11.969 1.00 20.98 ATOM 547 0 GLY A 102 57.179 38.593 12.768 1.00 22.33 ATOM 548 N GLU A 103 56.435 38.503 10.656 1.00 22.97 ATOM 549 CA GLU A 103 57.723 38.867 10.062 1.00 22.35 ATOM 550 CB GLU A 103 57.952 38.059 8.787 1.00 21.09 ATOM 551 CG GLU A 103 58.004 36.564 8.992 1.00 24.78 ATOM 552 CD GLU A 103 58.049 35.808 7.683 1.00 26.81 ATOM 553 OE1 GLU A 103 57.014 35.763 6.980 1.00 26.94 ATOM 554 OE2 GLU A 103 59.125 35.266 7.353 1.00 29.11 ATOM 555 C GLU A 103 57.883 40.342 9.713 1.00 21.88 ATOM 556 0 GLU A 103 58.999 40.806 9.500 1.00 22.98 ATOM 557 N ALA A 104 56.784 41.084 9.651 1.00 21.38 ATOM 558 CA ALA A 104 56.870 42.491 9.269 1.00 20.31 ATOM 559 CB ALA A 104 56.378 42.650 7.841 1.00 17.37 ATOM 560 C ALA A 104 56.116 43.451 10.175 1.00 19.53 ATOM 561 O ALA A 104 55.704 44.523 9.738 1.00 18.99 ATOM 562 N VAL A 105 55.945 43.079 11.436 1.00 19.90 ATOM 563 CA VAL A 105 55.216 43.924 12.375 1.00 19.69 ATOM 564 CB VAL A 105 55.345 43.387 13.808 1.00 19.43 ATOM 565 CG1 VAL A 105 54.673 44.339 14.779 1.00 17.75 ATOM 566 CG2 VAL A 105 54.725 41.997 13.892 1.00 17.02 ATOM 567 C VAL A 105 55.660 45.386 12.361 1.00 20.42 ATOM 568 0 VAL A 105 54.831 46.293 12.260 1.00 21.86 ATOM 569 N ASP A 106 56.965 45.615 12.454 1.00 18.26

ATOM 570 CA ASP A 106 57.489 46.975 12.472 1.00 19.05 ATOM 571 CB ASP A 106 58.962 46.960 12.888 1.00 18.62 ATOM 572 CG ASP A 106 59.144 46.470 14.308 1.00 19.89 ATOM 573 OD1 ASP A 106 59.732 45.383 14.502 1.00 21.15 ATOM 574 OD2 ASP A 106 58.677 47.171 15.231 1.00 19.02 ATOM 575 C ASP A 106 57.315 47.721 11.158 1.00 18.20 ATOM 576 O ASP A 106 57.043 48.924 11.154 1.00 18.32 ATOM 577 N GLY A 107 57.474 47. 013 10.048 1.00 15.97 ATOM 578 CA GLY A 107 57.300 47.645 8.756 1.00 16.89 ATOM 579 C GLY A 107 55.847 48.039 8.558 1.00 18.68 ATOM 580 0 GLY A 107 55.542 48.944 7.781 1.00 20.07 ATOM 581 N LEU A 108 54.945 47.361 9.265 1.00 17.60 ATOM 582 CA LEU A 108 53.519 47.655 9.163 1.00 17. 75 ATOM 583 CB LEU A 108 52.694 46.456 9.649 1.00 18.20 ATOM 584 CG LEU A 108 52.741 45.283 8.662 1.00 17.32 ATOM 585 CD1 LEU A 108 52.194 44.020 9.297 1.00 15.87 ATOM 586 CD2 LEU A 108 51.954 45.655 7.415 1.00 18.07 ATOM 587 C LEU A 108 53.150 48.923 9.931 1.00 17.52 ATOM 588 O LEU A 108 52.326 49.706 9.465 1.00 17.59 ATOM 589 N TYR A 109 53.747 49.132 11.103 1.00 17.99 ATOM 590 CA TYR A 109 53.475 50.356 11.863 1.00 19.57 ATOM 591 CB TYR A 109 54.181 50.346 13.231 1.00 17.67 ATOM 592 CG TYR A 109 53.572 49.412 14.257 1.00 15.68 ATOM 593 CD1 TYR A 109 54.319 48.386 14.818 1.00 15.06 ATOM 594 CE1 TYR A 109 53.761 47.514 15.739 1.00 16.14 ATOM 595 CD2 TYR A 109 52.244 49.546 14.649 1.00 14.34 ATOM 596 CE2 TYR A 109 51.677 48.681 15.571 1.00 14.45 ATOM 597 CZ TYR A 109 52.439 47.665 16.110 1.00 16.08 ATOM 598 OH TYR A 109 51.877 46.785 17.006 1.00 15.83 ATOM 599 C TYR A 109 54.017 51.522 11.039 1.00 20.38 ATOM 600 0 TYR A 109 53.438 52.610 11.014 1.00 20.47 ATOM 601 N LYS A 110 55.138 51.285 10.365 1.00 20.32 ATOM 602 CA LYS A 110 55.761 52.310 9.542 1.00 22.38 ATOM 603 CB LYS A 110 57.145 51.851 9.077 1.00 22.88 ATOM 604 CG LYS A 110 57.824 52.849 8.162 1.00 26.65 ATOM 605 CD LYS A 110 59.186 52.374 7.706 1.00 30.71 ATOM 606 CE LYS A 110 59.848 53.417 6.812 1.00 33.71

ATOM 607 NZ LYS A 110 61.216 53.007 6.386 1.00 37.17 ATOM 608 C LYS A 110 54.900 52.651 8.327 1.00 22.82 ATOM 609 O LYS A 110 55.035 53.729 7.742 1.00 21.86 ATOM 610 N MET A 111 54.020 51.726 7.953 1.00 22.62 ATOM 611 CA MET A 111 53.134 51.921 6.810 1.00 21.33 ATOM 612 CB MET A 111 52.596 50.568 6.330 1.00 22.37 ATOM 613 CG MET A 111 52.116 50.555 4.883 1.00 23.26 ATOM 614 SD MET A 111 51.647 48.908 4.295 1.00 22.91 ATOM 615 CE MET A 111 53.239 48.159 4.039 1.00 22.34 ATOM 616 C MET A 111 51.979 52.849 7.198 1.00 21.50 ATOM 617 O MET A 111 51.237 53.332 6.341 1.00 21.61 ATOM 618 N GLY A 112 51.829 53.095 8.497 1.00 20.35 ATOM 619 CA GLY A 112 50.774 53.981 8.954 1.00 18.20 ATOM 620 C GLY A 112 49.652 53.346 9.754 1.00 17.70 ATOM 621 O GLY A 112 48.757 54.049 10.222 1.00 18.34 ATOM 622 N PHE A 113 49.687 52.027 9.922 1.00 15.93 ATOM 623 CA PHE A 113 48.640 51.340 10.676 1.00 15.61 ATOM 624 CB PHE A 113 48.761 49.824 10.503 1.00 15.10 ATOM 625 CG PHE A 113 48.390 49.340 9.132 1.00 15.46 ATOM 626 CD1 PHE A 113 49.361 48.889 8.254 1.00 15.32 ATOM 627 CD2 PHE A 113 47.064 49.328 8.724 1.00 15.07 ATOM 628 CE1 PHE A 113 49.017 48.428 6.991 1.00 17.40 ATOM 629 CE2 PHE A 113 46.710 48.870 7.464 1.00 15.20 ATOM 630 CZ PHE A 113 47.687 48.418 6.596 1.00 16.29 ATOM 631 C PHE A 113 48.664 51.686 12.157 1.00 14.59 ATOM 632 O PHE A 113 49.726 51.750 12.768 1.00 15.40 ATOM 633 N GLY A 114 47.482 51.908 12.726 1.00 13.85 ATOM 634 CA GLY A 114 47.372 52.246 14.136 1.00 13.80 ATOM 635 C GLY A 114 47.582 51.040 15.032 1.00 15.27 ATOM 636 0 GLY A 114 47.808 51.175 16.232 1.00 16.43 ATOM 637 N PHE A 115 47.479 49.850 14.452 1.00 15.37 ATOM 638 CA PHE A 115 47.692 48.623 15.199 1.00 15.37 ATOM 639 CB PHE A 115 46.548 48.373 16.197 1.00 15.72 ATOM 640 CG PHE A 115 45.216 48.075 15.568 1.00 14.48 ATOM 641 CD1 PHE A 115 44.723 46.781 15.547 1.00 13.96 ATOM 642 CD2 PHE A 115 44.431 49.096 15.050 1.00 14.85 ATOM 643 CE1 PHE A 115 43.468 46.505 15.026 1.00 13.14

ATOM 644 CE2 PHE A 115 43.174 48.828 14.526 1.00 14.58 ATOM 645 CZ PHE A 115 42.694 47.528 14.516 1.00 14.33 ATOM 646 C PHE A 115 47.865 47.457 14.240 1.00 15.74 ATOM 647 0 PHE A 115 47.335 47.467 13.132 1.00 15.07 ATOM 648 N VAL A 116 48.636 46.463 14.668 1.00 16.41 ATOM 649 CA VAL A 116 48.926 45.301 13.844 1.00 15.02 ATOM 650 CB VAL A 116 50.460 45.168 13.617 1.00 15.50 ATOM 651 CG1 VAL A 116 50.778 43.903 12.810 1.00 11.14 ATOM 652 CG2 VAL A 116 50.992 46.415 12.911 1.00 13.00 ATOM 653 C VAL A 116 48.422 43.998 14.450 1.00 16.38 ATOM 654 0 VAL A 116 48.447 43.815 15.669 1.00 16.18 ATOM 655 N GLU A 117 47.957 43.100 13.585 1.00 16.09 ATOM 656 CA GLU A 117 47.487 41.786 14.007 1.00 17.47 ATOM 657 CB GLU A 117 45. 975-41. 659 13.838 1.00 15.90 ATOM 658 CG GLU A 117 45.431 40.316 14.303 1.00 16.28 ATOM 659 CD GLU A 117 43.919 40.264 14.271 1.00 17.25 ATOM 660 OE1 GLU A 117 43.365 39.320 13.664 1.00 15.76 ATOM 661 OE2 GLU A 117 43.291 41.171 14.856 1.00 14.09 ATOM 662 C GLU A 117 48.188 40.778 13.109 1.00 17.93 ATOM 663 0 GLU A 117 48.071 40.850 11.886 1.00 19.54 ATOM 664 N ILE A 118 48.921 39.840 13.697 1.00 17.75 ATOM 665 CA ILE A 118 49.626 38.874 12.873 1.00 20.53 ATOM 666 CB ILE A 118 50.982 38.474 13.503 1.00 18.57 ATOM 667 CG2 ILE A 118 51.865 39.707 13.612 1.00 20.32 ATOM 668 CG1 ILE A 118 50.790 37.870 14.887 1.00 18.39 ATOM 669 CD1 ILE A 118 52.086 37.427 15.508 1.00 18.60 ATOM 670 C ILE A 118 48.782 37.649 12.554 1.00 21.57 ATOM 671 0 ILE A 118 48.186 37.040 13.441 1.00 19.31 ATOM 672 N GLY A 119 48.730 37.343 11.255 1.00 26.73 ATOM 673 CA GLY A 119 47.954 36.242 10.701 1.00 23.17 ATOM 674 C GLY A 119 47.786 35.075 11.630 1.00 24.76 ATOM 675 0 GLY A 119 48.553 34.929 12.584 1.00 25.45 ATOM 676 N SER A 120 46.791 34.236 11.348 1.00 22.08 ATOM 677 CA SER A 120 46.528 33.078 12.191 1.00 20.62 ATOM 678 CB SER A 120 45.364 32.255 11.634 1.00 20.16 ATOM 679 OG SER A 120 44.124 32.899 11.883 1.00 19.34 ATOM 680 C SER A 120 47. 746 32.192 12.354 1.00 19.19

ATOM 681 0 SER A 120 48.446 31.888 11.389 1.00 19.88 ATOM 682 N VAL A 121 47.990 31.786 13.593 1.00 18.69 ATOM 683 CA VAL A 121 49.112 30.922 13.930 1.00 15.40 ATOM 684 CB VAL A 121 50.010 31.571 15.016 1.00 15.21 ATOM 685 CG1 VAL A 121 51.319 30.784 15.169 1.00 9.68 ATOM 686 CG2 VAL A 121 50.281 33.032 14.663 1.00 12.28 ATOM 687 C VAL A 121 48.534 29.624 14.485 1.00 16.35 ATOM 688 0 VAL A 121 47.607 29.646 15.300 1.00 15.33 ATOM 689 N THR A 122 49.067 28.497 14.028 1.00 15.14 ATOM 690 CA THR A 122 48.617 27.194 14.495 1.00 16.81 ATOM 691 CB THR A 122 48.447 26.210 13.308 1.00 16.39 ATOM 692 OG1 THR A 122 49.671 26.118 12.572 1.00 16.99 ATOM 693 CG2 THR A 122 47.351 26. 701. 12.372 1.00 16.20 ATOM 694 C THR A 122 49.668 26.680 15.480 1.00 16.05 ATOM 695 0 THR A 122 50.811 27.120 15.446 1.00 17.14 ATOM 696 N PRO A 123 49.289 25. 768 16.390 1.00 17.33 ATOM 697 CD PRO A 123 47.925 25.295 16.685 1.00 16.88 ATOM 698 CA PRO A 123 50.249 25.234 17.369 1.00 18.81 ATOM 699 CB PRO A 123 49.423 24.203 18.128 1.00 17.77 ATOM 700 CG PRO A 123 48.054 24.837 18.126 1.00 17.60 ATOM 701 C PRO A 123 51.500 24.634 16.732 1.00 20.92 ATOM 702 0 PRO A 123 52.625 25.008 17.074 1.00 21.41 ATOM 703 N LYS A 124 51.300 23.700 15.810 1.00 21.70 ATOM 704 CA LYS A 124 52.413 23.074 15.113 1.00 23.21 ATOM 705 CB LYS A 124 52.190 21.561 14.967 1.00 26.03 ATOM 706 CG LYS A 124 51.885 20.840 16.270 1.00 30.90 ATOM 707 CD LYS A 124 52. 954 21.122 17.314 1.00 36.86 ATOM 708 CE LYS A 124 52.546 20.585 18.679 1.00 41.85 ATOM 709 NZ LYS A 124 53.576 20.858 19.723 1.00 43.99 ATOM 710 C LYS A 124 52.482 23.701 13.732 1.00 23.17 ATOM 711 0 LYS A 124 51.500 24.267 13.245 1.00 23.15 ATOM 712 N PRO A 125 53.651 23.629 13.087 1.00 21.56 ATOM 713 CD PRO A 125 54.955 23.187 13.617 1.00 21.14 ATOM 714 CA PRO A 125 53.785 24.204 11.748 1.00 20.21 ATOM 715 CB PRO A 125 55.288 24.096 11.470 1.00 20.65 ATOM 716 CG PRO A 125 55.917 24.036 12.842 1.00 19.52 ATOM 717 C PRO A 125 52.972 23.351 10.766 1.00 19.97

ATOM 718 0 PRO A 125 52.731 22.172 11.016 1.00 18.81 ATOM 719 N GLN A 126 52.539 23.951 9.664 1.00 19.59 ATOM 720 CA GLN A 126 51.802 23.224 8.634 1.00 20.28 ATOM 721 CB GLN A 126 50.354 22.921 9.064 1.00 21.32 ATOM 722 CG GLN A 126 49.449 24.115 9.324 1.00 20.84 ATOM 723 CD GLN A 126 47.998 23.694 9.555 1.00 22.01 ATOM 724 OE1 GLN A 126 47.718 22.753 10. 309 1.00 19.72 ATOM 725 NE2 GLN A 126 47.070 24.398 8.914 1.00 20.71 ATOM 726 C GLN A 126 51.840 24.032 7.343 1.00 20.63 ATOM 727 0 GLN A 126 51.800 25.260 7.366 1.00 20.52 ATOM 728 N GLU A 127 51.932 23.332 6.220 1.00 23.02 ATOM 729 CA GLU A 127 52.034 23.978 4.917 1.00 26.27 ATOM 730 CB GLU A 127 52.620 22.989 3.903 1.00 30.03 ATOM 731 CG GLU A 127 53.967 22.418 4.329 1.00 37.96 ATOM 732 CD GLU A 127 54.686 21.687 3.208 1.00 43.29 ATOM 733 OE1 GLU A 127 54.069 20.799 2.577 1.00 46.06 ATOM 734 OE2 GLU A 127 55.873 21.998 2.963 1.00 45.91 ATOM 735 C GLU A 127 50.764 24.596 4.345 1.00 24.39 ATOM 736 0 GLU A 127 50.839 25.493 3.508 1.00 22.88 ATOM 737 N GLY A 128 49.604 24.131 4.791 1.00 23.27 ATOM 738 CA GLY A 128 48.365 24.667 4.263 1.00 23.54 ATOM 739 C GLY A 128 48.014 23.952 2.971 1.00 25.46 ATOM 740 0 GLY A 128 48.638 22.943 2.631 1.00 24.72 ATOM 741 N ASN A 129 47.021 24.462 2.246 1.00 25.50 ATOM 742 CA ASN A 129 46.608 23.841 0.992 1.00 25.75 ATOM 743 CB ASN A 129 45.268 24.412 0.524 1.00 24.81 ATOM 744 CG ASN A 129 44.126 24.050 1.447 1.00 25.93 ATOM 745 OD1 ASN A 129 44.056 22.927 1.948 1.00 26.55 ATOM 746 ND2 ASN A 129 43.214 24.993 1.666 1.00 21.27 ATOM 747 C ASN A 129 47.642 24.024-0. 113 1.00 26.24 ATOM 748 O ASN A 129 48.488 24.915-0. 050 1.00 25.50 ATOM 749 N PRO A 130 47.587 23.165-1. 140 1.00 26.81 ATOM 750 CD PRO A 130 46.723 21.973-1. 221 1.00 25.39 ATOM 751 CA PRO A 130 48.515 23.226-2. 274 1.00 26.99 ATOM 752 CB PRO A 130 48.284 21.887-2. 978 1.00 26.46 ATOM 753 CG PRO A 130 46.849 21. 581-2. 671 1.00 25.27 ATOM 754 C PRO A 130 48.227 24.424-3. 180 1.00 28.67

ATOM 755 0 PRO A 130 47.087 24.880-3. 263 1.00 29.58 ATOM 756 N ARG A 131 49.262 24.931-3. 846 1.00 29.41 ATOM 757 CA ARG A 131 49.124 26.075-4. 746 1.00 31.07 ATOM 758 CB ARG A 131 50.482 26.732-4. 998 1.00 32.70 ATOM 759 CG ARG A 131 51.180 27. 354-3. 797 1.00 34.79 ATOM 760 CD ARG A 131 52.260 28.298-4. 315 1.00 40.39 ATOM 761 NE ARG A 131 53.147 28.840-3. 287 1.00 45.17 ATOM 762 CZ ARG A 131 54.017 29.827-3. 508 1.00 45.61 ATOM 763 NH1 ARG A 131 54.107 30.376-4. 714 1.00 44.09 ATOM 764 NH2 ARG A 131 54.802 30.261-2. 529 1.00 45.19 ATOM 765 C ARG A 131 48.543 25.652-6. 096 1.00 32.15 ATOM 766 0 ARG A 131 48.760 24.530-6. 548 1.00 33.75 ATOM 767 N PRO A 132 47.800 26.552-6. 764 1.00 30. 94 ATOM 768 CD PRO A 132 47.331 26.344-8. 145 1.00 31.60 ATOM 769 CA PRO A 132 47.488 27.913-6. 316 1.00 28.61 ATOM 770 CB PRO A 132 47.078 28.607-7. 612 1.00 29.31 ATOM 771 CG PRO A 132 46.386 27.513-8. 350 1.00 30.17 ATOM 772 C PRO A 132 46.375 27.914-5. 268 1.00 25.00 ATOM 773 O PRO A 132 45.484 27.068-5. 296 1.00 23.59 ATOM 774 N ARG A 133 46.431 28.869-4. 347 1.00 21.85 ATOM 775 CA ARG A 133 45.438 28.952-3. 290 1.00 19.55 ATOM 776 CB ARG A 133 46.013 28.323-2. 017 1.00 21.24 ATOM 777 CG ARG A 133 47.422 28.794-1. 688 1.00 18.90 ATOM 778 CD ARG A 133 48.095 27.880-0. 678 1.00 16.85 ATOM 779 NE ARG A 133 49.426 28.373-0. 334 1.00 17.49 ATOM 780 CZ ARG A 133 50.196 27.856 0.617 1.00 15.57 ATOM 781 NH1 ARG A 133 51.389 28.377 0.861 1.00 13.29 ATOM 782 NH2 ARG A 133 49.775 26.818 1.323 1.00 15.73 ATOM 783 C ARG A 133 44.954 30.376-3. 023 1.00 19.32 ATOM 784 0 ARG A 133 44.233 30.627-2. 056 1.00 19.05 ATOM 785 N VAL A 134 45.357 31.307-3. 882 1.00 18.51 ATOM 786 CA VAL A 134 44.937 32.700-3. 763 1.00 18.75 ATOM 787 CB VAL A 134 46.058 33.613-3. 222 1.00 18.82 ATOM 788 CG1 VAL A 134 45.451 34.900-2. 680 1.00 15.57 ATOM 789 CG2 VAL A 134 46.848 32.896-2. 162 1.00 18.29 ATOM 790 C VAL A 134 44.600 33.157-5. 173 1.00 18.69 ATOM 791 O VAL A 134 45.294 32.800-6. 119 1.00 20.02

ATOM 792 N PHE A 135 43.542 33.944-5. 320 1.00 19.00 ATOM 793 CA PHE A 135 43.146 34.398-6. 643 1.00 17.47 ATOM 794 CB PHE A 135 42.059 33.476-7. 198 1.00 17.16 ATOM 795 CG PHE A 135 42.387 32.011-7. 067 1.00 17.50 ATOM 796 CD1 PHE A 135 42.102 31.325-5. 894 1.00 16.24 ATOM 797 CD2 PHE A 135 43.029 31.334-8. 097 1.00 18.52 ATOM 798 CE1 PHE A 135 42.453 29.988-5. 749 1.00 17.65 ATOM 799 CE2 PHE A 135 43.384 29.998-7. 960 1.00 16.80 ATOM 800 CZ PHE A 135 43.096 29.325-6. 784 1.00 16.83 ATOM 801 C PHE A 135 42.664 35.841-6. 657 1.00 18.35 ATOM 802 0 PHE A 135 41.996 36.303-5. 729 1.00 17.26 ATOM 803 N ARG A 136 43.026 36.554-7. 717 1.00 17.14 ATOM 804 CA ARG A 136 42.628 37.939-7. 874 1.00 17. 83 ATOM 805 CB ARG A 136 43.726 38.754-8. 567 1.00 19.09 ATOM 806 CG ARG A 136 45.089 38.802-7. 892 1.00 21.68 ATOM 807 CD ARG A 136 45.990 39.767-8. 661 1.00 23.63 ATOM 808 NE ARG A 136 47.345 39.863-8. 121 1.00 29.57 ATOM 809 CZ ARG A 136 48.412 39.256-8. 638 1.00 31.45 ATOM 810 NH1 ARG A 136 49.600 39.408-8. 070 1.00 31. 05 ATOM 811 NH2 ARG A 136 48.297 38.504-9. 726 1.00 31.93 ATOM 812 C ARG A 136 41.375 38.029-8. 739 1.00 17.93 ATOM 813 0 ARG A 136 41.218 37.266-9. 699 1.00 17.19 ATOM 814 N LEU A 137 40.488 38.953-8. 377 1.00 15.76 ATOM 815 CA LEU A 137 39.268 39.241-9. 132 1.00 14.78 ATOM 816 CB LEU A 137 38.006 38.849-8. 359 1.00 15. 58 ATOM 817 CG LEU A 137 37.574 37.378-8. 285 1.00 17.50 ATOM 818 CD1 LEU A 137 38. 617 36.547-7. 540 1.00 17.15 ATOM 819 CD2 LEU A 137 36.231 37.301-7. 580 1.00 12.95 ATOM 820 C LEU A 137 39.324 40.759-9. 273 1.00 15.42 ATOM 821 O LEU A 137 38.583 41.485-8. 608 1.00 14.16 ATOM 822 N PRO A 138 40.233 41.258-10. 126 1.00 15.71 ATOM 823 CD PRO A 138 41.193 40.490-10. 941 1.00 15.13 ATOM 824 CA PRO A 138 40.389 42.701-10. 338 1.00 16.47 ATOM 825 CB PRO A 138 41.537 42.789-11. 354 1.00 15.41 ATOM 826 CG PRO A 138 41.515 41.448-12. 048 1.00 15.79 ATOM 827 C PRO A 138 39.132 43.456-10. 773 1.00 16.15 ATOM 828 0 PRO A 138 38.948 44.611-10. 399 1.00 16.79

ATOM 829 N GLU A 139 38.263 42.814-11. 545 1.00 16.16 ATOM 830 CA GLU A 139 37.037 43.479-11. 981 1.00 17.26 ATOM 831 CB GLU A 139 36.310 42.648-13. 046 1.00 18.03 ATOM 832 CG GLU A 139 37.059 42.477-14. 367 1.00 21.85 ATOM 833 CD GLU A 139 38.073 41.340-14. 348 1.00 24.50 ATOM 834 OE1 GLU A 139 38.713 41.115-15. 397 1.00 27.97 ATOM 835 OE2 GLU A 139 38.234 40.671-13. 300 1.00 23.28 ATOM 836 C GLU A 139 36.083 43.714-10. 807 1.00 17.84 ATOM 837 O GLU A 139 35.157 44.522-10. 902 1.00 17.94 ATOM 838 N ASP A 140 36.308 43.008-9. 702 1.00 14.82 ATOM 839 CA ASP A 140 35.448 43.132-8. 531 1.00 12.95 ATOM 840 CB ASP A 140 34.943 41.749-8. 100 1.00 10.76 ATOM 841 CG ASP A 140 34.317 40.968-9. 245 1.00 13.87 ATOM 842 OD1 ASP A 140 33.260 41.395-9. 756 1.00 12.48 ATOM 843 OD2 ASP A 140 34.882 39.922-9. 635 1.00 14.76 ATOM 844 C ASP A 140 36.187 43.761-7. 362 1.00 13.94 ATOM 845 0 ASP A 140 35.609 43. 956-6. 287 1.00 12.55 ATOM 846 N GLN A 141 37.460 44.084-7. 574 1.00 14.25 ATOM 847 CA GLN A 141 38.279 44.639-6. 508 1.00 14.42 ATOM 848 CB GLN A 141 37.791 46.038-6. 125 1.00 15.62 ATOM 849 CG GLN A 141 38.168 47.096-7. 160 1.00 22.74 ATOM 850 CD GLN A 141 37.666 48.493-6. 819 1.00 25.08 ATOM 851 OE1 GLN A 141 37.883 48.998-5. 713 1.00 28.72 ATOM 852 NE2 GLN A 141 37.002 49.130-7. 779 1.00 25.38 ATOM 853 C GLN A 141 38.157 43.669-5. 336 1.00 14.40 ATOM 854 0 GLN A 141 37.979 44.067-4. 182 1.00 15.04 ATOM 855 N ALA A 142 38.244 42.380-5. 661 1.00 13.51 ATOM 856 CA ALA A 142 38.138 41.322-4. 669 1.00 13.56 ATOM 857 CB ALA A 142 36.775 40.644-4. 780 1.00 11.87 ATOM 858 C ALA A 142 39.245 40.278-4. 801 1.00 13.69 ATOM 859 O ALA A 142 39.996 40.255-5. 779 1.00 12.41 ATOM 860 N VAL A 143 39.328 39.414-3. 795 1.00 13.04 ATOM 861 CA VAL A 143 40.302 38.337-3. 753 1.00 11.89 ATOM 862 CB VAL A 143 41.527 38.696-2. 852 1.00 13.64 ATOM 863 CG1 VAL A 143 42.349 37.439-2. 551 1.00 9.11 ATOM 864 CG2 VAL A 143 42.410 39.735-3. 541 1.00 8.79 ATOM 865 C VAL A 143 39.615 37.112-3. 163 1.00 14.15

ATOM 866 o VAL A 143 38.687 37.234-2. 364 1.00 16. 13 ATOM 867 N ILE A 144 40.052 35.933-3. 585 1.00 14.22 ATOM 868 CA ILE A 144 39.522 34.685-3. 057 1.00 13.02 ATOM 869 CB ILE A 144 38.737 33.883-4. 121 1.00 13.56 ATOM 870 CG2 ILE A 144 38.571 32.429-3. 673 1.00 10.97 ATOM 871 CG1 ILE A 144 37.362 34.519-4. 339 1.00 11.41 ATOM 872 CD1 ILE A 144 36.502 33.760-5. 312 1.00 14.19 ATOM 873 C ILE A 144 40.744 33.895-2. 630 1.00 13.99 ATOM 874 0 ILE A 144 41.722 33.807-3. 378 1.00 14.68 ATOM 875 N ASN A 145 40.706 33.334-1. 428 1.00 13.97 ATOM 876 CA ASN A 145 41.846 32.571-0. 942 1.00 13.60 ATOM 877 CB ASN A 145 42.716 33.455-0. 040 1.00 13.33 ATOM 878 CG ASN A 145 42.255 33.447 1.412 1.00 16. 34 ATOM 879 OD1 ASN A 145 42.556 32.518 2.163 1.00 14.09 ATOM 880 ND2 ASN A 145 41.510 34.478 1.809 1.00 15.79 ATOM 881 C ASN A 145 41.426 31.328-0. 170 1.00 14.55 ATOM 882 0 ASN A 145 40.380 31.308 0.485 1.00 13.20 ATOM 883 N. ARG A 146 42.249 30.289-0. 262 1.00 14.22 ATOM 884 CA ARG A 146 42.011 29.047 0.458 1.00 15.92 ATOM 885 CB ARG A 146 41.327 28.007-0. 440 1.00 14.93 ATOM 886 CG ARG A 146 41.972 27.778-1. 797 1.00 14.62 ATOM 887 CD ARG A 146 41.403 26.513-2. 428 1.00 15.20 ATOM 888 NE ARG A 146 41.958 26.231-3. 751 1.00 15.82 ATOM 889 CZ ARG A 146 41.423 26.632-4. 903 1.00 16.69 ATOM 890 NH1 ARG A 146 40.305 27.344-4. 917 1.00 16.41 ATOM 891 NH2 ARG A 146 42.008 26.311-6. 050 1.00 18.44 ATOM 892 C ARG A 146 43.352 28.519 0.965 1.00 18.18 ATOM 893 O ARG A 146 43.697 27.355 0.758 1.00 18.08 ATOM 894 N TYR A 147 44.104 29.394 1.632 1.00 18.01 ATOM 895 CA TYR A 147 45.410 29.039 2.171 1.00 19.04 ATOM 896 CB TYR A 147 45.993 30.199 2.979 1.00 18.66 ATOM 897 CG TYR A 147 46.860 31.121 2.166 1.00 18.81 ATOM 898 CD1 TYR A 147 46.405 32.371 1.774 1.00 19.25 ATOM 899 CE1 TYR A 147 47.196 33.208 1.007 1.00 22.14 ATOM 900 CD2 TYR A 147 48.135 30.728 1.768 1.00 20.06 ATOM 901 CE2 TYR A 147 48.933 31.555 1.000 1.00 21.49 ATOM 902 CZ TYR A 147 48.458 32.793 0.624 1.00 22.84

ATOM 903 OH TYR A 147 49.244 33.617-0. 147 1.00 28.55 ATOM 904 C TYR A 147 45.381 27.795 3.042 1.00 19.59 ATOM 905 O TYR A 147 46.232 26.917 2.903 1.00 21.39 ATOM 906 N GLY A 148 44.409 27.732 3.946 1.00 19.48 ATOM 907 CA GLY A 148 44.288 26.589 4.830 1.00 17.98 ATOM 908 C GLY A 148 45.183 26.683 6.052 1.00 19.49 ATOM 909 0 GLY A 148 45.692 25.671 6.534 1.00 20.15 ATOM 910 N PHE A 149 45.389 27.897 6.551 1.00 19.05 ATOM 911 CA PHE A 149 46.218 28.097 7.738 1.00 19.22 ATOM 912 CB PHE A 149 45.632 27.334 8.935 1.00 18.23 ATOM 913 CG PHE A 149 44.456 28.009 9.586 1.00 19.24 ATOM 914 CD1 PHE A 149 43.609 27.289 10.423 1.00 20.94 ATOM 915 CD2 PHE A 149 44.203 29.354 9.386 1.00 20. 56 ATOM 916 CE1 PHE A 149 42.529 27.903 11.046 1.00 22.07 ATOM 917 CE2 PHE A 149 43.124 29.976 10.007 1.00 21.74 ATOM 918 CZ PHE A 149 42.286 29.251 10.836 1.00 21.98 ATOM 919 C PHE A 149 47.678 27.673 7.569 1.00 19.04 ATOM 920 O PHE A 149 48.191 26.895 8.370 1. 00 20. 36 ATOM 921 N ASN A 150 48.346 28.150 6.527 1.00 17.55 ATOM 922 CA ASN A 150 49.753 27.821 6.369 1.00 18.25 ATOM 923 CB ASN A 150 50.277 28.309 5.013 1.00 16.65 ATOM 924 CG ASN A 150 49.959 29.768 4.752 1.00 18.63 ATOM 925 OD1 ASN A 150 48.805 30.191 4.846 1.00 18.40 ATOM 926 ND2 ASN A 150 50.981 30.544 4.409 1.00 17.11 ATOM 927 C ASN A 150 50.389 28.597 7.524 1.00 19.71 ATOM 928 0 ASN A 150 50.140 29.793 7.676 1.00 20.26 ATOM 929 N SER A 151 51.188 27.925 8.346 1.00 18.09 ATOM 930 CA SER A 151 51.781 28.589 9.498 1.00 18.68 ATOM 931 CB SER A 151 50.775 28.556 10.655 1.00 17.80 ATOM 932 OG SERA 151 51.372 28.931 11.883 1.00 16.50 ATOM 933 C SER A 151 53.117 28.017 9.974 1.00 19.15 ATOM 934 0 SER A 151 53.339 26.802 9.931 1.00 18.28 ATOM 935 N HIS A 152 53.992 28.911 10.438 1.00 18.31 ATOM 936 CA HIS A 152 55.307 28.532 10.956 1.00 18.93 ATOM 937 CB HIS A 152 56.217 29.762 11.083 1.00 18.91 ATOM 938 CG HIS A 152 56.661 30.333 9.771 1.00 21.17 ATOM 939 CD2 HIS A 152 56. 387 29.964 8.496 1.00 21.16

ATOM 940 ND1 HIS A 152 57.499 31.424 9.681 1.00 22.49 ATOM 941 CE1 HIS A 152 57.721 31.704 8.409 1.00 20.95 ATOM 942 NE2 HIS A 152 57.058 30.833 7.669 1.00 22.06 ATOM 943 C HIS A 152 55.165 27.877 12.329 1.00 18.38 ATOM 944 0 HIS A 152 56.096 27.235 12.818 1.00 17.60 ATOM 945 N GLY A 153 54.001 28.053 12.953 1.00 17.75 ATOM 946 CA GLY A 153 53.774 27.460 14.259 1.00 16.61 ATOM 947 C GLY A 153 54.052 28.398 15.419 1.00 15.59 ATOM 948 O GLY A 153 54.717 29.419 15.262 1.00 13.71 ATOM 949 N LEU A 154 53.546 28.035 16.592 1.00 15.84 ATOM 950 CA LEU A 154 53.713 28.837 17.799 1.00 16.70 ATOM 951 CB LEU A 154 52.984 28.164 18.970 1.00 13.15 ATOM 952 CG LEU A 154 51.456 28.175 18.853 1.00 14.44 ATOM 953 CD1 LEU A 154 50.819 27.344 19.964 1.00 9.83 ATOM 954 CD2 LEU A 154 50.969 29.622 18.911 1.00 12.21 ATOM 955 C LEU A 154 55.167 29.127 18.189 1.00 17.86 ATOM 956 0 LEU A 154 55.521 30.286 18.426 1.00 18.59 ATOM 957 N SER A 155 56.001 28.088 18.264 1.00 17.56 ATOM 958 CA SER A 155 57.410 28.262 18.638 1.00 19.51 ATOM 959 CB SER A 155 58.181 26.944 18.510 1.00 17.58 ATOM 960 OG SER A 155 57.825 26.045 19.536 1.00 26.25 ATOM 961 C SER A 155 58.139 29.320 17.816 1.00 19.49 ATOM 962 0 SER A 155 58.681 30.283 18.366 1.00 19.42 ATOM 963 N VAL A 156 58.171 29.131 16.500 1.00 17.97 ATOM 964 CA VAL A 156 58.856 30.081 15.640 1.00 19.36 ATOM 965 CB VAL A 156 58.746 29.679 14.152 1.00 19.76 ATOM 966 CG1 VAL A 156 59.197 30.834 13.270 1.00 18.20 ATOM 967 CG2 VAL A 156 59.616 28.452 13.884 1.00 15.89 ATOM 968 C VAL A 156 58.346 31.509 15.821 1.00 19.10 ATOM 969 0 VAL A 156 59.141 32.440 15.945 1.00 21.48 ATOM 970 N VAL A 157 57.029 31.686 15.846 1.00 17.35 ATOM 971 CA VAL A 157 56.465 33.021 16.013 1.00 17.52 ATOM 972 CB VAL A 157 54.927 33.012 15.806 1.00 18.44 ATOM 973 CG1 VAL A 157 54.354 34.404 16.046 1.00 15.23 ATOM 974 CG2 VAL A 157 54.600 32.545 14.393 1.00 16.29 ATOM 975 C VAL A 157 56.792 33.557 17.404 1.00 17.04 ATOM 976 0 VAL A 157 57. 067 34.742 17.576 1.00 16.81

ATOM 977 N GLU A 158 56.770 32.668 18.393 1.00 18.06 ATOM 978 CA GLU A 158 57.073 33.031 19.772 1.00 17.48 ATOM 979 CB GLU A 158 57.027 31.784 20.657 1.00 18.28 ATOM 980 CG GLU A 158 57.403 32.037 22.108 1.00 20.80 ATOM 981 CD GLU A 158 57.983 30.802 22. 777 1.00 22.98 ATOM 982 OE1 GLU A 158 57.303 29.760 22.803 1.00 27.17 ATOM 983 OE2 GLU A 158 59.123 30.871 23.276 1.00 24.43 ATOM 984 C GLU A 158 58.456 33.679 19.877 1.00 16.66 ATOM 985 0 GLU A 158 58.604 34.773 20.423 1.00 15.53 ATOM 986 N HIS A 159 59.467 32.999 19.350 1.00 16. 18 ATOM 987 CA HIS A 159 60.831 33.515 19.395 1.00 18.93 ATOM 988 CB HIS A 159 61.809 32.435 18.925 1.00 20.44 ATOM 989 CG HIS A 159 61.858 31.248 19.833 1.00 25. 76 ATOM 990 CD2 HIS A 159 62.038 31.161 21.173 1.00 26.46 ATOM 991 ND1 HIS A 159 61.666 29.957 19.388 1.00 29.18 ATOM 992 CE1 HIS A 159 61.723 29.127 20.414 1.00 29.23 ATOM 993 NE2 HIS A 159 61.947 29.832 21.508 1.00 30.03 ATOM 994 C HIS A 159 60.986 34.772 18.555 1.00 17.73 ATOM 995 0 HIS A 159 61.760 35.664 18.892 1.00 18.91 ATOM 996 N ARG A 160 60.237 34.840 17.465 1.00 17.89 ATOM 997 CA ARG A 160 60.281 35.990 16.574 1.00 19.60 ATOM 998 CB ARG A 160 59.516 35.652 15.293 1.00 20.86 ATOM 999 CG ARG A 160 59.537 36.703 14.206 1.00 21.57 ATOM'1000 CD ARG A 160 58.928 36.111 12.933 1.00 24.64 ATOM 1001 NE ARG A 160 59.805 35.113 12.323 1.00 23.48 ATOM 1002 CZ ARG A 160 59.388 34.084 11.587 1.00 24.74 ATOM 1003 NH1 ARG A 160 58.092 33.895 11.365 1.00 22.08 ATOM 1004 NH2 ARG A 160 60.273 33.250 11.056 1.00 21.93 ATOM 1005 C ARG A 160 59.693 37.227 17.269 1.00 20. 13 ATOM 1006 0 ARG A 160 60.167 38.346 17.069 1.00 20.73 ATOM 1007 N LEU A 161 58.669 37.030 18.093 1.00 19.56 ATOM 1008 CA LEU A 161 58.073 38.154 18.812 1.00 19.51 ATOM 1009 CB LEU A 161 56.632 37.833 19.226 1.00 19.35 ATOM 1010 CG LEU A 161 55.606 37.704 18.092 1.00 20.03 ATOM 1011 CD1 LEU A 161 54.225 37.460 18.685 1.00 18. 09 ATOM 1012 CD2 LEU A 161 55.599 38.974 17.248 1.00 16. 90 ATOM 1013 C LEU A 161 58.911 38.497 20.048 1.00 18.36

ATOM 1014 0 LEU A 161 58.990 39.654 20.454 1.00 17.75 ATOM 1015 N ARG A 162 59.545 37.489 20.640 1.00 17.94 ATOM 1016 CA ARG A 162 60.385 37.717 21.814 1.00 17.80 ATOM 1017 CB ARG A 162 60.853 36.392 22.412 1.00 16.66 ATOM 1018 CG ARG A 162 59.814 35.688 23.264 1.00 17.05 ATOM 1019 CD ARG A 162 60.431 34.482 23.946 1.00 16.29 ATOM 1020 NE ARG A 162 59.503 33.831 24.862 1.00 15.68 ATOM 1021 CZ ARG A 162 59.806 32.758 25.584 1.00 16.71 ATOM 1022 NH1 ARG A 162 61.018 32.219 25.493 1.00 15.01 ATOM 1023 NH2 ARG A 162 58.900 32.220 26.391 1.00 16.25 ATOM 1024 C ARG A 162 61.605 38.566 21.482 1.00 17.51 ATOM 1025 O ARG A 162 62.080 39.329 22.320 1.00 17.44 ATOM 1026 N ALA A 163 62.106 38.431 20.258 1.00 17.07 ATOM 1027 CA ALA A 163 63.275 39.188 19.825 1.00 16.71 ATOM 1028 CB ALA A 163 63.727 38.711 18.450 1.00 15.44 ATOM 1029 C ALA A 163 62.998 40.688 19.786 1.00 16.78 ATOM 1030 O ALA A 163 63.927 41.489 19.687 1.00 14.49 ATOM 1031 N ARG A 164 61.723 41.062 19.867 1.00 17.00 ATOM 1032 CA ARG A 164 61.334 42.468 19.834 1.00 18.86 ATOM 1033 CB ARG A 164 60.782 42.836 18.451 1.00 19.13 ATOM 1034 CG ARG A 164 59.511 42.079 18.068 1.00 19.61 ATOM 1035 CD ARG A 164 59.029 42.462 16.674 1.00 17.87 ATOM 1036 NE ARG A 164 58.541 43.837 16.610 1.00 17.41 ATOM 1037 CZ ARG A 164 57.361 44.237 17.074 1.00 19.05 ATOM 1038 NH1 ARG A 164 56.533 43.364 17.639 1.00 17.96 ATOM 1039 NH2 ARG A 164 57.004 45.511 16.970 1.00 18.08 ATOM 1040 C ARG A 164 60.278 42.776 20.882 1.00 19.19 ATOM 1041 0 ARG A 164 59.597 43.797 20.795 1.00 19.50 ATOM 1042 N GLN A 165 60.152 41.900 21.874 1.00 20.49 ATOM 1043 CA GLN A 165 59.155 42.073 22.924 1.00 20.58 ATOM 1044 CB GLN A 165 59.274 40.936 23.954 1.00 20.12 ATOM 1045 CG GLN A 165 58.313 41.046 25.145 1.00 21.82 ATOM 1046 CD GLN A 165 58.141 39.729 25.904 1.00 22.47 ATOM 1047 OE1 GLN A 165 59.064 38.921 25.994 1.00 22.27 ATOM 1048 NE2 GLN A 165 56.954 39.520 26.464 1.00 21.18 ATOM 1049 C GLN A 165 59.205 43.433 23.623 1.00 21.76 ATOM 1050 0 GLN A 165 58. 161 44.037 23.888 1.00 22.56

ATOM 1051 N GLN A 166 60.405 43.926 23.914 1.00 21.90 ATOM 1052 CA GLN A 166 60.533 45.209 24.595 1.00 22.73 ATOM 1053 CB GLN A 166 61.931 45.366 25.194 1.00 25.53 ATOM 1054 CG GLN A 166 62. 185 44.389 26.321 1.00 27.06 ATOM 1055 CD GLN A 166 61.005 44.313 27.268 1.00 28.22 ATOM 1056 OE1 GLN A 166 60.585 45.321 27.834 1.00 28.38 ATOM 1057 NE2 GLN A 166 60.456 43.116 27.437 1.00 29.05 ATOM 1058 C GLN A 166 60.218 46.382 23.693 1.00 22.07 ATOM 1059 0 GLN A 166 59.645 47.378 24.138 1.00 20.88 ATOM 1060 N LYS A 167 60.597 46.271 22.425 1.00 21.93 ATOM 1061 CA LYS A 167 60.307 47.334 21.478 1.00 21.45 ATOM 1062 CB LYS A 167 60.884 47.006 20.101 1.00 21.05 ATOM 1063 CG LYS A 167 60.402 47.954 19.027 1.00 25.54 ATOM 1064 CD LYS A 167 60. 905 47.574 17.648 1.00 30.01 ATOM 1065 CE LYS A 167 62.375 47.894 17.486 1.00 33.62 ATOM 1066 NZ LYS A 167 62.788 47.798 16.057 1.00 36.58 ATOM 1067 C LYS A 167 58.787 47.467 21.379 1.00 20.51 ATOM 1068 0 LYS A 167 58.248 48.574 21.405 1.00 20.50 ATOM 1069 N GLN A 168 58.102 46.330 21.274 1.00 19.09 ATOM 1070 CA GLN A 168 56.646 46.330 21.172 1.00 18.76 ATOM 1071 CB GLN A 168 56.114 44.906 20.982 1.00 17.10 ATOM 1072 CG GLN A 168 54.593 44.830 20.823 1.00 17.73 ATOM 1073 CD GLN A 168 54.072 45.640 19.636 1.00 18.32 ATOM 1074 OE1 GLN A 168 54.439 45.390 18.483 1.00 17.02 ATOM 1075 NE2 GLN A 168 53.210 46.615 19.918 1.00 16.42 ATOM 1076 C GLN A 168 56.027 46.954 22.413 1.00 17.97 ATOM 1077 0 GLN A168 55.049 47.689 22.315 1.00 17.66 ATOM 1078 N ALA A 169 56.608 46.678 23.579 1.00 17.93 ATOM 1079 CA ALA A 169 56.089 47.243 24.824 1.00 18.74 ATOM 1080 CB ALA A 169 56.957 46.817 26.005 1.00 18.28 ATOM 1081 C ALA A 169 56.042 48.766 24.728 1.00 18.92 ATOM 1082 0 ALA A 169 55.083 49.394 25.177 1.00 19.50 ATOM 1083 N LYS A 170 57.078 49.359 24.143 1.00 19.73 ATOM 1084 CA LYS A 170 57.122 50.809 23.992 1.00 22.09 ATOM 1085 CB LYS A 170 58.536 51.278 23.637 1.00 23.45 ATOM 1086 CG LYS A 170 59.524 51.155 24.791 1.00 28.29 ATOM 1087 CD LYS A 170 60.839 51.866 24.492 1.00 30.12

ATOM 1088 CE LYS A 170 61.786 51.792 25. 680 1.00 30.79 ATOM 1089 NZ LYS A 170 62.112 50.377 26.041 1.00 34.64 ATOM 1090 C LYS A 170 56.138 51.275 22.925 1.00 20.81 ATOM 1091 O LYS A 170 55.509 52.321 23.072 1.00 20.80 ATOM 1092 N LEU A 171 56.010 50.499 21.852 1.00 19.17 ATOM 1093 CA LEU A 171 55.082 50.839 20.778 1.00 18.67 ATOM 1094 CB LEU A 171 55.199 49.823 19. 639 1.00 17.59 ATOM 1095 CG LEU A 171 56.489 49.947 18.823 1.00 16.99 ATOM 1096 CD1 LEU A 171 56.702 48.707 17.965 1.00 12.77 ATOM 1097 CD2 LEU A 171 56.411 51.210 17.968 1.00 14.39 ATOM 1098 C LEU A 171 53.651 50.867 21.315 1.00 18.05 ATOM 1099 O LEU A 171 52.890 51.797 21.040 1.00 15.95 ATOM 1100 N THR A 172 53.295 49.845 22.088 1.00 18.35 ATOM 1101 CA THR A 172 51.964 49.756 22.677 1.00 19.52 ATOM 1102 CB THR A 172 51.801 48.442 23.473 1.00 17.84 ATOM 1103 OG1 THR A 172 51.889 47.330 22.572 1.00 16.09 ATOM 1104 CG2 THR A 172 50.456 48.409 24.186 1.00 14.72 ATOM 1105 C THR A 172 51.708 50.956 23.595 1.00 21.19 ATOM 1106 0 THR A 172 50.658 51.596 23.517 1.00 19.87 ATOM 1107 N GLU A 173 52.675 51.263 24.454 1.00 23.39 ATOM 1108 CA GLU A 173 52.553 52.398 25.362 1.00 26.67 ATOM 1109 CB GLU A 173 53.799 52.506 26.246 1.00 30.55 ATOM 1110 CG GLU A 173 53.745 53.637 27.265 1.00 38.76 ATOM 1111 CD GLU A 173 52.656 53.438 28.317 1.00 43.68 ATOM 1112 OE1 GLU A 173 52.394 54.389 29.089 1.00 44.95 ATOM 1113 OE2 GLU A 173 52.067 52.333 28.378 1.00 45.55 ATOM 1114 C GLU A 173 52.396 53.673 24.533 1.00 26.37 ATOM 1115 0 GLU A 173 51.811 54.657 24.982 1.00 25.62 ATOM 1116 N ASP A 174 52.918 53.637 23.313 1.00 27.07 ATOM 1117 CA ASP A 174 52.845 54.772 22.405 1.00 28.13 ATOM 1118 CB ASP A 174 54.059 54.770 21. 481 1.00 32.94 ATOM 1119 CG ASP A 174 54.971 55.946 21.724 1.00 38.63 ATOM 1120 OD1 ASP A 174 54.537 57.094 21.468 1.00 40.07 ATOM 1121 OD2 ASP A 174 56.117 55.722 22.176 1.00 40. 59 ATOM 1122 C ASP A 174 51.570 54.793 21.560 1.00 27.18 ATOM 1123 O ASP A 174 51.445 55. 610 20.649 1.00 27.16 ATOM 1124 N GLY A 175 50.636 53.892 21.851 1.00 24.85

ATOM 1125 CA GLY A 175 49.393 53.856 21.100 1.00 24.01 ATOM 1126 C GLY A 175 49.405 52. 977 19.860 1.00 23.65 ATOM 1127 O GLY A 175 48.579 53.159 18.965 1.00 23.96 ATOM 1128 N LEU A 176 50.330 52.021 19.804 1.00 22.56 ATOM 1129 CA LEU A 176 50.439 51.117 18.658 1.00 20.60 ATOM 1130 CB LEU A 176 51.726 51.419 17.887 1.00 19.76 ATOM 1131 CG LEU A 176 51.773 52.805 17.236 1.00 20.88 ATOM 1132 CD1 LEU A 176 53.156 53.073 16.645 1.00 20.36 ATOM 1133 CD2 LEU A 176 50.698 52.885 16.155 1.00 21.58 ATOM 1134 C LEU A 176 50.422 49.654 19.107 1.00 19.32 ATOM 1135 O LEU A 176 51.444 48.968 19.071 1.00 19.23 ATOM 1136 N PRO A 177 49.241 49.160 19.520 1.00 17.22 ATOM 1137 CD PRO A 177 48.007 49.957 19.601 1.00 14.81 ATOM 1138 CA PRO A 177 49.000 47.795 19.998 1.00 16.26 ATOM 1139 CB PRO A 177 47.534 47.831 20.437 1.00 16.17 ATOM 1140 CG PRO A 177 47.281 49.277 20.721 1.00 15.79 ATOM 1141 C PRO A 177 49.264 46.660 19.003 1.00 15.92 ATOM 1142 O PRO A 177 49.265 46.851 17.784 1.00 15.28 ATOM 1143 N LEU A 178 49.467 45.470 19.557 1.00 14.24 ATOM 1144 CA LEU A 178 49.728 44.268 18.779 1.00 15.03 ATOM 1145 CB LEU A 178 51.130 43.738 19.087 1.00 12.96 ATOM 1146 CG LEU A 178 51.516 42.404 18.444 1.00 14.74 ATOM 1147 CD1 LEU A 178 51.571 42.573 16.932 1.00 14.67 ATOM 1148 CD2 LEU A 178 52.869 41.938 18.976 1.00 11.17 ATOM 1149 C LEU A 178 48.702 43.190 19.116 1.00 14.20 ATOM 1150 0 LEU A 178 48.456 42.897 20.283 1.00 15.66 ATOM 1151 N GLY A 179 48.096 42.609 18.090 1.00 14.51 ATOM 1152 CA GLY A 179 47.131 41.552 18.309 1.00 11.48 ATOM 1153 C GLY A 179 47.674 40.287 17.677 1.00 12.92 ATOM 1154 0 GLY A 179 48.433 40.355 16.706 1.00 11.41 ATOM 1155 N VAL A 180 47.312 39.137 18.235 1.00 12.74 ATOM 1156 CA VAL A 180 47.754 37.857 17.700 1.00 12.66 ATOM 1157 CB VAL A 180 48.702 37.135 18.670 1.00 13.16 ATOM 1158 CG1 VAL A 180 49.025 35.746 18.135 1.00 11.92 ATOM 1159 CG2 VAL A 180 49.981 37.946 18.838 1. 00 14.00 ATOM 1160 C VAL A 180 46.535 36.981 17.437 1.00 14.54 ATOM 1161 0 VAL A 180 45.723 36.733 18.334 1.00 15.05

ATOM 1162 N ASN A 181 46.411 36.523 16.197 1.00 14.43 ATOM 1163 CA ASN A 181 45.285 35.701 15.774 1.00 16.18 ATOM 1164 CB ASN A 181 44.913 36.081 14.337 1.00 16.86 ATOM 1165 CG ASN A 181 43.622 35.450 13.872 1.00 18.28 ATOM 1166 OD1 ASN A 181 43.439 34.233 13.961 1.00 16.72 ATOM 1167 ND2 ASN A 181 42.717 36.278 13.353 1.00 17.72 ATOM 1168 C ASN A 181 45.657 34.217 15.867 1.00 16.98 ATOM 1169 0 ASN A 181 46.650 33.781 15.281 1.00 17.21 ATOM 1170 N LEU A 182 44.843 33.452 16.593 1.00 15.71 ATOM 1171 CA LEU A 182 45.079 32.029 16.804 1.00 16.75 ATOM 1172 CB LEU A 182 44.890 31.691 18.283 1.00 15.56 ATOM 1173 CG LEU A 182 45.709 32.502 19.285 1.00 16.48 ATOM 1174 CD1 LEU A 182 45.285 32.136 20.703 1.00 14.81 ATOM 1175 CD2 LEU A 182 47.190 32.233 19.068 1.00 14.85 ATOM 1176 C LEU A 182 44.187 31.105 15.980 1.00 17.41 ATOM 1177 0 LEU A 182 42.981 31.309 15.876 1.00 18.39 ATOM 1178 N GLY A 183 44.800 30.078 15.406 1.00 17.73 ATOM 1179 CA GLY A 183 44.066 29.113 14.613 1.00 18.55 ATOM 1180 C GLY A 183 44.348 27.733 15.176 1.00 20.03 ATOM 1181 0 GLY A 183 44.939 27.602 16.250 1.00 18.94 ATOM 1182 N LYS A 184 43.931 26.695 14.465 1.00 20.89 ATOM 1183 CA LYS A 184 44.172 25.346 14.943 1.00 22.37 ATOM 1184 CB LYS A 184 42.898 24.755 15.553 1.00 24.26 ATOM 1185 CG LYS A 184 41.916 24.217 14.540 1.00 28.42 ATOM 1186 CD LYS A 184 40.864 23.363 15.221 1.00 32.20 ATOM 1187 CE LYS A 184 40.116 22.506 14.210 1.00 35.25 ATOM 1188 NZ LYS A 184 41.029 21.545 13.531 1.00 35.90 ATOM 1189 C LYS A 184 44.672 24.465 13.808 1.00 20.68 ATOM 1190 O LYS A 184 44.369 24.700 12.644 1.00 21.35 ATOM 1191 N ASN A 185 45.449 23.452 14.157 1.00 21.49 ATOM 1192 CA ASN A 185 45.997 22.547 13.161 1.00 22.53 ATOM 1193 CB ASN A 185 47.052 21.645 13.801 1.00 20.30 ATOM 1194 CG ASN A 185 48.371 22.360 14.025 1.00 20.21 ATOM 1195 OD1 ASN A 185 48.812 22.536 15.161 1.00 20.64 ATOM 1196 ND2 ASN A 185 49.010 22.773 12.938 1.00 19.38 ATOM 1197 C ASN A 185 44.940 21.692 12.469 1.00 24.32 ATOM 1198 0 ASN A 185 43.929 21.307 13.063 1.00 22.56

ATOM 1199 N LYS A 186 45.200 21.392 11.201 1.00 27.23 ATOM 1200 CA LYS A 186 44.305 20. 582 10.390 1.00 30.05 ATOM 1201 CB LYS A 186 44.886 20.441 8.982 1.00 30.82 ATOM 1202 CG LYS A 186 44.054 19. 581 8.047 1.00 33.61 ATOM 1203 CD LYS A 186 44.711 19.487 6.685 1.00 35.69 ATOM 1204 CE LYS A 186 43.865 18.692 5.710 1.00 37.08 ATOM 1205 NZ LYS A 186 44.525 18.604 4.374 1.00 39.36 ATOM 1206 C LYS A 186 44.051 19.190 10.981 1.00 31.18 ATOM 1207 0 LYS A 186 42.914 18.726 11.013 1.00 30.53 ATOM 1208 N THR A 187 45.107 18.530 11.449 1.00 33.43 ATOM 1209 CA THR A 187 44.973 17.187 12.011 1.00 36.34 ATOM 1210 CB THR A 187 46.204 16.314 11. 685' 1.00 36.53 ATOM 1211 OG1 THR A 187 47.348 16.819 12.389 1.00 35. 83 ATOM 1212 CG2 THR A 187 46.480 16.323 10.184 1.00 35.68 ATOM 1213 C THR A 187 44.776 17.175 13.524 1.00 38.23 ATOM 1214 0 THR A 187 44.924 16.134 14.169 1.00 39.65 ATOM 1215 N SER A 188 44.449 18.330 14.091 1.00 38.70 ATOM 1216 CA SER A 188 44.225 18.424 15.524 1.00 38.55 ATOM 1217 CB SER A 188 44.078 19.886 15.940 1.00 38.64 ATOM 1218 OG SER A 188 43.782 19.988 17.320 1.00 40.20 ATOM 1219 C SER A 188 42.964 17.654 15.904 1.00 39.15 ATOM 1220 0 SER A 188 42.006 17.601 15.134 1.00 38.68 ATOM 1221 N VAL A 189 42.971 17.061 17.094 1.00 39.48 ATOM 1222 CA VAL A 189 41.829 16.296 17.583 1.00 41.01 ATOM 1223 CB VAL A 189 42.284 14.984 18.260 1.00 41.97 ATOM 1224 CG1 VAL A 189 41.102 14.309 18.927 1.00 42.79 ATOM 1225 CG2 VAL A 189 42.910 14.052 17.230 1.00 41.86 ATOM 1226 C VAL A 189 41.015 17.101 18.595 1.00 41.66 ATOM 1227 0 VAL A 189 39.789 16.980 18.660 1.00 43.36 ATOM 1228 N ASP A 190 41.704 17.925 19.379 1.00 40.34 ATOM 1229 CA ASP A 190 41.055 18.748 20.394 1.00 38.77 ATOM 1230 CB ASP A 190 41.708 18.502 21.755 1.00 41.42 ATOM 1231 CG ASP A 190 40.907 19.084 22.900 1.00 43.96 ATOM 1232 OD1 ASP A 190 40.362 20.197 22.746 1.00 44.17 ATOM 1233 OD2 ASP A 190 40.831 18.431 23.961 1.00 48.33 ATOM 1234 C ASP A 190 41.176 20.228 20.031 1.00 36.65 ATOM 1235 O ASP A 190 42.153 20.886 20.396 1.00 36.03

ATOM 1236 N ALA A 191 40.178 20.749 19.322 1.00 33.62 ATOM 1237 CA ALA A 191 40.181 22.147 18.902 1.00 30.36 ATOM 1238 CB ALA A 191 38.860 22.493 18.232 1.00 30.25 ATOM 1239 C ALA A 191 40.433 23.101 20.060 1.00 28.52 ATOM 1240 0 ALA A 191 41.192 24.058 19.930 1.00 26.66 ATOM 1241 N ALA A 192 39.793 22.835 21.193 1.00 26.87 ATOM 1242 CA ALA A 192 39.942 23.685 22.367 1.00 25.59 ATOM 1243 CB ALA A 192 39.013 23.205 23.479 1.00 23.07 ATOM 1244 C ALA A 192 41.382 23.740 22.871 1.00 25.06 ATOM 1245 0 ALA A 192 41.863 24.804 23.248 1.00 26.91 ATOM 1246 N GLU A 193 42.067 22.600 22.881 1.00 24.69 ATOM 1247 CA GLU A 193 43.449 22.553 23.348 1. 00 25. 36 ATOM 1248 CB GLU A 193 43.941 21.104 23.430 1.00 2, 8. 55 ATOM 1249 CG GLU A 193 45.386 20.980 23.892 1.00 33.86 ATOM 1250 CD GLU A 193 45.625 21.605 25.259 1.00 38.09 ATOM 1251 OE1 GLU A 193 46.803 21.800 25.628 1.00 40.81 ATOM 1252 OE2 GLU A 193 44.637 21.895 25.969 1.00 40.22 ATOM 1253 C GLU A 193 44.373 23.373 22.444 1.00 23.89 ATOM 1254 0 GLU A 193 45.281 24.050 22.929 1.00 23.13 ATOM 1255 N ASP A 194 44.137 23.309 21.136 1.00 21.11 ATOM 1256 CA ASP A 194 44.925 24.071 20.171 1.00 21.43 ATOM 1257 CB ASP A 194 44.373 23.875 18.755 1.00 22.24 ATOM 1258 CG ASP A 194 45.043 22.736 18.017 1.00 22.08 ATOM 1259 OD1 ASP A 194 45.526 21.802 18.679 1.00 25.23 ATOM 1260 OD2 ASP A 194 45.080 22.768 16.769 1.00 23.80 ATOM 1261 C ASP A 194 44.910 25.561 20.520 1.00 21.42 ATOM 1262 0 ASP A 194 45.962 26.207 20.552 1.00 22.27 ATOM 1263 N TYR A 195 43.723 26.110 20.771 1.00 19.34 ATOM 1264 CA TYR A 195 43.618 27.522 21.119 1.00 19.62 ATOM 1265 CB TYR A 195 42.159 27.999 21.080 1.00 18.69 ATOM 1266 CG TYR A 195 41.558 28.005 19.693 1.00 19.61 ATOM 1267 CD1 TYR A 195 40.769 26.953 19.250 1.00 19.06 ATOM 1268 CE1 TYR A 195 40.262 26.930 17.968 1.00 19.80 ATOM 1269 CD2 TYR A 195 41.819 29.043 18.809 1. 00 19.96 ATOM 1270 CE2 TYR A 195 41.316 29.030 17.520 1.00 20.62 ATOM 1271 CZ TYR A 195 40.539 27.970 17.106 1.00 21.15 ATOM 1272 OH TYR A 195 40.043 27.943 15.822 1.00 22.18

ATOM 1273 C TYR A 195 44.199 27.762 22.504 1.00 19.30 ATOM 1274 0 TYR A 195 44.812 28.799 22.755 1.00 19.17 ATOM 1275 N ALA A 196 44.006 26.800 23.401 1.00 19.01 ATOM 1276 CA ALA A 196 44.530 26.918 24.756 1.00 19.63 ATOM 1277 CB ALA A 196 44.143 25.697 25.578 1.00 19.27 ATOM 1278 C ALA A 196 46.051 27.058 24.699 1.00 19.64 ATOM 1279 0 ALA A 196 46.634 27.865 25.426 1.00 19.80 ATOM 1280 N GLU A 197 46.685 26.274 23.828 1.00 18.51 ATOM 1281 CA GLU A 197 48.136 26.320 23.667 1.00 21.13 ATOM 1282 CB GLU A 197 48.615 25.222 22.708 1.00 24.77 ATOM 1283 CG GLU A 197 48.308 23.810 23.169 1.00 34.07 ATOM 1284 CD GLU A 197 49.001 22.761 22.321 1.00 38.95 ATOM 1285 OE1 GLU A 197 48.692 21.560 22.478 1.00 40.42 ATOM 1286 OE2 GLU A 197 49.863 23.141 21.501 1.00 43.50 ATOM 1287 C GLU A 197 48.564 27.679 23.125 1.00 19.10 ATOM 1288 0 GLU A 197 49.540 28.264 23.598 1.00 17.04 ATOM 1289 N GLY A 198 47.830 28.168 22.128 1.00 16.78 ATOM 1290 CA GLY A 198 48.136 29.460 21.545 1.00 15.98 ATOM 1291 C GLY A 198 48.061 30.564 22.582 1.00 14.72 ATOM 1292 0 GLY A 198 48.887 31.476 22.595 1.00 14.32 ATOM 1293 N VAL A 199 47.061 30.483 23.453 1.00 15.12 ATOM 1294 CA VAL A 199 46.887 31.471 24.508 1.00 15.39 ATOM 1295 CB VAL A 199 45.619 31.187 25.345 1. 00 15. 96 ATOM 1296 CG1 VAL A 199 45.617 32.059 26.599 1.00 12.02 ATOM 1297 CG2 VAL A 199 44.371 31.445 24.505 1.00 15.82 ATOM 1298 C VAL A 199 48.084 31.458 25.452 1.00 17.58 ATOM 1299 O VAL A 199 48.561 32.511 25.876 1.00 18.81 ATOM 1300 N ARG A 200 48.576 30.263 25.769 1.00 16.78 ATOM 1301 CA ARG A 200 49.709 30.132 26.679 1.00 19.56 ATOM 1302 CB ARG A 200 49.822 28.693 27.193 1.00 21.47 ATOM 1303 CG ARG A 200 48.759 28.305 28.205 1.00 24.99 ATOM 1304 CD ARG A 200 49.163 27.043 28.944 1.00 26.41 ATOM 1305 NE ARG A 200 49.109 25.863 28.092 1.00 28.52 ATOM 1306 CZ ARG A 200 48.004 25.167 27.861 1.00 30.32 ATOM 1307 NH1 ARG A 200 46.865 25.536 28.425 1.00 31.74 ATOM 1308 NH2 ARG A 200 48.037 24.102 27.069 1.00 31.33 ATOM 1309 C ARG A 200 51.052 30.549 26.098 1.00 18.41

ATOM 1310 0 ARG A 200 51.892 31.109 26.805 1.00 18.76 ATOM 1311 N VAL A 201 51.258 30.281 24.815 1.00 16.94 ATOM 1312 CA VAL A 201 52.525 30.610 24.181 1.00 14.62 ATOM 1313 CB VAL A 201 52.843 29.618 23.035 1.00 15.42 ATOM 1314 CG1 VAL A 201 54.164 30.004 22.367 1.00 13.35 ATOM 1315 CG2 VAL A 201 52.919 28.188 23.585 1.00 8.55 ATOM 1316 C VAL A 201 52.627 32.037 23.643 1.00 16.13 ATOM 1317 O VAL A 201 53.659 32.691 23.816 1.00 13.21 ATOM 1318 N LEU A 202 51.565 32.529 23.006 1.00 15.76 ATOM 1319 CA LEU A 202 51.598 33.875 22.445 1.00 14.49 ATOM 1320 CB LEU A 202 51.104 33.852 20.999 1.00 15.50 ATOM 1321 CG LEU A 202 51.984 33.075 20.017 1.00 16.36 ATOM 1322 CD1 LEU A 202 51.499 33.329 18.595 1.00 15.07 ATOM 1323 CD2 LEU A 202 53.439 33.511 20.170 1.00 15.62 ATOM 1324 C LEU A 202 50.828 34.931 23.233 1.00 15.05 ATOM 1325 0 LEU A 202 51.067 36.125 23.068 1.00 14.28 ATOM 1326 N GLY A 203 49.906 34.498 24.086 1.00 15.24 ATOM 1327 CA GLY A 203 49.143 35.444 24.878 1.00 16.41 ATOM 1328 C GLY A 203 50.007 36.412 25.675 1.00 16.95 ATOM 1329 0 GLY A 203 49.647 37.582 25.841 1.00 13.97 ATOM 1330 N PRO A 204 51.155 35.953 26.195 1.00 17.99 ATOM 1331 CD PRO A 204 51.561 34.543 26.328 1.00 17.43 ATOM 1332 CA PRO A 204 52.045 36.824 26.976 1.00 18.92 ATOM 1333 CB PRO A 204 53.032 35.835 27.605 1.00 16.96 ATOM 1334 CG PRO A 204 52.254 34.545 27.658 1.00 17.45 ATOM 1335 C PRO A 204 52.761 37.885 26.132 1.00 19.12 ATOM 1336 0 PRO A 204 53.361 38.820 26.672 1.00 20.34 ATOM 1337 N LEU A 205 52.693 37.740 24.812 1.00 17.62 ATOM 1338 CA LEU A 205 53.355 38.676 23.901 1.00 16.92 ATOM 1339 CB LEU A 205 54.234 37.896 22.918 1.00 16.82 ATOM 1340 CG LEU A 205 55.406 37.112 23.519 1.00 18.96 ATOM 1341 CD1 LEU A 205 55.752 35.918 22.646 1.00 16.58 ATOM 1342 CD2 LEU A 205 56.599 38.040 23.679 1.00 17.87 ATOM 1343 C LEU A 205 52.388 39.558 23.110 1.00 17.18 ATOM 1344 0 LEU A 205 52.810 40.324 22.241 1.00 16.67 ATOM 1345 N ALA A 206 51.099 39.469 23.417 1.00 16.36 ATOM 1346 CA ALA A 206 50.108 40.243 22.686 1.00 16.19

ATOM 1347 CB ALA A 206 49.216 39.295 21.900 1.00 16.04 ATOM 1348 C ALA A 206 49.245 41.166 23.532 1.00 17.13 ATOM 1349 0 ALA A 206 48.995 40.912 24.708 1.00 18.07 ATOM 1350 N ASP A 207 48.788 42.251 22.924 1.00 17.38 ATOM 1351 CA ASP A 207 47.913 43.169 23.627 1.00 18.09 ATOM 1352 CB ASP A 207 47.941 44.542 22.964 1.00 17.76 ATOM 1353 CG ASP A 207 49.253 45.267 23.216 1.00 20.83 ATOM 1354 OD1 ASP A 207 49.628 45.409 24.400 1.00 22.34 ATOM 1355 OD2 ASP A 207 49.912 45.691 22.245 1.00 19. 95 ATOM 1356 C ASP A 207 46.519 42.547 23.600 1.00 16.94 ATOM 1357 0 ASP A 207 45.740 42.702 24.534 1.00 16.96 ATOM 1358 N TYR A 208 46.217 41.825 22.526 1.00 16.01 ATOM 1359 CA TYR A 208 44.941 41.136 22.420 1.00 16. 14 ATOM 1360 CB TYR A 208 43.843 42.043 21.830 1.00 16.24 ATOM 1361 CG TYR A 208 43.913 42.321 20.340 1.00 16.53 ATOM 1362 CD1 TYR A 208 44.391 43.540 19.861 1.00 17.20 ATOM 1363 CE1 TYR A 208 44.403 43.824 18.504 1.00 16.56 ATOM 1364 CD2 TYR A 208 43.454 41.388 19.414 1.00 15.47 ATOM 1365 CE2 TYR A 208 43.465 41.659 18.055 1.00 14.96 ATOM 1366 CZ TYR A 208 43.939 42.878 17.605 1.00 18.58 ATOM 1367 OH TYR A 208 43.955 43.148 16.254 1.00 18.48 ATOM 1368 C TYR A 208 45.102 39.879 21.579 1.00 16.18 ATOM 1369 0 TYR A 208 45.899 39.842 20.640 1.00 15.69 ATOM 1370 N LEU A 209 44.361 38.842 21.951 1.00 16.49 ATOM 1371 CA LEU A 209 44.385 37.570 21.244 1.00 17.41 ATOM 1372 CB LEU A 209 44.519 36.407 22.226 1.00 16.83 ATOM 1373 CG LEU A 209 45.850 36.202 22.939 1.00 17.95 ATOM 1374 CD1 LEU A 209 45.708 35.059 23.936 1.00 18.86 ATOM 1375 CD2 LEU A 209 46.940 35.901 21.916 1.00 16.17 ATOM 1376 C LEU A 209 43.082 37.413 20.479 1.00 17.21 ATOM 1377 0 LEU A 209 42.036 37.885 20.919 1.00 17.18 ATOM 1378 N VAL A 210 43.148 36.742 19.336 1.00 18.27 ATOM 1379 CA VAL A 210 41.962 36.525 18.525 1.00 17.38 ATOM 1380 CB VAL A 210 42.105 37.155 17.122 1.00 17.53 ATOM 1381 CG1 VAL A 210 40.819 36.931 16.314 1.00 15.25 ATOM 1382 CG2 VAL A 210 42.424 38.633 17.242 1.00 13.97 ATOM 1383 C VAL A 210 41.688 35.045 18.334 1.00 18.13

ATOM 1384 0 VAL A 210 42.503 34.323 17.767 1.00 18.42 ATOM 1385 N VAL A 211 40.545 34.589 18.826 1.00 18.92 ATOM 1386 CA VAL A 211 40.168 33. 198 18.638 1.00 18.84 ATOM 1387 CB VAL A 211 39. 141 32.732 19.691 1.00 17.39 ATOM 1388 CG1 VAL A 211 38.712 31.309 19.395 1.00 14.12 ATOM 1389 CG2 VAL A 211 39.741 32.826 21.086 1.00 17.05 ATOM 1390 C VAL A 211 39.514 33.164 17.256 1.00 19.52 ATOM 1391 0 VAL A 211 38.355 33.554 17.100 1.00 18.05 ATOM 1392 N ASN A 212 40.265 32.728 16.250 1.00 19.73 ATOM 1393 CA ASN A 212 39.725 32.665 14.904 1.00 20.91 ATOM 1394 CB ASN A 212 40.835 32.725 13.858 1.00 19.36 ATOM 1395 CG ASN A 212 40.287 32.677 12.448 1.00 18.94 ATOM 1396 OD1 ASN A 212 39.074 32.682 12.253 1.00 19.73 ATOM 1397 ND2 ASN A 212 41.169 32.632 11.461 1.00 18.71 ATOM 1398 C ASN A 212 38.924 31.388 14.714 1.00 22.66 ATOM 1399 O ASN A 212 39.479 30.291 14.606 1.00 23.56 ATOM 1400 N VAL A 213 37.610 31.538 14.660 1.00 21.24 ATOM 1401 CA VAL A 213 36.744 30.387 14.499 1.00 22.82 ATOM 1402 CB VAL A 213 35.893 30.196 15.768 1.00 23.98 ATOM 1403 CG1 VAL A 213 34.778 31.242 15.822 1.00 23.80 ATOM 1404 CG2 VAL A 213 35.343 28. 8, 11 15.800 1.00 27.23 ATOM 1405 C VAL A 213 35.838 30.579 13.282 1.00 21.82 ATOM 1406 0 VAL A 213 34.813 29.904 13.134 1.00 21.63 ATOM 1407 N SER A 214 36.243 31.492 12.402 1.00 21.12 ATOM 1408 CA SER A 214 35.468 31.811 11.211 1.00 19.76 ATOM 1409 CB SER A 214 35.010 33.270 11.273 1.00 19.69 ATOM 1410 OG SER A 214 36.100 34.142 11.527 1.00 15.15 ATOM 1411 C SER A 214 36.181 31.556 9.887 1.00 20.87 ATOM 1412 O SER A 214 35.712 31.995 8.837 1.00 18.78 ATOM 1413 N SER A 215 37.311 30.859 9.921 1.00 22.57 ATOM 1414 CA SER A 215 38.012 30.570 8.678 1.00 23.58 ATOM 1415 CB SER A 215 39.388 29.976 8.951 1.00 25.79 ATOM 1416 OG SER A 215 40.016 29.608 7.732 1.00 25.68 ATOM 1417 C SER A 215 37.187 29.571 7.874 1.00 24.56 ATOM 1418 0 SER A 215 36.750 28.544 8.393 1.00 24.98 ATOM 1419 N PRO A 216 36.955 29.866 6.591 1.00 26.27 ATOM 1420 CD PRO A 216 37.219 31.148 5.908 1.00 24.27

ATOM 1421 CA PRO A 216 36.174 28.969 5.737 1.00 27. 15 ATOM 1422 CB PRO A 216 35.594 29.921 4.703 1.00 26.46 ATOM 1423 CG PRO A 216 36.739 30.875 4.492 1.00 24.79 ATOM 1424 C PRO A 216 37.035 27.897 5.084 1.00 28.49 ATOM 1425 0 PRO A 216 36.519 27.019 4.398 1.00 30.31 ATOM 1426 N ASN A 217 38.345 27.966 5.308 1.00 30. 00 ATOM 1427 CA ASN A 217 39.270 27.026 4.686 1.00 31.48 ATOM 1428 CB ASN A 217 40.438 27.803 4.080 1.00 31.24 ATOM 1429 CG ASN A 217 39.969 28.926 3.176 1.00 32.97 ATOM 1430 OD1 ASN A 217 39.213 28.699 2.230 1.00 33.41 ATOM 1431 ND2 ASN A 217 40.410 30.147 3.465 1.00 32.16 ATOM 1432 C ASN A 217 39.792 25.889 5.554 1.00 32.38 ATOM 1433 0 ASN A 217 40.776 25.234 5.204 1.00 31. 80 ATOM 1434 N THR A 218 39.135 25.658 6.685 1.00 33.60 ATOM 1435 CA THR A 218 39.507 24.567 7.581 1.00 34.67 ATOM 1436 CB THR A 218 40.182 25.079 8.875 1.00 35.71 ATOM 1437 OG1 THR A 218 41.502 25.553 8.574 1.00 34.15 ATOM 1438 CG2 THR A 218 40.276 23.961 9.902 1.00 34.11 ATOM 1439 C THR A 218 38.231 23.809 7.933 1.00 35.34 ATOM 1440 0 THR A 218 37.313 24.365 8.539 1.00 35.59 ATOM 1441 N ALA A 219 38.182 22.541 7.531 1.00 35.68 ATOM 1442 CA ALA A 219 37.027 21.677 7.761 1.00 35.27 ATOM 1443 CB ALA A 219 37.366 20.243 7.356 1.00 33.44 ATOM 1444 C ALA A 219 36.482 21.693 9.185 1.00 35.21 ATOM 1445 0 ALA A 219 37. 205 21.424 10.145 1.00 35.80 ATOM 1446 N GLY A 220 35.196 22.013 9.304 1.00 35.33 ATOM 1447 CA GLY A 220 34.533 22.038 10.598 1.00 35.53 ATOM 1448 C GLY A 220 34.909 23.125 11.589 1.00 35.22 ATOM 1449 0 GLY A 220 34.434 23.102 12.723 1.00 35.56 ATOM 1450 N LEU A 221 35.743 24.079 11.183 1.00 34.69 ATOM 1451 CA LEU A 221 36.157 25.148 12.088 1.00 34.37 ATOM 1452 CB LEU A 221 37.303 25.961 11.478 1.00 34.53 ATOM 1453 CG LEU A 221 37.918 26.976 12.450 1.00 34.35 ATOM 1454 CD1 LEU A 221 38.857 26.238 13.396 1.00 35.01 ATOM 1455 CD2 LEU A 221 38.671 28.060 11.695 1.00 33.25 ATOM 1456 C LEU A 221 35.012 26.095 12.443 1.00 34.00 ATOM 1457 0 LEU A 221 34.831 26.462 13.605 1.00 34.07

ATOM 1458 N ARG A 222 34.240 26.491 11.438 1.00 34.48 ATOM 1459 CA ARG A 222 33.124 27.404 11.650 1.00 34.48 ATOM 1460 CB ARG A 222 32.544 27.837 10.304 1.00 34.91 ATOM 1461 CG ARG A 222 33.445 28.786 9.525 1.00 35.80 ATOM 1462 CD ARG A 222 32.870 29.056 8.148 1.00 38.02 ATOM 1463 NE ARG A 222 32.938 27.873 7.293 1.00 38.82 ATOM 1464 CZ ARG A 222 32.210 27.700 6.195 1.00 39.23 ATOM 1465 NH1 ARG A 222 31.349 28.635 5.812 1.00 37.27 ATOM 1466 NH2 ARG A 222 32.348 26.593 5.476 1.00 38.53 ATOM 1467 C ARG A 222 32.018 26.836 12.536 1.00 34.30 ATOM 1468 O ARG A 222 31.224 27.592 13.100 1.00 33.00 ATOM 1469 N SER A 223 31.963 25.514 12.665 1.00 34.10 ATOM 1470 CA SERA 223 30.940 24.892 13.498 1.00 33.94 ATOM 1471 CB SERA 223 30.930 23.371 13.311 1.00 32.71 ATOM 1472 OG SERA 223 32.106 22.778 13.831 1.00 36.35 ATOM 1473 C SER A 223 31.212 25.236 14.959 1.00 33.63 ATOM 1474 0 SER A 223 30.335 25.103 15.814 1.00 32.92 ATOM 1475 N LEU A 224 32.433 25.683 15.240 1.00 33.63 ATOM 1476 CA LEU A 224 32.806 26.062 16.598 1.00 34.04 ATOM 1477 CB LEU A 224 34.328 26.196 16.721 1.00 33.19 ATOM 1478 CG LEU A 224 35.192 24.950 16.506 1.00 34.59 ATOM 1479 CD1 LEU A 224 36.664 25.336 16.506 1.00 31.62 ATOM 1480 CD2 LEU A 224 34.900 23.932 17.599 1.00 31.62 ATOM 1481 C LEU A 224 32.135 27.384 16.974 1.00 33.88 ATOM 1482 0 LEU A 224 32.244 27.845 18.110 1.00 33.46 ATOM 1483 N GLN A 225 31.452 27.997 16.011 1.00 34.56 ATOM 1484 CA GLN A 225 30.751 29.251 16.270 1.00 35.35 ATOM 1485 CB GLN A 225 30.539 30.046 14.970 1.00 34.80 ATOM 1486 CG GLN A 225 31.825 30.373 14.212 1.00 35.04 ATOM 1487 CD GLN A 225 31.583 31.194 12.951 1.00 34.62 ATOM 1488 OE1 GLN A 225 31.541 32.428 12.991 1.00 32.02 ATOM 1489 NE2 GLN A 225 31.410 30.508 11.824 1.00 32.11 ATOM 1490 C GLN A 225 29.402 28.920 16.910 1.00 34.70 ATOM 1491 0 GLN A 225 28. 696 29.809 17.386 1.00 34.24 ATOM 1492 N GLY A 226 29.055 27.634 16.917 1.00 34.70 ATOM 1493 CA GLY A 226 27.802 27.198 17.516 1.00 34.95 ATOM 1494 C GLY A 226 27.786 27.497 19.005 1.00 35.26

ATOM 1495 O GLY A 226 28.831 27.463 19.654 1.00 36.21 ATOM 1496 N LYS A 227 26.604 27.772 19.549 1.00 34.42 ATOM 1497 CA LYS A 227 26.453 28.116 20.964 1.00 34. 17 ATOM 1498 CB LYS A 227 24.968 28.234 21.321 1.00 32.71 ATOM 1499 CG LYS A 227 24.712 28.922 22.658 1.00 32.69 ATOM 1500 CD LYS A 227 23.236 29.227 22.852 1.00 32.86 ATOM 1501 CE LYS A 227 22.974 29.932 24.175 1.00 34.60 ATOM 1502 NZ LYS A 227 23.622 31.274 24.244 1.00 37.35 ATOM 1503 C LYS A 227 27.142 27.193 21.968 1.00 34.30 ATOM 1504 O LYS A 227 27.965 27.648 22.764 1.00 33.44 ATOM 1505 N ALA A 228 26.807 25.906 21.942 1.00 34.25 ATOM 1506 CA ALA A 228 27.403 24.950 22.877 1.00 35.39 ATOM 1507 CB ALA A 228 26.742 23.585 22.722 1.00 33.05 ATOM 1508 C ALA A 228 28.912 24.822 22.681 1.00 35.36 ATOM 1509 0 ALA A 228 29.685 24.947 23.629 1.00 34.05 ATOM 1510 N GLU A 229 29.322 24.566 21.443 1.00 36.97 ATOM 1511 CA GLU A 229 30.733 24.424 21.108 1.00 38.17 ATOM 1512 CB GLU A 229 30.885 24.141 19.608 1.00 42.08 ATOM 1513 CG GLU A 229 31.463 22.771 19.271 1.00 48.40 ATOM 1514 CD GLU A 229 31.399 22.459 17.782 1.00 51.77 ATOM 1515 OE1 GLU A 229 30.279 22.273 17.258 1.00 54.82 ATOM 1516 OE2 GLU A 229 32.467 22.402 17.133 1.00 53.10 ATOM 1517 C GLU A 229 31.506 25.691 21.470 1.00 35.95 ATOM 1518 0 GLU A 229 32.587 25.627 22.052 1.00 36.51 ATOM 1519 N LEU A 230 30.935 26.842 21.133 1.00 33.64 ATOM 1520 CA LEU A 230 31.573 28.123 21.399 1.00 30.71 ATOM 1521 CB LEU A 230 30.768 29.265 20.763 1.00 28.43 ATOM 1522 CG LEU A 230 31.388 30.665 20.836 1.00 26.75 ATOM 1523 CD1 LEU A 230 32.723 30.679 20.096 1.00 24.08 ATOM 1524 CD2 LEU A 230 30.438 31.680 20.223 1.00 26.42 ATOM 1525 C LEU A 230 31.751 28.401 22.884 1.00 29.09 ATOM 1526 O LEU A 230 32.787 28.918 23.300 1.00 28.84 ATOM 1527 N ARG A 231 30.745 28.065 23.684 1.00 28.50 ATOM 1528 CA ARG A 231 30.820 28.312 25.118 1.00 28.34 ATOM 1529 CB ARG A 231 29.473 28.016 25.787 1.00 29.52 ATOM 1530 CG ARG A 231 29.427 28.407 27.260 1.00 32.29 ATOM 1531 CD ARG A 231 28.148 27.937 27.936 1.00 36.19

ATOM 1532 NE ARG A 231 26.969 28.685 27.506 1.00 38.72 ATOM 1533 CZ ARG A 231 25.885 28.128 26.974 1.00 39.27 ATOM 1534 NH1 ARG A 231 25.833 26.815 26.799 1.00 40.30 ATOM 1535 NH2 ARG A 231 24.848 28. 881 26.632 1.00 38.91 ATOM 1536 C ARG A 231 31.925 27.492 25.788 1.00 27.28 ATOM 1537 O ARG A 231 32.681 28.015 26.601 1.00 25.62 ATOM 1538 N ARG A 232 32.014 26.210 25.448 1.00 27.02 ATOM 1539 CA ARG A 232 33.035 25.343 26.026 1.00 28.51 ATOM 1540 CB ARG A 232 32.813 23.887 25.603 1.00 31.69 ATOM 1541 CG ARG A 232 33.898 22.937 26.103 1.00 37.81 ATOM 1542 CD ARG A 232 33.653 21.483 25.692 1.00 42.26 ATOM 1543 NE ARG A 232 32.323 21.016 26.081 1.00 46.87 ATOM 1544 CZ ARG A 232 31.239 21.131 25.318 1.00 49.45 ATOM 1545 NH1 ARG A 232 31.329 21.691 24.118 1.00 49.90 ATOM 1546 NH2 ARG A 232 30.064 20.697 25.758 1.00 49.90 ATOM 1547 C ARG A 232 34.421 25.793 25.584 1.00 26.98 ATOM 1548 0 ARG A 232 35.372 25.776 26.363 1.00 26.34 ATOM 1549 N LEU A 233 34.529 26.196 24.324 1.00 25.27 ATOM 1550 CA LEU A 233 35.796 26.657 23.782 1.00 24.87 ATOM 1551 CB LEU A 233 35.655 26.912 22.282 1.00 25.82 ATOM 1552 CG LEU A 233 36.829 27.628 21.615 1.00 26.85 ATOM 1553 CD1 LEU A 233 38.077 26.783 21.734 1.00 28.70 ATOM 1554 CD2 LEU A 233 36.500 27.896 20.161 1.00 28.50 ATOM 1555 C LEU A 233 36.285 27.932 24.475 1.00 24.30 ATOM 1556 0 LEU A 233 37.423 27.995 24.943 1.00 22.17 ATOM 1557 N LEU A 234 35.417 28.939 24.546 1.00 22.83 ATOM 1558 CA LEU A 234 35.767 30.222 25.153 1.00 22.68 ATOM 1559 CB LEU A 234 34.721 31.278 24.782 1.00 23.83 ATOM 1560 CG LEU A 234 34.666 31.550 23.275 1.00 26.75 ATOM 1561 CD1 LEU A 234 33.574 32.559 22.952 1.00 28.02 ATOM 1562 CD2 LEU A 234 36.025 32.053 22.815 1.00 26.81 ATOM 1563 C LEU A 234 35.956 30.183 26.665 1.00 21.66 ATOM 1564 0 LEU A 234 36.697 30.991 27.221 1.00 20.64 ATOM 1565 N THR A 235 35.286 29.257 27.336 1.00 21.48 ATOM 1566 CA THR A 235 35.447 29.143 28.779 1.00 22.71 ATOM 1567 CB THR A 235 34.468 28.115 29.378 1.00 23.15 ATOM 1568 OG1 THR A 235 33.136 28.640 29.321 1.00 24.32

ATOM 1569 CG2 THR A 235 34.833 27.812 30.824 1.00 20.23 ATOM 1570 C THR A 235 36.882 28.701 29.075 1.00 21.92 ATOM 1571 0 THR A 235 37.530 29.227 29.980 1.00 22.20 ATOM 1572 N LYS A 236 37.371 27.743 28.293 1.00 19.41 ATOM 1573 CA LYS A 236 38.724 27.233 28.456 1.00 21.47 ATOM 1574 CB LYS A 236 38.906 25.956 27.634 1.00 23.11 ATOM 1575 CG LYS A 236 40.249 25.277 27.855 1.00 30.29 ATOM 1576 CD LYS A 236 40.274 23.875 27.258 1.00 32.54 ATOM 1577 CE LYS A 236 41.569 23.162 27.600 1.00 35.14 ATOM 1578 NZ LYS A 236 41.531 21.727 27.194 1.00 38.21 ATOM 1579 C LYS A 236 39.766 28.276 28.043 1.00 20.48 ATOM 1580 0 LYS A 236 40.778 28.455 28.720 1.00 19.24 ATOM 1581 N VAL A 237 39.512 28.966 26.937 1.00 19. 58 ATOM 1582 CA VAL A 237 40.425 29.997 26.456 1.00 19.48 ATOM 1583 CB VAL A 237 39.911 30.614 25.138 1.00 19.06 ATOM 1584 CG1 VAL A 237 40.647 31.918 24.836 1.00 15.24 ATOM 1585 CG2 VAL A 237 40.104 29.621 24.003 1.00 17.14 ATOM 1586 C VAL A 237 40.587 31.104 27.495 1.00 20.14 ATOM 1587 O VAL A 237 41.708 31.499 27.826 1.00 20.24 ATOM 1588 N LEU A 238 39.462 31.594 28.010 1.00 20.89 ATOM 1589 CA LEU A 238 39.462 32.657 29.013 1.00 21.10 ATOM 1590 CB LEU A 238 38.032 33.116 29.296 1.00 19.72 ATOM 1591 CG LEU A 238 37.359 33.891 28.159 1.00 21.61 ATOM 1592 CD1 LEU A 238 35.889 34.122 28.486 1.00 21.43 ATOM 1593 CD2 LEU A 238 38.079 35.218 27.956 1.00 21.42 ATOM 1594 C LEU A 238 40.132 32.228 30.315 1.00 21.64 ATOM 1595 0 LEU A 238 40.772 33.041 30.989 1.00 20.34 ATOM 1596 N GLN A 239 39.986 30.954 30.669 1.00 21.87 ATOM 1597 CA GLN A 239 40.601 30.446 31.888 1.00 22.65 ATOM 1598 CB GLN A 239 40.119 29.023 32.185 1.00 24.73 ATOM 1599 CG GLN A 239 40.644 28.468 33.500 1.00 29.71 ATOM 1600 CD GLN A 239 40.120 27.073 33.799 1.00 36.85 ATOM 1601 OE1 GLN A 239 38.906 26.850 33.859 1.00 40.00 ATOM 1602 NE2 GLN A 239 41.033 26.126 33.991 1.00 35.90 ATOM 1603 C GLN A 239 42.122 30.460 31.739 1.00 20.03 ATOM 1604 O GLN A 239 42.839 30.880 32.645 1.00 20.49 ATOM 1605 N GLU A 240 42. 611 29.996 30.596 1.00 19.71

ATOM 1606 CA GLU A 240 44.049 29.985 30.344 1.00 20.04 ATOM 1607 CB GLU A 240 44.346 29.343 28.989 1.00 21.58 ATOM 1608 CG GLU A 240 44.001 27.864 28. 918 1.00 28.50 ATOM 1609 CD GLU A 240 44.957 26.990 29.720 1.00 32.28 ATOM 1610 OE1 GLU A 240 44.689 25.775 29.834 1.00 36.62 ATOM 1611 OE2 GLU A 240 45.980 27.504 30.225 1.00 32.81 ATOM 1612 C GLU A 240 44.566 31.424 30.358 1.00 19.32 ATOM 1613 O GLU A 240 45.654 31.697 30.860 1.00 20.01 ATOM 1614 N ARG A 241 43.767 32.337 29.811 1.00 17.04 ATOM 1615 CA ARG A 241 44.120 33.750 29.754 1.00 17.15 ATOM 1616 CB ARG A 241 43.081 34.504 28.914 1.00 15.66 ATOM 1617 CG ARG A 241 43.402 35.966 28.629 1.00 15.53 ATOM 1618 CD ARG A 241 43.191 36.870 29.840 1.00 13.45 ATOM 1619 NE ARG A 241 41.804 36.911 30.299 1.00 15.41 ATOM 1620 CZ ARG A 241 40.832 37.624 29.731 1.00 16.80 ATOM 1621 NH1 ARG A 241 39.605 37.584 30.236 1.00 14.85 ATOM 1622 NH2 ARG A 241 41.077 38.384 28.669 1.00 13.90 ATOM 1623 C ARG A 241 44.218 34.369 31.149 1.00 18.11 ATOM 1624 O ARG A 241 45.172 35.090 31.445 1.00 16.96 ATOM 1625 N ASP A 242 43.234 34.093 32.004 1.00 18.89 ATOM 1626 CA ASP A 242 43.233 34.643 33.358 1.00 18.99 ATOM 1627 CB ASP A 242 41.902 34.352 34.071 1.00 18.23 ATOM 1628 CG ASP A 242 40.708 35.016 33.391 1.00 20.88 ATOM 1629 OD1 ASP A 242 40. 884 36.078 32.759 1.00 20.84 ATOM 1630 OD2 ASP A 242 39.583 34.484 33.506 1.00 20.07 ATOM 1631 C ASP A 242 44.393 34.097 34.196 1.00 18.74 ATOM 1632 0 ASP A 242 44.788 34.709 35.188 1.00 18.25 ATOM 1633 N GLY A 243 44.939 32.955 33.789 1.00 17.54 ATOM 1634 CA GLY A 243 46.050 32.365 34.517 1.00 17.70 ATOM 1635 C GLY A 243 47.396 33.010 34.212 1.00 18.91 ATOM 1636 0 GLY A 243 48.415 32.658 34.813 1.00 18.37 ATOM 1637 N LEU A 244 47.417 33.954 33.277 1.00 18.18 ATOM 1638 CA LEU A 244 48.665 34.629 32.930 1.00 19.11 ATOM 1639 CB LEU A 244 48.623 35.130 31.481 1.00 16.84 ATOM 1640 CG LEU A 244 48.395 34.083 30.391 1.00 17.33 ATOM 1641 CD1 LEU A 244 48.265 34.771 29.046 1.00 16.03 ATOM 1642 CD2 LEU A 244 49.545 33.085 30.388 1.00 18.05

ATOM 1643 C LEU A 244 48.908 35.810 33.864 1.00 19.01 ATOM 1644 0 LEU A 244 47.964 36.402 34.387 1.00 18.42 ATOM 1645 N ARG A 245 50.176 36.147 34.073 1.00 19.39 ATOM 1646 CA ARG A 245 50.523 37.272 34.930 1.00 20.56 ATOM 1647 CB ARG A 245 52.046 37.354 35.091 1.00 19.53 ATOM 1648 CG ARG A 245 52.602 36.290 36.052 1.00 19.09 ATOM 1649 CD ARG A 245 54.072 35.987 35.813 1.00 18.19 ATOM 1650 NE ARG A 245 54.973 37.051 36.252 1.00 19.29 ATOM 1651 CZ ARG A 245 55.412 37.201 37.499 1.00 19.63 ATOM 1652 NH1 ARG A 245 56.233 38.201 37.796 1.00 15.65 ATOM 1653 NH2 ARG A 245 55.036 36.350 38.449 1.00 17.09 ATOM 1654 C ARG A 245 49.951 38.569 34.353 1.00 22.53 ATOM 1655 O ARG A 245 49.890 38.748 33.133 1.00 21.12 ATOM 1656 N ARG A 246 49.525 39.456 35.250 1.00 25.32 ATOM 1657 CA ARG A 246 48.920 40.747 34.914 1.00 27.15 ATOM 1658 CB ARG A 246 49.004 41.683 36.124 1.00 30.54 ATOM 1659 CG ARG A 246 48.337 41.129 37.369 1.00 37.47 ATOM 1660 CD ARG A 246 46.817 41.284 37.328 1.00 41.51 ATOM 1661 NE ARG A 246 46.136 40.393 38.270 1.00 41.54 ATOM 1662 CZ ARG A 246 46.497 40.210 39.536 1.00 40.36 ATOM 1663 NH1 ARG A 246 47.545 40.851 40.037 1.00 39.56 ATOM 1664 NH2 ARG A 246 45.806 39.382 40.305 1.00 41.42 ATOM 1665 C ARG A 246 49.442 41.490 33.687 1.00 26.72 ATOM 1666 0 ARG A 246 48.677 41.765 32.762 1.00 26.83 ATOM 1667 N VAL A 247 50.730 41.829 33.672 1.00 24.53 ATOM 1668 CA VAL A 247 51.277 42.569 32.538 1.00 24.80 ATOM 1669 CB VAL A 247 52.717 43.100 32.833 1.00 26.08 ATOM 1670 CG1 VAL A 247 52.681 44.081 34.000 1.00 23.05 ATOM 1671 CG2 VAL A 247 53.653 41.955 33.144 1.00 26.28 ATOM 1672 C VAL A 247 51.285 41.778 31.233 1.00 24.65 ATOM 1673 0 VAL A 247 51.421 42.354 30.155 1.00 26.53 ATOM 1674 N HIS A 248 51.117 40.463 31.331 1.00 23.77 ATOM 1675 CA HIS A 248 51.114 39.592 30.156 1.00 22.18 ATOM 1676 CB HIS A 248 52.113 38.451 30.365 1.00 21.01 ATOM 1677 CG HIS A 248 53.530 38.911 30.488 1.00 21.43 ATOM 1678 CD2 HIS A 248 54.309 39.116 31.576 1.00 21.00 ATOM 1679 ND1 HIS A 248 54. 285 39.292 29.399 1.00 20.19

ATOM 1680 CE1 HIS A 248 55.466 39.715 29.812 1.00 21.23 ATOM 1681 NE2 HIS A 248 55.506 39.619 31.129 1.00 21.42 ATOM 1682 C HIS A 248 49.730 39. 011 29.877 1.00 21.79 ATOM 1683 O HIS A 248 49.606 37.986 29.205 1.00 20.09 ATOM 1684 N ARG A 249 48.697 39.677 30.384 1.00 20.02 ATOM 1685 CA ARG A 249 47.321 39.218 30.215 1.00 21.28 ATOM 1686 CB ARG A 249 46.593 39.354 31.553 1.00 21.65 ATOM 1687 CG ARG A 249 45.352 38.510 31.701 1.00 23.99 ATOM 1688 CD ARG A 249 44.761 38.702 33.092 1.00 25.10 ATOM 1689 NE ARG A 249 45.644 38.192 34.136 1.00 25.46 ATOM 1690 CZ ARG A 249 45.657 38.631 35.390 1.00 26.82 ATOM 1691 NH1 ARG A 249 44.838 39.601 35.769 1.00 26.65 ATOM 1692 NH2 ARG A 249 46.487 38.092 36.272 1.00 28.01 ATOM 1693 C ARG A 249 46.585 40.002 29.115 1.00 21.29 ATOM 1694 0 ARG A 249 46.166 41.144 29.315 1.00 20.84 ATOM 1695 N PRO A 250 46.405 39.382 27.938 1.00 19.97 ATOM 1696 CD PRO A 250 46.882 38.037 27.565 1.00 19.93 ATOM 1697 CA PRO A 250 45.728 40.015 26.805 1.00 19.36 ATOM 1698 CB PRO A 250 46.268 39.231 25.621 1.00 17.55 ATOM 1699 CG PRO A 250 46.266 37.837 26.173 1.00 18.15 ATOM 1700 C PRO A 250 44. 202 39.976 26.834 1.00 19.85 ATOM 1701 O PRO A 250 43.586 39.166 27.541 1.00 18. 01 ATOM 1702 N ALA A 251 43.603 40.868 26.052 1.00 18.13 ATOM 1703 CA ALA A 251 42.158 40.914 25.916 1.00 17.04 ATOM 1704 CB ALA A 251 41.730 42.233 25.293 1.00 15.49 ATOM 1705 C ALA A 251 41.862 39.761 24.958 1.00 16.50 ATOM 1706 O ALA A 251 42.714 39. 395 24. 142 1.00 15.91 ATOM 1707 N VAL A 252 40.675 39.178 25.059 1.00 15.16 ATOM 1708 CA VAL A 252 40.318 38.081 24.174 1.00 16.05 ATOM 1709 CB VAL A 252 39. 994 36.794 24.971 1.00 17.17 ATOM 1710 CG1 VAL A 252 39.431 35.727 24.033 1.00 13.39 ATOM 1711 CG2 VAL A 252 41.260 36.279 25.668 1.00 14.93 ATOM 1712 C VAL A 252 39.121 38.436 23.296 1.00 17.27 ATOM 1713 0 VAL A 252 38.048 38.778 23.791 1.00 17.33 ATOM 1714 N LEU A 253 39.322 38.370 21.984 1.00 17.39 ATOM 1715 CA LEU A 253 38.261 38.659 21.030 1.00 16.46 ATOM 1716 CB LEU A 253 38.670 39.792 20.082 1.00 16.40

ATOM 1717 CG LEU A 253 38.850 41.201 20.660 1.00 17.88 ATOM 1718 CD1 LEU A 253 40.172 41.298 21.409 1.00 18.95 ATOM 1719 CD2 LEU A 253 38.818 42.212 19.530 1.00 17.21 ATOM 1720 C LEU A 253 37.987 37.397 20.224 1.00 16.20 ATOM 1721 0 LEU A 253 38.817 36.489 20.186 1.00 15.34 ATOM 1722 N VAL A 254 36.817 37.345 19.595 1.00 15.06 ATOM 1723 CA VAL A 254 36.424 36.212 18.768 1.00 15.95 ATOM 1724 CB VAL A 254 35.152 35.510 19.335 1.00 17.77 ATOM 1725 CG1 VAL A 254 34.647 34.452 18.363 1.00 18.39 ATOM 1726 CG2 VAL A 254 35.471 34.858 20.671 1.00 17.11 ATOM 1727 C VAL A 254 36.136 36.737 17.363 1.00 15.21 ATOM 1728 0 VAL A 254 35.395 37.697 17.197 1.00 16.49 ATOM 1729 N LYS A 255 36.739 36.120 16.355 1.00 15.79 ATOM 1730 CA LYS A 255 36.526 36.546 14.978 1.00 15.67 ATOM 1731 CB LYS A 255 37.831 36.464 14.181 1.00 14.99 ATOM 1732 CG LYS A 255 37.716 36.986 12.763 1.00 16.27 ATOM 1733 CD LYS A 255 39.091 37.270 12.164 1.00 17.90 ATOM 1734 CE LYS A 255 38.977 37.918 10.785 1.00 16.12 ATOM 1735 NZ LYS A 255 40.306 38.385 10.305 1.00 17.24 ATOM 1736 C LYS A 255 35.464 35.660 14.343 1.00 17.11 ATOM 1737 0 LYS A 255 35.618 34.437 14.262 1.00 15.75 ATOM 1738 N ILE A 256 34.389 36.288 13.883 1.00 15.78 ATOM 1739 CA ILE A 256 33.284 35.555 13.294 1.00 15.09 ATOM 1740 CB ILE A 256 31.970 35.932 13.992 1.00 14.37 ATOM 1741 CG2 ILE A 256 32.129 35.743 15.489 1.00 14.88 ATOM 1742 CG1 ILE A 256 31.611 37.391 13.687 1.00 13.35 ATOM 1743 CD1 ILE A 256 30.324 37.871 14.348 1.00 10.32 ATOM 1744 C ILE A 256 33.119 35.753 11.794 1.00 15.04 ATOM 1745 0 ILE A 256 33.681 36.678 11.203 1.00 12.31 ATOM 1746 N ALA A 257 32.335 34.869 11.189 1.00 14.83 ATOM 1747 CA ALA A 257 32.074 34.922 9.758 1.00 18.10 ATOM 1748 CB ALA A 257 31.756 33.517 9.236 1.00 19.52 ATOM 1749 C ALA A 257 30.922 35.868 9.426 1.00 18.66 ATOM 1750 O ALA A 257 30.195 36.328 10.310 1.00 18.10 ATOM 1751 N PRO A 258 30.771 36.194 8.135 1.00 18.73 ATOM 1752 CD PRO A 258 31.860 36.055 7.148 1.00 17.46 ATOM 1753 CA PRO A 258 29.722 37.075 7.621 1.00 19.04

ATOM 1754 CB PRO A 258 30.441 37.839 6.524 1.00 17.64 ATOM 1755 CG PRO A 258 31.295 36.767 5.926 1.00 16.87 ATOM 1756 C PRO A 258 28.571 36.234 7.059 1.00 21.92 ATOM 1757 0 PRO A 258 27.612 36.769 6.500 1.00 22.89 ATOM 1758 N ASP A 259 28.677 34.915 7.214 1.00 21.14 ATOM 1759 CA ASP A 259 27.668 33.995 6.699 1.00 22.52 ATOM 1760 CB ASP A 259 28.346 32.914 5.849 1.00 20.83 ATOM 1761 CG ASP A 259 29.371 33.489 4.889 1.00 22.44 ATOM 1762 OD1 ASP A 259 29.029 34.444 4.159 1.00 19.29 ATOM 1763 OD2 ASP A 259 30.518 32.985 4.861 1.00 22.71 ATOM 1764 C ASP A 259 26.849 33.333 7.803 1.00 23.56 ATOM 1765 0 ASP A 259 26.277 32.265 7.605 1.00 24.81 ATOM 1766 N LEU A 260 26.790 33.975 8.963 1.00 23. 55 ATOM 1767 CA LEU A 260 26.048 33.440 10.097 1.00 22.28 ATOM 1768 CB LEU A 260 26.566 34.064 11.397 1.00 22.44 ATOM 1769 CG LEU A 260 28.031 33.801 11.760 1.00 24.01 ATOM 1770 CD1 LEU A 260 28.439 34.667 12.947 1.00 25.25 ATOM 1771 CD2 LEU A 260 28.215 32.329 12.079 1.00 22.47 ATOM 1772 C LEU A 260 24.552 33.705 9.978 1.00 21.83 ATOM 1773 0 LEU A 260 24.140 34.741 9.461 1.00 23.40 ATOM 1774 N THR A 261 23.742 32.764 10.453 1.00 20.47 ATOM 1775 CA THR A 261 22.291 32.925 10.433 1.00 19.70 ATOM 1776 CB THR A 261 21.558 31.590 10.712 1.00 18.67 ATOM 1777 OG1 THR A 261 21.930 31.106 12.011 1.00 18.39 ATOM 1778 CG2 THR A 261 21.908 30.545 9.665 1.00 12.17 ATOM 1779 C THR A 261 21.951 33.882 11.576 1.00 21.78 ATOM 1780 O THR A 261 22.805 34.185 12.411 1.00 22.78 ATOM 1781 N SER A 262 20.714 34.361 11.619 1.00 21.77 ATOM 1782 CA SER A 262 20.312 35.256 12.696 1.00 22.54 ATOM 1783 CB SER A 262 18.882 35.748 12.474 1.00 23.02 ATOM 1784 OG SER A 262 18.810 36.562 11.322 1.00 26.73 ATOM 1785 C SER A 262 20.403 34.525 14.038 1.00 22.61 ATOM 1786 0 SER A 262 20.634 35.143 15.076 1.00 21.53 ATOM 1787 N GLN A 263 20.222 33.208 14.007 1.00 21.94 ATOM 1788 CA GLN A 263 20.291 32.400 15.219 1.00 22.83 ATOM 1789 CB GLN A 263 19.786 30.981 14.944 1.00 23.57 ATOM 1790 CG GLN A 263 19.863 30.049 16.148 1.00 30.01

ATOM 1791 CD GLN A 263 18.723 30.250 17.133 1.00 31.49 ATOM 1792 OE1 GLN A 263 17.588 29.856 16.870 1.00 32.99 ATOM 1793 NE2 GLN A 263 19.022 30.868 18.269 1.00 32.25 ATOM 1794 C GLN A 263 21.723 32.338 15.756 1.00 21.26 ATOM 1795 O GLN A 263 21.947 32.488 16.959 1.00 20.81 ATOM 1796 N ASP A 264 22.688 32.119 14.865 1.00 21.06 ATOM 1797 CA ASP A 264 24.088 32.042 15.270 1.00 19.84 ATOM 1798 CB ASP A 264 25.000 31.772 14.069 1.00 22.89 ATOM 1799 CG ASP A 264 24.752 30.414 13.431 1.00 25.22 ATOM 1800 OD1 ASP A 264 24.372 29.471 14.158 1.00 22.28 ATOM 1801 OD2 ASP A 264 24.954 30.293 12.201 1.00 26.91 ATOM 1802 C ASP A 264 24.530 33.334 15.937 1.00 19.05 ATOM 1803 0 ASP A 264 25.200 33.315 16.970 1.00 19.15 ATOM 1804 N LYS A 265 24.154 34.459 15.340 1.00 17.89 ATOM 1805 CA LYS A 265 24.518 35.759 15.877 1.00 19.66 ATOM 1806 CB LYS A 265 24.060 36.864 14.925 1.00 19.31 ATOM 1807 CG LYS A 265 24.763 36.821 13.580 1.00 19.49 ATOM 1808 CD LYS A 265 24.098 37.754 12.586 1.00 23.63 ATOM 1809 CE LYS A 265 24.453 37.370 11.162 1.00 24.49 ATOM 1810 NZ LYS A 265 23.506 37.954 10.171 1.00 27.62 ATOM 1811 C LYS A 265 23.931 35.968 17.263 1.00 20.65 ATOM 1812 0 LYS A 265 24.612 36.470 18.157 1.00 21.98 ATOM 1813 N GLU A 266 22.667 35.590 17.442 1.00 21.27 ATOM 1814 CA GLU A 266 22.024 35.721 18.743 1.00 20.98 ATOM 1815 CB GLU A 266 20.566 35.239 18.683 1.00 20.85 ATOM 1816 CG GLU A 266 19.657 36.112 17.833 1.00 25.52 ATOM 1817 CD GLU A 266 18.228 35.590 17.739 1.00 26.89 ATOM 1818 OE1 GLU A 266 17.438 36.187 16.983 1.00 29.13 ATOM 1819 OE2 GLU A 266 17.889 34.592 18.414 1.00 27.61 ATOM 1820 C GLU A 266 22.798 34.886 19.766 1.00 19.97 ATOM 1821 0 GLU A 266 23.099 35.358 20.860 1.00 18.00 ATOM 1822 N ASP A 267 23.126 33.647 19.402 1.00 20.17 ATOM 1823 CA ASP A 267 23.860 32.769 20.310 1.00 21.48 ATOM 1824 CB ASP A 267 24.015 31.365 19.714 1.00 21.94 ATOM 1825 CG ASP A 267 22.695 30.622 19.619 1.00 25.04 ATOM 1826 OD1 ASP A 267 21.762 30.968 20.376 1.00 23.89 ATOM 1827 OD2 ASP A 267 22.592 29.685 18.797 1.00 27.05

ATOM 1828 C ASP A 267 25.232 33.336 20.648 1.00 21.55 ATOM 1829 0 ASP A 267 25.619 33.386 21.816 1.00 22.82 ATOM 1830 N ILE A 268 25.967 33.765 19.628 1.00 19.94 ATOM 1831 CA ILE A 268 27.287 34.329 19.856 1.00 19.42 ATOM 1832 CB ILE A 268 27.954 34.753 18.531 1.00 19.50 ATOM 1833 CG2 ILE A 268 29.181 35.611 18.815 1.00 16.97 ATOM 1834 CG1 ILE A 268 28.324 33.505 17.726 1.00 20.05 ATOM 1835 CD1 ILE A 268 28.914 33.798 16.367 1.00 21.73 ATOM 1836 C ILE A 268 27.201 35.532 20.784 1.00 18.16 ATOM 1837 O ILE A 268 28.025 35.688 21.683 1.00 18.08 ATOM 1838 N ALA A 269 26.197 36.376 20.573 1.00 17.88 ATOM 1839 CA ALA A 269 26.023 37.563 21.405 1.00 19.04 ATOM 1840 CB ALA A 269 24.885 38.414 20.872 1.00 17.94 ATOM 1841 C ALA A 269 25.739 37.151 22.845 1.00 20.04 ATOM 1842 O ALA A 269 26.225 37.769 23.791 1.00 19.17 ATOM 1843 N SER A 270 24.951 36.094 22.999 1.00 20.63 ATOM 1844 CA SER A 270 24.598 35.590 24.317 1.00 20.97 ATOM 1845 CB SER A 270 23.517 34.514 24.182 1.00 20.46 ATOM 1846 OG SER A 270 23.269 33.883 25.423 1.00 23.18 ATOM 1847 C SER A 270 25.823 35.024 25.042 1.00 20.72 ATOM 1848 0 SER A 270 26.067 35.351 26.200 1.00 22.09 ATOM 1849 N VAL A 271 26.590 34.177 24.361 1.00 20.12 ATOM 1850 CA VAL A 271 27.782 33.582 24.958 1.00 20.78 ATOM 1851 CB VAL A 271 28.432 32.561 24.004 1.00 19.82 ATOM 1852 CG1 VAL A 271 29.748 32.060 24.592 1.00 20.03 ATOM 1853 CG2 VAL A 271 27.487 31.398 23.773 1.00 16.90 ATOM 1854 C VAL A 271 28.820 34.647 25.315 1.00 23.07 ATOM 1855 0 VAL A 271 29.419 34.614 26.389 1.00 21.64 ATOM 1856 N VAL A 272 29.023 35.595 24.406 1.00 25.16 ATOM 1857 CA VAL A 272 29.981 36.670 24.620 1.00 27.00 ATOM 1858 CB VAL A 272 29.977 37.649 23.421 1.00 27.76 ATOM 1859 CG1 VAL A 272 30.548 38.995 23.834 1.00 27.78 ATOM 1860 CG2 VAL A 272 30.798 37.058 22.275 1.00 25.76 ATOM 1861 C VAL A 272 29.710 37.439 25.911 1.00 28.67 ATOM 1862 0 VAL A 272 30.631 37.722 26.682 1.00 29.19 ATOM 1863 N LYS A 273 28.447 37.767 26.154 1.00 29.06 ATOM 1864 CA LYS A 273 28.086 38.510 27.356 1.00 31.31

ATOM 1865 CB LYS A 273 26.736 39.211 27.152 1.00 31.93 ATOM 1866 CG LYS A 273 26.814 40.342 26.115 1.00 34.44 ATOM 1867 CD LYS A 273 25.516 41.133 26.008 1.00 36.38 ATOM 1868 CE LYS A 273 24.367 40.261 25.534 1.00 35.40 ATOM 1869 NZ LYS A 273 23.122 41.050 25.352 1.00 36.63 ATOM 1870 C LYS A 273 28.065 37.636 28.607 1.00 30.65 ATOM 1871 0 LYS A 273 28.303 38.115 29.714 1.00 30.52 ATOM 1872 N GLU A 274 27.793 36.350 28.426 1.00 29.82 ATOM 1873 CA GLU A 274 27.765 35.416 29.542 1.00 29.43 ATOM 1874 CB GLU A 274 27.191 34.074 29.083 1.00 30.26 ATOM 1875 CG GLU A 274 27.098 33.026 30.176 1.00 35.07 ATOM 1876 CD GLU A 274 27.060 31.611 29.623 1.00 38.26 ATOM 1877 OE1 GLU A 274 26.381 31.388 28.599 1.00 39.06 ATOM 1878 OE2 GLU A 274 27.706 30.717 30.215 1.00 41.36 ATOM 1879 C GLU A 274 29.179 35.188 30.094 1.00 29.77 ATOM 1880 0 GLU A 274 29.387 35.174 31.309 1.00 29.55 ATOM 1881 N LEU A 275 30.145 35.021 29.191 1.00 27.28 ATOM 1882 CA LEU A 275 31.531 34.754 29.574 1.00 24.61 ATOM 1883 CB LEU A 275 32.184 33.835 28.542 1.00 22.55 ATOM 1884 CG LEU A 275 31.489 32.496 28.298 1.00 22.58 ATOM 1885 CD1 LEU A 275 32.236 31.717 27.224 1.00 20.96 ATOM 1886 CD2 LEU A 275 31.435 31.711 29.600 1.00 22.06 ATOM 1887 C LEU A 275 32.412 35.979 29.764 1.00 23.92 ATOM 1888 0 LEU A 275 33.511 35.873 30.300 1.00 24.92 ATOM 1889 N GLY A 276 31.943 37.138 29.322 1.00 23.96 ATOM 1890 CA GLY A 276 32.743 38.340 29.466 1.00 22.49 ATOM 1891 C GLY A 276 33.783 38.516 28.368 1.00 24.06 ATOM 1892 0 GLY A 276 34.834 39.115 28.597 1.00 23.35 ATOM 1893 N ILE A 277 33.504 37.991 27.176 1.00 24.12 ATOM 1894 CA ILE A 277 34.426 38.138 26.051 1.00 22.72 ATOM 1895 CB ILE A 277 33.814 37.595 24.744 1.00 23.36 ATOM 1896 CG2 ILE A 277 34.734 37.891 23.570 1.00 22.55 ATOM 1897 CG1 ILE A 277 33.609 36.086 24.863 1.00 23.90 ATOM 1898 CD1 ILE A 277 34.891 35.331 25.133 1.00 27.10 ATOM 1899 C ILE A 277 34.724 39.627 25.885 1.00 22.38 ATOM 1900 O ILE A 277 33.817 40.461 25.921 1.00 20.66 ATOM 1901 N ASP A 278 35.997 39.954 25.702 1.00 21.22

ATOM 1902 CA ASP A 278 36.426 41.340 25.578 1.00 19.68 ATOM 1903 CB ASP A 278 37.940 41.420 25.751 1.00 19.24 ATOM 1904 CG ASP A 278 38.389 40.902 27.093 1.00 18.89 ATOM 1905 OD1 ASP A 278 37.973 41.489 28.114 1.00 20.89 ATOM 1906 OD2 ASP A 278 39.145 39.909 27.130 1.00 18. 95 ATOM 1907 C ASP A 278 36.027 42.056 24.300 1.00 19.50 ATOM 1908 0 ASP A 278 35.888 43.277 24.294 1.00 20.84 ATOM 1909 N GLY A 279 35.844 41.312 23.216 1.00 17.90 ATOM 1910 CA GLY A 279 35.473 41.961 21.977 1.00 17.02 ATOM 1911 C GLY A 279 35.240 41.031 20.809 1.00 16.34 ATOM 1912 0 GLY A 279 35.461 39.825 20.896 1.00 16.62 ATOM 1913 N LEU A 280 34.794 41.609 19.702 1.00 16.08 ATOM 1914 CA LEU A 280 34.511 40.843 18.501 1.00 1'6. 76 ATOM 1915 CB LEU A 280 32.999 40.798 18.239 1.00 14.21 ATOM 1916 CG LEU A 280 32.073 40.052 19.205 1.00 16.52 ATOM 1917 CD1 LEU A 280 30.617 40.361 18.865 1.00 14.62 ATOM 1918 CD2 LEU A 280 32.335 38.555 19.123 1.00 14.09 ATOM 1919 C LEU A 280 35.190 41.450 17.284 1.00 15.76 ATOM 1920 O LEU A 280 35.264 42.673 17.142 1.00 15.21 ATOM 1921 N ILE A 281 35.714 40.586 16.425 1.00 13.97 ATOM 1922 CA ILE A 281 36.316 41.040 15.188 1.00 14.74 ATOM 1923 CB ILE A 281 37.668 40.375 14.910 1.00 12.59 ATOM 1924 CG2 ILE A 281 38.237 40.914 13.603 1.00 13.24 ATOM 1925 CG1 ILE A 281 38.637 40.691 16.057 1.00 11.42 ATOM 1926 CD1 ILE A 281 40.099 40.695 15.650 1.00 9.11 ATOM 1927 C ILE A 281 35.255 40.567 14.218 1.00 16.53 ATOM 1928 0 ILE A 281 35.042 39.362 14.036 1.00 15.17 ATOM 1929 N VAL A 282 34.561 41.513 13.603 1.00 18.83 ATOM 1930 CA VAL A 282 33.469 41.111 12.753 1.00 20.72 ATOM 1931 CB VAL A 282 32.257 42.012 13.007 1.00 20.08 ATOM 1932 CG1 VAL A 282 31.069 41.563 12.177 1.00 15.79 ATOM 1933 CG2 VAL A 282 31.914 41.941 14.486 1.00 15.44 ATOM 1934 C VAL A 282 33.702 40.896 11.274 1.00 23.98 ATOM 1935 0 VAL A 282 34.040 41.793 10.498 1.00 22.59 ATOM 1936 N THR A 283 33.464 39.629 10.953 1.00 26.57 ATOM 1937 CA THR A 283 33.562 38.963 9.669 1.00 24.80 ATOM 1938 CB THR A 283 32.550 39.499 8.604 1.00 22.20

ATOM 1939 OG1 THR A 283 33.258 39.909 7.430 1.00 20. 11 ATOM 1940 CG2 THR A 283 31.692 40.619 9.158 1.00 25.27 ATOM 1941 C THR A 283 34.915 38.764 9.022 1.00 23.47 ATOM 1942 O THR A 283 35.729 39.672 8.824 1.00 22.34 ATOM 1943 N ASN A 284 35.117 37.490 8.739 1.00 20.14 ATOM 1944 CA ASN A 284 36.271 36.955 8.080 1.00 17.94 ATOM 1945 CB ASN A 284 36.427 35.498 8.507 1.00 16.23 ATOM 1946 CG ASN A 284 37.822 34.989 8.327 1.00 15.24 ATOM 1947 OD1 ASN A 284 38.370 35.042 7.234 1.00 16.87 ATOM 1948 ND2 ASN A 284 38.411 34.484 9.406 1.00 15.85 ATOM 1949 C ASN A 284 35.793 37.038 6.633 1.00 17.29 ATOM 1950 O ASN A 284 34.912 37.843 6.314 1.00 17.42 ATOM 1951 N THR A 285 36.346 36.208 5.762 1.00 15.65 ATOM 1952 CA THR A 285 35.920 36.215 4.371 1.00 14.49 ATOM 1953 CB THR A 285 36.970 35.548 3.469 1.00 13.54 ATOM 1954 OG1 THR A 285 37.344 34.284 4.030 1.00 11.73 ATOM 1955 CG2 THR A 285 38.205 36.435 3.348 1.00 11.58 ATOM 1956 C THR A 285 34.600 35.454 4.268 1.00 14.94 ATOM 1957 O THR A 285 34.250 34.681 5.164 1.00 13.05 ATOM 1958 N THR A 286 33.872 35.679 3.177 1.00 13.81 ATOM 1959 CA THR A 286 32.585 35.020 2.961 1.00 12.17 ATOM 1960 CB THR A 286 31.535 36.022 2.419 1.00 10.38 ATOM 1961 OG1 THR A 286 30.296 35.346 2.200 1.00 13.59 ATOM 1962 CG2 THR A 286 31.996 36.620 1.096 1.00 9.39 ATOM 1963 C THR A 286 32.679 33.864 1.965 1.00 12.82 ATOM 1964 O THR A 286 33.406 33.953 0.969 1.00 11.73 ATOM 1965 N VAL A 287 31.945 32.785 2.234 1.00 12.56 ATOM 1966 CA VAL A 287 31.926 31.639 1.330 1.00 15.17 ATOM 1967 CB VAL A 287 31.700 30.290 2.067 1.00 15.85 ATOM 1968 CG1 VAL A 287 32.817 30.045 3.059 1.00 16.20 ATOM 1969 CG2 VAL A 287 30.347 30.285 2.764 1.00 16.12 ATOM 1970 C VAL A 287 30.783 31.846 0.337 1.00 16.66 ATOM 1971 O VAL A 287 30.541 31.013-0. 536 1.00 16.82 ATOM 1972 N SERA 288 30.073 32.959 0.483 1.00 15.63 ATOM 1973 CA SERA 288 28.985 33.266-0. 432 1.00 15.70 ATOM 1974 CB SERA 288 28.001 34.259 0.197 1.00 14.48 ATOM 1975 OG SERA 288 28.554 35.568 0.229 1.00 13.23

ATOM 1976 C SER A 288 29.611 33.903-1. 665 1.00 16.39 ATOM 1977 O SER A 288 30.764 34.334-1. 635 1.00 15.81 ATOM 1978 N ARG A 289 28.847 33.960-2. 747 1.00 17.38 ATOM 1979 CA ARG A 289 29.318 34.563-3. 985 1.00 18.89 ATOM 1980 CB ARG A 289 29.629 33.480-5. 019 1.00 18.09 ATOM 1981 CG ARG A 289 30.839 32.628-4. 671 1.00 18.05 ATOM 1982 CD ARG A 289 32.125 33.435-4. 745 1.00 16.68 ATOM 1983 NE ARG A 289 33.299 32.594-4. 532 1.00 15.91 ATOM 1984 CZ ARG A 289 33.787 32.261-3. 340 1.00 16.31 ATOM 1985 NH1 ARG A 289 34. 858 31.477-3. 261 1.00 13.06 ATOM 1986 NH2 ARG A 289 33.220 32.721-2. 229 1.00 13.64 ATOM 1987 C ARG A 289 28.206 35.475-4. 480 1.00 20.53 ATOM 1988 0 ARG A 289 27.368 35.079-5. 296 1.00 21. 36 ATOM 1989 N PRO A 290 28.182 36.715-3. 975 1.00 19.53 ATOM 1990 CD PRO A 290 29.209 37.305-3. 100 1.00 17.95 ATOM 1991 CA PRO A 290 27.176 37.710-4. 343 1.00 18.26 ATOM 1992 CB PRO A 290 27.763 39.008-3. 793 1.00 18.04 ATOM 1993 CG PRO A 290 28.515 38.546-2. 589 1.00 17.02 ATOM 1994 C PRO A 290 26.964 37.767-5. 845 1.00 18.99 ATOM 1995 O PRO A 290 27.921 37.684-6. 617 1.00 19.64 ATOM 1996 N ALA A 291 25.707 37.889-6. 262 1.00 18.82 ATOM 1997 CA ALA A 291 25.405 37., 987-7. 685 1.00 16.85 ATOM 1998 CB ALA A 291 23.901 38.084-7. 899 1.00 14.77 ATOM 1999 C ALA A 291 26.090 39.255-8. 189 1.00 14.94 ATOM 2000 0 ALA A 291 26.138 40.258-7. 482 1.00 15.17 ATOM 2001 N GLY A 292 26.636 39.206-9. 398 1.00 13.56 ATOM 2002 CA GLY A 292 27.295 40.377-9. 939 1.00 14.88 ATOM 2003 C GLY A 292 28.797 40.238-10. 102 1.00 15.80 ATOM 2004 0 GLY A 292 29.403 41.002-10. 852 1.00 17.47 ATOM 2005 N LEU A 293 29.406 39.286-9. 398 1.00 15.22 ATOM 2006 CA LEU A 293 30.846 39.074-9. 520 1.00 15.55 ATOM 2007 CB LEU A 293 31.282 37.831-8. 739 1.00 15.69 ATOM 2008 CG LEU A 293 31.174 37.866-7. 210 1.00 14.60 ATOM 2009 CD1 LEU A 293 31.673 36.545-6. 650 1.00 14.40 ATOM 2010 CD2 LEU A 293 31.995 39.020-6. 647 1.00 12.10 ATOM 2011 C LEU A 293 31.185 38.891-10. 991 1.00 15.60 ATOM 2012 O LEU A 293 30. 510 38.147-11. 702 1.00 16.58

ATOM 2013 N GLN A 294 32.230 39.576-11. 444 1.00 16.80 ATOM 2014 CA GLN A 294 32.653 39.503-12. 835 1.00 17. 11 ATOM 2015 CB GLN A 294 32.859 40.913-13. 390 1.00 18.48 ATOM 2016 CG GLN A 294 31.589 41.728-13. 450 1.00 19.20 ATOM 2017 CD GLN A 294 30.512 41.030-14. 249 1.00 19.74 ATOM 2018 OE1 GLN A 294 30.709 40.716-15. 420 1.00 20.35 ATOM 2019 NE2 GLN A 294 29.366 40.780-13. 620 1.00 17.29 ATOM 2020 C GLN A 294 33.929 38.701-13. 029 1.00 18.33 ATOM 2021 0 GLN A 294 34.145 38.122-14. 097 1.00 19.34 ATOM 2022 N GLY A 295 34.772 38.678-11. 999 1.00 16.78 ATOM 2023 CA GLY A 295 36.029 37.960-12. 076 1.00 14.58 ATOM 2024 C GLY A 295 35.915 36.580-12. 693 1.00 17.14 ATOM 2025 0 GLY A 295 34.976 35.828-12. 413 1.00 15. 75 ATOM 2026 N ALA A 296 36.878 36.244-13. 541 1.00 16.27 ATOM 2027 CA ALA A 296 36.890 34.942-14. 195 1.00 16.90 ATOM 2028 CB ALA A 296 38.039 34. 880-15. 206 1.00 14.08 ATOM 2029 C ALA A 296 37.030 33.812-13. 175 1.00 16.05 ATOM 2030 0 ALA A 296 36.515 32.712-13. 381 1.00 16.89 ATOM 2031 N LEU A 297 37.712 34.101-12. 068 1.00 15.74 ATOM 2032 CA LEU A 297 37.967 33.112-11. 019 1.00 15.01 ATOM 2033 CB LEU A 297 39.379 33.327-10. 467 1.00 12.31 ATOM 2034 CG LEU A 297 40.468 33.402-11. 544 1.00 14.81 ATOM 2035 CD1 LEU A 297 41.783 33.870-10. 927 1.00 14.19 ATOM 2036 CD2 LEU A 297 40.627 32.039-12. 214 1.00 12.20 ATOM 2037 C LEU A 297 36.965 33.148-9. 867 1.00 14.73 ATOM 2038 0 LEU A 297 37.250 32.650-8. 774 1.00 14.27 ATOM 2039 N ARG A 298 35.793 33.724-10. 123 1.00 15.51 ATOM 2040 CA ARG A 298 34.743 33.865-9. 112 1.00 15.51 ATOM 2041 CB ARG A 298 33.558 34.641-9. 699 1.00 14.80 ATOM 2042 CG ARG A 298 32.734 33.858-10. 711 1.00 14.58 ATOM 2043 CD ARG A 298 31.673 34.741-11. 370 1.00 15.06 ATOM 2044 NE ARG A 298 30.782 33.966-12. 229 1.00 14.79 ATOM 2045 CZ ARG A 298 29.917 34.491-13. 093 1.00 15.35 ATOM 2046 NH1 ARG A 298 29.151 33.695-13. 828 1.00 8.68 ATOM 2047 NH2 ARG A 298 29.822 35.812-13. 233 1.00 14.16 ATOM 2048 C ARG A 298 34.233 32.553-8. 519 1.00 16.08 ATOM 2049 0 ARG A 298 33.719 32.537-7. 398 1.00 16.02

ATOM 2050 N SER A 299 34.371 31.458-9. 261 1.00 15.60 ATOM 2051 CA SER A 299 33.899 30. 168-8. 780 1.00 16.40 ATOM 2052 CB SER A 299 33.206 29.409-9. 910 1.00 15.38 ATOM 2053 OG SER A 299 31.920 29.958-10. 140 1.00 14.75 ATOM 2054 C SER A 299 34.958 29.285-8. 124 1.00 17.70 ATOM 2055 0 SER A 299 34.742 28.088-7. 934 1.00 19.57 ATOM 2056 N GLU A 300 36.099 29.873-7. 782 1.00 15.48 ATOM 2057 CA GLU A 300 37.153 29.135-7. 096 1.00 16.69 ATOM 2058 CB GLU A 300 38.473 29.921-7. 109 1.00 15.70 ATOM 2059 CG GLU A 300 39.177 29.968-8. 460 1.00 19.09 ATOM 2060 CD GLU A 300 39.894 28.668-8. 796 1.00 19.66 ATOM 2061 OE1 GLU A 300 40.293 28.485-9. 965 1.00 21.52 ATOM 2062 OE2 GLU A 300 40.069 27.831-7. 887 1.00 20.79 ATOM 2063 C GLU A 300 36.698 28.957-5. 644 1.00 17.50 ATOM 2064 O GLU A 300 36.012 29.818-5. 085 1.00 18.25 ATOM 2065 N THR A 301 37.075 27.837-5. 043 1.00 16.77 ATOM 2066 CA THR A 301 36.733 27.560-3. 657 1.00 15.87 ATOM 2067 CB THR A 301 37.035 26.089-3. 302 1.00 16.02 ATOM 2068 OG1 THR A 301 36.030 25.245-3. 873 1.00 19.42 ATOM 2069 CG2 THR A 301 37.077 25.894-1. 798 1.00 14.14 ATOM 2070 C THR A 301 37.564 28.465-2. 747 1.00 14.56 ATOM 2071 O THR A 301 38.729 28.745-3. 037 1.00 13.06 ATOM 2072 N GLY A 302 36.968 28.923-1. 651 1.00 14.25 ATOM 2073 CA GLY A 302 37.697 29.778-0. 732 1.00 13.34 ATOM 2074 C GLY A 302 36.874 30.924-0. 184 1.00 14.22 ATOM 2075 O GLY A 302 35.682 31.042-0. 471 1.00 13.86 ATOM 2076 N GLY A 303 37.514 31.769 0.619 1.00 14.41 ATOM 2077 CA GLY A 303 36.829 32.906 1.199 1.00 12.84 ATOM 2078 C GLY A 303 37.005 34.138 0.337 1.00 12.25 ATOM 2079 0 GLY A 303 38.109 34.439-0. 115 1.00 12.09 ATOM 2080 N LEU A 304 35.906 34.850 0. 109 1.00 12.88 ATOM 2081 CA LEU A 304 35.912 36.057-0. 709 1.00 12.21 ATOM 2082 CB LEU A 304 34.588 36.171-1. 470 1.00 13.65 ATOM 2083 CG LEU A 304 34.314 37.450-2. 269 1.00 15.74 ATOM 2084 CD1 LEU A 304 35.287 37.566-3. 428 1.00 16.08 ATOM 2085 CD2 LEU A 304 32.881 37.412-2. 792 1.00 20.89 ATOM 2086 C LEU A 304 36.120 37.301 0.147 1.00 12.48

ATOM 2087 0 LEU A 304 35.517 37.447 1.211 1.00 14.13 ATOM 2088 N SER A 305 36.970 38.201-0. 326 1.00 12.36 ATOM 2089 CA SER A 305 37.253 39.432 0.396 1.00 13.71 ATOM 2090 CB SER A 305 38.636 39.348 1.042 1.00 13.43 ATOM 2091 OG SER A 305 39.640 39.207 0.051 1.00 13.79 ATOM 2092 C SER A 305 37.205 40.615-0. 566 1.00 13.39 ATOM 2093 0 SER A 305 37.120 40.428-1. 778 1.00 14.42 ATOM 2094 N GLY A 306 37.262 41.830-0. 029 1.00 13.29 ATOM 2095 CA GLY A 306 37.230 43.002-0. 887 1.00 12.97 ATOM 2096 C GLY A 306 35.877 43.690-0. 938 1.00 14.84 ATOM 2097 0 GLY A 306 35.009 43.444-0. 096 1.00 14.46 ATOM 2098 N LYS A 307 35.686 44.539-1. 945 1.00 16.17 ATOM 2099 CA LYS A 307 34.444 45.290-2. 088 1.00 16.52 ATOM 2100 CB LYS A 307 34.460 46.120-3. 385 1.00 18.40 ATOM 2101 CG LYS A 307 33.422 47.261-3. 379 1.00 25.17 ATOM 2102 CD LYS A 307 33.336 48.025-4. 705 1.00 27.88 ATOM 2103 CE LYS A 307 34.621 48.787-5. 010 1.00 29.73 ATOM 2104 NZ LYS A 307 34.986 49.758-3. 934 1.00 29.23 ATOM 2105 C LYS A 307 33.157 44.466-2. 012 1.00 15.26 ATOM 2106 O LYS A 307 32.194 44.881-1. 367 1.00 16.38 ATOM 2107 N PRO A 308 33.114 43.292-2. 663 1.00 14.54 ATOM 2108 CD PRO A 308 34.114 42.680-3. 556 1.00 14.56 ATOM 2109 CA PRO A 308 31.894 42.475-2. 613 1.00 14.08 ATOM 2110 CB PRO A 308 32.255 41.259-3. 465 1.00 14.39 ATOM 2111 CG PRO A 308 33.248 41.818-4. 448 1.00 15.27 ATOM 2112 C PRO A 308 31.478 42.074-1. 196 1.00 15.08 ATOM 2113 0 PRO A 308 30.313 41.764-0. 945 1.00 16.18 ATOM 2114 N LEU A 309 32.436 42.079-0. 276 1.00 15.24 ATOM 2115 CA LEU A 309 32.182 41.709 1.114 1.00 15.60 ATOM 2116 CB LEU A 309 33.405 40.979 1.679 1.00 14.32 ATOM 2117 CG LEU A 309 33.524 40.802 3.201 1.00 13.34 ATOM 2118 CD1 LEU A 309 32.452 39.850 3.714 1.00 12.74 ATOM 2119 CD2 LEU A 309 34.903 40.251 3.532 1.00 12.50 ATOM 2120 C LEU A 309 31.854 42.890 2.032 1.00 16.28 ATOM 2121 0 LEU A 309 31.229 42.710 3.076 1.00 17.72 ATOM 2122 N ARG A 310 32.264 44. 090 1.633 1.00 14.78 ATOM 2123 CA ARG A 310 32.084 45.286 2.453 1.00 15.52

ATOM 2124 CB ARG A 310 32.340 46.553 1.623 1.00 12.86 ATOM 2125 CG ARG A 310 32.388 47.832 2.468 1.00 14.96 ATOM 2126 CD ARG A 310 32.520 49.072 1.597 1.00 12.65 ATOM 2127 NE ARG A 310 31.446 49.104 0.611 1.00 14.57 ATOM 2128 CZ ARG A 310 31.450 49.852-0. 485 1.00 13.39 ATOM 2129 NH1 ARG A 310 30.422 49.793-1. 320 1.00 11.24 ATOM 2130 NH2 ARG A 310 32.479 50.652-0. 747 1.00 12.51 ATOM 2131 C ARG A 310 30.772 45.455 3.215 1.00 16.19 ATOM 2132 0 ARG A 310 30.757 45.412 4.445 1.00 16.77 ATOM 2133 N ASP A 311 29.675 45.659 2.496 1.00 17.50 ATOM 2134 CA ASP A 311 28.391 45.878 3.147 1.00 17.75 ATOM 2135 CB ASP A 311 27.381 46.369 2.109 1.00 19.42 ATOM 2136 CG ASP A 311 27.661 47.809 1.676 1.00 21.08 ATOM 2137 OD1 ASP A 311 28.771 48.309 1.974 1.00 20.69 ATOM 2138 OD2 ASP A 311 26.787 48.441 1.046 1.00 20.67 ATOM 2139 C ASP A 311 27.864 44.687 3.942 1.00 18.47 ATOM 2140 O ASP A 311 27.205 44.862 4.969 1.00 17.98 ATOM 2141 N LEU A 312 28.162 43.478 3.483 1.00 17.76 ATOM 2142 CA LEU A 312 27.741 42.289 4.207 1.00 17.86 ATOM 2143 CB LEU A 312 28.179 41.027 3.459 1.00 18.99 ATOM 2144 CG LEU A 312 27.783 39.686 4.084 1.00 23.39 ATOM 2145 CD1 LEU A 312 26.265 39.602 4.207 1.00 22.84 ATOM 2146 CD2 LEU A 312 28.308 38.538 3.217 1.00 23.42 ATOM 2147 C LEU A 312 28.410 42.346 5.585 1.00 17.48 ATOM 2148 O LEU A 312 27.812 41.959 6.592 1.00 16.53 ATOM 2149 N SER A 313 29.649 42.840 5.621 1.00 16.16 ATOM 2150 CA SER A 313 30.397 42.971 6.873 1.00 17.10 ATOM 2151 CB SER A 313 31.873 43.309 6.610 1.00 17.49 ATOM 2152 OG SER A 313 32.612 42.163 6.244 1.00 23.70 ATOM 2153 C SER A 313 29.808 44.067 7.749 1.00 15.96 ATOM 2154 0 SER A 313 29.607 43.875 8.949 1.00 16.85 ATOM 2155 N THR A 314 29.549 45.221 7.143 1.00 13.84 ATOM 2156 CA THR A 314 28.993 46.353 7.869 1.00 14.33 ATOM 2157 CB THR A 314 28.745 47.551 6.934 1.00 13.64 ATOM 2158 OG1 THR A 314 29.981 47.935 6.321 1.00 13.07 ATOM 2159 CG2 THR A 314 28.190 48.731 7.715 1.00 12.00 ATOM 2160 C THR A 314 27.686 45.969 8.541 1.00 14.80

ATOM 2161 0 THR A 314 27.470 46.292 9.707 1.00 16.48 ATOM 2162 N GLN A 315 26.820 45. 269 7.811 1.00 15.30 ATOM 2163 CA GLN A 315 25.544 44.848 8.370 1.00 14.88 ATOM 2164 CB GLN A 315 24.658 44.219 7.288 1.00 13.95 ATOM 2165 CG GLN A 315 24.136 45.209 6.245 1.00 15.23 ATOM 2166 CD GLN A 315 23.176 46.250 6.828 1.00 15.21 ATOM 2167 OE1 GLN A 315 23.529 46.999 7.735 0.50 14.28 ATOM 2168 NE2 GLN A 315 21.963 46.297 6.297 0.50 12.79 ATOM 2169 C GLN A 315 25.743 43.869 9.523 1.00 14.34 ATOM 2170 0 GLN A 315 24.981 43.887 10.487 1.00 15.66 ATOM 2171 N THR A 316 26.765 43.019 9.439 1.00 14.94 ATOM 2172 CA THR A 316 27.021 42.062 10.521 1.00 13.97 ATOM 2173 CB THR A 316 28.103 41.018 10.130 1.00 13.18 ATOM 2174 OG1 THR A 316 27.681 40.314 8.958 1.00 14.58 ATOM 2175 CG2 THR A 316 28.306 40.000 11.255 1.00 11.68 ATOM 2176 C THR A 316 27.479 42.839 11.752 1.00 13.29 ATOM 2177 0 THR A 316 27.133 42.498 12.881 1.00 13.77 ATOM 2178 N ILE A 317 28.247 43.897 11.522 1.00 13.34 ATOM 2179 CA ILE A 317 28.728 44.738 12.609 1.00 13.60 ATOM 2180 CB ILE A 317 29.711 45.803 12.095 1.00 12.88 ATOM 2181 CG2 ILE A 317 29.990 46.820 13.199 1.00 12.51 ATOM 2182 CG1 ILE A 317 30.998 45.132 11.609 1.00 8.92 ATOM 2183 CD1 ILE A 317 31.890 46.038 10.782 1.00 8.20 ATOM 2184 C ILE A 317 27.548 45.450 13.256 1.00 15.33 ATOM 2185 0 ILE A 317 27.442 45.508 14.482 1.00 14.07 ATOM 2186 N ARG A 318 26.664 45.985 12.415 1.00 15.26 ATOM 2187 CA ARG A 318 25.482 46.704 12.876 1.00 16.00 ATOM 2188 CB ARG A 318 24.653 47.163 11.664 1.00 16.04 ATOM 2189 CG ARG A 318 23.632 48.262 11.957 1.00 16.53 ATOM 2190 CD ARG A 318 22.865 48.683 10.697 1.00 15.60 ATOM 2191 NE ARG A 318 23.731 49.237 9.655 1.00 13.88 ATOM 2192 CZ ARG A 318 24.404 50.379 9.759 1.00 13.49 ATOM 2193 NH1 ARG A 318 24.316 51.104 10.862 1.00 12.45 ATOM 2194 NH2 ARG A 318 25.178 50.792 8.762 1.00 11.39 ATOM 2195 C ARG A 318 24.647 45.790 13.781 1.00 17.91 ATOM 2196 O ARG A 318 24.223 46.179 14.874 1.00 17.43 ATOM 2197 N GLU A 319 24.438 44.562 13.326 1.00 17.86

ATOM 2198 CA GLU A 319 23.659 43.589 14.072 1.00 17.86 ATOM 2199 CB GLU A 319 23.380 42.377 13.176 1.00 20.79 ATOM 2200 CG GLU A 319 22.533 41.286 13.802 1.00 27.72 ATOM 2201 CD GLU A 319 21.855 40.408 12.757 1.00 32.40 ATOM 2202 OE1 GLU A 319 22.456 40.189 11.684 1.00 34.24 ATOM 2203 OE2 GLU A 319 20.725 39.929 13.009 1.00 36.06 ATOM 2204 C GLU A 319 24.317 43.156 15.388 1.00 17.83 ATOM 2205 O GLU A 319 23.662 43.149 16.431 1.00 16.48 ATOM 2206 N MET A 320 25.603 42.806 15.359 1.00 17.34 ATOM 2207 CA MET A 320 26.273 42.379 16.590 1.00 16.86 ATOM 2208 CB MET A 320 27.683 41.857 16.291 1.00 16.42 ATOM 2209 CG MET A 320 27.732 40.636 15.371 1.00 13.96 ATOM 2210 SD MET A 320 26.645 39.265 15.876 1.00 18. 68 ATOM 2211 CE MET A 320 27.333 38.814 17.496 1.00 14.45 ATOM 2212 C MET A 320 26.340 43.509 17.627 1.00 17.09 ATOM 2213 O MET A 320 26.256 43.267 18.833 1.00 16.35 ATOM 2214 N TYR A 321 26.480 44.741 17.151 1.00 17.09 ATOM 2215 CA TYR A 321 26.542 45.901 18.036 1.00 17.65 ATOM 2216 CB TYR A 321 26.738 47.172 17.211 1.00 17.64 ATOM 2217 CG TYR A 321 26.925 48.429 18.032 1.00 18.64 ATOM 2218 CD1 TYR A 321 28.145 48.716 18.637 1.00 17.99 ATOM 2219 CE1 TYR A 321 28.323 49.875 19.369 1.00 17.38 ATOM 2220 CD2 TYR A 321 25.886 49.339 18.187 1.00 16.94 ATOM 2221 CE2 TYR A 321 26.052 50.497 18.916 1.00 15.57 ATOM 2222 CZ TYR A 321 27.272 50.761 19.504 1.00 17.79 ATOM 2223 OH TYR A 321 27.439 51.917 20.228 1.00 18.99 ATOM 2224 C TYR A 321 25.245 46.012 18.844 1.00 18.22 ATOM 2225 0 TYR A 321 25.272 46.221 20.058 1.00 16.92 ATOM 2226 N ALA A 322 24.115 45.871 18.154 1.00 18.07 ATOM 2227 CA ALA A 322 22.798 45.951 18.779 1.00 18.52 ATOM 2228 CB ALA A 322 21.708 46.022 17.698 1.00 15.28 ATOM 2229 C ALA A 322 22.539 44.764 19.714 1.00 18.01 ATOM 2230 0 ALA A 322 21.979 44.929 20.793 1.00 19.87 ATOM 2231 N LEU A 323 22.945 43.570 19.301 1.00 17.20 ATOM 2232 CA LEU A 323 22.752 42.382 20.128 1.00 18.74 ATOM 2233 CB LEU A 323 23.129 41.124 19.343 1.00 17.37 ATOM 2234 CG LEU A 323 22.147 40.738 18.232 1.00 18.08

ATOM 2235 CD1 LEU A 323 22.713 39.592 17.407 1.00 15.53 ATOM 2236 CD2 LEU A 323 20.807 40.352 18.854 1.00 16.70 ATOM 2237 C LEU A 323 23.565 42.446 21.422 1.00 19. 90 ATOM 2238 0 LEU A 323 23.201 41.822 22.419 1.00 21.10 ATOM 2239 N THR A 324 24.664 43.199 21.404 1.00 19.51 ATOM 2240 CA THR A 324 25.509 43.334 22.585 1.00 19.82 ATOM 2241 CB THR A 324 27.016 43.159 22.226 1.00 19.33 ATOM 2242 OG1 THR A 324 27.408 44.134 21.250 1.00 17.08 ATOM 2243 CG2 THR A 324 27.269 41.768 21.662 1.00 18.20 ATOM 2244 C THR A 324 25.304 44.679 23.291 1.00 21.29 ATOM 2245 0 THR A 324 26.094 45.066 24.151 1.00 21.80 ATOM 2246 N GLN A 325 24.242 45.388 22.920 1.00 22.83 ATOM 2247 CA GLN A 325 23.925 46.679 23.525 1.00 24.26 ATOM 2248 CB GLN A 325 23.529 46.502 24.995 1.00 27.36 ATOM 2249 CG GLN A 325 22.185 45. 830 25.223 1.00 30.52 ATOM 2250 CD GLN A 325 22.121 44.440 24.633 1.00 35.25 ATOM 2251 OE1 GLN A 325 22.909 43.563 24.991 1.00 38.03 ATOM 2252 NE2 GLN A 325 21.178 44.227 23.721 1.00 37.42 ATOM 2253 C GLN A 325 25.073 47.671 23.446 1.00 23.75 ATOM 2254 0 GLN A 325 25.188 48.557 24.293 1.00 23.87 ATOM 2255 N GLY A 326 25.916 47.526 22.430 1.00 23.08 ATOM 2256 CA GLY A 326 27.043 48.428 22.275 1.00 23.27 ATOM 2257 C GLY A 326 28.025 48.394 23.435 1.00 22.83 ATOM 2258 0 GLY A 326 28.797 49.327 23.621 1.00 21.36 ATOM 2259 N ARG A 327 28.006 47.317 24.213 1.00 24.94 ATOM 2260 CA ARG A 327 28.900 47.192 25.361 1.00 27.26 ATOM 2261 CB ARG A 327 28.134 46.627 26.559 1.00 29.79 ATOM 2262 CG ARG A 327 27.058 47.569 27.075 1.00 36.59 ATOM 2263 CD ARG A 327 26.163 46.918 28.119 1.00 41.47 ATOM 2264 NE ARG A 327 25.082 47.821 28.508 1.00 48.27 ATOM 2265 CZ ARG A 327 24.011 47.459 29.208 1.00 50.35 ATOM 2266 NH1 ARG A 327 23.869 46.201 29.606 1.00 52.09 ATOM 2267 NH2 ARG A 327 23.076 48.354 29.499 1.00 50.26 ATOM 2268 C ARG A 327 30.115 46.320 25.068 1.00 26.50 ATOM 2269 0 ARG A 327 31.016 46.196 25.897 1.00 27.91 ATOM 2270 N VAL A 328 30.137 45.716 23.887 1.00 24.28 ATOM 2271 CA VAL A 328 31.244 44.860 23.497 1.00 21.47

ATOM 2272 CB VAL A 328 30.749 43.465 23.088 1.00 20.24 ATOM 2273 CG1 VAL A 328 31.923 42.598 22.686 1.00 18.37 ATOM 2274 CG2 VAL A 328 29.973 42.833 24.236 1.00 18.95 ATOM 2275 C VAL A 328 31.992 45.476 22.325 1.00 20.97 ATOM 2276 0 VAL A 328 31.440 45.624 21.237 1.00 21.49 ATOM 2277 N PRO A 329 33.260 45.854 22.543 1.00 18.84 ATOM 2278 CD PRO A 329 33.969 45.768 23.831 1.00 19.11 ATOM 2279 CA PRO A 329 34.113 46.461 21.518 1.00 18.46 ATOM 2280 CB PRO A 329 35.471 46.552 22.211 1.00 17.66 ATOM 2281 CG PRO A 329 35.095 46.754 23.641 1.00 18.87 ATOM 2282 C PRO A 329 34.168 45.612 20.246 1.00 18. 00 ATOM 2283 O PRO A 329 34.356 44.390 20.296 1.00 15.48 ATOM 2284 N ILE A 330 34.001 46.268 19.107 1.00 15.14 ATOM 2285 CA ILE A 330 34.038 45.571 17.835 1.00 15.79 ATOM 2286 CB ILE A 330 32.662 45.635 17.129 1.00 15.18 ATOM 2287 CG2 ILE A 330 32.770 45.067 15.733 1.00 13.79 ATOM 2288 CG1 ILE A 330 31.614 44.869 17.941 1.00 15.97 ATOM 2289 CD1 ILE A 330 30.211 44.945 17.348 1.00 16.11 ATOM 2290 C ILE A 330 35.086 46.148 16.888 1.00 14.82 ATOM 2291 O ILE A 330 35.266 47.369 16.796 1.00 13.07 ATOM 2292 N ILE A 331 35.789 45.257 16.200 1.00 13.52 ATOM 2293 CA ILE A 331 36.780 45.662 15.209 1.00 13.29 ATOM 2294 CB ILE A 331 38.114 44.896 15.371 1.00 12.04 ATOM 2295 CG2 ILE A 331 39.082 45.301 14.267 1.00 9.01 ATOM 2296 CG1 ILE A 331 38.722 45. 191. 16.748 1.00 12.74 ATOM 2297 CD1 ILE A 331 40.103 44.564 16.970 1.00 9.69 ATOM 2298 C ILE A 331 36.154 45.300 13.863 1.00 13.53 ATOM 2299 0 ILE A 331 35.952 44.120 13.568 1.00 14.03 ATOM 2300 N GLY A 332 35.825 46.317 13.069 1.00 12.79 ATOM 2301 CA GLY A 332 35.209 46.097 11.770 1.00 11.23 ATOM 2302 C GLY A 332 36.199 45.784 10.670 1.00 12.17 ATOM 2303 O GLY A 332 37.187 46.495 10.498 1.00 15.29 ATOM 2304 N VAL A 333 35.920 44.726 9.912 1.00 14.17 ATOM 2305 CA VAL A 333 36.789 44.275 8.825 1.00 13.37 ATOM 2306 CB VAL A 333 37.667 43.082 9.268 1.00 14.07 ATOM 2307 CG1 VAL A 333 38.941 43.040 8.443 1.00 12.39 ATOM 2308 CG2 VAL A 333 37. 936 43.148 10.749 1.00 16.53

ATOM 2309 C VAL A 333 35.962 43.767 7.646 1.00 12.46 ATOM 2310 O VAL A 333 34. 982 43.053 7.836 1. 00 11.94 ATOM 2311 N GLY A 334 36.376 44.104 6.431 1.00 12.77 ATOM 2312 CA GLY A 334 35.651 43.639 5.264 1.00 13.14 ATOM 2313 C GLY A 334 35.402 44.690 4.197 1.00 15.69 ATOM 2314 O GLY A 334 34.449 45.473 4.287 1.00 14.19 ATOM 2315 N GLY A 335 36.265 44.708 3.184 1.00 14.95 ATOM 2316 CA GLY A 335 36.111 45.651 2.093 1.00 15.32 ATOM 2317 C GLY A 335 36.332 47.119 2.412 1.00 16.47 ATOM 2318 0 GLY A 335 35.742 47.983 1.766 1.00 18.02 ATOM 2319 N VAL A 336 37.162 47.422 3.403 1.00 16.45 ATOM 2320 CA VAL A 336 37.434 48.817 3.721 1.00 15.37 ATOM 2321 CB VAL A 336 37.868 48.994 5.185 1.00 16.95 ATOM 2322 CG1 VAL A 336 38.430 50.402 5.396 1.00 17.10 ATOM 2323 CG2 VAL A 336 36.681 48.757 6.104 1.00 15.58 ATOM 2324 C VAL A 336 38.547 49.313 2.798 1.00 15.63 ATOM 2325 0 VAL A 336 39.664 48.788 2.808 1.00 12.87 ATOM 2326 N SER A 337 38.235 50.323 1.994 1.00 15.71 ATOM 2327 CA SER A 337 39.210 50.861 1.054 1.00 17.36 ATOM 2328 CB SER A 337 38.909 50.320-0. 348 1.00 19.55 ATOM 2329 OG SER A 337 39.881 50.746-1. 281 1.00 26.27 ATOM 2330 C SER A 337 39.225 52.391 1.026 1.00 16.87 ATOM 2331 O SER A 337 39. 985 52.995 0.270 1.00 16.56 ATOM 2332 N SER A 338 38.392 53.013 1.856 1.00 15.02 ATOM 2333 CA SER A 338 38.311 54.466 1.895 1.00 14.94 ATOM 2334 CB SER A 338 37.337 54.958 0.816 1.00 15.62 ATOM 2335 OG SER A 338 35.993 54.649 1.163 1.00 12.43 ATOM 2336 C SER A 338 37.836 54.972 3.257 1.00 14.83 ATOM 2337 0 SER A 338 37.402 54.193 4.108 1.00 15.32 ATOM 2338 N GLY A 339 37.913 56.283 3.451 1.00 13.85 ATOM 2339 CA GLY A 339 37.466 56.867 4.700 1.00 13.96 ATOM 2340 C GLY A 339 35.992 56.577 4.911 1.00 14.77 ATOM 2341 0 GLY A 339 35.568 56.266 6.024 1.00 15.11 ATOM 2342 N GLN A 340 35.205 56.675 3.840 1.00 13.56 ATOM 2343 CA GLN A 340 33.775 56.410 3.929 1.00 14.73 ATOM 2344 CB GLN A 340 33.075 56.650 2.583 1.00 14.84 ATOM 2345 CG GLN A 340 31.606 56.231 2.606 1.00 16.68

ATOM 2346 CD GLN A 340 30.869 56. 527 1.309 1.00 17.07 ATOM 2347 OE1 GLN A 340 30.787 57.678 0.873 1.00 17.10 ATOM 2348 NE2 GLN A 340 30.322 55.487 0.691 1.00 15.72 ATOM 2349 C GLN A 340 33.521 54.976 4.376 1.00 14.91 ATOM 2350 0 GLN A 340 32.690 54.736 5.258 1.00 15.89 ATOM 2351 N ASP A 341 34.231 54.027 3.766 1.00 11.85 ATOM 2352 CA ASP A 341 34.072 52.622 4.129 1.00 12.88 ATOM 2353 CB ASP A 341 35.014 51.723 3.311 1.00 12.35 ATOM 2354 CG ASP A 341 34.759 51.806 1.813 1.00 14.51 ATOM 2355 OD1 ASP A 341 33.624 52.149 1.416 1.00 15.79 ATOM 2356 OD2 ASP A 341 35.690 51.512 1.031 1.00 13.03 ATOM 2357 C ASP A 341 34.385 52.458 5.613 1.00 11.93 ATOM 2358 0 ASP A 341 33.689 51.748 6.336 1.00 11.87 ATOM 2359 N ALA A 342 35.441 53.124 6.064 1.00 11.66 ATOM 2360 CA ALA A 342 35.843 53.046 7.460 1.00 11.86 ATOM 2361 CB ALA A 342 37.183 53.751 7.657 1.00 11.31 ATOM 2362 C ALA A 342 34.788 53.652 8.381 1.00 12.51 ATOM 2363 O ALA A 342 34.421 53.052 9.390 1.00 13.16 ATOM 2364 N LEU A 343 34.295 54.835 8.026 1.00 11.81 ATOM 2365 CA LEU A 343 33.296 55.518 8.841 1.00 12.88 ATOM 2366 CB LEU A 343 33.117 56.960 8.355 1.00 12.38 ATOM 2367 CG LEU A 343 32.210 57.840 9.220 1.00 12.11 ATOM 2368 CD1 LEU A 343 32.755 57.858 10.646 1.00 12.07 ATOM 2369 CD2 LEU A 343 32.137 59.262 8.644 1.00 9.24 ATOM 2370 C LEU A 343 31.935 54.816 8.893 1.00 13.84 ATOM 2371 0 LEU A 343 31.257 54.864 9.916 1.00 16.26 ATOM 2372 N GLU A 344 31.517 54.178 7.802 1.00 14.81 ATOM 2373 CA GLU A 344 30.234 53.483 7.821 1.00 14.29 ATOM 2374 CB GLU A 344 29.892 52.902 6.447 1.00 15.56 ATOM 2375 CG GLU A 344 29.631 53.943 5.363 1.00 16.52 ATOM 2376 CD GLU A 344 29.003 53.345 4.105 1.00 17.36 ATOM 2377 OE1 GLU A 344 29.284 52.169 3.793 1.00 17.77 ATOM 2378 OE2 GLU A 344 28.240 54.056 3.417 1.00 15.41 ATOM 2379 C GLU A 344 30.291 52.366 8.862 1.00 14.33 ATOM 2380 O GLU A 344 29.335 52.147 9.608 1.00 14.20 ATOM 2381 N LYS A 345 31.423 51.669 8.921 1.00 14.34 ATOM 2382 CA LYS A 345 31.599 50.591 9.888 1.00 15.17

ATOM 2383 CB LYS A 345 32.865 49.790 9.576 1.00 13.40 ATOM 2384 CG LYS A 345 32.673 48.774 8.460 1.00 13.33 ATOM 2385 CD LYS A 345 33.934 47.958 8.217 1.00 10.82 ATOM 2386 CE LYS A 345 33.622 46.670 7.470 1.00 11.36 ATOM 2387 NZ LYS A 345 32.935 46.896 6.170 1.00 11.03 ATOM 2388 C LYS A 345 31.658 51.143 11.308 1.00 15.43 ATOM 2389 0 LYS A 345 31.113 50.547 12.237 1.00 15.78 ATOM 2390 N ILE A 346 32.312 52.286 11.478 1.00 15.51 ATOM 2391 CA ILE A 346 32.396 52.903 12.796 1.00 16.19 ATOM 2392 CB ILE A 346 33.364 54.115 12.787 1.00 16.23 ATOM 2393 CG2 ILE A 346 33.293 54.866 14.117 1.00 14.17 ATOM 2394 CG1 ILE A 346 34.791 53.618 12.528 1.00 15.33 ATOM 2395 CD1 ILE A 346 35.816 54.718 12.423 1.00 16. 06 ATOM 2396 C ILE A 346 30.995 53.344 13.234 1.00 16.44 ATOM 2397 0 ILE A 346 30.582 53.075 14.362 1.00 16.11 ATOM 2398 N ARG A 347 30.256 54.002 12.343 1.00 15.77 ATOM 2399 CA ARG A 347 28.899 54.435 12.679 1.00 16.90 ATOM 2400 CB ARG A 347 28.298 55.277 11.548 1.00 17.76 ATOM 2401 CG ARG A 347 28.955 56.649 11.348 1.00 18.67 ATOM 2402 CD ARG A 347 28.227 57.437 10.259 1.00 19.78 ATOM 2403 NE ARG A 347 26.818 57.633 10.594 1.00 22.78 ATOM 2404 CZ ARG A 347 26.283 58.796 10.962 1.00 26.59 ATOM 2405 NH1 ARG A 347 27.037 59.889 11.038 1.00 26.85 ATOM 2406 NH2 ARG A 347 24.994 58.864 11.273 1.00 24.22 ATOM 2407 C ARG A 347 28.007 53.220 12.948 1.00 15.86 ATOM 2408 0 ARG A 347 27.079 53.283 13.748 1.00 15.48 ATOM 2409 N ALA A 348 28.296 52.109 12.278 1.00 15.92 ATOM 2410 CA ALA A 348 27.521 50.892 12.471 1.00 15.49 ATOM 2411 CB ALA A 348 27.792 49.902 11.333 1.00 15.25 ATOM 2412 C ALA A 348 27.848 50.252 13.820 1.00 15.76 ATOM 2413 0 ALA A 348 27.095 49.401 14.301 1.00 16.58 ATOM 2414 N GLY A 349 28.966 50.653 14.431 1.00 13.86 ATOM 2415 CA GLY A 349 29.315 50.098 15.730 1.00 13.25 ATOM 2416 C GLY A 349 30.759 49.684 15.979 1.00 14.61 ATOM 2417 0 GLY A 349 31.097 49.268 17.088 1.00 15.21 ATOM 2418 N ALA A 350 31.617 49.797 14.972 1.00 14.16 ATOM 2419 CA ALA A 350 33.014 49.418 15.134 1.00 16.29

ATOM 2420 CB ALA A 350 33.637 49.115 13.774 1.00 16.52 ATOM 2421 C ALA A 350 33.836 50.485 15.843 1.00 17.09 ATOM 2422 0 ALA A 350 33.737 51.674 15.531 1.00 17.36 ATOM 2423 N SER A 351 34.646 50.051 16.805 1.00 17.54 ATOM 2424 CA SERA 351 35.515 50. 963 17.540 1.00 16.20 ATOM 2425 CB SERA 351 35.821 50.411 18.932 1.00 15.23 ATOM 2426 OG SERA 351 34.684 50.491 19.767 1.00 18.04 ATOM 2427 C SER A 351 36.812 51.112 16.754 1.00 16.11 ATOM 2428 0 SER A 351 37.503 52.131 16.851 1.00 15.72 ATOM 2429 N LEU A 352 37.127 50.078 15.977 1.00 14.13 ATOM 2430 CA LEU A 352 38.328 50.046 15.149 1.00 15.05 ATOM 2431 CB LEU A 352 39.457 49.286 15.859 1.00 13.12 ATOM 2432 CG LEU A 352 39.909 49.717 17.254 1.00 14.84 ATOM 2433 CD1 LEU A 352 40.771 48.610 17.869 1.00 11.84 ATOM 2434 CD2 LEU A 352 40.674 51.033 17.171 1.00 13.14 ATOM 2435 C LEU A 352 37.999 49.308 13.857 1.00 13.72 ATOM 2436 O LEU A 352 37.021 48.565 13.795 1.00 11.22 ATOM 2437 N VAL A 353 38.820 49.514 12.831 1.00 12.75 ATOM 2438 CA VAL A 353 38.626 48.828 11.564 1.00 13.86 ATOM 2439 CB VAL A 353 38.055 49.761 10.470 1.00 15.70 ATOM 2440 CG1 VAL A 353 36.770 50.417 10.960 1.00 14.25 ATOM 2441 CG2 VAL A 353 39.090 50.799 10.071 1.00 13.83 ATOM 2442 C VAL A 353 39.962 48.281 11.081 1.00 14.67 ATOM 2443 0 VAL A 353 41.024 48.711 11.536 1.00 12.91 ATOM 2444 N GLN A 354 39.897 47.316 10.172 1.00 14.28 ATOM 2445 CA GLN A 354 41.089 46.710 9.596 1.00 14.04 ATOM 2446 CB GLN A 354 41.347 45.307 10.175 1.00 14.77 ATOM 2447 CG GLN A 354 41.594 45.223 11.678 1.00 15.51 ATOM 2448 CD GLN A 354 41.763 43.774 12.147 1.00 18.24 ATOM 2449 OE1 GLN A 354 41.005 42.888 11.745 1.00 16.59 ATOM 2450 NE2 GLN A 354 42.756 43.534 13.000 1.00 16.98 ATOM 2451 C GLN A 354 40.852 46.574 8.100 1.00 14.33 ATOM 2452 O GLN A 354 39.715 46.634 7.626 1.00 13.37 ATOM 2453 N LEU A 355 41.931 46.394 7.354 1.00 14.18 ATOM 2454 CA LEU A 355 41.822 46.213 5.919 1.00 15.51 ATOM 2455 CB LEU A 355 41.899 47.561 5.188 1.00 13.52 ATOM 2456 CG LEU A 355 43.166 48.417 5.312 1.00 13.61

ATOM 2457 CD1 LEU A 355 44.262 47.879 4.399 1.00 13.33 ATOM 2458 CD2 LEU A 355 42.838 49.854 4.943 1.00 10.85 ATOM 2459 C LEU A 355 42.955 45.306 5.482 1.00 16.16 ATOM 2460 0 LEU A 355 43.963 45.176 6.179 1.00 15.14 ATOM 2461 N TYR A 356 42.775 44.657 4.340 1.00 17.37 ATOM 2462 CA TYR A 356 43.805 43.785 3.804 1.00 17.28 ATOM 2463 CB TYR A 356 43.639 42.352 4.333 1.00 16.02 ATOM 2464 CG TYR A 356 44.703 41.377 3.852 1.00 15.51 ATOM 2465 CD1 TYR A 356 44.774 40.087 4.363 1.00 16.04 ATOM 2466 CE1 TYR A 356 45.714 39.182 3.897 1.00 14.34 ATOM 2467 CD2 TYR A 356 45.611 41.735 2.862 1.00 16.62 ATOM 2468 CE2 TYR A 356 46.551 40.838 2.387 1.00 16.21 ATOM 2469 CZ TYR A 356 46.597 39.565 2.905 1.00 16.13 ATOM 2470 OH TYR A 356 47.518 38.669 2.414 1.00 17.60 ATOM 2471 C TYR A 356 43.739 43.803 2.287 1.00 17.12 ATOM 2472 O TYR A 356 44.671 44.261 1.629 1.00 18.15 ATOM 2473 N THR A 357 42.637 43.308 1.738 1.00 16.53 ATOM 2474 CA THR A 357 42.472 43.250 0.292 1.00 16.40 ATOM 2475 CB THR A 357 41.059 42. 753-0. 080 1.00 16.96 ATOM 2476 OG1 THR A 357 40.868 41.429 0.439 1.00 13.18 ATOM 2477 CG2 THR A 357 40.886 42.727-1. 589 1.00 16.23 ATOM 2478 C THR A 357 42.731 44.590-0. 401 1.00 15.65 ATOM 2479 O THR A 357 43.312 44.633-1. 484 1.00 15.49 ATOM 2480 N ALA A 358 42.307 45.683 0.223 1.00 15.19 ATOM 2481 CA ALA A 358 42.507 47.002-0. 367 1.00 15.24 ATOM 2482 CB ALA A 358 41.921 48.070 0.534 1.00 11.12 ATOM 2483 C ALA A 358 43.995 47.255-0. 584 1.00 16.21 ATOM 2484 0 ALA A 358 44.394 47.872-1. 572 1.00 15.43 ATOM 2485 N LEU A 359 44.810 46.770 0.348 1.00 16.24 ATOM 2486 CA LEU A 359 46.255 46.943 0.273 1.00 16.57 ATOM 2487 CB LEU A 359 46.916 46.409 1.548 1.00 17.72 ATOM 2488 CG LEU A 359 48.442 46.485 1.620 1.00 17.63 ATOM 2489 CD1 LEU A 359 48.894 47.933 1.559 1.00 17.25 ATOM 2490 CD2 LEU A 359 48.919 45.829 2.908 1.00 18.09 ATOM 2491 C LEU A 359 46.846 46.239-0. 942 1.00 15.68 ATOM 2492 0 LEU A 359 47.800 46.725-1. 541 1.00 14.17 ATOM 2493 N THR A 360 46.270 45.099-1. 309 1.00 15.77

ATOM 2494 CA THR A 360 46.762 44.336-2. 450 1.00 16.61 ATOM 2495 CB THR A 360 46.189 42.906-2. 454 1.00 16.18 ATOM 2496 OG1 THR A 360 44.804 42.943-2. 829 1.00 17.30 ATOM 2497 CG2 THR A 360 46.331 42.280-1. 068 1.00 10.83 ATOM 2498 C THR A 360 46.444 44.986-3. 795 1.00 18.77 ATOM 2499 O THR A 360 47.034 44.628-4. 813 1.00 21.01 ATOM 2500 N PHE A 361 45.516 45.937-3. 810 1.00 18.81 ATOM 2501 CA PHE A 361 45.165 46.606-5. 060 1.00 20.17 ATOM 2502 CB PHE A 361 43.644 46.760-5. 197 1.00 21.09 ATOM 2503 CG PHE A 361 42.922 45.482-5. 517 1.00 22.40 ATOM 2504 CD1 PHE A 361 42.189 44.821-4. 547 1.00 19.17 ATOM 2505 CD2 PHE A 361 42.988 44.935-6. 791 1.00 24.26 ATOM 2506 CE1 PHE A 361 41.537 43.641-4. 838 1.00 22.16 ATOM 2507 CE2 PHE A 361 42.335 43.748-7. 089 1.00 23.23 ATOM 2508 CZ PHE A 361 41.609 43.102-6. 109 1.00 22.64 ATOM 2509 C PHE A 361 45.796 47.988-5. 195 1.00 20.92 ATOM 2510 O PHE A 361 46.302 48.344-6. 255 1.00 22.01 ATOM 2511 N TRP A 362 45.769 48.761-4. 116 1.00 22.57 ATOM 2512 CA TRP A 362 46.286 50.122-4. 144 1.00 23.30 ATOM 2513 CB TRP A 362 45.259 51.043-3. 480 1.00 24.63 ATOM 2514 CG TRP A 362 43.846 50.707-3. 893 1.00 28.77 ATOM 2515 CD2 TRP A 362 43.360 50.512-5. 232 1.00 30.31 ATOM 2516 CE2 TRP A 362 42.000 50.158-5. 134 1.00 30.43 ATOM 2517 CE3 TRP A 362 43.945 50.600-6. 501 1.00 30.78 ATOM 2518 CD1 TRP A 362 42.785 50.474-3. 068 1.00 28.42 ATOM 2519 NE1 TRP A 362 41. 674 50.141-3. 804 1.00 28.43 ATOM 2520 CZ2 TRP A 362 41.213 49.890-6. 258 1.00 32.37 ATOM 2521 CZ3 TRP A 362 43.163 50.334-7. 616 1.00 31.79 ATOM 2522 CH2 TRP A 362 41.812 49.983-7. 487 1.00 32.17 ATOM 2523 C TRP A 362 47.667 50.312-3. 514 1.00 22. 63 ATOM 2524 O TRP A 362 48.320 51.334-3. 737 1.00 22.22 ATOM 2525 N GLY A 363 48.107 49.329-2. 736 1.00 21.03 ATOM 2526 CA GLY A 363 49.408 49.416-2. 098 1.00 19.14 ATOM 2527 C GLY A 363 49.417 50.228-0. 817 1.00 19.51 ATOM 2528 O GLY A 363 48.372 50.693-0. 359 1.00 20.28 ATOM 2529 N PRO A 364 50.601 50.418-0. 214 1.00 19.32 ATOM 2530 CD PRO A 364 51.869 49.874-0. 739 1.00 19.56

ATOM 2531 CA PRO A 364 50.831 51.169 1.026 1.00 19.42 ATOM 2532 CB PRO A 364 52.349 51.331 1.051 1.00 18.75 ATOM 2533 CG PRO A 364 52.816 50.041 0.441 1.00 18.97 ATOM 2534 C PRO A 364 50.110 52. 514 1.150 1.00 20.15 ATOM 2535 O PRO A 364 49.578 52.837 2.210 1.00 21.62 ATOM 2536 N PRO A 365 50.082 53.317 0.072 1.00 20.37 ATOM 2537 CD PRO A 365 50.657 53.076-1. 263 1.00 19.69 ATOM 2538 CA PRO A 365 49.415 54.624 0.118 1.00 19.12 ATOM 2539 CB PRO A 365 49.567 55.143-1. 311 1.00 19.93 ATOM 2540 CG PRO A 365 50.829 54.477-1. 787 1.00 20.52 ATOM 2541 C PRO A 365 47.950 54.588 0.551 1.00 18.92 ATOM 2542 0 PRO A 365 47.412 55.593 1. 011 1.00 19.97 ATOM 2543 N VAL A 366 47.302 53.437 0.411 1.00 18.53 ATOM 2544 CA VAL A 366 45.895 53.343 0.779 1.00 18.39 ATOM 2545 CB VAL A 366 45.306 51.950 0.449 1.00 18.99 ATOM 2546 CG1 VAL A 366 45.762 50.925 1.473 1.00 17.14 ATOM 2547 CG2 VAL A 366 43.793 52.032 0.403 1.00 18.85 ATOM 2548 C VAL A 366 45.680 53.635 2.257 1.00 18.00 ATOM 2549 O VAL A 366 44.627 54.130 2.653 1.00 19.45 ATOM 2550 N VAL A 367 46.689 53.341 3.069 1.00 17.67 ATOM 2551 CA VAL A 367 46.599 53.568 4.506 1.00 17.92 ATOM 2552 CB VAL A 367 47.845 53.038 5.224 1.00 17.49 ATOM 2553 CG1 VAL A 367 47.685 53.213 6.717 1.00 15.94 ATOM 2554 CG2 VAL A 367 48.069 51.566 4.858 1.00 18.38 ATOM 2555 C VAL A 367 46.429 55.050 4.844 1.00 18.04 ATOM 2556 0 VAL A 367 45.555 55.418 5.628 1.00 16.97 ATOM 2557 N GLY A 368 47.269 55.894 4.254 1.00 19.26 ATOM 2558 CA GLY A 368 47.179 57.320 4.507 1.00 19.38 ATOM 2559 C GLY A 368 45.899 57.881 3.924 1.00 21.58 ATOM 2560 0 GLY A 368 45.281 58.782 4.500 1.00 20.55 ATOM 2561 N LYS A 369 45.491 57.331 2.781 1.00 22.53 ATOM 2562 CA LYS A 369 44.271 57.773 2.110 1.00 22.83 ATOM 2563 CB LYS A 369 44.059 56.997 0.804 1.00 22.47 ATOM 2564 CG LYS A 369 43.053 57.659-0. 123 1.00 24.45 ATOM 2565 CD LYS A 369 42.550 56.727-1. 215 1.00 23.16 ATOM 2566 CE LYS A 369 41.613 55.684-0. 638 1.00 24.02 ATOM 2567 NZ LYS A 369 40.829 54.997-1. 695 1.00 24.58

ATOM 2568 C LYS A 369 43.062 57.564 3.016 1.00 21. 99 ATOM 2569 0 LYS A 369 42.264 58.481 3.231 1.00 22.20 ATOM 2570 N VAL A 370 42.933 56.354 3.549 1.00 19.95 ATOM 2571 CA VAL A 370 41.814 56.036 4.424 1.00 18.95 ATOM 2572 CB VAL A 370 41.853 54.559 4.876 1.00 16.89 ATOM 2573 CG1 VAL A 370 40.745 54.297 5.883 1.00 14.26 ATOM 2574 CG2 VAL A 370 41.692 53.643 3.668 1.00 15.62 ATOM 2575 C VAL A 370 41.795 56. 936 5.655 1.00 19.62 ATOM 2576 0 VAL A 370 40.743 57.447 6.041 1.00 18.54 ATOM 2577 N LYS A 371 42.957 57.134 6.268 1.00 19.57 ATOM 2578 CA LYS A 371 43.036 57.982 7.449 1.00 20.77 ATOM 2579 CB LYS A 371 44.437 57.906 8.068 1.00 20.80 ATOM 2580 CG LYS A 371 44.714 56.573 8.755 1.00 20.84 ATOM 2581 CD LYS A 371 46.007 56.598 9.547 1.00 20.94 ATOM 2582 CE LYS A 371 47.211 56.772 8.643 1.00 20.99 ATOM 2583 NZ LYS A 371 48.475 56.737 9.422 1.00 21.34 ATOM 2584 C LYS A 371 42.675 59.433 7.142 1.00 20.94 ATOM 2585 0 LYS A 371 41.944 60.067 7.901 1.00 20.23 ATOM 2586 N ARG A 372 43.181 59.954 6. 029 1.00 22.39 ATOM 2587 CA ARG A 372 42.899 61.332 5.635 1.00 24.04 ATOM 2588 CB ARG A 372 43.711 61.711 4.392 1.00 25.41 ATOM 2589 CG ARG A 372 43.497 63.151 3.942 1.00 30.23 ATOM 2590 CD ARG A 372 44.290 63.505 2.680 1.00 32.89 ATOM 2591 NE ARG A 372 43.774 62.832 1.487 1.00 37.10 ATOM 2592 CZ ARG A 372 44.382 61.822 0.871 1.00 36.84 ATOM 2593 NH1 ARG A 372 45.538 61.362 1.331 1.00 37.88 ATOM 2594 NH2 ARG A 372 43. 830 61.272-0. 204 1.00 35.98 ATOM 2595 C ARG A 372 41.410 61.554 5.351 1.00 23.65 ATOM 2596 O ARG A 372 40.832 62.551 5.785 1.00 23.32 ATOM 2597 N GLU A 373 40.793 60.626 4.624 1.00 22.04 ATOM 2598 CA GLU A 373 39.377 60.748 4.290 1.00 21.15 ATOM 2599 CB GLU A 373 38.990 59.724 3.214 1.00 21.21 ATOM 2600 CG GLU A 373 39.790 59.861 1.919 1.00 21.35 ATOM 2601 CD GLU A 373 39.474 58.770 0.908 1.00 24.25 ATOM 2602 OE1 GLU A 373 39.337 57.600 1.318 1.00 27.16 ATOM 2603 OE2 GLU A 373 39.376 59.074-0. 299 1.00 24.09 ATOM 2604 C GLU A 373 38. 517 60.559 5.530 1.00 20.97

ATOM 2605 O GLU A 373 37.475 61.196 5.675 1.00 23.42 ATOM 2606 N LEU A 374 38.954 59.684 6.428 1.00 19.50 ATOM 2607 CA LEU A 374 38.213 59.442 7.655 1.00 19.13 ATOM 2608 CB LEU A 374 38.885 58.340 8.479 1.00 16.43 ATOM 2609 CG LEU A 374 38.240 58.031 9.837 1.00 15.24 ATOM 2610 CD1 LEU A 374 36.785 57.640 9.636 1.00 12.59 ATOM 2611 CD2 LEU A 374 39.005 56.911 10.534 1.00 13.82 ATOM 2612 C LEU A 374 38.157 60.729 8.472 1.00 20.52 ATOM 2613 O LEU A 374 37.091 61.132 8.939 1.00 22.71 ATOM 2614 N GLU A 375 39.310 61.367 8.641 1.00 20.39 ATOM 2615 CA GLU A 375 39.403 62.609 9.399 1.00 23.59 ATOM 2616 CB GLU A 375 40.846 63.119 9.404 1.00 26.05 ATOM 2617 CG GLU A 375 41.083 64.272 10.360 1.00 33.07 ATOM 2618 CD GLU A 375 42. 508 64.792 10.310 1.00 37.24 ATOM 2619 OE1 GLU A 375 43.445 63.966 10.363 1.00 39.09 ATOM 2620 OE2 GLU A 375 42.689 66.027 10.229 1.00 41.20 ATOM 2621 C GLU A 375 38.485 63.679 8.815 1.00 22.79 ATOM 2622 O GLU A 375 37.710 64.302 9.537 1.00 22.67 ATOM 2623 N ALA A 376 38.571 63.881 7.503 1.00 22.58 ATOM 2624 CA ALA A 376 37.740 64.871 6.827 1.00 22.81 ATOM 2625 CB ALA A 376 38.087 64.926 5.330 1.00 20.94 ATOM 2626 C ALA A 376 36.260 64.557 7.010 1.00 23.09 ATOM 2627 0 ALA A 376 35.464 65.454 7.283 1.00 25.43 ATOM 2628 N LEU A 377 35.890 63.286 6.859 1.00 22.26 ATOM 2629 CA LEU A 377 34.495 62.881 7.016 1.00 21.07 ATOM 2630 CB LEU A 377 34.316 61.403 6.661 1.00 18.38 ATOM 2631 CG LEU A 377 34.395 61.099 5.166 1.00 19.86 ATOM 2632 CD1 LEU A 377 34.336 59.603 4.947 1.00 17.99 ATOM 2633 CD2 LEU A 377 33.257 61.809 4.438 1.00 15.21 ATOM 2634 C LEU A 377 33.982 63.126 8.427 1.00 21.76 ATOM 2635 0 LEU A 377 32.835 63.529 8.610 1.00 20.90 ATOM 2636 N LEU A 378 34.828 62.872 9.423 1.00 22.73 ATOM 2637 CA LEU A 378 34.442 63.086 10.814 1.00 23.95 ATOM 2638 CB LEU A 378 35.567 62.642 11.757 1.00 19.58 ATOM 2639 CG LEU A 378 35.806 61.133 11.865 1.00 18.89 ATOM 2640 CD1 LEU A 378 37.114 60.854 12.585 1.00 16.40 ATOM 2641 CD2 LEU A 378 34.638 60.484 12.594 1.00 16.69

ATOM 2642 C LEU A 378 34.114 64. 563 11.048 1.00 24.69 ATOM 2643 0 LEU A 378 33.081 64.888 11.633 1.00 24.07 ATOM 2644 N LYS A 379 34.994 65. 449 10.588 1.00 25.59 ATOM 2645 CA LYS A 379 34.783 66.885 10.747 1.00 29.22 ATOM 2646 CB LYS A 379 35.977 67.667 10.197 1.00 30.45 ATOM 2647 CG LYS A 379 37.288 67.406 10.926 1.00 34.68 ATOM 2648 CD LYS A 379 38.436 68.182 10.296 1.00 36.27 ATOM 2649 CE LYS A 379 39.747 67.898 11.010 1.00 40.47 ATOM 2650 NZ LYS A 379 40.904 68.609 10.389 1.00 42.09 ATOM 2651 C LYS A 379 33.528 67.294 9.993 1.00 30.46 ATOM 2652 0 LYS A 379 32.638 67.951 10.533 1.00 29.89 ATOM 2653 N GLU A 380 33.475 66.888 8.732 1.00 31.45 ATOM 2654 CA GLU A 380 32.358 67.186 7.853 1.00 33.02 ATOM 2655 CB GLU A 380 32.606 66.511 6.502 1.00 34.90 ATOM 2656 CG GLU A 380 31.467 66.591 5.519 1.00 41.07 ATOM 2657 CD GLU A 380 31.820 65.940 4.195 1.00 44.70 ATOM 2658 OE1 GLU A 380 30.909 65.725 3.367 1.00 47.15 ATOM 2659 OE2 GLU A 380 33.016 65.649 3.982 1.00 46.06 ATOM 2660 C GLU A 380 31.013 66.748 8.433 1.00 32.34 ATOM 2661 0 GLU A 380 29.979 67.353 8.144 1.00 31.13 ATOM 2662 N GLN A 381 31.023 65.708 9.260 1.00 31.07 ATOM 2663 CA GLN A 381 29.780 65.218 9.846 1.00 31.01 ATOM 2664 CB GLN A 381 29.695 63.693 9.688 1.00 30.16 ATOM 2665 CG GLN A 381 29.351 63.272 8.256 1.00 29.66 ATOM 2666 CD GLN A 381 29.445 61.774 8.025 1.00 30.22 ATOM 2667 OE1 GLN A 381 29.049 60.975 8.872 1.00 29.82 ATOM 2668 NE2 GLN A 381 29.953 61.388 6.858 1.00 30.17 ATOM 2669 C GLN A 381 29.546 65.632 11.301 1.00 30.95 ATOM 2670 0 GLN A 381 28.634 65.131 11.959 1.00 30.74 ATOM 2671 N GLY A 382 30.375 66. 546 11.796 1.00 30.35 ATOM 2672 CA GLY A 382 30.210 67.043 13.150 1.00 30.34 ATOM 2673 C GLY A 382 30.737 66.225 14.311 1.00 30.42 ATOM 2674 0 GLY A 382 30.443 66.539 15.463 1.00 30.46 ATOM 2675 N PHE A 383 31.507 65.181 14.037 1.00 29.60 ATOM 2676 CA PHE A 383 32.053 64.371 15.119 1.00 28.66 ATOM 2677 CB PHE A 383 32.309 62.941 14.644 1.00 26.51 ATOM 2678 CG PHE A 383 31. 065 62.205 14.243 1.00 24.25

ATOM 2679 CD1 PHE A 383 30.798 61.945 12.910 1.00 23.46 ATOM 2680 CD2 PHE A 383 30.163 61.774 15.200 1.00 21.40 ATOM 2681 CE1 PHE A 383 29.654 61.264 12.536 1.00 22.91 ATOM 2682 CE2 PHE A 383 29.021 61.096 14. 833 1. 00 22.41 ATOM 2683 CZ PHE A 383 28.765 60.839 13.498 1.00 22.25 ATOM 2684 C PHE A 383 33.352 64.975 15.641 1.00 29.41 ATOM 2685 0 PHE A 383 34.237 65.332 14.864 1.00 30.63 ATOM 2686 N GLY A 384 33.460 65.094 16.960 1.00 29.35 ATOM 2687 CA GLY A 384 34.666 65.646 17.548 1.00 29.12 ATOM 2688 C GLY A 384 35.834 64.700 17.353 1.00 29.26 ATOM 2689 0 GLY A 384 36.994 65.111 17.356 1.00 30.18 ATOM 2690 N GLY A 385 35.518 63.422 17.179 1.00 28.99 ATOM 2691 CA GLY A 385 36.546 62.419 16.978 1.00 27.13 ATOM 2692 C GLY A 385 35.935 61.062 16.695 1.00 26.35 ATOM 2693 0 GLY A 385 34.713 60.913 16.712 1.00 26.39 ATOM 2694 N VAL A 386 36.787 60.075 16.435 1.00 25.90 ATOM 2695 CA VAL A 386 36.348 58.715 16.145 1.00 23.97 ATOM 2696 CB VAL A 386 37.558 57.756 16.023 1. 00 24.97 ATOM 2697 CG1 VAL A 386 37.078 56.317 15.893 1.00 23.00 ATOM 2698 CG2 VAL A 386 38.414 58.143 14.826 1.00 24.99 ATOM 2699 C VAL A 386 35.431 58.187 17.241 1.00 24.14 ATOM 2700 O VAL A 386 34.377 57.614 16.961 1.00 23.65 ATOM 2701 N THR A 387 35.844 58.389 18.488 1.00 24.08 ATOM 2702 CA THR A 387 35.090 57.929 19.649 1.00 25.04 ATOM 2703 CB THR A 387 35.730 58.441 20.955 1.00 26.36 ATOM 2704 OG1 THR A 387 37.126 58.116 20.960 1.00 29.95 ATOM 2705 CG2 THR A 387 35.066 57.797 22.161 1.00 24.13 ATOM 2706 C THR A 387 33.634 58.377 19.624 1.00 24.22 ATOM 2707 0 THR A 387 32.746 57.651 20.062 1.00 24.33 ATOM 2708 N ASP A 388 33.400 59.577 19.106 1.00 24.01 ATOM 2709 CA ASP A 388 32.058 60.142 19.034 1.00 23.47 ATOM 2710 CB ASP A 388 32.150 61.642 18.747 1.00 27.09 ATOM 2711 CG ASP A 388 32.861 62.399 19.842 1.00 30.40 ATOM 2712 OD1 ASP A 388 33.719 63.251 19.515 1.00 33.28 ATOM 2713 OD2 ASP A 388 32.557 62.147 21. 028 1.00 32.49 ATOM 2714 C ASP A 388 31.195 59.487 17.965 1.00 21.54 ATOM 2715 0 ASP A 388 29. 975 59.459 18.079 1.00 20.53

ATOM 2716 N ALA A 389 31.835 58.969 16.924 1.00 21.30 ATOM 2717 CA ALA A 389 31.123 58.341 15.821 1.00 19.74 ATOM 2718 CB ALA A 389 31.935 58.498 14.536 1.00 20. 68 ATOM 2719 C ALA A 389 30.770 56.873 16.035 1.00 18.26 ATOM 2720 0 ALA A 389 29.862 56.356 15.386 1.00 19.21 ATOM 2721 N ILE A 390 31.485 56.196 16.930 1.00 17.78 ATOM 2722 CA ILE A 390 31.225 54.778 17. 193 1.00 15.62 ATOM 2723 CB ILE A 390 32.106 54.253 18.358 1.00 15.31 ATOM 2724 CG2 ILE A 390 31.813 52.784 18.613 1.00 12.29 ATOM 2725 CG1 ILE A 390 33.588 54.424 18.013 1.00 15.83 ATOM 2726 CD1 ILE A 390 34.527 54.138 19.169 1.00 14.86 ATOM 2727 C ILE A 390 29.754 54.510 17.529 1.00 15.04 ATOM 2728 0 ILE A 390 29.250 54.962 18.554 1.00 16. 25 ATOM 2729 N GLY A 391 29.071 53.782 16. 651 1.00 15.63 ATOM 2730 CA GLY A 391 27.671 53.453 16.872 1.00 15.37 ATOM 2731 C GLY A 391 26.652 54.560 16.631 1.00 15.79 ATOM 2732 O GLY A 391 25.466 54.374 16.893 1.00 15.96 ATOM 2733 N ALA A 392 27.097 55.699 16.114 1.00 16.55 ATOM 2734 CA ALA A 392 26.207 56.836 15.867 1.00 18.78 ATOM 2735 CB ALA A 392 26.968 57.944 15.133 1.00 16.54 ATOM 2736 C ALA A 392 24.918 56.504 15.112 1.00 19.86 ATOM 2737 O ALA A 392 23.880 57.119 15.361 1.00 19.15 ATOM 2738 N ASP A 393 24.972 55.543 14.191 1.00 20.27 ATOM 2739 CA ASP A 393 23.777 55.182 13.426 1.00 21.17 ATOM 2740 CB ASP A 393 24.092 54.124 12.360 1.00 21.34 ATOM 2741 CG ASP A 393 24.905 54.671 11.196 1.00 25.41 ATOM 2742 OD1 ASP A 393 24.915 55.904 10.981 1.00 24.65 ATOM 2743 OD2 ASP A 393 25.520 53.851 10.479 1.00 26.65 ATOM 2744 C ASP A 393 22.670 54.642 14.328 1.00 22.02 ATOM 2745 0 ASP A 393 21.487 54.823 14.046 1.00 22.08 ATOM 2746 N HIS A 394 23.062 53.976 15.410 1.00 22.05 ATOM 2747 CA HIS A 394 22.107 53.383 16.342 1.00 23.30 ATOM 2748 CB HIS A 394 22.818 52.342 17.212 1.00 18.42 ATOM 2749 CG HIS A 394 23.430 51.219 16.431 1.00 18.64 ATOM 2750 CD2 HIS A 394 24.557 51.165 15.680 1.00 15.81 ATOM 2751 ND1 HIS A 394 22.855 49.968 16.347 1.00 15.16 ATOM 2752 CE1 HIS A 394 23.600 49.193 15.580 1.00 15.16

ATOM 2753 NE2 HIS A 394 24.639 49.895 15.163 1.00 16.24 ATOM 2754 C HIS A 394 21.415 54.406 17.237 1.00 25.83 ATOM 2755 O HIS A 394 20.373 54.121 17.821 1.00 26.50 ATOM 2756 N ARG A 395 21.994 55.595 17.344 1.00 28.78 ATOM 2757 CA ARG A 395 21.428 56.635 18.188 1.00 33.50 ATOM 2758 CB ARG A 395 22.550 57.376 18.926 1.00 33.09 ATOM 2759 CG ARG A 395 23.384 56.469 19.829 1.00 34.73 ATOM 2760 CD ARG A 395 24.289 57.266 20.759 1.00 35.29 ATOM 2761 NE ARG A 395 25.446 57.851 20.083 1.00 36.20 ATOM 2762 CZ ARG A 395 26.557 57.184 19.781 1.00 36.50 ATOM 2763 NH1 ARG A 395 27.557 57.804 19.165 1.00 35.10 ATOM 2764 NH2 ARG A 395 26.674 55.900 20.100 1.00 35.17 ATOM 2765 C ARG A 395 20.568 57.623 17.408 1.00 37.62 ATOM 2766 0 ARG A 395 19.865 58.441 17.996 1.00 39.11 ATOM 2767 N ARG A 396 20.619 57.543 16.083 1.00 41.81 ATOM 2768 CA ARG A 396 19.828 58.434 15.245 1.00 45.90 ATOM 2769 CB ARG A 396 20.541 58.683 13.908 1.00 48.15 ATOM 2770 CG ARG A 396 20.571 57.500 12.955 1.00 50.79 ATOM 2771 CD ARG A 396 21.552 57.745 11.810 1.00 52.97 ATOM 2772 NE ARG A 396 21.368 59.062 11.207 1.00 54.80 ATOM 2773 CZ ARG A 396 20.262 59.449 10.582 1.00 56.47 ATOM 2774 NH1 ARG A 396 20.179 60.669 10.065 1.00 57.12 ATOM 2775 NH2 ARG A 396 19.240 58.614 10.466 1.00 57.75 ATOM 2776 C ARG A 396 18.439 57.842 15.007 1.00 47.29 ATOM 2777 O ARG A 396 17.445 58.588 15.139 1.00 47.81 ATOM 2778 OXT ARG A 396 18.361 56.637 14.688 1.00 49.38 TER 1 ARG A 396 END

Figure 3 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.011031 0.006369 0.000000 0.00000 SCALE2 0.000000 0.012738 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008125 0.00000 ATOM 2779 N1 FMN 398 41.768 36.138 8.642 1.00 13.07 ATOM 2780 C2 FMN 398 42.156 35.495 9.777 1.00 16.23 ATOM 2781 02 FMN 398 41.553 35.602 10.828 1.00 15.63 ATOM 2782 N3 FMN 398 43.332 34.661 9.720 1.00 15.17 ATOM 2783 C4 FMN 398 44.083 34.463 8.624 1.00 14.98 ATOM 2784 04 FMN 398 45.078 33.724 8.673 1.00 15.42 ATOM 2785 C4A FMN 398 43.663 35.157 7.395 1.00 13.75 ATOM 2786 N5 FMN 398 44.353 35.021 6.251 1.00 13.73 ATOM 2787 C5A FMN 398 43.937 35.699 5.122 1.00 11.46 ATOM 2788 C6 FMN 398 44.677 35.580 3.868 1.00 10.75 ATOM 2789 C7 FMN 398 44.299 36.258 2.716 1.00 11.50 ATOM 2790 C7M FMN 398 45.115 36.107 1.416 1.00 9.29 ATOM 2791 C8 FMN 398 43.129 37.121 2.736 1.00 11.87 ATOM 2792 C8M FMN 398 42.661 37.903 1.514 1.00 14.22 ATOM 2793 C9 FMN 398 42.407 37.240 3.918 1.00 11.46 ATOM 2794 C9A FMN 398 42.774 36.557 5.116 1.00 13.45 ATOM 2795 N10 FMN 398 42.055 36.664 6.366 1.00 13.69 ATOM 2796 C10 FMN 398 42.452 36.003 7.508 1.00 14.43 ATOM 2797 C1* FMN 398 40.854 37.510 6.446 1.00 12.50 ATOM 2798 C2* FMN 398 41.120 39.004 6.623 1.00 13.52 ATOM 2799 02* FMN 398 41.785 39.192 7.913 1.00 13.74 ATOM 2800 C3* FMN 398 39.791 39.809 6.666 1.00 12.06 ATOM 2801 03* FMN 398 38.934 39.288 7.740 1.00 12.59 ATOM 2802 C4* FMN 398 38.960 39.696 5.359 1.00 12.31 ATOM 2803 04* FMN 398 39.810 39.464 4.208 1.00 11.80 ATOM 2804 C5* FMN 398 38.118 40.946 5.100 1.00 10.70 ATOM 2805 05* FMN 398 38.915 42.126 4.951 1.00 14.11 ATOM 2806 P FMN 398 39.371 42.728 3.527 1.00 13.60 ATOM 2807 O1P FMN 398 40.438 41.814 2.959 1.00 14.55

ATOM 2808 02P FMN 398 39.878 44.114 3.849 1.00 12.57 ATOM 2809 03P FMN 398 38.126 42.785 2.627 1.00 14.12 ATOM 2810 N1 ORO 399 41.674 32.379 4.935 1.00 16.78 ATOM 2811 C2 ORO 399 40.657 33.292 5.240 1.00 16.40 ATOM 2812 02 ORO 399 40.049 33.934 4.386 1.00 20.50 ATOM 2813 N3 ORO 399 40.350 33.452 6.592 1.00 14.80 ATOM 2814 C4 ORO 399 40.960 32.786 7.660 1.00 15.08 ATOM 2815 04 ORO 399 40.634 32.987 8.809 1.00 14.56 ATOM 2816 C5 ORO 399 42.020 31.838 7.284 1.00 14.43 ATOM 2817 C6 ORO 399 42.319 31.684 5.976 1.00 16.70 ATOM 2818 C7 ORO 399 43.405 30.715 5.533 1.00 17.56 ATOM 2819 071 ORO 399 44.524 30.703 6.023 1.00 19.26 ATOM 2820 072 ORO 399 42.925 29.978 4.631 1.00 18.83 ATOM 2821 S S04 400 56.424 40.112 34.639 1.00 35.18 ATOM 2822 01 S04 400 56.120 41.429 35.225 1.00 35.51 ATOM 2823 02 S04 400 55.199 39.292 34.609 1.00 36.32 ATOM 2824 03 S04 400 56.937 40.294 33.270 1.00 36.60 ATOM 2825 04 S04 400 57.452 39.437 35.452 1.00 37.26 ATOM 2826 C ACT 401 24.652 49.256 4.973 1.00 33.65 ATOM 2827 0 ACT 401 23.471 49.645 4.685 1.00 32.94 ATOM 2828 OXT ACT 401 24.974 48.967 6.159 1.00 34.73 ATOM 2829 CH3 ACT 401 24.990 48.159 3.937 1.00 30.22 ATOM 2830 S S04 402 56.685 36.631 28.249 1.00 42.93 ATOM 2831 01 S04 402 55.412 37.351 28.128 1.00 51.57 ATOM 2832 02 S04 402 56.420 35.196 28.444 1.00 49.22 ATOM 2833 03 S04 402 57.455 36.828 27.009 1.00 51.20 ATOM 2834 04 S04 402 57.439 37.165 29.395 1.00 49.80 ATOM 2835 S S04 403 48.265 43.940 28.781 1.00 91.18 ATOM 2836 O1 S04 403 49.259 43.050 28.152 1.00 90.53 ATOM 2837 02 S04 403 47.958 43.450 30.139 1.00 90.33 ATOM 2838 03 S04 403 48.812 45.308 28.869 1.00 90.28 ATOM 2839 04 S04 403 47.033 43.952 27.967 1.00 90.50 ATOM 2840 S S04 404 32.854 23.140 6.523 1.00 78.69 ATOM 2841 O1 S04 404 32.858 24.227 7.521 1.00 79.26 ATOM 2842 02 S04 404 31.949 23.493 5.413 1.00 78.75 ATOM 2843 03 S04 404 34.218 22.943 6.001 1.00 78.59 ATOM 2844 04 S04 404 32.383 21.897 7.160 1.00 78.61

ATOM 2845 Cl INH 1 55.156 47.244 0.347 1.00 30.61 ATOM 2846 C2 INH 1 55.673 48.190-0. 610 1.00 30.81 ATOM 2847 C3 INH 1 55.194 48.186-2. 013 1.00 31.97 ATOM 2848 C4 INH 1 54.168 47.203-2. 451 1.00 30.44 ATOM 2849 C5 INH 1 53.641 46.233-1. 459 1.00 27.61 ATOM 2850 C6 INH 1 52.670 45.202-1. 696 1.00 26.48 ATOM 2851 C7 INH 1 54.170 46.288-0. 060 1.00 27.48 ATOM 2852 C8 INH 1 51.525 45.016-0. 763 1.00 23.90 ATOM 2853 C9 INH 1 50.573 43.949-0. 981 1.00 23.42 ATOM 2854 F10 INH 1 49.575 43.791-0. 145 1.00 23.87 ATOM 2855 Cll INH 1 50.717 43.023-2. 127 1.00 25.29 ATOM 2856 N12 INH 1 49.793 41.980-2. 283 1.00 23.77 ATOM 2857 C13 INH 1 51.835 43.209-3. 060 1.00 26.41 ATOM 2858 F14 INH 1 52.000 42.413-4. 092 1.00 28.14 ATOM 2859 C15 INH 1 52.801 44.276-2. 856 1.00 25.96 ATOM 2860 C16 INH 1 49.489 40.832-1. 506 1.00 28.49 ATOM 2861 C17 INH 1 48.466 39.833-1. 867 1.00 27.98 ATOM 2862 018 INH 1 50.135 40.651-0. 448 1.00 29.29 ATOM 2863 C19 INH 1 47.901 39.565-3. 090 1.00 29.14 ATOM 2864 C20 INH 1 46.915 38.457-2. 940 1.00 28.65 ATOM 2865 C21 INH 1 47.316 37.772-1. 629 1.00 30.35 ATOM 2866 C22 INH 1 47.906 38.930-0. 821 1.00 26.78 ATOM 2867 C23 INH 1 48.115 40.176-4. 438 1.00 31.81 ATOM 2868 024 INH 1 48.914 41.107-4. 671 1.00 35.53 ATOM 2869 025 INH 1 47.417 39.721-5. 498 1.00 35.32 ATOM 2870 026 INH 1 55.734 49.119-2. 892 1.00 38.75 ATOM 2871 C27 INH 1 57.015 48.727-3. 548 1.00 41.33 ATOM 2872 F28 INH 1 56.944 47.600-4. 240 1.00 44.03 ATOM 2873 F29 INH 1 57.367 49.716-4. 345 1.00 41.94 ATOM 2874 F30 INH 1 57.952 48.575-2. 624 1.00 42.63 ATOM 2875 OH2 INH 1 55.935 42.939-3. 322 1.00 73.19 ATOM 2876 OH2 TIP 2 35.544 55.453-5. 436 1.00 27.04 ATOM 2877 OH2 TIP 3 38.368 45.691 5.463 1.00 9.92 ATOM 2878 OH2 TIP 4 26.254 32.568-2. 682 1.00 18.84 ATOM 2879 OH2 TIP 5 32.726 49.693 5.055 1.00 4.99 ATOM 2880 OH2 TIP 6 40.177 36.456 0.169 1.00 8.72 ATOM 2881 OH2 TIP 7 28.792 46.338 21.197 1.00 9.84

ATOM 2882 OH2 TIP 8 50.114 40.162 27.019 1.00 11.00 ATOM 2883 OH2 TIP 9 52.707 35.109 39.872 1.00 13.09 ATOM 2884 OH2 TIP 10 32.631 48.935 19.270 1.00 8.68 ATOM 2885 OH2 TIP 11 31.665 31.398 6.495 1.00 16.03 ATOM 2886 OH2 TIP 12 54.419 36.452 7.881 1.00 14.67 ATOM 2887 OH2 TIP 13 48.765 30.201-4. 577 1.00 18.66 ATOM 2888 OH2 TIP 14 52.910 44.774 24.574 1.00 22.00 ATOM 2889 OH2 TIP 15 56.888 41.478 19.935 1.00 12.09 ATOM 2890 OH2 TIP 16 24.269 48.184 0.615 1.00 10.81 ATOM 2891 OH2 TIP 17 35.600 30.673-11. 563 1.00 18.80 ATOM 2892 OH2 TIP 19 27.032 52.989 8.555 1.00 13.56 ATOM 2893 OH2 TIP 20 33.133 44.845-12. 581 1.00 21.06 ATOM 2894 OH2 TIP 21 41.790 40.235 11.640 1. 00 9. 31 ATOM 2895 OH2 TIP 22 42.183 27.776 7.444 1.00 15.77 ATOM 2896 OH2 TIP 23 55.486 43.118 24.318 1.00 20.63 ATOM 2897 OH2 TIP 24 22.597 45.848 3.191 1.00 20.55 ATOM 2898 OH2 TIP 25 40.155 46.055 2.091 1.00 11.51 ATOM 2899 OH2 TIP 28 52.870 40.844 35.692 1.00 26.47 ATOM 2900 OH2 TIP 29 39.343 36.863-11. 603 1.00 15.79 ATOM 2901 OH2 TIP 30 29.725 63.303 4.807 1.00 30.86 ATOM 2902 OH2 TIP 31 31.090 52.803 1.908 1.00 16.92 ATOM 2903 OH2 TIP 33 48.470 40.672 9.314 1.00 16.35 ATOM 2904 OH2 TIP 34 48.163 60.787-5. 517 1.00 35.72 ATOM 2905 OH2 TIP 35 33.797 25.032-2. 216 1.00 28.04 ATOM 2906 OH2 TIP 36 27.528 36.090-15. 399 1.00 19.76 ATOM 2907 OH2 TIP 37 36.123 58.320 1.544 1.00 18.50 ATOM 2908 OH2 TIP 38 18.456 32.031 12.116 1.00 32.11 ATOM 2909 OH2 TIP 39 30.093 49.596 4.396 1.00 26.44 ATOM 2910 OH2 TIP 40 22.244 50.960 6.710 1.00 14.55 ATOM 2911 OH2 TIP 41 25.186 53.850 20.632 1.00 36.61 ATOM 2912 OH2 TIP 42 28.377 43.052 0.368 1.00 16.28 ATOM 2913 OH2 TIP 43 48.044 30.947 8.834 1.00 23.93 ATOM 2914 OH2 TIP 44 37.358 35.976 32.382 1.00 31.38 ATOM 2915 OH2 TIP 45 36.077 52.311-1. 386 1.00 20.23 ATOM 2916 OH2 TIP 46 48.137 51.093 24.342 1.00 27.05 ATOM 2917 OH2 TIP 47 31.755 42.556-7. 956 1.00 13.30 ATOM 2918 OH2 TIP 48 60.161 28.707 24.481 1.00 22.24

ATOM 2919 OH2 TIP 49 39.447 48.502-3. 656 1.00 28.66 ATOM 2920 OH2 TIP 50 48.327 58.128 0.959 1.00 30.23 ATOM 2921 OH2 TIP 51 55.679 32.342 25.492 1.00 27.36 ATOM 2922 OH2 TIP 52 64.173 35.374 20.180 1.00 20.52 ATOM 2923 OH2 TIP 53 58.849 49.917 15.132 1.00 26.47 ATOM 2924 OH2 TIP 54 51.767 31.449 11.360 1.00 14.19 ATOM 2925 OH2 TIP 55 39.550 45.797-2. 540 1.00 15.41 ATOM 2926. OH2 TIP 56 24.397 28.632 17.367 1.00 22.23 ATOM 2927 OH2 TIP 57 51.705 20.271 6.838 1.00 27.23 ATOM 2928 OH2 TIP 58 41.383 26.162-9. 699 1.00 21.02 ATOM 2929 OH2 TIP 59 25.050 40.672 6.953 1.00 20.47 ATOM 2930 OH2 TIP 60 23.999 41.157 9.453 1.00 26.17 ATOM 2931 OH2 TIP 61 37.989 29.525-11. 423 1.00 22.38 ATOM 2932 OH2 TIP 62 36.293 47.969-1. 074 1.00 31.20 ATOM 2933 OH2 TIP 63 38.463 26.067 1.663 1.00 29.91 ATOM 2934 OH2 TIP 64 53.273 23.516 20.214 1.00 39.87 ATOM 2935 OH2 TIP 65 59.232 43.479 12.582 1.00 16.61 ATOM 2936 OH2 TIP 66 19.667 42.932 12.630 1.00 37.55 ATOM 2937 OH2 TIP 67 34.515 51.648 22.411 1.00 33.64 ATOM 2938 OH2 TIP 68 47.217 63.075 3.678 1.00 40.93 ATOM 2939 OH2 TIP 69 44.997 42.094-5. 482 1.00 31.45 ATOM 2940 OH2 TIP 70 61.350 39.669 15.129 1.00 33.76 ATOM 2941 OH2 TIP 71 63.503 33.512 24.526 1.00 30.64 ATOM 2942 OH2 TIP 72 56.502 35.138 4.193 1.00 40.13 ATOM 2943 OH2 TIP 73 38.388 59.732 19.181 1.00 28.57 ATOM 2944 OH2 TIP 74 44.184 24.050 9.776 1.00 20.28 ATOM 2945 OH2 TIP 75 59.066 44.574 9.932 1.00 18.52 ATOM 2946 OH2 TIP 76 57.161 34.373 26.054 1.00 15.82 ATOM 2947 OH2 TIP 77 39.582 50.272 27.336 1.00 30.32 ATOM 2948 OH2 TIP 78 18.410 33.056 20.307 1.00 38.31 ATOM 2949 OH2 TIP 80 46.234 28.316 18.714 1.00 22.78 ATOM 2950 OH2 TIP 81 21.447 37.332 21.766 1.00 21.05 ATOM 2951 OH2 TIP 82 20.551 32.666 22.014 1.00 27.65 ATOM 2952 OH2 TIP 83 24.658 41.207-5. 227 1.00 22.79 ATOM 2953 OH2 TIP 84 55.011 41.531 26.497 1.00 25.92 ATOM 2954 OH2 TIP 85 38.296 32.264 33.902 1.00 23.13 ATOM 2955 OH2 TIP 86 44.369 24.267-3. 546 1.00 35.96

ATOM 2956 OH2 TIP 87 27.475 36.860 9.747 1.00 32.20 ATOM 2957 OH2 TIP 88 31.150 49.186 21.566 1.00 26.94 ATOM 2958 OH2 TIP 89 47.779 20.892 17.543 1.00 25.36 ATOM 2959 OH2 TIP 91 38.494 53.244-2. 751 1.00 35.05 ATOM 2960 OH2 TIP 92 46.323 60.192 17.190 1.00 27.65 ATOM 2961 OH2 TIP 93 28.667 66.884 4.567 1.00 40.54 ATOM 2962 OH2 TIP 94 60.846 30.830 9.609 1.00 32.28 ATOM 2963 OH2 TIP 96 19.909 46.368 21.678 1.00 28.96 ATOM 2964 OH2 TIP 97 45.477 23.130 6.094 1.00 27.25 ATOM 2965 OH2 TIP 98 55.212 41.460 21.964 1.00 16.08 ATOM 2966 OH2 TIP 99 47.327 53.836-3. 806 1.00 22.48 ATOM 2967 OH2 TIP 100 39.042 57.052-2. 132 1.00 23.68 ATOM 2968 OH2 TIP 101 42.080 65.105 6.196 1.00 23.98 ATOM 2969 OH2 TIP 102 50.195 38.982 37.861 1.00 33.16 ATOM 2970 OH2 TIP 103 24.816 38.106 6.274 1.00 46.68 ATOM 2971 OH2 TIP 104 37.606 19.200 18.942 1.00 40.91 ATOM 2972 OH2 TIP 105 34.078 23.126 21.682 1.00 37.32 ATOM 2973 OH2 TIP 106 50.938 24.646 25.853 1.00 23.41 ATOM 2974 OH2 TIP 108 43.762 44.620 28.111 1.00 46.21 ATOM 2975 OH2 TIP 109 31.113 28.188 31.316 1.00 32.77 ATOM 2976 OH2 TIP 110 20.949 49.041 19.756 1.00 45.06 ATOM 2977 OH2 TIP 111 52.664 36.212 5.983 1.00 26.36 ATOM 2978 OH2 TIP 112 58.238 26.573 11.032 1.00 36.46 ATOM 2979 OH2 TIP 113 43.014 36.746 36.299 1.00 43.53 ATOM 2980 OH2 TIP 114 24.151 50.266 27. 793 1.00 47.09 ATOM 2981 OH2 TIP 115 30.305 30.980-7. 851 1.00 30.68 ATOM 2982 OH2 TIP 116 48.285 22.108 6.645 1.00 25.39 ATOM 2983 OH2 TIP 117 39.224 37.972-14. 257 1.00 30.69 ATOM 2984 OH2 TIP 119 46.568 32.155-8. 891 1.00 39.93 ATOM 2985 OH2 TIP 121 20.118 49.260 17.291 1.00 30.89 ATOM 2986 OH2 TIP 122 35.058 44.421 26.773 1.00 41.84 ATOM 2987 OH2 TIP 124 49.192 64.702 8.137 1.00 52.76 ATOM 2988 OH2 TIP 125 37.968 56.298 22.605 1.00 44.63 ATOM 2989 OH2 TIP 126 35.175 25.867 8.190 1.00 40.87 ATOM 2990 OH2 TIP 128 53.373 48.412 27.185 1.00 34.68 ATOM 2991 OH2 TIP 130 31.753 41.370 27.331 1.00 50.15 ATOM 2992 OH2 TIP 133 45.057 19.603 20.174 1.00 49.23

ATOM 2993 OH2 TIP 135 62.120 49.293 13.816 1.00 51.24 ATOM 2994 OH2 TIP 136 36.392 24.415 5.232 1.00 36.40 ATOM 2995 OH2 TIP 137 37.190 47.914 25.973 1.00 42.47 ATOM 2996 OH2 TIP 139 33.803 32.622 6.980 1.00 20.75 ATOM 2997 OH2 TIP 140 37.790 20.683 21.494 1.00 33.84 ATOM 2998 OH2 TIP 141 27.946 24.070 16.098 1.00 35.29 ATOM 2999 OH2 TIP 142 28.752 24.561 25.979 1.00 42.61 ATOM 3000 OH2 TIP 143 29.987 30.644 9.290 1.00 24.83 ATOM 3001 OH2 TIP 145 32.739 65.991 1.259 1.00 38.09 ATOM 3002 OH2 TIP 146 43.015 23.319 7.628 1.00 40.80 ATOM 3003 OH2 TIP 149 45.126 45.040 12.866 1.00 30.92 ATOM 3004 OH2 TIP 150 56.775 54.277 24.966 1.00 36.42 ATOM 3005 OH2 TIP 154 28.318 35.749-8. 783 1.00 35.84 ATOM 3006 OH2 TIP 157 49.259 20.639 1.116 1.00 39.43 ATOM 3007 OH2 TIP 161 35.449 24.493 28.851 1.00 31.87 ATOM 3008 OH2 TIP 162 48.248 19.447 10.858 1.00 50.81 ATOM 3009 OH2 TIP 170 52.224 41.827 26.920 1.00 30.09 ATOM 3010 OH2 TIP 171 43.427 68.248 20.208 1.00 50.00 ATOM 3011 OH2 TIP 173 30.664 59.693 2.724 1.00 43.97 ATOM 3012 OH2 TIP 177 49.139 23.639 29.923 1.00 44.34 ATOM 3013 OH2 TIP 179 34.884 68.231 14.420 1.00 40.57 ATOM 3014 OH2 TIP 180 34.202 33.407 32.184 1.00 40.76 ATOM 3015 OH2 TIP 183 23.453 59.860 15.855 1.00 39.15 ATOM 3016 OH2 TIP 184 37.128 22.982-4. 060 1.00 31.12 ATOM 3017 OH2 TIP 186 59.884 32.942 5.715 1.00 48.15 ATOM 3018 OH2 TIP 187 38.634 46.165-0. 230 1.00 13.80 ATOM 3019 OH2 TIP 188 52.932 26.954 2.812 1.00 21.19 ATOM 3020 OH2 TIP 189 56.883 26.650 15.220 1.00 17.90 ATOM 3021 OH2 TIP 190 55.314 25.380 16.994 1.00 13.14 ATOM 3022 OH2 TIP 191 51.598 53.602 12.473 1.00 17.75 ATOM 3023 OH2 TIP 192 27.662 23.982 18.954 1.00 34.96 ATOM 3024 OH2 TIP 193 28.692 32.840-8. 937 1.00 31.39 ATOM 3025 OH2 TIP 194 20.591 38.731 10.804 1.00 31.46 ATOM 3026 OH2 TIP 195 24.147 43.407 2.885 1.00 28.20 ATOM 3027 OH2 TIP 196 21.907 27.234 26.192 1.00 42.64 ATOM 3028 OH2 TIP 197 63.736 33.840 22.009 1.00 35.07 ATOM 3029 OH2 TIP 198 32.794 49.844 23.701 1.00 37.84

ATOM 3030 OH2 TIP 199 58.947 40.782 13.015 1.00 31.28 ATOM 3031 OH2 TIP 200 22.450 49.976 21.694 1.00 38.42 ATOM 3032 OH2 TIP 201 49.606 32.017-6. 528 1.00 33.11 ATOM 3033 OH2 TIP 202 19.479 32.757 24.557 1.00 42.15 ATOM 3034 OH2 TIP 203 18.243 43.892 25.199 1.00 34.82 ATOM 3035 OH2 TIP 204 31.973 23.449 9.946 1.00 40.37 ATOM 3036 OH2 TIP 205 59.437 39.072 29.736 1.00 46.69 ATOM 3037 OH2 TIP 206 24.737 35.038-2. 305 1.00 38.20 ATOM 3038 OH2 TIP 207 51.798 24.226 23.337 1.00 43.38 ATOM 3039 OH2 TIP 208 41.169 63.155 0.607 1.00 47.72 ATOM 3040 OH2 TIP 209 44.987 24.799-6. 919 1.00 58.95 ATOM 3041 OH2 TIP 210 60.282 33.507 0.942 1.00 44.42 ATOM 3042 OH2 TIP 211 55.312 57.953-5. 133 1.00 61.46 ATOM 3043 OH2 TIP 212 26.359 34.821 3.588 1.00 40.79 ATOM 3044 OH2 TIP 213 57.280 58.607 2.155 1.00 54.60 ATOM 3045 OH2 TIP 214 48.954 19.470 7.776 1.00 37.71 ATOM 3046 OH2 TIP 215 18.783 34.339 22.498 1.00 38.96 ATOM 3047 OH2 TIP 216 50.074 55.671 3.640 1.00 42.87 ATOM 3048 OH2 TIP 217 23.725 39.251-3. 750 1.00 39.29 ATOM 3049 OH2 TIP 219 30.541 25.110 28.408 1.00 47.74 ATOM 3050 OH2 TIP 220 26.037 30.541 16.867 1.00 34.87 ATOM 3051 OH2 TIP 222 54.963 58.119 2.970 1.00 48.85 ATOM 3052 OH2 TIP 223 59.416 53.101-2. 816 1.00 55.72 ATOM 3053 OH2 TIP 224 51.466 23.460 28.005 1.00 42.28 ATOM 3054 OH2 TIP 225 37.482 39.527 29.584 1.00 30.27 ATOM 3055 OH2 TIP 226 20.502 42.025 22.632 1.00 58.53 ATOM 3056 OH2 TIP 227 38.047 51.915-4. 933 1.00 42.64 ATOM 3057 OH2 TIP 228 52.324 32.574 0.838 1.00 56.08 ATOM 3058 OH2 TIP 229 58.093 50.903 12.906 1.00 32.98 ATOM 3059 OH2 TIP 230 56.078 24.544 3.822 1.00 52.30 ATOM 3060 OH2 TIP 231 51.692 20.080 23.166 1.00 44.78 ATOM 3061 OH2 TIP 232 48. 112 18.431 16.203 1.00 49.60 ATOM 3062 OH2 TIP 233 49.693 20.764 19.679 1.00 38.77 ATOM 3063 OH2 TIP 234 61.205 40.496 27.215 1.00 39.59 ATOM 3064 OH2 TIP 235 60.244 28.451 9.868 1.00 37.16 ATOM 3065 OH2 TIP 236 39.531 20.627 25.697 1.00 40.03 ATOM 3066 OH2 TIP 237 21.925 38.965 24.059 1.00 48.68

ATOM 3067 OH2 TIP 238 41.611 40.577-15. 266 1.00 43.37 ATOM 3068 OH2 TIP 239 53.812 60.797 4.864 1.00 52.56 ATOM 3069 OH2 TIP 240 34.937 52.939-3. 717 1.00 35.04 ATOM 3070 OH2 TIP 241 55.261 34.522-10. 080 1.00 38.74 ATOM 3071 OH2 TIP 243 26.373 37.574-0. 254 1.00 36.58 ATOM 3072 OH2 TIP 244 51. 004 60.496 4.046 1.00 64.83 ATOM 3073 OH2 TIP 246 30.279 56.190 21.218 1.00 46.59 ATOM 3074 OH2 TIP 247 25.538 38.352 8.582 1.00 38.19 ATOM 3075 OH2 TIP 248 56.454 42.725 28.580 1.00 44.75 ATOM 3076 OH2 TIP 249 50.714 57.646 7.941 1.00 34.81 ATOM 3077 OH2 TIP 250 41.382 43.205 29.087 1.00 39.12 ATOM 3078 OH2 TIP 251 45.042 22.868 28.329 1.00 54.10 ATOM 3079 OH2 TIP 252 20.370 42.693 15.093 1.00 54.24 ATOM 3080 OH2 TIP 253 26.348 66.037 8.706 1.00 45.05 ATOM 3081 OH2 TIP 254 45.856 38.418-11. 622 1.00 53.29 ATOM 3082 OH2 TIP 255 42.753 41.622 34.537 1.00 39.32 ATOM 3083 OH2 TIP 256 48.240 52.734 26.556 1.00 43.67 ATOM 3084 OH2 TIP 257 39.530 58.162 23.453 1.00 48.05 ATOM 3085 OH2 TIP 258 37.524 57.192 25.020 1.00 42.73 ATOM 3086 OH2 TIP 259 50.658 56.406 11.908 1.00 31.97 ATOM 3087 OH2 TIP 260 59.957 24.763 12.383 1.00 36.65 ATOM 3088 OH2 TIP 261 23.929 35.872 6.187 1.00 42.26 ATOM 3089 OH2 TIP 262 64.700 52.165 26.674 1.00 64.00 ATOM 3090 OH2 TIP 263 35.594 61.. 606 20.210 1.00 48.50 ATOM 3091 OH2 TIP 264 43.651 65.314-7. 509 1.00 43.95 ATOM 3092 OH2 TIP 266 60.950 47.871 27.401 1.00 52.99 ATOM 3093 OH2 TIP 268 51.791 34.626 42.320 1.00 47.15 ATOM 3094 OH2 TIP 269 29.427 40.210 30.677 1.00 39.59 ATOM 3095 OH2 TIP 270 22.940 53.289 8.458 1.00 42.16 ATOM 3096 OH2 TIP 272 42.734 30.666 35.715 1.00 52.70 ATOM 3097 OH2 TIP 273 39.864 24.360 0.437 1.00 45.07 ATOM 3098 OH2 TIP 274 45.910 43.449 32.324 1.00 44.86 ATOM 3099 OH2 TIP 276 60.434 26.488 22.662 1.00 54.68 ATOM 3100 OH2 TIP 277 33.494 19.625 7.705 1.00 40.02 ATOM 3101 OH2 TIP 278 31.089 37.331 32.964 1.00 52.04 ATOM 3102 OH2 TIP 279 54.523 24.762 22.058 1.00 49.06 ATOM 3103 OH2 TIP 280 47.202 60.156 19.785 1.00 46.35

ATOM 3104 OH2 TIP 282 54.383 30.983 0.296 1.00 60.14 ATOM 3105 OH2 TIP 283 61.892 32.292 15.089 1.00 36.30 ATOM 3106 OH2 TIP 284 24.888 34.429-6. 950 1.00 41.74 ATOM 3107 OH2 TIP 285 24.688 32.139 26. 844 1.00 41.60 ATOM 3108 OH2 TIP 286 32.645 60.472 1.036 1.00 46.38 ATOM 3109 OH2 TIP 287 55.123 56.214 24.983 1.00 43.87 ATOM 3110 OH2 TIP 288 43.629 38.590 39.015 1.00 50.94 ATOM 3111 OH2 TIP 292 20.728 36.639 8.936 1.00 42.54 ATOM 3112 OH2 TIP 293 46.563 64.900 9.456 1.00 50.04 ATOM 3113 OH2 TIP 294 17.012 60.160 10.502 1.00 48.90 ATOM 3114 OH2 TIP 295 17.480 28.871 19.492 1.00 42.05 ATOM 3115 OH2 TIP 297 36.366 31.406 32.340 1.00 42.47 ATOM 3116 OH2 TIP 300 46.719 59.238-13. 542 1.00 50.25 ATOM 3117 OH2 TIP 301 29.641 25.448 9.713 1.00 41.77 ATOM 3118 OH2 TIP 302 50.828 58.438 0.448 1.00 42.42 ATOM 3119 OH2 TIP 303 29.614 52.009 22.188 1.00 37.94 ATOM 3120 OH2 TIP 304 34.557 62.012 23.304 1.00 43.17 ATOM 3121 OH2 TIP 305 28.994 20.961 23.471 1.00 43.02 ATOM 3122 OH2 TIP 306 50.941 49.902 28.007 1.00 48.48 ATOM 3123 OH2 TIP 307 18.496 51.343 16.991 1.00 44.97 ATOM 3124 OH2 TIP 309 42.051 36.930-13. 933 1.00 44.70 ATOM 3125 OH2 TIP 310 45.128 42.750-9. 449 1.00 47.67 TER 1 TIP 310 ATOM 1 CB MET A 30 59.712 55.163-5. 647 1.00 80.31 ATOM 2 CG MET A 30 59.865 54.409-6. 958 1.00 80.66 ATOM 3 SD MET A 30 59.205 52.733-6. 845 1.00 80.85 ATOM 4 CE MET A 30 60.589 51.860-6. 102 1.00 80.82 ATOM 5 C MET A 30 58.219 55.645-3. 704 1.00 79.00 ATOM 6 0 MET A 30 57.240 55.324-3. 032 1.00 78.32 ATOM 7 N MET A 30 57.620 56.445-6. 003 1.00 79.37 ATOM 8 CA MET A 30 58.259 55.360-5. 203 1.00 79.50 ATOM 9 N ALA A 31 59.288 56.244-3. 187 1.00 78.38 ATOM 10 CA ALA A 31 59.378 56.571-1. 767 1.00 76.94 ATOM 11 CB ALA A 31 60.826 56.867-1. 390 1.00 77.21 ATOM 12 C ALA A 31 58.492 57.763-1. 419 1.00 75.64 ATOM 13 0 ALA A 31 58.167 57.987-0. 252 1.00 75.52 ATOM 14 N THR A 32 58.104 58.523-2. 438 1.00 74.06

ATOM 15 CA THR A 32 57.254 59.694-2. 249 1.00 71.96 ATOM 16 CB THR A 32 57.059 60. 455-3. 576 1.00 72.87 ATOM 17 OG1 THR A 32 58.330 60.918-4. 054 1.00 72.48 ATOM 18 CG2 THR A 32 56.124 61.644-3. 379 1.00 72.82 ATOM 19 C THR A 32 55.887 59.290-1. 703 1.00 69. 77 ATOM 20 O THR A 32 55.268 60.030-0. 935 1.00 70.16 ATOM 21 N GLY A 33 55.419 58.114-2. 107 1.00 66.46 ATOM 22 CA GLY A 33 54.136 57.630-1. 637 1.00 61.99 ATOM 23 C GLY A 33 52.945 58.292-2. 296 1.00 58.74 ATOM 24 O GLY A 33 52.090 58.860-1. 617 1.00 59.57 ATOM 25 N ASP A 34 52.881 58.221-3. 621 1.00 54.17 ATOM 26 CA ASP A 34 51.772 58.820-4. 347 1.00 49.04 ATOM 27 CB ASP A 34 52.274 59.467-5. 635 1.00 48.74 ATOM 28 CG ASP A 34 51.157 60.059-6. 457 1.00 48.55 ATOM 29 OD1 ASP A 34 50.669 59.367-7. 375 1.00 48.93 ATOM 30 OD2 ASP A 34 50.757 61.211-6. 178 1.00 49.18 ATOM 31 C ASP A 34 50.692 57.784-4. 652 1.00 46.02 ATOM 32 0 ASP A 34 50. 959 56.738-5. 248 1.00 43.47 ATOM 33 N GLU A 35 49.469 58.095-4. 232 1.00 43.20 ATOM 34 CA GLU A 35 48.325 57.211-4. 415 1.00 40.89 ATOM 35 CB GLU A 35 47.077 57.866-3. 811 1.00 40.86 ATOM 36 CG GLU A 35 47.070 57.852-2. 283 1.00 42.25 ATOM 37 CD GLU A 35 46.082 58.836-1. 674 1.00 43.75 ATOM 38 OE1 GLU A 35 44.971 58.997-2. 224 1.00 45.16 ATOM 39 OE2 GLU A 35 46.416 59.439-0. 631 1.00 41.85 ATOM 40 C GLU A 35 48.063 56.784-5. 858 1.00 39.00 ATOM 41 0 GLU A 35 47.816 55.606-6. 114 1.00 37.91 ATOM 42 N ARG A 36 48.122 57.726-6. 799 1.00 37.60 ATOM 43 CA ARG A 36 47.883 57.394-8. 201 1.00 36.88 ATOM 44 CB ARG A 36 47.776 58.651-9. 066 1.00 40.39 ATOM 45 CG ARG A 36 46.472 59.413-8. 956 1.00 45.00 ATOM 46 CD ARG A 36 46.295 60.312-10. 173 1.00 47.46 ATOM 47 NE ARG A 36 45.485 61.487-9. 880 1.00 51.68 ATOM 48 CZ ARG A 36 45.837 62.440-9. 020 1.00 53.65 ATOM 49 NH1 ARG A 36 46.988 62.355-8. 367 1.00 54.00 ATOM 50 NH2 ARG A 36 45.041 63.482-8. 817 1.00 54.73 ATOM 51 C ARG A 36 48.965 56.510-8. 795 1.00 35.07

ATOM 52 O ARG A 36 48.669 55.565-9. 524 1.00 34.58 ATOM 53 N PHE A 37 50.221 56.822-8. 494 1.00 33.78 ATOM 54 CA PHE A 37 51.325 56.042-9. 030 1.00 33.03 ATOM 55 CB PHE A 37 52.671 56.593-8. 558 1.00 33.86 ATOM 56 CG PHE A 37 53.846 55. 870-9. 146 1.00 36.09 ATOM 57 CD1 PHE A 37 54.113 55.953-10. 503 1.00 36.07 ATOM 58 CD2 PHE A 37 54.660 55.077-8. 353 1.00 37.36 ATOM 59 CE1 PHE A 37 55.171 55.256-11. 059 1.00 38.02 ATOM 60 CE2 PHE A 37 55.720 54.376-8. 903 1.00 37.55 ATOM 61 CZ PHE A 37 55.975 54.466-10. 257 1.00 38.09 ATOM 62 C PHE A 37 51.228 54.575-8. 643 1.00 30.97 ATOM 63 0 PHE A 37 51.393 53.693-9. 484 1.00 30.44 ATOM 64 N TYR A 38 50.969 54.311-7. 368 1.00 30.50 ATOM 65 CA TYR A 38 50.856 52.933-6. 910 1.00 31.45 ATOM 66 CB TYR A 38 50.826 52.873-5. 381 1.00 30.08 ATOM 67 CG TYR A 38 52.197 52.901-4. 749 1.00 29.63 ATOM 68 CD1 TYR A 38 52.936 54.078-4. 693 1.00 29.71 ATOM 69 CE1 TYR A 38 54.202 54.099-4. 132 1.00 29.16 ATOM 70 CD2 TYR A 38 52.764 51.742-4. 226 1.00 26.96 ATOM 71 CE2 TYR A 38 54.026 51.751-3. 668 1.00 27.02 ATOM 72 CZ TYR A 38 54.740 52.931-3. 624 1.00 29.27 ATOM 73 OH TYR A 38 56.001 52.940-3. 086 1.00 30.40 ATOM 74 C TYR A 38 49.619 52.256-7. 474 1.00 32.16 ATOM 75 0 TYR A 38 49.684 51. 126-7. 953 1.00 31.25 ATOM 76 N ALA A 39 48.494 52.960-7. 425 1.00 33.95 ATOM 77 CA ALA A 39 47.234 52.425-7. 918 1.00 36.26 ATOM 78 CB ALA A 39 46.094 53.349-7. 517 1.00 36.53 ATOM 79 C ALA A 39 47.215 52.209-9. 428 1.00 37.90 ATOM 80 0 ALA A 39 46.781 51. 158-9. 909 1.00 37.48 ATOM 81 N GLU A 40 47.696 53.201-10. 171 1.00 40.13 ATOM 82 CA GLU A 40 47.696 53.134-11. 629 1.00 41.55 ATOM 83 CB GLU A 40 47.512 54.540-12. 215 1.00 43.53 ATOM 84 CG GLU A 40 46.262 55.264-11. 735 1.00 47.12 ATOM 85 CD GLU A 40 46.122 56.651-12. 340 1.00 49.89 ATOM 86 OE1 GLU A 40 46.081 56.751-13. 585 1.00 52.64 ATOM 87 OE2 GLU A 40 46.051 57.639-11. 574 1.00 50.61 ATOM 88 C GLU A 40 48.911 52.489-12. 286 1.00 40.57

ATOM 89 O GLU A 40 48.785 51. 894-13. 354 1.00 40.85 ATOM 90 N HIS A 41 50.083 52. 587-11. 664 1.00 39.75 ATOM 91 CA HIS A 41 51.275 52. 024-12. 293 1.00 38.62 ATOM 92 CB HIS A 41 52.266 53.146-12. 621 1.00 40.78 ATOM 93 CG HIS A 41 51.689 54.227-13. 479 1.00 44.09 ATOM 94 CD2 HIS A 41 51.777 54.451-14. 811 1.00 45.23 ATOM 95 ND1 HIS A 41 50.876 55.222-12. 977 1.00 46.21 ATOM 96 CE1 HIS A 41 50.488 56.011-13. 963 1.00 46.60 ATOM 97 NE2 HIS A 41 51.021 55.565-15. 086 1.00 47.61 ATOM 98 C HIS A 41 52.032 50.903-11. 594 1.00 35.71 ATOM 99 O HIS A 41 52.177 49.812-12. 146 1.00 35.85 ATOM 100 N LEU A 42 52.525 51.165-10. 392 1.00 33.29 ATOM 101 CA LEU A 42 53.311 50.161-9. 682 1.00 32.13 ATOM 102 CB LEU A 42 53.883 50.761-8. 393 1.00 31.28 ATOM 103 CG LEU A 42 55.057 49.987-7. 781 1.00 34.33 ATOM 104 CD1 LEU A 42 55.897 50.923-6. 925 1.00 33.63 ATOM 105 CD2 LEU A 42 54.542 48.804-6. 967 1.00 34.74 ATOM 106 C LEU A 42 52.581 48.850-9. 382 1.00 30.26 ATOM 107 O LEU A 42 52.981 47.794-9. 871 1.00 31.23 ATOM 108 N MET A 43 51.519 48.911-8. 586 1.00 27.76 ATOM 109 CA MET A 43 50.772 47.706-8. 232 1.00 27.76 ATOM 110 CB MET A 43 49.552 48.066-7. 379 1.00 24.10 ATOM 111 CG MET A 43 49.918 48.634-6. 022 1.00 23.32 ATOM 112 SD MET A 43 51.075 47.574-5. 113 1.00 25.43 ATOM 113 CE MET A 43 49.970 46.252-4. 615 1.00 21.95 ATOM 114 C MET A 43 50.343 46.878-9. 440 1.00 28.21 ATOM 115 0 MET A 43 50.517 45.661-9. 454 1.00 27.46 ATOM 116 N PRO A 44 49.766 47.524-10. 466 1.00 29.90 ATOM 117 CD PRO A 44 49.323 48.929-10. 518 1.00 28.73 ATOM 118 CA PRO A 44 49.333 46.797-11. 664 1.00 30. 50 ATOM 119 CB PRO A 44 48.757 47.902-12. 542 1.00 30.16 ATOM 120 CG PRO A 44 48.222 48.875-11. 541 1.00 30.35 ATOM 121 C PRO A 44 50.499 46.075-12. 343 1.00 32.56 ATOM 122 O PRO A 44 50.369 44.927-12. 770 1.00 33.27 ATOM 123 N THR A 45 51.637 46.756-12. 442 1.00 33.42 ATOM 124 CA THR A 45 52.821 46.180-13. 071 1.00 34.86 ATOM 125 CB THR A 45 53.950 47.225-13. 197 1.00 36.09

ATOM 126 OG1 THR A 45 53.499 48.323-14. 001 1.00 33.74 ATOM 127 CG2 THR A 45 55.187 46.599-13. 837 1.00 35.67 ATOM 128 C THR A 45 53.335 45.012-12. 242 1.00 36.57 ATOM 129 0 THR A 45 53.717 43.970-12. 774 1.00 36.59 ATOM 130 N LEU A 46 53.342 45.199-10. 928 1.00 38.25 ATOM 131 CA LEU A 46 53.801 44.170-10. 008 1.00 38.66 ATOM 132 CB LEU A 46 53.726 44.694-8. 575 1.00 39.21 ATOM 133 CG LEU A 46 54.329 43.815-7. 483 1.00 41.10 ATOM 134 CD1 LEU A 46 55.784 43.519-7. 815 1.00 43.25 ATOM 135 CD2 LEU A 46 54.222 44.528-6. 144 1.00 41.41 ATOM 136 C LEU A 46 52.946 42.914-10. 144 1.00 38.98 ATOM 137 O LEU A 46 53.466 41.800-10. 187 1.00 39.35 ATOM 138 N GLN A 47 51.633 43.102-10. 219 1.00 38.99 ATOM 139 CA GLN A 47 50.709 41.981-10. 339 1.00 40.71 ATOM 140 CB GLN A 47 49.300 42.425-9. 929 1.00 40.91 ATOM 141 CG GLN A 47 49.228 42.899-8. 478 1.00 42.99 ATOM 142 CD GLN A 47 47.833 43.314-8. 052 1.00 45.00 ATOM 143 OE1 GLN A 47 47.222 44.195-8. 657 1.00 47.02 ATOM 144 NE2 GLN A 47 47.323 42.683-7. 001 1.00 45.03 ATOM 145 C GLN A 47 50.701 41.373-11. 741 1.00 39.99 ATOM 146 0 GLN A 47 50.246 40.246-11. 937 1.00 39. 01 ATOM 147 N GLY A 48 51.216 42.119-12. 712 1.00 40.83 ATOM 148 CA GLY A 48 51.276 41.616-14. 073 1.00 39.56 ATOM 149 C GLY A 48 52.526 40.780-14. 291 1.00 39.27 ATOM 150 0 GLY A 48 52.678 40.135-15. 327 1.00 40.98 ATOM 151 N LEU A 49 53.422 40.784-13. 308 1.00 37.67 ATOM 152 CA LEU A 49 54.667 40.027-13. 396 1.00 37.43 ATOM 153 CB LEU A 49 55.867 40.954-13. 186 1.00 38.73 ATOM 154 CG LEU A 49 56.105 42.068-14. 208 1.00 38.96 ATOM 155 CD1 LEU A 49 57.270 42.932-13. 755 1.00 38.41 ATOM 156 CD2 LEU A 49 56.384 41.457-15. 571 1.00 39.54 ATOM 157 C LEU A 49 54.741 38.899-12. 376 1.00 36.89 ATOM 158 0 LEU A 49 55.451 37.918-12. 582 1.00 37.19 ATOM 159 N LEU A 50 54.010 39.041-11. 275 1.00 36.34 ATOM 160 CA LEU A 50 54. 019 38.038-10. 214 1.00 34.90 ATOM 161 CB LEU A 50 54.607 38.644-8. 935 1.00 35.62 ATOM 162 CG LEU A 50 56.057 39.128-8. 994 1.00 36.46

ATOM 163 CD1 LEU A 50 56.396 39.878-7. 717 1.00 36.33 ATOM 164 CD2 LEU A 50 56.988 37.937-9. 185 1.00 35.82 ATOM 165 C LEU A 50 52.635 37.484-9. 904 1.00 34.02 ATOM 166 O LEU A 50 51.647 38.219-9. 902 1.00 34.02 ATOM 167 N ASP A 51 52.566 36.183-9. 637 1.00 32.65 ATOM 168 CA ASP A 51 51.294 35.563-9. 299 1.00 32.66 ATOM 169 CB ASP A 51 51.403 34.036-9. 364 1.00 33.88 ATOM 170 CG ASP A 51 52.350 33.476-8. 329 1.00 36.45 ATOM 171 OD1 ASP A 51 53.554 33.802-8. 389 1.00 38.39 ATOM 172 OD2 ASP A 51 51.889 32.709-7. 456 1.00 37.67 ATOM 173 C ASP A 51 50.939 36.026-7. 882 1.00 30.84 ATOM 174 O ASP A 51 51.812 36.467-7. 130 1.00 30.91 ATOM 175 N PRO A 52 49.656 35. 931-7. 502 1.00 28.67 ATOM 176 CD PRO A 52 48.574 35.295-8. 273 1.00 27.32 ATOM 177 CA PRO A 52 49.174 36.347-6. 179 1.00 27.35 ATOM 178 CB PRO A 52 47.804 35.684-6. 094 1.00 28.92 ATOM 179 CG PRO A 52 47.339 35.728-7. 514 1.00 27.85 ATOM 180 C PRO A 52 50.072 35.989-4. 994 1.00 25.30 ATOM 181 O PRO A 52 50.509 36.867-4. 255 1.00 25.37 ATOM 182 N GLU A 53 50.357 34.707-4. 814 1.00 24.59 ATOM 183 CA GLU A 53 51.190 34.285-3. 696 1.00 25.59 ATOM 184 CB GLU A 53 51.233 32.758-3. 614 1.00 25.66 ATOM 185 CG GLU A 53 51.907 32.257-2. 353 1.00 27.24 ATOM 186 CD GLU A 53 51.431 30.882-1. 929 1.00 28.48 ATOM 187 OE1 GLU A 53 51.979 30.357-0. 940 1.00 31.42 ATOM 188 OE2 GLU A 53 50.512 30.329-2. 574 1.00 27.49 ATOM 189 C GLU A 53 52.614 34.856-3. 722 1.00 25.68 ATOM 190 0 GLU A 53 53.119 35.298-2. 688 1.00 24.08 ATOM 191 N SER A 54 53.259 34.850-4. 887 1.00 24.37 ATOM 192 CA SERA 54 54.609 35.396-4. 996 1.00 24.85 ATOM 193 CB SER A 54 55.175 35.184-6. 404 1.00 25.94 ATOM 194 OG SER A 54 55.400 33.810-6. 667 1.00 28.92 ATOM 195 C SER A 54 54.592 36.887-4. 683 1.00 25.02 ATOM 196 0 SER A 54 55.511 37.408-4. 048 1.00 25.15 ATOM 197 N ALA A 55 53.545 37.570-5. 140 1.00 23.67 ATOM 198 CA ALA A 55 53.401 38.999-4. 904 1.00 22.81 ATOM 199 CB ALA A 55 52.155 39.525-5. 617 1.00 21.78

ATOM 200 C ALA A 55 53.290 39.236-3. 400 1.00 22.62 ATOM 201 0 ALA A 55 53. 913 40.143-2. 850 1.00 22.65 ATOM 202 N HIS A 56 52.492 38.410-2. 737 1.00 22.22 ATOM 203 CA HIS A 56 52.316 38.538-1. 300 1.00 23.60 ATOM 204 CB HIS A 56 51.296 37.523-0. 792 1.00 19.67 ATOM 205 CG HIS A 56 51.232 37.449 0.699 1.00 19.95 ATOM 206 CD2 HIS A 56 51.489 36.432 1.554 1.00 17.66 ATOM 207 ND1 HIS A 56 50.908 38.537 1.482 1.00 20.51 ATOM 208 CE1 HIS A 56 50.969 38.192 2.754 1.00 19.63 ATOM 209 NE2 HIS A 56 51.321 36.921 2.826 1.00 18.97 ATOM 210 C HIS A 56 53.627 38.344-0. 539 1.00 25.30 ATOM 211 0 HIS A 56 53.952 39.119 0.367 1.00 24.97 ATOM 212 N ARG A 57 54.373 37.306-0. 906 1.00 26.20 ATOM 213 CA ARG A 57 55.641 37.006-0. 253 1.00 29.31 ATOM 214 CB ARG A 57 56.233 35.715-0. 822 1.00 32.99 ATOM 215 CG ARG A 57 55.250 34.553-0. 767 1.00 40.69 ATOM 216 CD ARG A 57 55.893 33.223-1. 118 1.00 45.69 ATOM 217 NE ARG A 57 56.865 32. 810-0. 111 1.00 51.83 ATOM 218 CZ ARG A 57 57.386 31.591-0. 034 1.00 54.55 ATOM 219 NH1 ARG A 57 57.027 30.657-0. 907 1.00 55.29 ATOM 220 NH2 ARG A 57 58.264 31.302 0.920 1.00 56.65 ATOM 221 C ARG A 57 56.630 38.152-0. 400 1.00 27.88 ATOM 222 0 ARG A 57 57.344 38.483 0.543 1.00 28.70 ATOM 223 N LEU A 58 56.665 38.762-1. 579 1.00 27.01 ATOM 224 CA LEU A 58 57.561 39.886-1. 823 1.00 27.01 ATOM 225 CB LEU A 58 57.540 40.266-3. 306 1.00 29.93 ATOM 226 CG LEU A 58 58.560 41.316-3. 754 1.00 32.39 ATOM 227 CD1 LEU A 58 59.969 40.741-3. 628 1.00 33.40 ATOM 228 CD2 LEU A 58 58.280 41.729-5. 193 1.00 33.62 ATOM 229 C LEU A 58 57.095 41.074-0. 979 1.00 26.41 ATOM 230 0 LEU A 58 57.906 41.846-0. 462 1.00 25.09 ATOM 231 N ALA A 59 55.777 41.211-0. 851 1.00 24.78 ATOM 232 CA ALA A 59 55.177 42.286-0. 069 1.00 22.97 ATOM 233 CB ALA A 59 53.657 42.189-0. 125 1.00 21.53 ATOM 234 C ALA A 59 55.645 42.196 1.373 1.00 20.70 ATOM 235 0 ALA A 59 56.011 43.199 1.982 1.00 20.94 ATOM 236 N VAL A 60 55.621 40.987 1.919 1.00 19.75

ATOM 237 CA VAL A 60 56.053 40.776 3.292 1.00 19.54, ATOM 238 CB VAL A 60 55.804 39.312 3.732 1.00 18.51 ATOM 239 CG1 VAL A 60 56.381 39.070 5.125 1.00 16.83 ATOM 240 CG2 VAL A 60 54.308 39.022 3.722 1.00 14.84 ATOM 241 C VAL A 60 57.540 41.117 3.421 1.00 20.80 ATOM 242 0 VAL A 60 57.945 41.783 4.372 1.00 20.78 ATOM 243 N ARG A 61 58.346 40.674 2.458 1.00 23.54 ATOM 244 CA ARG A 61 59.782 40.954 2.477 1.00 27.19 ATOM 245 CB ARG A 61 60.483 40.362 1.249 1.00 29.60 ATOM 246 CG ARG A 61 60.452 38.847 1.135 1.00 38.29 ATOM 247 CD ARG A 61 61.547 38.376 0.170 1.00 44.72 ATOM 248 NE ARG A 61 61.507 36.938-0. 097 1.00 50.19 ATOM 249 CZ ARG A 61 60.690 36.356-0. 972 1.00 51.81 ATOM 250 NH1 ARG A 61 59.836 37.086-1. 678 1.00 51.44 ATOM 251 NH2 ARG A 61 60.728 35. 040-1. 143 1.00 52.85 ATOM 252 C ARG A 61 60.056 42.456 2.503 1.00 26.67 ATOM 253 0 ARG A 61 60.766 42.951 3.380 1.00 25.34 ATOM 254 N PHE A 62 59.496 43.174 1.534 1.00 26.17 ATOM 255 CA PHE A 62 59.704 44.613 1.447 1.00 28.72 ATOM 256 CB PHE A 62 58.977 45.187 0.229 1.00 31.46 ATOM 257 CG PHE A 62 59.783 45.127-1. 035 1.00 35.66 ATOM 258 CD1 PHE A 62 60.279 43.921-1. 501 1.00 36.94 ATOM 259 CD2 PHE A 62 60.052 46.279-1. 756 1.00 39.16 ATOM 260 CE1 PHE A 62 61.029 43.865-2. 663 1.00 38.76 ATOM 261 CE2 PHE A 62 60.803 46.231-2. 919 1.00 40.51 ATOM 262 CZ PHE A 62 61.291 45.020-3. 373 1.00 39.34 ATOM 263 C PHE A 62 59.262 45.347 2.700 1.00 28.83 ATOM 264 0 PHE A 62 59.946 46.260 3.166 1.00 28.57 ATOM 265 N THR A 63 58.117 44.948 3.244 1.00 28.55 ATOM 266 CA THR A 63 57.594 45.580 4.444 1.00 27.95 ATOM 267 CB THR A 63 56.193 45.030 4.800 1.00 26.73 ATOM 268 OG1 THR A 63 55.292 45.280 3.715 1.00 25.39 ATOM 269 CG2 THR A 63 55.656 45.706 6.048 1.00 26.61 ATOM 270 C THR A 63 58.538 45.346 5.619 1.00 28.75 ATOM 271 O THR A 63 58.847 46.272 6.372 1.00 27.36 ATOM 272 N SER A 64 59.003 44.109 5.769 1.00 28.81 ATOM 273 CA SER A 64 59.905 43.783 6.867 1.00 31.26

ATOM 274 CB SER A 64 60.234 42.287 6.866 1.00 30.34 ATOM 275 OG SER A 64 61.025 41.938 5.744 1.00 34.64 ATOM 276 C SER A 64 61.193 44.596 6.771 1.00 31.63 ATOM 277 0 SER A 64 61.794 44.939 7.785 1.00 31.52 ATOM 278 N LEU A 65 61.606 44.914 5.547 1.00 33.19 ATOM 279 CA LEU A 65 62.828 45.686 5.332 1.00 34.17 ATOM 280 CB LEU A 65 63.500 45.257 4.026 1.00 33.79 ATOM 281 CG LEU A 65 63.988 43.807 3.993 1.00 36.63 ATOM 282 CD1 LEU A 65 64.621 43.507 2.646 1.00 34.56 ATOM 283 CD2 LEU A 65 64.990 43.579 5.124 1.00 37.33 ATOM 284 C LEU A 65 62.596 47.196 5.316 1.00 33.85 ATOM 285 O LEU A 65 63.542 47.969 5.195 1.00 34.26 ATOM 286 N GLY A 66 61.341 47.614 5.430 1.00 33.45 ATOM 287 CA GLY A 66 61.040 49.035 5.437 1.00 34.55 ATOM 288 C GLY A 66 61.062 49.729 4.083 1.00 35.86 ATOM 289 0 GLY A 66 61.103 50.961 4.016 1.00 35.51 ATOM 290 N LEU A 67 61.036 48.953 3.003 1.00 36.35 ATOM 291 CA LEU A 67 61.043 49.522 1.658 1.00 37.31 ATOM 292 CB LEU A 67 61.467 48.456 0.640 1.00 38.96 ATOM 293 CG LEU A 67 62.781 47.731 0.967 1.00 41.48 ATOM 294 CD1 LEU A 67 63.077 46.689-0. 099 1.00 41.55 ATOM 295 CD2 LEU A 67 63.922 48.739 1.059 1.00 42.89 ATOM 296 C LEU A 67 59.628 50.012 1.361 1.00 36.64 ATOM 297 0 LEU A 67 58.894 49.406 0.583 1.00 35.87 ATOM 298 N LEU A 68 59.259 51.119 1.996 1.00 37.15 ATOM 299 CA LEU A 68 57.927 51.693 1.858 1.00 38.24 ATOM 300 CB LEU A 68 57.184 51.573 3.188 1.00 38.62 ATOM 301 CG LEU A 68 57.210 50.196 3.851 1.00 39.70 ATOM 302 CD1 LEU A 68 56.699 50.303 5.275 1.00 39.82 ATOM 303 CD2 LEU A 68 56.373 49.226 3.037 1.00 40.12 ATOM 304 C LEU A 68 57.967 53.160 1.450 1.00 38.59 ATOM 305 0 LEU A 68 58.903 53.884 1.782 1.00 39.27 ATOM 306 N PRO A 69 56.932 53.616 0.729 1.00 38.61 ATOM 307 CD PRO A 69 55.779 52.813 0.291 1.00 37.91 ATOM 308 CA PRO A 69 56.807 54.997 0.257 1.00 39.04 ATOM 309 CB PRO A 69 55.590 54.932-0. 660 1.00 38.47 ATOM 310 CG PRO A 69 54.754 53.878-0. 023 1.00 38.21

ATOM 311 C PRO A 69 56.620 55.991 1.400 1.00 39.37 ATOM 312 0 PRO A 69 56.828 55.657 2.566 1.00 39.95 ATOM 313 N PHE A 73 51.580 61.610 6.291 1.00 57.27 ATOM 314 CA PHE A 73 50.360 61.873 7.047 1.00 57.38 ATOM 315 CB PHE A 73 49.221 60.966 6.569 1.00 57.90 ATOM 316 CG PHE A 73 47.951 61.126 7.361 1.00 58.13 ATOM 317 CD1 PHE A 73 47.092 62.186 7.116 1.00 58.39 ATOM 318 CD2 PHE A 73 47.638 60.241 8.381 1.00 58.13 ATOM 319 CE1 PHE A 73 45.947 62.362 7.876 1.00 58.24 ATOM 320 CE2 PHE A 73 46.495 60.412 9.144 1.00 57.41 ATOM 321 CZ PHE A 73 45.649 61.473 8.891 1.00 57.23 ATOM 322 C PHE A 73 50.553 61.656 8.543 1.00 56.41 ATOM 323 O PHE A 73 50.901 60.557 8.979 1.00 56.28 ATOM 324 N GLN A 74 50.320 62.705 9.326 1.00 55.49 ATOM 325 CA GLN A 74 50.443 62.615 10.776 1.00 53.88 ATOM 326 CB GLN A 74 51.072 63.883 11.356 1.00 55.26 ATOM 327 CG GLN A 74 52.570 64.009 11.142 1.00 57.78 ATOM 328 CD GLN A 74 53.176 65.133 11.970 1.00 59.54 ATOM 329 OE1 GLN A 74 52.910 66.314 11.733 1.00 59.29 ATOM 330 NE2 GLN A 74 53.988 64.767 12.957 1.00 59.59 ATOM 331 C GLN A 74 49.061 62.421 11.384 1.00 51.65 ATOM 332 0 GLN A 74 48.124 63.149 11.063 1.00 50.88 ATOM 333 N ASP A 75 48.941 61.430 12.257 1.00 49.61 ATOM 334 CA ASP A 75 47.673 61.140 12.912 1.00 47.33 ATOM 335 CB ASP A 75 47.786 59.839 13.712 1.00 46.31 ATOM 336 CG ASP A 75 48.187 58.657 12.849 1.00 44.20 ATOM 337 OD1 ASP A 75 48.706 57.661 13.399 1.00 41.48 ATOM 338 OD2 ASP A 75 47.974 58.724 11.621 1.00 44.07 ATOM 339 C ASP A 75 47.329 62.291 13.851 1.00 46.57 ATOM 340 0 ASP A 75 48.192 62.785 14.576 1.00 46.45 ATOM 341 N SER A 76 46.073 62.724 13.833 1.00 45.69 ATOM 342 CA SER A 76 45.645 63.809 14.706 1.00 44.11 ATOM 343 CB SER A 76 44.700 64.758 13.965 1.00 44.07 ATOM 344 OG SER A 76 43.480 64.113 13.647 1.00 46.09 ATOM 345 C SER A 76 44. 931 63.210 15.905 1.00 42.29 ATOM 346 0 SER A 76 44.517 62.054 15.872 1.00 43.18 ATOM 347 N ASP A 77 44.793 63.997 16.964 1.00 41.16

ATOM 348 CA ASP A 77 44.122 63.541 18.174 1.00 41.04 ATOM 349 CB ASP A 77 43.962 64.709 19.150 1.00 43.43 ATOM 350 CG ASP A 77 45.296 65.278 19. 605 1.00 47.07 ATOM 351 OD1 ASP A 77 45.294 66.321 20.293 1.00 48.75 ATOM 352 OD2 ASP A 77 46.347 64.682 19.281 1.00 48.82 ATOM 353 C ASP A 77 42.753 62.939 17.861 1.00 39. 12 ATOM 354 0 ASP A 77 42.286 62.045 18.564 1.00 38.74 ATOM 355 N MET A 78 42.118 63.435 16.802 1.00 37.74 ATOM 356 CA MET A 78 40.797 62.961 16.385 1.00 36.19 ATOM 357 CB MET A 78 40.349 63.676 15.109 1.00 37.19 ATOM 358 CG MET A 78 40.014 65.135 15.267 1.00 39.81 ATOM 359 SD MET A 78 39.364 65.773 13.711 1.00 44.22 ATOM 360 CE MET A 78 37.676 65.136 13.771 1.00 41. 40 ATOM 361 C MET A 78 40.737 61.460 16.118 1.00 33.43 ATOM 362 O MET A 78 39.739 60.807 16.423 1.00 32.83 ATOM 363 N LEU A 79 41.803 60.923 15.534 1.00 29.93 ATOM 364 CA LEU A 79 41.847 59.508 15.201 1.00 28.79 ATOM 365 CB LEU A 79 42.839 59.273 14.059 1.00 26.98 ATOM 366 CG LEU A 79 42.524 60. 001 12.745 1.00 28.06 ATOM 367 CD1 LEU A 79 43.498 59.551 11.662 1.00 25.66 ATOM 368 CD2 LEU A 79 41.085 59.712 12.321 1.00 25.01 ATOM 369 C LEU A 79 42.186 58.599 16.375 1.00 28.13 ATOM 370 0 LEU A 79 42.097 57.377 16.258 1.00 27.01 ATOM 371 N GLU A 80 42.562 59.187 17.505 1.00 27.26 ATOM 372 CA GLU A 80 42.909 58.392 18.672 1.00 28.24 ATOM 373 CB GLU A 80 43.622 59.248 19.724 1.00 30.41 ATOM 374 CG GLU A 80 43.753 58.555 21.080 1.00 36.61 ATOM 375 CD GLU A 80 44.624 59.320 22.067 1.00 40.69 ATOM 376 OE1 GLU A 80 44.508 59.059 23.284 1.00 41.38 ATOM 377 OE2 GLU A 80 45.432 60.171 21.630 1.00 43.40 ATOM 378 C GLU A 80 41.686 57.735 19.291 1.00 27.76 ATOM 379 0 GLU A 80 40.636 58.356 19.437 1.00 29.08 ATOM 380 N VAL A 81 41.831 56.469 19.652 1.00 26.18 ATOM 381 CA VAL A 81 40.747 55.717 20.258 1.00 26.74 ATOM 382 CB VAL A 81 40.134 54.702 19.259 1.00 27.51 ATOM 383 CG1 VAL A 81 38.943 53.996 19.895 1.00 26.14 ATOM 384 CG2 VAL A 81 39.723 55.407 17.981 1.00 27.18

ATOM 385 C VAL A 81 41.292 54.936 21.441 1.00 26.74 ATOM 386 O VAL A 81 42.455 54.525 21.441 1.00 27.00 ATOM 387 N ARG A 82 40.457 54.735 22.452 1.00 27.63 ATOM 388 CA ARG A 82 40.878 53.971 23.613 1.00 29.47 ATOM 389 CB ARG A 82 40.960 54.852 24.862 1.00 32.41 ATOM 390 CG ARG A 82 42.027 54.360 25.826 1.00 40.18 ATOM 391 CD ARG A 82 41.648 54.500 27.294 1.00 45.31 ATOM 392 NE ARG A 82 42.675 53.907 28.156 1.00 48.83 ATOM 393 CZ ARG A 82 43.075 52.639 28.082 1.00 48.91 ATOM 394 NH1 ARG A 82 42.538 51.818 27.188 1.00 49.58 ATOM 395 NH2 ARG A 82 44.021 52.192 28.895 1.00 50.35 ATOM 396 C ARG A 82 39.898 52.835 23.855 1.00 28.41 ATOM 397 0 ARG A 82 38.730 53.070 24.154 1.00 29.65 ATOM 398 N VAL A 83 40.382 51.604 23.713 1.00 28.37 ATOM 399 CA VAL A 83 39.570 50.407 23.918 1.00 28.82 ATOM 400 CB VAL A 83 38.745 50.038 22.662 1.00 29.44 ATOM 401 CG1 VAL A 83 37.511 50.915 22.570 1.00 30.89 ATOM 402 CG2 VAL A 83 39.608 50.181 21.413 1.00 25.04 ATOM 403 C VAL A 83 40.457 49.217 24.235 1.00 29.77 ATOM 404 0 VAL A 83 41.673 49.281 24.066 1.00 29.28 ATOM 405 N LEU A 84 39.836 48.130 24.688 1.00 31.31 ATOM 406 CA LEU A 84 40.559 46.902 25.009 1.00 32.35 ATOM 407 CB LEU A 84 41.071 46.250 23.714 1.00 31.07 ATOM 408 CG LEU A 84 40.002 45.965 22.649 1.00 31.01 ATOM 409 CD1 LEU A 84 40.659 45.510 21.363 1.00 30.37 ATOM 410 CD2 LEU A 84 39.028 44.917 23.160 1.00 26.83 ATOM 411 C LEU A 84 41.731 47.144 25.961 1.00 33.06 ATOM 412 O LEU A 84 42.730 46.424 25.914 1.00 34.52 ATOM 413 N GLY A 85 41.602 48.154 26.819 1.00 33.14 ATOM 414 CA GLY A 85 42.655 48.469 27.774 1.00 31.49 ATOM 415 C GLY A 85 43.893 49.069 27.133 1.00 31.37 ATOM 416 0 GLY A 85 44.996 48.980 27.680 1.00 29.38 ATOM 417 N HIS A 86 43.713 49.691 25.972 1.00 30.74 ATOM 418 CA HIS A 86 44.827 50.294 25.255 1.00 31.19 ATOM 419 CB HIS A 86 45.421 49.287 24.261 1.00 33.63 ATOM 420 CG HIS A 86 45.956 48.046 24.903 1.00 36.97 ATOM 421 CD2 HIS A 86 45.488 46.775 24.913 1.00 38.23

ATOM 422 ND1 HIS A 86 47.100 48. 039 25.672 1.00 38.35 ATOM 423 CE1 HIS A 86 47.313 46.817 26.130 1.00 38.39 ATOM 424 NE2 HIS A 86 46.349 46.031 25.685 1.00 40.10 ATOM 425 C HIS A 86 44.442 51.556 24.493 1.00 30.01 ATOM 426 0 HIS A 86 43.268 51.837 24.249 1.00 29.30 ATOM 427 N LYS A 87 45.459 52.315 24.116 1.00 29.25 ATOM 428 CA LYS A 87 45.266 53.528 23.350 1.00 28.62 ATOM 429 CB LYS A 87 46.126 54.656 23.921 1.00 31.36 ATOM 430 CG LYS A 87 46.098 55.934 23.105 1.00 36.49 ATOM 431 CD LYS A 87 47.040 56.982 23.680 1.00 40.20 ATOM 432 CE LYS A 87 48.488 56.523 23.617 1.00 42.08 ATOM 433 NZ LYS A 87 49.419 57.556 24.157 1.00 44.04 ATOM 434 C LYS A 87 45.710 53.205 21.928 1.00 26.31 ATOM 435 0 LYS A 87 46.727 52.532 21.729 1.00 25.00 ATOM 436 N PHE A 88 44.932 53.655 20.948 1.00 22.41 ATOM 437 CA PHE A 88 45.260 53.440 19.543 1.00 21.20 ATOM 438 CB PHE A 88 44.160 52.635 18.839 1.00 18.24 ATOM 439 CG PHE A 88 43.981 51.235 19.369 1.00 17.32 ATOM 440 CD1 PHE A 88 43.462 51.014 20.637 1.00 15.98 ATOM 441 CD2 PHE A 88 44.315 50.139 18.588 1.00 14.22 ATOM 442 CE1 PHE A 88 43.277 49.730 21.114 1.00 15.75 ATOM 443 CE2 PHE A 88 44.134 48.857 19.057 1.00 14.62 ATOM 444 CZ PHE A 88 43.614 48.649 20.321 1.00 16.23 ATOM 445 C PHE A 88 45.359 54.828 18.912 1.00 21.47 ATOM 446 0 PHE A 88 44.371 55.563 18.897 1.00 21.28 ATOM 447 N ARG A 89 46.531 55.195 18.395 1.00 21.89 ATOM 448 CA ARG A 89 46.683 56.522 17.797 1.00 24.22 ATOM 449 CB ARG A 89 48.145 56.814 17.437 1.00 27.64 ATOM 450 CG ARG A 89 48.743 55.954 16.360 1.00 34.35 ATOM 451 CD ARG A 89 50.110 56.502 15.978 1.00 39.78 ATOM 452 NE ARG A 89 50.936 56.747 17.157 1.00 43.12 ATOM 453 CZ ARG A 89 52.226 57.066 17.115 1.00 45.70 ATOM 454 NH1 ARG A 89 52.846 57.180 15.946 1.00 46.09 ATOM 455 NH2 ARG A 89 52.898 57.264 18.242 1.00 46.23 ATOM 456 C ARG A 89 45.774 56.724 16.586 1.00 21.57 ATOM 457 O ARG A 89 45.382 57.846 16.289 1.00 20.90 ATOM 458 N ASN A 90 45.461 55.644 15.878 1.00 19.52

ATOM 459 CA ASN A 90 44.525 55.712 14.756 1.00 19.26 ATOM 460 CB ASN A 90 45.227 56.049 13.419 1.00 17.47 ATOM 461 CG ASN A 90 45.921 54. 873 12.783 1.00 17.14 ATOM 462 OD1 ASN A 90 45.286 53.893 12.402 1.00 19.02 ATOM 463 ND2 ASN A 90 47.239 54.973 12.641 1.00 18.11 ATOM 464 C ASN A 90 43.816 54.359 14.759 1.00 18.80 ATOM 465 0 ASN A 90 44.381 53.354 15.198 1.00 20.27 ATOM 466 N PRO A 91 42.558 54.323 14.304 1.00 17.37 ATOM 467 CD PRO A 91 41.808 55.489 13.797 1.00 17.95 ATOM 468 CA PRO A 91 41.725 53.119 14.258 1.00 16.60 ATOM 469 CB PRO A 91 40.323 53.702 14.336 1.00 17.12 ATOM 470 CG PRO A 91 40.447 54.890 13.434 1.00 14.17 ATOM 471 C PRO A 91 41.876 52.188 13.062 1.00 17.11 ATOM 472 0 PRO A 91 41.084 51.260 12.903 1.00 16.80 ATOM 473 N VAL A 92 42.885 52.423 12.230 1.00 17.06 ATOM 474 CA VAL A 92 43.085 51.606 11.034 1.00 17.33 ATOM 475 CB VAL A 92 43.397 52.506 9.813 1.00 17.14 ATOM 476 CG1 VAL A 92 43.517 51.672 8.551 1.00 13.98 ATOM 477 CG2 VAL A 92 42.314 53.559 9.666 1.00 16. 18 ATOM 478 C VAL A 92 44.204 50.584 11.201 1.00 17.94 ATOM 479 0 VAL A 92 45.376 50.942 11.278 1.00 18.09 ATOM 480 N GLY A 93 43.836 49.308 11.251 1.00 17.48 ATOM 481 CA GLY A 93 44.833 48.270 11.410 1.00 16.24 ATOM 482 C GLY A 93 44.900 47.330 10.227 1.00 16.29 ATOM 483 0 GLY A 93 44.035 47.356 9.355 1.00 17.30 ATOM 484 N ILE A 94 45.947 46.512 10.185 1.00 15.88 ATOM 485 CA ILE A 94 46.113 45.536 9.114 1.00 13.94 ATOM 486 CB ILE A 94 47.612 45.320 8.770 1.00 14.90 ATOM 487 CG2 ILE A 94 48.408 44.996 10.024 1.00 13.27 ATOM 488 CG1 ILE A 94 47.756 44.209 7.726 1.00 14.95 ATOM 489 CD1 ILE A 94 47.281 44.608 6.336 1.00 14.84 ATOM 490 C ILE A 94 45.492 44.227 9.603 1.00 14.64 ATOM 491 0 ILE A 94 45.872 43.698 10.647 1.00 14.21 ATOM 492 N ALA A 95 44.520 43.717 8.856 1.00 14.20 ATOM 493 CA ALA A 95 43.840 42.487 9.233 1.00 14.41 ATOM 494 CB ALA A 95 42.675 42.227 8.279 1.00 14.00 ATOM 495 C ALA A 95 44.778 41.282 9.255 1.00 14.74

ATOM 496 0 ALA A 95 45.885 41.333 8.724 1.00 13.48 ATOM 497 N ALA A 96 44.327 40.204 9.887 1.00 13.92 ATOM 498 CA ALA A 96 45.111 38. 982 9.964 1.00 16.74 ATOM 499 CB ALA A 96 44.417 37.967 10.867 1.00 15.50 ATOM 500 C ALA A 96 45.254 38.415 8.557 1.00 17.13 ATOM 501 O ALA A 96 44.393 38.634 7.703 1.00 18.95 ATOM 502 N GLY A 97 46.343 37.695 8.312 1.00 17.82 ATOM 503 CA GLY A 97 46.546 37.112 6.999 1.00 16.65 ATOM 504 C GLY A 97 47.708 37.683 6.212 1.00 15.52 ATOM 505 0 GLY A 97 48.423 36.936 5.553 1.00 16.01 ATOM 506 N PHE A 98 47.903 38.998 6.255 1.00 15.36 ATOM 507 CA PHE A 98 49.014 39.583 5.515 1.00 16.42 ATOM 508 CB PHE A 98 48.962 41.112 5.519 1.00 16.50 ATOM 509 CG PHE A 98 50.095 41.739 4.761 1.00 18.21 ATOM 510 CD1 PHE A 98 50.149 41.650 3.376 1.00 19.68 ATOM 511 CD2 PHE A 98 51.140 42.355 5.431 1.00 18.88 ATOM 512 CE1 PHE A 98 51.225 42.159 2.674 1.00 19.14 ATOM 513 CE2 PHE A 98 52.223 42.868 4.735 1.00 19.22 ATOM 514 CZ PHE A 98 52.266 42.770 3.355 1.00 20.69 ATOM 515 C PHE A 98 50.325 39.129 6.149 1.00 15.73 ATOM 516 0 PHE A 98 51.219 38.636 5.467 1.00 15.56 ATOM 517 N ASP A 99 50.434 39.312 7.459 1.00 15.88 ATOM 518 CA ASP A 99 51.627 38.898 8.193 1.00 15.70 ATOM 519 CB ASP A 99 52.156 40.068 9.025 1.00 15.27 ATOM 520 CG ASP A 99 53.534 39.800 9.607 1.00 17.99 ATOM 521 OD1 ASP A 99 54.160 38.786 9.234 1.00 16.77 ATOM 522 OD2 ASP A 99 53.996 40.616 10.432 1.00 19.28 ATOM 523 C ASP A 99 51.233 37.723 9.096 1.00 16.32 ATOM 524 O ASP A 99 51.003 37.891 10.295 1.00 14.93 ATOM 525 N LYS A 100 51.138 36.538 8.498 1.00 16.61 ATOM 526 CA LYS A 100 50.756 35.330 9.220 1.00 17.25 ATOM 527 CB LYS A 100 50.490 34.187 8.231 1.00 19.41 ATOM 528 CG LYS A 100 49.159 34.247 7. 483 1.00 20. 97 ATOM 529 CD LYS A 100 49.092 33.131 6.437 1.00 23.93 ATOM 530 CE LYS A 100 47.732 33.042 5.730 1.00 25.43 ATOM 531 NZ LYS A 100 46.656 32.457 6.595 1.00 22.86 ATOM 532 C LYS A 100 51.774 34.848 10.253 1.00 18.16

ATOM 533 O LYS A 100 51.398 34.268 11.274 1.00 18.89 ATOM 534 N HIS A 101 53.058 35.084 10.000 1.00 17.48 ATOM 535 CA HIS A 101 54.095 34.603 10.911 1.00 19.25 ATOM 536 CB HIS A 101 55.114 33.779 10.118 1.00 16.89 ATOM 537 CG HIS A 101 54.516 33.041 8.961 1.00 18.72 ATOM 538 CD2 HIS A 101 54.771 33.111 7.632 1.00 17.76 ATOM 539 ND1 HIS A 101 53.504 32.115 9.108 1.00 18.28 ATOM 540 CE1 HIS A 101 53.162 31.648 7.920 1.00 17.69 ATOM 541 NE2 HIS A 101 53.916 32.235 7.007 1.00 16.65 ATOM 542 C HIS A 101 54.826 35.679 11.712 1.00 19.41 ATOM 543 0 HIS A 101 55.871 35.407 12.296 1.00 21.11 ATOM 544 N GLY A 102 54.281 36.892 11.736 1.00 20.30 ATOM 545 CA GLY A 102 54.904 37.977 12.478 1.00 20.25 ATOM 546 C GLY A 102 56.284 38.376 11.984 1.00 20.48 ATOM 547 0 GLY A 102 57.188 38.599 12.781 1.00 21.67 ATOM 548 N GLU A 103 56.445 38.491 10.670 1.00 22.35 ATOM 549 CA GLU A 103 57.732 38.855 10.076 1.00 21.64 ATOM 550 CB GLU A 103 57.964 38.041 8.804 1.00 20.45 ATOM 551 CG GLU A 103 58.008 36.546 9.009 1.00 23.87 ATOM 552 CD GLU A 103 58.054 35.792 7.697 1.00 26.38 ATOM 553 OE1 GLU A 103 57.019 35.749 6.993 1.00 26.70 ATOM 554 OE2 GLU A 103 59.130 35.251 7.365 1.00 28.54 ATOM 555 C GLU A 103 57.884 40.329 9.719 1.00 21.18 ATOM 556 0 GLU A 103 58.997 40.797 9.493 1.00 22.35 ATOM 557 N ALA A 104 56.782 41.067 9.665 1.00 20.64 ATOM 558 CA ALA A 104 56.858 42.471 9.274 1.00 19.54 ATOM 559 CB ALA A 104 56.348 42.618 7.851 1.00 16.12 ATOM 560 C ALA A 104 56.111 43.435 10.181 1.00 19.23 ATOM 561 O ALA A 104 55.690 44.502 9.741 1.00 18.91 ATOM 562 N VAL A 105 55.955 43.074 11.446 1.00 19.88 ATOM 563 CA VAL A 105 55.231 43.924 12.384 1.00 19.66 ATOM 564 CB VAL A 105 55.361 43.389 13.814 1.00 19.24 ATOM 565 CG1 VAL A 105 54.667 44.328 14.781 1.00 18.21 ATOM 566 CG2 VAL A 105 54.767 41.990 13.892 1.00 17.39 ATOM 567 C VAL A 105 55.669 45.389 12.372 1.00 20.45 ATOM 568 O VAL A 105 54.836 46.294 12.292 1.00 21.75 ATOM 569 N ASP A 106 56.974 45.622 12.444 1.00 18.45

ATOM 570 CA ASP A 106 57.493 46.984 12.467 1.00 19.17 ATOM 571 CB ASP A 106 58.967 46.970 12.880 1.00 18.60 ATOM 572 CG ASP A 106 59.154 46.476 14.297 1.00 19.83 ATOM 573 OD1 ASP A 106 59.731 45.382 14.485 1.00 21.21 ATOM 574 OD2 ASP A 106 58.701 47.179 15.225 1.00 19.11 ATOM 575 C ASP A 106 57.313 47.739 11. 159 1.00 18.26 ATOM 576 O ASP A 106 57.040 48.941 11.164 1.00 18.22 ATOM 577 N GLY A 107 57.468 47.039 10.043 1.00 16.23 ATOM 578 CA GLY A 107 57.288 47.677 8.755 1.00 17.23 ATOM 579 C GLY A 107 55.832 48.061 8.554 1.00 18.78 ATOM 580 O GLY A 107 55.521 48.958 7.770 1.00 20.34 ATOM 581 N LEU A 108 54.934 47.383 9.267 1.00 17.72 ATOM 582 CA LEU A 108 53.507 47.668 9.166 1.00 17.68 ATOM 583 CB LEU A 108 52.690 46.463 9.650 1.00 18.56 ATOM 584 CG LEU A 108 52.748 45.288 8.665 1.00 17.20 ATOM 585 CD1 LEU A 108 52.205 44.023 9.300 1.00 15.49 ATOM 586 CD2 LEU A 108 51.964 45.654 7.413 1.00 18.33 ATOM 587 C LEU A 108 53.140 48.930 9.943 1.00 17.62 ATOM 588 O LEU A 108 52.320 49.718 9.482 1.00 17.86 ATOM 589 N TYR A 109 53.734 49.127 11.118 1.00 17.88 ATOM 590 CA TYR A 109 53.464 50.347 11.883 1.00 19.37 ATOM 591 CB TYR A 109 54.179 50.335 13.246 1.00 17.43 ATOM 592 CG TYR A 109 53.573 49.401 14.273 1.00 15.80 ATOM 593 CD1 TYR A 109 54.324 48.381 14.840 1.00 14.92 ATOM 594 CE1 TYR A 109 53.767 47.507 15.760 1.00 16.08 ATOM 595 CD2 TYR A 109 52.243 49.529 14.660 1.00 14.37 ATOM 596 CE2 TYR A 109 51.677 48.663 15.580 1.00 14.70 ATOM 597 CZ TYR A 109 52.443 47.651 16.125 1.00 15.77 ATOM 598 OH TYR A 109 51.880 46.769 17.019 1.00 15.33 ATOM 599 C TYR A 109 54.006 51. 509 11.053 1.00 20.25 ATOM 600 0 TYR A 109 53.430 52.598 11.023 1.00 20.30 ATOM 601 N LYS A 110 55.125 51.265 10.378 1.00 20.12 ATOM 602 CA LYS A 110 55.747 52.287 9.551 1.00 22.39 ATOM 603 CB LYS A 110 57.123 51.821 9.074 1.00 23.00 ATOM 604 CG LYS A 110 57.804 52.825 8.169 1.00 26.93 ATOM 605 CD LYS A 110 59.140 52.328 7.667 1.00 31.08 ATOM 606 CE LYS A 110 59.795 53.371 6.769 1.00 33.97

ATOM 607 NZ LYS A 110 61.123 52.922 6.263 1.00 37.79 ATOM 608 C LYS A 110 54.880 52.635 8.342 1.00 22.91 ATOM 609 O LYS A 110 55.002 53.722 7.772 1.00 21.83 ATOM 610 N MET A 111 54. 009 51.706 7.955 1.00 22.68 ATOM 611 CA MET A 111 53.123 51.912 6.814 1.00 21.52 ATOM 612 CB MET A 111 52.576 50.565 6.331 1.00 22.57 ATOM 613 CG MET A 111 52.097 50.560 4.885 1.00 23.41 ATOM 614 SD MET A 111 51.657 48.907 4.289 1.00 22.54 ATOM 615 CE MET A 111 53.262 48.165 4.105 1.00 21.48 ATOM 616 C MET A 111 51.976 52.850 7.201 1.00 21.63 ATOM 617 0 MET A 111 51.250 53.352 6.341 1.00 21.82 ATOM 618 N GLY A 112 51.817 53.084 8.500 1.00 20.62 ATOM 619 CA GLY A 112 50.768 53.980 8.955 1.00 18.24 ATOM 620 C GLY A 112 49.644 53.347 9.752 1.00 17.64 ATOM 621 O GLY A 112 48.736 54.048 10.198 1.00 18.17 ATOM 622 N PHE A 113 49.691 52.032 9.941 1.00 16.29 ATOM 623 CA PHE A 113 48.644 51.344 10.693 1.00 15.85 ATOM 624 CB PHE A 113 48.769 49.829 10.520 1.00 15.16 ATOM 625 CG PHE A 113 48.390 49.346 9.153 1.00 15.73 ATOM 626 CD1 PHE A 113 49.355 48.898 8.269 1.00 15.73 ATOM 627 CD2 PHE A 113 47.062 49.334 8.755 1.00 15.52 ATOM 628 CE1 PHE A 113 49.003 48.442 7.007 1.00 18.04 ATOM 629 CE2 PHE A 113 46.699 48.881 7.498 1.00 15.62 ATOM 630 CZ PHE A 113 47.669 48.433 6.621 1.00 17.05 ATOM 631 C PHE A 113 48.662 51.690 12.175 1.00 14.70 ATOM 632 0 PHE A 113 49.722 51.759 12.788 1.00 15.50 ATOM 633 N GLY A 114 47.477 51.911 12.738 1.00 13.84 ATOM 634 CA GLY A 114 47.361 52.248 14.148 1.00 13.69 ATOM 635 C GLY A 114 47.578 51.041 15.042 1.00 14.92 ATOM 636 0 GLY A 114 47.813 51.174 16.240 1.00 16.13 ATOM 637 N PHE A 115 47.470 49.852 14.463 1.00 15.20 ATOM 638 CA PHE A 115 47.690 48.624 15.209 1.00 15.32 ATOM 639 CB PHE A 115 46.547 48.364 16.206 1.00 15.74 ATOM 640 CG PHE A 115 45.214 48.071 15.575 1.00 14.70 ATOM 641 CD1 PHE A 115 44.715 46.778 15.553 1.00 14.33 ATOM 642 CD2 PHE A 115 44.430 49.095 15.061 1.00 14.87 ATOM 643 CE1 PHE A 115 43.456 46.507 15.034 1.00 13.48

ATOM 644 CE2 PHE A 115 43.170 48.831 14.539 1.00 15.39 ATOM 645 CZ PHE A 115 42.684 47.533 14.528 1.00 14.35 ATOM 646 C PHE A 115 47.871 47.464 14.247 1.00 15.52 ATOM 647 0 PHE A 115 47.350 47.481 13.136 1.00 15.04 ATOM 648 N VAL A 116 48.638 46.468 14.675 1.00 16.15 ATOM 649 CA VAL A 116 48.931 45.311 13.845 1.00 14.61 ATOM 650 CB VAL A 116 50.464 45.183 13.615 1.00 15.46 ATOM 651 CG1 VAL A 116 50.782 43.920 12. 803 1.00 10.90 ATOM 652 CG2 VAL A 116 50.991 46.434 12.912 1.00 12.53 ATOM 653 C VAL A 116 48.431 44.006 14.448 1.00 15.98 ATOM 654 0 VAL A 116 48.469 43.817 15.664 1.00 16.18 ATOM 655 N GLU A 117 47.955 43. 113 13.584 1.00 15.89 ATOM 656 CA GLU A 117 47.490 41.796 14.009 1.00 17.58 ATOM 657 CB GLU A 117 45.977 41.668 13.845 1.00 16.28 ATOM 658 CG GLU A 117 45.442 40.307 14.263 1.00 16.44 ATOM 659 CD GLU A 117 43.929 40.257 14.255 1.00 17.58 ATOM 660 OE1 GLU A 117 43.366 39.304 13.671 1.00 16.31 ATOM 661 OE2 GLU A 117 43.309 41.173 14.837 1.00 14.25 ATOM 662 C GLU A 117 48.190 40.782 13.115 1.00 17.75 ATOM 663 0 GLU A 117 48.077 40.853 11.892 1.00 19.22 ATOM 664 N ILE A 118 48.917 39.840 13.706 1.00 17.57 ATOM 665 CA ILE A 118 49.619 38.870 12.882 1.00 20.33 ATOM 666 CB ILE A 118 50.981 38.473 13.503 1.00 18.22 ATOM 667 CG2 ILE A 118 51.869 39.704 13.594 1.00 20.47 ATOM 668 CG1 ILE A 118 50.801 37.879 14.893 1.00 18.20 ATOM 669 CD1 ILE A 118 52.101 37.437 15.500 1.00 18.29 ATOM 670 C ILE A 118 48.777 37.643 12. 566 1.00 21.46 ATOM 671 0 ILE A 118 48.183 37.032 13.453 1.00 18. 99 ATOM 672 N GLY A 119 48.729 37.336 11.266 1.00 26.74 ATOM 673 CA GLY A 119 47.955 36.234 10.707 1.00 23.10 ATOM 674 C GLY A 119 47.785 35.068 11.633 1.00 24.55 ATOM 675 0 GLY A 119 48.548 34.923 12.591 1.00 25.31 ATOM 676 N SER A 120 46.793 34.229 11.345 1.00 21.80 ATOM 677 CA SER A 120 46.529 33.069 12.185 1.00 20.39 ATOM 678 CB SER A 120 45.371 32.243 11.623 1.00 19.81 ATOM 679 OG SER A 120 44.128 32.878 11.874 1.00 18.88 ATOM 680 C SER A 120 47.750 32.187 12.352 1.00 19. 19

ATOM 681 0 SER A 120 48.453 31.881 11.389 1.00 19.54 ATOM 682 N VAL A 121 47.992 31.785 13.594 1.00 18.84 ATOM 683 CA VAL A 121 49.115 30.924 13.936 1.00 15.63 ATOM 684 CB VAL A 121 50.007 31. 580 15.023 1.00 15.71 ATOM 685 CG1 VAL A 121 51.322 30.801 15.174 1.00 10.48 ATOM 686 CG2 VAL A 121 50.268 33.045 14.670 1.00 12.14 ATOM 687 C VAL A 121 48.538 29.622 14.488 1.00 16.66 ATOM 688 0 VAL A 121 47.610 29.641 15.302 1.00 15.77 ATOM 689 N THR A 122 49.071 28.496 14.028 1.00 15.22 ATOM 690 CA THR A 122 48.619 27.192 14.493 1.00 16.76 ATOM 691 CB THR A 122 48.448 26.211 13.304 1.00 15.90 ATOM 692 OG1 THR A 122 49.666 26.132 12.557 1.00 16.51 ATOM 693 CG2 THR A 122 47.343 26.693 12.378 1.00 16.10 ATOM 694 C THR A 122 49.668 26.677 15.480 1.00 16.25 ATOM 695 O THR A 122 50.814 27.112 15.443 1.00 17.59 ATOM 696 N PRO A 123 49.285 25.770 16.393 1.00 17.47 ATOM 697 CD PRO A 123 47.920 25.301 16.691 1.00 16.85 ATOM 698 CA PRO A 123 50.244 25.236 17.373 1.00 18.92 ATOM 699 CB PRO A 123 49.420 24.203 18.128 1.00 17.69 ATOM 700 CG PRO A 123 48.052 24.841 18.132 1.00 17.76 ATOM 701 C PRO A 123 51.499 24.642 16.736 1.00 20.99 ATOM 702 O PRO A 123 52.621 25.028 17.074 1.00 21.78 ATOM 703 N LYS A 124 51.305 23.701 15.819 1.00 21.75 ATOM 704 CA LYS A 124 52.420 23.079 15.119 1.00 23.14 ATOM 705 CB LYS A 124 52.202 21.563 14.973 1.00 25.62 ATOM 706 CG LYS A 124 51.920 20.840 16.279 1.00 30.22 ATOM 707 CD LYS A 124 52.985 21.160 17.320 1.00 36.14 ATOM 708 CE LYS A 124 52.562 20.694 18.707 1.00 40.67 ATOM 709 NZ LYS A 124 53.568 21.045 19.751 1.00 42.17 ATOM 710 C LYS A 124 52.488 23.707 13.736 1.00 23.21 ATOM 711 0 LYS A 124 51.504 24.267 13.245 1.00 23.64 ATOM 712 N PRO A 125 53.660 23.644 13.095 1.00 21.67 ATOM 713 CD PRO A 125 54.966 23.207 13.623 1.00 21.13 ATOM 714 CA PRO A 125 53.790 24.220 11.756 1.00 20.12 ATOM 715 CB PRO A 125 55.292 24.112 11.473 1.00 20.06 ATOM 716 CG PRO A 125 55.924 24.057 12.844 1.00 19.41 ATOM 717 C PRO A 125 52.976 23.368 10.775 1.00 20.04

ATOM 718 0 PRO A 125 52.738 22.187 11.024 1.00 19.30 ATOM 719 N GLN A 126 52.536 23.965 9.674 1.00 19.35 ATOM 720 CA GLN A 126 51.801 23. 229 8.650 1.00 20.20 ATOM 721 CB GLN A 126 50.352 22.926 9.078 1.00 21.37 ATOM 722 CG GLN A 126 49.441 24. 118 9.337 1.00 20.47 ATOM 723 CD GLN A 126 47.993 23.689 9.578 1.00 21.76 ATOM 724 OE1 GLN A 126 47.725 22.742 10.330 1.00 19.13 ATOM 725 NE2 GLN A 126 47.056 24.391 8.949 1.00 19.73 ATOM 726 C GLN A 126 51.844 24.027 7.357 1.00 20.40 ATOM 727 0 GLN A 126 51.827 25.255 7.375 1.00 20.14 ATOM 728 N GLU A 127 51.914 23.323 6.234 1.00 22.71 ATOM 729 CA GLU A 127 52.018 23.970 4.933 1.00 26.01 ATOM 730 CB GLU A 127 52.622 22.989 3.922 1.00 29.64 ATOM 731 CG GLU A 127 53.987 22.463 4.345 1.00 37.72 ATOM 732 CD GLU A 127 54.735 21.770 3.220 1.00 43.15 ATOM 733 OE1 GLU A 127 54.150 20.871 2.574 1.00 46.06 ATOM 734 OE2 GLU A 127 55.914 22.120 2.986 1.00 45.97 ATOM 735 C GLU A 127 50.752 24.584 4.352 1.00 24.16 ATOM 736 O GLU A 127 50.832 25.468 3.503 1.00 22.80 ATOM 737 N GLY A 128 49.589 24.133 4.805 1.00 23.12 ATOM 738 CA GLY A 128 48.353 24.669 4.267 1.00 23.32 ATOM 739 C GLY A 128 48.007 23.957 2.972 1.00 25.32 ATOM 740 0 GLY A 128 48.637 22.951 2.629 1.00 24.84 ATOM 741 N ASN A 129 47.013 24.465 2.247 1.00 25.42 ATOM 742 CA ASN A 129 46.602 23.847 0.992 1.00 25.80 ATOM 743 CB ASN A 129 45.256 24.411 0.530 1.00 24.97 ATOM 744 CG ASN A 129 44.122 24.051 1.466 1.00 25.95 ATOM 745 OD1 ASN A 129 44.069 22.938 1.988 1.00 27.09 ATOM 746 ND2 ASN A 129 43.198 24.985 1.670 1.00 21.37 ATOM 747 C ASN A 129 47.631 24.031-0. 118 1.00 26.37 ATOM 748 0 ASN A 129 48.474 24.927-0. 065 1.00 25.71 ATOM 749 N PRO A 130 47.577 23.167-1. 141 1.00 26.97 ATOM 750 CD PRO A 130 46.708 21.978-1. 222 1.00 25.53 ATOM 751 CA PRO A 130 48.501 23.228-2. 279 1.00 27.02 ATOM 752 CB PRO A 130 48.271 21.888-2. 979 1.00 26.16 ATOM 753 CG PRO A 130 46.835 21.584-2. 672 1.00 25.45 ATOM 754 C PRO A 130 48.213 24.422-3. 188 1.00 28.78

ATOM 755 0 PRO A 130 47.072 24.874-3. 278 1.00 29.43 ATOM 756 N ARG A 131 49.250 24. 933-3. 849 1.00 29.59 ATOM 757 CA ARG A 131 49.113 26.073-4. 754 1.00 31.09 ATOM 758 CB ARG A 131 50.475 26.715-5. 026 1.00 32.79 ATOM 759 CG ARG A 131 51.191 27.347-3. 841 1.00 35.14 ATOM 760 CD ARG A 131 52.247 28.306-4. 389 1.00 40.85 ATOM 761 NE ARG A 131 53.156 28.865-3. 389 1.00 45. 50 ATOM 762 CZ ARG A 131 53.991 29.877-3. 630 1.00 45.91 ATOM 763 NH1 ARG A 131 54.024 30.440-4. 834 1.00 44.20 ATOM 764 NH2 ARG A 131 54.801 30.322-2. 676 1.00 45.31 ATOM 765 C ARG A 131 48.517 25.640-6. 096 1.00 31.92 ATOM 766 0 ARG A 131 48.732 24.516-6. 542 1.00 33.62 ATOM 767 N PRO A 132 47.764 26.533-6. 762 1.00 30.70 ATOM 768 CD PRO A 132 47.273 26.311-8. 134 1.00 31.37 ATOM 769 CA PRO A 132 47.455 27.896-6. 321 1.00 28.34 ATOM 770 CB PRO A 132 47.035 28.583-7. 617 1.00 28.99 ATOM 771 CG PRO A 132 46.335 27.486-8. 341 1.00 30.32 ATOM 772 C PRO A 132 46.350 27.900-5. 265 1.00 24.58 ATOM 773 0 PRO A 132 45.461 27.052-5. 282 1.00 22.71 ATOM 774 N ARG A 133 46.411 28.860-4. 350 1.00 21.45 ATOM 775 CA ARG A 133 45.426 28.948-3. 288 1.00 19.40 ATOM 776 CB ARG A 133 46.003 28.314-2. 020 1.00 20.88 ATOM 777 CG ARG A 133 47.407 28.788-1. 693 1.00 18.79 ATOM 778 CD ARG A 133 48.079 27.880-0. 680 1.00 16.96 ATOM 779 NE ARG A 133 49.405 28.380-0. 333 1.00 17.39 ATOM 780 CZ ARG A 133 50.178 27.861 0.614 1.00 15.76 ATOM 781 NH1 ARG A 133 51.367 28.387 0.862 1.00 13.75 ATOM 782 NH2 ARG A 133 49.761 26.816 1.311 1.00 15.94 ATOM 783 C ARG A 133 44.959 30.377-3. 019 1.00 19.15 ATOM 784 0 ARG A 133 44.253 30.634-2. 044 1.00 18.90 ATOM 785 N VAL A 134 45.360 31.304-3. 884 1.00 18.67 ATOM 786 CA VAL A 134 44.954 32.702-3. 768 1.00 19.00 ATOM 787 CB VAL A 134 46.082 33.609-3. 230 1.00 19.66 ATOM 788 CG1 VAL A 134 45.482 34.904-2. 693 1.00 16.74 ATOM 789 CG2 VAL A 134 46.868 32.889-2. 168 1.00 19.63 ATOM 790 C VAL A 134 44.621 33.162-5. 178 1.00 19.08 ATOM 791 0 VAL A 134 45.318 32.807-6. 124 1.00 19.65

ATOM 792 N PHE A 135 43.565 33.951-5. 324 1.00 19.21 ATOM 793 CA PHE A 135 43.165 34.409-6. 645 1.00 17.86 ATOM 794 CB PHE A 135 42.074 33.489-7. 198 1.00 17.21 ATOM 795 CG PHE A 135 42.393 32. 023-7. 056 1.00 17.38 ATOM 796 CD1 PHE A 135 42.116 31.349-5. 876 1.00 15.76 ATOM 797 CD2 PHE A 135 43.022 31.332-8. 087 1.00 18.52 ATOM 798 CE1 PHE A 135 42.462 30.012-5. 721 1.00 17.54 ATOM 799 CE2 PHE A 135 43.372 29.995-7. 941 1.00 16.71 ATOM 800 CZ PHE A 135 43.091 29.335-6. 756 1.00 16.55 ATOM 801 C PHE A 135 42.680 35.852-6. 650 1.00 18.55 ATOM 802 O PHE A 135 42.010 36.302-5. 718 1.00 17.50 ATOM 803 N ARG A 136 43.038 36.575-7. 705 1.00 17.21 ATOM 804 CA ARG A 136 42.634 37.960-7. 852 1.00 17.96 ATOM 805 CB ARG A 136 43.732 38.785-8. 532 1.00 19. 09 ATOM 806 CG ARG A 136 45.099 38.812-7. 862 1.00 21.38 ATOM 807 CD ARG A 136 46.005 39.773-8. 631 1.00 23.13 ATOM 808 NE ARG A 136 47.367 39.847-8. 108 1.00 28.99 ATOM 809 CZ ARG A 136 48.424 39.246-8. 653 1.00 30.96 ATOM 810 NH1 ARG A 136 49.621 39.379-8. 097 1.00 30. 96 ATOM 811 NH2 ARG A 136 48.291 38.516-9. 754 1.00 31.45 ATOM 812 C ARG A 136 41.382 38.045-8. 724 1.00 18.26 ATOM 813 0 ARG A 136 41.231 37.280-9. 684 1.00 18.07 ATOM 814 N LEU A 137 40.487 38.965-8. 366 1.00 16.02 ATOM 815 CA LEU A 137 39.264 39.245-9. 124 1.00 14.64 ATOM 816 CB LEU A 137 38.005 38.850-8. 348 1.00 14.99 ATOM 817 CG LEU A 137 37.568 37.381-8. 289 1.00 16.86 ATOM 818 CD1 LEU A 137 38.611 36.533-7. 567 1.00 16.16 ATOM 819 CD2 LEU A 137 36.234 37.302-7. 572 1.00 12.39 ATOM 820 C LEU A 137 39.312 40.762-9. 270 1.00 15.43 ATOM 821 0 LEU A 137 38.557 41.487-8. 619 1.00 13.75 ATOM 822 N PRO A 138 40.230 41.261-10. 114 1.00 15.66 ATOM 823 CD PRO A 138 41.182 40.481-10. 927 1.00 15.43 ATOM 824 CA PRO A 138 40.389 42.701-10. 339 1.00 16.74 ATOM 825 CB PRO A 138 41.536 42.776-11. 359 1.00 16.03 ATOM 826 CG PRO A 138 41.505 41.426-12. 042 1.00 16. 02 ATOM 827 C PRO A 138 39.133 43.455-10. 778 1.00 16.37 ATOM 828 0 PRO A 138 38. 947 44.611-10. 407 1.00 17. 51

ATOM 829 N GLU A 139 38.267 42.812-11. 551 1.00 16.27 ATOM 830 CA GLU A 139 37.044 43. 478-11. 988 1.00 17.29 ATOM 831 CB GLU A 139 36.312 42. 646-13. 049 1.00 17.90 ATOM 832 CG GLU A 139 37.056 42.476-14. 371 1.00 21.52 ATOM 833 CD GLU A 139 38.072 41.341-14. 353 1.00 24.56 ATOM 834 OE1 GLU A 139 38.733 41.139-15. 393 1.00 28.04 ATOM 835 OE2 GLU A 139 38.211 40.652-13. 314 1.00 23.31 ATOM 836 C GLU A 139 36.097 43.717-10. 811 1.00 17.97 ATOM 837 0 GLU A 139 35.181 44.538-10. 899 1.00 18.18 ATOM 838 N ASP A 140 36.317 43.000-9. 712 1.00 15.32 ATOM 839 CA ASP A 140 35.462 43.125-8. 535 1.00 13.52 ATOM 840 CB ASP A 140 34.958 41.745-8. 099 1.00 11.56 ATOM 841 CG ASP A 140 34.317 40.965-9. 235 1.00 14.42 ATOM 842 OD1 ASP A 140 33.256 41.394-9. 737 1.00 12.89 ATOM 843 OD2 ASP A 140 34.875 39.916-9. 626 1.00 14.92 ATOM 844 C ASP A 140 36.205 43.756-7. 368 1.00 14.63 ATOM 845 O ASP A 140 35.629 43.958-6. 292 1.00 13.69 ATOM 846 N GLN A 141 37.480 44.071-7. 580 1.00 15.16 ATOM 847 CA GLN A 141 38.302 44.629-6. 516 1.00 15.06 ATOM 848 CB GLN A 141 37.812 46.028-6. 139 1.00 16.60 ATOM 849 CG GLN A 141 38.184 47.085-7. 174 1.00 23.33 ATOM 850 CD GLN A 141 37.655 48.473-6. 843 1.00 25.68 ATOM 851 OE1 GLN A 141 37.850 48.983-5. 734 1.00 29.01 ATOM 852 NE2 GLN A 141 36.991 49.098-7. 812 1.00 26.01 ATOM 853 C GLN A 141 38.179 43.665-5. 340 1.00 14.75 ATOM 854 0 GLN A 141 38.013 44.069-4. 187 1.00 15.25 ATOM 855 N ALA A 142 38.250 42.376-5. 660 1.00 13.65 ATOM 856 CA ALA A 142 38.140 41.322-4. 663 1.00 13.75 ATOM 857 CB ALA A 142 36.773 40.647-4. 773 1.00 11.94 ATOM 858 C ALA A 142 39.246 40.274-4. 793 1.00 13.78 ATOM 859 0 ALA A 142 39.999 40.248-5. 769 1.00 12.61 ATOM 860 N VAL A 143 39.326 39.411-3. 786 1.00 13.55 ATOM 861 CA VAL A 143 40.298 38.333-3. 743 1.00 12.13 ATOM 862 CB VAL A 143 41.522 38.688-2. 836 1.00 13.66 ATOM 863 CG1 VAL A 143 42.332 37.430-2. 521 1.00 9.03 ATOM 864 CG2 VAL A 143 42.419 39.713-3. 528 1.00 8.76 ATOM 865 C VAL A 143 39.604 37.110-3. 156 1.00 14.44

ATOM 866 O VAL A 143 38.669 37.234-2. 365 1.00 16.13 ATOM 867 N ILE A 144 40. 041 35.930-3. 574 1.00 14.55 ATOM 868 CA ILE A 144 39.507 34.683-3. 050 1.00 13.21 ATOM 869 CB ILE A 144 38.725 33.884-4. 116 1.00 13.83 ATOM 870 CG2 ILE A 144 38.563 32.426-3. 673 1.00 10.86 ATOM 871 CG1 ILE A 144 37.348 34.514-4. 329 1.00 11.70 ATOM 872 CD1 ILE A 144 36. 505 33.768-5. 324 1.00 14.85 ATOM 873 C ILE A 144 40.729 33.893-2. 627 1.00 14.02 ATOM 874 0ILE A 144 41.700 33.795-3. 382 1.00 14.77 ATOM 875 N ASN A 145 40.700 33.341-1. 421 1.00 14.01 ATOM 876 CA ASN A 145 41.841 32.575-0. 945 1.00 13.47 ATOM 877 CB ASN A 145 42.717 33.455-0. 046 1.00 13.34 ATOM 878 CG ASN A 145 42.256 33.451 1.407 1.00 16.62 ATOM 879 OD1 ASN A 145 42.562 32.525 2.161 1.00 14.82 ATOM 880 ND2 ASN A 145 41.507 34.481 1.801 1.00 15.48 ATOM 881 C ASN A 145 41.423 31.330-0. 176 1.00 14.78 ATOM 882 O ASN A 145 40.369 31.299 0.468 1.00 13.11 ATOM 883 NARG A 146 42. 258 30.300-0. 257 1.00 14.90 ATOM 884 CA ARG A 146 42.025 29.057 0.461 1.00 16.46 ATOM 885 CB ARG A 146 41.335 28.021-0. 435 1.00 15.83 ATOM 886 CG ARG A 146 41.964 27.806-1. 803 1.00 15.41 ATOM 887 CD ARG A 146 41.394 26.539-2. 428 1.00 16.11 ATOM 888 NE ARG A 146 41. 950 26.245-3. 747 1.00 16.55 ATOM 889 CZ ARG A 146 41.419 26.640-4. 902 1.00 17.12 ATOM 890 NH1 ARG A 146 40.303 27.357-4. 922 1.00 16.98 ATOM 891 NH2 ARG A 146 42.004 26.308-6. 045 1.00 19.03 ATOM 892 C ARG A 146 43.368 28.527 0.963 1.00 18.74 ATOM 893 0 ARG A 146 43.712 27.363 0.752 1.00 18.99 ATOM 894 N TYR A 147 44.122 29.401 1.630 1.00 18.17 ATOM 895 CA TYR A 147 45.429 29.043 2.165 1.00 18.86 ATOM 896 CB TYR A 147 46.020 30.205 2.964 1.00 18.76 ATOM 897 CG TYR A 147 46.884 31.127 2.146 1.00 18.93 ATOM 898 CD1 TYR A 147 46.428 32.377 1.754 1.00 19.69 ATOM 899 CE1 TYR A 147 47.220 33.216 0.987 1.00 22.27 ATOM 900 CD2 TYR A 147 48.160 30.736 1.748 1.00 20.18 ATOM 901 CE2 TYR A 147 48.958 31.565 0.981 1.00 21.33 ATOM 902 CZ TYR A 147 48.483 32.802 0.604 1.00 22.73

ATOM 903 OH TYR A 147 49.271 33.626-0. 164 1.00 28. 16 ATOM 904 C TYR A 147 45.393 27.806 3.047 1.00 19.56 ATOM 905 O TYR A 147 46.249 26.930 2.928 1.00 21.06 ATOM 906 N GLY A 148 44.408 27.746 3.937 1.00 19.63 ATOM 907 CA GLY A 148 44.280 26.611 4.831 1.00 17.88 ATOM 908 C GLY A 148 45.174 26.702 6.055 1.00 19.35 ATOM 909 O GLY A 148 45.677 25.687 6.538 1.00 20.24 ATOM 910 N PHE A 149 45.385 27.913 6.558 1.00 19.11 ATOM 911 CA PHE A 149 46.216 28.106 7.746 1.00 19.25 ATOM 912 CB PHE A 149 45.629 27.343 8.942 1.00 18.52 ATOM 913 CG PHE A 149 44.462 28.026 9.603 1.00 19.93 ATOM 914 CD1 PHE A 149 43.605 27. 308 10.431 1.00 21.48 ATOM 915 CD2 PHE A 149 44.224 29.377 9.415 1.00 20.70 ATOM 916 CE1 PHE A 149 42.530 27.928 11.058 1.00 22.80 ATOM 917 CE2 PHE A 149 43.151 30.005 10.039 1.00 21.90 ATOM 918 CZ PHE A 149 42.303 29.281 10.860 1.00 22.32 ATOM 919 C PHE A 149 47.674 27.677 7.577 1.00 19.22 ATOM 920 O PHE A 149 48.185 26.895 8.376 1.00 20.27 ATOM 921 N ASN A 150 48.343 28.155 6.536 1.00 17.52 ATOM 922 CA ASN A 150 49.748 27.822 6.375 1.00 18.34 ATOM 923 CB ASN A 150 50.269 28.307 5.018 1.00 16.68 ATOM 924 CG ASN A 150 49.967 29.769 4.765 1.00 18.37 ATOM 925 OD1 ASN A 150 48.819 30.205 4.866 1.00 18.33 ATOM 926 ND2 ASN A 150 50.996 30.536 4.423 1.00 17.29 ATOM 927 C ASN A 150 50.385 28.604 7.525 1.00 19.77 ATOM 928 O ASN A 150 50.135 29.800 7.673 1.00 20.24 ATOM 929 N SER A 151 51.185 27.936 8.349 1.00 18.05 ATOM 930 CA SER A 151 51.779 28.604 9.497 1.00 18.67 ATOM 931 CB SER A 151 50.774 28.580 10.654 1.00 17.61 ATOM 932 OG SER A 151 51.380 28.930 11.884 1.00 16.00 ATOM 933 C SER A 151 53.111 28.029 9.977 1.00 19.35 ATOM 934 0 SER A 151 53.329 26.812 9.940 1.00 18.88 ATOM 935 N HIS A 152 53.987 28.920 10.440 1.00 18.69 ATOM 936 CA HIS A 152 55.300 28.539 10.960 1.00 18.85 ATOM 937 CB HIS A 152 56.208 29.770 11.094 1.00 18.68 ATOM 938 CG HIS A 152 56.662 30.341 9.785 1.00 20.96 ATOM 939 CD2 HIS A 152 56.389 29.978 8.508 1.00 20.68

ATOM 940 ND1 HIS A 152 57.513 31.422 9.701 1.00 22.15 ATOM 941 CE1 HIS A 152 57.746 31.700 8.430 1.00 20.45 ATOM 942 NE2 HIS A 152 57.075 30.839 7.686 1.00 21.40 ATOM 943 C HIS A 152 55.154 27.875 12.329 1.00 18.49 ATOM 944 O HIS A 152 56.082 27.224 12. 815 1.00 17.98 ATOM 945 N GLY A 153 53.991 28.050 12.954 1.00 17.52 ATOM 946 CA GLY A 153 53.764 27.451 14.256 1.00 16.27 ATOM 947 C GLY A 153 54.047 28.392 15.412 1.00 15.14 ATOM 948 0 GLY A 153 54.711 29.411 15.248 1.00 13.16 ATOM 949 N LEU A 154 53.546 28.035 16.589 1.00 15.48 ATOM 950 CA LEU A 154 53.717 28.845 17.791 1.00 16.27 ATOM 951 CB LEU A 154 52.982 28.184 18.966 1.00 12.85 ATOM 952 CG LEU A 154 51.455 28.194 18.838 1.00 14. 19 ATOM 953 CD1 LEU A 154 50.811 27.354 19.940 1.00 9.42 ATOM 954 CD2 LEU A 154 50.965 29.638 18.898 1.00 11.87 ATOM 955 C LEU A 154 55.168 29.136 18.187 1.00 17.92 ATOM 956 0 LEU A 154 55.520 30.295 18.425 1.00 18.40 ATOM 957 N SER A 155 56.001 28.096 18.266 1.00 18.05 ATOM 958 CA SER A 155 57.408 28.268 18.647 1.00 19.71 ATOM 959 CB SER A 155 58.173 26.946 18.528 1.00 18.07 ATOM 960 OG SER A 155 57.775 26.035 19.528 1.00 26.58 ATOM 961 C SER A 155 58.143 29.319 17.820 1.00 19.87 ATOM 962 0 SER A 155 58.706 30.272 18.368 1.00 19.91 ATOM 963 N VAL A 156 58.158 29.134 16.503 1.00 18.27 ATOM 964 CA VAL A 156 58.846 30.077 15.637 1.00 19.17 ATOM 965 CB VAL A 156 58.723 29.672 14.153 1.00 19.48 ATOM 966 CG1 VAL A 156 59.158 30.829 13.264 1.00 18.32 ATOM 967 CG2 VAL A 156 59.597 28.452 13.880 1.00 15.72 ATOM 968 C VAL A 156 58.346 31.508 15.817 1.00 18.93 ATOM 969 0 VAL A 156 59.146 32.435 15.936 1.00 21.37 ATOM 970'N VAL A 157 57.030 31.691 15.848 1.00 17.16 ATOM 971 CA VAL A 157 56.470 33.027 16.013 1.00 17.31 ATOM 972 CB VAL A 157 54.936 33.021 15.790 1.00 18.26 ATOM 973 CG1 VAL A 157 54.368 34.417 16.001 1.00 15.69 ATOM 974 CG2 VAL A 157 54.620 32.532 14.380 1.00 15.91 ATOM 975 C VAL A 157 56.785 33.562 17.408 1.00 16.86 ATOM 976 0 VAL A 157 57.047 34.750 17.584 1.00 16.79

ATOM 977 N GLU A 158 56.771 32.670 18. 394 1.00 17.65 ATOM 978 CA GLU A 158 57.065 33.034 19.774 1.00 16.94 ATOM 979 CB GLU A158 57.009 31.790 20. 661 1.00 17.93 ATOM 980 CG GLU A 158 57.397 32.041 22.110 1.00 20.56 ATOM 981 CD GLU A 158 57.966 30.802 22.779 1.00 22.55 ATOM 982 OE1 GLU A 158 57.274 29.769 22.816 1.00 26.93 ATOM 983 OE2 GLU A 158 59.110 30.857 23.269 1.00 24.61 ATOM 984 C GLU A 158 58.449 33.675 19.887 1.00 16.25 ATOM 985 O GLU A 158 58.600 34.760 20.450 1.00 14.87 ATOM 986 N HIS A 159 59.458 33.000 19.350 1.00 15.71 ATOM 987 CA HIS A 159 60.823 33.515 19.402 1.00 18.49 ATOM 988 CB HIS A 159 61.808 32.435 18. 945. 1.00 20.42 ATOM 989 CG HIS A 159 61.867 31.260 19.868 1.00 25.61 ATOM 990 CD2 HIS A 159 62.134 31.183 21.193 1.00 26.32 ATOM 991 ND1 HIS A 159 61.582 29.974 19.460 1.00 28.74 ATOM 992 CE1 HIS A 159 61.669 29.156 20.494 1.00 28.74 ATOM 993 NE2 HIS A 159 62.002 29.865 21.558 1.00 29.76 ATOM 994 C HIS A 159 60.988 34.768 18.557 1.00 17.35 ATOM 995 O HIS A 159 61.779 35.648 18.884 1.00 18.51 ATOM 996 N ARG A 160 60.227 34.846 17.474 1.00 17.65 ATOM 997 CA ARG A 160 60.278 35.992 16.579 1.00 19.47 ATOM 998 CB ARG A 160 59.514 35.655 15.297 1.00 20.64 ATOM 999 CG ARG A 160 59.535 36.710 14.214 1.00 21.36 ATOM 1000 CD ARG A 160 58.908 36.135 12.943 1.00 24.65 ATOM 1001 NE ARG A 160 59.770 35.132 12.317 1.00 24.10 ATOM 1002 CZ ARG A 160 59.334 34.096 11.602 1.00 24.79 ATOM 1003 NH1 ARG A 160 58.034 33.901 11.420 1.00 21.67 ATOM 1004 NH2 ARG A 160 60.206 33.260 11.051 1.00 22.81 ATOM 1005 C ARG A 160 59.696 37.235 17.266 1.00 20.02 ATOM 1006 0 ARG A 160 60.174 38.351 17.057 1.00 21.08 ATOM 1007 N LEU A 161 58.673 37.046 18.093 1.00 19.43 ATOM 1008 CA LEU A 161 58.079 38.172 18.812 1.00 19.27 ATOM 1009 CB LEU A 161 56.638 37.853 19.224 1.00 19.24 ATOM 1010 CG LEU A 161 55.611 37.741 18.090 1.00 19.93 ATOM 1011 CD1 LEU A 161 54.227 37.519 18.685 1.00 18.11 ATOM 1012 CD2 LEU A 161 55.626 39.012 17.245 1.00 16.76 ATOM 1013 C LEU A 161 58.912 38.510 20.051 1.00 18.22

ATOM 1014 O LEU A 161 58.995 39.667 20.457 1.00 17.78 ATOM 1015 N ARG A 162 59.533 37.497 20.648 1.00 17.88 ATOM 1016 CA ARG A 162 60.370 37.715 21.826 1.00 17.59 ATOM 1017 CB ARG A 162 60.843 36.385 22.412 1.00 16.52 ATOM 1018 CG ARG A 162 59.806 35.670 23.257 1.00 16.27 ATOM 1019 CD ARG A 162 60.424 34.465 23.941 1.00 15.33 ATOM 1020 NE ARG A 162 59.500 33.825 24.871 1.00 15.04 ATOM 1021 CZ ARG A 162 59.804 32.759 25.602 1.00 15.93 ATOM 1022 NH1 ARG A 162 61.013 32.217 25.508 1.00 14.79 ATOM 1023 NH2 ARG A 162 58.902 32.231 26.422 1.00 14.97 ATOM 1024 C ARG A 162 61.586 38.566 21.490 1.00 17.29 ATOM 1025 O ARG A 162 62.058 39.338 22.322 1.00 16.65 ATOM 1026 N ALA A 163 62.084 38.423 20.265 1.00 16.93 ATOM 1027 CA ALA A 163 63.250 39.175 19.816 1.00 16.63 ATOM 1028 CB ALA A 163 63.685 38.689 18.440 1.00 15.17 ATOM 1029 C ALA A 163 62.983 40.677 19.775 1.00 17.05 ATOM 1030 O ALA A 163 63.917 41.470 19.668 1.00 14.83 ATOM 1031 N ARG A 164 61.709 41.061 19.860 1.00 17.20 ATOM 1032 CA ARG A 164 61.329 42.471 19.827 1.00 18.88 ATOM 1033 CB ARG A 164 60.772 42.841 18.446 1.00 18.87 ATOM 1034 CG ARG A 164 59.504 42.079 18.063 1.00 19.81 ATOM 1035 CD ARG A 164 59.017 42.460 16.670 1.00 17.62 ATOM 1036 NE ARG A 164 58.529 43.835 16.611 1.00 17.21 ATOM 1037 CZ ARG A 164 57.354 44.237 17.087 1.00 18.36 ATOM 1038 NH1 ARG A 164 56.532 43.366 17.663 1.00 17.29 ATOM 1039 NH2 ARG A 164 56.995 45.511 16.984 1.00 16.99 ATOM 1040 C ARG A 164 60.279 42.785 20.878 1.00 19.51 ATOM 1041 O ARG A 164 59.604 43.812 20.796 1.00 19.66 ATOM 1042 N GLN A 165 60.151 41.907 21.870 1.00 20.83 ATOM 1043 CA GLN A 165 59.158 42.079 22.924 1.00 20.81 ATOM 1044 CB GLN A 165 59.280 40.942 23.952 1.00 20.22 ATOM 1045 CG GLN A 165 58.312 41.047 25.136 1.00 22.04 ATOM 1046 CD GLN A 165 58.155 39.735 25.903 1.00 22.82 ATOM 1047 OE1 GLN A 165 59.083 38.932 25.987 1.00 22.86 ATOM 1048 NE2 GLN A 165 56.975 39.523 26.476 1.00 21.38 ATOM 1049 C GLN A 165 59.208 43.437 23.626 1.00 22.14 ATOM 1050 0 GLN A 165 58.164 44.037 23.897 1.00 22.79

ATOM 1051 N GLN A 166 60.409 43.930 23.914 1.00 22.12 ATOM 1052 CA GLN A 166 60.537 45.212 24.598 1.00 22.70 ATOM 1053 CB GLN A 166 61.937 45.371 25.188 1.00 25.51 ATOM 1054 CG GLN A 166 62.201 44.385 26.301 1.00 27.11 ATOM 1055 CD GLN A 166 61.020 44.285 27.244 1.00 28.49 ATOM 1056 OE1 GLN A 166 60.591 45.282 27.823 1.00 28.75 ATOM 1057 NE2 GLN A 166 60.480 43.081 27.394 1.00 29.17 ATOM 1058 C GLN A 166 60.217 46.381 23.696 1.00 21.88 ATOM 1059 O GLN A 166 59.636 47.372 24.140 1.00 20.81 ATOM 1060 N LYS A 167 60.601 46.272 22.429 1.00 21.75 ATOM 1061 CA LYS A 167 60.308 47.331 21.480 1.00 21.20 ATOM 1062 CB LYS A 167 60.888 47.002 20.105 1.00 20.78 ATOM 1063 CG LYS A 167 60.386 47.931 19.023 1.00 25.29 ATOM 1064 CD LYS A 167 60.917 47.567 17.651 1.00 29.48 ATOM 1065 CE LYS A 167 62.372 47.952 17.502 1.00 33.26 ATOM 1066 NZ LYS A 167 62.806 47.876 16.078 1.00 36.00 ATOM 1067 C LYS A 167 58.788 47.459 21.380 1.00 20.64 ATOM 1068 O LYS A 167 58.246 48.565 21.406 1.00 20.50 ATOM 1069 N GLN A 168 58.105 46.320 21.278 1.00 19.29 ATOM 1070 CA GLN A 168 56.649 46.318 21.175 1.00 18.72 ATOM 1071 CB GLN A 168 56.117 44.894 20.986 1.00 17.31 ATOM 1072 CG GLN A 168 54.598 44.820 20.821 1.00 17.69 ATOM 1073 CD GLN A 168 54.086 45.620 19.624 1.00 18.27 ATOM 1074 OE1 GLN A 168 54.449 45.349 18.474 1.00 16.59 ATOM 1075 NE2 GLN A 168 53.239 46.610 19.894 1.00 16.80 ATOM 1076 C GLN A 168 56.028 46. 944 22.416 1.00 17.89 ATOM 1077 0 GLN A 168 55.043 47.669 22.318 1.00 17.45 ATOM 1078 N ALA A 169 56.615 46.680 23.581 1.00 17.92 ATOM 1079 CA ALA A 169 56.098 47.247 24.825 1.00 18.33 ATOM 1080 CB ALA A 169 56.972 46.831 26.006 1.00 17.47 ATOM 1081 C ALA A 169 56.043 48.770 24.722 1.00 18.61 ATOM 1082 O ALA A 169 55.075 49.394 25.159 1.00 19.23 ATOM 1083 N LYS A 170 57.082 49.368 24.146 1.00 19.44 ATOM 1084 CA LYS A 170 57.121 50.818 23.986 1.00 21.87 ATOM 1085 CB LYS A 170 58.535 51.290 23.629 1.00 23.58 ATOM 1086 CG LYS A 170 59.517 51.205 24.793 1.00 28.39 ATOM 1087 CD LYS A 170 60.837 51.900 24.472 1.00 30.60

ATOM 1088 CE LYS A 170 61.785 51.860 25.663 1.00 31.30 ATOM 1089 NZ LYS A 170 62.110 50.456 26.065 1.00 35.39 ATOM 1090 C LYS A 170 56.136 51.284 22.919 1.00 20.75 ATOM 1091 0 LYS A 170 55.505 52.328 23.068 1.00 21.15 ATOM 1092 N LEU A 171 56.011 50.511 21.844 1.00 19.14 ATOM 1093 CA LEU A 171 55.078 50.851 20.771 1.00 18.56 ATOM 1094 CB LEU A 171 55.186 49.835 19.633 1.00 17.57 ATOM 1095 CG LEU A 171 56.467 49.956 18.807 1.00 17.13 ATOM 1096 CD1 LEU A 171 56.664 48.719 17.947 1.00 13. 91 ATOM 1097 CD2 LEU A 171 56. 385 51.217 17.954 1.00 14.77 ATOM 1098 C LEU A 171 53.650 50.878 21.311 1.00 17.89 ATOM 1099 0 LEU A 171 52.891 51.810 21.041 1.00 15.97 ATOM 1100 N THR A 172 53.294 49.850 22.078 1.00 18.22 ATOM 1101 CA THR A 172 51.965 49.758 22.669 1.00 19.38 ATOM 1102 CB THR A 172 51.805 48.444 23.467 1.00 17.92 ATOM 1103 OG1 THR A 172 51.885 47.330 22.566 1.00 16.29 ATOM 1104 CG2 THR A 172 50.465 48.412 24.188 1.00 14.36 ATOM 1105 C THR A 172 51.708 50.956 23.587 1.00 21.01 ATOM 1106 O THR A 172 50.659 51.598 23.507 1.00 19.74 ATOM 1107 N GLU A 173 52.674 51.261 24.447 1.00 23.19 ATOM 1108 CA GLU A 173 52.551 52.395 25.356 1.00 26.29 ATOM 1109 CB GLU A 173 53.800 52.506 26.235 1.00 30.21 ATOM 1110 CG GLU A 173 53.738 53.624 27.267 1.00 38.62 ATOM 1111 CD GLU A 173 52.659 53.398 28.323 1.00 43.67 ATOM 1112 OE1 GLU A 173 52.386 54.338 29.103 1.00 44.97 ATOM 1113 OE2 GLU A 173 52.089 52.283 28.380 1.00 45.74 ATOM 1114 C GLU A 173 52.387 53.667 24.524 1.00 26.14 ATOM 1115 0 GLU A 173 51.782 54.643 24.964 1.00 25.40 ATOM 1116 N ASP A 174 52.926 53.636 23.311 1.00 26.93 ATOM 1117 CA ASP A 174 52.855 54.766 22.395 1.00 27.97 ATOM 1118 CB ASP A 174 54.062 54.748 21.462 1.00 32.88 ATOM 1119 CG ASP A 174 54.992 55.914 21.696 1.00 38.17 ATOM 1120 OD1 ASP A 174 54.577 57.066 21.429 1.00 39.41 ATOM 1121 OD2 ASP A 174 56.133 55.675 22.150 1.00 40.28 ATOM 1122 C ASP A 174 51.576 54. 795 21.556 1.00 26.80 ATOM 1123 O ASP A 174 51.448 55.620 20.653 1.00 26.81 ATOM 1124 N GLY A 175 50.642 53.891 21.841 1.00 24.53

ATOM 1125 CA GLY A 175 49.397 53.864 21.092 1.00 23.66 ATOM 1126 C GLY A 175 49.402 52.979 19.856 1.00 23.36 ATOM 1127 O GLY A 175 48.568 53.153 18.967 1.00 23.88 ATOM 1128 N LEU A 176 50.332 52.026 19.799 1.00 22.36 ATOM 1129 CA LEU A 176 50.440 51.116 18.657 1.00 20.26 ATOM 1130 CB LEU A 176 51.730 51.411 17.886 1.00 19.38 ATOM 1131 CG LEU A 176 51.783 52.791 17.220 1.00 20.05 ATOM 1132 CD1 LEU A 176 53.163 53.045 16.621 1.00 19.87 ATOM 1133 CD2 LEU A 176 50.706 52.866 16.142 1.00 20.92 ATOM 1134 C LEU A 176 50.419 49.654 19.110 1.00 19.21 ATOM 1135 0 LEU A 176 51.443 48.967 19.083 1.00 18.80 ATOM 1136 N PRO A 177 49.235 49.160 19.515 1.00 17.06 ATOM 1137 CD PRO A 177 48.000 49.955 19.595 1.00 14.58 ATOM 1138 CA PRO A 177 48.994 47.795 19.995 1.00 16.17 ATOM 1139 CB PRO A 177 47.529 47.834 20.437 1.00 16.09 ATOM 1140 CG PRO A 177 47.276 49.277 20.718 1.00 15.02 ATOM 1141 C PRO A 177 49.252 46.660 18.998 1.00 16.11 ATOM 1142 0 PRO A 177 49.238 46.851 17.780 1.00 15.91 ATOM 1143 N LEU A 178 49.469 45.471 19.549 1.00 14.60 ATOM 1144 CA LEU A 178 49.725 44.272 18.768 1.00 15.30 ATOM 1145 CB LEU A 178 51.126 43.735 19.072 1.00 13.15 ATOM 1146 CG LEU A 178 51.497 42.403 18.417 1.00 14.53 ATOM 1147 CD1 LEU A 178 51.552 42.587 16.908 1.00 13.70 ATOM 1148 CD2 LEU A 178 52.843 41.914 18.945 1. 00 10. 81 ATOM 1149 C LEU A 178 48.700 43.197 19.109 1.00 14.34 ATOM 1150 0 LEU A 178 48.451 42.913 20.277 1.00 16.02 ATOM 1151 N GLY A 179 48.100 42.606 18.086 1.00 14.80 ATOM 1152 CA GLY A 179 47.134 41.551 18.312 1.00 11.92 ATOM 1153 C GLY A 179 47.677 40.287 17.677 1.00 13.13 ATOM 1154 0 GLY A 179 48.431 40.358 16.703 1.00 11.81 ATOM 1155 N VAL A 180 47.320 39.136 18.237 1.00 12.90 ATOM 1156 CA VAL A 180 47.758 37.855 17.701 1.00 12.61 ATOM 1157 CB VAL A 180 48.702 37.128 18.671 1.00 13.26 ATOM 1158 CG1 VAL A 180 49.023 35.738 18.132 1.00 11.53 ATOM 1159 CG2 VAL A 180 49.983 37.938 18.846 1.00 14.43 ATOM 1160 C VAL A 180 46.534 36.986 17.436 1.00 14.18 ATOM 1161 0 VAL A 180 45.710 36.758 18.326 1.00 14.98

ATOM 1162 N ASN A 181 46.421 36.513 16.200 1.00 14.07 ATOM 1163 CA ASN A 181 45.293 35.696 15.774 1.00 15.82 ATOM 1164 CB ASN A 181 44.929 36.081 14.335 1.00 16.86 ATOM 1165 CG ASN A 181 43.629 35.469 13.868 1.00 18.54 ATOM 1166 OD1 ASN A 181 43.430 34.254 13.948 1.00 16.81 ATOM 1167 ND2 ASN A 181 42.734 36.313 13.356 1.00 18.07 ATOM 1168 C ASN A 181 45.656 34.209 15.870 1.00 16.41 ATOM 1169 0 ASN A 181 46.649 33.767 15.290 1.00 16.63 ATOM 1170 N LEU A 182 44.838 33.448 16.595 1.00 15.13 ATOM 1171 CA LEU A 182 45.070 32.023 16.807 1.00 16.25 ATOM 1172 CB LEU A 182 44.865 31.684 18.284 1.00 15.13 ATOM 1173 CG LEU A 182 45.680 32.500 19.285 1.00 16.55 ATOM 1174 CD1 LEU A 182 45.267 32.128 20.704 1.00 14.83 ATOM 1175 CD2 LEU A 182 47.163 32.246 19.060 1.00 15.51 ATOM 1176 C LEU A 182 44.185 31.102 15.970 1.00 16.80 ATOM 1177 O LEU A 182 42.981 31.307 15.857 1.00 18.12 ATOM 1178 N GLY A 183 44.802 30.078 15.397 1.00 17.17 ATOM 1179 CA GLY A 183 44.073 29.118 14.594 1.00 17.88 ATOM 1180 C GLY A 183 44.345 27.738 15.160 1.00 19.65 ATOM 1181 O GLY A 183 44.918 27.605 16.244 1.00 18.50 ATOM 1182 N LYS A 184 43.939 26.702 14.441 1.00 20.40 ATOM 1183 CA LYS A 184 44.174 25.353 14.921 1.00 22.00 ATOM 1184 CB LYS A 184 42. 895 24.767 15.529 1.00 23.77 ATOM 1185 CG LYS A 184 41.908 24.238 14.518 1.00 27.06 ATOM 1186 CD LYS A 184 40.885 23.350 15.198 1.00 31.45 ATOM 1187 CE LYS A 184 40.161 22.473 14.186 1.00 34.64 ATOM 1188 NZ LYS A 184 41.100 21.535 13.509 1.00 34.99 ATOM 1189 C LYS A 184 44.677 24.470 13.791 1.00 20.60 ATOM 1190 0 LYS A 184 44.382 24.705 12.624 1.00 21.08 ATOM 1191 N ASN A 185 45.449 23.454 14.146 1.00 21.53 ATOM 1192 CA ASN A 185 46.000 22.545 13.157 1.00 22.66 ATOM 1193 CB ASN A 185 47.050 21.643 13.804 1.00 20.05 ATOM 1194 CG ASN A 185 48.367 22.358 14.035 1.00 19.87 ATOM 1195 OD1 ASN A 185 48.806 22.523 15.172 1.00 20.27 ATOM 1196 ND2 ASN A 185 49.006 22.781 12.952 1.00 18.79 ATOM 1197 C ASN A 185 44.945 21.689 12.464 1.00 24.39 ATOM 1198 O ASN A 185 43.932 21.308 13.058 1.00 23.03

ATOM 1199 N LYS A 186 45.209 21.385 11.198 1.00 27.14 ATOM 1200 CA LYS A 186 44.319 20.572 10.385 1.00 29.82 ATOM 1201 CB LYS A 186 44.908 20.425 8.982 1.00 30.42 ATOM 1202 CG LYS A 186 44.080 19.567 8.044 1.00 33.06 ATOM 1203 CD LYS A 186 44.744 19.470 6.687 1.00 35.37 ATOM 1204 CE LYS A 186 43.899 18.682 5.706 1.00 36.58 ATOM 1205 NZ LYS A 186 44.566 18.585 4.374 1.00 38.37 ATOM 1206 C LYS A 186 44.061 19.184 10. 980 1.00 31.17 ATOM 1207 O LYS A 186 42.924 18.719 11.006 1.00 31.03 ATOM 1208 N THR A 187 45.113 18.527 11.460 1.00 33.25 ATOM 1209 CA THR A 187 44.974 17.186 12.027 1.00 36.04 ATOM 1210 CB THR A 187 46.211 16.316 11.719 1.00 36.38 ATOM 1211 OG1 THR A 187 47.351 16.838 12.416 1.00 35.74 ATOM 1212 CG2 THR A 187 46.489 16.300 10.216 1.00 35.36 ATOM 1213 C THR A 187 44.755 17.181 13.537 1.00 37.75 ATOM 1214 O THR A 187 44.844 16.134 14.182 1.00 39.15 ATOM 1215 N SER A 188 44.474 18.349 14.100 1.00 38.10 ATOM 1216 CA SER A 188 44.233 18.451 15.530 1.00 37.99 ATOM 1217 CB SER A 188 44.062 19.915 15.929 1.00 37.74 ATOM 1218 OG SER A 188 43.772 20.028 17.309 1.00 39.67 ATOM 1219 C SER A 188 42.977 17.666 15.899 1.00 38.60 ATOM 1220 O SER A 188 42.034 17.586 15.113 1.00 37.87 ATOM 1221 N VAL A 189 42.971 17.088 17.097 1.00 39.17 ATOM 1222 CA VAL A 189 41.830 16.313 17.576 1.00 40.90 ATOM 1223 CB VAL A 189 42.290 14.987 18.225 1.00 42.04 ATOM 1224 CG1 VAL A 189 41.117 14.308 18.903 1.00 42.79 ATOM 1225 CG2 VAL A 189 42.890 14.068 17.168 1.00 41.83 ATOM 1226 C VAL A 189 41.024 17.101 18.607 1.00 41.62 ATOM 1227 0 VAL A 189 39.803 16.950 18.708 1.00 43.26 ATOM 1228 N ASP A 190 41.714 17.947 19.366 1.00 40.63 ATOM 1229 CA ASP A 190 41.078 18.761 20.396 1.00 39.16 ATOM 1230 CB ASP A 190 41.755 18.507 21.745 1.00 41.81 ATOM 1231 CG ASP A 190 40.974 19.080 22.907 1.00 44.27 ATOM 1232 OD1 ASP A 190 40.345 20.147 22.741 1.00 44.15 ATOM 1233 OD2 ASP A 190 41.000 18.468 23.995 1.00 48.15 ATOM 1234 C ASP A 190 41.201 20.242 20.036 1.00 37.02 ATOM 1235 0 ASP A 190 42.176 20.899 20.409 1.00 36.48

ATOM 1236 N ALA A 191 40.210 20.763 19.318 1.00 33.89 ATOM 1237 CA ALA A 191 40.214 22.162 18.899 1.00 30.62 ATOM 1238 CB ALA A 191 38.896 22.505 18.218 1.00 30.65 ATOM 1239 C ALA A 191 40.458 23.120 20.055 1.00 28.69 ATOM 1240 0 ALA A 191 41.217 24.077 19.926 1.00 26.95 ATOM 1241 N ALA A 192 39.809 22.860 21.185 1.00 27.16 ATOM 1242 CA ALA A 192 39.952 23.713 22.359 1.00 25.90 ATOM 1243 CB ALA A 192 39.019 23.237 23.467 1.00 23.51 ATOM 1244 C ALA A 192 41.389 23.758 22.866 1.00 25.40 ATOM 1245 O ALA A 192 41.880 24.821 23.231 1.00 27.26 ATOM 1246 N GLU A 193 42.062 22.610 22.890 1.00 25.06 ATOM 1247 CA GLU A 193 43.442 22.555 23.359 1.00 25.56 ATOM 1248 CB GLU A 193 43.925 21.103 23.449 1.00 28.82 ATOM 1249 CG GLU A 193 45.366 20.970 23.923 1.00 33.91 ATOM 1250 CD GLU A 193 45.599 21.600 25.290 1.00 38.03 ATOM 1251 OE1 GLU A 193 46.776 21.781 25.672 1.00 40.48 ATOM 1252 OE2 GLU A 193 44.607 21.909 25.986 1.00 40.31 ATOM 1253 C GLU A 193 44.371 23.363 22.451 1.00 24.11 ATOM 1254 0 GLU A 193 45.293 24.025 22.931 1.00 23.27 ATOM 1255 N ASP A 194 44.124 23.308 21.145 1.00 21.29 ATOM 1256 CA ASP A 194 44.919 24.062 20.179 1.00 21.47 ATOM 1257 CB ASP A 194 44.370 23.860 18.762 1.00 22.50 ATOM 1258 CG ASP A 194 45.052 22.725 18.025 1.00 22.41 ATOM 1259 OD1 ASP A 194 45.566 21.806 18.686 1.00 25.90 ATOM 1260 OD2 ASP A 194 45.068 22.746 16.776 1.00 24.02 ATOM 1261 C ASP A 194 44.905 25.554 20.523 1.00 21.24 ATOM 1262 O ASP A 194 45.957 26.199 20.556 1.00 21.63 ATOM 1263 N TYR A 195 43.718 26.104 20.773 1.00 19.11 ATOM 1264 CA TYR A 195 43.615 27.517 21.118 1.00 19.37 ATOM 1265 CB TYR A 195 42.157 27.996 21.078 1.00 18.34 ATOM 1266 CG TYR A 195 41.555 27.995 19.692 1.00 19. 08 ATOM 1267 CD1 TYR A 195 40.775 26.935 19.252 1.00 18.54 ATOM 1268 CE1 TYR A 195 40.267 26.906 17.972 1.00 19.33 ATOM 1269 CD2 TYR A 195 41.808 29.034 18.806 1.00 19.55 ATOM 1270 CE2 TYR A 195 41.303 29.013 17.518 1.00 19. 90 ATOM 1271 CZ TYR A 195 40.535 27.946 17.108 1.00 20.74 ATOM 1272 OH TYR A 195 40.041 27.910 15.823 1.00 21.90

ATOM 1273 C TYR A 195 44.197 27.759 22. 500 1.00 18.97 ATOM 1274 0 TYR A 195 44.819 28.791 22.745 1.00 19.13 ATOM 1275 N ALA A 196 43.993 26.806 23.404 1.00 18.98 ATOM 1276 CA ALA A 196 44.518 26.925 24.759 1.00 19.56 ATOM 1277 CB ALA A 196 44.132 25.705 25.581 1.00 19.04 ATOM 1278 C ALA A 196 46.040 27.062 24.699 1.00 19.48 ATOM 1279 0 ALA A 196 46.625 27.874 25.419 1.00 19.62 ATOM 1280 N GLU A 197 46.670 26.271 23.834 1.00 18.28 ATOM 1281 CA GLU A 197 48.120 26.312 23.671 1.00 21.11 ATOM 1282 CB GLU A 197 48.592 25.208 22.716 1.00 25.12 ATOM 1283 CG GLU A 197 48.254 23.800 23.169 1.00 34.80 ATOM 1284 CD GLU A 197 48.965 22.741 22.346 1.00 40.02 ATOM 1285 OE1 GLU A 197 48.613 21.546 22.466 1.00 41.16 ATOM 1286 OE2 GLU A 197 49.885 23.106 21.583 1.00 44.59 ATOM 1287 C GLU A 197 48.557 27.668 23.129 1.00 19.25 ATOM 1288 0 GLU A 197 49.545 28.242 23.595 1.00 17.18 ATOM 1289 N GLY A 198 47.819 28.170 22.141 1.00 16.72 ATOM 1290 CA GLY A 198 48.136 29.461 21.560 1.00 16.16 ATOM 1291 C GLY A 198 48.061 30.570 22.594 1.00 15.20 ATOM 1292 O GLY A 198 48.885 31.485 22.603 1.00 14.79 ATOM 1293 N VAL A 199 47.063 30.489 23.466 1.00 15.52 ATOM 1294 CA VAL A 199 46.884 31.477 24.520 1.00 15.90 ATOM 1295 CB VAL A 199 45.622 31.184 25.361 1.00 16.38 ATOM 1296 CG1 VAL A 199 45.625 32.046 26.619 1.00 12.29 ATOM 1297 CG2 VAL A 199 44.368 31.442 24.530 1.00 16.31 ATOM 1298 C VAL A 199 48.085 31.465 25.458 1.00 18.10 ATOM 1299 O VAL A 199 48.575 32.519 25.867 1.00 19.32 ATOM 1300 N ARG A 200 48.564 30.269 25.786 1.00 17.75 ATOM 1301 CA ARG A 200 49.699 30.129 26.691 1.00 20.29 ATOM 1302 CB ARG A 200 49.814 28.683 27.186 1.00 22.43 ATOM 1303 CG ARG A 200 48.752 28.276 28.191 1.00 25.39 ATOM 1304 CD ARG A 200 49.160 27.005 28.914 1.00 26.71 ATOM 1305 NE ARG A 200 49. 080 25.828 28.060 1.00 28.79 ATOM 1306 CZ ARG A 200 47.967 25.134 27.859 1.00 30.88 ATOM 1307 NH1 ARG A 200 46.846 25.505 28.457 1.00 32.47 ATOM 1308 NH2 ARG A 200 47.973 24.071 27.063 1.00 31.75 ATOM 1309 C ARG A 200 51.039 30.551 26.106 1.00 19.06

ATOM 1310 0 ARG A 200 51.873 31.128 26.805 1.00 19.67 ATOM 1311 N VAL A 201 51.249 30.267 24.826 1.00 17.35 ATOM 1312 CA VAL A 201 52.514 30.599 24.189 1.00 14.77 ATOM 1313 CB VAL A 201 52.828 29.606 23.044 1.00 15.43 ATOM 1314 CG1 VAL A 201 54.145 29.990 22.369 1.00 13.31 ATOM 1315 CG2 VAL A 201 52. 906 28.177 23.596 1.00 9.07 ATOM 1316 C VAL A 201 52.618 32.027 23.652 1.00 16.34 ATOM 1317 0 VAL A 201 53. 651 32.680 23.826 1.00 13.79 ATOM 1318 N LEU A 202 51.556 32.520 23.016 1.00 16. 01 ATOM 1319 CA LEU A 202 51.590 33.867 22.453 1.00 14.71 ATOM 1320 CB LEU A 202 51.104 33.840 21.003 1.00 15.87 ATOM 1321 CG LEU A 202 51.994 33.063 20.029 1.00 16.57 ATOM 1322 CD1 LEU A 202 51.515 33.304 18.603 1.00 15.39 ATOM 1323 CD2 LEU A 202 53.444 33.510 20.185 1.00 15.53 ATOM 1324 C LEU A 202 50.815 34.924 23.235 1.00 15.25 ATOM 1325 O LEU A 202 51.056 36.117 23.070 1.00 14.50 ATOM 1326 N GLY A 203 49.890 34.492 24.084 1.00 15.32 ATOM 1327 CA GLY A 203 49.128 35.441 24.873 1.00 16.45 ATOM 1328 C GLY A 203 49.993 36.407 25.672 1.00 16.99 ATOM 1329 0 GLY A 203 49.628 37.574 25.838 1.00 14.26 ATOM 1330 N PRO A 204 51.145 35.954 26.193 1.00 18.28 ATOM 1331 CD PRO A 204 51.566 34.547 26.321 1.00 17.79 ATOM 1332 CA PRO A 204 52.029 36.831 26.975 1.00 18.93 ATOM 1333 CB PRO A 204 53.021 35.849 27.608 1.00 16.96 ATOM 1334 CG PRO A 204 52.257 34.552 27.654 1.00 17.70 ATOM 1335 C PRO A 204 52.744 37.892 26.132 1.00 18.89 ATOM 1336 0 PRO A 204 53.331 38.836 26.672 1.00 20.25 ATOM 1337 N LEU A 205 52.689 37.736 24.812 1.00 17.55 ATOM 1338 CA LEU A 205 53.351 38.669 23.898 1.00 16.80 ATOM 1339 CB LEU A 205 54.220 37.883 22.910 1.00 16.30 ATOM 1340 CG LEU A 205 55.394 37.098 23.508 1.00 18.10 ATOM 1341 CD1 LEU A 205 55.731 35.902 22.640 1.00 15.74 ATOM 1342 CD2 LEU A 205 56.589 38.023 23.657 1.00 17.13 ATOM 1343 C LEU A 205 52.389 39.562 23.113 1.00 17.23 ATOM 1344 0 LEU A 205 52.815 40.337 22.256 1.00 16.66 ATOM 1345 N ALA A 206 51.097 39.471 23.413 1.00 16.47 ATOM 1346 CA ALA A 206 50.111 40.254 22.684 1.00 16.01

ATOM 1347 CB ALA A 206 49.215 39.315 21.890 1.00 16.02 ATOM 1348 C ALA A 206 49.253 41.173 23.536 1.00 16.71 ATOM 1349 O ALA A 206 49.019 40.921 24.715 1.00 17.69 ATOM 1350 N ASP A 207 48.782 42.253 22.928 1.00 17.04 ATOM 1351 CA ASP A 207 47.909 43.171 23.635 1.00 17.84 ATOM 1352 CB ASP A 207 47.940 44.546 22.977 1.00 17.96 ATOM 1353 CG ASP A 207 49.256 45.264 23.222 1.00 20.68 ATOM 1354 OD1 ASP A 207 49.642 45.391 24.403 1.00 22.88 ATOM 1355 OD2 ASP A 207 49.907 45.698 22.250 1.00 20.09 ATOM 1356 C ASP A 207 46.515 42.552 23.601 1.00 16.42 ATOM 1357 0ASP A 207 45.732 42.708 24.530 1.00 16.76 ATOM 1358 N TYR A 208 46.217 41.833 22.525 1. 00 15.49 ATOM 1359 CA TYR A 208 44.941 41.145 22.412 1.00 15.74 ATOM 1360 CB TYR A 208 43.844 42.052 21.815 1.00 15.84 ATOM 1361 CG TYR A 208 43.919 42.333 20.326 1.00 16.08 ATOM 1362 CD1 TYR A 208 44.387 43.558 19.852 1.00 16.67 ATOM 1363 CE1 TYR A 208 44.400 43.846 18.496 1.00 16.45 ATOM 1364 CD2 TYR A 208 43.471 41.399 19.396 1.00 15.39 ATOM 1365 CE2 TYR A 208 43.483 41.675 18.037 1.00 14.91 ATOM 1366 CZ TYR A 208 43.947 42.900 17.593 1.00 18.55 ATOM 1367 OH TYR A 208 43.966 43.179 16.243 1.00 18.49 ATOM 1368 C TYR A 208 45.106 39.887 21.575 1.00 15.90 ATOM 1369 O TYR A 208 45.915 39.845 20.646 1.00 15.17 ATOM 1370 N LEU A 209 44.355 38.853 21.940 1.00 16.34 ATOM 1371 CA LEU A 209 44.382 37.580 21.235 1.00 17.24 ATOM 1372 CB LEU A 209 44.520 36.418 22.217 1.00 16.47 ATOM 1373 CG LEU A 209 45.855 36.203 22.920 1.00 17.92 ATOM 1374 CD1 LEU A 209 45.716 35.042 23.899 1.00 18.62 ATOM 1375 CD2 LEU A 209 46.942 35.917 21.889 1.00 15.83 ATOM 1376 C LEU A 209 43.077 37.420 20.472 1.00 16.93 ATOM 1377 0LEU A 209 42.031 37.890 20.914 1.00 16.94 ATOM 1378 N VAL A 210 43.142 36.749 19.330 1.00 18.06 ATOM 1379 CA VAL A 210 41.955 36.527 18.523 1.00 16.88 ATOM 1380 CB VAL A 210 42.096 37.153 17.119 1.00 16.81 ATOM 1381 CG1 VAL A 210 40.811 36.928 16.310 1.00 14.14 ATOM 1382 CG2 VAL A 210 42.414 38.631 17.239 1.00 12.93 ATOM 1383 C VAL A 210 41.683 35.045 18.338 1.00 17.75

ATOM 1384 0 VAL A 210 42.509 34.318 17.794 1.00 18.14 ATOM 1385 N VAL A 211 40.531 34.592 18.813 1.00 18.47 ATOM 1386 CA VAL A 211 40.155 33.199 18.629 1.00 18.41 ATOM 1387 CB VAL A 211 39.128 32.731 19.682 1.00 16.92 ATOM 1388 CG1 VAL A 211 38.707 31.304 19.389 1.00 13.30 ATOM 1389 CG2 VAL A 211 39.725 32.832 21.079 1.00 16.37 ATOM 1390 C VAL A 211 39.501 33.158 17.247 1.00 19.20 ATOM 1391 O VAL A 211 38.338 33.534 17.090 1.00 17.95 ATOM 1392 N ASN A 212 40.258 32.729 16.243 1.00 19.49 ATOM 1393 CA ASN A 212 39.721 32.661 14.896 1.00 20.70 ATOM 1394 CB ASN A 212 40.834 32.722 13.854 1.00 19.05 ATOM 1395 CG ASN A 212 40.291 32.666 12.444 1.00 18.45 ATOM 1396 OD1 ASN A 212 39.081 32.697 12.243 1.00 19.17 ATOM 1397 ND2 ASN A 212 41.177 32.585 11.463 1.00 18.72 ATOM 1398 C ASN A 212 38.925 31.381 14.712 1.00 22.66 ATOM 1399 O ASN A 212 39.484 30.282 14.621 1.00 23.43 ATOM 1400 N VAL A 213 37.611 31.529 14.646 1.00 21.15 ATOM 1401 CA VAL A 213 36.745 30.379 14.489 1.00 22.75 ATOM 1402 CB VAL A 213 35.893 30.194 15.760 1.00 23.97 ATOM 1403 CG1 VAL A 213 34.781 31.241 15.810 1.00 23.80 ATOM 1404 CG2 VAL A 213 35.341 28.810 15.799 1.00 27.69 ATOM 1405 C VAL A 213 35.841 30.572 13.272 1.00 21.59 ATOM 1406 0 VAL A 213 34.820 29.893 13.120 1.00 21.53 ATOM 1407 N SER A 214 36.242 31.492 12.397 1.00 20.91 ATOM 1408 CA SER A 214 35.469 31.813 11.206 1.00 19.69 ATOM 1409 CB SER A 214 35.015 33.275 11.267 1.00 19.18 ATOM 1410 OG SER A 214 36.110 34.144 11.508 1.00 14.56 ATOM 1411 C SER A 214 36.180 31.556 9.881 1.00 20.92 ATOM 1412 O SER A 214 35.712 31.996 8.832 1.00 19.05 ATOM 1413 N SER A 215 37.309 30.856 9.914 1.00 22.56 ATOM 1414 CA SER A 215 38. 010 30.563 8.672 1.00 23.82 ATOM 1415 CB SER A 215 39.385 29.968 8.945 1.00 25.73 ATOM 1416 OG SER A 215 40.010 29.597 7.726 1.00 25.27 ATOM 1417 C SER A 215 37.186 29.564 7.867 1.00 24.98 ATOM 1418 0 SER A 215 36.744 28.539 8.387 1.00 25.15 ATOM 1419 N PRO A 216 36.961 29.857 6.582 1.00 26.90 ATOM 1420 CD PRO A 216 37.238 31.138 5.900 1.00 24.99

ATOM 1421 CA PRO A 216 36.182 28.963 5.721 1.00 27.74 ATOM 1422 CB PRO A 216 35.606 29.920 4.690 1.00 27.00 ATOM 1423 CG PRO A 216 36.755 30.872 4.482 1.00 25. 45 ATOM 1424 c PRO A 216 37.045 27.895 5.066 1.00 29.18 ATOM 1425 O PRO A 216 36.531 27.026 4.368 1.00 30.98 ATOM 1426 N ASN A 217 38.353 27.958 5.302 1.00 30.72 ATOM 1427 CA ASN A 217 39.283 27.022 4.679 1.00 32.10 ATOM 1428 CB ASN A 217 40.446 27.804 4.072 1.00 31.89 ATOM 1429 CG ASN A 217 39.971 28.926 3.170 1.00 33.35 ATOM 1430 OD1 ASN A 217 39.220 28.696 2.220 1.00 33.84 ATOM 1431 ND2 ASN A 217 40.400 30.149 3.465 1.00 32.31 ATOM 1432 C ASN A 217 39.814 25.889 5.548 1.00 33.08 ATOM 1433 0 ASN A 217 40.812 25.250 5.204 1.00 32.64 ATOM 1434 N THR A 218 39.149 25.644 6.671 1.00 34.23 ATOM 1435 CA THR A 218 39.523 24.556 7.570 1.00 35. 11 ATOM 1436 CB THR A 218 40.191 25.073 8.867 1.00 35.66 ATOM 1437 OG1 THR A 218 41.508 25.556 8.568 1.00 34.06 ATOM 1438 CG2 THR A 218 40.293 23.956 9.895 1.00 33.99 ATOM 1439 C THR A 218 38.243 23.801 7.915 1.00 35.83 ATOM 1440 0 THR A 218 37.315 24.367 8.497 1.00 36.15 ATOM 1441 N ALA A 219 38.200 22.526 7.532 1.00 36.11 ATOM 1442 CA ALA A 219 37.041 21.666 7.760 1.00 35.60 ATOM 1443 CB ALA A 219 37.372 20.234 7.347 1.00 33.81 ATOM 1444 C ALA A 219 36.502 21.678 9.187 1.00 35.62 ATOM 1445 0 ALA A 219 37.232 21.414 10.143 1.00 36.09 ATOM 1446 N GLY A 220 35.214 21.992 9.313 1.00 35.71 ATOM 1447 CA GLY A 220 34.556 22.014 10.609 1.00 35.84 ATOM 1448 C GLY A 220 34.916 23.111 11.596 1.00 35.60 ATOM 1449 0 GLY A 220 34.418 23.100 12.720 1.00 36.18 ATOM 1450 N LEU A 221 35.759 24.058 11.197 1.00 34.93 ATOM 1451 CA LEU A 221 36.162 25.135 12.099 1.00 34.46 ATOM 1452 CB LEU A 221 37.307 25. 951 11.489 1.00 34.46 ATOM 1453 CG LEU A 221 37.951 26.938 12.470 1.00 34.17 ATOM 1454 CD1 LEU A 221 38.908 26.171 13.375 1.00 35.09 ATOM 1455 CD2 LEU A 221 38.693 28.035 11.725 1.00 33.10 ATOM 1456 C LEU A 221 35.013 26.080 12.451 1.00 34.14 ATOM 1457 0 LEU A 221 34.823 26.438 13.615 1.00 34.17

ATOM 1458 N ARG A 222 34.248 26.483 11.444 1.00 34.57 ATOM 1459 CA ARG A 222 33.130 27.395 11.654 1.00 34.52 ATOM 1460 CB ARG A 222 32.554 27.826 10.307 1.00 35.12 ATOM 1461 CG ARG A 222 33.462 28.768 9.529 1.00 36.10 ATOM 1462 CD ARG A 222 32.904 29.017 8.143 1.00 38.44 ATOM 1463 NE ARG A 222 32.993 27.822 7.306 1.00 39.22 ATOM 1464 CZ ARG A 222 32.290 27.634 6.194 1.00 39.46 ATOM 1465 NH1 ARG A 222 31.435 28.564 5.784 1.00 37.86 ATOM 1466 NH2 ARG A 222 32.447 26.521 5.490 1.00 38.60 ATOM 1467 C ARG A 222 32.019 26.831 12.538 1.00 34.35 ATOM 1468 0 ARG A 222 31.231 27.589 13.108 1.00 32.92 ATOM 1469 N SER A 223 31.953 25.507 12.658 1.00 34.08 ATOM 1470 CA SER A 223 30.928 24.888 13.490 1.00 33.94 ATOM 1471 CB SER A 223 30.913 23.366 13.304 1.00 32.78 ATOM 1472 OG SER A 223 32.095 22.769 13.808 1.00 35.71 ATOM 1473 C SER A 223 31.206 25.234 14.949 1.00 33.87 ATOM 1474 0 SER A 223 30.325 25.123 15.803 1.00 33.34 ATOM 1475 N LEU A 224 32.435 25.660 15.227 1.00 33.97 ATOM 1476 CA LEU A 224 32.817 26.038 16.584 1.00 34.45 ATOM 1477 CB LEU A 224 34.340 26.172 16.697 1.00 33.66 ATOM 1478 CG LEU A 224 35.194 24.915 16.507 1.00 34.95 ATOM 1479 CD1 LEU A 224 36.670 25.288 16.515 1.00 31.91 ATOM 1480 CD2 LEU A 224 34.883 23.913 17.612 1.00 31.97 ATOM 1481 C LEU A 224 32.146 27.358 16.967 1.00 34.39 ATOM 1482 0 LEU A 224 32.243 27.807 18.109 1.00 33.98 ATOM 1483 N GLN A 225 31.474 27.984 16.004 1.00 35.00 ATOM 1484 CA GLN A 225 30.774 29.237 16.271 1.00 35.56 ATOM 1485 CB GLN A 225 30.571 30.043 14.976 1.00 34.95 ATOM 1486 CG GLN A 225 31.863 30.374 14.230 1.00 35.29 ATOM 1487 CD GLN A 225 31.628 31.191 12.966 1.00 34.79 ATOM 1488 OE1 GLN A 225 31.617 32.425 12.997 1.00 32.25 ATOM 1489 NE2 GLN A 225 31.427 30.501 11.846 1.00 32.30 ATOM 1490 C GLN A 225 29.421 28.905 16.904 1.00 34.76 ATOM 1491 0 GLN A 225 28.710 29.793 17.371 1.00 34.05 ATOM 1492 N GLY A 226 29.076 27.618 16.916 1.00 34.83 ATOM 1493 CA GLY A 226 27.822 27.183 17.512 1.00 35.53 ATOM 1494 C GLY A 226 27.803 27.504 18.997 1.00 36.05

ATOM 1495 0 GLY A 226 28.852 27.509 19.641 1.00 37.13 ATOM 1496 N LYS A 227 26.616 27.754 19.546 1.00 35.45 ATOM 1497 CA LYS A 227 26.465 28.116 20.957 1.00 34.81 ATOM 1498 CB LYS A 227 24.980 28.242 21.313 1.00 33.35 ATOM 1499 CG LYS A 227 24.723 28.929 22.652 1.00 32.92 ATOM 1500 CD LYS A 227 23.244 29.219 22.853 1.00 32.63 ATOM 1501 CE LYS A 227 22.980 29.911 24.182 1.00 34.34 ATOM 1502 NZ LYS A 227 23.617 31.256 24.261 1.00 36.79 ATOM 1503 C LYS A 227 27.150 27.204 21.974 1.00 35.00 ATOM 1504 O LYS A 227 27.985 27.663 22.755 1.00 33.88 ATOM 1505 N ALA A 228 26.797 25.922 21.975 1.00 34.83 ATOM 1506 CA ALA A 228 27.390 24.978 22.924 1.00 35.86 ATOM 1507 CB ALA A 228 26.719 23.615 22.795 1.00 33.42 ATOM 1508 C ALA A 228 28.897 24.837 22.723 1.00 35.90 ATOM 1509 O ALA A 228 29.674 24.941 23.671 1.00 34.64 ATOM 1510 N GLU A 229 29.301 24.597 21.481 1.00 37.47 ATOM 1511 CA GLU A 229 30.711 24.443 21.141 1.00 38.72 ATOM 1512 CB GLU A 229 30.852 24.145 19.644 1.00 42.88 ATOM 1513 CG GLU A 229 31.409 22.766 19.319 1.00 49.61 ATOM 1514 CD GLU A 229 31.311 22.429 17.838 1.00 53.45 ATOM 1515 OE1 GLU A 229 30.180 22.205 17.350 1.00 56.34 ATOM 1516 OE2 GLU A 229 32.361 22.393 17.159 1.00 55.01 ATOM 1517 C GLU A 229 31.498 25.704 21.490 1.00 36.50 ATOM 1518 0 GLU A 229 32.584 25.632 22.061 1.00 37.17 ATOM 1519 N LEU A 230 30.935 26.860 21.152 1.00 33.85 ATOM 1520 CA LEU A 230 31.588 28.135 21.409 1.00 30.53 ATOM 1521 CB LEU A 230 30.795 29.281 20.766 1.00 28. 19 ATOM 1522 CG LEU A 230 31.417 30.680 20.851 1.00 26.88 ATOM 1523 CD1 LEU A 230 32.750 30.701 20.106 1.00 24.02 ATOM 1524 CD2 LEU A 230 30.466 31.701 20.253 1.00 26.26 ATOM 1525 C LEU A 230 31.761 28.414 22.895 1.00 29. 06 ATOM 1526 O LEU A 230 32.795 28.935 23.312 1.00 28.63 ATOM 1527 N ARG A 231 30.753 28.076 23.693 1.00 28. 59 ATOM 1528 CA ARG A 231 30.826 28.324 25.128 1.00 28. 19 ATOM 1529 CB ARG A 231 29.484 28.021 25.803 1.00 29.46 ATOM 1530 CG ARG A 231 29.462 28.385 27.285 1.00 32.38 ATOM 1531 CD ARG A 231 28. 201 27.903 27.986 1.00 36.36

ATOM 1532 NE ARG A 231 27.009 28.660 27.608 1.00 39.08 ATOM 1533 CZ ARG A 231 25.952 28.134 26.995 1.00 39.48 ATOM 1534 NH1 ARG A 231 25.938 26.845 26.684 1.00 40.17 ATOM 1535 NH2 ARG A 231 24.901 28.893 26.710 1.00 39.24 ATOM 1536 C ARG A 231 31.931 27.503 25.793 1.00 27.19 ATOM 1537 0 ARG A 231 32.689 28.024 26.605 1.00 25.57 ATOM 1538 N ARG A 232 32.018 26.222 25.450 1.00 27.04 ATOM 1539 CA ARG A 232 33.042 25.355 26.022 1.00 28.55 ATOM 1540 CB ARG A 232 32.820 23.900 25.598 1.00 31.40 ATOM 1541 CG ARG A 232 33.906 22.951 26.097 1.00 37.46 ATOM 1542 CD ARG A 232 33.651 21.497 25.697 1.00 41.98 ATOM 1543 NE ARG A 232 32.314 21.050 26.084 1.00 46.56 ATOM 1544 CZ ARG A 232 31.240 21.146 25.305 1.00 49.01 ATOM 1545 NH1 ARG A 232 31.345 21.669 24.089 1.00 49.17 ATOM 1546 NH2 ARG A 232 30.057 20.732 25.746 1.00 49.45 ATOM 1547 C ARG A 232 34.428 25.807 25.579 1.00 27.29 ATOM 1548 O ARG A 232 35.377 25.795 26.361 1.00 26.97 ATOM 1549 N LEU A 233 34.538 26.203 24.318 1.00 25.58 ATOM 1550 CA LEU A 233 35.806 26.664 23.777 1.00 25.13 ATOM 1551 CB LEU A 233 35.669 26.912 22.275 1.00 26.34 ATOM 1552 CG LEU A 233 36.840 27.630 21.604 1.00 27.27 ATOM 1553 CD1 LEU A 233 38.097 26.800 21.736 1.00 29.09 ATOM 1554 CD2 LEU A 233 36.514 27.875 20.146 1.00 29.53 ATOM 1555 C LEU A 233 36.295 27.942 24.467 1.00 24.39 ATOM 1556 O LEU A 233 37.436 28.010 24.927 1.00 22.15 ATOM 1557 N LEU A 234 35.424 28.945 24.547 1.00 22.75 ATOM 1558 CA LEU A 234 35.774 30.228 25.154 1.00 22.29 ATOM 1559 CB LEU A 234 34.725 31.283 24.788 1.00 23.57 ATOM 1560 CG LEU A 234 34.647 31.536 23.280 1.00 26.28 ATOM 1561 CD1 LEU A 234 33.539 32.528 22.960 1.00 27.43 ATOM 1562 CD2 LEU A 234 35.995 32.047 22.794 1.00 26.22 ATOM 1563 C LEU A 234 35.963 30.180 26.663 1.00 21.30 ATOM 1564 0 LEU A 234 36.710 30.980 27.223 1.00 20.43 ATOM 1565 N THR A 235 35.285 29.256 27.330 1.00 21.31 ATOM 1566 CA THR A 235 35.444 29.135 28. 772 1.00 22.40 ATOM 1567 CB THR A 235 34.468 28.104 29.367 1.00 22.83 ATOM 1568 OG1 THR A 235 33.137 28.632 29.324 1.00 23.92

ATOM 1569 CG2 THR A 235 34.842 27.789 30.809 1.00 20.20 ATOM 1570 C THR A 235 36.877 28.691 29.069 1.00 21.59 ATOM 1571 O THR A 235 37.524 29.213 29.977 1.00 21.97 ATOM 1572 N LYS A 236 37.367 27.735 28.285 1.00 18.98 ATOM 1573 CA LYS A 236 38.720 27.227 28.451 1.00 20.97 ATOM 1574 CB LYS A 236 38.905 25.951 27.632 1.00 22.57 ATOM 1575 CG LYS A 236 40.256 25.283 27.844 1.00 29.29 ATOM 1576 CD LYS A 236 40.284 23.874 27.266 1.00 31.20 ATOM 1577 CE LYS A 236 41.588 23.177 27.602 1.00 34.02 ATOM 1578 NZ LYS A 236 41.554 21.739 27.212 1.00 37.66 ATOM 1579 C LYS A 236 39.758 28.273 28.036 1.00 20.11 ATOM 1580 O LYS A 236 40.773 28.454 28.710 1-. 00 18.99 ATOM 1581 N VAL A 237 39.500 28.963 26.931 1.00 19.39 ATOM 1582 CA VAL A 237 40.410 29.995 26.449 1.00 19.41 ATOM 1583 CB VAL A 237 39.892 30.619 25.137 1.00 19.28 ATOM 1584 CG1 VAL A 237 40.631 31.923 24.840 1.00 15.51 ATOM 1585 CG2 VAL A 237 40. 078 29.630 23.997 1.00 17.43 ATOM 1586 C VAL A 237 40.582 31.098 27.489 1.00 20.27 ATOM 1587 0 VAL A 237 41.705 31.484 27.817 1.00 20.76 ATOM 1588 N LEU A 238 39.462 31.597 28.007 1.00 21.31 ATOM 1589 CA LEU A 238 39.470 32.660 29.010 1.00 21.14 ATOM 1590 CB LEU A 238 38.042 33.127 29.295 1.00 19.77 ATOM 1591 CG LEU A 238 37.364 33.913 28.168 1.00 22.01 ATOM 1592 CD1 LEU A 238 35.894 34.143 28.506 1.00 21.78 ATOM 1593 CD2 LEU A 238 38.083 35.244 27.974 1.00 21.85 ATOM 1594 C LEU A 238 40.138 32.233 30.314 1.00 21.63 ATOM 1595 O LEU A 238 40.774 33.047 30.989 1.00 20.14 ATOM 1596 N GLN A 239 39.993 30.960 30.670 1.00 21.99 ATOM 1597 CA GLN A 239 40.609 30.458 31.891 1.00 22.84 ATOM 1598 CB GLN A 239 40.126 29.039 32.200 1.00 25.02 ATOM 1599 CG GLN A 239 40.681 28.489 33.504 1.00 29.97 ATOM 1600 CD GLN A 239 40.153 27.103 33.828 1.00 37.06 ATOM 1601 OE1 GLN A 239 38.940 26.895 33.941 1.00 40.00 ATOM 1602 NE2 GLN A 239 41.063 26.145 33.982 1.00 36.33 ATOM 1603 C GLN A 239 42.129 30.468 31.743 1.00 20.31 ATOM 1604 O GLN A 239 42.847 30.888 32.648 1.00 20.83 ATOM 1605 N GLU A 240 42.617 29.999 30.601 1.00 19. 91

ATOM 1606 CA GLU A 240 44. 054 29. 985 30. 348 1. 00 20. 13 ATOM 1607 CB GLU A 240 44. 348 29. 345 28. 992 1. 00 21. 91 ATOM 1608 CG GLU A 240 44. 002 27. 868 28. 918 1. 00 28. 96 ATOM 1609 CD GLU A 240 44. 945 26. 992 29. 735 1. 00 33. 18 ATOM 1610 OE1 GLU A 240 44. 662 25. 782 29. 865 1. 00 37. 45 ATOM 1611 OE2 GLU A 240 45. 973 27. 501 30. 237 1. 00 33. 72 ATOM 1612 C GLU A 240 44. 570 31. 423 30. 363 1. 00 19. 32 ATOM 1613 0 GLU A 240 45. 656 31. 695 30. 871 1. 00 20. 24 ATOM 1614 N ARG A 241 43. 775 32. 337 29. 812 1. 00 17. 22 ATOM 1615 CA ARG A 241 44. 131 33. 751 29. 755 1. 00 17. 57 ATOM 1616 CB ARG A 241 43. 094 34. 509 28. 915 1. 00 15. 94 ATOM 1617 CG ARG A 241 43. 423 35. 971 28. 625 1. 00 16. 24 ATOM 1618 CD ARG A 241 43. 210 36. 882 29. 829 1. 00 13. 73 ATOM 1619 NE ARG A 241 41. 826 36. 914 30. 293 1. 00 15. 88 ATOM 1620 CZ ARG A 241 40. 845 37. 616 29. 726 1. 00 17. 28 ATOM 1621 NH1 ARG A 241 39. 620 37. 568 30. 235 1. 00 15. 42 ATOM 1622 NH2 ARG A 241 41. 082 38. 374 28. 661 1. 00 14. 65 ATOM 1623 C ARG A 241 44. 227 34. 371 31. 150 1. 00 18. 35 ATOM 1624 0 ARG A 241 45. 174 35. 102 31. 442 1. 00 17. 69 ATOM 1625 N ASP A 242 43. 248 34. 082 32. 007 1. 00 19. 04 ATOM 1626 CA ASP A 242 43. 247 34. 631 33. 362 1. 00 19. 06 ATOM 1627 CB ASP A 242 41. 914 34. 344 34. 073 1. 00 18. 23 ATOM 1628 CG ASP A 242 40. 726 35. 019 33. 397 1. 00 20. 68 ATOM 1629 OD1 ASP A 242 40. 913 36. 078 32. 761 1. 00 20. 74 ATOM 1630 OD2 ASP A 242 39. 596 34. 499 33. 516 1. 00 19. 78 ATOM 1631 C ASP A 242 44. 404 34. 085 34. 201 1. 00 18. 63 ATOM 1632 0 ASP A 242 44. 793 34. 695 35. 195 1. 00 18. 12 ATOM 1633 N GLY A 243 44. 952 32. 944 33. 794 1. 00 17. 67 ATOM 1634 CA GLY A 243 46. 061 32. 353 34. 526 1. 00 17. 88 ATOM 1635 C GLY A 243 47. 407 32. 997 34. 216 1. 00 18. 89 ATOM 1636 0 GLY A 243 48. 429 32. 641 34. 807 1. 00 18. 71 ATOM 1637 N LEU A 244 47. 421 33. 945 33. 286 1. 00 18. 25 ATOM 1638 CA LEU A 244 48. 666 34. 622 32. 933 1. 00 19.00 ATOM 1639 CB LEU A 244 48. 613 35. 126 31. 485 1. 00 17. 15 ATOM 1640 CG LEU A 244 48. 385 34. 081 30. 392 1. 00 17. 74 ATOM 1641 CD1 LEU A 244 48. 274 34. 772 29. 044 1. 00 16. 09 ATOM 1642 CD2 LEU A 244 49. 526 33. 074 30. 400 1. 00 18.11

ATOM 1643 C LEU A 244 48.912 35.801 33.868 1.00 18.91 ATOM 1644 0 LEU A 244 47.970 36.388 34.401 1.00 18.13 ATOM 1645 N ARG A 245 50.180 36.143 34. 067 1.00 19.32 ATOM 1646 CA ARG A 245 50.529 37.269 34.924 1.00 20.36 ATOM 1647 CB ARG A 245 52.051 37.346 35.085 1.00 19.37 ATOM 1648 CG ARG A 245 52.601 36.269 36.035 1.00 19.13 ATOM 1649 CD ARG A 245 54.072 35.967 35.805 1.00 18.27 ATOM 1650 NE ARG A 245 54.965 37.032 36.254 1.00 19. 00 ATOM 1651 CZ ARG A 245 55.396 37.178 37.504 1.00 19.64 ATOM 1652 NH1 ARG A 245 56.211 38.181 37.811 1.00 16.23 ATOM 1653 NH2 ARG A 245 55.021 36.318 38.447 1.00 17.19 ATOM 1654 C ARG A 245 49.958 38.569 34.349 1.00 22.32 ATOM 1655 O ARG A 245 49.910 38.758 33.130 1.00 20.59 ATOM 1656 N ARG A 246 49.517 39.446 35.249 1.00 25.41 ATOM 1657 CA ARG A 246 48.906 40.737 34.920 1.00 26.97 ATOM 1658 CB ARG A 246 48.979 41.664 36.137 1.00 30.43 ATOM 1659 CG ARG A 246 48.315 41.093 37.380 1.00 37.76 ATOM 1660 CD ARG A 246 46.792 41.252 37.353 1.00 41. 81 ATOM 1661 NE ARG A 246 46.113 40.366 38.302 1.00 42.05 ATOM 1662 CZ ARG A 246 46.468 40.202 39.573 1.00 40.82 ATOM 1663 NH1 ARG A 246 47.505 40.859 40.073 1.00 40.20 ATOM 1664 NH2 ARG A 246 45.779 39.377 40.348 1.00 41.81 ATOM 1665 C ARG A 246 49.429 41.490 33.698 1.00 26.71 ATOM 1666 0 ARG A 246 48.659 41.784 32.781 1.00 26.44 ATOM 1667 N VAL A 247 50.720 41.816 33.678 1.00 24.35 ATOM 1668 CA VAL A 247 51.268 42.561 32.548 1.00 24.81 ATOM 1669 CB VAL A 247 52.703 43.101 32.853 1.00 26.12 ATOM 1670 CG1 VAL A 247 52.655 44.084 34.018 1.00 23.20 ATOM 1671 CG2 VAL A 247 53.644 41.962 33.171 1.00 26.44 ATOM 1672 C VAL A 247 51.290 41.768 31.244 1.00 24.54 ATOM 1673 0 VAL A 247 51.443 42.341 30.167 1.00 26.25 ATOM 1674 N HIS A 248 51.116 40.453 31.342 1.00 23.59 ATOM 1675 CA HIS A 248 51.123 39.580 30.169 1.00 21.97 ATOM 1676 CB HIS A 248 52.118 38.438 30. 387 1.00 20.64 ATOM 1677 CG HIS A 248 53.536 38.897 30.510 1.00 21.01 ATOM 1678 CD2 HIS A 248 54.312 39.108 31.598 1.00 20.81 ATOM 1679 ND1 HIS A 248 54.293 39.270 29.421 1.00 20.08

ATOM 1680 CE1 HIS A 248 55.474 39.696 29.833 1.00 20.69 ATOM 1681 NE2 HIS A 248 55. 510 39.608 31.150 1.00 21.17 ATOM 1682 C HIS A 248 49.741 38.999 29. 884 1.00 21.65 ATOM 1683 0 HIS A 248 49.620 37.980 29.205 1.00 19.83 ATOM 1684 N ARG A 249 48.705 39.658 30.395 1.00 20.25 ATOM 1685 CA ARG A 249 47.332 39.196 30.219 1.00 21.40 ATOM 1686 CB ARG A 249 46.598 39.334 31.553 1.00 21.77 ATOM 1687 CG ARG A 249 45.363 38.482 31.700 1.00 24.08 ATOM 1688 CD ARG A 249 44.769 38.681 33.090 1.00 25.21 ATOM 1689 NE ARG A 249 45.655 38.177 34.132 1.00 25.36 ATOM 1690 CZ ARG A 249 45.674 38.624 35.384 1.00 26.64 ATOM 1691 NH1 ARG A 249 44.858 39.598 35.760 1.00 26.33 ATOM 1692 NH2 ARG A 249 46.507 38.087 36.265 1.00 27.83 ATOM 1693 C ARG A 249 46.600 39.975 29.113 1.00 21.27 ATOM 1694 O ARG A 249 46.192 41.122 29.304 1.00 21.00 ATOM 1695 N PRO A 250 46.410 39.345 27.941 1.00 19.96 ATOM 1696 CD PRO A 250 46.878 37.994 27. 575 1.00 19.81 ATOM 1697 CA PRO A 250 45.735 39.977 26.807 1.00 19.13 ATOM 1698 CB PRO A 250 46.266 39.185 25.625 1.00 17.18 ATOM 1699 CG PRO A 250 46.263 37.792 26.184 1.00 18.21 ATOM 1700 C PRO A 250 44.208 39.953 26.837 1.00 19.62 ATOM 1701 O PRO A 250 43.587 39.152 27.546 1.00 17.65 ATOM 1702 N ALA A 251 43.616 40.850 26.054 1.00 18.39 ATOM 1703 CA ALA A 251 42.171 40.904 25.918 1.00 17.20 ATOM 1704 CB ALA A 251 41.747 42.226 25.296 1.00 15. 99 ATOM 1705 C ALA A 251 41.874 39.756 24.957 1.00 16.57 ATOM 1706 O ALA A 251 42.723 39.398 24.133 1.00 16.08 ATOM 1707 N VAL A 252 40.691 39.167 25.063 1.00 15.31 ATOM 1708 CA VAL A 252 40.332 38.073 24.176 1.00 15.76 ATOM 1709 CB VAL A 252 40.008 36.787 24.972 1.00 16.54 ATOM 1710 CG1 VAL A 252 39.416 35.731 24.040 1.00 13.14 ATOM 1711 CG2 VAL A 252 41.279 36.254 25.644 1.00 14.05 ATOM 1712 C VAL A 252 39.135 38.434 23.297 1.00 17.13 ATOM 1713 0 VAL A 252 38.062 38.774 23.793 1.00 17.25 ATOM 1714 N LEU A 253 39.337 38.376 21.985 1.00 17.15 ATOM 1715 CA LEU A 253 38.275 38.667 21.033 1.00 16.03 ATOM 1716 CB LEU A 253 38.682 39.802 20.086 1.00 16.00

ATOM 1717 CG LEU A 253 38.871 41.205 20.673 1.00 17.12 ATOM 1718 CD1 LEU A 253 40.194 41.292 21.418 1. 00 18. 46 ATOM 1719 CD2 LEU A 253 38.840 42.222 19.550 1.00 16.89 ATOM 1720 C LEU A 253 37.999 37.406 20.225 1.00 15.90 ATOM 1721 O LEU A 253 38.829 36.497 20.182 1.00 14.68 ATOM 1722 N VAL A 254 36.827 37.355 19.600 1.00 15.02 ATOM 1723 CA VAL A 254 36.428 36.222 18.775 1.00 15.71 ATOM 1724 CB VAL A 254 35.158 35.531 19.351 1.00 17.13 ATOM 1725 CG1 VAL A 254 34.663 34.449 18.404 1.00 17.46 ATOM 1726 CG2 VAL A 254 35.473 34.915 20.706 1.00 16.81 ATOM 1727 C VAL A 254 36.142 36.741 17.367 1.00 15. 10 ATOM 1728 O VAL A 254 35.406 37.704 17.195 1.00 16.08 ATOM 1729 N LYS A 255 36.738 36.116 16.361 1.00 15.28 ATOM 1730 CA LYS A 255 36.521 36.541 14.985 1.00 15.28 ATOM 1731 CB LYS A 255 37.826 36.463 14.186 1.00 14.88 ATOM 1732 CG LYS A 255 37.714 36.994 12.770 1.00 15.89 ATOM 1733 CD LYS A 255 39.092 37.270 12.172 1.00 16.96 ATOM 1734 CE LYS A 255 38.985 37.946 10.804 1.00 15.29 ATOM 1735 NZ LYS A 255 40.316 38.399 10.320 1.00 15.29 ATOM 1736 C LYS A 255 35.458 35.656 14.349 1.00 16.78 ATOM 1737 O LYS A 255 35.611 34.433 14.269 1.00 15.57 ATOM 1738 N ILE A 256 34.384 36.284 13.888 1.00 15.73 ATOM 1739 CA ILE A 256 33.280 35.553 13.295 1.00 15.18 ATOM 1740 CB ILE A 256 31.963 35.924 13.993 1.00 14.40 ATOM 1741 CG2 ILE A 256 32.115 35.716 15.485 1.00 14.47 ATOM 1742 CG1 ILE A 256 31.607 37.387 13.703 1.00 13.65 ATOM 1743 CD1 ILE A 256 30.305 37.857 14.348 1.00 10.70 ATOM 1744 C ILE A 256 33.118 35.758 11.795 1.00 15.17 ATOM 1745 0 ILE A 256 33.677 36.688 11.210 1.00 12.59 ATOM 1746 N ALA A 257 32.340 34.873 11.181 1.00 15.08 ATOM 1747 CA ALA A 257 32.084 34.934 9.750 1.00 18.08 ATOM 1748 CB ALA A 257 31.766 33.533 9.221 1.00 19.52 ATOM 1749 C ALA A 257 30.934 35.881 9.418 1.00 18.32 ATOM 1750 O ALA A 257 30.208 36.344 10.303 1.00 17.66 ATOM 1751 N PRO A 258 30.781 36.206 8.128 1.00 18.01 ATOM 1752 CD PRO A 258 31.867 36.066 7.138 1.00 16.50 ATOM 1753 CA PRO A 258 29.732 37.089 7.615 1.00 18.62

ATOM 1754 CB PRO A 258 30.449 37.850 6.515 1.00 16.96 ATOM 1755 CG PRO A 258 31.298 36.776 5.918 1.00 16.10 ATOM 1756 C PRO A 258 28.578 36.248 7.057 1.00 21.75 ATOM 1757 0 PRO A 258 27.619 36.785 6.498 1.00 23.00 ATOM 1758 N ASP A 259 28.682 34.930 7.218 1.00 20.77 ATOM 1759 CA ASP A 259 27.675 34.007 6.705 1.00 22.20 ATOM 1760 CB ASP A 259 28.355 32.919 5.867 1.00 20.49 ATOM 1761 CG ASP A 259 29.382 33.485 4.900 1.00 22.19 ATOM 1762 OD1 ASP A 259 29.043 34.442 4.170 1.00 19.06 ATOM 1763 OD2 ASP A 259 30.524 32.970 4.868 1.00 21.62 ATOM 1764 C ASP A 259 26.849 33.351 7.808 1.00 23.62 ATOM 1765 O ASP A 259 26.272 32.286 7.606 1.00 25.15 ATOM 1766 N LEU A 260 26.787 33.991 8.969 1.00 23.63 ATOM 1767 CA LEU A 260 26.039 33.454 10.097 1.00 22.23 ATOM 1768 CB LEU A 260 26.549 34.075 11.400 1.00 22.52 ATOM 1769 CG LEU A 260 28.015 33.815 11.761 1.00 23.59 ATOM 1770 CD1 LEU A 260 28.418 34.668 12.958 1.00 25.06 ATOM 1771 CD2 LEU A 260 28.205 32.341 12.063 1.00 21.98 ATOM 1772 C LEU A 260 24.544 33.715 9.973 1.00 22.15 ATOM 1773 0 LEU A 260 24.131 34.749 9.454 1.00 23.71 ATOM 1774 N THR A 261 23.736 32.769 10.444 1.00 20.79 ATOM 1775 CA THR A 261 22.285 32.926 10.419 1.00 19.86 ATOM 1776 CB THR A 261 21.556 31.590 10.694 1.00 19.22 ATOM 1777 OG1 THR A 261 21.909 31.118 12.003 1.00 18.63 ATOM 1778 CG2 THR A 261 21.933 30.539 9.661 1.00 12.85 ATOM 1779 C THR A 261 21.946 33.876 11.567 1.00 22.13 ATOM 1780 0 THR A 261 22.800 34.166 12.407 1.00 23.22 ATOM 1781 N SER A 262 20.712 34.364 11.611 1.00 22.17 ATOM 1782 CA SER A 262 20.316 35.256 12.696 1.00 22.97 ATOM 1783 CB SER A 262 18.886 35.748 12.484 1.00 22.97 ATOM 1784 OG SER A 262 18.791 36.509 11.298 1.00 26.68 ATOM 1785 C SER A 262 20.413 34.521 14.036 1.00 23.06 ATOM 1786 0 SER A 262 20.653 35.136 15.075 1.00 22.02 ATOM 1787 N GLN A 263 20.227 33.204 14.004 1.00 22.11 ATOM 1788 CA GLN A 263 20.297 32.393 15.215 1.00 23.04 ATOM 1789 CB GLN A 263 19.794 30.974 14.935 1.00 24.15 ATOM 1790 CG GLN A 263 19.870 30.039 16.136 1.00 30.55

ATOM 1791 CD GLN A 263 18.717 30.225 17.108 1.00 32.21 ATOM 1792 OE1 GLN A 263 17.581 29.856 16.815 1.00 33.90 ATOM 1793 NE2 GLN A 263 19.005 30.805 18.267 1.00 33.03 ATOM 1794 C GLN A 263 21.727 32.331 15.753 1.00 21.52 ATOM 1795 O GLN A 263 21.951 32.483 16.956 1.00 21.15 ATOM 1796 N ASP A 264 22.692 32.109 14.863 1.00 20.97 ATOM 1797 CA ASP A 264 24.090 32.034 15.272 1.00 19.77 ATOM. 1798 CB ASP A 264 25.007 31.755 14.076 1.00 22.91 ATOM 1799 CG ASP A 264 24.750 30.398 13.437 1.00 25.44 ATOM 1800 OD1 ASP A 264 24.364 29.457 14.163 1.00 23.04 ATOM 1801 OD2 ASP A 264 24.952 30.276 12.206 1.00 26.99 ATOM 1802 C ASP A 264 24.530 33.330 15.931 1.00 18.65 ATOM 1803 0 ASP A 264 25.201 33.315 16.962 1.00 18.71 ATOM 1804 N LYS A 265 24.149 34.453 15.333 1.00 17.32 ATOM 1805 CA LYS A 265 24.514 35.754 15.868 1.00 19.13 ATOM 1806 CB LYS A 265 24.063 36.860 14.915 1.00 19.32 ATOM 1807 CG LYS A 265 24.772 36.820 13.573 1.00 19.57 ATOM 1808 CD LYS A 265 24.127 37.779 12.589 1.00 23.29 ATOM 1809 CE LYS A 265 24.425 37.366 11.160 1.00 24.36 ATOM 1810 NZ LYS A 265 23.497 38.006 10.187 1.00 27.53 ATOM 1811 C LYS A 265 23.927 35.971 17.253 1.00 20.16 ATOM 1812 O LYS A 265 24.611 36.473 18.144 1.00 21.28 ATOM 1813 N GLU A 266 22.661 35.598 17.434 1.00 20.98 ATOM 1814 CA GLU A 266 22.014 35.734 18.736 1.00 20.75 ATOM 1815 CB GLU A 266 20.558 35.247 18.677 1.00 20.43 ATOM 1816 CG GLU A 266 19.640 36.121 17.839 1.00 25.19 ATOM 1817 CD GLU A 266 18.213 35.587 17.743 1.00 26.74 ATOM 1818 OE1 GLU A 266 17.414 36.194 17.003 1.00 28.84 ATOM 1819 OE2 GLU A 266 17.886 34.573 18.399 1.00 27.22 ATOM 1820 C GLU A 266 22.787 34.905 19.763 1.00 19.77 ATOM 1821 0 GLU A 266 23.080 35.378 20.858 1.00 17.93 ATOM 1822 N ASP A 267 23.120 33.668 19.400 1.00 20.25 ATOM 1823 CA ASP A 267 23.854 32.790 20.305 1.00 21.56 ATOM 1824 CB ASP A 267 24.000 31.385 19.707 1.00 22.05 ATOM 1825 CG ASP A 267 22.674 30.651 19.611 1.00 25.11 ATOM 1826 OD1 ASP A 267 21.737 31.015 20.353 1.00 24.11 ATOM 1827 OD2 ASP A 267 22.570 29.701 18.803 1.00 26.91

ATOM 1828 C ASP A 267 25.229 33.352 20.640 1.00 21.65 ATOM 1829 0 ASP A 267 25.618 33.404 21.808 1.00 22.61 ATOM 1830 N ILE A 268 25.965 33.776 19.619 1.00 20.24 ATOM 1831 CA ILE A 268 27.287 34.336 19.843 1.00 19.65 ATOM 1832 CB ILE A 268 27.949 34.762 18.517 1.00 19.77 ATOM 1833 CG2 ILE A 268 29.181 35.615 18.796 1.00 18.25 ATOM 1834 CG1 ILE A 268 28.312 33.516 17.706 1.00 20.48 ATOM 1835 CD1 ILE A 268 28.903 33.813 16.347 1.00 21.71 ATOM 1836 C ILE A 268 27.209 35.538 20.774 1.00 18.66 ATOM 1837 O ILE A 268 28.037 35.689 21.671 1.00 18.66 ATOM 1838 N ALA A 269 26.208 36.386 20.567 1.00 18.12 ATOM 1839 CA ALA A 269 26.042 37.573 21.401 1.00 19.02 ATOM 1840 CB ALA A 269 24.906 38.429 20.872 1.00 17.83 ATOM 1841 C ALA A 269 25.760 37.165 22.842 1.00 19.92 ATOM 1842 O ALA A 269 26.246 37.785 23.786 1.00 19.07 ATOM 1843 N SER A 270 24.971 36.108 22.998 1.00 20.50 ATOM 1844 CA SER A 270 24.616 35.604 24.314 1.00 20.79 ATOM 1845 CB SER A 270 23.528 34.536 24.175 1.00 20.34 ATOM 1846 OG SER A 270 23.261 33.914 25.417 1.00 22.74 ATOM 1847 C SER A 270 25.837 35.031 25.039 1.00 20.69 ATOM 1848 O SER A 270 26.084 35.356 26.198 1.00 22.32 ATOM 1849 N VAL A 271 26.596 34.178 24.358 1.00 20.01 ATOM 1850 CA VAL A 271 27.786 33.578 24.955 1.00 20.35 ATOM 1851 CB VAL A 271 28.435 32.556 23.998 1.00 19.34 ATOM 1852 CG1 VAL A 271 29.753 32.056 24.584 1.00 19.49 ATOM 1853 CG2 VAL A 271 27.491 31.390 23.767 1.00 15.58 ATOM 1854 C VAL A 271 28.819 34.649 25.308 1.00 22.65 ATOM 1855 0 VAL A 271 29.420 34.621 26.382 1.00 21.15 ATOM 1856 N VAL A 272 29.015 35.597 24.398 1.00 24.64 ATOM 1857 CA VAL A 272 29.968 36.677 24.609 1.00 26.34 ATOM 1858 CB VAL A 272 29.957 37.656 23.411 1.00 27.45 ATOM 1859 CG1 VAL A 272 30.522 39.005 23.824 1.00 27.55 ATOM 1860 CG2 VAL A 272 30.780 37.070 22.264 1.00 25.36 ATOM 1861 C VAL A 272 29.691 37.446 25.897 1.00 27.85 ATOM 1862 O VAL A 272 30.610 37.748 26.662 1.00 28.31 ATOM 1863 N LYS A 273 28.424 37.750 26.146 1.00 28.61 ATOM 1864 CA LYS A 273 28.054 38.491 27.345 1.00 30.76

ATOM 1865 CB LYS A 273 26.695 39.173 27. 137 1.00 31. 43 ATOM 1866 CG LYS A 273 26.759 40.293 26.087 1.00 34. 55 ATOM 1867 CD LYS A 273 25.463 41.089 25.987 1.00 36. 45 ATOM 1868 CE LYS A 273 24.312 40.229 25.501 1.00 36.17 ATOM 1869 NZ LYS A 273 23.073 41.031 25.320 1.00 38. 03 ATOM 1870 C LYS A 273 28.042 37.615 28.595 1.00 30.26 'ATOM 1871 O LYS A 273 28.295 38.091 29.701 1.00 30. 38 ATOM 1872 N GLU A 274 27.765 36.331 28.414 1.00 29. 22 ATOM 1873 CA GLU A 274 27.745 35.396 29.527 1.00 28.71 ATOM 1874 CB GLU A 274 27.184 34.051 29. 064 1.00 29.65 ATOM 1875 CG GLU A 274 27.100 32.996 30.152 1.00 34. 63 ATOM 1876 CD GLU A 274 27.077 31.583 29.590 1.00 37.55 ATOM 1877 OE1 GLU A 274 26.405 31.360 28.562 1.00 38.36 ATOM 1878 OE2 GLU A 274 27.727 30.691 30.180 1.00 40.62 ATOM 1879 C GLU A 274 29.159 35.179 30.084 1.00 29.15 ATOM 1880 0 GLU A 274 29.361 35.158 31.300 1.00 28.97 ATOM 1881 N LEU A 275 30.135 35.032 29.185 1.00 26.95 ATOM 1882 CA LEU A 275 31.522 34.772 29.575 1.00 24.76 ATOM 1883 CB LEU A 275 32.181 33.842 28.556 1.00 22.52 ATOM 1884 CG LEU A 275 31.494 32.500 28.313 1.00 22.79 ATOM 1885 CD1 LEU A 275 32.250 31.719 27.247 1.00 21. 36 ATOM 1886 CD2 LEU A 275 31.436 31.721 29.617 1.00 22.41 ATOM 1887 C LEU A 275 32.413 35.992 29.761 1.00 24.23 ATOM 1888 O LEU A 275 33.522 35.874 30.276 1.00 25.42 ATOM 1889 N GLY A 276 31.944 37.158 29.338 1.00 24.12 ATOM 1890 CA GLY A 276 32.758 38.351 29.479 1.00 22.44 ATOM 1891 C GLY A 276 33.796 38.517 28.378 1.00 23.67 ATOM 1892 0 GLY A 276 34.851 39.110 28.605 1.00 23.44 ATOM 1893 N ILE A 277 33.515 37.992 27.186 1.00 23.83 ATOM 1894 CA ILE A 277 34.440 38.134 26.062 1.00 22.17 ATOM 1895 CB ILE A 277 33.829 37.586 24.754 1.00 22.72 ATOM 1896 CG2 ILE A 277 34.746 37.888 23.577 1.00 21. 72 ATOM 1897 CG1 ILE A 277 33.635 36.077 24.871 1.00 22. 65 ATOM 1898 CD1 ILE A 277 34.926 35.332 25.123 1.00 26.25 ATOM 1899 C ILE A 277 34.735 39.623 25.899 1.00 22.15 ATOM 1900 0 ILE A 277 33.828 40.456 25.949 1.00 20.17 ATOM 1901 N ASP A 278 36.006 39.953 25.701 1.00 20.80

ATOM 1902 CA ASP A 278 36.431 41.340 25.578 1.00 19.25 ATOM 1903 CB ASP A 278 37.945 41.421 25.753 1.00 18.89 ATOM 1904 CG ASP A 278 38.392 40.898 27.094 1.00 18.41 ATOM 1905 OD1 ASP A 278 37.974 41.485 28.115 1.00 20.16 ATOM 1906 OD2 ASP A 278 39.147 39.903 27.131 1.00 17.97 ATOM 1907 C ASP A 278 36.029 42.062 24.303 1.00 19.25 ATOM 1908 0 ASP A 278 35.907 43.286 24.299 1.00 20.39 ATOM 1909 N GLY A 279 35.825 41.320 23.221 1.00 17.95 ATOM 1910 CA GLY A 279 35.451 41.970 21.981 1.00 16.99 ATOM 1911 C GLY A 279 35.229 41.038 20.812 1.00 16.55 ATOM 1912 0 GLY A 279 35.455 39.833 20.902 1.00 16.99 ATOM 1913 N LEU A 280 34.788 41.613 19.700 1.00 16.23 ATOM 1914 CA LEU A 280 34.515 40.848 18.495 1.00 16.29 ATOM 1915 CB LEU A 280 33.006 40.804 18.222 1.00 14.21 ATOM 1916 CG LEU A 280 32.071 40.069 19.187 1.00 16.53 ATOM 1917 CD1 LEU A 280 30.623 40.395 18.840 1.00 14.51 ATOM 1918 CD2 LEU A 280 32.315 38.568 19.110 1.00 14.28 ATOM 1919 C LEU A 280 35.197 41.457 17.283 1.00 15.25 ATOM 1920 O LEU A 280 35.274 42.681 17.145 1.00 14.60 ATOM 1921 N ILE A 281 35.718 40.596 16.420 1.00 13.70 ATOM 1922 CA ILE A 281 36.325 41.051 15.186 1.00 14.56 ATOM 1923 CB ILE A 281 37.675 40.382 14.911 1.00 12.34 ATOM 1924 CG2 ILE A 281 38.259 40.937 13.619 1.00 12.73 ATOM 1925 CG1 ILE A 281 38.640 40.684 16.065 1.00 11.34 ATOM 1926 CD1 ILE A 281 40.103 40.703 15.660 1.00 9.52 ATOM 1927 C ILE A 281 35.264 40.584 14.213 1.00 16.31 ATOM 1928 0 ILE A 281 35.038 39.382 14.036 1.00 15.34 ATOM 1929 N VAL A 282 34.584 41.535 13.590 1.00 18.61 ATOM 1930 CA VAL A 282 33.493 41.138 12.738 1.00 20.29 ATOM 1931 CB VAL A 282 32.273 42.022 13.010 1.00 19.32 ATOM 1932 CG1 VAL A 282 31.089 41.577 12.175 1.00 15.46 ATOM 1933 CG2 VAL A 282 31.931 41.917 14.484 1.00 14.77 ATOM 1934 C VAL A 282 33.718 40.940 11.257 1.00 23.76 ATOM 1935 0 VAL A 282 34.031 41.849 10.483 1.00 21.79 ATOM 1936 N THR A 283 33.500 39.669 10.937 1.00 26.44 ATOM 1937 CA THR A 283 33.591 38.994 9.657 1.00 24.63 ATOM 1938 CB THR A 283 32.573 39.520 8.593 1.00 22.04

ATOM 1939 OG1 THR A 283 33.276 39.969 7.431 1.00 20.72 ATOM 1940 CG2 THR A 283 31.680 40.606 9.165 1.00 24.57 ATOM 1941 C THR A 283 34.939 38.783 9.006 1.00 23.16 ATOM 1942 0 THR A 283 35.758 39.683 8.794 1.00 22.01 ATOM 1943 N ASN A 284 35.133 37.504 8.741 1.00 19.80 ATOM 1944 CA ASN A 284 36.279 36.955 8.085 1.00 17.61 ATOM 1945 CB ASN A 284 36.417 35.497 8.515 1.00 15.52 ATOM 1946 CG ASN A 284 37.812 34.981 8.365 1.00 14.49 ATOM 1947 OD1 ASN A 284 38.384 35.036 7.285 1.00 15.69 ATOM 1948 ND2 ASN A 284 38.375 34.467 9.453 1.00 14.96 ATOM 1949 C ASN A 284 35.796 37.043 6.641 1.00 16.90 ATOM 1950 0 ASN A 284 34.917 37.850 6.326 1.00 17.24 ATOM 1951 N THR A 285 36.344 36.214 5.766 1.00 15.67 ATOM 1952 CA THR A 285 35.914 36.225 4.377 1.00 14.29 ATOM 1953 CB THR A 285 36.971 35.569 3.468 1.00 13.61 ATOM 1954 OG1 THR A 285 37.347 34.296 4.012 1.00 11.23 ATOM 1955 CG2 THR A 285 38.206 36.462 3.366 1.00 10.88 ATOM 1956 C THR A 285 34.593 35.461 4.274 1.00 14.86 ATOM 1957 0 THR A 285 34.238 34.697 5.176 1.00 12.89 ATOM 1958 N THR A 286 33.868 35.676 3.179 1.00 14.02 ATOM 1959 CA THR A 286 32.582 35.016 2.960 1.00 11.85 ATOM 1960 CB THR A 286 31.533 36.015 2.411 1.00 9.54 ATOM 1961 OG1 THR A 286 30.298 35.335 2.179 1.00 12.88 ATOM 1962 CG2 THR A 286 32.000 36.614 1.091 1.00 8.80 ATOM 1963 C THR A 286 32.682 33.861 1.964 1.00 12.60 ATOM 1964 0 THR A 286 33.413 33.953 0.970 1.00 11.62 ATOM 1965 N VAL A 287 31.951 32.778 2.230 1.00 12.37 ATOM 1966 CA VAL A 287 31.939 31.636 1.320 1.00 14.81 ATOM 1967 CB VAL A 287 31.725 30.281 2.047 1.00 15.55 ATOM 1968 CG1 VAL A 287 32.846 30.035 3.035 1.00 16.38 ATOM 1969 CG2 VAL A 287 30.372 30.261 2.748 1.00 16.45 ATOM 1970 C VAL A 287 30.789 31.844 0.336 1.00 16.38 ATOM 1971 0 VAL A 287 30.525 31.001-0. 521 1.00 16.63 ATOM 1972 N SER A 288 30.096 32.969 0.473 1.00 15.25 ATOM 1973 CA SER A 288 29.001 33.278-0. 433 1.00 15.37 ATOM 1974 CB SER A 288 28.026 34.275 0.202 1.00 14.24 ATOM 1975 OG SER A 288 28.580 35.583 0.215 1.00 13. 66

ATOM 1976 C SER A 288 29.620 33.910-1. 672 1.00 15.99 ATOM 1977 0 SER A 288 30.772 34.339-1. 653 1.00 15.45 ATOM 1978 N ARG A 289 28.848 33. 965-2. 749 1.00 17.27 ATOM 1979 CA ARG A 289 29.312 34.562-3. 992 1.00 19.15 ATOM 1980 CB ARG A 289 29.620 33.473-5. 022 1.00 18.24 ATOM 1981 CG ARG A 289 30. 830 32.621-4. 669 1.00 18.25 ATOM 1982 CD ARG A 289 32.121 33.425-4. 740 1.00 16.51 ATOM 1983 NE ARG A 289 33.291 32.580-4. 521 1.00 15.70 ATOM 1984 CZ ARG A 289 33.785 32.259-3. 328 1.00 15.56 ATOM 1985 NH1 ARG A 289 34.850 31.469-3. 246 1.00 12.48 ATOM 1986 NH2 ARG A 289 33.230 32.736-2. 219 1.00 13.20 ATOM 1987 C ARG A 289 28.198 35.472-4. 488 1.00 20.73 ATOM 1988 0 ARG A 289 27.361 35.073-5. 305 1.00 21.86 ATOM 1989 N PRO A 290 28.172 36.714-3. 985 1.00 19.73 ATOM 1990 CD PRO A 290 29.204 37.305-3. 117 1.00 17.99 ATOM 1991 CA PRO A 290 27.165 37.710-4. 349 1.00 18.33 ATOM 1992 CB PRO A 290 27.754 39.008-3. 799 1.00 18.12 ATOM 1993 CG PRO A 290 28.512 38.545-2. 599 1.00 16.66 ATOM 1994 C PRO A 290 26.952 37.769-5. 850 1.00 18.94 ATOM 1995 0 PRO A 290 27.910 37.702-6. 623 1.00 19.73 ATOM 1996 N ALA A 291 25.694 37.876-6. 267 1.00 18.87 ATOM 1997 CA ALA A 291 25.392 37.974-7. 691 1.00 16.81 ATOM 1998 CB ALA A 291 23.890 38.075-7. 905 1.00 14.68 ATOM 1999 C ALA A 291 26.082 39.244-8. 191 1.00 15.05 ATOM 2000 0 ALA A 291 26.121 40.247-7. 484 1.00 15.36 ATOM 2001 N GLY A 292 26.640 39.196-9. 394 1.00 13.71 ATOM 2002 CA GLY A 292 27.302 40.370-9. 925 1.00 14.53 ATOM 2003 C GLY A 292 28.803 40.235-10. 097 1.00 15.49 ATOM 2004 0 GLY A 292 29.400 40.997-10. 857 1.00 17.37 ATOM 2005 N LEU A 293 29.422 39.291-9. 392 1.00 14.91 ATOM 2006 CA LEU A 293 30.862 39.082-9. 521 1.00 15.19 ATOM 2007 CB LEU A 293 31.304 37.838-8. 746 1.00 15.22 ATOM 2008 CG LEU A 293 31.184 37.854-7. 218 1.00 13.79 ATOM 2009 CD1 LEU A 293 31.680 36.528-6. 668 1.00 13.53 ATOM 2010 CD2 LEU A 293 31.997 39.001-6. 637 1.00 11.50 ATOM 2011 C LEU A 293 31.199 38.904-10. 994 1.00 15.17 ATOM 2012 O LEU A 293 30.523 38.162-11. 708 1.00 16.42

ATOM 2013 N GLN A 294 32.243 39.589-11. 446 1.00 16.27 ATOM 2014 CA GLN A 294 32.660 39.517-12. 838 1.00 16.80 ATOM 2015 CB GLN A 294 32. 865 40.929-13. 391 1.00 17.50 ATOM 2016 CG GLN A 294 31.593 41.745-13. 445 1.00 18.23 ATOM 2017 CD GLN A 294 30.511 41.048-14. 238 1.00 18. 91 ATOM 2018 OE1 GLN A 294 30.707 40.720-15. 404 1.00 20.05 ATOM 2019 NE2 GLN A 294 29.362 40.812-13. 607 1.00 16. 51 ATOM 2020 C GLN A 294 33.936 38.712-13. 038 1.00 18.25 ATOM 2021 O GLN A 294 34.154 38.143-14. 111 1.00 18.99 ATOM 2022 N GLY A 295 34.774 38.675-12. 004 1.00 16.83 ATOM 2023 CA GLY A 295 36.029 37. 954-12. 083 1.00 15.09 ATOM 2024 C GLY A 295 35.916 36.574-12. 704 1.00 17.40 ATOM 2025 0 GLY A 295 34.975 35.823-12. 431 1.00 15.89 ATOM 2026 N ALA A 296 36.884 36.238-13. 546 1.00 16.27 ATOM 2027 CA ALA A 296 36.894 34.936-14. 201 1.00 17.04 ATOM 2028 CB ALA A 296 38.046 34.870-15. 208 1.00 14.05 ATOM 2029 C ALA A 296 37.030 33.808-13. 179 1.00 16.37 ATOM 2030 O ALA A 296 36.512 32.709-13. 383 1.00 17.15 ATOM 2031 N LEU A 297 37.710 34.098-12. 072 1.00 16.31 ATOM 2032 CA LEU A 297 37.964 33.113-11. 019 1.00 14.92 ATOM 2033 CB LEU A 297 39.375 33.333-10. 467 1.00 12.34 ATOM 2034 CG LEU A 297 40.466 33.409-11. 544 1.00 14.84 ATOM 2035 CD1 LEU A 297 41.782 33.872-10. 924 1.00 14.02 ATOM 2036 CD2 LEU A 297 40.625 32.047-12. 216 1.00 12.49 ATOM 2037 C LEU A 297 36.962 33.148-9. 867 1.00 14.64 ATOM 2038 O LEU A 297 37.247 32.650-8. 774 1.00 14.34 ATOM 2039 N ARG A 298 35.789 33.722-10. 122 1.00 15.32 ATOM 2040 CA ARG A 298 34.742 33.858-9. 109 1.00 15.13 ATOM 2041 CB ARG A 298 33.557 34.642-9. 687 1.00 14.29 ATOM 2042 CG ARG A 298 32.751 33.880-10. 727 1.00 14.22 ATOM 2043 CD ARG A 298 31.674 34.763-11. 358 1.00 14.90 ATOM 2044 NE ARG A 298 30.796 33.992-12. 234 1.00 14.82 ATOM 2045 CZ ARG A 298 29.930 34.523-13. 094 1.00 15.76 ATOM 2046 NH1 ARG A 298 29.177 33.731-13. 845 1.00 9.49 ATOM 2047 NH2 ARG A 298 29.823 35.844-13. 213 1.00 14.55 ATOM 2048 C ARG A 298 34.230 32.544-8. 517 1.00 15.68 ATOM 2049 O ARG A 298 33.714 32.527-7. 397 1.00 15.39

ATOM 2050 N SER A 299 34.367 31. 448-9. 259 1.00 15.50 ATOM 2051 CA SER A 299 33.893 30.160-8. 773 1.00 16.47 ATOM 2052 CB SER A 299 33.196 29.397-9. 898 1.00 15.50 ATOM 2053 OG SER A 299 31.911 29.949-10. 126 1.00 15.72 ATOM 2054 C SER A 299 34.951 29.280-8. 117 1.00 17.56 ATOM 2055 0 SER A 299 34.733 28.085-7. 916 1.00 19.41 ATOM 2056 N GLU A 300 36.095 29.869-7. 786 1.00 15.71 ATOM 2057 CA GLU A 300 37.151 29.135-7. 100 1.00 16.76 ATOM 2058 CB GLU A 300 38.469 29.926-7. 116 1.00 15.74 ATOM 2059 CG GLU A 300 39.165 29.978-8. 471 1.00 18.89 ATOM 2060 CD GLU A 300 39.888 28.684-8. 808 1.00 19.42 ATOM 2061 OE1 GLU A 300 40.297 28.509-9. 975 1.00 21.22 ATOM 2062 OE2 GLU A 300 40.057 27.844-7. 902 1.00 20.90 ATOM 2063 C GLU A 300 36.700 28.958-5. 648 1.00 17.51 ATOM 2064 0 GLU A 300 36.012 29.818-5. 087 1.00 18.05 ATOM 2065 N THR A 301 37.080 27.838-5. 050 1.00 16.82 ATOM 2066 CA THR A 301 36.744 27.556-3. 664 1.00 15.60 ATOM 2067 CB THR A 301 37.055 26.084-3. 318 1.00 15.47 ATOM 2068 OG1 THR A 301 36.037 25.241-3. 867 1.00 18.75 ATOM 2069 CG2 THR A 301 37.132 25.886-1. 816 1.00 13.34 ATOM 2070 C THR A 301 37.571 28.462-2. 753 1.00 14.33 ATOM 2071 0 THR A 301 38.739 28.735-3. 034 1.00 13.01 ATOM 2072 N GLY A 302 36.968 28.929-1. 663 1.00 14.07 ATOM 2073 CA GLY A 302 37.697 29.783-0. 743 1.00 13.12 ATOM 2074 C GLY A 302 36.880 30.929-0. 186 1.00 14.13 ATOM 2075 0 GLY A 302 35.687 31.054-0. 468 1.00 13.77 ATOM 2076 N GLY A 303 37.529 31.764 0.619 1.00 14.37 ATOM 2077 CA GLY A 303 36.855 32.902 1.210 1.00 12.82 ATOM 2078 C GLY A 303 37.024 34.135 0.347 1.00 12.16 ATOM 2079 0 GLY A 303 38.127 34.440-0. 105 1.00 12.51 ATOM 2080 N LEU A 304 35.921 34.842 0.122 1.00 12.72 ATOM 2081 CA LEU A 304 35.916 36.049-0. 694 1.00 11.93 ATOM 2082 CB LEU A 304 34.591 36.149-1. 457 1.00 13.90 ATOM 2083 CG LEU A 304 34.302 37.429-2. 248 1.00 16.01 ATOM 2084 CD1 LEU A 304 35.263 37.557-3. 414 1.00 16.08 ATOM 2085 CD2 LEU A 304 32.865 37.382-2. 756 1.00 20.99 ATOM 2086 C LEU A 304 36.110 37.295 0.162 1.00 12.47

ATOM 2087 0 LEU A 304 35. 500 37.438 1.225 1.00 13.78 ATOM 2088 N SER A 305 36.957 38.199-0. 313 1.00 12.54 ATOM 2089 CA SER A 305 37.239 39.434 0.402 1.00 13.57 ATOM 2090 CB SER A 305 38.617 39.349 1.056 1.00 13.12 ATOM 2091 OG SER A 305 39.626 39.209 0.068 1.00 13.73 ATOM 2092 C SER A 305 37.201 40.615-0. 563 1.00 13.51 ATOM 2093 O SER A 305 37.114 40.428-1. 775 1.00 14.24 ATOM 2094 N GLY A 306 37.273 41.829-0. 026 1.00 13.39 ATOM 2095 CA GLY A 306 37.250 43.002-0. 884 1.00 13.15 ATOM 2096 C GLY A 306 35.896 43.685-0. 937 1.00 15.03 ATOM 2097 0 GLY A 306 35.028 43.435-0. 096 1.00 14.92 ATOM 2098 N LYS A 307 35.704 44.532-1. 944 1.00 16.11 ATOM 2099 CA LYS A 307 34.461 45.281-2. 089 1.00 16.67 ATOM 2100 CB LYS A 307 34.479 46.114-3. 385 1.00 18.76 ATOM 2101 CG LYS A 307 33.436 47.248-3. 381 1.00 25.21 ATOM 2102 CD LYS A 307 33.375 48.040-4. 692 1.00 28.15 ATOM 2103 CE LYS A 307 34.659 48.824-4. 944 1.00 29.58 ATOM 2104 NZ LYS A 307 35.009 49.744-3. 819 1.00 29.15 ATOM 2105 C LYS A 307 33.173 44.458-2. 014 1.00 15.62 ATOM 2106 0 LYS A 307 32.211 44.872-1. 365 1.00 16.68 ATOM 2107 N PRO A 308 33.129 43.285-2. 670 1.00 14.78 ATOM 2108 CD PRO A 308 34.126 42.668-3. 562 1.00 14.76 ATOM 2109 CA PRO A 308 31.905 42.473-2. 617 1.00 14.19 ATOM 2110 CB PRO A 308 32.261 41.252-3. 466 1.00 14.85 ATOM 2111 CG PRO A 308 33.257 41.804-4. 452 1.00 15.81 ATOM 2112 C PRO A 308 31.492 42.079-1. 198 1.00 15.30 ATOM 2113 0 PRO A 308 30.324 41.786-0. 941 1.00 16.37 ATOM 2114 N LEU A 309 32.454 42.072-0. 281 1.00 15.32 ATOM 2115 CA LEU A 309 32.202 41.706 1.111 1.00 15.37 ATOM 2116 CB LEU A 309 33.434 40.995 1.682 1.00 13.97 ATOM 2117 CG LEU A 309 33.538 40.793 3.201 1.00 12.70 ATOM 2118 CD1 LEU A 309 32.468 39.821 3.683 1.00 12.47 ATOM 2119 CD2 LEU A 309 34.920 40.250 3.541 1.00 11.41 ATOM 2120 C LEU A 309 31.855 42.887 2.023 1.00 16.22 ATOM 2121 0 LEU A 309 31.211 42.707 3.056 1.00 17.60 ATOM 2122 N ARG A 310 32.269 44.087 1.632 1.00 14.52 ATOM 2123 CA ARG A 310 32.076 45.283 2.448 1.00 15.17

ATOM 2124 CB ARG A 310 32.323 46. 548 1.614 1.00 12.82 ATOM 2125 CG ARG A 310 32.391 47.825 2.458 1.00 14.88 ATOM 2126 CD ARG A 310 32.530 49.062 1.582 1.00 12.41 ATOM 2127 NE ARG A 310 31.453 49.099 0.600 1.00 14.40 ATOM 2128 CZ ARG A 310 31.454 49.851-0. 492 1.00 12.91 ATOM 2129 NH1 ARG A 310 30.422 49.797-1. 323 1.00 10.64 ATOM 2130 NH2 ARG A 310 32.482 50.652-0. 753 1.00 12.19 ATOM 2131 C ARG A 310 30.766 45.448 3.214 1.00 16.11 ATOM 2132 0 ARG A 310 30.753 45.395 4.444 1.00 17.04 ATOM 2133 N ASP A 311 29.668 45.663 2.499 1.00 17.60 ATOM 2134 CA ASP A 311 28.385 45.880 3.153 1.00 17.43 ATOM 2135 CB ASP A 311 27.374 46.374 2.117 1.00 18.97 ATOM 2136 CG ASP A 311 27.651 47.817 1.689 1.00 20.40 ATOM 2137 OD1 ASP A 311 28.760 48.320 1.985 1.00 19.94 ATOM 2138 OD2 ASP A 311 26.774 48.447 1.060 1.00 19.67 ATOM 2139 C ASP A 311 27.855 44.688 3.945 1.00 18.29 ATOM 2140 0 ASP A 311 27.188 44.862 4.969 1.00 17.82 ATOM 2141 N LEU A 312 28.156 43.480 3.485 1.00 17.49 ATOM 2142 CA LEU A 312 27.734 42.290 4.204 1.00 17.70 ATOM 2143 CB LEU A 312 28.172 41.033 3.451 1.00 18.87 ATOM 2144 CG LEU A 312 27.778 39.688 4.066 1.00 23.26 ATOM 2145 CD1 LEU A 312 26.260 39.596 4.183 1.00 22.82 ATOM 2146 CD2 LEU A 312 28.312 38.549 3.193 1.00 23.37 ATOM 2147 C LEU A 312 28.409 42.349 5.578 1.00 17.59 ATOM 2148 0 LEU A 312 27.818 41.959 6.588 1.00 16.95 ATOM 2149 N SER A 313 29.646 42.851 5.607 1.00 16.39 ATOM 2150 CA SER A 313 30.405 42.992 6.853 1.00 16.85 ATOM 2151 CB SER A 313 31.869 43.359 6.575 1.00 17.49 ATOM 2152 OG SER A 313 32.646 42.218 6.280 1.00 23.42 ATOM 2153 C SER A 313 29.811 44.079 7.736 1.00 15.83 ATOM 2154 0 SER A 313 29.612 43.878 8.936 1.00 16.72 ATOM 2155 N THR A 314 29.549 45.236 7.136 1.00 13.67 ATOM 2156 CA THR A 314 28.989 46.362 7.866 1.00 13.92 ATOM 2157 CB THR A 314 28.752 47.567 6.938 1.00 13.42 ATOM 2158 OG1 THR A 314 29.990 47.938 6.323 1.00 13.10 ATOM 2159 CG2 THR A 314 28.215 48.748 7.726 1.00 11.72 ATOM 2160 C THR A 314 27.678 45.978 8.534 1.00 14.57

ATOM 2161 0 THR A 314 27.453 46.317 9.693 1.00 16.40 ATOM 2162 N GLN A 315 26.823 45.259 7.811 1.00 14.98 ATOM 2163 CA GLN A 315 25.546 44.836 8.371 1.00 14.55 ATOM 2164 CB GLN A 315 24.656 44.215 7.288 1.00 13.68 ATOM 2165 CG GLN A 315 24.143 45.209 6.244 1.00 14.38 ATOM 2166 CD GLN A 315 23.178 46.249 6.821 1.00 14.67 ATOM 2167 OE1 GLN A 315 23.518 46.986 7.743 0.50 13.22 ATOM 2168 NE2 GLN A 315 21.975 46.310 6.268 0.50 11.94 ATOM 2169 C GLN A 315 25.741 43.852 9.522 1.00 13.89 ATOM 2170 0 GLN A 315 24.962 43.853 10.472 1.00 15.26 ATOM 2171 N THR A 316 26.777 43.017 9.451 1.00 14.65 ATOM 2172 CA THR A 316 27.032 42.059 10.534 1.00 14.00 ATOM 2173 CB THR A 316 28.114 41.012 10.150 1.00 13.24 ATOM 2174 OG1 THR A 316 27.691 40.295 8.986 1.00 14.44 ATOM 2175 CG2 THR A 316 28.321 40.005 11.284 1.00 11.52 ATOM 2176 C THR A 316 27.489 42.835 11.767 1.00 13.16 ATOM 2177 O THR A 316 27.143 42.492 12.896 1.00 13.83 ATOM 2178 N ILE A 317 28.255 43.895 11.537 1.00 13.37 ATOM 2179 CA ILE A 317 28.736 44.741 12.622 1.00 13.69 ATOM 2180 CB ILE A 317 29.716 45.810 12.103 1.00 12.91 ATOM 2181 CG2 ILE A 317 30.004 46.824 13.206 1.00 11.97 ATOM 2182 CG1 ILE A 317 31.001 45.141 11.605 1.00 9.12 ATOM 2183 CD1 ILE A 317 31.901 46.053 10.797 1.00 7.71 ATOM 2184 C ILE A 317 27.554 45.452 13.268 1.00 15.49 ATOM 2185 0 ILE A 317 27.451 45.522 14.494 1.00 14.24 ATOM 2186 N ARG A 318 26.662 45.971 12.424 1.00 15.63 ATOM 2187 CA ARG A 318 25.477 46.689 12.880 1.00 16.16 ATOM 2188 CB ARG A 318 24.657 47.153 11.664 1.00 16.16 ATOM 2189 CG ARG A 318 23.631 48.248 11.955 1.00 16.61 ATOM 2190 CD ARG A 318 22. 868 48.675 10.694 1.00 15.44 ATOM 2191 NE ARG A 318 23.738 49.227 9.653 1.00 13.75 ATOM 2192 CZ ARG A 318 24.409 50.371 9.753 1.00 13.69 ATOM 2193 NH1 ARG A 318 24.318 51. 105 10.851 1.00 12.53 ATOM 2194 NH2 ARG A 318-25. 184 50.780 8.755 1.00 11.64 ATOM 2195 C ARG A 318 24.636 45.776 13.782 1.00 17.52 ATOM 2196 0 ARG A 318 24.204 46.167 14.869 1.00 17.25 ATOM 2197 N GLU A 319 24.432 44.546 13.331 1.00 17.44

ATOM 2198 CA GLU A 319 23.651 43.577 14.081 1.00 17.47 ATOM 2199 CB GLU A 319 23.373 42.360 13.190 1.00 20.17 ATOM 2200 CG GLU A 319 22.491 41.289 13.803 1.00 26.82 ATOM 2201 CD GLU A 319 21.819 40.419 12.747 1.00 31.60 ATOM 2202 OE1 GLU A 319 22.427 40.206 11.677 1.00 33.28 ATOM 2203 OE2 GLU A 319 20.686 39.940 12.988 1.00 35.27 ATOM 2204 C GLU A 319 24.311 43.153 15.398 1.00 17.42 ATOM 2205 0 GLU A 319 23.662 43.160 16.443 1.00 16.52 ATOM 2206 N MET A 320 25.596 42.797 15.368 1.00 17.15 ATOM 2207 CA MET A 320 26.272 42.378 16.599 1.00 16.53 ATOM 2208 CB MET A 320 27.685 41.865 16.298 1.00 16.03 ATOM 2209 CG MET A 320 27.739 40.641 15.383 1.00 13.63 ATOM 2210 SD MET A 320 26.655 39.271 15.894 1.00 18. 40 ATOM 2211 CE MET A 320 27.359 38.810 17.506 1.00 13.96 ATOM 2212 C MET A 320 26.338 43.509 17.632 1.00 16.54 ATOM 2213 0 MET A 320 26.255 43.270 18.838 1.00 16.13 ATOM 2214 N TYR A 321 26.478 44.740 17. 153 1.00 16.60 ATOM 2215 CA TYR A 321 26.541 45.901 18.034 1.00 17.25 ATOM 2216 CB TYR A 321 26.734 47.171 17.207 1.00 16.92 ATOM 2217 CG TYR A 321 26.919 48.428 18.029 1.00 18.08 ATOM 2218 CD1 TYR A 321 28.139 48.716 18.633 1.00 17.27 ATOM 2219 CE1 TYR A 321 28.313 49.874 19.368 1.00 17.13 ATOM 2220 CD2 TYR A 321 25.877 49.334 18.189 1.00 16.65 ATOM 2221 CE2 TYR A 321 26.039 50.491 18.922 1.00 14.99 ATOM 2222 CZ TYR A 321 27.260 50.756 19.508 1.00 17.32 ATOM 2223 OH TYR A 321 27.429 51.912 20.232 1.00 18.90 ATOM 2224 C TYR A 321 25.247 46.013 18.845 1.00 17.69 ATOM 2225 0 TYR A 321 25.279 46.220 20.059 1.00 16.80 ATOM 2226 N ALA A 322 24.115 45.872 18.159 1.00 17.52 ATOM 2227 CA ALA A 322 22.800 45.951 18.787 1.00 18.13 ATOM 2228 CB ALA A 322 21.708 46.037 17.709 1.00 14.74 ATOM 2229 C ALA A 322 22.537 44.757 19.713 1.00 18.09 ATOM 2230 0 ALA A 322 21.958 44.914 20.783 1.00 20.05 ATOM 2231 N LEU A 323 22.957 43.566 19.303 1.00 17.18 ATOM 2232 CA LEU A 323 22.759 42.377 20.128 1.00 18.68 ATOM 2233 CB LEU A 323 23.137 41.117 19.344 1.00 17.23 ATOM 2234 CG LEU A 323 22. 151 40.724 18.239 1.00 17.86

ATOM 2235 CD1 LEU A 323 22.725 39.591 17.402 1.00 15.10 ATOM 2236 CD2 LEU A 323 20.821 40.316 18.869 1.00 16.30 ATOM 2237 C LEU A 323 23.571 42.441 21.422 1.00 19.74 ATOM 2238 0 LEU A 323 23.206 41.819 22.419 1.00 20.81 ATOM 2239 N THR A 324 24.669 43.194 21.404 1.00 19.53 ATOM 2240 CA THR A 324 25.515 43.330 22.584 1.00 20.06 ATOM 2241 CB THR A 324 27.023 43.166 22.223 1.00 19.26 ATOM 2242 OG1 THR A 324 27.408 44.147 21.249 1.00 17.20 ATOM 2243 CG2 THR A 324 27.285 41.778 21.654 1.00 17.70 ATOM 2244 C THR A 324 25.302 44.672 23.295 1.00 21.64 ATOM 2245 O THR A 324 26.085 45.055 24.163 1.00 22.12 ATOM 2246 N GLN A 325 24.241 45.381 22.921 1.00 22.94 ATOM 2247 CA GLN A 325 23.919 46.670 23.528 1.00 24. 57 ATOM 2248 CB GLN A 325 23.522 46.491 24.999 1.00 27.95 ATOM 2249 CG GLN A 325 22.175 45.828 25.230 1.00 30.78 ATOM 2250 CD GLN A 325 22.100 44.441 24.636 1.00 35.70 ATOM 2251 OE1 GLN A 325 22.901 43.565 24.967 1.00 38.45 ATOM 2252 NE2 GLN A 325 21.131 44.229 23.751 1.00 38.29 ATOM 2253 C GLN A 325 25.063 47.668 23.453 1.00 23.94 ATOM 2254 0 GLN A 325 25.177 48.548 24.306 1.00 23.91 ATOM 2255 N GLY A 326 25.904 47.534 22.434 1.00 23.24 ATOM 2256 CA GLY A 326 27.027 48.443 22.282 1.00 23.28 ATOM 2257 C GLY A 326 28.016 48.409 23.436 1.00 22.96 ATOM 2258 O GLY A 326 28.793 49.339 23.614 1.00 21.52 ATOM 2259 N ARG A 327 27.999 47.334 24.217 1.00 25.30 ATOM 2260 CA ARG A 327 28.899 47.206 25.361 1.00 27.57 ATOM 2261 CB ARG A 327 28.138 46.638 26.562 1.00 30.57 ATOM 2262 CG ARG A 327 27.083 47.587 27.105 1.00 37.38 ATOM 2263 CD ARG A 327 26.178 46.924 28.131 1.00 42.63 ATOM 2264 NE ARG A 327 25.129 47.846 28.565 1.00 49.69 ATOM 2265 CZ ARG A 327 24.028 47.483 29.217 1.00 51.85 ATOM 2266 NH1 ARG A 327 23.823 46.207 29.521 1.00 53.56 ATOM 2267 NH2 ARG A 327 23.126 48.397 29.554 1.00 52.17 ATOM 2268 C ARG A 327 30.116 46.335 25.068 1.00 26.53 ATOM 2269 0 ARG A 327 31.021 46.222 25.893 1.00 27.60 ATOM 2270 N VAL A 328 30.133 45.720 23.892 1.00 24.01 ATOM 2271 CA VAL A 328 31.240 44.864 23.504 1.00 21. 11

ATOM 2272 CB VAL A 328 30.744 43.469 23.096 1.00 19.81 ATOM 2273 CG1 VAL A 328 31.914 42.606 22.672 1.00 17.59 ATOM 2274 CG2 VAL A 328 29.987 42.831 24.255 1.00 17.80 ATOM 2275 C VAL A 328 31.991 45.481 22.334 1.00 20.87 ATOM 2276 0 VAL A 328 31.442 45.632 21.246 1.00 21.52 ATOM 2277 N PRO A 329 33.258 45.856 22.553 1.00 18.86 ATOM 2278 CD PRO A 329 33.971 45.781 23.840 1.00 19.19 ATOM 2279 CA PRO A 329 34.105 46.463 21.524 1.00 18.28 ATOM 2280 CB PRO A 329 35.465 46.562 22.212 1.00 17.54 ATOM 2281 CG PRO A 329 35.091 46.773 23.641 1.00 18.63 ATOM 2282 C PRO A 329 34.160 45.615 20.250 1.00 17.72 ATOM 2283 O PRO A 329 34.349 44.392 20.298 1.00 15.04 ATOM 2284 N ILE A 330 33.990 46.273 19.112 1.00 14.63 ATOM 2285 CA ILE A 330 34.029 45.580 17.838 1.00 15.12 ATOM 2286 CB ILE A 330 32.657 45.651 17.123 1.00 14.81 ATOM 2287 CG2 ILE A 330 32.768 45.073 15.732 1.00 13.87 ATOM 2288 CG1 ILE A 330 31.598 44.895 17.928 1.00 15.39 ATOM 2289 CD1 ILE A 330 30.206 44.971 17.315 1.00 15.21 ATOM 2290 C ILE A 330 35.085 46.158 16.898 1.00 14.12 ATOM 2291 O ILE A 330 35.274 47.377 16.816 1.00 12.39 ATOM 2292 N ILE A 331 35.786 45.267 16.207 1.00 13.16 ATOM 2293 CA ILE A 331 36.781 45.671 15.220 1.00 12.79 ATOM 2294 CB ILE A 331 38.109 44.896 15.382 1.00 11.95 ATOM 2295 CG2 ILE A 331 39.078 45.288 14.274 1.00 8.71 ATOM 2296 CG1 ILE A 331 38.723 45.190 16.755 1.00 12.47 ATOM 2297 CD1 ILE A 331 40.105 44.566 16.970 1.00 10.17 ATOM 2298 C ILE A 331 36.153 45.306 13.875 1.00 13.43 ATOM 2299 O ILE A 331 35.949 44.125 13.584 1.00 14.21 ATOM 2300 N GLY A 332 35.824 46.319 13.077 1.00 12.41 ATOM 2301 CA GLY A 332 35.206 46.086 11.782 1.00 11.36 ATOM 2302 C GLY A 332 36.193 45.783 10.675 1.00 12.22 ATOM 2303 0 GLY A 332 37.166 46.510 10.493 1.00 15.34 ATOM 2304 N VAL A 333 35.925 44.718 9.921 1.00 14.28 ATOM 2305 CA VAL A 333 36.793 44.280 8.826 1.00 13.45 ATOM 2306 CB VAL A 333 37.684 43.091 9.256 1.00 14.21 ATOM 2307 CG1 VAL A 333 38.950 43.057 8.412 1.00 12.25 ATOM 2308 CG2 VAL A 333 37.971 43.157 10.734 1.00 16.51

ATOM 2309 C VAL A 333 35.961 43.770 7.649 1.00 12.59 ATOM 2310 0 VAL A 333 34.980 43.058 7.845 1.00 12.06 ATOM 2311 N GLY A 334 36.373 44.103 6.431 1.00 12.29 ATOM 2312 CA GLY A 334 35.643 43.639 5.266 1.00 12.70 ATOM 2313 C GLY A 334 35.389 44.687 4.198 1.00 15.26 ATOM 2314 O GLY A 334 34.428 45.458 4.284 1.00 13.77 ATOM 2315 N GLY A 335 36.256 44.715 3.187 1.00 14.74 ATOM 2316 CA GLY A 335 36.098 45.658 2.095 1.00 15.16 ATOM 2317 C GLY A 335 36.323 47.127 2.409 1.00 16.18 ATOM 2318 0 GLY A 335 35.736 47.992 1.760 1.00 17.52 ATOM 2319 N VAL A 336 37.154 47.429 3.400 1.00 16.08 ATOM 2320 CA VAL A 336 37.434 48.822 3.723 1.00 14.99 ATOM 2321 CB VAL A 336 37.869 48.991 5.187 1.00 16.76 ATOM 2322 CG1 VAL A 336 38.404 50.408 5.411 1.00 16.87 ATOM 2323 CG2 VAL A 336 36.690 48.720 6.107 1.00 15.70 ATOM 2324 C VAL A 336 38.547 49.319 2.801 1.00 15.40 ATOM 2325 O VAL A 336 39.670 48.805 2.821 1.00 12.42 ATOM 2326 N SER A 337 38.230 50.321 1.990 1.00 15.42 ATOM 2327 CA SER A 337 39.204 50.859 1.051 1.00 17.10 ATOM 2328 CB SER A 337 38.895 50.322-0. 351 1.00 19.36 ATOM 2329 OG SER A 337 39.848 50.768-1. 295 1.00 25.95 ATOM 2330 C SER A 337 39.225 52.388 1.030 1.00 16.56 ATOM 2331 0 SER A 337 39.991 52.992 0.280 1.00 16.38 ATOM 2332 N SER A 338 38.393 53.012 1.860 1.00 14.64 ATOM 2333 CA SER A 338 38.320 54.465 1.899 1.00 14.67 ATOM 2334 CB SER A 338 37.349 54.961 0.819 1.00 14.99 ATOM 2335 OG SER A 338 36.003 54.656 1.164 1.00 12.44 ATOM 2336 C SER A 338 37.848 54.977 3.258 1.00 14.59 ATOM 2337 0 SER A 338 37.415 54.201 4.112 1.00 15.42 ATOM 2338 N GLY A 339 37.922 56.289 3.446 1.00 13.82 ATOM 2339 CA GLY A 339 37.478 56.877 4.694 1.00 13.48 ATOM 2340 C GLY A 339 36.003 56.588 4.906 1.00 14.71 ATOM 2341 0 GLY A 339 35.578 56.290 6.023 1.00 15.22 ATOM 2342 N GLN A 340 35.217 56.674 3.834 1.00 13.41 ATOM 2343 CA GLN A 340 33.786 56.410 3.925 1.00 14.35 ATOM 2344 CB GLN A 340 33.085 56.650 2.581 1.00 14.35 ATOM 2345 CG GLN A 340 31.618 56.236 2.611 1.00 16.02

ATOM 2346 CD GLN A 340 30.880 56.527 1.314 1.00 16.82 ATOM 2347 OE1 GLN A 340 30.797 57.676 0.873 1.00 16.80 ATOM 2348 NE2 GLN A 340 30.333 55.484 0.701 1.00 15.54 ATOM 2349 C GLN A 340 33.529 54.978 4.372 1.00 14.64 ATOM 2350 0 GLN A 340 32.696 54.741 5.253 1.00 16.30 ATOM 2351 N ASP A 341 34.237 54.028 3.763 1.00 11.52 ATOM 2352 CA ASP A 341 34.078 52.623 4.127 1.00 12.53 ATOM 2353 CB ASP A 341 35.023 51.726 3.310 1.00 11.88 ATOM 2354 CG ASP A 341 34.767 51.803 1.813 1.00 13.90 ATOM 2355 OD1 ASP A 341 33.638 52.168 1.416 1.00 15.59 ATOM 2356 OD2 ASP A 341 35.689 51.483 1.029 1.00 12.73 ATOM 2357 C ASP A 341 34.388 52.456 5.611 1.00 11.81 ATOM 2358 0 ASP A 341 33.694 51.742 6.332 1.00 11.96 ATOM 2359 N ALA A 342 35.439 53.126 6.067 1.00 11.76 ATOM 2360 CA ALA A 342 35.833 53.044 7.465 1.00 11.81 ATOM 2361 CB ALA A 342 37.176 53.738 7.667 1.00 11.59 ATOM 2362 C ALA A 342 34.780 53.655 8.385 1.00 12.36 ATOM 2363 O ALA A 342 34.412 53.057 9.396 1.00 12.99 ATOM 2364 N LEU A 343 34.288 54.840 8.029 1.00 11.54 ATOM 2365 CA LEU A 343 33.291 55.524 8.845 1.00 12.58 ATOM 2366 CB LEU A 343 33.119 56.971 8.367 1.00 12.32 ATOM 2367 CG LEU A 343 32.194 57.846 9.219 1.00 11.92 ATOM 2368 CD1 LEU A 343 32.722 57.868 10.649 1.00 12.03 ATOM 2369 CD2 LEU A 343 32.115 59.269 8.648 1.00 8.59 ATOM 2370 C LEU A 343 31.928 54.829 8.891 1.00 13.74 ATOM 2371 0 LEU A 343 31.238 54.894 9.905 1.00 16.00 ATOM 2372 N GLU A 344 31.521 54.178 7.803 1.00 14.78 ATOM 2373 CA GLU A 344 30.237 53.485 7.817 1.00 14.04 ATOM 2374 CB GLU A 344 29.900 52.905 6.440 1.00 15.85 ATOM 2375 CG GLU A 344 29.651 53.948 5.354 1.00 17.05 ATOM 2376 CD GLU A 344 29.008 53.356 4.101 1.00 17.77 ATOM 2377 OE1 GLU A 344 29.281 52.178 3.784 1.00 18.22 ATOM 2378 OE2 GLU A 344 28.239 54.071 3.423 1.00 15.65 ATOM 2379 C GLU A 344 30.291 52.365 8.855 1.00 14.33 ATOM 2380 0 GLU A 344 29.325 52.135 9.589 1.00 14.32 ATOM 2381 N LYS A 345 31.429 51.678 8.925 1.00 14.23 ATOM 2382 CA LYS A 345 31. 607 50.597 9.891 1.00 14.82

ATOM 2383 CB LYS A 345 32.874 49.798 9.577 1.00 13.09 ATOM 2384 CG LYS A 345 32.684 48.787 8.455 1.00 13.42 ATOM 2385 CD LYS A 345 33.950 47.983 8.198 1.00 11.05 ATOM 2386 CE LYS A 345 33.644 46.692 7.449 1.00 11.82 ATOM 2387 NZ LYS A 345 32.954 46.910 6.149 1.00 11.61 ATOM 2388 C LYS A 345 31.668 51.150 11.310 1.00 14.91 ATOM 2389 O LYS A 345 31.127 50.554 12.240 1.00 15.66 ATOM 2390 N ILE A 346 32.320 52.295 11.478 1.00 14.92 ATOM 2391 CA ILE A 346 32.402 52.911 12.796 1.00 15.79 ATOM 2392 CB ILE A 346 33.369 54.121 12.789 1.00 16.10 ATOM 2393 CG2 ILE A 346 33.290 54.875 14.116 1.00 14.25 ATOM 2394 CG1 ILE A 346 34.797 53.623 12.538 1.00 14.97 ATOM 2395 CD1 ILE A 346 35.817 54.721 12.416 1.00 16.00 ATOM 2396 C ILE A 346 31.001 53.350 13.234 1.00 16.25 ATOM 2397 0 ILE A 346 30.591 53.083 14.363 1.00 16.13 ATOM 2398 N ARG A 347 30.260 54.007 12.342 1.00 15.62 ATOM 2399 CA ARG A 347 28.902 54.438 12.679 1.00 16.59 ATOM 2400 CB ARG A 347 28.295 55.277 11.548 1.00 17.49 ATOM 2401 CG ARG A 347 28.941 56.653 11.343 1.00 18.28 ATOM 2402 CD ARG A 347 28.202 57.433 10.253 1.00 19.60 ATOM 2403 NE ARG A 347 26.798 57.641 10.603 1.00 22.54 ATOM 2404 CZ ARG A 347 26.277 58.810 10.972 1.00 26.53 ATOM 2405 NH1 ARG A 347 27.041 59.897 11.035 1.00 26.79 ATOM 2406 NH2 ARG A 347 24.991 58.890 11.298 1.00 24.26 ATOM 2407 C ARG A 347 28.012 53.219 12.946 1.00 15.67 ATOM 2408 O ARG A 347 27.085 53.279 13.747 1.00 15.54 ATOM 2409 N ALA A 348 28.301 52.110 12.272 1.00 15.61 ATOM 2410 CA ALA A 348 27.526 50.891 12.464 1.00 15.15 ATOM 2411 CB ALA A 348 27.797 49.900 11.325 1.00 14.45 ATOM 2412 C ALA A 348 27.850 50.250 13.813 1.00 15.53 ATOM 2413 0 ALA A 348 27.090 49.407 14.295 1.00 16.19 ATOM 2414 N GLY A 349 28.973 50.642 14.423 1.00 13.70 ATOM 2415 CA GLY A 349 29.320 50.084 15.722 1.00 12.86 ATOM 2416 C GLY A 349 30.763 49.672 15.980 1.00 14.30 ATOM 2417 0 GLY A 349 31.101 49.272 17.096 1.00 14.51 ATOM 2418 N ALA A 350 31.621 49.770 14.971 1.00 13.70 ATOM 2419 CA ALA A 350 33.019 49.392 15.136 1.00 15.96

ATOM 2420 CB ALA A 350 33.643 49.085 13.777 1.00 16.02 ATOM 2421 C ALA A 350 33.836 50.463 15.841 1.00 16.80 ATOM 2422 0 ALA A 350 33.729 51.652 15.527 1.00 17.12 ATOM 2423 N SER A 351 34.651 50.034 16.801 1.00 17.39 ATOM 2424 CA SER A 351 35.520 50.950 17.534 1.00 16.33 ATOM 2425 CB SER A 351 35.833 50.400 18.926 1.00 15.21 ATOM 2426 OG SER A 351 34.706 50.492 19.773 1.00 17.81 ATOM 2427 C SER A 351 36.817 51.109 16.748 1.00 16.42 ATOM 2428 O SERA 351 37.501 52.131 16.847 1.00 16.42 ATOM 2429 N LEU A 352 37.141 50.076 15.971 1.00 14.86 ATOM 2430 CA LEU A 352 38.343 50.051 15.142 1.00 15.16 ATOM 2431 CB LEU A 352 39.475 49.292 15.849 1.00 12.61 ATOM 2432 CG LEU A 352 39.911 49.711 17.252 1.00 14.17 ATOM 2433 CD1 LEU A 352 40.762 48.598 17.870 1.00 10.97 ATOM 2434 CD2 LEU A 352 40.676 51.026 17.187 1.00 12.18 ATOM 2435 C LEU A 352 38.013 49.313 13.851 1.00 13.91 ATOM 2436 0 LEU A 352 37.037 48.564 13.792 1.00 11.65 ATOM 2437 N VAL A 353 38.829 49.523 12.823 1.00 13.16 ATOM 2438 CA VAL A 353 38.631 48.835 11.558 1.00 14.12 ATOM 2439 CB VAL A 353 38.062 49.767 10.463 1.00 15.89 ATOM 2440 CG1 VAL A 353 36.764 50.405 10.946 1.00 14.47 ATOM 2441 CG2 VAL A 353 39.090 50.819 10.078 1.00 13.72 ATOM 2442 C VAL A 353 39.966 48.288 11.082 1.00 14.87 ATOM 2443 0 VAL A 353 41.026 48.706 11.554 1.00 13.31 ATOM 2444 N GLN A 354 39.902 47.336 10.158 1.00 14.46 ATOM 2445 CA GLN A 354 41.092 46.725 9.586 1.00 14.10 ATOM 2446 CB GLN A 354 41.343 45.324 10.168 1.00 14.76 ATOM 2447 CG GLN A 354 41.579 45.243 11.671 1.00 15.41 ATOM 2448 CD GLN A 354 41.760 43.796 12.139 1.00 18.05 ATOM 2449 OE1 GLN A 354 41.012 42.904 11.732 1.00 16.89 ATOM 2450 NE2 GLN A 354 42.750 43.564 12.997 1.00 17.31 ATOM 2451 C GLN A 354 40.861 46.586 8.088 1.00 14.25 ATOM 2452 0 GLN A 354 39.726 46.651 7.608 1.00 13.09 ATOM 2453 N LEU A 355 41.942 46.395 7.349 1.00 14.08 ATOM 2454 CA LEU A 355 41.835 46.209 5.914 1.00 15.37 ATOM 2455 CB LEU A 355 41.910 47.555 5.180 1.00 13.53 ATOM 2456 CG LEU A 355 43.170 48.420 5.302 1.00 13.38

ATOM 2457 CD1 LEU A 355 44.270 47.896 4.383 1.00 13.17 ATOM 2458 CD2 LEU A 355 42.825 49.855 4.938 1.00 10.64 ATOM 2459 C LEU A 355 42.965 45.302 5.478 1.00 15.97 ATOM 2460 0 LEU A 355 43.971 45.169 6.175 1.00 15.47 ATOM 2461 N TYR A 356 42.786 44.656 4.334 1.00 16.99 ATOM 2462 CA TYR A 356 43.815 43.784 3.802 1.00 16.94 ATOM 2463 CB TYR A 356 43.645 42.351 4.334 1.00 15.18 ATOM 2464 CG TYR A 356 44.707 41.373 3.857 1.00 14.99 ATOM 2465 CD1 TYR A 356 44.767 40.080 4.362 1.00 15.31 ATOM 2466 CE1 TYR A 356 45.700 39.171 3.893 1.00 13.63 ATOM 2467 CD2 TYR A 356 45.620 41.728 2.869 1.00 15.99 ATOM 2468 CE2 TYR A 356 46.553 40.826 2.391 1.00 15.09 ATOM 2469 CZ TYR A 356 46.588 39.551 2.904 1.00 15.51 ATOM 2470 OH TYR A 356 47.502 38.651 2.408 1.00 17.24 ATOM 2471 C TYR A 356 43.747 43.805 2.285 1.00 16.84 ATOM 2472 0 TYR A 356 44.675 44.272 1.628 1.00 17.11 ATOM 2473 N THR A 357 42.646 43.305 1.735 1.00 16.44 ATOM 2474 CA THR A 357 42.478 43.251 0.289 1.00 16.13 ATOM 2475 CB THR A 357 41.066 42.747-0. 080 1.00 16.57 ATOM 2476 OG1 THR A 357 40.874 41.433 0.460 1.00 13.38 ATOM 2477 CG2 THR A 357 40.899 42.689-1. 588 1.00 16.25 ATOM 2478 C THR A 357 42.727 44.596-0. 400 1.00 15.53 ATOM 2479 0 THR A 357 43.292 44.640-1. 491 1.00 15.19 ATOM 2480 N ALA A 358 42.314 45.689 0.233 1.00 14.89 ATOM 2481 CA ALA A 358 42.508 47.012-0. 356 1.00 15.09 ATOM 2482 CB ALA A 358 41.917 48.075 0.546 1.00 11.21 ATOM 2483 C ALA A 358 43.993 47.277-0. 572 1.00 16.40 ATOM 2484 0 ALA A 358 44.389 47.910-1. 551 1.00 15.75 ATOM 2485 N LEU A 359 44.810 46.786 0.355 1.00 16.78 ATOM 2486 CA LEU A 359 46.254 46.967 0.284 1.00 17.50 ATOM 2487 CB LEU A 359 46.912 46.440 1.566 1.00 18.55 ATOM 2488 CG LEU A 359 48.438 46.517 1.659 1.00 19.27 ATOM 2489 CD1 LEU A 359 48.888 47.968 1.604 1.00 17.73 ATOM 2490 CD2 LEU A 359 48.897 45.862 2.955 1.00 18.92 ATOM 2491 C LEU A 359 46.844 46.258-0. 932 1.00 16.82 ATOM 2492 0 LEU A 359 47.773 46.762-1. 558 1.00 15.67 ATOM 2493 N THR A 360 46.293 45.096-1. 269 1.00 16.87

ATOM 2494 CA THR A 360 46.783 44.325-2. 406 1.00 17.52 ATOM 2495 CB THR A 360 46.203 42.896-2. 402 1.00 17.31 ATOM 2496 OG1 THR A 360 44.839 42.927-2. 843 1.00 16.95 ATOM 2497 CG2 THR A 360 46.262 42.310-0. 993 1.00 13.68 ATOM 2498 C THR A 360 46.474 44.971-3. 757 1.00 19.33 ATOM 2499 0 THR A 360 47.081 44.616-4. 768 1.00 21.20 ATOM 2500 N PHE A 361 45.538 45.916-3. 783 1.00 19.66 ATOM 2501 CA PHE A 361 45.186 46.590-5. 034 1.00 20.68 ATOM 2502 CB PHE A 361 43.663 46.753-5. 171 1.00 21.37 ATOM 2503 CG PHE A 361 42.933 45.484-5. 510 1.00 22.02 ATOM 2504 CD1 PHE A 361 42.179 44.825-4. 554 1.00 18.66 ATOM 2505 CD2 PHE A 361 43.012 44.944-6. 786 1.00 23.48 ATOM 2506 CE1 PHE A 361 41.520 43.653-4. 861 1.00 21.36 ATOM 2507 CE2 PHE A 361 42.353 43.764-7. 099 1.00 22.19 ATOM 2508 CZ PHE A 361 41.607 43.119-6. 134 1.00 21.74 ATOM 2509 C PHE A 361 45.814 47.973-5. 168 1.00 21.60 ATOM 2510 O PHE A 361 46.323 48.330-6. 226 1.00 23.15 ATOM 2511 N TRP A 362 45.777 48.750-4. 091 1.00 23.22 ATOM 2512 CA TRP A 362 46.291 50.113-4. 118 1.00 23.91 ATOM 2513 CB TRP A 362 45.264 51.031-3. 449 1.00 25.18 ATOM 2514 CG TRP A 362 43.854 50.699-3. 871 1.00 29.81 ATOM 2515 CD2 TRP A 362 43.375 50.514-5. 214 1.00 31.67 ATOM 2516 CE2 TRP A 362 42.015 50.155-5. 126 1.00 31.90 ATOM 2517 CE3 TRP A 362 43.966 50.614-6. 480 1.00 32.33 ATOM 2518 CD1 TRP A 362 42.789 50.457-3. 053 1.00 29.44 ATOM 2519 NE1 TRP A 362 41.683 50.128-3. 798 1.00 29.93 ATOM 2520 CZ2 TRP A 362 41.234 49.895-6. 257 1.00 33.85 ATOM 2521 CZ3 TRP A 362 43.190 50.355-7. 601 1.00 33.08 ATOM 2522 CH2 TRP A 362 41.839 50.000-7. 481 1.00 33.33 ATOM 2523 C TRP A 362 47.671 50.307-3. 494 1.00 22.99 ATOM 2524 0 TRP A 362 48.318 51.334-3. 713 1.00 22.54 ATOM 2525 N GLY A 363 48.119 49.321-2. 725 1.00 21.66 ATOM 2526 CA GLY A 363 49.422 49.408-2. 094 1.00 20.23 ATOM 2527 C GLY A 363 49.423 50.222-0. 815 1.00 20.57 ATOM 2528 0 GLY A 363 48.373 50.675-0. 358 1.00 20.51 ATOM 2529 N PRO A 364 50.606 50.428-0. 215 1.00 20.18 ATOM 2530 CD PRO A 364 51.880 49.909-0. 750 1.00 20.17

ATOM 2531 CA PRO A 364 50.833 51.183 1.024 1.00 20.20 ATOM 2532 CB PRO A 364 52.353 51.338 1.057 1.00 19.15 ATOM 2533 CG PRO A 364 52.820 50.058 0.437 1.00 19.46 ATOM 2534 C PRO A 364 50. 118 52.533 1.143 1.00 20.39 ATOM 2535 0 PRO A 364 49.604 52.870 2.209 1.00 22.16 ATOM 2536 N PRO A 365 50.079 53.327 0.058 1.00 20.34 ATOM 2537 CD PRO A 365 50.655 53.090-1. 277 1.00 19.58 ATOM 2538 CA PRO A 365 49.414 54.635 0.110 1.00 18.92 ATOM 2539 CB PRO A 365 49.568 55.161-1. 318 1.00 19.47 ATOM 2540 CG PRO A 365 50.826 54.495-1. 798 1.00 20.15 ATOM 2541 C PRO A 365 47.950 54.601 0.542 1.00 18.73 ATOM 2542 0 PRO A 365 47.409 55.610 0.994 1.00 20.00 ATOM 2543 N VAL A 366 47.304 53.447 0.411 1.00 18.05 ATOM 2544 CA VAL A 366 45.898 53.351 0.779 1.00 18.28 ATOM 2545 CB VAL A 366 45.315 51.954 0.450 1.00 18.78 ATOM 2546 CG1 VAL A 366 45.801 50.926 1.455 1.00 16.44 ATOM 2547 CG2 VAL A 366 43.800 52.024 0.432 1.00 18.48 ATOM 2548 C VAL A 366 45.674 53.645 2.257 1.00 17.96 ATOM 2549 0 VAL A 366 44.621 54.152 2.645 1.00 19.15 ATOM 2550 N VAL A 367 46.673 53.340 3.076 1.00 17.52 ATOM 2551 CA VAL A 367 46.576 53.566 4.512 1.00 17.49 ATOM 2552 CB VAL A 367 47.814 53.021 5.234 1.00 16.98 ATOM 2553 CG1 VAL A 367 47.646 53.187 6.728 1.00 14.72 ATOM 2554 CG2 VAL A 367 48.028 51.551 4.857 1.00 17.23 ATOM 2555 C VAL A 367 46.415 55.046 4.859 1.00 17.78 ATOM 2556 0 VAL A 367 45.553 55.413 5.655 1.00 17.04 ATOM 2557 N GLY A 368 47.252 55.891 4.264 1.00 19.06 ATOM 2558 CA GLY A 368 47.169 57.316 4.525 1.00 19.05 ATOM 2559 C GLY A 368 45.890 57.877 3.942 1.00 21.25 ATOM 2560 0 GLY A 368 45.269 58.774 4.522 1.00 20.35 ATOM 2561 N LYS A 369 45.488 57.332 2.795 1.00 22.08 ATOM 2562 CA LYS A 369 44.270 57.771 2.118 1.00 22.27 ATOM 2563 CB LYS A 369 44.063 56.989 0.813 1.00 21.63 ATOM 2564 CG LYS A 369 43.072 57.652-0. 132 1.00 23.91 ATOM 2565 CD LYS A 369 42.558 56.712-1. 216 1.00 22.29 ATOM 2566 CE LYS A 369 41.611 55.682-0. 630 1.00 23.00 ATOM 2567 NZ LYS A 369 40. 826 54.976-1. 675 1.00 23.30

ATOM 2568 C LYS A 369 43.060 57.561 3.022 1.00 21.33 ATOM 2569 O LYS A 369 42.255 58.474 3.228 1.00 21.31 ATOM 2570 N VAL A 370 42.936 56.353 3.563 1.00 19.60 ATOM 2571 CA VAL A 370 41.816 56.032 4.436 1.00 18.55 ATOM 2572 CB VAL A 370 41.855 54.555 4.889 1.00 16.90 ATOM 2573 CG1 VAL A 370 40.748 54.295 5.897 1.00 14.02 ATOM 2574 CG2 VAL A 370 41.693 53.636 3.682 1.00 15.42 ATOM 2575 C VAL A 370 41.794 56.930 5.667 1.00 19.20 ATOM 2576 0 VAL A 370 40.740 57.439 6.054 1.00 18.26 ATOM 2577 N LYS A 371 42.956 57.128 6.280 1.00 19.20 ATOM 2578 CA LYS A 371 43.040 57.974 7.462 1.00 20.21 ATOM 2579 CB LYS A 371 44.444 57.897 8.075 1.00 20.24 ATOM 2580 CG LYS A 371 44.726 56.563 8.759 1.00 19.89 ATOM 2581 CD LYS A 371 46.018 56.590 9.551 1.00 19.73 ATOM 2582 CE LYS A 371 47.218 56.781 8. 647 1.00 20.14 ATOM 2583 NZ LYS A 371 48.488 56.743 9.416 1.00 20.57 ATOM 2584 C LYS A 371 42.678 59.426 7.155 1.00 20.46 ATOM 2585 0 LYS A 371 41.956 60.063 7.917 1.00 19.82 ATOM 2586 N ARG A 372 43.177 59.943 6.036 1.00 21.92 ATOM 2587 CA ARG A 372 42.895 61.319 5.639 1.00 23.46 ATOM 2588 CB ARG A 372 43.702 61.689 4.390 1.00 24.84 ATOM 2589 CG ARG A 372 43.493 63.125 3.930 1.00 29.50 ATOM 2590 CD ARG A 372 44.269 63.452 2.649 1.00 32.37 ATOM 2591 NE ARG A 372 43.723 62.769 1.475 1.00 36.28 ATOM 2592 CZ ARG A 372 44.333 61.781 0.829 1.00 36.09 ATOM 2593 NH1 ARG A 372 45.519 61.352 1.240 1.00 36.80 ATOM 2594 NH2 ARG A 372 43.755 61.220-0. 227 1.00 35.12 ATOM 2595 C ARG A 372 41.405 61.541 5.360 1.00 23.29 ATOM 2596 0 ARG A 372 40.823 62.530 5.809 1.00 22.86 ATOM 2597 N GLU A 373 40.791 60.622 4.619 1.00 21.51 ATOM 2598 CA GLU A 373 39.376 60.744 4.288 1.00 20.70 ATOM 2599 CB GLU A 373 38.987 59.727 3.206 1.00 21.22 ATOM 2600 CG GLU A 373 39.796 59.863 1.918 1.00 21.34 ATOM 2601 CD GLU A 373 39.475 58.778 0.904 1.00 24.10 ATOM 2602 OE1 GLU A 373 39.326 57.609 1.313 1.00 26.50 ATOM 2603 OE2 GLU A 373 39.385 59.085-0. 302 1.00 24.10 ATOM 2604 C GLU A 373 38.516 60.548 5.525 1.00 20.60

ATOM 2605 O GLU A 373 37.472 61.181 5.671 1.00 23.32 ATOM 2606 N LEU A 374 38.951 59.671 6.420 1.00 19.33 ATOM 2607 CA LEU A 374 38.203 59.429 7.643 1.00 19.28 ATOM 2608 CB LEU A 374 38.860 58.314 8.462 1.00 16.56 ATOM 2609 CG LEU A 374 38.206 58.007 9.816 1.00 15.77 ATOM 2610 CD1 LEU A 374 36.750 57.618 9.607 1.00 12.63 ATOM 2611 CD2 LEU A 374 38.968 56.885 10.520 1.00 14.15 ATOM 2612 C LEU A 374 38.153 60.713 8.468 1.00 20.85 ATOM 2613 0 LEU A 374 37.091 61.114 8.943 1.00 23.22 ATOM 2614 N GLU A 375 39.306 61.353 8.635 1.00 20.32 ATOM 2615 CA GLU A 375 39.398 62.592 9.399 1.00 23.08 ATOM 2616 CB GLU A 375 40.840 63.099 9.412 1.00 25.75 ATOM 2617 CG GLU A 375 41.075 64.247 10.371 1.00 32.67 ATOM 2618 CD GLU A 375 42.494 64.777 10.308 1.00 37.01 ATOM 2619 OE1 GLU A 375 43.438 63.960 10.365 1.00 39.17 ATOM 2620 OE2 GLU A 375 42.664 66.012 10.209 1.00 41.03 ATOM 2621 C GLU A 375 38.487 63.667 8.813 1.00 22.51 ATOM 2622 0 GLU A 375 37.720 64.300 9.536 1.00 22.31 ATOM 2623 N ALA A 376 38.571 63.865 7.501 1.00 22.41 ATOM 2624 CA ALA A 376 37.746 64.859 6.822 1.00 22.75 ATOM 2625 CB ALA A 376 38.096 64.910 5.325 1.00 21.03 ATOM 2626 C ALA A 376 36.262 64.556 7.003 1.00 23.07 ATOM 2627 0 ALA A 376 35.470 65.461 7.258 1.00 25.45 ATOM 2628 N LEU A 377 35.885 63.285 6.868 1.00 22.11 ATOM 2629 CA LEU A 377 34.487 62.890 7.022 1.00 20.80 ATOM 2630 CB LEU A 377 34.298 61.417 6.655 1.00 18.44 ATOM 2631 CG LEU A 377 34.362 61.131 5.155 1.00 19.93 ATOM 2632 CD1 LEU A 377 34.310 59.637 4.918 1.00 18.66 ATOM 2633 CD2 LEU A 377 33.212 61.842 4.449 1.00 15.51 ATOM 2634 C LEU A 377 33.973 63.131 8.433 1.00 21.64 ATOM 2635 0 LEU A 377 32.826 63.536 8.615 1.00 20.67 ATOM 2636 N LEU A 378 34.816 62.870 9.430 1.00 22.64 ATOM 2637 CA LEU A 378 34.429 63.081 10.822 1.00 23.81 ATOM 2638 CB LEU A 378 35.555 62.637 11.764 1.00 19.85 ATOM 2639 CG LEU A 378 35.811 61.131 11.866 1.00 18.67 ATOM 2640 CD1 LEU A 378 37. 123 60.867 12.585 1.00 16.23 ATOM 2641 CD2 LEU A 378 34.650 60.466 12.592 1.00 16.80

ATOM 2642 C LEU A 378 34.104 64. 558 11.059 1.00 24.84 ATOM 2643 0 LEU A 378 33.079 64.884 11.658 1.00 24.64 ATOM 2644 N LYS A 379 34.979 65.443 10.587 1.00 25.82 ATOM 2645 CA LYS A 379 34.775 66.880 10.745 1.00 29.39 ATOM 2646 CB LYS A 379 35.972 67.656 10.191 1.00 30.69 ATOM 2647 CG LYS A 379 37.283 67.388 10.916 1.00 34.84 ATOM 2648 CD LYS A 379 38.430 68.176 10.299 1.00 36.48 ATOM 2649 CE LYS A 379 39.740 67.884 11.014 1.00 40.34 ATOM 2650 NZ LYS A 379 40.898 68.607 10.410 1.00 42.08 ATOM 2651 C LYS A 379 33.524 67.295 9.991 1.00 30.60 ATOM 2652 0 LYS A 379 32.634 67.950 10.531 1.00 30.06 ATOM 2653 N GLU A 380 33.476 66.892 8.729 1.00 31.82 ATOM 2654 CA GLU A 380 32.365 67.193 7.845 1.00 33.48 ATOM 2655 CB GLU A 380 32.618 66.512 6.499 1.00 35.73 ATOM 2656 CG GLU A 380 31.528 66.676 5.475 1.00 42.73 ATOM 2657 CD GLU A 380 31.886 66.003 4.164 1.00 46.67 ATOM 2658 OE1 GLU A 380 31.007 65.891 3.284 1.00 49.93 ATOM 2659 OE2 GLU A 380 33.055 65.588 4.016 1.00 48.55 ATOM 2660 C GLU A 380 31.020 66.757 8.424 1.00 32.66 ATOM 2661 0 GLU A 380 29.984 67.357 8.131 1.00 31.37 ATOM 2662 N GLN A 381 31.032 65.721 9.256 1.00 31.27 ATOM 2663 CA GLN A 381 29.790 65.231 9.844 1.00 30.92 ATOM 2664 CB GLN A 381 29.709 63.706 9.693 1.00 30.23 ATOM 2665 CG GLN A 381 29.397 63.274 8.258 1.00 29.83 ATOM 2666 CD GLN A 381 29.461 61.772 8.047 1.00 30.64 ATOM 2667 OE1 GLN A 381 29.032 60.993 8.897 1.00 30.52 ATOM 2668 NE2 GLN A 381 29.982 61.359 6.894 1.00 30.34 ATOM 2669 C GLN A 381 29.561 65.652 11.296 1.00 30.74 ATOM 2670 0 GLN A 381 28.644 65.164 11.956 1.00 30.23 ATOM 2671 N GLY A 382 30.401 66.559 11.786 1.00 30.20 ATOM 2672 CA GLY A 382 30.244 67.065 13. 138 1.00 30.10 ATOM 2673 C GLY A 382 30.755 66.241 14.302 1.00 30.25 ATOM 2674 0 GLY A 382 30.454 66.554 15.452 1.00 30.34 ATOM 2675 N PHE A 383 31.520 65.192 14.033 1.00 29.37 ATOM 2676 CA PHE A 383 32.051 64.377 15.118 1.00 28.29 ATOM 2677 CB PHE A 383 32.310 62.948 14.641 1.00 26.27 ATOM 2678 CG PHE A 383 31.068 62.210 14.240 1.00 24.23

ATOM 2679 CD1 PHE A 383 30.803 61.945 12.908 1.00 23.49 ATOM 2680 CD2 PHE A 383 30.164 61.784 15.197 1.00 21.41 ATOM 2681 CE1 PHE A 383 29.658 61.264 12.535 1.00 22.95 ATOM 2682 CE2 PHE A 383 29.021 61.106 14.830 1.00 22.42 ATOM 2683 CZ PHE A 383 28.767 60.845 13.496 1.00 22.22 ATOM 2684 C PHE A 383 33.346 64.978 15.652 1.00 29.12 ATOM 2685 0 PHE A 383 34.229 65.354 14.882 1.00 30.28 ATOM 2686 N GLY A 384 33.452 65.073 16.973 1.00 28.98 ATOM 2687 CA GLY A 384 34.655 65.619 17.573 1.00 29.01 ATOM 2688 C GLY A 384 35.827 64. 681 17. 363 1.00 29.23 ATOM 2689 0 GLY A 384 36.983 65.101 17.345 1.00 30.19 ATOM 2690 N GLY A 385 35.518 63.399 17.198 1.00 28.93 ATOM 2691 CA GLY A 385 36.548 62.402 16.983 1.00 27. 17 ATOM 2692 C GLY A 385 35.933 61.048 16.690 1.00 26.43 ATOM 2693 0 GLY A 385 34.712 60.903 16.701 1.00 26.73 ATOM 2694 N VAL A 386 36.781 60.057 16.430 1.00 25.91 ATOM 2695 CA VAL A 386 36.336 58.700 16.132 1.00 23.85 ATOM 2696 CB VAL A 386 37.545 57.736 16.010 1.00 24.56 ATOM 2697 CG1 VAL A 386 37.061 56.300 15.881 1.00 22.43 ATOM 2698 CG2 VAL A 386 38.400 58.119 14.812 1.00 24.35 ATOM 2699 C VAL A 386 35.413 58.174 17.224 1.00 24.03 ATOM 2700 0 VAL A 386 34.355 57.608 16.940 1.00 23.33 ATOM 2701 N THR A 387 35.825 58.368 18.473 1.00 23.99 ATOM 2702 CA THR A 387 35.068 57.909 19.632 1.00 24.92 ATOM 2703 CB THR A 387 35.716 58.406 20.939 1.00 26.36 ATOM 2704 OG1 THR A 387 37.104 58.047 20.950 1.00 30.29 ATOM 2705 CG2 THR A 387 35.034 57.782 22.144 1.00 24.51 ATOM 2706 C THR A 387 33.616 58.369 19.612 1.00 24.16 ATOM 2707 0 THR A 387 32.723 57.652 20.057 1.00 24.55 ATOM 2708 N ASP A 388 33.389 59.570 19.094 1.00 23.85 ATOM 2709 CA ASP A 388 32.052 60.144 19.024 1.00 23.14 ATOM 2710 CB ASP A 388 32.154 61.640 18.724 1.00 26.77 ATOM 2711 CG ASP A 388 32.878 62.399 19.806 1.00 30.24 ATOM 2712 OD1 ASP A 388 33.722 63.260 19.469 1.00 33.20 ATOM 2713 OD2 ASP A 388 32.597 62.138 20.996 1.00 33.14 ATOM 2714 C ASP A 388 31.187 59.486 17.960 1.00 21.34 ATOM 2715 0 ASP A 388 29. 968 59.454 18.077 1.00 19.97

ATOM 2716 N ALA A 389 31.828 58.968 16.918 1.00 20.96 ATOM 2717 CA ALA A 389 31.122 58.335 15.815 1.00 19.43 ATOM 2718 CB ALA A 389 31.944 58.481 14.536 1.00 20.22 ATOM 2719 C ALA A 389 30.762 56.870 16.036 1.00 18.17 ATOM 2720 O ALA A 389 29.841 56.357 15.399 1.00 19.04 ATOM 2721 N ILE A 390 31.485 56.191 16.923 1.00 17.77 ATOM 2722 CA ILE A 390 31.222 54.774 17.193 1.00 15.58 ATOM 2723 CB ILE A 390 32.105 54.251 18.355 1.00 15.12 ATOM 2724 CG2 ILE A 390 31.802 52.784 18.617 1.00 12.26 ATOM 2725 CG1 ILE A 390 33.589 54.412 18.005 1.00 15.87 ATOM 2726 CD1 ILE A 390 34.530 54.143 19.163 1.00 13.96 ATOM 2727 C ILE A 390 29.753 54.514 17.539 1.00 15.15 ATOM 2728 0 ILE A 390 29.254 54.982 18.561 1.00 16.23 ATOM 2729 N GLY A 391 29.066 53.774 16.676 1.00 15.83 ATOM 2730 CA GLY A 391 27.665 53.450 16.907 1.00 15.35 ATOM 2731 C GLY A 391 26.649 54.555 16.651 1.00 15.84 ATOM 2732 0 GLY A 391 25.460 54.366 16.896 1.00 15.88 ATOM 2733 N ALA A 392 27.100 55.695 16.139 1.00 16.70 ATOM 2734 CA ALA A 392 26.214 56.832 15.877 1.00 18.63 ATOM 2735 CB ALA A 392 26.985 57.936 15.145 1.00 16.34 ATOM 2736 C ALA A 392 24.928 56.505 15.114 1.00 19.71 ATOM 2737 0 ALA A 392 23.893 57.130 15.355 1.00 19.45 ATOM 2738 N ASP A 393 24.980 55.541 14.196 1.00 20.17 ATOM 2739 CA ASP A 393 23.786 55.187 13.424 1.00 20.89 ATOM 2740 CB ASP A 393 24.099 54.129 12.356 1.00 21.04 ATOM 2741 CG ASP A 393 24.899 54.680 11.185 1.00 25.12 ATOM 2742 OD1 ASP A 393 24.911 55.914 10.973 1.00 24.48 ATOM 2743 OD2 ASP A 393 25.505 53.860 10.459 1.00 26.24 ATOM 2744 C ASP A 393 22.678 54.646 14.321 1.00 21.66 ATOM 2745 O ASP A 393 21.495 54.824 14.034 1.00 21.79 ATOM 2746 N HIS A 394 23.068 53.980 15.404 1.00 21.55 ATOM 2747 CA HIS A 394 22.113 53.388 16.334 1.00 22.75 ATOM 2748 CB HIS A 394 22.825 52.353 17.208 1.00 17.96 ATOM 2749 CG HIS A 394 23.439 51.228 16.430 1.00 18.66 ATOM 2750 CD2 HIS A 394 24.567 51.172 15.683 1.00 15.93 ATOM 2751 ND1 HIS A 394 22.860 49.979 16.342 1.00 15.56 ATOM 2752 CE1 HIS A 394 23.605 49.204 15.576 1.00 15.23

ATOM 2753 NE2 HIS A 394 24.647 49.903 15.163 1.00 16.20 ATOM 2754 C'HIS A 394 21.415 54.414 17.222 1.00 25.26 ATOM 2755 0 HIS A 394 20.369 54.132 17.798 1.00 26.08 ATOM 2756 N ARG A 395 21.996 55.602 17.332 1.00 28.23 ATOM 2757 CA ARG A 395 21.426 56.647 18.170 1.00 32.93 ATOM 2758 CB ARG A 395 22.545 57.387 18.911 1.00 32.49 ATOM 2759 CG ARG A 395 23.385 56.481 19.809 1.00 34.34 ATOM 2760 CD ARG A 395 24.306 57.282 20.723 1.00 34.96 ATOM 2761 NE ARG A 395 25.452 57.866 20.029 1.00 36.24 ATOM 2762 CZ ARG A 395 26.561 57.199 19.715 1.00 36.79 ATOM 2763 NH1 ARG A 395 27.552 57.817 19.083 1.00 35.26 ATOM 2764 NH2 ARG A 395 26.684 55.916 20.038 1.00 35.52 ATOM 2765 C ARG A 395 20.577 57.637 17.377 1.00 36.89 ATOM 2766 0 ARG A 395 19.863 58.453 17.956 1.00 38.27 ATOM 2767 N ARG A 396 20.650 57.561 16.053 1.00 41.09 ATOM 2768 CA ARG A 396 19.876 58.454 15.202 1.00 45.29 ATOM 2769 CB ARG A 396 20.594 58.671 13.862 1.00 47.75 ATOM 2770 CG ARG A 396 20.593 57.476 12.923 1.00 50.83 ATOM 2771 CD ARG A 396 21.562 57.692 11.761 1.00 53.11 ATOM 2772 NE ARG A 396 21.411 59.015 11.162 1.00 55.40 ATOM 2773 CZ ARG A 396 20.296 59.453 10.587 1.00 57.11 ATOM 2774 NH1 ARG A 396 20.246 60.674 10.069 1.00 57.93 ATOM 2775 NH2 ARG A 396 19.231 58.668 10.524 1.00 58.62 ATOM 2776 C ARG A 396 18.478 57.885 14.970 1.00 46.68 ATOM 2777 O ARG A 396 17.498 58.657 15.061 1.00 47.16 ATOM 2778 OXT ARG A 396 18.379 56.671 14.696 1.00 48.86 TER 1 ARG A 396 END

Figure 4 CRYST1 90.692 90.692 123.221 90. 00 90. 00 120.00 P 32 2 1 12 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1. 0.00000 SCALE1 0.011026 0.006366 0.000000 0.00000 SCALE2 0.000000 0.012732 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008115 0.00000 ATOM 2779 N1 FMN 398 48.982 36.086 32.351 1.00 13.65 ATOM 2780 C2 FMN 398 48.621 35.465 31.196 1.00 15.79 ATOM 2781 02 FMN 398 49.207 35.572 30.149 1.00 16.16 ATOM 2782 N3 FMN 398 47.453 34.623 31.236 1.00 15.84 ATOM 2783 C4 FMN 398 46.691 34.411 32.352 1.00 15.69 ATOM 2784 04 FMN 398 45.690 33.661 32.297 1.00 18.13 ATOM 2785 C4A FMN 398 47.084 35.083 33.587 1.00 14.70 ATOM 2786 N5 FMN 398 46.390 34.934 34.726 1.00 16.27 ATOM 2787 C5A FMN 398 46.793 35.607 35.867 1.00 13.36 ATOM 2788 C6 FMN 398 46.064 35.496 37.124 1.00 10.34 ATOM 2789 C7 FMN 398 46.419 36.162 38.280 1.00 11.27 ATOM 2790 C7M FMN 398 45.627 36.037 39.591 1.00 12.50 ATOM 2791 C8 FMN 398 47.597 37.031 38.258 1.00 12.24 ATOM 2792 C8M FMN 398 48.067 37.811 39.455 1.00 12.12 ATOM 2793 C9 FMN 398 48.309 37.142 37.069 1.00 11.89 ATOM 2794 C9A FMN 398 47.965 36.475 35.873 1.00 13.80 ATOM 2795 N10 FMN 398 48.680 36.591 34.639 1.00 15.34 ATOM 2796 C10 FMN 398 48.300 35.943 33.489 1.00 15.60 ATOM 2797 C1* FMN 398 49.889 37.455 34.581 1.00 13.44 ATOM 2798 C2* FMN 398 49.650 38.935 34.357 1.00 13.38 ATOM 2799 02* FMN 398 49.014 39.163 33.083 1.00 14.11 ATOM 2800 C3* FMN 398 50.988 39.727 34.356 1.00 12.71 ATOM 2801 03* FMN 398 51.831 39.225 33.274 1.00 11.59 ATOM 2802 C4* FMN 398 51.799 39.592 35.655 1.00 12.19 ATOM 2803 04* FMN 398 50.908 39.382 36.778 1.00 9.70 ATOM 2804 C5* FMN 398 52.667 40.790 35.978 1.00 13.16

ATOM 2805 05* FMN 398 51.923 42. 012 36.092 1.00 14.37 ATOM 2806 P FMN 398 51.422 42.666 37.461 1.00 15.94 ATOM 2807 01P FMN 398 50.317 41.745 37.973 1.00 15.70 ATOM 2808 02P FMN 398 50.895 44.013 37.089 1.00 15.09 ATOM 2809 03P FMN 398 52.652 42.679 38.391 1.00 16.83 ATOM 2810 N1 ORO 399 49.032 32.288 36.152 1.00 18.25 ATOM 2811 C2 ORO 399 50.025 33.225 35.839 1.00 17.42 ATOM 2812 03 ORO 399 50.604 33.882 36.700 1.00 19.91 ATOM 2813 N4 ORO 399 50.326 33.372 34.500 1.00 15.40 ATOM 2814 C5 ORO 399 49.749 32.688 33.445 1.00 16.04 ATOM 2815 06 ORO 399 50.091 32.895 32.302 1.00 15.47 ATOM 2816 C7 ORO 399 48.718 31.722 33.822 1.00 15.22 ATOM 2817 C8 ORO 399 48.415 31.571 35.132 1.00 18.83 ATOM 2818 C9 ORO 399 47.365 30.573 35.616 1.00 19.59 ATOM 2819 O10 ORO 399 47.594 29.817 36.545 1.00 21.79 ATOM 2820 Oll ORO 399 46.323 30.677 34.919 1.00 21.84 ATOM 2821 Cl INH 400 35.607 47.222 40.518 1.00 24.78 ATOM 2822 C2 INH 400 35.062 48.080 41.508 1.00 23.86 ATOM 2823 C3 INH 400 35.535 48.013 42.863 1.00 24.02 ATOM 2824 C4 INH 400 36.569 47.072 43.218 1.00 24.44 ATOM 2825 C5 INH 400 37.128 46.196 42.209 1.00 22.48 ATOM 2826 C6 INH 400 38.133 45.216 42.490 1.00 22.48 ATOM 2827 C7 INH 400 36.623 46.291 40.860 1.00 22.67 ATOM 2828 C8 INH 400 38.032 44.391 43.667 1.00 20.92 ATOM 2829 C9 INH 400 38.992 43.378 43.923 1.00 22.05 ATOM 2830 C10 INH 400 40.088 43.146 43.018 1.00 21.93 ATOM 2831 Nll INH 400 40.994 42.107 43.283 1.00 19.47 ATOM 2832 C12 INH 400 40.206 43.966 41.854 1.00 20.67 ATOM 2833 F13 INH 400 41.192 43.777 40.999 1.00 23.37 ATOM 2834 C14 INH 400 39.242 44.990 41.586 1.00 21.17 ATOM 2835 C15 INH 400 41.311 41.338 44.410 1.00 21.10 ATOM 2836 C16 INH 400 42.300 40.258 44.384 1.00 18.97 ATOM 2837 017 INH 400 40.713 41.559 45.466 1.00 24.88 ATOM 2838 C18 INH 400 42.725 39.520 43.331 1.00 18.81 ATOM 2839 C19 INH 400 43.719 38.514 43.792 1.00 18.57 ATOM 2840 C20 INH 400 44.202 39.048 45.143 1.00 18.27 ATOM 2841 C21 INH 400 42.981 39.825 45.638 1.00 16.93

ATOM 2842 C22 INH 400 42.339 39.571 41.901 1.00 19.11 ATOM 2843 023 INH 400 41.535 40.384 41.444 1.00 20.87 ATOM 2844 024 INH 400 42.882 38.689 41.022 1.00 19.27 ATOM 2845 025 INH 400 34.997 48.846 43.813 1.00 26.96 ATOM 2846 C26 INH 400 33.649 48.435 44.070 1.00 28.19 ATOM 2847 C ACT 401 66.322 48.953 35.993 1.00 31.77 ATOM 2848 0 ACT 401 67.328 49.644 36.341 1.00 30.18 ATOM 2849 OXT ACT 401 65.833 48.910 34.832 1.00 32.50 ATOM 2850 CH3 ACT 401 65.696 48.119 37.112 1.00 30.07 ATOM 2851 S S04 402 34.333 40.203 6.362 1.00 35.89 ATOM 2852 O1 S04 402 34.721 41.545 5.893 1.00 38.88 ATOM 2853 02 S04 402 35.521 39.335 6.395 1.00 37.76 ATOM 2854 03 S04 402 33.760 40.298 7.717 1.00 39.48 ATOM 2855 04 S04 402 33.326 39.642 5.444 1.00 38.73 ATOM 2856 S S04 403 36.080 30.092 37.260 1.00 59.73 ATOM 2857 01 S04 403 36.357 31.501 36.909 1.00 59.29 ATOM 2858 02 S04 403 37.023 29.206 36.551 1.00 57.64 ATOM 2859 03 S04 403 36.237 29.908 38.718 1.00 59.62 ATOM 2860 04 S04 403 34.697 29.758 36.868 1.00 59.77 ATOM 2861 OH2 TIP 1 60.060 30.725 53.700 1.00 3.85 ATOM 2862 OH2 TIP 2 52.367 45.630 35.605 1.00 9.31 ATOM 2863 OH2 TIP 3 58.030 49.528 35.970 1.00 11.67 ATOM 2864 OH2 TIP 4 50.550 36.383 40.910 1.00 9.15 ATOM 2865 OH2 TIP 5 58.035 48.907 21.969 1.00 15.13 ATOM 2866 OH2 TIP 6 49.097 40.172 29.373 1.00 13.46 ATOM 2867 OH2 TIP 7 56.666 28.089 42.316 1.00 12.52 ATOM 2868 OH2 TIP 8 37.855 27.076 38.255 1.00 22.25 ATOM 2869 OH2 TIP 9 59.045 31.393 34.498 1.00 17.43 ATOM 2870 OH2 TIP 10 61.985 46.199 19.869 1.00 20.90 ATOM 2871 OH2 TIP 11 33.724 41.447 21.286 1.00 16.51 ATOM 2872 OH2 TIP 12 64.454 32.508 43.713 1.00 25.03 ATOM 2873 OH2 TIP 13 35.247 43.126 16.686 1.00 22.09 ATOM 2874 OH2 TIP 14 58.994 42.404 49.027 1.00 12.52 ATOM 2875 OH2 TIP 15 57.581 44.787 53.944 1.00 22.80 ATOM 2876 OH2 TIP 16 39.067 31.534 29.620 1.00 16.07 ATOM 2877 OH2 TIP 17 42.346 60.681 46.719 1.00 34.08 ATOM 2878 OH2 TIP 18 36.301 36.571 33.168 1.00 15.41

ATOM 2879 OH2 TIP 19 41. 935 30.030 45.729 1.00 19.39 ATOM 2880 OH2 TIP 20 42.353 40.596 31.923 1.00 13.54 ATOM 2881 OH2 TIP 21 40.520 40.057 13.943 1.00 15.83 ATOM 2882 OH2 TIP 22 39.285 53.585 28.554 1.00 17.52 ATOM 2883 OH2 TIP 23 35.343 25.302 23.916 1.00 17.49 ATOM 2884 OH2 TIP 24 60.804 49.477 36.760 1.00 18.25 ATOM 2885 OH2 TIP 25 39.416 24.528 14.376 1.00 27.09 ATOM 2886 OH2 TIP 26 50.670 45.964 38.922 1.00 12.31 ATOM 2887 OH2 TIP 27 51.502 36.631 52.577 1.00 18.23 ATOM 2888 OH2 TIP 28 54.818 52.146 42.516 1.00 22.73 ATOM 2889 OH2 TIP 29 33.864 26.690 25.789 1.00 19.94 ATOM 2890 OH2 TIP 30 65.696 40.626 33.942 1.00 21.89 ATOM 2891 OH2 TIP 31 56.168 51.708 18.745 1.00 29.01 ATOM 2892 OH2 TIP 32 54.982 30.599 52.611 1.00 18.21 ATOM 2893 OH2 TIP 33 38.144 40.983 5.331 1.00 31.87 ATOM 2894 OH2 TIP 34 33.676 34.519 15.071 1.00 23.56 ATOM 2895 OH2 TIP 35 62.221 42.445 44.141 1.00 20.83 ATOM 2896 OH2 TIP 36 59.679 52.708 39.168 1.00 20.48 ATOM 2897 OH2 TIP 37 51.513 48.458 44.581 1.00 28.15 ATOM 2898 OH2 TIP 38 51.079 45.614 43.529 1.00 16.70 ATOM 2899 OH2 TIP 39 32.029 49.946 26.001 1.00 26.17 ATOM 2900 OH2 TIP 40 35.203 32.402 15.435 1.00 26.10 ATOM 2901 OH2 TIP 41 68.467 50.979 34.362 1.00 21.55 ATOM 2902 OH2 TIP 42 52.544 29.461 52.556 1.00 23.72 ATOM 2903 OH2 TIP 43 48.533 27.810 33.536 1.00 19. 98 ATOM 2904 OH2 TIP 44 63.782 52.953 32.497 1.00 19.82 ATOM 2905 OH2 TIP 45 66.426 48.144 40.544 1.00 15.64 ATOM 2906 OH2 TIP 46 63.396 36.742 31.190 1.00 34.59 ATOM 2907 OH2 TIP 47 65.569 53.618 20.355 1.00 33.40 ATOM 2908 OH2 TIP 48 43.542 29.587 9.732 1.00 24.10 ATOM 2909 OH2 TIP 49 72.437 31.865 28.980 1.00 27.82 ATOM 2910 OH2 TIP 50 38.905 23.141 44.956 1.00 37.59 ATOM 2911 OH2 TIP 51 42.809 30.953 32.234 1.00 27.21 ATOM 2912 OH2 TIP 52 43.248 53.783 44.946 1.00 21.23 ATOM 2913 OH2 TIP 53 53.351 36.194 8.506 1.00 36.32 ATOM 2914 OH2 TIP 54 56.693 24.667 43.143 1.00 39.40 ATOM 2915 OH2 TIP 55 66.806 41.088 31.475 1.00 30.36

ATOM 2916 OH2 TIP 56 37.574 23.750 20.244 1.00 41.77 ATOM 2917 OH2 TIP 57 70.299 32.603 18.834 1.00 32.10 ATOM 2918 OH2 TIP 58 54.515 58.147 39.651 1.00 28.68 ATOM 2919 OH2 TIP 59 51.721 56.894 43.342 1.00 19.99 ATOM 2920 OH2 TIP 60 38.442 41.829 13.935 1.00 25.07 ATOM 2921 OH2 TIP 61 43.655 62.897 37.603 1.00 43.03 ATOM 2922 OH2 TIP 62 45.750 42.115 46.652 1.00 26.72 ATOM 2923 OH2 TIP 63 69.417 37.196 19.214 1.00 23. 58 ATOM 2924 OH2 TIP 64 31.743 44.583 31.047 1.00 22.02 ATOM 2925 OH2 TIP 65 31.729 43.466 28.354 1.00 20.77 ATOM 2926 OH2 TIP 66 49.885 61.184 42.216 1.00 36.18 ATOM 2927 OH2 TIP 67 34.384 35.165 36.872 1.00 40.36 ATOM 2928 OH2 TIP 68 51.653 37.967 55.085 1.00 22.01 ATOM 2929 OH2 TIP 69 29.355 39.640 25.875 1.00 26.40 ATOM 2930 OH2 TIP 70 42.464 21.852 34.480 1.00 28.86 ATOM 2931 OH2 TIP 71 45.229 22.919 34.845 1.00 31.09 ATOM 2932 OH2 TIP 72 42.964 20.824 23.475 1.00 27.79 ATOM 2933 OH2 TIP 73 60.952 63.544 36.337 1.00 27.14 ATOM 2934 OH2 TIP 74 63.312 23.939 22.011 1.00 37.06 ATOM 2935 OH2 TIP 75 66.301 28.555 23.465 1.00 28.01 ATOM 2936 OH2 TIP 76 60.676 38.163 57.470 1.00 34.78 ATOM 2937 OH2 TIP 77 52.460 26.054 39.635 1.00 40.06 ATOM 2938 OH2 TIP 78 62.406 35.903 49.759 1.00 27.79 ATOM 2939 OH2 TIP 79 52.178 53.523 44.125 1.00 35.13 ATOM 2940 OH2 TIP 80 42.554 58.098 40.280 1.00 33.38 ATOM 2941 OH2 TIP 81 58.030 41.857 58.164 1.00 30.26 ATOM 2942 OH2 TIP 82 59.733 49.051 19.405 1.00 27.97 ATOM 2943 OH2 TIP 83 36.034 27.617 34.567 1.00 34.15 ATOM 2944 OH2 TIP 84 26.557 35.421 20.896 1.00 29.67 ATOM 2945 OH2 TIP 85 55.473 51.440 48.459 1.00 33.01 ATOM 2946 OH2 TIP 86 42.649 50.960 16.828 1.00 31.38 ATOM 2947 OH2 TIP 87 66.170 32.041 14.438 1.00 35.56 ATOM 2948 OH2 TIP 88 70.923 46.419 19.569 1.00 29.27 ATOM 2949 OH2 TIP 89 56.751 32.577 34.130 1.00 25.63 ATOM 2950 OH2 TIP 90 42.493 35.941 41.050 1.00 33.08 ATOM 2951 OH2 TIP 91 30.681 28.816 16.556 1.00 27.33 ATOM 2952 OH2 TIP 92 46.460 24.293 44.169 1.00 34.16

ATOM 2953 OH2 TIP 93 48.432 24.353 11.034 1.00 34.69 ATOM 2954 OH2 TIP 94 52.557 59.642 21.794 1.00 25.61 ATOM 2955 OH2 TIP 95 41.084 32.123 47.677 1.00 29.77 ATOM 2956 OH2 TIP 96 46.793 44.614 13.529 1.00 44.70 ATOM 2957 OH2 TIP 97 53.521 22.830 45.046 1.00 29.14 ATOM 2958 OH2 TIP 98 29.812 30.485 31.098 1.00 33.09 ATOM 2959 OH2 TIP 99 32.089 40.898 27.978 1.00 25.82 ATOM 2960 OH2 TIP 100 52.375 32.327 7.043 1.00 32.25 ATOM 2961 OH2 TIP 101 62.327 42.900 40.662 1.00 22.77 ATOM 2962 OH2 TIP 102 64.175 37.371 41.404 1.00 35.08 ATOM 2963 OH2 TIP 103 59.638 59.791 38.765 1.00 31.48 ATOM 2964 OH2 TIP 104 32.709 26.673 29.792 1.00 28.88 ATOM 2965 OH2 TIP 105 51.017 50.179 13.353 1.00 42. 02 ATOM 2966 OH2 TIP 106 44.398 28.252 22.452 1.00 27.78 ATOM 2967 OH2 TIP 107 47.749 23.069 33.446 1.00 41.42 ATOM 2968 OH2 TIP 108 45.086 48.695 49.919 1.00 43.00 ATOM 2969 OH2 TIP 109 44.998 67.007 24.798 1.00 47.56 ATOM 2970 OH2 TIP 110 54.365 45.236 14.693 1.00 40.44 ATOM 2971 OH2 TIP 111 53.518 47.725 14.954 1.00 35.35 ATOM 2972 OH2 TIP 112 59.581 28.126 10.019 1.00 33.27 ATOM 2973 OH2 TIP 113 64.379 34.664 37.556 1.00 37.42 ATOM 2974 OH2 TIP 114 35.688 41.444 14.660 1.00 30.13 ATOM 2975 OH2 TIP 115 37.327 48.122 13.936 1.00 33.07 ATOM 2976 OH2 TIP 116 39.099 24.372 17.130 1.00 44.61 ATOM 2977 OH2 TIP 117 66.062 41.012 46.358 1.00 29.39 ATOM 2978 OH2 TIP 118 47.642 36.763 4.574 1.00 35.65 ATOM 2979 OH2 TIP 119 65.270 38.095 32.836 1.00 41.52 ATOM 2980 OH2 TIP 120 48.628 65.085 34.950 1.00 37.26 ATOM 2981 OH2 TIP 121 25.753 46.099 24.755 1.00 44.46 ATOM 2982 OH2 TIP 122 37.685 32.073 40.100 1.00 37.09 ATOM 2983 OH2 TIP 123 63.723 66.856 33.778 1.00 37.70 ATOM 2984 OH2 TIP 124 61.504 51.786 18.568 1.00 41.55 ATOM 2985 OH2 TIP 125 46.476 24.073 31.375 1.00 23.40 ATOM 2986 OH2 TIP 126 60.304 30.723 48.847 1.00 32.91 ATOM 2987 OH2 TIP 127 54.304 24.230 35.850 1.00 41.67 ATOM 2988 OH2 TIP 129 66.979 38.849 45.036 1.00 41.82 ATOM 2989 OH2 TIP 130 42.233 35.385 38.170 1.00 27.93

ATOM 2990 OH2 TIP 131 60.719 30.545 31.856 1.00 38.36 ATOM 2991 OH2 TIP 132 40.738 39.057 2.892 1.00 32.59 ATOM 2992 OH2 TIP 133 62.708 23.986 25.043 1.00 42.43 ATOM 2993 OH2 TIP 134 35.497 41.399 19.114 1.00 25.27 ATOM 2994 OH2 TIP 135 53.296 39.609 11.264 1.00 38.06 ATOM 2995 OH2 TIP 136 32.634 36.735 38.827 1.00 45.72 ATOM 2996 OH2 TIP 137 51.884 57.784 17.735 1.00 44.09 ATOM 2997 OH2 TIP 138 52.590 51.257 45.492 1.00 41.96 ATOM 2998 OH2 TIP 139 69.561 35.796 14.477 1.00 45.47 ATOM 2999 OH2 TIP 140 43.069 52.778 14.466 1.00 38.58 ATOM 3000 OH2 TIP 141 44.350 60.071 23.707 1.00 34.18 ATOM 3001 OH2 TIP 142 40.145 56.197 29.092 1.00 32.21 ATOM 3002 OH2 TIP 143 68.741 38.750 17.070 1.00 47. 07 ATOM 3003 OH2 TIP 144 42.642 19.568 29.836 1.00 36.77 ATOM 3004 OH2 TIP 145 40.366 33.392 37.870 1.00 31.48 ATOM 3005 OH2 TIP 146 71.730 51.850 23.663 1.00 42.26 ATOM 3006 OH2 TIP 147 49.116 40.579 56.678 1.00 46.10 ATOM 3007 OH2 TIP 148 47.913 30.808 5.178 1.00 46.45 ATOM 3008 OH2 TIP 149 38.099 34.045 36.957 1.00 42.98 ATOM 3009 OH2 TIP 150 64.592 30.466 24.304 1.00 40.67 ATOM 3010 OH2 TIP 151 28.792 49.500 27.018 1.00 47.07 ATOM 3011 OH2 TIP 152 38.062 36.480 35.087 1.00 34.16 ATOM 3012 OH2 TIP 153 55.920 46.433 49.521 1.00 45.73 ATOM 3013 OH2 TIP 154 44.328 37.046 1.316 1.00 46.31 TER 1 TIP 154 ATOM 1 CB MET A 30 31.574 53.310 46.169 1.00 84.87 ATOM 2 CG MET A 30 31.623 52.655 47.538 1.00 86.03 ATOM 3 SD MET A 30 30.794 51.051 47.554 1.00 88.57 ATOM 4 CE MET A 30 29.099 51.544 47.904 1.00 88.24 ATOM 5 C MET A 30 32.230 55.176 44.652 1.00 83.28 ATOM 6 0 MET A 30 33.176 55.117 43.866 1.00 82.94 ATOM 7 N MET A 30 31.862 55.601 47.078 1.00 84.20 ATOM 8 CA MET A 30 32.359 54.621 46.067 1.00 84.06 ATOM 9 N ALA A 31 31.054 55.713 44.336 1.00 82.18 ATOM 10 CA ALA A 31 30.785 56.279 43.017 1.00 80.47 ATOM 11 CB ALA A 31 29.325 56.713 42.925 1.00 80.79 ATOM 12 C ALA A 31 31.701 57.461 42.704 1.00 79.07

ATOM 13 O ALA A 31 32.146 57.628 41.567 1.00 78.92 ATOM 14 N THR A 32 31. 976 58.280 43.716 1.00 77.24 ATOM 15 CA THR A 32 32.841 59.446 43.550 1.00 74.71 ATOM 16 CB THR A 32 33.148 60.116 44.908 1.00 75.25 ATOM 17 OG1 THR A 32 31.953 60.706 45.435 1.00 74.93 ATOM 18 CG2 THR A 32 34.216 61.190 44.743 1.00 75.54 ATOM 19 C THR A 32 34.163 59.066 42.892 1.00 71.95 ATOM 20 0THR A 32 34.569 59.666 41.896 1.00 72.33 ATOM 21 N GLY A 33 34.831 58.065 43.457 1.00 68.40 ATOM 22 CA GLY A 33 36.100 57.626 42.908 1.00 63.03 ATOM 23 C GLY A 33 37.268 58.373 43.508 1.00 58.58 ATOM 24 0 GLY A 33 37.724 59.370 42.951 1.00 59.69 ATOM 25 N ASP A 34 37.758 57.889 44.643 1.00 53.42 ATOM 26 CA ASP A 34 38.876 58.532 45.315 1.00 47.16 ATOM 27 CB ASP A 34 38.365 59.272 46.551 1.00 46.88 ATOM 28 CG ASP A 34 39.476 59.876 47.365 1.00 45.83 ATOM 29 OD1 ASP A 34 40.058 59.148 48.193 1.00 46.55 ATOM 30 OD2 ASP A 34 39.772 61.075 47.172 1.00 46.46 ATOM 31 C ASP A 34 39.979 57.542 45.687 1.00 44.21 ATOM 32 0ASP A 34 39.731 56.508 46.310 1.00 40.97 ATOM 33 N GLU A 35 41.202 57. 878 45.290 1.00 41.79 ATOM 34 CA GLU A 35 42.369 57.041 45.536 1.00 39.52 ATOM 35 CB GLU A 35 43.618 57.733 44.988 1.00 39.60 ATOM 36 CG GLU A 35 43.639 57.855 43.471 1.00 41.54 ATOM 37 CD GLU A 35 44.721 58.798 42.973 1.00 43.04 ATOM 38 OE1 GLU A 35 45.780 58.884 43.631 1.00 44.35 ATOM 39 OE2 GLU A 35 44.519 59.441 41.919 1.00 42.18 ATOM 40 C GLU A 35 42.587 56.669 46.998 1.00 37.40 ATOM 41 O GLU A 35 42.891 55.518 47.308 1.00 36.91 ATOM 42 N ARG A 36 42.428 57.634 47.896 1.00 36.05 ATOM 43 CA ARG A 36 42.636 57.377 49.315 1.00 34.31 ATOM 44 CB ARG A 36 42.756 58.699 50.077 1.00 38.49 ATOM 45 CG ARG A 36 44.042 58.824 50.893 1.00 43.28 ATOM 46 CD ARG A 36 44.289 60.252 51.356 1.00 47.33 ATOM 47 NE ARG A 36 44.557 61.139 50.225 1.00 52.51 ATOM 48 CZ ARG A 36 44.701 62.459 50.316 1.00 54.87 ATOM 49 NH1 ARG A 36 44.603 63.067 51.492 1.00 56.47

ATOM 50 NH2 ARG A 36 44.948 63.173 49.225 1.00 55.27 ATOM 51 C ARG A 36 41.534 56.517 49.920 1.00 31.92 ATOM 52 O ARG A 36 41.799 55.667 50.771 1.00 31.50 ATOM 53 N PHE A 37 40.301 56.721 49.472 1.00 29.13 ATOM 54 CA PHE A 37 39.185 55.945 49.996 1.00 27.89 ATOM 55 CB PHE A 37 37.853 56.469 49.451 1.00 28.59 ATOM 56 CG PHE A 37 36.673 55.643 49.867 1.00 30.69 ATOM 57 CD1 PHE A 37 36.289 55.582 51.197 1.00 32.45 ATOM 58 CD2 PHE A 37 35.977 54.885 48.938 1.00 31.58 ATOM 59 CE1 PHE A 37 35.234 54.778 51.594 1.00 32.16 ATOM 60 CE2 PHE A 37 34.921 54.078 49.329 1.00 32.49 ATOM 61 CZ PHE A 37 34.551 54.025 50.659 1.00 31.20 ATOM 62 C PHE A 37 39.314 54.463 49.660 1.00 26.36 ATOM 63 0 PHE A 37 39.115 53.603 50.516 1.00 25.18 ATOM 64 N TYR A 38 39.638 54.164 48.408 1.00 25.54 ATOM 65 CA TYR A 38 39.778 52.777 47.992 1.00 25.07 ATOM 66 CB TYR A 38 39.877 52.682 46.471 1.00 24.76 ATOM 67 CG TYR A 38 38.533 52.662 45.790 1.00 23.78 ATOM 68 CD1 TYR A 38 37.778 53.820 45.660 1.00 22.64 ATOM 69 CE1 TYR A 38 36.536 53.792 45.061 1.00 23.66 ATOM 70 CD2 TYR A 38 38.007 51.473 45.301 1.00 20.64 ATOM 71 CE2 TYR A 38 36.771 51.433 44.706 1.00 21.87 ATOM 72 CZ TYR A 38 36.039 52.591 44.588 1.00 23.46 ATOM 73 OH TYR A 38 34.804 52.542 44.000 1.00 25.38 ATOM 74 C TYR A 38 40.982 52.105 48.622 1.00 25.60 ATOM 75 0 TYR A 38 40.892 50.976 49.105 1.00 23.56 ATOM 76 N ALA A 39 42.106 52.814 48.617 1.00 27.30 ATOM 77 CA ALA A 39 43.350 52.299 49.172 1.00 29.38 ATOM 78 CB ALA A 39 44.489 53.265 48.860 1.00 29.11 ATOM 79 C ALA A 39 43.288 52.045 50.673 1.00 31.61 ATOM 80 0 ALA A 39 43.717 50.992 51.153 1.00 31.66 ATOM 81 N GLU A 40 42.745 53.006 51.414 1.00 34.51 ATOM 82 CA GLU A 40 42.670 52.889 52.867 1.00 36.59 ATOM 83 CB GLU A 40 42.856 54.268 53.511 1.00 37.79 ATOM 84 CG GLU A 40 44.205 54.910 53.224 1.00 40.73 ATOM 85 CD GLU A 40 44.332 56.299 53.821 1.00 43.21 ATOM 86 OE1 GLU A 40 44.189 56.439 55.057 1.00 44.07

ATOM 87 OE2 GLU A 40 44.579 57. 252 53.055 1.00 42.96 ATOM 88 C GLU A 40 41.415 52.246 53.443 1.00 36.74 ATOM 89 0 GLU A 40 41.452 51.743 54.567 1.00 37.63 ATOM 90 N HIS A 41 40.310 52.242 52.700 1.00 35.29 ATOM 91 CA HIS A 41 39.088 51.664 53.253 1.00 33.66 ATOM 92 CB HIS A 41 38.084 52.777 53.566 1.00 34.87 ATOM 93 CG HIS A 41 38.580 53.754 54.581 1.00 36.99 ATOM 94 CD2 HIS A 41 38.568 53.714 55.934 1.00 37.45 ATOM 95 ND1 HIS A 41 39.253 54.907 54.237 1.00 38.03 ATOM 96 CE1 HIS A 41 39.636 55.534 55.334 1.00 38.68 ATOM 97 NE2 HIS A 41 39.234 54.831 56.378 1.00 39.29 ATOM 98 C HIS A 41 38.372 50.557 52.497 1.00 31.54 ATOM 99 0 HIS A 41 38.222 49.450 53.016 1.00 31.30 ATOM 100 N LEU A 42 37.917 50.843 51.285 1.00 29.85 ATOM 101 CA LEU A 42 37.186 49.839 50.533 1.00 28.77 ATOM 102 CB LEU A 42 36.677 50.426 49.208 1.00 28.98 ATOM 103 CG LEU A 42 35.637 49.562 48.477 1.00 29.95 ATOM 104 CD1 LEU A 42 34.785 50.431 47.569 1.00 29.75 ATOM 105 CD2 LEU A 42 36.336 48.459 47.687 1.00 29.98 ATOM 106 C LEU A 42 37.970 48.552 50.278 1.00 27.67 ATOM 107 O LEU A 42 37.522 47.470 50.662 1.00 28.28 ATOM 108 N MET A 43 39.133 48.655 49.643 1.00 25.24 ATOM 109 CA MET A 43 39.919 47.457 49.347 1.00 24.82 ATOM 110 CB MET A 43 41.166 47.820 48.535 1.00 22.03 ATOM 111 CG MET A 43 40.856 48.385 47.150 1.00 20.76 ATOM 112 SD MET A 43 39.792 47.312 46.142 1.00 22.83 ATOM 113 CE MET A 43 40. 970 46.112 45.560 1.00 16.61 ATOM 114 C MET A 43 40.311 46.660 50.593 1.00 24.94 ATOM 115 0 MET A 43 40.160 45.441 50.627 1.00 24.63 ATOM 116 N PRO A 44 40.822 47.335 51.632 1.00 26.27 ATOM 117 CD PRO A 44 41.271 48.738 51.698 1.00 25.74 ATOM 118 CA PRO A 44 41.204 46.603 52.844 1.00 27.11 ATOM 119 CB PRO A 44 41.767 47.700 53.742 1.00 27.91 ATOM 120 CG PRO A 44 42.352 48.671 52.747 1.00 27.46 ATOM 121 C PRO A 44 40.016 45.877 53.483 1.00 28.57 ATOM 122 O PRO A 44 40. 156 44.762 53.984 1.00 29.09 ATOM 123 N THR A 45 38.848 46.510 53.463 1.00 29.17

ATOM 124 CA THR A 45 37.651 45.903 54.038 1.00 30.69 ATOM 125 CB THR A 45 36.456 46.884 54.021 1.00 31.67 ATOM 126 OG1 THR A 45 36.729 47.984 54.897 1.00 32.25 ATOM 127 CG2 THR A 45 35.180 46.182 54.469 1.00 29.83 ATOM 128 C THR A 45 37.270 44.660 53.244 1.00 30.58 ATOM 129 0 THR A 45 36.945 43.617 53.808 1.00 31.05 ATOM 130 N LEU A 46 37.316 44.782 51. 925 1.00 30.78 ATOM 131 CA LEU A 46 36.982 43.677 51.041 1.00 31.05 ATOM 132 CB LEU A 46 37.128 44.127 49.587 1.00 30.41 ATOM 133 CG LEU A 46 36.837 43.103 48.493 1.00 32.94 ATOM 134 CD1 LEU A 46 35.421 42.563 48.647 1.00 33.88 ATOM 135 CD2 LEU A 46 37.010 43.761 47.133 1.00 33.97 ATOM 136 C LEU A 46 37.878 42.466 51.305 1.00 31.41 ATOM 137 O LEU A 46 37.402 41.332 51.363 1.00 31.43 ATOM 138 N GLN A 47 39.175 42.711 51.472 1.00 31.41 ATOM 139 CA GLN A 47 40.133 41.635 51.717 1.00 33.75 ATOM 140 CB GLN A 47 41.565 42.151 51.542 1.00 34.91 ATOM 141 CG GLN A 47 41.812 42.791 50.186 1.00 38.32 ATOM 142 CD GLN A 47 41.505 41.859 49.019 1.00 39.37 ATOM 143 OE1 GLN A 47 41.452 42.296 47.870 1.00 41.29 ATOM 144 NE2 GLN A 47 41.311 40.573 49.307 1.00 37.71 ATOM 145 C GLN A 47 39. 981 40.999 53.094 1.00 33.50 ATOM 146 0 GLN A 47 40.391 39.861 53.306 1.00 32.66 ATOM 147 N GLY A 48 39.393 41.739 54.027 1.00 34.33 ATOM 148 CA GLY A 48 39. 193 41.209 55.361 1.00 34.12 ATOM 149 C GLY A 48 37.925 40.379 55.422 1.00 34.95 ATOM 150 0 GLY A 48 37.744 39.576 56.336 1.00 36.30 ATOM 151 N LEU A 49 37.049 40.562 54.438 1.00 33.88 ATOM 152 CA LEU A 49 35.785 39.829 54.399 1.00 33.94 ATOM 153 CB LEU A 49 34.644 40.762 53.979 1.00 34.56 ATOM 154 CG LEU A 49 34.289 41.903 54.934 1.00 35.63 ATOM 155 CD1 LEU A 49 33.179 42.746 54.335 1.00 33.76 ATOM 156 CD2 LEU A 49 33.862 41.324 56.277 1.00 35.21 ATOM 157 C LEU A 49 35.794 38.627 53.469 1.00 32.93 ATOM 158 0 LEU A 49 35.129 37.629 53.734 1.00 34.79 ATOM 159 N LEU A 50 36.542 38.719 52.377 1.00 31.80 ATOM 160 CA LEU A 50 36.590 37.633 51.405 1.00 30.50

ATOM 161 CB LEU A 50 35. 997 38.106 50.074 1.00 31. 09 ATOM 162 CG LEU A 50 34.525 38.517 50.048 1.00 32.47 ATOM 163 CD1 LEU A 50 34.219 39.247 48.745 1.00 32.88 ATOM 164 CD2 LEU A 50 33.651 37.283 50.193 1.00 30.73 ATOM 165 C LEU A 50 37.991 37.107 51.146 1.00 29.49 ATOM 166 0 LEU A 50 38.979 37.818 51.326 1.00 29.57 ATOM 167 N ASP A 51 38.068 35.852 50.717 1.00 28.16 ATOM 168 CA ASP A 51 39.346 35.250 50.384 1.00 27.52 ATOM 169 CB ASP A 51 39.212 33.727 50.313 1.00 29.07 ATOM 170 CG ASP A 51 38.180 33.279 49.300 1.00 33.09 ATOM 171 OD1 ASP A 51 36.984 33.589 49.495 1.00 35.70 ATOM 172 OD2 ASP A 51 38.565 32.621 48.308 1.00 33.73 ATOM 173 C ASP A 51 39.723 35.833 49.015 1.00 26.45 ATOM 174 0 ASP A 51 38.863 36.344 48.292 1.00 25.84 ATOM 175 N PRO A 52 41.009 35.764 48.643 1.00 24.56 ATOM 176 CD PRO A 52 42.083 35.090 49.390 1.00 22.91 ATOM 177 CA PRO A 52 41.519 36.286 47.371 1.00 23.09 ATOM 178 CB PRO A 52 42.928 35.707 47.308 1.00 23.93 ATOM 179 CG PRO A 52 43.319 35.645 48.731 1.00 23.45 ATOM 180 C PRO A 52 40.698 35.940 46.129 1.00 21.14 ATOM 181 0 PRO A 52 40.314 36.828 45.370 1.00 20.30 ATOM 182 N GLU A 53 40.424 34.658 45.918 1.00 19.62 ATOM 183 CA GLU A 53 39.664 34.265 44.739 1.00 20.75 ATOM 184 CB GLU A 53 39.626 32.741 44.597 1.00 20.17 ATOM 185 CG GLU A 53 38.933 32.290 43.320 1.00 21.25 ATOM 186 CD GLU A 53 39.243 30.855 42.944 1.00 22.83 ATOM 187 OE1 GLU A 53 38.632 30.361 41.975 1.00 25.63 ATOM 188 OE2 GLU A 53 40.093 30.220 43.603 1.00 23.30 ATOM 189 C GLU A 53 38.245 34.833 44.734 1.00 21.37 ATOM 190 0 GLU A 53 37.789 35.355 43.712 1.00 20.91 ATOM 191 N SER A 54 37.552 34.745 45.867 1.00 20.10 ATOM 192 CA SER A 54 36.196 35.274 45.951 1.00 20.81 ATOM 193 CB SER A 54 35.588 34.995 47.327 1.00 21.56 ATOM 194 OG SER A 54 35.420 33.606 47.532 1.00 23.22 ATOM 195 C SER A 54 36.208 36.776 45.698 1.00 20.03 ATOM 196 0 SER A 54 35.305 37.314 45.055 1.00 19. 91 ATOM 197 N ALA A 55 37.237 37.448 46.206 1.00 18.25

ATOM 198 CA ALA A 55 37.363 38.887 46. 027 1.00 17.25 ATOM 199 CB ALA A 55 38.584 39.404 46.781 1.00 18.23 ATOM 200 C ALA A 55 37.491 39.191 44.540 1.00 17.58 ATOM 201 0 ALA A 55 36.888 40.136 44.038 1.00 18.04 ATOM 202 N HIS A 56 38.279 38.382 43.837 1.00 17.22 ATOM 203 CA HIS A 56 38.466 38.563 42.404 1.00 18.71 ATOM 204 CB HIS A 56 39.509 37.575 41.875 1.00 17.37 ATOM 205 CG HIS A 56 39.537 37.479 40.383 1.00 16.55 ATOM 206 CD2 HIS A 56 39.262 36.449 39.551 1.00 17.62 ATOM 207 ND1 HIS A 56 39.827 38.558 39.575 1.00 20.55 ATOM 208 CE1 HIS A 56 39.729 38.196 38.309 1.00 17.33 ATOM 209 NE2 HIS A 56 39.387 36.921 38.267 1.00 19.33 ATOM 210 C HIS A 56 37.146 38.368 41.646 1.00 20.76 ATOM 211 0 HIS A 56 36.775 39.196 40.806 1.00 20.87 ATOM 212 N ARG A 57 36.444 37.275 41.943 1.00 21.25 ATOM 213 CA ARG A 57 35.172 36.988 41.287 1.00 23.72 ATOM 214 CB ARG A 57 34.548 35.704 41.846 1.00 27.11 ATOM 215 CG ARG A 57 35.395 34.453 41.619 1.00 33.78 ATOM 216 CD ARG A 57 34.691 33.191 42.119 1.00 38.40 ATOM 217 NE ARG A 57 33.504 32.870 41.328 1.00 44.51 ATOM 218 CZ ARG A 57 33.536 32.421 40.074 1.00 47.98 ATOM 219 NH1 ARG A 57 34.699 32.231 39.460 1.00 48.55 ATOM 220 NH2 ARG A 57 32.404 32.169 39.426 1.00 49.25 ATOM 221 C ARG A 57 34.198 38.148 41.458 1.00 22.08 ATOM 222 0 ARG A 57 33.547 38.561 40.503 1.00 22.37 ATOM 223 N LEU A 58 34.103 38.676 42.674 1.00 22.22 ATOM 224 CA LEU A 58 33.206 39.798 42.941 1.00 21.56 ATOM 225 CB LEU A 58 33.211 40.140 44.434 1.00 22.30 ATOM 226 CG LEU A 58 32.224 41.206 44.926 1.00 23.79 ATOM 227 CD1 LEU A 58 30.798 40.778 44.615 1.00 21.41 ATOM 228 CD2 LEU A 58 32.400 41.405 46.430 1.00 24.56 ATOM 229 C LEU A 58 33.660 41.006 42.121 1.00 21.85 ATOM 230 0 LEU A 58 32.839 41.785 41.636 1.00 21.96 ATOM 231 N ALA A 59 34.973 41.150 41.964 1.00 21.62 ATOM 232 CA ALA A 59 35.548 42.251 41.191 1.00 21.13 ATOM 233 CB ALA A 59 37.063 42.195 41.256 1.00 19.47 ATOM 234 C ALA A 59 35.097 42.166 39.738 1.00 20.15

ATOM 235 O ALA A 59 34.778 43.178 39.110 1.00 20.52 ATOM 236 N VAL A 60 35.090 40.952 39.202 1.00 19.14 ATOM 237 CA VAL A 60 34.674 40.742 37.826 1.00 19.94 ATOM 238 CB VAL A 60 34.888 39.266 37.395 1.00 20.28 ATOM 239 CG1 VAL A 60 34.306 39.029 35.995 1.00 17.45 ATOM 240 CG2 VAL A 60 36.377 38.941 37.401 1.00 16.77 ATOM 241 C VAL A 60 33.206 41.118 37.678 1.00 21.14 ATOM 242 0 VAL A 60 32.827 41.770 36.709 1.00 21.64 ATOM 243 N ARG A 61 32.386 40.718 38.646 1.00 23.53 ATOM 244 CA ARG A 61 30.958 41.024 38.614 1.00 26.90 ATOM 245 CB ARG A 61 30.233 40.410 39.821 1.00 28.84 ATOM 246 CG ARG A 61 30.228 38.890 39.867 1.00 37.63 ATOM 247 CD ARG A 61 29.007 38.376 40.646 1.00 43.68 ATOM 248 NE ARG A 61 28.948 36.915 40.714 1.00 48.20 ATOM 249 CZ ARG A 61 29.617 36.174 41.595 1.00 50. 86 ATOM 250 NH1 ARG A 61 30.401 36.753 42.500 1.00 50.24 ATOM 251 NH2 ARG A 61 29.503 34.850 41.568 1.00 51.48 ATOM 252 C ARG A 61 30.698 42.530 38.605 1.00 26.52 ATOM 253 0 ARG A 61 30.004 43.043 37.727 1.00 25.59 ATOM 254 N PHE A 62 31.250 43.230 39.592 1.00 26.34 ATOM 255 CA PHE A 62 31.061 44.670 39.697 1.00 28.44 ATOM 256 CB PHE A 62 31.812 45.227 40.910 1.00 29.57 ATOM 257 CG PHE A 62 31.012 45.197 42.182 1.00 33.68 ATOM 258 CD1 PHE A 62 30.562 43.997 42.709 1.00 34.80 ATOM 259 CD2 PHE A 62 30.699 46.373 42.844 1.00 35.83 ATOM 260 CE1 PHE A 62 29.813 43.970 43.876 1.00 35.32 ATOM 261 CE2 PHE A 62 29.950 46.353 44.011 1.00 38.21 ATOM 262 CZ PHE A 62 29.507 45.146 44.526 1.00 36.55 ATOM 263 C PHE A 62 31.523 45.388 38.445 1.00 28.73 ATOM 264 0 PHE A 62 30.866 46.318 37.974 1.00 29. 92 ATOM 265 N THR A 63 32.657 44.952 37.908 1.00 27.65 ATOM 266 CA THR A 63 33.205 45.569 36.715 1.00 26.81 ATOM 267 CB THR A 63 34.612 45.017 36.408 1.00 26.29 ATOM 268 OG1 THR A 63 35.493 45.331 37.494 1.00 23.98 ATOM 269 CG2 THR A 63 35.154 45.626 35.129 1.00 23.92 ATOM 270 C THR A 63 32.296 45.342 35.513 1.00 27.15 ATOM 271 O THR A 63 32.031 46. 268 34.750 1.00 26. 07

ATOM 272 N SER A 64 31.812 44.116 35.350 1.00 27.56 ATOM 273 CA SER A 64 30.938 43.802 34.224 1.00 30.29 ATOM 274 CB SER A 64 30.608 42.311 34.204 1.00 29.40 ATOM 275 OG SER A 64 29.850 41.959 35.345 1.00 32.57 ATOM 276 C SER A 64 29.646 44.606 34.312 1.00 31.20 ATOM 277 0 SER A 64 29.007 44.880 33.297 1.00 30.61 ATOM 278 N LEU A 65 29.273 44.984 35.532 1.00 31.93 ATOM 279 CA LEU A 65 28.057 45.756 35.766 1.00 33.43 ATOM 280 CB LEU A 65 27.416 45.335 37.093 1.00 32.99 ATOM 281 CG LEU A 65 26.891 43.899 37.148 1.00 35.43 ATOM 282 CD1 LEU A 65 26.483 43.545 38.573 1.00 33. 63 ATOM 283 CD2 LEU A 65 25.712 43.756 36.189 1.00 34.95 ATOM 284 C LEU A 65 28.318 47.263 35.781 1.00 33.55 ATOM 285 0 LEU A 65 27.397 48.057 35.964 1.00 34.23 ATOM 286 N GLY A 66 29.573 47.654 35.599 1.00 32.60 ATOM 287 CA GLY A 66 29.901 49.068 35.592 1.00 33.27 ATOM 288 C GLY A 66 29.833 49.755 36.948 1.00 34.31 ATOM 289 0 GLY A 66 29.785 50.983 37.017 1.00 34.03 ATOM 290 N LEU A 67 29.823 48.975 38.027 1.00 33.85 ATOM 291 CA LEU A 67 29.776 49.542 39.372 1.00 34.20 ATOM 292 CB LEU A 67 29.338 48.476 40.383 1.00 35.31 ATOM 293 CG LEU A 67 27.989 47.797 40.101 1.00 37.76 ATOM 294 CD1 LEU A 67 27.648 46.833 41.231 1.00 37.88 ATOM 295 CD2 LEU A 67 26.894 48.850 39.959 1.00 37.81 ATOM 296 C LEU A 67 31.181 50.044 39.699 1.00 33.76 ATOM 297 0 LEU A 67 31.889 49.467 40.527 1.00 31.48 ATOM 298 N LEU A 68 31.568 51.128 39.035 1.00 34.01 ATOM 299 CA LEU A 68 32.894 51.713 39.189 1.00 34.57 ATOM 300 CB LEU A 68 33.635 51.632 37.856 1.00 33.46 ATOM 301 CG LEU A 68 33.665 50.257 37. 193 1.00 33.94 ATOM 302 CD1 LEU A 68 34.112 50.389 35.752 1.00 35.15 ATOM 303 CD2 LEU A 68 34.596 49.347 37.966 1.00 32.93 ATOM 304 C LEU A 68 32.858 53.166 39.641 1.00 35.27 ATOM 305 0 LEU A 68 31.884 53.880 39.411 1.00 36.69 ATOM 306 N PRO A 69 33.937 53.622 40.291 1.00 35.09 ATOM 307 CD PRO A 69 35.096 52.799 40.678 1.00 35.32 ATOM 308 CA PRO A 69 34.084 54.987 40.795 1.00 35.10

ATOM 309 CB PRO A 69 35.296 54.876 41.711 1.00 35.36 ATOM 310 CG PRO A 69 36.126 53.847 41.031 1.00 35.57 ATOM 311 C PRO A 69 34.298 55.987 39.664 1.00 34.95 ATOM 312 0 PRO A 69 34.206 55.632 38.488 1.00 35.36 ATOM 313 N PHE A 73 39.366 61.866 34.983 1.00 57.11 ATOM 314 CA PHE A 73 40.556 62.093 34.169 1.00 56.79 ATOM 315 CB PHE A 73 41.700 61.180 34.627 1.00 57.43 ATOM 316 CG PHE A 73 42.919 61.254 33.747 1.00 58.50 ATOM 317 CD1 PHE A 73 43.795 62.325 33.837 1.00 59.04 ATOM 318 CD2 PHE A 73 43.162 60.276 32.793 1.00 58.27 ATOM 319 CE1 PHE A 73 44.891 62.421 32.990 1.00 58.38 ATOM 320 CE2 PHE A 73 44.254 60.368 31.944 1.00 58.17 ATOM 321 CZ PHE A 73 45.119 61.442 32.042 1.00 57.71 ATOM 322 C PHE A 73 40. 302 61.851 32.681 1.00 55.94 ATOM 323 O PHE A 73 39.909 60.755 32.279 1.00 55.31 ATOM 324 N GLN A 74 40.534 62.875 31.866 1.00 54.83 ATOM 325 CA GLN A 74 40.352 62.752 30.425 1.00 53.34 ATOM 326 CB GLN A 74 39.707 64.013 29.848 1.00 55.61 ATOM 327 CG GLN A 74 38.222 64.153 30.133 1.00 57.81 ATOM 328 CD GLN A 74 37.578 65.243 29.291 1.00 59.81 ATOM 329 OE1 GLN A 74 37.852 66.432 29.472 1.00 60.73 ATOM 330 NE2 GLN A 74 36.725 64.840 28.353 1.00 59.42 ATOM 331 C GLN A 74 41.698 62.517 29.749 1.00 51.28 ATOM 332 O GLN A 74 42.650 63.267 29.964 1.00 50.95 ATOM 333 N ASP A 75 41.774 61.471 28.935 1.00 48.79 ATOM 334 CA ASP A 75 43.006 61.145 28.229 1.00 46.68 ATOM 335 CB ASP A 75 42.824 59.856 27.421 1.00 45.00 ATOM 336 CG ASP A 75 42.570 58.642 28.299 1.00 43.45 ATOM 337 OD1 ASP A 75 42.067 57.627 27.770 1.00 41.56 ATOM 338 OD2 ASP A 75 42.881 58.696 29.508 1.00 41.80 ATOM 339 C ASP A 75 43.378 62.286 27.288 1.00 46.07 ATOM 340 O ASP A 75 42.529 62.798 26.558 1.00 45.66 ATOM 341 N SER A 76 44.645 62.688 27.308 1.00 45.37 ATOM 342 CA SER A 76 45.105 63.763 26.437 1.00 44.09 ATOM 343 CB SER A 76 46.045 64.706 27.193 1.00 44.35 ATOM 344 OG SER A 76 47.276 64.074 27.492 1.00 45.29 ATOM 345 C SER A 76 45.830 63.171 25.236 1.00 42.66

ATOM 346 O SER A 76 46.194 61.997 25.240 1.00 42.40 ATOM 347 N ASP A 77 46.033 63.987 24.209 1.00 42.12 ATOM 348 CA ASP A 77 46.719 63.545 23.001 1.00 41.76 ATOM 349 CB ASP A 77 46.909 64.727 22.047 1.00 44.71 ATOM 350 CG ASP A 77 45.595 65.295 21.551 1.00 47. 31 ATOM 351 OD1 ASP A 77 45.623 66.334 20.859 1.00 50.25 ATOM 352 OD2 ASP A 77 44.535 64.702 21.846 1.00 48.62 ATOM 353 C ASP A 77 48.080 62.931 23.318 1.00 40.11 ATOM 354 O ASP A 77 48.532 62.019 22.627 1.00 39.81 ATOM 355 N MET A 78 48.728 63.440 24.361 1.00 37.97 ATOM 356 CA MET A 78 50.044 62.949 24.769 1.00 36.17 ATOM 357 CB MET A 78 50.517 63.660 26.036 1.00 37.17 ATOM 358 CG MET A 78 50.848 65.124 25.881 1.00 39.57 ATOM 359 SD MET A 78 51.536 65.736 27.440 1.00 42.24 ATOM 360 CE MET A 78 53.252 65.210 27.264 1.00 41.08 ATOM 361 C MET A 78 50.067 61.452 25.044 1.00 32.99 ATOM 362 0 MET A 78 51.070 60.786 24.799 1.00 31.46 ATOM 363 N LEU A 79 48.965 60.927 25.567 1.00 30.29 ATOM 364 CA LEU A 79 48.899 59.512 25.893 1.00 29.12 ATOM 365 CB LEU A 79 47.916 59.285 27.045 1.00 27.76 ATOM 366 CG LEU A 79 48.297 59.972 28.363 1.00 27.32 ATOM 367 CD1 LEU A 79 47.400 59.469 29.489 1.00 25.53 ATOM 368 CD2 LEU A 79 49.756 59.681 28.687 1.00 23.95 ATOM 369 C LEU A 79 48.545 58.604 24.721 1.00 28.57 ATOM 370 0 LEU A 79 48.563 57.379 24.863 1.00 28.17 ATOM 371 N GLU A 80 48.238 59.188 23.567 1.00 26.89 ATOM 372 CA GLU A 80 47.890 58.382 22.407 1.00 27.84 ATOM 373 CB GLU A 80 47.230 59.221 21.309 1.00 29.86 ATOM 374 CG GLU A 80 46.633 58.344 20.206 1.00 36.28 ATOM 375 CD GLU A 80 46.323 59.094 18.918 1.00 39.58 ATOM 376 OE1 GLU A 80 47.270 59.411 18.165 1.00 40.87 ATOM 377 OE2 GLU A 80 45.129 59.362 18.659 1.00 41.08 ATOM 378 C GLU A 80 49.118 57.705 21.822 1.00 27.25 ATOM 379 0 GLU A 80 50.192 58.298 21.748 1.00 26.76 ATOM 380 N VAL A 81 48.949 56.461 21.395 1.00 26.60 ATOM 381 CA VAL A 81 50.040 55.701 20.810 1.00 26.88 ATOM 382 CB VAL A 81 50.640 54.702 21.830 1.00 27.64

ATOM 383 CG1 VAL A 81 51.781 53.927 21.190 1.00 27.14 ATOM 384 CG2 VAL A 81 51.114 55.435 23. 066 1.00 27.80 ATOM 385 C VAL A 81 49.515 54.900 19.634 1.00 27.49 ATOM 386 0 VAL A 81 48.376 54.442 19.651 1.00 29.86 ATOM 387 N ARG A 82 50.337 54.741 18.605 1.00 28.74 ATOM 388 CA ARG A 82 49. 936 53.947 17.453 1.00 30.33 ATOM 389 CB ARG A 82 49.821 54.804 16.186 1.00 32.47 ATOM 390 CG ARG A 82 49.899 53.969 14.905 1.00 38.74 ATOM 391 CD ARG A 82 49.248 54.638 13.697 1.00 44.42 ATOM 392 NE ARG A 82 47.836 54.269 13.548 1.00 48.91 ATOM 393 CZ ARG A 82 47.397 53.029 13.330 1.00 48.71 ATOM 394 NH1 ARG A 82 48.252 52.018 13.233 1.00 47.85 ATOM 395 NH2 ARG A 82 46.096 52.799 13.205 1.00 50.04 ATOM 396 C ARG A 82 50.939 52.822 17.228 1.00 29.93 ATOM 397 0 ARG A 82 52.115 53.068 16.972 1.00 29.16 ATOM 398 N VAL A 83 50.461 51.587 17.347 1.00 29.81 ATOM 399 CA VAL A 83 51.281 50.394 17.157 1.00 31.73 ATOM 400 CB VAL A 83 52.080 50.023 18.432 1.00 32.09 ATOM 401 CG1 VAL A 83 53.222 50.992 18.638 1.00 34.42 ATOM 402 CG2 VAL A 83 51.154 50.021 19.640 1.00 30.34 ATOM 403 C VAL A 83 50.370 49.218 16.838 1.00 32.50 ATOM 404 0 VAL A 83 49.155 49.307 17.005 1.00 31.46 ATOM 405 N LEU A 84 50.968 48.119 16.384 1.00 33.48 ATOM 406 CA LEU A 84 50.223 46.906 16.062 1.00 33.72 ATOM 407 CB LEU A 84 49.674 46.274 17.350 1.00 32.58 ATOM 408 CG LEU A 84 50.683 45.955 18.458 1.00 32.62 ATOM 409 CD1 LEU A 84 49.948 45.447 19.680 1.00 31.27 ATOM 410 CD2 LEU A 84 51.692 44.926 17.974 1.00 30.95 ATOM 411 C LEU A 84 49.072 47.158 15.089 1.00 33.95 ATOM 412 0 LEU A 84 48.077 46.429 15.097 1.00 34.81 ATOM 413 N GLY A 85 49.210 48.191 14.259 1.00 34.10 ATOM 414 CA GLY A 85 48.177 48.517 13.286 1.00 33.41 ATOM 415 C GLY A 85 46.908 49.089 13.895 1.00 34.00 ATOM 416 0 GLY A 85 45.814 48.929 13.346 1.00 32.49 ATOM 417 N HIS A 86 47.056 49.765 15.032 1.00 33.02 ATOM 418 CA HIS A 86 45.922 50.356 15.729 1.00 32.41 ATOM 419 CB HIS A 86 45.284 49.323 16.669 1.00 35.18

ATOM 420 CG HIS A 86 44.707 48.131 15.968 1.00 37.48 ATOM 421 CD2 HIS A 86 45.181 46.872 15.816 1.00 38.23 ATOM 422 ND1 HIS A 86 43.504 48.171 15.298 1.00 38.86 ATOM 423 CE1 HIS A 86 43.260 46.988 14.763 1.00 38.09 ATOM 424 NE2 HIS A 86 44.263 46.182 15.062 1.00 39.89 ATOM 425 C HIS A 86 46.331 51.577 16.552 1.00 31.23 ATOM 426 0 HIS A 86 47.505 51.788 16.854 1.00 29.77 ATOM 427 N LYS A 87 45.343 52.383 16.912 1.00 30.25 ATOM 428 CA LYS A 87 45.586 53.554 17.734 1.00 29.97 ATOM 429 CB LYS A 87 44.787 54.748 17.211 1.00 32.13 ATOM 430 CG LYS A 87 44.628 55.873 18.224 1.00 36.96 ATOM 431 CD LYS A 87 43.748 56.993 17.684 1.00 41.35 ATOM 432 CE LYS A 87 42.362 56.487 17.312 1.00 43.33 ATOM 433 NZ LYS A 87 41.497 57.581 16.779 1.00 46.62 ATOM 434 C LYS A 87 45.135 53.214 19.154 1.00 28.11 ATOM 435 0 LYS A 87 44.115 52.545 19.342 1.00 27.33 ATOM 436 N PHE A 88 45.909 53.650 20.144 1.00 23.77 ATOM 437 CA PHE A 88 45.573 53.423 21.544 1.00 22.55 ATOM 438 CB PHE A 88 46.655 52.587 22.239 1.00 20.08 ATOM 439 CG PHE A 88 46.807 51.192 21.687 1.00 19.53 ATOM 440 CD1 PHE A 88 47.346 50.981 20.426 1.00 18.13 ATOM 441 CD2 PHE A 88 46.427 50.090 22.442 1.00 16.88 ATOM 442 CE1 PHE A 88 47.506 49.698 19.929 1.00 17.99 ATOM 443 CE2 PHE A 88 46.583 48.806 21.953 1.00 16.38 ATOM 444 CZ PHE A 88 47.122 48.608 20.696 1.00 17.99 ATOM 445 C PHE A 88 45.497 54.804 22.185 1.00 22.18 ATOM 446 O PHE A 88 46.494 55.520 22.225 1.00 21. 05 ATOM 447 N ARG A 89 44.324 55.184 22.683 1.00 23.63 ATOM 448 CA ARG A 89 44.175 56.506 23.284 1.00 25.47 ATOM 449 CB ARG A 89 42.700 56.800 23.577 1.00 28.55 ATOM 450 CG ARG A 89 42.038 55.912 24.596 1.00 35.93 ATOM 451 CD ARG A 89 40.528 56.029 24.444 1.00 41.44 ATOM 452 NE ARG A 89 40.131 57.382 24.066 1.00 44.82 ATOM 453 CZ ARG A 89 38.899 57.725 23.701 1.00 47.58 ATOM 454 NH1 ARG A 89 37.934 56.813 23.666 1.00 46.73 ATOM 455 NH2 ARG A 89 38.635 58.981 23.358 1.00 48.84 ATOM 456 C ARG A 89 45.049 56.721 24.522 1.00 23.67

ATOM 457 O ARG A 89 45.374 57.854 24.859 1.00 22.06 ATOM 458 N ASN A 90 45.413 55.637 25.204 1.00 21.74 ATOM 459 CA ASN A 90 46.322 55.709 26. 348 1.00 20.23 ATOM 460 CB ASN A 90 45.590 56.038 27.671 1.00 20.14 ATOM 461 CG ASN A 90 44.945 54.836 28.327 1.00 20.24 ATOM 462 OD1 ASN A 90 45.623 53.893 28.744 1.00 20.28 ATOM 463 ND2 ASN A 90 43.621 54.877 28.449 1.00 19.47 ATOM 464 C ASN A 90 47.025 54.356 26.353 1.00 20.03 ATOM 465 O ASN A 90 46.446 53.348 25.943 1.00 21.07 ATOM 466 N PRO A 91 48.293 54.323 26.783 1.00 19.07 ATOM 467 CD PRO A 91 49.025 55.490 27.309 1.00 19.27 ATOM 468 CA PRO A 91 49.137 53.127 26.837 1.00 17.79 ATOM 469 CB PRO A 91 50.532 53.720 26.810 1.00 18.33 ATOM 470 CG PRO A 91 50.367 54.889 27.730 1.00 17.60 ATOM 471 C PRO A 91 48.966 52.189 28.014 1.00 17.38 ATOM 472 O PRO A 91 49.753 51.252 28.170 1.00 16.67 ATOM 473 N VAL A 92 47.953 52.430 28.838 1.00 16.23 ATOM 474 CA VAL A 92 47.736 51.601 30.019 1.00 16.20 ATOM 475 CB VAL A 92 47.444 52.487 31.249 1.00 15.65 ATOM 476 CG1 VAL A 92 47.342 51.635 32.500 1.00 14.38 ATOM 477 CG2 VAL A 92 48.538 53.535 31.394 1.00 14.11 ATOM 478 C VAL A 92 46.602 50.591 29.852 1.00 16.68 ATOM 479 0 VAL A 92 45.433 50.966 29.778 1.00 16.63 ATOM 480 N GLY A 93 46.955 49.309 29.800 1.00 15.93 ATOM 481 CA GLY A 93 45.945 48.276 29.645 1.00 13.68 ATOM 482 C GLY A 93 45.845 47.336 30.833 1.00 14.71 ATOM 483 0 GLY A 93 46.692 47.349 31.721 1.00 15.24 ATOM 484 N ILE A 94 44.788 46.532 30.865 1.00 15.38 ATOM 485 CA ILE A 94 44.606 45.560 31.937 1.00 15.09 ATOM 486 CB ILE A 94 43.103 45.352 32.267 1.00 15.86 ATOM 487 CG2 ILE A 94 42.326 44.977 31.008 1.00 15.73 ATOM 488 CG1 ILE A 94 42.945 44.275 33.341 1.00 16.69 ATOM 489 CD1 ILE A 94 43.321 44.733 34.740 1.00 15.99 ATOM 490 C ILE A 94 45.218 44.251 31.436 1.00 15.45 ATOM 491 O ILE A 94 44.815 43.724 30.397 1.00 16.68 ATOM 492 N ALA A 95 46.207 43.744 32.166 1.00 15.14 ATOM 493 CA ALA A 95 46.894 42.508 31.802 1.00 14.33

ATOM 494 CB ALA A 95 48.074 42.274 32.746 1.00 11.97 ATOM 495 C ALA A 95 45.986 41.282 31.807 1.00 15.28 ATOM 496 0 ALA A 95 44.927 41.275 32.437 1.00 14.75 ATOM 497 N ALA A 96 46.418 40.245 31.097 1.00 14.38 ATOM 498 CA ALA A 96 45.673 38.996 31.022 1.00 15.14 ATOM 499 CB ALA A 96 46.389 38.014 30.096 1.00 12.19 ATOM 500 C ALA A 96 45.556 38.399 32.417 1.00 16.35 ATOM 501 0 ALA A 96 46.460 38.549 33.250 1.00 16.20 ATOM 502 N GLY A 97 44.441 37.723 32.675 1.00 16.89 ATOM 503 CA GLY A 97 44.250 37.110 33.977 1.00 16.58 ATOM 504 C GLY A 97 43.097 37.675 34.780 1.00 16.24 ATOM 505 0 GLY A 97 42.389 36.925 35.445 1.00 18.73 ATOM 506 N PHE A 98 42.903 38.989 34.741 1.00 15.41 ATOM 507 CA PHE A 98 41.805 39.573 35.490 1.00 14.93 ATOM 508 CB PHE A 98 41.879 41.098 35.501 1.00 15.74 ATOM 509 CG PHE A 98 40.754 41.736 36.260 1.00 17.64 ATOM 510 CD1 PHE A 98 40.677 41.611 37.642 1.00 16.91 ATOM 511 CD2 PHE A 98 39.736 42.402 35.592 1.00 17.91 ATOM 512 CE1 PHE A 98 39.607 42.134 38.344 1.00 16.70 ATOM 513 CE2 PHE A 98 38.656 42.930 36.290 1.00 17.89 ATOM 514 CZ PHE A 98 38.592 42.794 37.667 1.00 17.68 ATOM 515 C PHE A 98 40.483 39.145 34.867 1.00 15.52 ATOM 516 O PHE A 98 39.554 38.756 35.572 1.00 16.20 ATOM 517 N ASP A 99 40.398 39.232 33.543 1.00 15.16 ATOM 518 CA ASP A 99 39.187 38.834 32.827 1.00 15.45 ATOM 519 CB ASP A 99 38.647 40.008 31.990 1.00 14.91 ATOM 520 CG ASP A 99 37.235 39.753 31.452 1.00 18.47 ATOM 521 OD1 ASP A 99 36.640 38.706 31.793 1.00 18.16 ATOM 522 OD2 ASP A 99 36.712 40.604 30.692 1.00 17.82 ATOM 523 C ASP A 99 39.553 37.654 31.926 1.00 15.19 ATOM 524 0 ASP A 99 39.735 37.811 30.720 1.00 14.17 ATOM 525 N LYS A 100 39.671 36.474 32.527 1.00 14.99 ATOM 526 CA LYS A 100 40.030 35.269 31.793 1.00 15.35 ATOM 527 CB LYS A 100 40.278 34.113 32.772 1.00 17.26 ATOM 528 CG LYS A 100 41.615 34.153 33.517 1.00 18.99 ATOM 529 CD LYS A 100 41.680 33.041 34.571 1.00 22.00 ATOM 530 CE LYS A 100 43.053 32.945 35.250 1.00 22.40

ATOM 531 NZ LYS A 100 44.125 32.441 34.326 1.00 21.47 ATOM 532 C LYS A 100 39.012 34.813 30.743 1.00 16.92 ATOM 533 0 LYS A 100 39.394 34.243 29.716 1.00 15.83 ATOM 534 N HIS A 101 37.729 35.075 30.981 1.00 16.62 ATOM 535 CA HIS A 101 36.684 34.616 30.060 1.00 19.07 ATOM 536 CB HIS A 101 35.668 33.777 30.842 1.00 16.73 ATOM 537 CG HIS A 101 36.265 33.037 32.000 1.00 17.69 ATOM 538 CD2 HIS A 101 36.040 33.138 33.333 1.00 17.45 ATOM 539 ND1 HIS A 101 37.242 32.075 31.849 1.00 18.04 ATOM 540 CE1 HIS A 101 37.592 31.615 33.038 1.00 17.28 ATOM 541 NE2 HIS A 101 36.878 32.244 33.956 1.00 16.78 ATOM 542 C HIS A 101 35.945 35.698 29.265 1.00 20.21 ATOM 543 0 HIS A 101 34.887 35.434 28.686 1.00 20.90 ATOM 544 N GLY A 102 36.497 36.908 29.240 1.00 21.33 ATOM 545 CA GLY A 102 35.878 37.998 28.505 1.00 20.61 ATOM 546 C GLY A 102 34.498 38.398 28.997 1.00 21.28 ATOM 547 0 GLY A 102 33.588 38.595 28.201 1.00 21.11 ATOM 548 N GLU A 103 34.341 38.545 30.307 1.00 22.37 ATOM 549 CA GLU A 103 33.046 38.913 30.874 1.00 22.31 ATOM 550 CB GLU A 103 32.763 38.062 32.112 1.00 21.38 ATOM 551 CG GLU A 103 32.758 36.577 31.849 1.00 23.32 ATOM 552 CD GLU A 103 32.669 35.773 33.124 1.00 23.87 ATOM 553 OE1 GLU A 103 33.622 35.821 33.929 1.00 23.22 ATOM 554 OE2 GLU A 103 31.642 35.094 33.323 1.00 27.00 ATOM 555 C GLU A 103 32.914 40.377 31.270 1.00 21.22 ATOM 556 0 GLU A 103 31.805 40.870 31.462 1.00 22.46 ATOM 557 N ALA A 104 34.033 41.078 31.388 1.00 20.39 ATOM 558 CA ALA A 104 33.983 42.468 31.828 1.00 19.96 ATOM 559 CB ALA A 104 34.494 42.554 33.259 1.00 17.08 ATOM 560 C ALA A 104 34.734 43.458 30.955 1.00 18.70 ATOM 561 O ALA A 104 35.166 44.505 31.432 1.00 18.68 ATOM 562 N VAL A 105 34.869 43.139 29.675 1.00 19.67 ATOM 563 CA VAL A 105 35.585 44.004 28.747 1.00 18.98 ATOM 564 CB VAL A 105 35.482 43.473 27.309 1.00 18.35 ATOM 565 CG1 VAL A 105 36.203 44.413 26.361 1.00 17.12 ATOM 566 CG2 VAL A 105 36.077 42.076 27.230 1.00 17.81 ATOM 567 C VAL A 105 35.113 45.458 28.753 1.00 20.21

ATOM 568 0VAL A 105 35.927 46.384 28.840 1.00 21.83 ATOM 569 N ASP A 106 33.805 45.667 28.654 1.00 17.79 ATOM 570 CA ASP A 106 33.286 47.024 28.633 1.00 19.14 ATOM 571 CB ASP A 106 31.800 47.026 28.256 1.00 18.51 ATOM 572 CG ASP A 106 31.569 46.509 26.853 1.00 21.68 ATOM 573 OD1 ASP A 106 31.007 45.402 26.704 1.00 23.82 ATOM 574 OD2 ASP A 106 31.968 47.204 25.894 1.00 21.96 ATOM 575 C ASP A 106 33.511 47.737 29.960 1.00 17.72 ATOM 576 O ASP A 106 33.881 48.907 29.981 1.00 17.97 ATOM 577 N GLY A 107 33.301 47.035 31.065 1.00 16.46 ATOM 578 CA GLY A 107 33.526 47.656 32.359 1.00 17.38 ATOM 579 C GLY A 107 34.971 48.111 32.495 1.00 17.35 ATOM 580 O GLY A 107 35.255 49.153 33.084 1.00 19.25 ATOM 581 N LEU A 108 35.890 47.326 31.942 1.00 16.97 ATOM 582 CA LEU A 108 37.309 47.650 31.996 1.00 17.36 ATOM 583 CB LEU A 108 38.125 46.437 31.529 1.00 17. 86 ATOM 584 CG LEU A 108 38.062 45.272 32.526 1.00 17.10 ATOM 585 CD1 LEU A 108 38.470 43.978 31.867 1.00 15.95 ATOM 586 CD2 LEU A 108 38.968 45.584 33.715 1.00 18.93 ATOM 587 C LEU A 108 37.660 48.912 31.184 1.00 17.60 ATOM 588 0LEU A 108 38.488 49.713 31.617 1.00 17.54 ATOM 589 N TYR A 109 37.049 49.091 30.014 1.00 17.36 ATOM 590 CA TYR A 109 37.308 50.300 29.226 1.00 18.50 ATOM 591 CB TYR A 109 36.579 50.270 27.873 1.00 16.29 ATOM 592 CG TYR A 109 37.220 49.373 26.842 1.00 15.60 ATOM 593 CD1 TYR A 109 36.483 48.389 26.196 1.00 13.47 ATOM 594 CE1 TYR A 109 37.074 47.542 25.273 1.00 14.70 ATOM 595 CD2 TYR A 109 38.568 49.494 26.531 1.00 15.56 ATOM 596 CE2 TYR A 109 39.169 48.657 25.605 1.00 15.08 ATOM 597 CZ TYR A 109 38.416 47.682 24.982 1.00 15.11 ATOM 598 OH TYR A 109 39.008 46.842 24.073 1.00 14.37 ATOM 599 C TYR A 109 36.781 51.476 30.038 1.00 19.94 ATOM 600 O TRY A 109 37.402 52.538 30.099 1.00 19.20 ATOM 601 N LYS A 110 35.627 51.274 30.665 1.00 19.60 ATOM 602 CA LYS A 110 35.026 52.316 31.478 1.00 22.98 ATOM 603 CB LYS A 110 33.652 51.869 31.984 1.00 22.64 ATOM 604 CG LYS A 110 32.978 52.883 32.884 1.00 25.49

ATOM 605 CD LYS A 110 31.614 52.398 33.349 1.00 28.43 ATOM 606 CE LYS A 110 30.978 53.387 34.316 1.00 29.85 ATOM 607 NZ LYS A 110 29.639 52.924 34.779 1.00 32.33 ATOM 608 C LYS A 110 35.931 52.656 32.660 1.00 23.71 ATOM 609 O LYS A 110 35.911 53.779 33.159 1.00 24.86 ATOM 610 N MET A 111 36.724 51.683 33.105 1.00 23.14 ATOM 611 CA MET A 111 37.635 51.896 34.227 1.00 22.28 ATOM 612 CB MET A 111 38.200 50.556 34.710 1.00 23.75 ATOM 613 CG MET A 111 38.638 50.548 36.169 1.00 22.53 ATOM 614 SD MET A 111 39.196 48.918 36.741 1.00 22.26 ATOM 615 CE MET A 111 37.667 48.079 37.039 1.00 21.23 ATOM 616 C MET A 111 38.775 52.825 33.802 1.00 22.11 ATOM 617 O MET A 111 39.489 53.375 34.641 1.00 22.69 ATOM 618 N GLY A 112 38.949 52.995 32.496 1.00 20.34 ATOM 619 CA GLY A 112 39.991 53.883 32.015 1.00 18.15 ATOM 620 C GLY A 112 41.119 53.247 31.226 1.00 18.34 ATOM 621 0 GLY A 112 42.003 53.956 30.741 1.00 18.29 ATOM 622 N PHE A 113 41.105 51.924 31.083 1.00 16.38 ATOM 623 CA PHE A 113 42.169 51.256 30.341 1.00 16.66 ATOM 624 CB PHE A 113 42.085 49.736 30.519 1.00 15.73 ATOM 625 CG PHE A 113 42.439 49.268 31.907 1.00 15.86 ATOM 626 CD1 PHE A 113 41.461 48.785 32.763 1.00 13.52 ATOM 627 CD2 PHE A 113 43.750 49.325 32.358 1.00 15.66 ATOM 628 CE1 PHE A 113 41.783 48.366 34.049 1.00 16.31 ATOM 629 CE2 PHE A 113 44.082 48.911 33.640 1.00 15.91 ATOM 630 CZ PHE A 113 43.097 48.430 34.488 1.00 17.25 ATOM 631 C PHE A 113 42.123 51.613 28.860 1.00 17.48 ATOM 632 O PHE A 113 41.050 51.697 28.262 1.00 18.96 ATOM 633 N GLY A 114 43.298 51.833 28.280 1.00 17.21 ATOM 634 CA GLY A 114 43.387 52.183 26.875 1.00 17.10 ATOM 635 C GLY A 114 43.185 50.974 25.983 1.00 17.43 ATOM 636 0 GLY A 114 42.940 51.105 24.781 1.00 18.13 ATOM 637 N PHE A 115 43.321 49.790 26.567 1.00 15.88 ATOM 638 CA PHE A 115 43.118 48.554 25.827 1.00 15.94 ATOM 639 CB PHE A 115 44.278 48.279 24.855 1.00 14. 80 ATOM 640 CG PHE A 115 45.594 47.961 25.516 1.00 15. 10 ATOM 641 CD1 PHE A 115 46.118 46.678 25.455 1.00 13.34

ATOM 642 CD2 PHE A 115 46.352 48. 960 26.114 1.00 15.38 ATOM 643 CE1 PHE A 115 47.375 46.391 25.968 1.00 13.45 ATOM 644 CE2 PHE A 115 47.613 48.684 26.631 1.00 15.60 ATOM 645 CZ PHE A 115 48.126 47.394 26.556 1.00 16.23 ATOM 646 C PHE A 115 42.924 47.404 26.797 1.00 15.57 ATOM 647 O PHE A 115 43.407 47.441 27.925 1.00 15.80 ATOM 648 N VAL A 116 42.195 46.391 26.350 1.00 14.53 ATOM 649 CA VAL A 116 41.886 45.245 27.184 1.00 13.55 ATOM 650 CB VAL A 116 40.352 45.155 27.428 1.00 12.30 ATOM 651 CG1 VAL A 116 39.999 43.863 28.178 1.00 11.26 ATOM 652 CG2 VAL A 116 39.888 46.366 28.199 1.00 9.84 ATOM 653 C VAL A 116 42.342 43.936 26.573 1.00 13.19 ATOM 654 0 VAL A 116 42.195 43.716 25.371 1.00 13.44 ATOM 655 N GLU A 117 42.896 43.070 27.411 1.00 13.85 ATOM 656 CA GLU A 117 43.342 41.752 26.972 1.00 15.89 ATOM 657 CB GLU A 117 44.856 41.608 27.145 1.00 15.80 ATOM 658 CG GLU A 117 45.399 40.231 26.767 1.00 16.39 ATOM 659 CD GLU A 117 46.916 40.177 26.798 1.00 18.77 ATOM 660 OE1 GLU A 117 47.467 39.207 27.369 1.00 16.54 ATOM 661 OE2 GLU A 117 47.553 41.101 26.245 1.00 15.23 ATOM 662 C GLU A 117 42.611 40.759 27.867 1.00 16.46 ATOM 663 0 GLU A 117 42.710 40.840 29.088 1.00 17.95 ATOM 664 N ILE A 118 41.864 39.831 27.283 1.00 18.07 ATOM 665 CA ILE A 118 41.139 38.885 28.117 1.00 19.92 ATOM 666 CB ILE A 118 39.789 38.483 27.484 1.00 18.14 ATOM 667 CG2 ILE A 118 38.863 39.685 27.481 1.00 16.23 ATOM 668 CG1 ILE A 118 39.990 37.954 26.066 1.00 18.31 ATOM 669 CD1 ILE A 118 38.708 37.447 25.441 1.00 19.68 ATOM 670 C ILE A 118 41.964 37.656 28.465 1.00 21.94 ATOM 671 0 ILE A 118 42.582 37.044 27.597 1.00 20.77 ATOM 672 N GLY A 119 41.971 37.348 29.766 1.00 26.52 ATOM 673 CA GLY A 119 42.725 36.240 30.343 1.00 23.76 ATOM 674 C GLY A 119 42.913 35.080 29.411 1.00 24.45 ATOM 675 0 GLY A 119 42.145 34.933 28.455 1.00 22.92 ATOM 676 N SER A 120 43.921 34.254 29.691 1.00 21.74 ATOM 677 CA SER A 120 44.207 33.102 28.843 1.00 20.99 ATOM 678 CB SER A 120 45.383 32.290 29.396 1.00 21.02

ATOM 679 OG SER A 120 46.621 32.902 29.074 1.00 21.19 ATOM 680 C SER A 120 43.004 32.195 28.669 1.00 19.92 ATOM 681 O SER A 120 42.319 31.853 29.637 1.00 19.73 ATOM 682 N VAL A 121 42.761 31.817 27.420 1.00 18.41 ATOM 683 CA VAL A 121 41.652 30.945 27.064 1.00 17.15 ATOM 684 CB VAL A 121 40.762 31.588 25.973 1.00 17.17 ATOM 685 CG1 VAL A 121 39.474 30.770 25.791 1.00 15.03 ATOM 686 CG2 VAL A 121 40.451 33.036 26.337 1.00 15.07 ATOM 687 C VAL A 121 42.216 29.637 26.510 1.00 17.36 ATOM 688 0 VAL A 121 43.129 29.649 25.685 1.00 17.64 ATOM 689 N THR A 122 41.679 28.516 26.977 1.00 15.93 ATOM 690 CA THR A 122 42.112 27.204 26.513 1.00 18.45 ATOM 691 CB THR A 122 42.255 26.209 27.692 1.00 18.19 ATOM 692 OG1 THR A 122 41.041 26.182 28.446 1.00 20.07 ATOM 693 CG2 THR A 122 43.385 26.624 28.607 1.00 17.93 ATOM 694 C THR A 122 41.056 26.694 25.532 1.00 19.33 ATOM 695 0 THR A 122 39.897 27.099 25.595 1.00 20.13 ATOM 696 N PRO A 123 41.447 25.817 24.599 1.00 19.88 ATOM 697 CD PRO A 123 42.813 25.347 24.312 1.00 20.45 ATOM 698 CA PRO A 123 40.495 25.283 23.618 1.00 21.16 ATOM 699 CB PRO A 123 41.326 24.252 22.864 1.00 20.64 ATOM 700 CG PRO A 123 42.693 24.893 22.870 1.00 20.94 ATOM 701 C PRO A 123 39.244 24.684 24.259 1.00 22.19 ATOM 702 0 PRO A 123 38.122 25.084 23.948 1.00 21.78 ATOM 703 N LYS A 124 39.439 23.727 25.155 1.00 22.48 ATOM 704 CA LYS A 124 38.314 23.107 25.834 1.00 24.61 ATOM 705 CB LYS A 124 38.518 21.589 25.943 1.00 26.75 ATOM 706 CG LYS A 124 38.853 20.915 24.624 1.00 31.52 ATOM 707 CD LYS A 124 37.838 21.287 23.548 1.00 36.94 ATOM 708 CE LYS A 124 38.268 20.790 22.173 1.00 39.83 ATOM 709 NZ LYS A 124 37.347 21.270 21.104 1.00 41.97 ATOM 710 C LYS A 124 38.214 23.710 27.226 1.00 24.06 ATOM 711 0 LYS A 124 39.197 24.224 27.760 1.00 24.29 ATOM 712 N PRO A 125 37.016 23.679 27.823 1.00 23.56 ATOM 713 CD PRO A 125 35.731 23.209 27.272 1.00 22.50 ATOM 714 CA PRO A 125 36.849 24.235 29.169 1.00 22.94 ATOM 715 CB PRO A 125 35.345 24.099 29.424 1.00 23.90

ATOM 716 CG PRO A 125 34.736 24. 031 28.039 1.00 23.27 ATOM 717 C PRO A 125 37.652 23.386 30.156 1.00 23.04 ATOM 718 0 PRO A 125 37.809 22. 183 29.955 1.00 22.12 ATOM 719 N GLN A 126 38.173 24. 012 31.204 1.00 22.29 ATOM 720 CA GLN A 126 38.908 23.286 32.235 1.00 22.14 ATOM 721 CB GLN A 126 40.345 22.953 31.794 1.00 23.41 ATOM 722 CG GLN A 126 41.271 24.132 31.558 1.00 21.69 ATOM 723 CD GLN A 126 42.719 23.691 31.384 1.00 21.50 ATOM 724 OE1 GLN A 126 43.012 22.748 30.640 1.00 17.39 ATOM 725 NE2 GLN A 126 43.633 24.376 32.067 1.00 19.78 ATOM 726 C GLN A 126 38.907 24.109 33.516 1.00 22.34 ATOM 727 O GLN A 126 39.050 25.329 33.485 1.00 21.16 ATOM 728 N GLU A 127 38.742 23.421 34.640 1.00 23.72 ATOM 729 CA GLU A 127 38.657 24.053 35.950 1.00 26.48 ATOM 730 CB GLU A 127 38.023 23.071 36.940 1.00 30.25 ATOM 731 CG GLU A 127 36.718 22.476 36.444 1.00 38.37 ATOM 732 CD GLU A 127 35.966 21.732 37.527 1.00 43.74 ATOM 733 OE1 GLU A 127 36.591 20.898 38.223 1.00 46.79 ATOM 734 OE2 GLU A 127 34.748 21.979 37.678 1.00 45.76 ATOM 735 C GLU A 127 39.936 24.614 36. 559 1.00 24.46 ATOM 736 O GLU A 127 39.874 25.515 37.395 1.00 21. 80 ATOM 737 N GLY A 128 41.085 24.083 36.158 1.00 23.10 ATOM 738 CA GLY A 128 42.337 24.559 36.715 1.00 23.08 ATOM 739 C GLY A 128 42.681 23.831 38.005 1.00 24.88 ATOM 740 O GLY A 128 42.088 22.794 38.317 1.00 22.39 ATOM 741 N ASN A 129 43.635 24.371 38.761 1.00 25.51 ATOM 742 CA ASN A 129 44.060 23.752 40.013 1.00 26.86 ATOM 743 CB ASN A 129 45.401 24.333 40.475 1.00 26.95 ATOM 744 CG ASN A 129 46.545 23.948 39.564 1.00 29.42 ATOM 745 OD1 ASN A 129 46.684 22.784 39.191 1.00 29.57 ATOM 746 ND2 ASN A 129 47.379 24.922 39.206 1.00 27.28 ATOM 747 C ASN A 129 43.044 23.916 41.130 1.00 27.75 ATOM 748 O ASN A 129 42.222 24.832 41.112 1.00 28.72 ATOM 749 N PRO A 130 43.090 23.016 42.123 1.00 28.29 ATOM 750 CD PRO A 130 43.976 21.840 42.196 1.00 28.29 ATOM 751 CA PRO A 130 42.176 23.057 43.266 1.00 28.70 ATOM 752 CB PRO A 130 42.415 21.708 43. 943 1.00 28.73

ATOM 753 CG PRO A 130 43.849 21.432 43.648 1.00 28.52 ATOM 754 C PRO A 130 42.519 24.238 44.170 1.00 30.37 ATOM 755 0 PRO A 130 43.658 24.703 44.181 1.00 30.70 ATOM 756 N ARG A 131 41.535 24.728 44.916 1.00 31.62 ATOM 757 CA ARG A 131 41.753 25.857 45.813 1.00 33.50 ATOM 758 CB ARG A 131 40.420 26.515 46.178 1.00 35.74 ATOM 759 CG ARG A 131 39.613 27.089 45.017 1.00 38.80 ATOM 760 CD ARG A 131 38.514 27.985 45.580 1.00 42.56 ATOM 761 NE ARG A 131 37.622 28.555 44.573 1.00 47.82 ATOM 762 CZ ARG A 131 36.761 29.545 44.818 1.00 49.92 ATOM 763 NH1 ARG A 131 36.682 30.074 46.035 1.00 48.66 ATOM 764 NH2 ARG A 131 35.974 30.006 43.853 1.00 49.91 ATOM 765 C ARG A 131 42.461 25.422 47.103 1.00 33.57 ATOM 766 0 ARG A 131 42.376 24.265 47.515 1.00 34.25 ATOM 767 N PRO A 132 43.194 26.345 47.743 1.00 31.72 ATOM 768 CD PRO A 132 43.813 26.140 49.065 1.00 32.80 ATOM 769 CA PRO A 132 43.370 27.730 47.297 1.00 29.67 ATOM 770 CB PRO A 132 43.810 28.437 48.572 1.00 30.49 ATOM 771 CG PRO A 132 44.655 27.389 49.233 1.00 31.39 ATOM 772 C PRO A 132 44.432 27.774 46.198 1.00 26.70 ATOM 773 0 PRO A 132 45.304 26.907 46.143 1.00 25.75 ATOM 774 N ARG A 133 44.363 28.779 45.329 1.00 23.15 ATOM 775 CA ARG A 133 45.315 28.882 44.232 1.00 20.71 ATOM 776 CB ARG A 133 44.701 28.268 42.972 1.00 20.72 ATOM 777 CG ARG A 133 43.273 28.731 42.700 1.00 19.27 ATOM 778 CD ARG A 133 42.596 27.848 41.651 1.00 19.00 ATOM 779 NE ARG A 133 41.216 28.261 41.400 1.00 17.68 ATOM 780 CZ ARG A 133 40.462 27.779 40.418 1.00 16. 01 ATOM 781 NH1 ARG A 133 39.221 28.209 40.258 1.00 13.83 ATOM 782 NH2 ARG A 133 40.952 26.866 39.592 1.00 16.14 ATOM 783 C ARG A 133 45.789 30.303 43.952 1.00 20.50 ATOM 784 O ARG A 133 46.444 30.562 42.941 1.00 20.67 ATOM 785 N VAL A 134 45.447 31.225 44.842 1.00 19. 19 ATOM 786 CA VAL A 134 45.876 32.609 44.702 1.00 18.94 ATOM 787 CB VAL A 134 44.805 33.483 43.977 1.00 18.31 ATOM 788 CG1 VAL A 134 43.524 33.555 44.790 1.00 17.25 ATOM 789 CG2 VAL A 134 45.366 34.876 43.720 1.00 16.42

ATOM 790 C VAL A 134 46.136 33.109 46.121 1.00 19.93 ATOM 791 0 VAL A 134 45.393 32.784 47.044 1.00 21.00 ATOM 792 N PHE A 135 47.208 33.870 46.303 1.00 19.43 ATOM 793 CA PHE A 135 47.558 34.352 47.630 1.00 18.68 ATOM 794 CB PHE A 135 48.619 33.437 48.244 1.00 18.25 ATOM 795 CG PHE A 135 48.311 31.968 48.099 1.00 17.64 ATOM 796 CD1 PHE A 135 48.567 31.305 46.909 1.00 17.96 ATOM 797 CD2 PHE A 135 47.730 31.262 49.142 1.00 18.54 ATOM 798 CE1 PHE A 135 48.248 29.963 46.758 1.00 17.71 ATOM 799 CE2 PHE A 135 47.407 29.921 49.001 1.00 17.69 ATOM 800 CZ PHE A 135 47.667 29.272 47.804 1.00 18.64 ATOM 801 C PHE A 135 48.060 35.791 47.635 1.00 19.58 ATOM 802 0 PHE A 135 48.769 36.227 46.724 1.00 19.26 ATOM 803 N ARG A 136 47.684 36.522 48.676 1.00 18.78 ATOM 804 CA ARG A 136 48.087 37.907 48.821 1.00 18.85 ATOM 805 CB ARG A 136 46.945 38.734 49.440 1.00 18.08 ATOM 806 CG ARG A 136 45.648 38.704 48.639 1.00 21.63 ATOM 807 CD ARG A 136 44.493 39.450 49.317 1.00 22.90 ATOM 808 NE ARG A 136 44.669 40.900 49.298 1.00 31.55 ATOM 809 CZ ARG A 136 45.236 41.604 50.277 1.00 34.11 ATOM 810 NH1 ARG A 136 45.358 42.922 50.170 1.00 33.96 ATOM 811 NH2 ARG A 136 45.663 40.995 51.374 1.00 36.33 ATOM 812 C ARG A 136 49.319 37.991 49.714 1.00 18.61 ATOM 813 0 ARG A 136 49.460 37.220 50.663 1.00 16.80 ATOM 814 N LEU A 137 50.214 38.918 49.376 1.00 17.15 ATOM 815 CA LEU A 137 51.432 39.182 50.141 1.00 15.58 ATOM 816 CB LEU A 137 52.685 38.735 49.383 1.00 14.90 ATOM 817 CG LEU A 137 53.070 37.252 49.326 1.00 16.15 ATOM 818 CD1 LEU A 137 52.002 36.449 48.591 1.00 14.54 ATOM 819 CD2 LEU A 137 54.416 37.119 48.613 1.00 14.08 ATOM 820 C LEU A 137 51.442 40.700 50.288 1.00 16.26 ATOM 821 0 LEU A 137 52.240 41.396 49.653 1.00 14.07 ATOM 822 N PRO A 138 50.524 41.229 51.113 1.00 15.45 ATOM 823 CD PRO A 138 49.555 40.439 51.895 1.00 15.39 ATOM 824 CA PRO A 138 50.371 42.661 51.379 1.00 15.67 ATOM 825 CB PRO A 138 49.263 42.711 52.442 1.00 16.12 ATOM 826 CG PRO A 138 49.300 41.332 53.076 1.00 16.29

ATOM 827 C PRO A 138 51.642 43.386 51.806 1.00 16.69 ATOM 828 0 PRO A 138 51.878 44.518 51.382 1.00 16.05 ATOM 829 N GLU A 139 52.460 42.750 52.638 1. 00 16.00 ATOM 830 CA GLU A 139 53.694 43.391 53.072 1.00 18.28 ATOM 831 CB GLU A 139 54.414 42.551 54.135 1.00 19.48 ATOM 832 CG GLU A 139 53.660 42.377 55.455 1.00 21.64 ATOM 833 CD GLU A 139 52.648 41.240 55.418 1.00 23.74 ATOM 834 OE1 GLU A 139 51.996 41.000 56.460 1.00 24.15 ATOM 835 OE2 GLU A 139 52.504 40.589 54.356 1.00 21.93 ATOM 836 C GLU A 139 54.640 43.610 51.890 1.00 19.58 ATOM 837 0 GLU A 139 55.566 44.423 51.974 1.00 20.31 ATOM 838 N ASP A 140 54.406 42.892 50.792 1.00 16.14 ATOM 839 CA ASP A 140 55.256 43.010 49.608 1.00 15.71 ATOM 840 CB ASP A 140 55.743 41.628 49.155 1.00 14.25 ATOM 841 CG ASP A 140 56.369 40.833 50.277 1.00 16.28 ATOM 842 OD1 ASP A 140 57.398 41.284 50.819 1.00 15.84 ATOM 843 OD2 ASP A 140 55.829 39.755 50.618 1.00 17.81 ATOM 844 C ASP A 140 54.522 43.649 48.448 1.00 15.94 ATOM 845 O ASP A 140 55.112 43.886 47.387 1.00 15.41 ATOM 846 N GLN A 141 53.237 43.928 48.645 1.00 16.39 ATOM 847 CA GLN A 141 52.424 44.492 47.576 1.00 16.60 ATOM 848 CB GLN A 141 52.891 45.907 47.239 1.00 17.74 ATOM 849 CG GLN A 141 52.463 46.925 48.283 1.00 21.42 ATOM 850 CD GLN A 141 52.966 48.321 47.992 1.00 22.86 ATOM 851 OE1 GLN A 141 52.811 48.829 46.879 1.00 25.58 ATOM 852 NE2 GLN A 141 53.560 48.961 48.999 1.00 20.82 ATOM 853 C GLN A 141 52.584 43.563 46.379 1.00 16.15 ATOM 854 0 GLN A 141 52.779 44.000 45.243 1.00 16.04 ATOM 855 N ALA A 142 52.502 42.265 46.664 1.00 15.11 ATOM 856 CA ALA A 142 52.639 41.230 45.655 1.00 16.24 ATOM 857 CB ALA A 142 54.011 40.566 45.776 1.00 14.95 ATOM 858 C ALA A 142 51.543 40.173 45.790 1.00 16.14 ATOM 859 0 ALA A 142 50.822 40.128 46.786 1.00 16.05 ATOM 860 N VAL A 143 51.434 39.327 44.770 1.00 14.61 ATOM 861 CA VAL A 143 50.463 38.248 44.751 1.00 13.30 ATOM 862 CB VAL A 143 49.232 38.585 43.848 1.00 15.01 ATOM 863 CG1 VAL A 143 48.372 37.345 43.658 1.00 12.24

ATOM 864 CG2 VAL A 143 48.392 39.705 44.469 1.00 12.72 ATOM 865 C VAL A 143 51.153 37.022 44.169 1.00 15.22 ATOM 866 O VAL A 143 52.098 37.140 43.386 1.00 17.23 ATOM 867 N ILE A 144 50.702 35.845 44.581 1.00 15.07 ATOM 868 CA ILE A 144 51.228 34.597 44.050 1.00 14.14 ATOM 869 CB ILE A 144 51.994 33.783 45.113 1.00 15.13 ATOM 870 CG2 ILE A 144 52.184 32.340 44.627 1.00 12.58 ATOM 871 CG1 ILE A 144 53.357 34.429 45.382 1.00 14.50 ATOM 872 CD1 ILE A 144 54.167 33.719 46.437 1.00 15.10 ATOM 873 C ILE A 144 50.007 33.812 43.597 1.00 15.18 ATOM 874 0 ILE A 144 49.014 33.728 44.325 1.00 14.61 ATOM 875 N ASN A 145 50.063 33.247 42.397 1.00 14.87 ATOM 876 CA ASN A 145 48.926 32.492 41.896 1.00 14.98 ATOM 877 CB ASN A 145 48.079 33.381 40.981 1.00 14.70 ATOM 878 CG ASN A 145 48.613 33.431 39.558 1.00 16.21 ATOM 879 OD1 ASN A 145 48.327 32.549 38.747 1.00 15.94 ATOM 880 ND2 ASN A 145 49.404 34.457 39.253 1.00 15.29 ATOM 881 C ASN A 145 49.326 31.228 41.139 1.00 16.34 ATOM 882 0 ASN A 145 50.392 31.163 40.515 1.00 14.81 ATOM 883 N ARG A 146 48.457 30.224 41.207 1.00 15.88 ATOM 884 CA ARG A 146 48.667 28.965 40.512 1.00 16.71 ATOM 885 CB ARG A 146 49.355 27.941 41.429 1.00 17.60 ATOM 886 CG ARG A 146 48.672 27.686 42.775 1.00 16.03 ATOM 887 CD ARG A 146 49.242 26.427 43.427 1.00 16.96 ATOM 888 NE ARG A 146 48.682 26.156 44.751 1.00 18.10 ATOM 889 CZ ARG A 146 49.201 26.585 45.900 1.00 18.95 ATOM 890 NH1 ARG A 146 50.311 27.316 45.910 1.00 16.91 ATOM 891 NH2 ARG A 146 48.609 26.275 47.048 1.00 18.90 ATOM 892 C ARG A 146 47.317 28.429 40.026 1.00 17.77 ATOM 893 0 ARG A 146 46.987 27.260 40.226 1.00 18.14 ATOM 894 N TYR A 147 46.540 29.296 39.381 1.00 16.93 ATOM 895 CA TYR A 147 45.232 28.913 38.866 1.00 17.10 ATOM 896 CB TYR A 147 44.583 30.088 38.131 1.00 16.67 ATOM 897 CG TYR A 147 43.797 31.015 39.033 1.00 16.52 ATOM 898 CD1 TYR A 147 44.347 32.200 39.502 1.00 15.84 ATOM 899 CE1 TYR A 147 43.618 33.051 40.323 1.00 17.11 ATOM 900 CD2 TYR A 147 42.496 30.699 39.413 1.00 17. 14

ATOM 901 CE2 TYR A 147 41.761 31.540 40.233 1.00 17.07 ATOM 902 CZ TYR A 147 42.326 32.714 40.681 1.00 16.99 ATOM 903 OH TYR A 147 41.586 33.557 41.475 1.00 19.36 ATOM 904 C TYR A 147 45.289 27.704 37.937 1.00 18.90 ATOM 905 0 TYR A 147 44.454 26.799 38.030 1.00 19.56 ATOM 906 N GLY A 148 46.272 27.693 37.040 1.00 17.53 ATOM 907 CA GLY A 148 46.418 26.586 36.114 1.00 18.26 ATOM 908 C GLY A 148 45.518 26.661 34.892 1.00 18.89 ATOM 909 0 GLY A 148 45.036 25.635 34.409 1.00 18.59 ATOM 910 N PHE A 149 45.292 27.869 34.387 1.00 18.08 ATOM 911 CA PHE A 149 44.454 28.060 33.209 1.00 18.01 ATOM 912 CB PHE A 149 45.024 27.286 32.012 1.00 17.90 ATOM 913 CG PHE A 149 46.184 27.962 31.334 1.00 19.93 ATOM 914 CD1 PHE A 149 47.006 27.250 30.469 1.00 20.61 ATOM 915 CD2 PHE A 149 46.450 29.307 31.545 1.00 19.87 ATOM 916 CE1 PHE A 149 48.074 27.868 29.829 1.00 21.56 ATOM 917 CE2 PHE A 149 47.511 29.929 30.912 1.00 20.39 ATOM 918 CZ PHE A 149 48.326 29.211 30.053 1.00 21.63 ATOM 919 C PHE A 149 42.989 27.658 33.393 1.00 18.19 ATOM 920 O PHE A 149 42.459 26.885 32.598 1.00 16.88 ATOM 921 N ASN A 150 42.338 28.154 34.440 1.00 17.39 ATOM 922 CA ASN A 150 40.921 27.859 34.617 1.00 18.20 ATOM 923 CB ASN A 150 40.426 28.360 35.978 1.00 16.86 ATOM 924 CG ASN A 150 40.861 29.778 36.272 1.00 19.11 ATOM 925 OD1 ASN A 150 42.042 30.119 36.151 1.00 18.63 ATOM 926 ND2 ASN A 150 39.913 30.612 36.679 1.00 18.23 ATOM 927 C ASN A 150 40.296 28.653 33.469 1.00 18.25 ATOM 928 0 ASN A 150 40.556 29.849 33.329 1.00 17.98 ATOM 929 N SER A 151 39.495 27.994 32.636 1.00 17.60 ATOM 930 CA SER A 151 38.924 28.669 31.479 1.00 17.42 ATOM 931 CB SER A 151 39.948 28.625 30.337 1.00 16.39 ATOM 932 OG SER A 151 39.383 29.008 29.094 1.00 16.77 ATOM 933 C SER A 151 37.589 28.125 30.981 1.00 18.29 ATOM 934 O SER A 151 37.367 26.912 30.950 1.00 19. 11 ATOM 935 N HIS A 152 36.706 29.036 30.580 1.00 17.96 ATOM 936 CA HIS A 152 35.399 28.655 30.051 1.00 18.60 ATOM 937 CB HIS A 152 34.502 29.887 29.899 1.00 18. 50

ATOM 938 CG HIS A 152 34.020 30.450 31.200 1.00 20.25 ATOM 939 CD2 HIS A 152 34.271 30.083 32.480 1.00 21.79 ATOM 940 ND1 HIS A 152 33.157 31.523 31.271 1.00 21.65 ATOM 941 CE1 HIS A 152 32.896 31.791 32.538 1.00 20.98 ATOM 942 NE2 HIS A 152 33.559 30.932 33.292 1.00 21.39 ATOM 943 C HIS A 152 35.557 27.974 28.687 1.00 18.05 ATOM 944 0 HIS A 152 34.641 27.302 28.207 1.00 16.86 ATOM 945 N GLY A 153 36.721 28.149 28.064 1.00 16.67 ATOM 946 CA GLY A 153 36.953 27.536 26.766 1.00 15.79 ATOM 947 C GLY A 153 36.671 28.464 25.599 1.00 14.76 ATOM 948 O GLY A 153 35.935 29.442 25.727 1.00 13.73 ATOM 949 N LEU A 154 37.254 28.147 24.450 1.00 16.63 ATOM 950 CA LEU A 154 37.095 28.958 23.246 1.00 18.43 ATOM 951 CB LEU A 154 37.831 28.297 22.074 1.00 15.94 ATOM 952 CG LEU A 154 39.356 28.283 22.137 1.00 16.17 ATOM 953 CD1 LEU A 154 39.925 27.439 21.003 1.00 11.50 ATOM 954 CD2 LEU A 154 39.863 29.713 22.061 1.00 15.25 ATOM 955 C LEU A 154 35.640 29.198 22.847 1.00 20.28 ATOM 956 0 LEU A 154 35.227 30.337 22.613 1.00 20.49 ATOM 957 N SER A 155 34.872 28.118 22.768 1.00 20.71 ATOM 958 CA SER A 155 33.473 28.194 22.369 1.00 23.17 ATOM 959 CB SER A 155 32.824 26.818 22.520 1.00 24.18 ATOM 960 OG SER A 155 31.494 26.838 22.053 1.00 31.05 ATOM 961 C SER A 155 32.674 29.240 23.147 1.00 22.07 ATOM 962 0 SERA 155 32.091 30.153 22.562 1.00 21.98 ATOM 963 N VAL A 156 32.648 29.110 24.468 1.00 22.13 ATOM 964 CA VAL A 156 31.915 30.054 25.297 1.00 20.80 ATOM 965 CB VAL A 156 31.977 29.643 26.779 1.00 22.11 ATOM 966 CG1 VAL A 156 31.467 30.777 27.661 1.00 21.20 ATOM 967 CG2 VAL A 156 31.137 28.386 26.993 1.00 18.95 ATOM 968 C VAL A 156 32.433 31.486 25.136 1.00 20.60 ATOM 969 0 VAL A 156 31.647 32.424 25.025 1.00 20.47 ATOM 970 N VAL A 157 33.751 31.655 25.106 1.00 17.60 ATOM 971 CA VAL A 157 34. 325 32.983 24.955 1.00 16.63 ATOM 972 CB VAL A 157 35.854 32.953 25.181 1.00 16.62 ATOM 973 CG1 VAL A 157 36.459 34.308 24.880 1.00 14.21 ATOM 974 CG2 VAL A 157 36.149 32.556 26.616 1.00 16.01

ATOM 975 C VAL A 157 34.015 33.539 23.564 1.00 16.34 ATOM 976 O VAL A 157 33.786 34.738 23.401 1.00 15.07 ATOM 977 N GLU A 158 34.001 32.658 22.568 1.00 17.68 ATOM 978 CA GLU A 158 33.703 33.050 21.194 1.00 18.02 ATOM 979 CB GLU A 158 33.724 31.823 20.278 1.00 18.61 ATOM 980 CG GLU A 158 33.372 32.118 18.826 1.00 20.67 ATOM 981 CD GLU A 158 32.777 30.909 18.115 1.00 24.47 ATOM 982 OE1 GLU A 158 33.444 29.860 18.042 1.00 29.63 ATOM 983 OE2 GLU A 158 31.633 31.003 17.629 1.00 26.66 ATOM 984 C GLU A 158 32.323 33.708 21.121 1.00 18.60 ATOM 985 O GLU A 158 32.176 34.816 20.602 1.00 18.32 ATOM 986 N HIS A 159 31.315 33.022 21.648 1.00 18.17 ATOM 987 CA HIS A 159 29.951 33.543 21.621 1.00 21.55 ATOM 988 CB HIS A 159 28.970 32.459 22.078 1.00 21.45 ATOM 989 CG HIS A 159 28.883 31.307 21.127 1.00 26.95 ATOM 990 CD2 HIS A 159 28.642 31.271 19.794 1.00 25.37 ATOM 991 ND1 HIS A 159 29.117 30.002 21.509 1.00 29.08 ATOM 992 CE1 HIS A 159 29.027 29.214 20.452 1.00 28.39 ATOM 993 NE2 HIS A 159 28.741 29.960 19.399 1.00 27.32 ATOM 994 C HIS A 159 29.791 34.796 22.464 1.00 21.09 ATOM 995 0 HIS A 159 28.996 35.679 22.141 1.00 20.90 ATOM 996 N ARG A 160 30.565 34.874 23.538 1.00 21.00 ATOM 997 CA ARG A 160 30.519 36.020 24.429 1.00 22.35 ATOM 998 CB ARG A 160 31.346 35.714 25.684 1.00 22.67 ATOM 999 CG ARG A 160 31.199 36.704 26.824 1.00 23.49 ATOM 1000 CD ARG A 160 31.778 36.108 28.107 1.00 24.33 ATOM 1001 NE ARG A 160 30.914 35.082 28.688 1.00 22.62 ATOM 1002 CZ ARG A 160 31.348 34.044 29.399 1.00 24.90 ATOM 1003 NH1 ARG A 160 32.648 33.878 29.615 1.00 23.96 ATOM 1004 NH2 ARG A 160 30.480 33.183 29.921 1.00 23.86 ATOM 1005 C ARG A 160 31.056 37.256 23.701 1.00 21.87 ATOM 1006 0ARG A 160 30.532 38.357 23.861 1.00 22.45 ATOM 1007 N LEU A 161 32.096 37.073 22.892 1.00 20.79 ATOM 1008 CA LEU A 161 32.665 38.195 22.153 1.00 20.55 ATOM 1009 CB LEU A 161 34.105 37.890 21.726 1.00 19.07 ATOM 1010 CG LEU A 161 35.109 37.731 22.873 1.00 20.07 ATOM 1011 CD1 LEU A 161 36.506 37.526 22.299 1.00 17.41

ATOM 1012 CD2 LEU A 161 35.074 38.967 23.773 1.00 14.84 ATOM 1013 C LEU A 161 31.815 38.538 20.932 1.00 19.72 ATOM 1014 O LEU A 161 31.718 39.702 20.543 1.00 18.72 ATOM 1015 N ARG A 162 31.192 37.530 20.329 1.00 18.38 ATOM 1016 CA ARG A 162 30.345 37.781 19.166 1.00 19.35 ATOM 1017 CB ARG A 162 29.871 36.469 18.543 1.00 17.39 ATOM 1018 CG ARG A 162 30.917 35.783 17.676 1.00 18.97 ATOM 1019 CD ARG A 162 30.314 34.562 17.002 1.00 19.54 ATOM 1020 NE ARG A 162 31.228 33.917 16.068 1.00 19.77 ATOM 1021 CZ ARG A 162 30.929 32.814 15.395 1.00 20.70 ATOM 1022 NH1 ARG A 162 29.741 32.248 15.564 1.00 21.29 ATOM 1023 NH2 ARG A 162 31.808 32.277 14.560 1.00 19.65 ATOM 1024 C ARG A 162 29.133 38.631 19.535 1.00 18.62 ATOM 1025 0 ARG A 162 28.631 39.396 18.716 1.00 18.15 ATOM 1026 N ALA A 163 28.675 38.498 20.773 1.00 18.36 ATOM 1027 CA ALA A 163 27.518 39.251 21.248 1.00 19.15 ATOM 1028 CB ALA A 163 27.121 38.765 22.644 1.00 17.76 ATOM 1029 C ALA A 163 27.770 40.758 21.275 1.00 19.03 ATOM 1030 0 ALA A 163 26.829 41.544 21.340 1.00 17.57 ATOM 1031 N ARG A 164 29.041 41.152 21.221 1.00 19.26 ATOM 1032 CA ARG A 164 29.414 42.565 21.254 1.00 20.90 ATOM 1033 CB ARG A 164 29.975 42.924 22.637 1.00 21.75 ATOM 1034 CG ARG A 164 31.237 42.143 23.013 1.00 20.72 ATOM 1035 CD ARG A 164 31.734 42.494 24.411 1.00 18.57 ATOM 1036 NE ARG A 164 32.268 43.851 24.502 1.00 16.65 ATOM 1037 CZ ARG A 164 33.417 44.250 23.962 1.00 17.53 ATOM 1038 NH1 ARG A 164 34.174 43.398 23.281 1.00 15.56 ATOM 1039 NH2 ARG A 164 33.819 45.506 24.115 1.00 17.21 ATOM 1040 C ARG A 164 30.462 42.885 20.194 1.00 21.89 ATOM 1041 O ARG A 164 31.128 43.919 20.260 1.00 21.63 ATOM 1042 N GLN A 165 30.595 41.995 19.216 1.00 22.72 ATOM 1043 CA GLN A 165 31.576 42.151 18.157 1.00 23.14 ATOM 1044 CB GLN A 165 31.411 41.026 17.128 1.00 24.10 ATOM 1045 CG GLN A 165 32.334 41.139 15.926 1.00 26.13 ATOM 1046 CD GLN A 165 32.461 39.833 15.158 1.00 27.06 ATOM 1047 OE1 GLN A 165 31.513 39.057 15.068 1.00 27.74 ATOM 1048 NE2 GLN A 165 33.637 39.593 14.590 1.00 29. 00

ATOM 1049 C GLN A 165 31.538 43.507 17.462 1.00 24. 15 ATOM 1050 0 GLN A 165 32.587 44.092 17.189 1.00 23.74 ATOM 1051 N GLN A 166 30.343 44.013 17.178 1.00 23.33 ATOM 1052 CA GLN A 166 30.239 45.298 16.505 1.00 24. 01 ATOM 1053 CB GLN A 166 28.863 45.464 15.855 1.00 25.30 ATOM 1054 CG GLN A 166 28.623 44.498 14.703 1.00 26.42 ATOM 1055 CD GLN A 166 29.765 44.486 13.703 1.00 28.04 ATOM 1056 OE1 GLN A 166 30.215 45.538 13.241 1.00 29. 98 ATOM 1057 NE2 GLN A 166 30.234 43.291 13.356 1.00 28.88 ATOM 1058 C GLN A 166 30.522 46.450 17.451 1.00 22. 96 ATOM 1059 0 GLN A 166 31.075 47.471 17.042 1.00 22.74 ATOM 1060 N LYS A 167 30.147 46.298 18.715 1.00 22.13 ATOM 1061 CA LYS A 167 30.432 47.347 19.681 1.00 21.57 ATOM 1062 CB LYS A 167 29.868 47.004 21.060 1.00 21.33 ATOM 1063 CG LYS A 167 30.360 47.954 22.141 1.00 26.86 ATOM 1064 CD LYS A 167 29.860 47.587 23.528 1.00 30. 91 ATOM 1065 CE LYS A 167 28.377 47.871 23.681 1.00 34.06 ATOM 1066 NZ LYS A 167 27.936 47.697 25.092 1.00 36.77 ATOM 1067 C LYS A 167 31. 951 47.478 19.773 1.00 21.05 ATOM 1068 O LYS A 167 32.486 48.586 19.789 1.00 22.09 ATOM 1069 N GLN A 168 32.642 46.340 19.818 1.00 19.71 ATOM 1070 CA GLN A 168 34.100 46.339 19.909 1.00 18.61 ATOM 1071 CB GLN A 168 34.630 44.914 20.104 1.00 17.41 ATOM 1072 CG GLN A 168 36.150 44.837 20.262 1.00 16.23 ATOM 1073 CD GLN A 168 36.658 45.632 21.465 1.00 17.12 ATOM 1074 OE1 GLN A 168 36.286 45.356 22.609 1.00 16.33 ATOM 1075 NE2 GLN A 168 37.505 46.624 21.208 1.00 15.46 ATOM 1076 C GLN A 168 34. 732 46. 957 18.669 1.00 18. 91 ATOM 1077 0 GLN A 168 35.774 47.600 18.755 1.00 18.77 ATOM 1078 N ALA A 169 34.102 46.771 17.514 1.00 19.76 ATOM 1079 CA ALA A 169 34.643 47.341 16.282 1.00 20.87 ATOM 1080 CB ALA A 169 33.802 46.913 15.083 1.00 20.96 ATOM 1081 C ALA A 169 34.691 48.867 16.378 1.00 21.41 ATOM 1082 0 ALA A 169 35.629 49.498 15.890 1.00 21.80 ATOM 1083 N LYS A 170 33.682 49.459 17.009 1.00 22.29 ATOM 1084 CA LYS A 170 33.642 50.909 17.158 1.00 23.95 ATOM 1085 CB LYS A 170 32. 227 51.382 17.512 1.00 24.74

ATOM 1086 CG LYS A 170 31.236 51.279 16.347 1.00 29.74 ATOM 1087'CD LYS A 170 29.874 51.874 16.705 1.00 30.85 ATOM 1088 CE LYS A 170 28.915 51.843 15.512 1.00 33.49 ATOM 1089 NZ LYS A 170 28.547 50.458 15.087 1.00 32.56 ATOM 1090 C LYS A 170 34.629 51.372 18.223 1.00 23.26 ATOM 1091 0 LYS A 170 35.224 52.441 18.099 1.00 23.47 ATOM 1092 N LEU A 171 34.802 50.570 19.268 1.00 22.26 ATOM 1093 CA LEU A 171 35.742 50.921 20.328 1.00 22.16 ATOM 1094 CB LEU A 171 35.634 49.925 21.485 1.00 20.03 ATOM 1095 CG LEU A 171 34.340 50.039 22.300 1.00 20.45 ATOM 1096 CD1 LEU A 171 34.112 48.782 23.127 1.00 15.47 ATOM 1097 CD2 LEU A 171 34.418 51.280 23.188 1.00 20.39 ATOM 1098 C LEU A 171 37.161 50.926 19.757 1.00 21.88 ATOM 1099 0 LEU A 171 37.925 51.867 19.977 1.00 19.98 ATOM 1100 N THR A 172 37.500 49.877 19.013 1.00 22.29 ATOM 1101 CA THR A 172 38.821 49.763 18.396 1.00 22.96 ATOM 1102 CB THR A 172 38.940 48.457 17.581 1.00 21.62 ATOM 1103 OG1 THR A 172 38.883 47.335 18.474 1.00 21.62 ATOM 1104 CG2 THR A 172 40.249 48.424 16.799 1.00 19.50 ATOM 1105 C THR A 172 39.076 50.955 17.473 1.00 23.87 ATOM 1106 0 THR A 172 40.133 51.588 17. 528 1.00 23.14 ATOM 1107 N GLU A 173 38.100 51.257 16.628 1.00 24.87 ATOM 1108 CA GLU A 173 38.215 52.382 15.710 1.00 27.68 ATOM 1109 CB GLU A 173 36.962 52.477 14.835 1.00 31.02 ATOM 1110 CG GLU A 173 37.047 53.531 13.743 1.00 39.64 ATOM 1111 CD GLU A 173 38.105 53.207 12.696 1.00 43.67 ATOM 1112 OE1 GLU A 173 38.366 54.069 11.828 1.00 45.72 ATOM 1113 OE2 GLU A 173 38.669 52.089 12.736 1.00 46.35 ATOM 1114 C GLU A 173 38.371 53.666 16.528 1.00 27.22 ATOM 1115 0 GLU A 173 38.926 54.655 16.057 1.00 27.62 ATOM 1116 N ASP A 174 37.884 53.633 17.762 1.00 26.71 ATOM 1117 CA ASP A 174 37.959 54.781 18.652 1.00 27.64 ATOM 1118 CB ASP A 174 36.736 54.803 19.564 1.00 32.56 ATOM 1119 CG ASP A 174 35.901 56.045 19.380 1.00 38.04 ATOM 1120 OD1 ASP A 174 36.428 57. 159 19.615 1.00 39.70 ATOM 1121 OD2 ASP A 174 34.718 55.907 18.997 1.00 41.14 ATOM 1122 C ASP A 174 39.224 54.814 19.512 1.00 26.26

ATOM 1123 0 ASP A 174 39.353 55.667 20.382 1.00 25.02 ATOM 1124 N GLY A 175 40.143 53.879 19.281 1.00 24.50 ATOM 1125 CA GLY A 175 41.377 53.854 20.052 1.00 23.56 ATOM 1126 C GLY A 175 41.362 52.979 21.297 1.00 22.22 ATOM 1127 0 GLY A 175 42.154 53.190 22.210 1.00 22.02 ATOM 1128 N LEU A 176 40.469 51.996 21.332 1.00 21.00 ATOM 1129 CA LEU A 176 40.355 51.089 22.474 1.00 19.94 ATOM 1130 CB LEU A 176 39.066 51.392 23.245 1.00 17.55 ATOM 1131 CG LEU A 176 39.050 52.786 23.882 1.00 16.90 ATOM 1132 CD1 LEU A 176 37.707 53.069 24.539 1.00 16.22 ATOM 1133 CD2 LEU A 176 40.170 52.863 24.913 1.00 17.20 ATOM 1134 C LEU A 176 40.351 49.641 21.979 1.00 19.32 ATOM 1135 O LEU A 176 39.322 48.964 22.011 1.00 20.05 ATOM 1136 N PRO A 177 41.517 49.152 21.522 1.00 16.90 ATOM 1137 CD PRO A 177 42.774 49.917 21.486 1.00 15.26 ATOM 1138 CA PRO A 177 41.722 47.797 20.997 1.00 16.11 ATOM 1139 CB PRO A 177 43.185 47.814 20.534 1.00 16.45 ATOM 1140 CG PRO A 177 43.491 49.272 20.340 1.00 15.90 ATOM 1141 C PRO A 177 41.466 46.673 21.995 1.00 16.18 ATOM 1142 O PRO A 177 41.512 46.870 23.211 1.00 16.44 ATOM 1143 N LEU A 178 41.216 45.485 21.459 1.00 15.12 ATOM 1144 CA LEU A 178 40.958 44.303 22.268 1.00 15.59 ATOM 1145 CB LEU A 178 39.567 43.744 21.957 1.00 15.24 ATOM 1146 CG LEU A 178 39.190 42.414 22.620 1.00 15.95 ATOM 1147 CD1 LEU A 178 39.216 42.567 24.138 1.00 14.48 ATOM 1148 CD2 LEU A 178 37.804 41.986 22.152 1.00 14.88 ATOM 1149 C LEU A 178 42.006 43.239 21.965 1.00 14.93 ATOM 1150 0 LEU A 178 42.315 42.977 20.804 1.00 14.69 ATOM 1151 N GLY A 179 42.559 42.639 23.013 1.00 15.57 ATOM 1152 CA GLY A 179 43.546 41.592 22.832 1.00 13.53 ATOM 1153 C GLY A 179 43.036 40.292 23.430 1.00 13.94 ATOM 1154 0 GLY A 179 42.314 40.313 24.427 1.00 12.42 ATOM 1155 N VAL A 180 43.391 39.164 22.818 1.00 13.58 ATOM 1156 CA VAL A 180 42.985 37.856 23.326 1.00 13.10 ATOM 1157 CB VAL A 180 42.060 37.114 22.348 1.00 12.34 ATOM 1158 CG1 VAL A 180 41.785 35.713 22.872 1.00 10.35 ATOM 1159 CG2 VAL A 180 40.762 37.880 22.176 1.00 13.73

ATOM 1160 C VAL A 180 44.223 36.995 23.566 1.00 13.99 ATOM 1161 0 VAL A 180 45.028 36.769 22.658 1.00 14.16 ATOM 1162 N ASN A 181 44.360 36.519 24.797 1.00 14.29 ATOM 1163 CA ASN A 181 45.494 35.701 25.204 1.00 15.91 ATOM 1164 CB ASN A 181 45.891 36.089 26.632 1.00 16.63 ATOM 1165 CG ASN A 181 47.170 35.433 27.086 1.00 17.72 ATOM 1166 OD1 ASN A 181 47.332 34.214 26.986 1.00 16.04 ATOM 1167 ND2 ASN A 181 48.092 36.241 27.606 1.00 18.08 ATOM 1168 C ASN A 181 45.118 34.215 25.126 1.00 16.42 ATOM 1169 0 ASN A 181 44.143 33.775 25.744 1.00 14.66 ATOM 1170 N LEU A 182 45.903 33.456 24.366 1.00 16.83 ATOM 1171 CA LEU A 182 45.665 32.030 24.158 1.00 17.66 ATOM 1172 CB LEU A 182 45.895 31.683 22.688 1.00 16.07 ATOM 1173 CG LEU A 182 45.063 32.452 21.667 1.00 17.09 ATOM 1174 CD1 LEU A 182 45.506 32.068 20.259 1.00 15.57 ATOM 1175 CD2 LEU A 182 43.585 32.135 21.876 1.00 16.09 ATOM 1176 C LEU A 182 46.536 31.112 25.007 1.00 17.78 ATOM 1177 0 LEU A 182 47.742 31.310 25.121 1.00 19.45 ATOM 1178 N GLY A 183 45.913 30.091 25.581 1.00 19.38 ATOM 1179 CA GLY A 183 46.636 29.132 26.395 1.00 20.04 ATOM 1180 C GLY A 183 46.373 27.736 25. 863 1.00 21.64 ATOM 1181 0 GLY A 183 45.763 27.580 24.805 1.00 20.21 ATOM 1182 N LYS A 184 46.823 26.716 26.584 1.00 22.24 ATOM 1183 CA LYS A 184 46.608 25.345 26.141 1.00 23.65 ATOM 1184 CB LYS A 184 47.910 24.746 25.599 1.00 25.57 ATOM 1185 CG LYS A 184 48.874 24.293 26.670 1.00 28.71 ATOM 1186 CD LYS A 184 49.505 22.955 26.300 1.00 32.25 ATOM 1187 CE LYS A 184 50.079 22.260 27.534 1.00 35.22 ATOM 1188 NZ LYS A 184 50.604 20.898 27.229 1.00 37.42 ATOM 1189 C LYS A 184 46.067 24.466 27.266 1.00 23.40 ATOM 1190 0 LYS A 184 46.339 24.699 28.443 1.00 23.34 ATOM 1191 N ASN A 185 45.293 23.455 26.893 1.00 24.12 ATOM 1192 CA ASN A 185 44.712 22.542 27.866 1.00 24.81 ATOM 1193 CB ASN A 185 43.674 21.640 27.194 1.00 22.02 ATOM 1194 CG ASN A 185 42.349 22.341 26.979 1.00 21.04 ATOM 1195 OD1 ASN A 185 41.860 22.442 25.853 1.00 18.81 ATOM 1196 ND2 ASN A 185 41.758 22.830 28.064 1.00 19.40

ATOM 1197 C ASN A 185 45.758 21.684 28.567 1.00 26.33 ATOM 1198 0 ASN A 185 46.753 21.271 27.970 1.00 26.09 ATOM 1199 N LYS A 186 45.502 21.411 29.841 1.00 28.32 ATOM 1200 CA LYS A 186 46.389 20.610 30.672 1.00 31.00 ATOM 1201 CB LYS A 186 45.758 20.442 32.057 1.00 31.57 ATOM 1202 CG LYS A 186 46.588 19.640 33.039 1.00 34.30 ATOM 1203 CD LYS A 186 45.932 19.624 34.412 1.00 36.90 ATOM 1204 CE LYS A 186 46.830 18.965 35.444 1.00 38.54 ATOM 1205 NZ LYS A 186 46.265 19.074 36.824 1.00 42.77 ATOM 1206 C LYS A 186 46.707 19.236 30.080 1.00 31.61 ATOM 1207 0 LYS A 186 47.846 18.781 30.131 1.00 30.28 ATOM 1208 N THR A 187 45.696 18.584 29.516 1.00 33.93 ATOM 1209 CA THR A 187 45.868 17.253 28.944 1.00 36.41 ATOM 1210 CB THR A 187 44.687 16.339 29.318 1.00 36.67 ATOM 1211 OG1 THR A 187 43.495 16.815 28.678 1.00 35.00 ATOM 1212 CG2 THR A 187 44.479 16.335 30.830 1.00 36.74 ATOM 1213 C THR A 187 46.005 17.243 27.427 1.00 37.64 ATOM 1214 0 THR A 187 45.789 16.214 26.788 1.00 38.91 ATOM 1215 N SER A 188 46.359 18.382 26.847 1.00 38.56 ATOM 1216 CA SER A 188 46.524 18.457 25.402 1.00 38.88 ATOM 1217 CB SER A 188 46.703 19.908 24.962 1.00 39.09 ATOM 1218 OG SER A 188 46.982 19.984 23.576 1.00 39.52 ATOM 1219 C SER A 188 47.738 17.639 24.971 1.00 39.36 ATOM 1220 0 SER A 188 48.759 17.621 25.655 1.00 39.30 ATOM 1221 N VAL A 189 47.619 16.967 23.832 1.00 39.91 ATOM 1222 CA VAL A 189 48.702 16.146 23.302 1.00 41.03 ATOM 1223 CB VAL A 189 48.152 14.828 22.714 1.00 42.23 ATOM 1224 CG1 VAL A 189 49.287 14.003 22.127 1.00 43.91 ATOM 1225 CG2 VAL A 189 47.421 14.040 23.794 1.00 42.66 ATOM 1226 C VAL A 189 49.466 16.881 22.203 1.00 40.93 ATOM 1227 0 VAL A 189 50.556 16.469 21.807 1.00 42.30 ATOM 1228 N ASP A 190 48. 891 17.979 21.721 1.00 39.41 ATOM 1229 CA ASP A 190 49.493 18.764 20.649 1.00 36.64 ATOM 1230 CB ASP A 190 48.748 18.467 19.344 1.00 38.93 ATOM 1231 CG ASP A 190 49.462 19.001 18.120 1.00 40.37 ATOM 1232 OD1 ASP A 190 50. 152 20.038 18.225 1.00 40.59 ATOM 1233 OD2 ASP A 190 49.314 18.382 17.045 1.00 42.48

ATOM 1234 C ASP A 190 49.392 20.258 20.981 1.00 34.58 ATOM 1235 O ASP A 190 48.405 20.913 20.639 1.00 33.67 ATOM 1236 N ALA A 191 50.416 20.792 21.642 1.00 31.42 ATOM 1237 CA ALA A 191 50.432 22.200 22.033 1.00 27.87 ATOM 1238 CB ALA A 191 51.759 22.539 22.708 1.00 27.00 ATOM 1239 C ALA A 191 50.199 23.138 20.857 1.00 26.64 ATOM 1240 O ALA A 191 49.386 24.059 20.932 1.00 24.74 ATOM 1241 N ALA A 192 50.925 22.906 19.772 1.00 25.42 ATOM 1242 CA ALA A 192 50.796 23.739 18.590 1.00 25.28 ATOM 1243 CB ALA A 192 51.725 23.233 17.487 1.00 24.03 ATOM 1244 C ALA A 192 49.356 23.769 18.096 1.00 24.83 ATOM 1245 O ALA A 192 48.840 24.829 17.761 1.00 25.43 ATOM 1246 N GLU A 193 48.704 22.611 18.052 1.00 24.14 ATOM 1247 CA GLU A 193 47.325 22.565 17.587 1.00 24.59 ATOM 1248 CB GLU A 193 46.840 21.117 17.459 1.00 27.03 ATOM 1249 CG GLU A 193 45.429 20.999 16.885 1.00 31.53 ATOM 1250 CD GLU A 193 45. 284 21.623 15.496 1.00 35.25 ATOM 1251 OE1 GLU A 193 44.134 21.818 15.051 1.00 36.27 ATOM 1252 OE2 GLU A 193 46.312 21.911 14.842 1.00 37.72 ATOM 1253 C GLU A 193 46.407 23.356 18.522 1.00 24.21 ATOM 1254 O GLU A 193 45.480 24.022 18.059 1.00 23.61 ATOM 1255 N ASP A 194 46.664 23.292 19.828 1.00 21.48 ATOM 1256 CA ASP A 194 45.861 24.047 20.791 1.00 22.74 ATOM 1257 CB ASP A 194 46.396 23.855 22.214 1.00 21.86 ATOM 1258 CG ASP A 194 45.696 22.732 22.952 1.00 23.25 ATOM 1259 OD1 ASP A 194 45.166 21.826 22.282 1.00 26.44 ATOM 1260 OD2 ASP A 194 45.680 22.747 24.203 1.00 23.07 ATOM 1261 C ASP A 194 45.876 25.537 20.430 1.00 23.39 ATOM 1262 0 ASP A 194 44.822 26.167 20.304 1.00 24.67 ATOM 1263 N TYR A 195 47.066 26.102 20.255 1.00 20.91 ATOM 1264 CA TYR A 195 47.154 27.507 19.900 1.00 21.95 ATOM 1265 CB TYR A 195 48.609 27.981 19.918 1.00 22.02 ATOM 1266 CG TYR A 195 49.211 27.972 21.304 1.00 22.80 ATOM 1267 CD1 TYR A 195 50.009 26.921 21.732 1.00 25.25 ATOM 1268 CE1 TYR A 195 50.518 26.887 23.020 1.00 24.25 ATOM 1269 CD2 TYR A 195 48.939 28.992 22.202 1.00 22.50 ATOM 1270 CE2 TYR A 195 49.442 28.968 23.491 1.00 23.44

ATOM 1271 CZ TYR A 195 50.229 27.913 23.895 1.00 23.86 ATOM 1272 OH TYR A 195 50. 721- 27. 882 25.181 1.00 26.06 ATOM 1273 C TYR A 195 46.531 27.748 18.532 1.00 21.73 ATOM 1274 0 TYR A 195 45.922 28.788 18.300 1.00 20.92 ATOM 1275 N ALA A 196 46.676 26.776 17.635 1.00 22.63 ATOM 1276 CA ALA A 196 46.114 26.882 16.291 1.00 22.46 ATOM 1277 CB ALA A 196 46.454 25.641 15.477 1.00 21.74 ATOM 1278 C ALA A 196 44.599 27.057 16.366 1.00 22.46 ATOM 1279 0 ALA A 196 44.031 27.903 15.672 1.00 22.82 ATOM 1280 N GLU A 197 43.950 26.252 17.204 1.00 21.69 ATOM 1281 CA GLU A 197 42.501 26.342 17.364 1.00 23.49 ATOM 1282 CB GLU A 197 41.985 25.303 18.370 1.00 26.37 ATOM 1283 CG GLU A 197 42.357 23.863 18.050 1.00 35.55 ATOM 1284 CD GLU A 197 41.608 22.855 18.917 1.00 40.35 ATOM 1285 OE1 GLU A 197 42.041 21.682 18.981 1.00 40.76 ATOM 1286 OE2 GLU A 197 40.579 23.235 19.524 1.00 43.83 ATOM 1287 C GLU A 197 42.162 27.737 17.869 1.00 21.55 ATOM 1288 0 GLU A 197 41.214 28.368 17.396 1.00 20.17 ATOM 1289 N GLY A 198 42.955 28.208 18.831 1.00 19.05 ATOM 1290 CA GLY A 198 42.744 29.522 19.401 1.00 16.82 ATOM 1291 C GLY A 198 42.790 30.622 18.362 1.00 16.04 ATOM 1292 0 GLY A 198 41.967 31.538 18.381 1.00 13.85 ATOM 1293 N VAL A 199 43.757 30.538 17.455 1.00 16.13 ATOM 1294 CA VAL A 199 43.894 31.534 16.403 1.00 15.39 ATOM 1295 CB VAL A 199 45.144 31.268 15.543 1.00 15.53 ATOM 1296 CG1 VAL A 199 45.175 32.225 14.351 1.00 12.07 ATOM 1297 CG2 VAL A 199 46.400 31.424 16.393 1.00 14.66 ATOM 1298 C VAL A 199 42.666 31.502 15.500 1.00 16.99 ATOM 1299 0 VAL A 199 42.127 32.544 15.126 1.00 15.25 ATOM 1300 N ARG A 200 42.219 30.296 15.167 1.00 18.08 ATOM 1301 CA ARG A 200 41.062 30.119 14.296 1.00 20.59 ATOM 1302 CB ARG A 200 40.949 28.656 13.851 1.00 21.75 ATOM 1303 CG ARG A 200 42.052 28.201 12.911 1.00 25.45 ATOM 1304 CD ARG A 200 41.661 26.913 12.209 1.00 26.76 ATOM 1305 NE ARG A 200 41.756 25.748 13.079 1.00 27.81 ATOM 1306 CZ ARG A 200 42.857 25.022 13.229 1.00 31.77 ATOM 1307 NH1 ARG A 200 43. 957 25.343 12.562 1.00 32.51

ATOM 1308 NH2 ARG A 200 42.861 23.974 14.045 1.00 32.64 ATOM 1309 C ARG A 200 39.730 30.546 14.900 1.00 19.16 ATOM 1310 O ARG A 200 38.882 31.105 14.207 1.00 19.15 ATOM 1311 N VAL A 201 39.541 30.288 16.188 1.00 18.46 ATOM 1312 CA VAL A 201 38.276 30.624 16.825 1.00 16.58 ATOM 1313 CB VAL A 201 37.964 29.635 17.981 1.00 16.58 ATOM 1314 CG1 VAL A 201 36.661 30.031 18.685 1.00 13.59 ATOM 1315 CG2 VAL A 201 37.853 28.212 17.424 1.00 12.80 ATOM 1316 C VAL A 201 38.161 32.053 17.342 1.00 17.72 ATOM 1317 0 VAL A 201 37.132 32.702 17.138 1.00 17.43 ATOM 1318 N LEU A 202 39.208 32.555 17.994 1.00 16.85 ATOM 1319 CA LEU A 202 39.156 33.906 18.544 1.00 16.20 ATOM 1320 CB LEU A 202 39.657 33.895 19.990 1.00 16. 83 ATOM 1321 CG LEU A 202 38.747 33.119 20.947 1.00 18.98 ATOM 1322 CD1 LEU A 202 39.256 33.246 22.379 1.00 16.76 ATOM 1323 CD2 LEU A 202 37.325 33.664 20.831 1.00 16.77 ATOM 1324 C LEU A 202 39.903 34.962 17.741 1.00 16.51 ATOM 1325 O LEU A 202 39.632 36.157 17.872 1.00 15.03 ATOM 1326 N GLY A 203 40.839 34.521 16.909 1.00 16.09 ATOM 1327 CA GLY A 203 41.597 35.453 16.100 1.00 16.71 ATOM 1328 C GLY A 203 40.737 36.446 15.338 1.00 16.82 ATOM 1329 0 GLY A 203 41.079 37.626 15.261 1.00 15.75 ATOM 1330 N PRO A 204 39.611 36.003 14.760 1.00 17.04 ATOM 1331 CD PRO A 204 39.177 34.601 14.618 1.00 17.18 ATOM 1332 CA PRO A 204 38.729 36.900 14.003 1.00 17.32 ATOM 1333 CB PRO A 204 37.713 35.941 13.371 1.00 16.93 ATOM 1334 CG PRO A 204 38.451 34.630 13.306 1.00 17.12 ATOM 1335 C PRO A 204 38.043 37.955 14.869 1.00 17.63 ATOM 1336 O PRO A 204 37.494 38.928 14.354 1.00 17.99 ATOM 1337 N LEU A 205 38.079 37.759 16.184 1.00 17.45 ATOM 1338 CA LEU A 205 37.433 38.682 17.116 1.00 16.83 ATOM 1339 CB LEU A 205 36.565 37.888 18.101 1.00 16.28 ATOM 1340 CG LEU A 205 35.394 37.106 17.488 1.00 20.11 ATOM 1341 CD1 LEU A 205 35.041 35.896 18.335 1.00 17.62 ATOM 1342 CD2 LEU A 205 34.203 38.035 17.350 1.00 20.89 ATOM 1343 C LEU A 205 38.420 39.546 17.900 1.00 17.46 ATOM 1344 0 LEU A 205 38.015 40.316 18.772 1.00 16.55

ATOM 1345 N ALA A 206 39.706 39.443 17.580 1.00 15.70 ATOM 1346 CA ALA A 206 40.707 40.200 18.318 1.00 16.71 ATOM 1347 CB ALA A 206 41.608 39.229 19.077 1.00 17.67 ATOM 1348 C ALA A 206 41.563 41.150 17.494 1.00 18.08 ATOM 1349 0 ALA A 206 41.810 40.926 16.313 1.00 20.90 ATOM 1350 N ASP A 207 42.015 42.225 18.123 1.00 17.59 ATOM 1351 CA ASP A 207 42.877 43.159 17.431 1.00 18.07 ATOM 1352 CB ASP A 207 42.816 44.532 18.090 1.00 17.18 ATOM 1353 CG ASP A 207 41.508 45.246 17.787 1.00 18.63 ATOM 1354 OD1 ASP A 207 41.170 45.360 16.594 1.00 19.40 ATOM 1355 OD2 ASP A 207 40.813 45.684 18.725 1.00 19.83 ATOM 1356 C ASP A 207 44.270 42.553 17.470 1.00 18.03 ATOM 1357 0 ASP A 207 45. 050 42.708 16.533 1.00 17.72 ATOM 1358 N TYR A 208 44.572 41.843 18.554 1.00 17.96 ATOM 1359 CA TYR A 208 45.850 41.150 18.662 1.00 17.00 ATOM 1360 CB TYR A 208 46.946 42.049 19.267 1.00 17.79 ATOM 1361 CG TYR A 208 46.848 42.358 20.750 1.00 17.93 ATOM 1362 CD1 TYR A 208 46.344 43.577 21.197 1.00 18.65 ATOM 1363 CE1 TYR A 208 46.324 43.897 22.546 1.00 17.54 ATOM 1364 CD2 TYR A 208 47.324 41.461 21.699 1.00 16.58 ATOM 1365 CE2 TYR A 208 47.306 41.768 23.052 1.00 18.19 ATOM 1366 CZ TYR A 208 46.806 42.986 23.471 1.00 19.57 ATOM 1367 OH TYR A 208 46.776 43.286 24.817 1.00 18.19 ATOM 1368 C TYR A 208 45.691 39.866 19.475 1.00 16.78 ATOM 1369 0 TYR A 208 44.864 39.790 20.389 1.00 15.50 ATOM 1370 N LEU A 209 46.460 38.849 19.101 1.00 15.49 ATOM 1371 CA LEU A 209 46.437 37.562 19.783 1.00 17.52 ATOM 1372 CB LEU A 209 46.324 36.413 18.778 1.00 17.27 ATOM 1373 CG LEU A 209 44.998 36.199 18.047 1.00 18.45 ATOM 1374 CD1 LEU A 209 45.167 35.096 17.003 1.00 18.80 ATOM 1375 CD2 LEU A 209 43.916 35.825 19.044 1.00 16.66 ATOM 1376 C LEU A 209 47.729 37.400 20.570 1.00 17. 91 ATOM 1377 0 LEU A 209 48.780 37.893 20.160 1.00 17.96 ATOM 1378 N VAL A 210 47.653 36.701 21.695 1.00 17.39 ATOM 1379 CA VAL A 210 48.833 36.483 22.518 1.00 17.32 ATOM 1380 CB VAL A 210 48.673 37.088 23.933 1.00 17.21 ATOM 1381 CG1 VAL A 210 49.973 36.919 24.714 1.00 15.24

ATOM 1382 CG2 VAL A 210 48.279 38.559 23.840 1.00 16.48 ATOM 1383 C VAL A 210 49.109 35.003 22.695 1.00 17.74 ATOM 1384 O VAL A 210 48.290 34.276 23.257 1.00 18.14 ATOM 1385 N VAL A 211 50.256 34.552 22.204 1.00 18.02 ATOM 1386 CA VAL A 211 50.630 33.159 22.373 1.00 18.15 ATOM 1387 CB VAL A 211 51.608 32.682 21.271 1.00 17.93 ATOM 1388 CG1 VAL A 211 51.994 31.226 21.508 1.00 17.07 ATOM 1389 CG2 VAL A 211 50.953 32.819 19.905 1.00 17.85 ATOM 1390 C VAL A 211 51.318 33.115 23.734 1.00 18.99 ATOM 1391 0 VAL A 211 52.486 33.486 23.868 1.00 18.16 ATOM 1392 N ASN A 212 50.569 32.695 24.750 1.00 19.69 ATOM 1393 CA ASN A 212 51.100 32.615 26.098 1.00 19.88 ATOM 1394 CB ASN A 212 49.972 32.681 27.128 1.00 20.27 ATOM 1395 CG ASN A 212 50.492 32.616 28.547 1.00 18.89 ATOM 1396 OD1 ASN A 212 51.694 32.723 28.770 1.00 21.39 ATOM 1397 ND2 ASN A 212 49.597 32.444 29.511 1.00 17.08 ATOM 1398 C ASN A 212 51.899 31.333 26.279 1.00 21.25 ATOM 1399 O ASN A 212 51.346 30.238 26.408 1.00 21.20 ATOM 1400 N VAL A 213 53.214 31.489 26.305 1.00 20.47 ATOM 1401 CA VAL A 213 54.113 30.362 26.442 1.00 21.67 ATOM 1402 CB VAL A 213 55.010 30.280 25.182 1.00 23.71 ATOM 1403 CG1 VAL A 213 55.981 31.460 25.150 1.00 23.82 ATOM 1404 CG2 VAL A 213 55.748 28.982 25.152 1.00 27.31 ATOM 1405 C VAL A 213 54.975 30.539 27.698 1.00 21.91 ATOM 1406 0 VAL A 213 56.029 29.908 27.843 1.00 22.46 ATOM 1407 N SER A 214 54.506 31.384 28.614 1.00 20.82 ATOM 1408 CA SER A 214 55.255 31.684 29.829 1.00 20.65 ATOM 1409 CB SER A 214 55.741 33.136 29.782 1.00 20.36 ATOM 1410 OG SER A 214 54.666 34.034 29.547 1.00 15.52 ATOM 1411 C SER A 214 54.531 31.442 31.150 1.00 22.40 ATOM 1412 0 SER A 214 54.998 31. 881 32.207 1.00 19.56 ATOM 1413 N SER A 215 53.390 30.763 31.106 1.00 22.46 ATOM 1414 CA SER A 215 52.683 30.482 32.344 1.00 23.77 ATOM 1415 CB SER A 215 51.326 29.839 32.071 1.00 25.30 ATOM 1416 OG SER A 215 50.707 29.476 33.296 1.00 24.25 ATOM 1417 C SER A 215 53.531 29.518 33.168 1.00 23.82 ATOM 1418 0 SER A 215 53.986 28. 488 32.673 1.00 23.43

ATOM 1419 N PRO A 216 53.763 29.845 34.438 1.00 24.01 ATOM 1420 CD PRO A 216 53.529 31. 120 35.142 1.00 22.46 ATOM 1421 CA PRO A 216 54.572 28.931 35.244 1.00 25.17 ATOM 1422 CB PRO A 216 55.177 29.857 36.287 1.00 24.52 ATOM 1423 CG PRO A 216 54.042 30.826 36.538 1.00 23.00 ATOM 1424 C PRO A 216 53.712 27.841 35.881 1.00 26.39 ATOM 1425 0 PRO A 216 54.233 26.928 36.518 1.00 26.20 ATOM 1426 N ASN A 217 52.397 27.923 35.685 1.00 27.51 ATOM 1427 CA ASN A 217 51.485 26.964 36.304 1.00 29.22 ATOM 1428 CB ASN A 217 50.343 27.732 36.966 1.00 28.29 ATOM 1429 CG ASN A 217 50.851 28.799 37.913 1.00 29.28 ATOM 1430 OD1 ASN A 217 51.615 28.507 38.836 1.00 29.47 ATOM 1431 ND2 ASN A 217 50.440 30.046 37.686 1.00 27.94 ATOM 1432 C ASN A 217 50.931 25.825 35.452 1.00 30.25 ATOM 1433 O ASN A 217 49.928 25.204 35.808 1.00 29.74 ATOM 1434 N THR A 218 51.584 25.550 34.331 1.00 31.98 ATOM 1435 CA THR A 218 51.178 24.451 33.462 1.00 33.25 ATOM 1436 CB THR A 218 50.484 24.949 32.177 1.00 33.36 ATOM 1437 OG1 THR A 218 49.194 25.481 32.507 1.00 31.23 ATOM 1438 CG2 THR A 218 50.317 23.800 31.187 1.00 31.71 ATOM 1439 C THR A 218 52.440 23.680 33.096 1.00 33.78 ATOM 1440 O THR A 218 53.319 24.198 32.406 1.00 35.20 ATOM 1441 N ALA A 219 52.522 22.445 33.579 1.00 34.20 ATOM 1442 CA ALA A 219 53.675 21.578 33.353 1.00 34.19 ATOM 1443 CB ALA A 219 53.323 20.146 33.750 1.00 33.41 ATOM 1444 C ALA A 219 54.256 21.593 31.939 1.00 34.71 ATOM 1445 O ALA A 219 53.581 21.240 30.970 1.00 34.13 ATOM 1446 N GLY A 220 55.517 22.010 31.839 1.00 34.72 ATOM 1447 CA GLY A 220 56.212 22.041 30.562 1.00 35.48 ATOM 1448 C GLY A 220 55.842 23.107 29.544 1.00 35.40 ATOM 1449 0 GLY A 220 56.396 23.117 28.446 1.00 35.16 ATOM 1450 N LEU A 221 54.924 24.005 29.888 1.00 35.62 ATOM 1451 CA LEU A 221 54.518 25.049 28.949 1.00 36.17 ATOM 1452 CB LEU A 221 53.333 25.845 29.506 1.00 37.59 ATOM 1453 CG LEU A 221 52.702 26.794 28.481 1.00 37.81 ATOM 1454 CD1 LEU A 221 51.886 25.973 27.495 1.00 38.01 ATOM 1455 CD2 LEU A 221 51. 822 27.822 29.167 1.00 37.63

ATOM 1456 C LEU A 221 55.652 26.019 28.614 1.00 36.27 ATOM 1457 0 LEU A 221 55.829 26.407 27.457 1.00 36.24 ATOM 1458 N ARG A 222 56.415 26.410 29.630 1.00 35.57 ATOM 1459 CA ARG A 222 57.516 27.350 29.441 1.00 35.99 ATOM 1460 CB ARG A 222 58.064 27.787 30.801 1.00 35.50 ATOM 1461 CG ARG A 222 57.107 28.675 31.588 1.00 35.37 ATOM 1462 CD ARG A 222 57.621 28.891 32.997 1.00 37.33 ATOM 1463 NE ARG A 222 57.660 27.637 33.746 1.00 37.02 ATOM 1464 CZ ARG A 222 58.429 27.427 34.808 1.00 37.78 ATOM 1465 NH1 ARG A 222 59.228 28.391 35.246 1.00 37.31 ATOM 1466 NH2 ARG A 222 58.401 26.255 35.430 1.00 36.46 ATOM 1467 C ARG A 222 58.650 26.820 28.565 1.00 35.63 ATOM 1468 0 ARG A 222 59.436 27.599 28.021 1.00 34.70 ATOM 1469 N SER A 223 58.732 25.501 28.419 1.00 35.11 ATOM 1470 CA SER A 223 59.775 24.910 27.591 1.00 34.96 ATOM 1471 CB SER A 223 59.838 23.393 27.797 1.00 34.78 ATOM 1472 OG SER A 223 58.724 22.749 27.205 1.00 35.91 ATOM 1473 C SER A 223 59.491 25.222 26.123 1.00 34.64 ATOM 1474 0 SER A 223 60.346 25.025 25.261 1.00 34.71 ATOM 1475 N LEU A 224 58.286 25.709 25.839 1.00 34.48 ATOM 1476 CA LEU A 224 57.922 26.060 24.468 1.00 34.31 ATOM 1477 CB LEU A 224 56.401 26.201 24.328 1.00 33.45 ATOM 1478 CG LEU A 224 55.538 24.957 24.545 1.00 34.69 ATOM 1479 CD1 LEU A 224 54.063 25.342 24.517 1.00 33.25 ATOM 1480 CD2 LEU A 224 55.852 23.923 23.469 1.00 33.41 ATOM 1481 C LEU A 224 58.611 27.363 24.060 1.00 32.98 ATOM 1482 0 LEU A 224 58.511 27.800 22.914 1.00 32.26 ATOM 1483 N GLN A 225 59.302 27.987 25.012 1.00 33.62 ATOM 1484 CA GLN A 225 60.037 29.223 24.740 1.00 33.44 ATOM 1485 CB GLN A 225 60.248 30.028 26.034 1.00 32.87 ATOM 1486 CG GLN A 225 58.958 30.580 26.637 1.00 32.65 ATOM 1487 CD GLN A 225 59.166 31.235 27.994 1.00 31.96 ATOM 1488 OE1 GLN A 225 59.017 32.450 28.142 1.00 30.99 ATOM 1489 NE2 GLN A 225 59.513 30. 428 28.993 1.00 30.44 ATOM 1490 C GLN A 225 61.390 28.869 24.110 1.00 32.02 ATOM 1491 0 GLN A 225 62.107 29.746 23.630 1.00 30.91 ATOM 1492 N GLY A 226 61.725 27.578 24.119 1.00 31.76

ATOM 1493 CA GLY A 226 62.973 27.117 23.528 1.00 32. 16 ATOM 1494 C GLY A 226 62.982 27.411 22.037 1.00 32.87 ATOM 1495 O GLY A 226 61.932 27.372 21.390 1.00 33.10 ATOM 1496 N LYS A 227 64.161 27.685 21.483 1.00 31.88 ATOM 1497 CA LYS A 227 64.279 28.027 20.069 1.00 31.63 ATOM 1498 CB LYS A 227 65.750 28.190 19.673 1.00 29.76 ATOM 1499 CG LYS A 227 65.909 28.842 18.309 1.00 30.36 ATOM 1500 CD LYS A 227 67.320 29.337 18.047 1.00 31.75 ATOM 1501 CE LYS A 227 67.360 30.139 16.750 1.00 33.43 ATOM 1502 NZ LYS A 227 68.702 30.723 16.462 1.00 35.16 ATOM 1503 C LYS A 227 63.593 27.099 19.068 1.00 31.84 ATOM 1504 O LYS A 227 62.752 27.549 18.287 1.00 31.56 ATOM 1505 N ALA A 228 63.945 25.818 19.081 1.00 31.83 ATOM 1506 CA ALA A 228 63.357 24.862 18.141 1.00 33.57 ATOM 1507 CB ALA A 228 63.962 23.479 18.353 1.00 32.38 ATOM 1508 C ALA A 228 61.832 24.776 18.218 1.00 34.39 ATOM 1509 0 ALA A 228 61.149 24.865 17.197 1.00 34.34 ATOM 1510 N GLU A 229 61.305 24.598 19.426 1.00 35.55 ATOM 1511 CA GLU A 229 59.861 24.496 19.617 1.00 37.25 ATOM 1512 CB GLU A 229 59.540 23.960 21.017 1.00 40.77 ATOM 1513 CG GLU A 229 59.922 22.501 21.212 1.00 46.52 ATOM 1514 CD GLU A 229 59.367 21.915 22.496 1.00 51.23 ATOM 1515 OE1 GLU A 229 59.608 20.712 22.748 1.00 53.05 ATOM 1516 OE2 GLU A 229 58.692 22.652 23.251 1.00 52.90 ATOM 1517 C GLU A 229 59.123 25.812 19.399 1.00 35.01 ATOM 1518 O GLU A 229 57.995 25.817 18.911 1.00 35.28 ATOM 1519 N LEU A 230 59.749 26.926 19.759 1.00 31.93 ATOM 1520 CA LEU A 230 59.105 28.214 19.578 1.00 29.21 ATOM 1521 CB LEU A 230 59.935 29.341 20.210 1.00 27.50 ATOM 1522 CG LEU A 230 59.254 30.717 20.189 1.00 25.31 ATOM 1523 CD1 LEU A 230 57.949 30.639 20.966 1.00 22.54 ATOM 1524 CD2 LEU A 230 60.166 31.775 20.791 1.00 25.43 ATOM 1525 C LEU A 230 58.939 28.473 18.087 1.00 28.35 ATOM 1526 O LEU A 230 57.897 28.959 17.645 1.00 28.45 ATOM 1527 N ARG A 231 59.966 28.139 17.313 1.00 26.82 ATOM 1528 CA ARG A 231 59.923 28.349 15.875 1.00 26.87 ATOM 1529 CB ARG A 231 61. 260 27.965 15.232 1.00 27.39

ATOM 1530 CG ARG A 231 61.280 28.158 13.722 1.00 29.23 ATOM 1531 CD ARG A 231 62.568 27.648 13.079 1.00 32.62 ATOM 1532 NE ARG A 231 63.730 28.479 13.388 1.00 35.22 ATOM 1533 CZ ARG A 231 64.755 28.084 14.139 1.00 35.71 ATOM 1534 NH1 ARG A 231 64.764 26.866 14.665 1.00 35.83 ATOM 1535 NH2 ARG A 231 65.777 28.902 14.355 1.00 35.67 ATOM 1536 C ARG A 231 58.796 27.547 15.230 1.00 26.27 ATOM 1537 0 ARG A 231 58.007 28.083 14.452 1.00 24.54 ATOM 1538 N ARG A 232 58.723 26.264 15.563 1.00 26.74 ATOM 1539 CA ARG A 232 57.701 25.386 15.010 1.00 28.61 ATOM 1540 CB ARG A 232 57.938 23.948 15.481 1.00 31.33 ATOM 1541 CG ARG A 232 56.989 22.931 14.872 1.00 36.52 ATOM 1542 CD ARG A 232 57.345 21.497 15.274 1.00 40. 85 ATOM 1543 NE ARG A 232 58.727 21.154 14.936 1.00 45.04 ATOM 1544 CZ ARG A 232 59.747 21.220 15.788 1.00 46.48 ATOM 1545 NH1 ARG A 232 59.548 21.611 17.041 1.00 47.37 ATOM 1546 NH2 ARG A 232 60.971 20.899 15.387 1.00 45.94 ATOM 1547 C ARG A 232 56.311 25.860 15.426 1.00 28.53 ATOM 1548 0 ARG A 232 55.395 25.942 14.603 1.00 29.20 ATOM 1549 N LEU A 233 56.162 26.184 16.706 1.00 26.18 ATOM 1550 CA LEU A 233 54.891 26.659 17.229 1.00 24.46 ATOM 1551 CB LEU A 233 55.008 26.890 18.737 1.00 23.72 ATOM 1552 CG LEU A 233 53.841 27.633 19.387 1.00 25.00 ATOM 1553 CD1 LEU A 233 52.574 26.806 19.272 1.00 26.45 ATOM 1554 CD2 LEU A 233 54.168 27.907 20.842 1.00 27.05 ATOM 1555 C LEU A 233 54.409 27.948 16.544 1.00 24.04 ATOM 1556 0 LEU A 233 53.270 28.024 16.083 1.00 22.35 ATOM 1557 N LEU A 234 55.279 28.952 16.470 1.00 23.30 ATOM 1558 CA LEU A 234 54.911 30.231 15.864 1.00 24.03 ATOM 1559 CB LEU A 234 55.935 31.308 16.235 1.00 24.63 ATOM 1560 CG LEU A 234 56.001 31.602 17.736 1.00 27.77 ATOM 1561 CD1 LEU A 234 56.990 32.737 18.006 1.00 29.67 ATOM 1562 CD2 LEU A 234 54.612 31.965 18.237 1.00 26.11 ATOM 1563 C LEU A 234 54.731 30.183 14.352 1.00 23.42 ATOM 1564 O LEU A 234 53.975 30.974 13.790 1.00 24.20 ATOM 1565 N THR A 235 55.427 29.269 13.688 1.00 23.68 ATOM 1566 CA THR A 235 55.285 29.139 12.242 1.00 23.60

ATOM 1567 CB THR A 235 56.254 28.084 11.671 1.00 22.71 ATOM 1568 OG1 THR A 235 57.600 28.546 11.819 1.00 24.30 ATOM 1569 CG2 THR A 235 55.966 27.833 10.196 1.00 21.44 ATOM 1570 C THR A 235 53.846 28.699 11.959 1.00 23.27 ATOM 1571 0 THR A 235 53.188 29.221 11.060 1.00 22.47 ATOM 1572 N LYS A 236 53.364 27.745 12.750 1.00 21.09 ATOM 1573 CA LYS A 236 52.011 27.235 12.597 1.00 22.24 ATOM 1574 CB LYS A 236 51.827 25.988 13.468 1.00 23.70 ATOM 1575 CG LYS A 236 50.541 25.236 13.196 1.00 30.31 ATOM 1576 CD LYS A 236 50.512 23.894 13.916 1.00 33.61 ATOM 1577 CE LYS A 236 49.235 23.136 13.588 1.00 34.03 ATOM 1578 NZ LYS A 236 49.184 21.805 14.253 1.00 39.23 ATOM 1579 C LYS A 236 50.980 28.309 12.966 1.00 21.56 ATOM 1580 O LYS A 236 49.988 28.500 12.258 1.00 20.17 ATOM 1581 N VAL A 237 51.223 29.015 14.068 1.00 19.27 ATOM 1582 CA VAL A 237 50.320 30.075 14.502 1.00 19.15 ATOM 1583 CB VAL A 237 50.792 30.714 15.829 1.00 18.47 ATOM 1584 CG1 VAL A 237 50.037 32.014 16.080 1.00 13.34 ATOM 1585 CG2 VAL A 237 50.562 29.741 16.981 1.00 15.49 ATOM 1586 C VAL A 237 50.199 31.176 13.454 1.00 20.61 ATOM 1587 O VAL A 237 49.091 31.571 13.089 1.00 21.34 ATOM 1588 N LEU A 238 51.336 31.671 12.970 1.00 22.56 ATOM 1589 CA LEU A 238 51.337 32.729 11.960 1.00 23.63 ATOM 1590 CB LEU A 238 52.771 33.179 11.658 1.00 23.97 ATOM 1591 CG LEU A 238 53.528 33.907 12.780 1.00 26.60 ATOM 1592 CD1 LEU A 238 54.919 34.302 12.291 1.00 25.27 ATOM 1593 CD2 LEU A 238 52.757 35.147 13.205 1.00 24.92 ATOM 1594 C LEU A 238 50.656 32.270 10.668 1.00 23.77 ATOM 1595 O LEU A 238 50.020 33.066 9.967 1.00 22.47 ATOM 1596 N GLN A 239 50.785 30.983 10.363 1.00 23.65 ATOM 1597 CA GLN A 239 50.181 30.415 9.163 1.00 25.14 ATOM 1598 CB GLN A 239 50.674 28.981 8.971 1.00 28.29 ATOM 1599 CG GLN A 239 50.626 28.477 7.541 1.00 35.77 ATOM 1600 CD GLN A 239 51.286 27.113 7.398 1.00 41.56 ATOM 1601 OE1 GLN A 239 52.403 26.895 7.886 1.00 42.96 ATOM 1602 NE2 GLN A 239 50.601 26.187 6.726 1.00 40.56 ATOM 1603 C GLN A 239 48.657 30.441 9.305 1.00 23.70

ATOM 1604 0 GLN A 239 47.941 30.845 8.385 1.00 23.65 ATOM 1605 N GLU A 240 48.167 30.013 10.465 1.00 21.97 ATOM 1606 CA GLU A 240 46.734 30.010 10.730 1.00 20. 44 ATOM 1607 CB GLU A 240 46.448 29.386 12.095 1.00 22.95 ATOM 1608 CG GLU A 240 46.828 27.919 12.198 1.00 29.40 ATOM 1609 CD GLU A 240 45.887 26.998 11.430 1.00 33.44 ATOM 1610 OE1 GLU A 240 46.180 25.782 11.370 1.00 35.38 ATOM 1611 OE2 GLU A 240 44.855 27.476 10.900 1.00 32.33 ATOM 1612 C GLU A 240 46.221 31.447 10.701 1.00 19.08 ATOM 1613 0 GLU A 240 45.164 31.725 10.139 1.00 19.25 ATOM 1614 N ARG A 241 46.983 32.357 11.302 1.00 16.60 ATOM 1615 CA ARG A 241 46.618 33.770 11.342 1.00 16.03 ATOM 1616 CB ARG A 241 47.645 34.546 12.184 1.00 14.90 ATOM 1617 CG ARG A 241 47.330 36.025 12.422 1.00 14.73 ATOM 1618 CD ARG A 241 47.582 36.887 11.187 1.00 14.81 ATOM 1619 NE ARG A 241 48.978 36.867 10.751 1.00 16.28 ATOM 1620 CZ ARG A 241 49.961 37.579 11.303 1.00 18.91 ATOM 1621 NH1 ARG A 241 51.195 37.478 10.824 1.00 19.86 ATOM 1622 NH2 ARG A 241 49.719 38.400 12.321 1.00 15.94 ATOM 1623 C ARG A 241 46.529 34.366 9.934 1.00 16.63 ATOM 1624 0 ARG A 241 45.598 35.116 9.631 1.00 15.25 ATOM 1625 N ASP A 242 47.492 34.037 9.074 1.00 18.61 ATOM 1626 CA ASP A 242 47.494 34.565 7.708 1.00 19.30 ATOM 1627 CB ASP A 242 48.831 34.274 7.012 1.00 19.94 ATOM 1628 CG ASP A 242 49.997 35.047 7.626 1.00 22.29 ATOM 1629 OD1 ASP A 242 49.753 36.079 8.285 1.00 22.41 ATOM 1630 OD2 ASP A 242 51.158 34.631 7.438 1.00 21.78 ATOM 1631 C ASP A 242 46.344 34.020 6.860 1.00 19.63 ATOM 1632 0 ASP A 242 45.960 34.630 5.860 1.00 19.11 ATOM 1633 N GLY A 243 45.792 32.879 7.261 1.00 18.88 ATOM 1634 CA GLY A 243 44.690 32.299 6.516 1.00 18.95 ATOM 1635 C GLY A 243 43.362 32.995 6.781 1.00 20.52 ATOM 1636 0 GLY A 243 42.352 32.681 6.145 1.00 20.72 ATOM 1637 N LEU A 244 43.354 33.943 7.714 1.00 18.75 ATOM 1638 CA LEU A 244 42.127 34.665 8.044 1.00 20.57 ATOM 1639 CB LEU A 244 42.165 35.141 9.504 1.00 18.57 ATOM 1640 CG LEU A 244 42.365 34.061 10.570 1.00 20.12

ATOM 1641 CD1 LEU A 244 42.432 34.710 11.947 1.00 17.77 ATOM 1642 CD2 LEU A 244 41.228 33.051 10.500 1.00 17.79 ATOM 1643 C LEU A 244 41.893 35.870 7.131 1.00 20.23 ATOM 1644 0 LEU A 244 42.840 36.505 6.673 1.00 19.19 ATOM 1645 N ARG A 245 40.626 36.180 6.872 1.00 20.66 ATOM 1646 CA ARG A 245 40.283 37.325 6.036 1.00 21.47 ATOM 1647 CB ARG A 245 38.759 37.419 5.884 1.00 20.91 ATOM 1648 CG ARG A 245 38.193 36.330 4.950 1.00 20.87 ATOM 1649 CD ARG A 245 36.720 36.044 5.198 1.00 21.09 ATOM 1650 NE ARG A 245 35.835 37.118 4.758 1.00 22.13 ATOM 1651 CZ ARG A 245 35.416 37.283 3.506 1.00 23.36 ATOM 1652 NH1 ARG A 245 34.606 38.293 3.208 1.00 21.07 ATOM 1653 NH2 ARG A 245 35.798 36.438 2.553 1.00 20. 90 ATOM 1654 C ARG A 245 40.875 38.593 6. 662 1.00 23.84 ATOM 1655 0 ARG A 245 40.956 38.720 7.893 1.00 20.34 ATOM 1656 N ARG A 246 41.291 39.523 5.803 1.00 25.07 ATOM 1657 CA ARG A 246 41.939 40.756 6.232 1.00 26.56 ATOM 1658 CB ARG A 246 42.161 41.672 5.025 1.00 29.73 ATOM 1659 CG ARG A 246 43.280 41.141 4.145 1.00 37.20 ATOM 1660 CD ARG A 246 43.693 42.065 3.006 1.00 41.04 ATOM 1661 NE ARG A 246 44.801 41.472 2.258 1.00 40.54 ATOM 1662 CZ ARG A 246 44.727 40.307 1.624 1.00 40.16 ATOM 1663 NH1 ARG A 246 43.599 39.615 1.640 1.00 40.31 ATOM 1664 NH2 ARG A 246 45.787 39.821 0.996 1.00 41.87 ATOM 1665 C ARG A 246 41.371 41.555 7.394 1.00 25.25 ATOM 1666 0 ARG A 246 42.111 41.875 8.323 1.00 23.36 ATOM 1667 N VAL A 247 40.083 41.881 7.370 1.00 24.09 ATOM 1668 CA VAL A 247 39.527 42.654 8.473 1.00 24.28 ATOM 1669 CB VAL A 247 38.099 43.170 8.149 1.00 26.35 ATOM 1670 CG1 VAL A 247 38.126 43.983 6.861 1.00 25.68 ATOM 1671 CG2 VAL A 247 37.130 42.017 8.029 1.00 27.49 ATOM 1672 C VAL A 247 39.509 41.850 9.775 1.00 24.03 ATOM 1673 0 VAL A 247 39.357 42.413 10.857 1.00 23.84 ATOM 1674 N HIS A 248 39.695 40.536 9.665 1.00 23.16 ATOM 1675 CA HIS A 248 39.696 39.653 10.829 1.00 22.42 ATOM 1676 CB HIS A 248 38.703 38.506 10.606 1.00 23.50 ATOM 1677 CG HIS A 248 37.275 38.950 10.536 1.00 25.02

ATOM 1678 CD2 HIS A 248 36.461 39.171 9.476 1.00 25.76 ATOM 1679 ND1 HIS A 248 36.541 39.273 11.657 1.00 24.47 ATOM 1680 CE1 HIS A 248 35.337 39.675 11.291 1.00 25.12 ATOM 1681 NE2 HIS A 248 35.263 39.624 9.973 1.00 25.47 ATOM 1682 C HIS A 248 41.083 39.076 11.113 1.00 20.89 ATOM 1683 0 HIS A 248 41.216 38.084 11.831 1.00 18.62 ATOM 1684 N ARG A 249 42.110 39.708 10.559 1.00 19.69 ATOM 1685 CA ARG A 249 43.484 39.242 10.730 1.00 20.69 ATOM 1686 CB ARG A 249 44.226 39.385 9.399 1.00 20.68 ATOM 1687 CG ARG A 249 45.425 38.475 9.227 1.00 24.73 ATOM 1688 CD ARG A 249 46.029 38.640 7.830 1.00 24.81 ATOM 1689 NE ARG A 249 45.120 38.193 6.778 1.00 24.85 ATOM 1690 CZ ARG A 249 45.081 38.707 5.553 1.00 26.85 ATOM 1691 NH1 ARG A 249 45.899 39.695 5.220 1.00 27.97 ATOM 1692 NH2 ARG A 249 44.226 38.230 4.654 1.00 26.76 ATOM 1693 C ARG A 249 44. 193 40.043 11.830 1.00 19.79 ATOM 1694 0 ARG A 249 44.579 41.194 11.626 1.00 19.90 ATOM 1695 N PRO A 250 44.371 39.437 13.014 1.00 18.06 ATOM 1696 CD PRO A 250 43.843 38.125 13.435 1.00 16.95 ATOM 1697 CA PRO A 250 45.029 40.112 14.136 1.00 18.31 ATOM 1698 CB PRO A 250 44.465 39.376 15.343 1.00 16.97 ATOM 1699 CG PRO A 250 44.438 37.960 14.837 1.00 17.39 ATOM 1700 C PRO A 250 46.551 40.055 14.125 1.00 18.15 ATOM 1701 0 PRO A 250 47.160 39.265 13.396 1.00 18.56 ATOM 1702 N ALA A 251 47.155 40.911 14.940 1.00 17.21 ATOM 1703 CA ALA A 251 48.600 40.928 15.092 1.00 16.57 ATOM 1704 CB ALA A 251 49.050 42.240 15.712 1.00 15.93 ATOM 1705 C ALA A 251 48.861 39.775 16.056 1.00 15.37 ATOM 1706 O ALA A 251 47.978 39.414 16.839 1.00 13.89 ATOM 1707 N VAL A 252 50.051 39.185 15.986 1.00 15.17 ATOM 1708 CA VAL A 252 50.405 38.076 16.864 1.00 15.31 ATOM 1709 CB VAL A 252 50.732 36.796 16.060 1.00 16.18 ATOM 1710 CG1 VAL A 252 51.332 35.733 16.983 1.00 13.26 ATOM 1711 CG2 VAL A 252 49.455 36.255 15.397 1.00 15.46 ATOM 1712 C VAL A 252 51.601 38.422 17.747 1.00 17.46 ATOM 1713 O VAL A 252 52.667 38.806 17.258 1.00 16.99 ATOM 1714 N LEU A 253 51.407 38.287 19.054 1.00 17.27

ATOM 1715 CA LEU A 253 52.454 38.569 20.020 1.00 17.95 ATOM 1716 CB LEU A 253 52.044 39.727 20.936 1.00 18.28 ATOM 1717 CG LEU A 253 51.981 41.133 20.330 1.00 19.28 ATOM 1718 CD1 LEU A 253 50.743 41. 285 19.464 1.00 20.31 ATOM 1719 CD2 LEU A 253 51. 956 42.153 21.448 1.00 20.44 ATOM 1720 C LEU A 253 52.738 37.332 20.865 1.00 19.31 ATOM 1721 0 LEU A 253 51. 900 36.439 20.985 1.00 18.01 ATOM 1722 N VAL A 254 53.932 37.283 21.440 1.00 19.14 ATOM 1723 CA VAL A 254 54.319 36.171 22.290 1.00 19. 38 ATOM 1724 CB VAL A 254 55.595 35.473 21.753 1.00 19.88 ATOM 1725 CG1 VAL A 254 56.036 34.380 22.708 1.00 20.19 ATOM 1726 CG2 VAL A 254 55.326 34.893 20.377 1.00 19.39 ATOM 1727 C VAL A 254 54.592 36.723 23.686 1.00 17.52 ATOM 1728 0 VAL A 254 55.307 37.706 23.835 1.00 16.58 ATOM 1729 N LYS A 255 54.001 36.104 24.700 1.00 18.56 ATOM 1730 CA LYS A 255 54.204 36.539 26.078 1.00 17.98 ATOM 1731 CB LYS A 255 52.890 36.476 26.861 1.00 16.57 ATOM 1732 CG LYS A 255 52.994 37.018 28.277 1.00 17.78 ATOM 1733 CD LYS A 255 51.616 37.306 28.861 1. 00 18.41 ATOM 1734 CE LYS A 255 51.713 37.881 30.270 1.00 18.09 ATOM 1735 NZ LYS A 255 50.374 38.287 30.777 1.00 17. 48 ATOM 1736 C LYS A 255 55.250 35.630 26.716 1.00 18.74 ATOM 1737 O LYS A 255 55.067 34.412 26.799 1.00 18.62 ATOM 1738 N ILE A 256 56.339 36.239 27.176 1.00 17.14 ATOM 1739 CA ILE A 256 57.446 35.504 27.765 1.00 16.56 ATOM 1740 CB ILE A 256 58.769 35.898 27.080 1.00 16.85 ATOM 1741 CG2 ILE A 256 58.633 35.744 25.573 1.00 16.06 ATOM 1742 CG1 ILE A 256 59.122 37.348 27.422 1.00 15.70 ATOM 1743 CD1 ILE A 256 60.404 37.844 26.774 1.00 14.24 ATOM 1744 C ILE A 256 57.629 35.668 29.268 1.00 17.29 ATOM 1745 0 ILE A 256 57.076 36.579 29.895 1.00 15.74 ATOM 1746 N ALA A 257 58.433 34.778 29.835 1.00 16.30 ATOM 1747 CA ALA A 257 58.715 34.795 31.263 1.00 18.80 ATOM 1748 CB ALA A 257 59.079 33.381 31.740 1.00 17.75 ATOM 1749 C ALA A 257 59.846 35.765 31.605 1.00 18.13 ATOM 1750 0 ALA A 257 60.594 36.211 30.733 1.00 17.13 ATOM 1751 N PRO A 258 59.963 36.122 32.890 1.00 17.72

ATOM 1752 CD PRO A 258 58.899 35.989 33.904 1.00 16.97 ATOM 1753 CA PRO A 258 61.006 37.036 33.354 1.00 16.91 ATOM 1754 CB PRO A 258 60.299 37.815 34.446 1.00 16.77 ATOM 1755 CG PRO A 258 59.484 36.739 35.100 1.00 15.59 ATOM 1756 C PRO A 258 62.171 36.218 33.907 1.00 18.80 ATOM 1757 O PRO A 258 63.165 36.768 34.377 1.00 18.56 ATOM 1758 N ASP A 259 62.041 34.897 33.840 1.00 18.60 ATOM 1759 CA ASP A 259 63.068 34.003 34.362 1.00 20.43 ATOM 1760 CB ASP A 259 62.405 32.914 35.217 1.00 18.43 ATOM 1761 CG ASP A 259 61.400 33.482 36.218 1.00 20.36 ATOM 1762 OD1 ASP A 259 61.745 34.445 36.937 1.00 18.40 ATOM 1763 OD2 ASP A 259 60.263 32.963 36.288 1.00 19.98 ATOM 1764 C ASP A 259 63.921 33.356 33.269 1.00 21.61 ATOM 1765 0 ASP A 259 64.562 32.335 33.497 1.00 24.74 ATOM 1766 N LEU A 260 63.933 33.954 32.086 1.00 21.80 ATOM 1767 CA LEU A 260 64.705 33.419 30.969 1.00 21.12 ATOM 1768 CB LEU A 260 64.196 34.018 29.652 1.00 20.21 ATOM 1769 CG LEU A 260 62.714 33.826 29.301 1.00 20.54 ATOM 1770 CD1 LEU A 260 62.370 34.651 28.068 1.00 20.36 ATOM 1771 CD2 LEU A 260 62.421 32.355 29.064 1.00 17.51 ATOM 1772 C LEU A 260 66.203 33.699 31.096 1.00 21.45 ATOM 1773 O LEU A 260 66.612 34.727 31.638 1.00 22.50 ATOM 1774 N THR A 261 67.018 32.780 30.589 1.00 21.53 ATOM 1775 CA THR A 261 68.470 32.947 30.606 1.00 21.15 ATOM 1776 CB THR A 261 69.198 31.616 30.348 1.00 20.05 ATOM 1777 OG1 THR A 261 68.858 31.140 29.040 1.00 20.20 ATOM 1778 CG2 THR A 261 68.802 30.569 31.384 1.00 16.57 ATOM 1779 C THR A 261 68.816 33.882 29.452 1.00 22.22 ATOM 1780 0 THR A 261 67.957 34.197 28.629 1.00 21.75 ATOM 1781 N SER A 262 70.068 34.321 29.383 1.00 22.31 ATOM 1782 CA SER A 262 70.486 35.202 28.300 1.00 24.10 ATOM 1783 CB SER A 262 71.940 35.639 28.488 1.00 25.21 ATOM 1784 OG SER A 262 72.070 36.517 29.589 1.00 30.65 ATOM 1785 C SER A 262 70.346 34.475 26.967 1.00 23.76 ATOM 1786 0 SER A 262 70.027 35.087 25.944 1.00 23.73 ATOM 1787 N GLN A 263 70.586 33.167 26.992 1.00 22.66 ATOM 1788 CA GLN A 263 70.488 32.338 25.799 1.00 22.80

ATOM 1789 CB GLN A 263 70.984 30.919 26.099 1.00 23.32 ATOM 1790 CG GLN A 263 70.906 29.971 24.911 1.00 28.22 ATOM 1791 CD GLN A 263 71.986 30.228 23.870 1.00 30.88 ATOM 1792 OE1 GLN A 263 73.154 29.893 24.077 1.00 31.95 ATOM 1793 NE2 GLN A 263 71.599 30.829 22.749 1.00 30. 56 ATOM 1794 C GLN A 263 69.043 32.293 25.308 1.00 21.39 ATOM 1795 0 GLN A 263 68.781 32.465 24.113 1.00 20.07 ATOM 1796 N ASP A 264 68.108 32.064 26.231 1.00 21.04 ATOM 1797 CA ASP A 264 66.689 32.010 25.882 1.00 20.35 ATOM 1798 CB ASP A 264 65.806 31.813 27.125 1.00 23.87 ATOM 1799 CG ASP A 264 66.025 30.473 27.813 1.00 25.55 ATOM 1800 OD1 ASP A 264 66.306 29.475 27.122 1.00 24.81 ATOM 1801 OD2 ASP A 264 65.890 30.423 29.057 1.00 28.84 ATOM 1802 C ASP A 264 66.253 33.304 25. 204 1.00 19.30 ATOM 1803 0 ASP A 264 65. 540 33.282 24.205 1.00 19.20 ATOM 1804 N LYS A 265 66.681 34.435 25.753 1.00 19.99 ATOM 1805 CA LYS A 265 66.305 35.728 25.198 1.00 20.75 ATOM 1806 CB LYS A 265 66.742 36.851 26.139 1.00 21.01 ATOM 1807 CG LYS A 265 66.049 36.790 27.489 1.00 23.04 ATOM 1808 CD LYS A 265 66.718 37.703 28.504 1.00 25.84 ATOM 1809 CE LYS A 265 66.395 37.261 29.924 1.00 25.41 ATOM 1810 NZ LYS A 265 67.246 37.944 30.933 1.00 25.82 ATOM 1811 C LYS A 265 66.867 35.944 23.802 1.00 20.04 ATOM 1812 0 LYS A 265 66.161 36.443 22.924 1.00 21.04 ATOM 1813 N GLU A 266 68.127 35.568 23.594 1.00 19.65 ATOM 1814 CA GLU A 266 68.751 35.709 22.278 1.00 20.20 ATOM 1815 CB GLU A 266 70.208 35.228 22.304 1.00 18.79 ATOM 1816 CG GLU A 266 71.131 36.087 23.139 1.00 26.13 ATOM 1817 CD GLU A 266 72.540 35.514 23.258 1.00 28.06 ATOM 1818 OE1 GLU A 266 73.312 36.035 24.090 1.00 28.12 ATOM 1819 OE2 GLU A 266 72.875 34.554 22.525 1.00 29.89 ATOM 1820 C GLU A 266 67.977 34.881 21.255 1.00 19.59 ATOM 1821 0 GLU A 266 67.668 35.363 20.168 1.00 19.33 ATOM 1822 N ASP A 267 67.670 33.634 21.609 1.00 19.65 ATOM 1823 CA ASP A 267 66.937 32.746 20.709 1.00 21.97 ATOM 1824 CB ASP A 267 66.802 31.344 21.314 1.00 22.01 ATOM 1825 CG ASP A 267 68.137 30.637 21.456 1.00 24.73

ATOM 1826 OD1 ASP A 267 69.129 31.106 20.851 1.00 24.83 ATOM 1827 OD2 ASP A 267 68.193 29.606 22.166 1.00 23.73 ATOM 1828 C ASP A 267 65.553 33.292 20.381 1.00 21.47 ATOM 1829 0 ASP A 267 65.145 33.313 19.216 1.00 22.04 ATOM 1830 N ILE A 268 64.834 33.732 21.408 1.00 19.95 ATOM 1831 CA ILE A 268 63.503 34.275 21.211 1.00 19.17 ATOM 1832 CB ILE A 268 62.888 34.744 22.542 1.00 18.87 ATOM 1833 CG2 ILE A 268 61.705 35.656 22.274 1.00 16.95 ATOM 1834 CG1 ILE A 268 62.485 33.528 23.375 1.00 18.97 ATOM 1835 CD1 ILE A 268 61.948 33.877 24.746 1.00 23.19 ATOM 1836 C ILE A 268 63.552 35.450 20.248 1.00 20.01 ATOM 1837 0 ILE A 268 62.743 35.538 19.320 1.00 19.24 ATOM 1838 N ALA A 269 64.509 36.348 20.463 1.00 20.09 ATOM 1839 CA ALA A 269 64.651 37.515 19.601 1.00 21.80 ATOM 1840 CB ALA A 269 65.779 38.409 20.111 1.00 21.97 ATOM 1841 C ALA A 269 64.941 37.065 18.171 1.00 22.48 ATOM 1842 0 ALA A 269 64.396 37.613 17.212 1.00 21.58 ATOM 1843 N SER A 270 65.801 36.059 18.040 1.00 21.92 ATOM 1844 CA SER A 270 66.168 35.531 16.733 1.00 22.88 ATOM 1845 CB SER A 270 67.242 34.452 16.891 1.00 22.22 ATOM 1846 OG SER A 270 67.580 33.882 15.642 1.00 23.76 ATOM 1847 C SER A 270 64.949 34.957 16.006 1.00 23.52 ATOM 1848 O SER A 270 64.714 35.262 14.837 1.00 24.62 ATOM 1849 N VAL A 271 64.176 34.124 16.694 1.00 22.03 ATOM 1850 CA VAL A 271 62.987 33.537 16.088 1.00 23.28 ATOM 1851 CB VAL A 271 62.319 32.533 17.050 1.00 22.08 ATOM 1852 CG1 VAL A 271 60. 977 32.082 16.500 1.00 21.17 ATOM 1853 CG2 VAL A 271 63.232 31.339 17.252 1.00 20.02 ATOM 1854 C VAL A 271 61.987 34.632 15.707 1.00 24.31 ATOM 1855 0 VAL A 271 61.430 34.624 14.611 1.00 23.98 ATOM 1856 N VAL A 272 61.781 35.583 16.612 1.00 26.58 ATOM 1857 CA VAL A 272 60. 859 36.689 16.379 1.00 27.45 ATOM 1858 CB VAL A 272 60.911 37.701 17.551 1.00 27.39 ATOM 1859 CG1 VAL A 272 60.486 39.084 17.076 1.00 25.91 ATOM 1860 CG2 VAL A 272 59.999 37.229 18.675 1.00 26.08 ATOM 1861 C VAL A 272 61. 150 37.423 15.070 1.00 29.27 ATOM 1862 0 VAL A 272 60.241 37.702 14.285 1.00 28.76

ATOM 1863 N LYS A 273 62.418 37.730 14.829 1.00 30.44 ATOM 1864 CA LYS A 273 62.790 38.438 13. 612 1.00 33.44 ATOM 1865 CB LYS A 273 64.132 39.147 13.817 1.00 35.26 ATOM 1866 CG LYS A 273 64.046 40.267 14.863 1.00 39.31 ATOM 1867 CD LYS A 273 65.346 41. 039 15.002 1.00 41.83 ATOM 1868 CE LYS A 273 66.453 40.165 15.559 1.00 42.89 ATOM 1869 NZ LYS A 273 67.722 40.927 15.709 1.00 43.88 ATOM 1870 C LYS A 273 62.832 37.524 12.391 1.00 32.97 ATOM 1871 0 LYS A 273 62.728 37.986 11.258 1.00 33.61 ATOM 1872 N GLU A 274 62.959 36.225 12.628 1.00 32.69 ATOM 1873 CA GLU A 274 63.000 35.244 11.550 1. 00 32.33 ATOM 1874 CB GLU A 274 63.595 33.932 12.064 1.00 34.02 ATOM 1875 CG GLU A 274 63.777 32.860 11.005 1.00 38.20 ATOM 1876 CD GLU A 274 63.910 31.468 11.606 1.00 41.49 ATOM 1877 OE1 GLU A 274 64.611 31.326 12.631 1.00 43.83 ATOM 1878 OE2 GLU A 274 63.321 30.513 11.051 1.00 42.59 ATOM 1879 C GLU A 274 61.597 34.971 10.995 1.00 32.28 ATOM 1880 0 GLU A 274 61.427 34.748 9.796 1.00 32.54 ATOM 1881 N LEU A 275 60.594 34.991 11.871 1.00 29.68 ATOM 1882 CA LEU A 275 59.218 34.715 11.463 1.00 27.61 ATOM 1883 CB LEU A 275 58.547 33.794 12.482 1.00 26.94 ATOM 1884 CG LEU A 275 59.253 32.467 12.760 1.00 26.89 ATOM 1885 CD1 LEU A 275 58.481 31.695 13.822 1.00 26.39 ATOM 1886 CD2 LEU A 275 59.357 31.663 11.468 1.00 25.26 ATOM 1887 C LEU A 275 58.353 35.952 11.272 1.00 26.91 ATOM 1888 0 LEU A 275 57.278 35.873 10.685 1.00 27.65 ATOM 1889 N GLY A 276 58.808 37.091 11.772 1.00 26.85 ATOM 1890 CA GLY A 276 58.024 38.305 11.627 1.00 25.44 ATOM 1891 C GLY A 276 56.956 38.486 12.697 1.00 26.13 ATOM 1892 0 GLY A 276 55.893 39.050 12.427 1.00 26.58 ATOM 1893 N ILE A 277 57.224 38. 001 13.907 1.00 24.15 ATOM 1894 CA ILE A 277 56.282 38.151 15.008 1.00 23.32 ATOM 1895 CB ILE A 277 56.870 37.596 16.322 1.00 23.73 ATOM 1896 CG2 ILE A 277 55.978 37.967 17.500 1.00 22.70 ATOM 1897 CG1 ILE A 277 57.002 36.078 16.217 1.00 22.63 ATOM 1898 CD1 ILE A 277 55.695 35.400 15.862 1.00 25.70 ATOM 1899 C ILE A 277 55. 990 39.641 15.167 1.00 23.51

ATOM 1900 0 ILE A 277 56.900 40.464 15.133 1.00 24.00 ATOM 1901 N ASP A 278 54.721 39.984 15.347 1.00 22.59 ATOM 1902 CA ASP A 278 54.313 41.378 15.468 1.00 21.70 ATOM 1903 CB ASP A 278 52.800 41.478 15.291 1.00 20.81 ATOM 1904 CG ASP A 278 52.337 40.895 13.973 1.00 21.70 ATOM 1905 OD1 ASP A 278 52.800 41.381 12.921 1.00 23.06 ATOM 1906 OD2 ASP A 278 51.519 39.951 13.985 1.00 21. 16 ATOM 1907 C ASP A 278 54.725 42.090 16.753 1.00 22.21 ATOM 1908 O ASP A 278 54.861 43.317 16.767 1.00 22.86 ATOM 1909 N GLY A 279 54.922 41.335 17.828 1.00 20.59 ATOM 1910 CA GLY A 279 55.305 41.960 19.080 1.00 19. 11 ATOM 1911 C GLY A 279 55.495 41. 006 20.241 1.00 19.37 ATOM 1912 0 GLY A 279 55.215 39.810 20.149 1.00 20.05 ATOM 1913 N LEU A 280 55.965 41.554 21.354 1.00 19.59 ATOM 1914 CA LEU A 280 56.219 40.770 22.548 1.00 19. 01 ATOM 1915 CB LEU A 280 57.727 40.701 22.819 1.00 16.13 ATOM 1916 CG LEU A 280 58.636 39. 942 21.852 1.00 18.39 ATOM 1917 CD1 LEU A 280 60.090 40.186 22.215 1.00 17.15 ATOM 1918 CD2 LEU A 280 58.322 38.453 21.907 1.00 17.74 ATOM 1919 C LEU A 280 55.537 41.384 23.759 1.00 18.66 ATOM 1920 0 LEU A 280 55.483 42.607 23.899 1.00 19.48 ATOM 1921 N ILE A 281 54.992 40.533 24.620 1.00 16.58 ATOM 1922 CA ILE A 281 54.381 41. 008 25.850 1.00 16.94 ATOM 1923 CB ILE A 281 53.028 40.345 26.138 1.00 13.57 ATOM 1924 CG2 ILE A 281 52.571 40.719 27.537 1.00 12.68 ATOM 1925 CG1 ILE A 281 51.998 40.805 25.094 1.00 13.42 ATOM 1926 CD1 ILE A 281 50.543 40.631 25.526 1.00 9.50 ATOM 1927 C ILE A 281 55.433 40.543 26.832 1.00 19.04 ATOM 1928 0 ILE A 281 55.630 39.339 27.039 1.00 20.47 ATOM 1929 N VAL A 282 56.127 41.495 27.436 1.00 20.25 ATOM 1930 CA VAL A 282 57.222 41.107 28.288 1.00 20.82 ATOM 1931 CB VAL A 282 58.449 41.986 27.990 1.00 20.22 ATOM 1932 CG1 VAL A 282 59.658 41.516 28.781 1.00 15.02 ATOM 1933 CG2 VAL A 282 58.750 41.897 26.493 1.00 16.68 ATOM 1934 C VAL A 282 57.004 40.935 29.768 1.00 24.85 ATOM 1935 0 VAL A 282 56.667 41.850 30.525 1.00 23.91 ATOM 1936 N THR A 283 57.250 39.676 30.110 1.00 27.60

ATOM 1937 CA THR A 283 57.170 39.027 31.399 1.00 24.79 ATOM 1938 CB THR A 283 58.151 39.615 32.454 1.00 24.20 ATOM 1939 OG1 THR A 283 57.456 39.821 33.690 1.00 20.26 ATOM 1940 CG2 THR A 283 58.814 40.891 31.960 1.00 27.48 ATOM 1941 C THR A 283 55.823 38.783 32.033 1.00 23.31 ATOM 1942 O THR A 283 54.988 39.665 32.254 1.00 21.75 ATOM 1943 N ASN A 284 55.652 37.496 32.279 1.00 20.32 ATOM 1944 CA ASN A 284 54.513 36.914 32.923 1.00 16.76 ATOM 1945 CB ASN A 284 54.398 35.463 32.467 1.00 13.23 ATOM 1946 CG ASN A 284 53.008 34.918 32.624 1.00 13.70 ATOM 1947 OD1 ASN A 284 52.432 34.975 33.708 1.00 12.58 ATOM 1948 ND2 ASN A 284 52.454 34.384 31.537 1.00 11.64 ATOM 1949 C ASN A 284 54.967 36.982 34.383 1.00 15.03 ATOM 1950 0 ASN A 284 55.833 37.789 34.728 1.00 14.08 ATOM 1951 N THR A 285 54.405 36.143 35.239 1.00 14.23 ATOM 1952 CA THR A 285 54.809 36.143 36.638 1.00 14.14 ATOM 1953 CB THR A 285 53.748 35.471 37.520 1.00 13.30 ATOM 1954 OG1 THR A 285 53.423 34.190 36.974 1.00 15.78 ATOM 1955 CG2 THR A 285 52.490 36.323 37.587 1.00 14.21 ATOM 1956 C THR A 285 56.128 35.378 36.757 1.00 14.83 ATOM 1957 O THR A 285 56.488 34.613 35.863 1.00 13.04 ATOM 1958 N THR A 286 56.845 35.585 37.858 1.00 14.34 ATOM 1959 CA THR A 286 58.123 34.910 38.067 1.00 13.36 ATOM 1960 CB THR A 286 59.184 35.889 38.605 1.00 10.54 ATOM 1961 OG1 THR A 286 60.378 35.168 38.925 1.00 14.37 ATOM 1962 CG2 THR A 286 58.689 36.580 39.868 1.00 12.42 ATOM 1963 C THR A 286 58.030 33.739 39.047 1.00 13.96 ATOM 1964 0 THR A 286 57.276 33.794 40.020 1.00 14.35 ATOM 1965 N VAL A 287 58.790 32.678 38.784 1.00 14.22 ATOM 1966 CA VAL A 287 58.801 31.530 39.681 1.00 16.50 ATOM 1967 CB VAL A 287 59.043 30.187 38.945 1.00 17.45 ATOM 1968 CG1 VAL A 287 57.928 29.930 37.950 1.00 16.54 ATOM 1969 CG2 VAL A 287 60.413 30.192 38.264 1.00 17.41 ATOM 1970 C VAL A 287 59.924 31.732 40.692 1.00 16.94 ATOM 1971 O VAL A 287 60.149 30.892 41.557 1.00 17.91 ATOM 1972 N SER A 288 60.642 32.844 40.571 1.00 15.98 ATOM 1973 CA SER A 288 61.713 33.128 41.517 1.00 16.76

ATOM 1974 CB SER A 288 62.718 34.123 40.930 1.00 16.69 ATOM 1975 OG SER A 288 62.166 35.432 40.901 1.00 17.63 ATOM 1976 C SER A 288 61.060 33.756 42.743 1.00 17.52 ATOM 1977 O SER A 288 59. 885 34.135 42.712 1.00 16.42 ATOM 1978 N ARG A 289 61.826 33.862 43.821 1.00 17.88 ATOM 1979 CA ARG A 289 61.333 34.466 45.047 1.00 18.33 ATOM 1980 CB ARG A 289 61.026 33.388 46.091 1.00 18.54 ATOM 1981 CG ARG A 289 59.832 32.501 45.744 1.00 18.01 ATOM 1982 CD ARG A 289 58.509 33.273 45.794 1.00 16.90 ATOM 1983 NE ARG A 289 57.360 32.413 45.506 1.00 15.93 ATOM 1984 CZ ARG A 289 56.922 32.112 44.284 1.00 17.27 ATOM 1985 NH1 ARG A 289 55.874 31.311 44.134 1.00 16.11 ATOM 1986 NH2 ARG A 289 57.515 32.620 43.209 1.00 13.70 ATOM 1987 C ARG A 289 62.425 35.398 45.541 1.00 18.67 ATOM 1988 0 ARG A 289 63.272 35.012 46.344 1.00 19.04 ATOM 1989 N PRO A 290 62.425 36.642 45.044 1.00 18. 96 ATOM 1990 CD PRO A 290 61.414 37.188 44.118 1.00 19.15 ATOM 1991 CA PRO A 290 63.403 37.668 45.407 1.00 18.97 ATOM 1992 CB PRO A 290 62.753 38.952 44.897 1.00 18.09 ATOM 1993 CG PRO A 290 62.050 38.488 43.665 1.00 17.63 ATOM 1994 C PRO A 290 63.676 37.713 46.904 1.00 20.35 ATOM 1995 O PRO A 290 62.759 37.579 47.717 1.00 20.48 ATOM 1996 N ALA A 291 64.942 37.886 47.267 1.00 20.76 ATOM 1997 CA ALA A 291 65.306 37.975 48.676 1.00 19.97 ATOM 1998 CB ALA A 291 66.820 38.117 48.825 1.00 18.35 ATOM 1999 C ALA A 291 64.607 39.214 49.231 1.00 18.32 ATOM 2000 0 ALA A 291 64.572 40.256 48.574 1.00 18.54 ATOM 2001 N GLY A 292 64.036 39.100 50.423 1.00 16.06 ATOM 2002 CA GLY A 292 63.367 40.247 51. 011 1.00 15.84 ATOM 2003 C GLY A 292 61.861 40.134 51.148 1.00 15.05 ATOM 2004 0 GLY A 292 61.256 40.922 51.865 1.00 17.29 ATOM 2005 N LEU A 293 61.244 39.177 50.461 1.00 16.21 ATOM 2006 CA LEU A 293 59.794 39.002 50.567 1.00 15.09 ATOM 2007 CB LEU A 293 59.333 37.772 49.784 1.00 14.95 ATOM 2008 CG LEU A 293 59.498 37.772 48.261 1.00 15.03 ATOM 2009 CD1 LEU A 293 58.985 36.443 47.710 1.00 15.13 ATOM 2010 CD2 LEU A 293 58.726 38.944 47.644 1.00 14.56

ATOM 2011 C LEU A 293 59.457 38.813 52.034 1.00 14.63 ATOM 2012 0 LEU A 293 60.110 38.035 52.722 1.00 13.78 ATOM 2013 N GLN A 294 58.442 39.527 52.508 1.00 15.71 ATOM 2014 CA GLN A 294 58.025 39.444 53.902 1.00 17.52 ATOM 2015 CB GLN A 294 57.812 40.851 54.474 1.00 18.01 ATOM 2016 CG GLN A 294 59.072 41.680 54.535 1.00 19.97 ATOM 2017 CD GLN A 294 60.177 40.954 55.264 1.00 20.66 ATOM 2018 OE1 GLN A 294 60.000 40.540 56.404 1.00 22.11 ATOM 2019 NE2 GLN A 294 61.322 40.790 54.607 1.00 18.57 ATOM 2020 C GLN A 294 56.747 38.641 54.086 1.00 18.13 ATOM 2021 O GLN A 294 56.514 38.075 55.158 1.00 18.69 ATOM 2022 N GLY A 295 55.920 38.607 53.043 1.00 17.25 ATOM 2023 CA GLY A 295 54.657 37.891 53.106 1.00 15.78 ATOM 2024 C GLY A 295 54.750 36.505 53.712 1.00 15.71 ATOM 2025 0 GLY A 295 55.653 35.738 53.394 1.00 15.57 ATOM 2026 N ALA A 296 53.809 36.183 54.590 1.00 15.03 ATOM 2027 CA ALA A 296 53.784 34.873 55.233 1.00 17.37 ATOM 2028 CB ALA A 296 52.668 34.826 56.279 1.00 13.26 ATOM 2029 C ALA A 296 53.581 33.749 54.217 1.00 17.38 ATOM 2030 O ALA A 296 53.942 32.599 54.472 1.00 19.30 ATOM 2031 N LEU A 297 53.020 34.087 53.061 1.00 16.13 ATOM 2032 CA LEU A 297 52.733 33.091 52.034 1.00 16.03 ATOM 2033 CB LEU A 297 51.318 33.331 51.501 1.00 14.34 ATOM 2034 CG LEU A 297 50.289 33.400 52.634 1.00 15.64 ATOM 2035 CD1 LEU A 297 48.928 33.906 52.125 1.00 14.34 ATOM 2036 CD2 LEU A 297 50.173 32.014 53.261 1.00 14.99 ATOM 2037 C LEU A 297 53.734 33.105 50.886 1.00 15.69 ATOM 2038 0 LEU A 297 53.458 32.593 49.805 1.00 15.52 ATOM 2039 N ARG A 298 54.903 33.682 51.140 1.00 18.00 ATOM 2040 CA ARG A 298 55.955 33.799 50.134 1.00 17.07 ATOM 2041 CB ARG A 298 57.142 34.567 50.715 1.00 17.89 ATOM 2042 CG ARG A 298 57.956 33.765 51.710 1.00 19.96 ATOM 2043 CD ARG A 298 59.024 34.625 52.374 1.00 19.70 ATOM 2044 NE ARG A 298 59.866 33.837 53.271 1.00 19.62 ATOM 2045 CZ ARG A 298 60.717 34.362 54.146 1.00 19.91 ATOM 2046 NH1 ARG A 298 61.445 33.570 54.925 1.00 16.38 ATOM 2047 NH2 ARG A 298 60.832 35.683 54.248 1.00 19.27

ATOM 2048 C ARG A 298 56.454 32.478 49.560 1.00 16.46 ATOM 2049 0 ARG A 298 56.963 32.447 48.441 1.00 16.84 ATOM 2050 N SER A 299 56.323 31.387 50.307 1.00 15.46 ATOM 2051 CA SER A 299 56.795 30.104 49.799 1.00 16.47 ATOM 2052 CB SER A 299 57.508 29.315 50.900 1.00 16.12 ATOM 2053 OG SER A 299 58.770 29.897 51.192 1.00 17.77 ATOM 2054 C SERA 299 55.724 29.239 49.146 1.00 15.87 ATOM 2055 0 SER A 299 55.937 28.047 48.927 1.00 16.82 ATOM 2056 N GLU A 300 54.575 29.835 48.842 1.00 14.59 ATOM 2057 CA GLU A 300 53.506 29.113 48.153 1.00 15.91 ATOM 2058 CB GLU A 300 52.201 29.925 48.155 1.00 14.89 ATOM 2059 CG GLU A 300 51.489 30.000 49.499 1.00 19.34 ATOM 2060 CD GLU A 300 50.803 28.695 49.870 1.00 20.55 ATOM 2061 OE1 GLU A 300 50.331 28.570 51.018 1.00 23.41 ATOM 2062 OE2 GLU A 300 50.728 27.796 49.008 1.00 22.41 ATOM 2063 C GLU A 300 53.968 28.926 46.703 1.00 16.00 ATOM 2064 0 GLU A 300 54.659 29.780 46.142 1.00 15.73 ATOM 2065 N THR A 301 53.597 27.802 46.105 1.00 16.98 ATOM 2066 CA THR A 301 53.949 27.518 44.724 1.00 15.65 ATOM 2067 CB THR A 301 53.642 26.055 44.372 1.00 18.57 ATOM 2068 OG1 THR A 301 54.617 25.200 44.985 1.00 18.86 ATOM 2069 CG2 THR A 301 53.638 25.854 42.852 1.00 16.16 ATOM 2070 C THR A 301 53.138 28.408 43.786 1.00 15.99 ATOM 2071 0 THR A 301 51.956 28.672 44.030 1.00 14.76 ATOM 2072 N GLY A 302 53.769 28.867 42.711 1.00 14.89 ATOM 2073 CA GLY A 302 53.057 29.696 41.758 1.00 14.82 ATOM 2074 C GLY A 302 53.882 30.841 41.215 1.00 16.15 ATOM 2075 O GLY A 302 55.076 30.950 41.490 1.00 15.43 ATOM 2076 N GLY A 303 53.235 31.694 40.429 1.00 16.40 ATOM 2077 CA GLY A 303 53.916 32.836 39.852 1.00 14.72 ATOM 2078 C GLY A 303 53.739 34.053 40.735 1.00 14.35 ATOM 2079 0 GLY A 303 52.634 34.327 41.212 1.00 13.54 ATOM 2080 N LEU A 304 54.831 34.776 40.962 1.00 13.61 ATOM 2081 CA LEU A 304 54.807 35.975 41.795 1.00 14.28 ATOM 2082 CB LEU A 304 56.132 36.096 42.558 1.00 15.31 ATOM 2083 CG LEU A 304 56.432 37.328 43.419 1.00 16.52 ATOM 2084 CD1 LEU A 304 55.427 37.462 44.552 1.00 18.84

ATOM 2085 CD2 LEU A 304 57.832 37.182 43.991 1.00 19.39 ATOM 2086 C LEU A 304 54.586 37.208 40.918 1.00 14.66 ATOM 2087 0 LEU A 304 55.164 37.316 39.830 1.00 14.61 ATOM 2088 N SER A 305 53.743 38.127 41.387 1.00 12.97 ATOM 2089 CA SER A 305 53.449 39.353 40.646 1.00 13.05 ATOM 2090 CB SER A 305 52.061 39.272 40.001 1.00 11.51 ATOM 2091 OG SER A 305 51.044 39.187 40.991 1.00 11.71 ATOM 2092 C SER A 305 53.503 40.559 41.579 1.00 13.60 ATOM 2093 O SER A 305 53.588 40.404 42.799 1.00 14.71 ATOM 2094 N GLY A 306 53.458 41.762 41.013 1.00 12.19 ATOM 2095 CA GLY A 306 53.493 42.946 41.853 1.00 13.31 ATOM 2096 C GLY A 306 54.853 43.605 41.953 1.00 14.74 ATOM 2097 0 GLY A 306 55.739 43.350 41.133 1.00 15.44 ATOM 2098 N LYS A 307 55.034 44.432 42.979 1.00 15.30 ATOM 2099 CA LYS A 307 56.285 45.172 43.147 1.00 17.60 ATOM 2100 CB LYS A 307 56.244 46.009 44.439 1.00 19.20 ATOM 2101 CG LYS A 307 57.248 47.177 44.435 1.00 24.22 ATOM 2102 CD LYS A 307 57.307 47.949 45.766 1.00 28.95 ATOM 2103 CE LYS A 307 56.028 48.754 46.030 1.00 30.49 ATOM 2104 NZ LYS A 307 55.713 49.722 44.926 1.00 31.16 ATOM 2105 C LYS A 307 57.590 44.368 43.088 1.00 16.74 ATOM 2106 0 LYS A 307 58.560 44.810 42.474 1.00 17.98 ATOM 2107 N PRO A 308 57.640 43.184 43.720 1.00 15.79 ATOM 2108 CD PRO A 308 56.652 42.578 44. 632 1.00 15.73 ATOM 2109 CA PRO A 308 58.879 42.392 43.684 1.00 14.87 ATOM 2110 CB PRO A 308 58.552 41.196 44.579 1.00 15.23 ATOM 2111 CG PRO A 308 57.529 41.759 45.549 1.00 14.01 ATOM 2112 C PRO A 308 59.310 41.953 42.279 1.00 15.73 ATOM 2113 O PRO A 308 60.468 41.595 42.056 1.00 16.91 ATOM 2114 N LEU A 309 58.371 41.982 41.339 1.00 14.07 ATOM 2115 CA LEU A 309 58.632 41.581 39.963 1.00 14.46 ATOM 2116 CB LEU A 309 57.406 40.847 39.404 1.00 14.21 ATOM 2117 CG LEU A 309 57.307 40.671 37.880 1.00 13.52 ATOM 2118 CD1 LEU A 309 58.420 39.763 37.397 1.00 14.58 ATOM 2119 CD2 LEU A 309 55.948 40.080 37.504 1.00 12.51 ATOM 2120 C LEU A 309 58.961 42.760 39.041 1.00 16. 10 ATOM 2121 0 LEU A 309 59.589 42.579 37.994 1.00 15.89

ATOM 2122 N ARG A 310 58.549 43.958 39.445 1.00 14.15 ATOM 2123 CA ARG A 310 58.731 45.160 38.639 1.00 15.63 ATOM 2124 CB ARG A 310 58.485 46.415 39.485 1.00 14.41 ATOM 2125 CG ARG A 310 58.504 47.711 38.662 1.00 17.37 ATOM 2126 CD ARG A 310 58.331 48.936 39.539 1.00 16.00 ATOM 2127 NE ARG A 310 59.378 48.988 40.556 1.00 16.92 ATOM 2128 CZ ARG A 310 59.328 49.752 41.641 1.00 15.82 ATOM 2129 NH1 ARG A 310 60.328 49.723 42.511 1.00 12.25 ATOM 2130 NH2 ARG A 310 58.277 50.538 41.857 1.00 11.34 ATOM 2131 C ARG A 310 60.039 45.340 37.868 1.00 16.73 ATOM 2132 O ARG A 310 60.049 45.314 36.635 1.00 16.19 ATOM 2133 N ASP A 311 61.141 45.534 38.583 1.00 17.13 ATOM 2134 CA ASP A 311 62.415 45.768 37. 917 1.00 17.51 ATOM 2135 CB ASP A 311 63.413 46.309 38.941 1.00 16.83 ATOM 2136 CG ASP A 311 63.066 47.741 39.368 1.00 19.40 ATOM 2137 OD1 ASP A 311 61.901 48.154 39. 159 1.00 17.25 ATOM 2138 OD2 ASP A 311 63.938 48.454 39.904 1.00 18.54 ATOM 2139 C ASP A 311 62.954 44.576 37.130 1.00 17.90 ATOM 2140 O ASP A 311 63.648 44.748 36.125 1.00 17.56 ATOM 2141 N LEU A 312 62.623 43.368 37.567 1.00 17.93 ATOM 2142 CA LEU A 312 63.042 42.183 36.834 1.00 18.46 ATOM 2143 CB LEU A 312 62.583 40.921 37.564 1.00 19.59 ATOM 2144 CG LEU A 312 62.919 39.572 36.924 1.00 23.20 ATOM 2145 CD1 LEU A 312 64.430 39.435 36.725 1.00 24.90 ATOM 2146 CD2 LEU A 312 62.399 38.457 37.830 1.00 23.93 ATOM 2147 C LEU A 312 62.386 42.270 35.445 1.00 17.74 ATOM 2148 O LEU A 312 63.006 41.930 34.432 1.00 15.60 ATOM 2149 N SER A 313 61.136 42.744 35.404 1.00 16.62 ATOM 2150 CA SER A 313 60.408 42.898 34.136 1.00 18.24 ATOM 2151 CB SER A 313 58.923 43.211 34.372 1.00 19. 90 ATOM 2152 OG SER A 313 58.194 42.044 34.702 1.00 27.76 ATOM 2153 C SER A 313 61.004 44.020 33.296 1.00 16.66 ATOM 2154 0 SER A 313 61.262 43.846 32.105 1.00 16.80 ATOM 2155 N THR A 314 61.206 45.174 33.922 1.00 15. 56 ATOM 2156 CA THR A 314 61.770 46.322 33.231 1.00 15.84 ATOM 2157 CB THR A 314 62.014 47.496 34.202 1.00 15. 11 ATOM 2158 OG1 THR A 314 60.768 47.899 34.784 1.00 14.85

ATOM 2159 CG2 THR A 314 62.626 48.677 33.466 1.00 13.49 ATOM 2160 C THR A 314 63.085 45.932 32.564 1.00 16.33 ATOM 2161 0 THR A 314 63.317 46.264 31.399 1.00 18.25 ATOM 2162 N GLN A 315 63.935 45.210 33.290 1.00 15.30 ATOM 2163 CA GLN A 315 65.214 44.786 32.725 1.00 14.23 ATOM 2164 CB GLN A 315 66.093 44.140 33.804 1.00 12.18 ATOM 2165 CG GLN A 315 66.574 45.115 34.889 1.00 15.16 ATOM 2166 CD GLN A 315 67.541 46.186 34.362 1.00 18.05 ATOM 2167 OE1 GLN A 315 67.240 46.904 33.406 0.50 13.54 ATOM 2168 NE2 GLN A 315 68.699 46.297 34.999 0.50 15.47 ATOM 2169 C GLN A 315 65.018 43.822 31.551 1.00 14.24 ATOM 2170 0 GLN A 315 65.779 43.860 30.584 1.00 15.73 ATOM 2171 N THR A 316 64.001 42.966 31.625 1.00 14.27 ATOM 2172 CA THR A 316 63.737 42.014 30.546 1.00 14.28 ATOM 2173 CB THR A 316 62.649 40.967 30.937 1.00 15.87 ATOM 2174 OG1 THR A 316 63.020 40.306 32.156 1.00 15.52 ATOM 2175 CG2 THR A 316 62.506 39.915 29.838 1.00 13.35 ATOM 2176 C THR A 316 63.260 42.782 29.315 1.00 14.86 ATOM 2177 0 THR A 316 63.586 42.433 28.181 1.00 13.99 ATOM 2178 N ILE A 317 62.484 43.833 29.546 1.00 14.52 ATOM 2179 CA ILE A 317 61.987 44.654 28.451 1.00 14.79 ATOM 2180 CB ILE A 317 61.030 45.741 28.965 1.00 14.10 ATOM 2181 CG2 ILE A 317 60.796 46.788 27.883 1.00 13.16 ATOM 2182 CG1 ILE A 317 59.719 45.097 29.420 1.00 11.47 ATOM 2183 CD1 ILE A 317 58.834 46.020 30.221 1.00 9.53 ATOM 2184 C ILE A 317 63.175 45.333 27.794 1.00 16.65 ATOM 2185 O ILE A 317 63.290 45.380 26.565 1.00 16.75 ATOM 2186 N ARG A 318 64.062 45.850 28.640 1.00 16.88 ATOM 2187 CA ARG A 318 65.257 46.548 28.197 1.00 17.27 ATOM 2188 CB ARG A 318 66.049 47.026 29.422 1.00 16.80 ATOM 2189 CG ARG A 318 66.993 48.183 29.157 1.00 16.19 ATOM 2190 CD ARG A 318 67.763 48.572 30.420 1.00 15.62 ATOM 2191 NE ARG A 318 66.912 49.093 31.491 1.00 12.95 ATOM 2192 CZ ARG A 318 66.287 50.267 31.457 1.00 13.25 ATOM 2193 NH1 ARG A 318 66.406 51.058 30.402 1.00 12.39 ATOM 2194 NH2 ARG A 318 65.548 50.656 32.487 1.00 11.89 ATOM 2195 C ARG A 318 66.123 45.645 27.314 1.00 18.16

ATOM 2196 0 ARG A 318 66.580 46.063 26.248 1.00 18.08 ATOM 2197 N GLU A 319 66.330 44.402 27.742 1.00 18.16 ATOM 2198 CA GLU A 319 67.150 43.477 26.965 1.00 19.04 ATOM 2199 CB GLU A 319 67.505 42.228 27.793 1.00 21.85 ATOM 2200 CG GLU A 319 68.788 41.525 27.319 1.00 30.49 ATOM 2201 CD GLU A 319 69.140 40.265 28.118 1.00 36.16 ATOM 2202 OE1 GLU A 319 69.040 40.276 29.368 1.00 36.36 ATOM 2203 OE2 GLU A 319 69.538 39.261 27.487 1.00 39.86 ATOM 2204 C GLU A 319 66.479 43.052 25.657 1.00 18.06 ATOM 2205 0 GLU A 319 67. 143 42.957 24.632 1.00 18.69 ATOM 2206 N MET A 320 65.172 42.797 25.680 1.00 18.33 ATOM 2207 CA MET A 320 64.480 42.377 24.460 1.00 18.60 ATOM 2208 CB MET A 320 63.066 41.881 24.781 1.00 17.12 ATOM 2209 CG MET A 320 63.015 40.651 25.697 1.00 16.85 ATOM 2210 SD MET A 320 64.127 39.287 25.203 1.00 19.70 ATOM 2211 CE MET A 320 63.525 38.893 23.541 1.00 13.82 ATOM 2212 C MET A 320 64.419 43.497 23.415 1.00 18.70 ATOM 2213 0 MET A 320 64.518 43.245 22.214 1.00 18.14 ATOM 2214 N TYR A 321 64.267 44.732 23.879 1.00 19.06 ATOM 2215 CA TYR A 321 64.208 45.885 22.990 1.00 19.32 ATOM 2216 CB TYR A 321 64.026 47.167 23.804 1.00 17.79 ATOM 2217 CG TYR A 321 63.837 48.414 22.964 1.00 19.03 ATOM 2218 CD1 TYR A 321 62.629 48.666 22.319 1.00 18.88 ATOM 2219 CE1 TYR A 321 62.445 49.814 21.568 1.00 18.27 ATOM 2220 CD2 TYR A 321 64.861 49.348 22.828 1.00 18.63 ATOM 2221 CE2 TYR A 321 64.688 50.501 22.075 1.00 17.09 ATOM 2222 CZ TYR A 321 63.479 50.729 21.450 1.00 19.28 ATOM 2223 OH TYR A 321 63.295 51.874 20.710 1.00 20.77 ATOM 2224 C TYR A 321 65.506 45.982 22.189 1.00 19.97 ATOM 2225 0 TYR A 321 65.487 46.184 20.976 1.00 18.20 ATOM 2226 N ALA A 322 66.629 45.839 22.889 1.00 20.65 ATOM 2227 CA ALA A 322 67.952 45.910 22.277 1.00 20.61 ATOM 2228 CB ALA A 322 69.024 46.001 23.370 1.00 18.34 ATOM 2229 C ALA A 322 68.226 44.710 21.365 1.00 20.54 ATOM 2230 0 ALA A 322 68.820 44.853 20.303 1.00 19.72 ATOM 2231 N LEU A 323 67.794 43.528 21.782 1.00 21. 03 ATOM 2232 CA LEU A 323 68.003 42.334 20.972 1.00 22.34

ATOM 2233 CB LEU A 323 67.595 41.087 21.756 1.00 22.34 ATOM 2234 CG LEU A 323 68.535 40.722 22.908 1.00 23.73 ATOM 2235 CD1 LEU A 323 67.953 39.568 23.727 1.00 23.66 ATOM 2236 CD2 LEU A 323 69.893 40.342 22.332 1.00 24.68 ATOM 2237 C LEU A 323 67.218 42.410 19.664 1.00 22.79 ATOM 2238 0 LEU A 323 67.639 41.860 18.649 1.00 24.20 ATOM 2239 N THR A 324 66.079 43.096 19.688 1.00 22.20 ATOM 2240 CA THR A 324 65.261 43.232 18.489 1.00 20.96 ATOM 2241 CB THR A 324 63.755 43.053 18.811 1.00 19.95 ATOM 2242 OG1 THR A 324 63.345 44.007 19.801 1.00 17.13 ATOM 2243 CG2 THR A 324 63.495 41.646 19.326 1.00 17.79 ATOM 2244 C THR A 324 65.489 44.581 17.808 1.00 21.51 ATOM 2245 0 THR A 324 64.767 44.951 16.886 1.00 21.72 ATOM 2246 N GLN A 325 66.506 45.304 18.272 1.00 22.07 ATOM 2247 CA GLN A 325 66.872 46.605 17.718 1.00 22.99 ATOM 2248 CB GLN A 325 67.391 46.454 16.278 1.00 26.13 ATOM 2249 CG GLN A 325 68.721 45.719 16.143 1.00 30.04 ATOM 2250 CD GLN A 325 68.592 44.225 16.351 1.00 35.44 ATOM 2251 OE1 GLN A 325 67.920 43.539 15.580 1.00 40.43 ATOM 2252 NE2 GLN A 325 69.235 43.709 17.395 1.00 37.40 ATOM 2253 C GLN A 325 65.741 47.622 17.732 1.00 22.90 ATOM 2254 0 GLN A 325 65.660 48.479 16.851 1.00 23.32 ATOM 2255 N GLY A 326 64.875 47.534 18.734 1.00 22.53 ATOM 2256 CA GLY A 326 63.768 48.465 18.832 1.00 22.38 ATOM 2257 C GLY A 326 62.810 48.420 17.654 1.00 22.83 ATOM 2258 0 GLY A 326 62.076 49.378 17.419 1.00 21.73 ATOM 2259 N ARG A 327 62.804 47.310 16.919 1.00 23.29 ATOM 2260 CA ARG A 327 61.927 47.166 15.758 1.00 25.92 ATOM 2261 CB ARG A 327 62.728 46.639 14.561 1.00 28.46 ATOM 2262 CG ARG A 327 63.821 47.598 14.096 1.00 33.87 ATOM 2263 CD ARG A 327 64.739 46.980 13.050 1.00 38.29 ATOM 2264 NE ARG A 327 65.816 47.898 12.674 1.00 43.49 ATOM 2265 CZ ARG A 327 66.892 47.549 11.970 1.00 45.02 ATOM 2266 NH1 ARG A 327 67.043 46.296 11.555 1.00 45.41 ATOM 2267 NH2 ARG A 327 67.828 48.451 11.693 1.00 43.95 ATOM 2268 C ARG A 327 60.734 46.250 16.032 1.00 25.90 ATOM 2269 0 ARG A 327 59.890 46.037 15.164 1.00 26.33

ATOM 2270 N VAL A 328 60.671 45.702 17.240 1.00 24.56 ATOM 2271 CA VAL A 328 59.568 44.828 17.609 1.00 22.68 ATOM 2272 CB VAL A 328 60.068 43.433 18.031 1.00 22.99 ATOM 2273 CG1 VAL A 328 58.908 42.603 18.552 1.00 21.00 ATOM 2274 CG2 VAL A 328 60.723 42.737 16.842 1.00 21.97 ATOM 2275 C VAL A 328 58.809 45.454 18.767 1.00 21.90 ATOM 2276 0 VAL A 328 59.358 45.640 19.851 1.00 23.29 ATOM 2277 N PRO A 329 57.537 45.805 18.543 1.00 20.29 ATOM 2278 CD PRO A 329 56.804 45.685 17.271 1.00 19.73 ATOM 2279 CA PRO A 329 56.694 46.418 19.575 1.00 18.81 ATOM 2280 CB PRO A 329 55.329 46.509 18.895 1.00 18.78 ATOM 2281 CG PRO A 329 55.687 46. 689 17.448 1.00 17.49 ATOM 2282 C PRO A 329 56.651 45.575 20.853 1.00 18.50 ATOM 2283 0 PRO A 329 56.452 44.354 20.810 1.00 16.92 ATOM 2284 N ILE A 330 56.833 46.231 21.991 1.00 15.45 ATOM 2285 CA ILE A 330 56.804 45.528 23.257 1.00 15.61 ATOM 2286 CB ILE A 330 58.176 45.604 23.968 1.00 15.68 ATOM 2287 CG2 ILE A 330 58.062 45.057 25.379 1.00 14.36 ATOM 2288 CG1 ILE A 330 59.224 44.823 23.178 1.00 14.42 ATOM 2289 CD1 ILE A 330 60.631 44.968 23.735 1.00 15.43 ATOM 2290 C ILE A 330 55.754 46.078 24.212 1.00 16.03 ATOM 2291 0 ILE A 330 55.612 47.298 24.375 1.00 15.26 ATOM 2292 N ILE A 331 55.004 45.170 24.828 1.00 15.71 ATOM 2293 CA ILE A 331 54.016 45.559 25.824 1.00 15.25 ATOM 2294 CB ILE A 331 52.689 44.779 25.681 1.00 15.14 ATOM 2295 CG2 ILE A 331 51.736 45.170 26.810 1.00 12.02 ATOM 2296 CG1 ILE A 331 52.044 45.082 24.324 1.00 15.56 ATOM 2297 CD1 ILE A 331 50.696 44.422 24.124 1.00 13.64 ATOM 2298 C ILE A 331 54.670 45.189 27.153 1.00 16.63 ATOM 2299 0 ILE A 331 54.932 44.006 27.417 1.00 15.95 ATOM 2300 N GLY A 332 54.959 46.202 27.968 1.00 15.10 ATOM 2301 CA GLY A 332 55.592 45.975 29.259 1.00 14.50 ATOM 2302 C GLY A 332 54.609 45.654 30.371 1.00 14.08 ATOM 2303 0 GLY A 332 53.618 46.357 30.560 1.00 16.41 ATOM 2304 N VAL A 333 54.899 44.602 31.128 1.00 14.35 ATOM 2305 CA VAL A 333 54.021 44.170 32.209 1.00 13.53 ATOM 2306 CB VAL A 333 53. 091 43.023 31.750 1.00 14.02

ATOM 2307 CG1 VAL A 333 51.850 42.971 32.637 1.00 13.16 ATOM 2308 CG2 VAL A 333 52.739 43. 188 30.296 1.00 16.07 ATOM 2309 C VAL A 333 54.829 43. 634 33.378 1.00 12.62 ATOM 2310 O VAL A 333 55.777 42.875 33.189 1.00 12.37 ATOM 2311 N GLY A 334 54.435 44.010 34.589 1.00 13.68 ATOM 2312 CA GLY A 334 55.139 43.536 35.765 1.00 12.74 ATOM 2313 C GLY A 334 55.392 44.600 36.812 1.00 12.69 ATOM 2314 0 GLY A 334 56.300 45.422 36.666 1.00 12.36 ATOM 2315 N GLY A 335 54.576 44.591 37.864 1.00 13.87 ATOM 2316 CA GLY A 335 54.735 45.542 38.953 1.00 13.62 ATOM 2317 C GLY A 335 54.524 47.013 38.636 1.00 14.82 ATOM 2318 0 GLY A 335 55.149 47.877 39.253 1.00 16.20 ATOM 2319 N VAL A 336 53.667 47.317 37.673 1.00 15.48 ATOM 2320 CA VAL A 336 53.401 48.714 37.354 1.00 16.86 ATOM 2321 CB VAL A 336 52.932 48.892 35.899 1.00 17.58 ATOM 2322 CG1 VAL A 336 52.416 50.312 35.690 1.00 17.86 ATOM 2323 CG2 VAL A 336 54.080 48.611 34.949 1.00 17.23 ATOM 2324 C VAL A 336 52.299 49.189 38.292 1.00 17.67 ATOM 2325 O VAL A 336 51.202 48.626 38.316 1.00 18.02 ATOM 2326 N SER A 337 52.589 50.225 39.066 1.00 17.73 ATOM 2327 CA SER A 337 51.608 50.732 40.007 1.00 19.15 ATOM 2328 CB SER A 337 51.932 50.195 41.405 1.00 19.61 ATOM 2329 OG SER A 337 50.979 50.643 42.353 1.00 27.71 ATOM 2330 C SER A 337 51.534 52.258 40.037 1.00 18.75 ATOM 2331 0 SER A 337 50.711 52.829 40.750 1.00 19.78 ATOM 2332 N SER A 338 52.383 52.913 39.253 1.00 17.88 ATOM 2333 CA SER A 338 52.415 54.369 39.217 1.00 15.56 ATOM 2334 CB SER A 338 53.340 54.894 40.320 1.00 15.85 ATOM 2335 OG SER A 338 54.696 54.624 39.992 1.00 12.85 ATOM 2336 C SER A 338 52.925 54.887 37.875 1.00 14.63 ATOM 2337 0 SER A 338 53.390 54.116 37.033 1.00 15.49 ATOM 2338 N GLY A 339 52.850 56.202 37.697 1.00 13.08 ATOM 2339 CA GLY A 339 53.324 56.818 36.474 1.00 12.66 ATOM 2340 C GLY A 339 54.793 56.514 36.241 1.00 13.17 ATOM 2341 0 GLY A 339 55.203 56.222 35.118 1.00 12.67 ATOM 2342 N GLN A 340 55.591 56.579 37.301 1.00 13.06 ATOM 2343 CA GLN A 340 57.016 56.295 37.177 1.00 14.17

ATOM 2344 CB GLN A 340 57.741 56.523 38.508 1.00 14.21 ATOM 2345 CG GLN A 340 59.226 56.203 38.444 1.00 13.71 ATOM 2346 CD GLN A 340 59.936 56.441 39.761 1.00 14.67 ATOM 2347 OE1 GLN A 340 59.940 57.557 40.280 1.00 14.48 ATOM 2348 NE2 GLN A 340 60.542 55.391 40.310 1.00 11.42 ATOM 2349 C GLN A 340 57.252 54.859 36.708 1.00 14.11 ATOM 2350 0 GLN A 340 58.096 54.622 35.836 1.00 14.42 ATOM 2351 N ASP A 341 56.514 53.906 37.279 1.00 11.49 ATOM 2352 CA ASP A 341 56.663 52.502 36.884 1.00 12.60 ATOM 2353 CB ASP A 341 55.719 51.591 37.684 1.00 12.24 ATOM 2354 CG ASP A 341 55.960 51.665 39. 189 1.00 16. 04 ATOM 2355 OD1 ASP A 341 57.082 52.047 39.591 1.00 15.13 ATOM 2356 OD2 ASP A 341 55.031 51.327 39.965 1.00 13.13 ATOM 2357 C ASP A 341 56.365 52.343 35.395 1.00 13.28 ATOM 2358 0 ASP A 341 57.066 51.629 34.676 1.00 13.43 ATOM 2359 N ALA A 342 55.316 53.014 34.937 1.00 13.11 ATOM 2360 CA ALA A 342 54.934 52.953 33.537 1.00 12.86 ATOM 2361 CB ALA A 342 53.596 53.667 33.333 1.00 12.58 ATOM 2362 C ALA A 342 56.009 53.592 32.659 1.00 14.10 ATOM 2363 0 ALA A 342 56.454 52.997 31.667 1.00 14.84 ATOM 2364 N LEU A 343 56.432 54.796 33.031 1.00 12.15 ATOM 2365 CA LEU A 343 57.439 55.510 32.258 1.00 13.26 ATOM 2366 CB LEU A 343 57.654 56.922 32.816 1.00 12.73 ATOM 2367 CG LEU A 343 58.567 57.798 31.949 1.00 16.01 ATOM 2368 CD1 LEU A 343 58.063 57.773 30.503 1.00 12.43 ATOM 2369 CD2 LEU A 343 58.609 59.226 32.491 1.00 12.05 ATOM 2370 C LEU A 343 58.772 54.774 32.191 1.00 13.16 ATOM 2371 O LEU A 343 59.443 54.810 31.164 1.00 15.02 ATOM 2372 N GLU A 344 59.165 54.110 33.275 1.00 13.69 ATOM 2373 CA GLU A 344 60.426 53.378 33.263 1.00 13.68 ATOM 2374 CB GLU A 344 60.756 52.814 34.650 1.00 15.25 ATOM 2375 CG GLU A 344 61.171 53.877 35.661 1.00 16.62 ATOM 2376 CD GLU A 344 61.776 53.285 36.929 1.00 18.34 ATOM 2377 OE1 GLU A 344 61.446 52.128 37.263 1.00 20.22 ATOM 2378 OE2 GLU A 344 62.569 53.980 37.601 1.00 16.51 ATOM 2379 C GLU A 344 60.389 52.250 32.237 1.00 14.20 ATOM 2380 0 GLU A 344 61.382 51.994 31.553 1.00 14.32

ATOM 2381 N LYS A 345 59.246 51.577 32.121 1.00 13.49 ATOM 2382 CA LYS A 345 59.122 50.498 31.146 1.00 14.71 ATOM 2383 CB LYS A 345 57.874 49.658 31.438 1.00 14.57 ATOM 2384 CG LYS A 345 58.094 48.647 32.550 1.00 14.32 ATOM 2385 CD LYS A 345 56.844 47.839 32.832 1.00 15.62 ATOM 2386 CE LYS A 345 57.177 46.571 33.599 1.00 16.36 ATOM 2387 NZ LYS A 345 57.899 46.844 34.871 1.00 15.43 ATOM 2388 C LYS A 345 59.076 51.074 29.732 1.00 14.36 ATOM 2389 0 LYS A 345 59.661 50.518 28.802 1.00 13.74 ATOM 2390 N ILE A 346 58.386 52.195 29.571 1.00 14.93 ATOM 2391 CA ILE A 346 58.313 52.839 28.268 1.00 16.11 ATOM 2392 CB ILE A 346 57.371 54.069 28.305 1.00 16.07 ATOM 2393 CG2 ILE A 346 57.469 54.856 26.990 1.00 14. 19 ATOM 2394 CG1 ILE A 346 55.933 53.591 28.544 1.00 15.01 ATOM 2395 CD1 ILE A 346 54.929 54.691 28.737 1.00 15.20 ATOM 2396 C ILE A 346 59.720 53.259 27.828 1.00 16.73 ATOM 2397 0 ILE A 346 60.143 52.946 26.717 1.00 16.30 ATOM 2398 N ARG A 347 60.449 53.949 28.704 1.00 16.86 ATOM 2399 CA ARG A 347 61.809 54.382 28.378 1.00 16.55 ATOM 2400 CB ARG A 347 62.406 55.217 29.517 1.00 17.95 ATOM 2401 CG ARG A 347 61.684 56.539 29.803 1.00 20.16 ATOM 2402 CD ARG A 347 62.472 57.388 30.800 1.00 21.27 ATOM 2403 NE ARG A 347 63.840 57.588 30.338 1.00 25.93 ATOM 2404 CZ ARG A 347 64.480 58.754 30.349 1.00 29.53 ATOM 2405 NH1 ARG A 347 63.877 59.846 30.810 1.00 29.00 ATOM 2406 NH2 ARG A 347 65.719 58.832 29.874 1.00 26.21 ATOM 2407 C ARG A 347 62.713 53.177 28.118 1.00 16.64 ATOM 2408 0 ARG A 347 63.668 53.257 27.343 1.00 16.63 ATOM 2409 N ALA A 348 62.411 52.062 28.775 1.00 14.46 ATOM 2410 CA ALA A 348 63.197 50.851 28.603 1.00 14.27 ATOM 2411 CB ALA A 348 62.926 49.869 29.752 1.00 11.73 ATOM 2412 C ALA A 348 62.881 50.201 27.258 1.00 14.91 ATOM 2413 0 ALA A 348 63.626 49.326 26.799 1.00 16.61 ATOM 2414 N GLY A 349 61.781 50.617 26.626 1.00 12.73 ATOM 2415 CA GLY A 349 61.445 50.054 25.328 1.00 12.91 ATOM 2416 C GLY A 349 60.010 49.614 25.091 1.00 14.02 ATOM 2417 0 GLY A 349 59. 671 49.197 23.988 1.00 13.81

ATOM 2418 N ALA A 350 59.163 49. 702 26. 109 1. 00 13. 85 ATOM 2419 CA ALA A 350 57. 771 49. 303 25. 955 1. 00 16. 14 ATOM 2420 CB ALA A 350 57. 159 49. 002 27. 320 1. 00 15. 86 ATOM 2421 C ALA A 350 56. 961 50. 389 25. 255 1. 00 17. 71 ATOM 2422 O ALA A 350 57. 080 51. 572 25. 585 1. 00 16. 71 ATOM 2423 N SERA 351 56. 147 49. 983 24. 285 1. 00 16. 76 ATOM 2424 CA SERA 351 55. 297 50. 918 23. 559 1. 00 17. 15 ATOM 2425 CB SERA 351 55. 016 50. 403 22. 146 1. 00 16. 62 ATOM 2426 OG SERA 351 56. 181 50. 446 21. 345 1. 00 20. 56 ATOM 2427 C SERA 351 53. 980 51. 058 24. 323 1. 00 16. 46 ATOM 2428 0 SERA 351 53. 284 52. 068 24. 213 1. 00 16. 26 ATOM 2429 N LEU A 352 53. 658 50. 022 25. 091 1. 00 15. 13 ATOM 2430 CA LEU A 352 52. 446 49. 970 25. 904 1. 00 15. 38 ATOM 2431 CB LEU A 352 51. 334 49. 216 25. 169 1. 00 12. 70 ATOM 2432 CG LEU A 352 50. 889 49. 651 23. 773 1. 00 15. 23 ATOM 2433 CD1 LEU A 352 50. 006 48. 557 23. 165 1. 00 11. 58 ATOM 2434 CD2 LEU A 352 50. 138 50. 984 23. 853 1. 00 13. 14 ATOM 2435 C LEU A 352 52. 761 49. 208 27. 192 1. 00 13. 73 ATOM 2436 0 LEU A 352 53. 703 48. 415 27. 237 1. 00 12. 90 ATOM 2437 N VAL A 353 51. 976 49. 450 28. 235 1. 00 13. 10 ATOM 2438 CA VAL A 353 52. 166 48. 739 29. 490 1. 00 14. 60 ATOM 2439 CB VAL A 353 52. 772 49. 632 30. 608 1. 00 15. 22 ATOM 2440 CG1 VAL A 353 54. 074 50. 246 30. 131 1. 00 15. 03 ATOM 2441 CG2 VAL A 353 51. 778 50. 702 31. 036 1. 00 14. 13 ATOM 2442 C VAL A 353 50. 822 48. 231 29. 971 1. 00 15. 79 ATOM 2443 0 VAL A 353 49. 771 48. 707 29. 529 1. 00 15. 51 ATOM 2444 N GLN A 354 50. 869 47. 249 30. 863 1. 00 15. 70 ATOM 2445 CA GLN A 354 49. 668 46. 667 31. 447 1. 00 15. 81 ATOM 2446 CB GLN A 354 49. 376 45. 274 30. 875 1. 00 15. 87 ATOM 2447 CG GLN A 354 49. 121 45. 206 29. 378 1. 00 17. 93 ATOM 2448 CD GLN A 354 48. 967 43. 766 28. 899 1. 00 18. 91 ATOM 2449 OE1 GLN A 354 49. 736 42. 887 29. 294 1. 00 18. 78 ATOM 2450 NE2 GLN A 354 47. 981 43. 521 28. 042 1. 00 17. 21 ATOM 2451 C GLN A 354 49. 927 46. 517 32. 934 1. 00 15. 00 ATOM 2452 0 GLN A 354 51. 072 46. 529 33. 381 1. 00 15. 73 ATOM 2453 N LEU A 355 48. 859 46. 375 33. 700 1. 00 14. 64 ATOM 2454 CA LEU A 355 48. 997 46. 176 35. 130 1. 00 15. 27

ATOM 2455 CB LEU A 355 48.939 47.514 35.875 1.00 13.69 ATOM 2456 CG LEU A 355 47.681 48.387 35.758 1.00 13.82 ATOM 2457 CD1 LEU A 355 46.594 47.877 36.703 1.00 13.24 ATOM 2458 CD2 LEU A 355 48.044 49.828 36.101 1.00 12.06 ATOM 2459 C LEU A 355 47.867 45.270 35.575 1.00 16. 12 ATOM 2460 0 LEU A 355 46.827 45.184 34.913 1.00 15.56 ATOM 2461 N TYR A 356 48.084 44.566 36.677 1.00 16.25 ATOM 2462 CA TYR A 356 47.053 43.699 37.216 1.00 16.45 ATOM 2463 CB TYR A 356 47.214 42.258 36.696 1.00 14.66 ATOM 2464 CG TYR A 356 46.143 41.280 37.173 1.00 14.33 ATOM 2465 CD1 TYR A 356 46.053 40.004 36.630 1.00 13.71 ATOM 2466 CE1 TYR A 356 45.110 39.093 37.082 1.00 11.25 ATOM 2467 CD2 TYR A 356 45.248 41.618 38.188 1.00 13.31 ATOM 2468 CE2 TYR A 356 44.301 40.711 38.647 1.00 12.21 ATOM 2469 CZ TYR A 356 44.238 39.451 38.091 1.00 12.75 ATOM 2470 OH TYR A 356 43.300 38.542 38.540 1.00 11.10 ATOM 2471 C TYR A 356 47.121 43.739 38.733 1.00 16.00 ATOM 2472 0 TYR A 356 46.185 44.200 39.386 1.00 17.57 ATOM 2473 N THR A 357 48.237 43.284 39.289 1.00 16.04 ATOM 2474 CA THR A 357 48.396 43.236 40.740 1.00 15.39 ATOM 2475 CB THR A 357 49.803 42.738 41.115 1.00 14.82 ATOM 2476 OG1 THR A 357 50.003 41.441 40.544 1.00 11.74 ATOM 2477 CG2 THR A 357 49.953 42.641 42.630 1.00 13.55 ATOM 2478 C THR A 357 48.111 44.551 41.462 1.00 15.12 ATOM 2479 0 THR A 357 47.484 44.552 42.523 1.00 14.91 ATOM 2480 N ALA A 358 48.564 45.665 40.896 1.00 13.89 ATOM 2481 CA ALA A 358 48.332 46.966 41.513 1.00 13.56 ATOM 2482 CB ALA A 358 48.952 48.062 40.674 1.00 12.26 ATOM 2483 C ALA A 358 46.838 47.218 41.677 1.00 15.00 ATOM 2484 0 ALA A 358 46.410 47.833 42.654 1.00 15.57 ATOM 2485 N LEU A 359 46.045 46.745 40.718 1.00 15.00 ATOM 2486 CA LEU A 359 44.596 46.914 40.779 1.00 14.68 ATOM 2487 CB LEU A 359 43.950 46.429 39.479 1.00 16.11 ATOM 2488 CG LEU A 359 42.418 46.354 39.441 1.00 17.58 ATOM 2489 CD1 LEU A 359 41.818 47.752 39.545 1.00 15.57 ATOM 2490 CD2 LEU A 359 41.978 45.680 38.148 1.00 16.77 ATOM 2491 C LEU A 359 44.003 46.140 41.962 1.00 14.70

ATOM 2492 0 LEU A 359 43.009 46.562 42.548 1.00 14.02 ATOM 2493 N THR A 360 44.618 45.013 42.313 1.00 14.46 ATOM 2494 CA THR A 360 44.125 44.195 43.423 1.00 15.22 ATOM 2495 CB THR A 360 44.750 42.781 43.416 1.00 14.92 ATOM 2496 OG1 THR A 360 46.117 42.854 43.844 1.00 13.82 ATOM 2497 CG2 THR A 360 44.699 42.189 42.014 1.00 15.29 ATOM 2498 C THR A 360 44.384 44.820 44.793 1.00 16.37 ATOM 2499 0 THR A 360 43.793 44.400 45.785 1.00 18.61 ATOM 2500 N PHE A 361 45.267 45.812 44.855 1.00 16.42 ATOM 2501 CA PHE A 361 45.558 46.475 46.127 1.00 17.90 ATOM 2502 CB PHE A 361 47.071 46.634 46.335 1.00 17.58 ATOM 2503 CG PHE A 361 47.786 45.347 46.637 1.00 18.37 ATOM 2504 CD1 PHE A 361 48.595 44.748 45.686 1.00 14.59 ATOM 2505 CD2 PHE A 361 47.640 44.733 47.874 1.00 17.75 ATOM 2506 CE1 PHE A 361 49.246 43.566 45.959 1.00 16.05 ATOM 2507 CE2 PHE A 361 48.290 43.544 48.153 1.00 16.55 ATOM 2508 CZ PHE A 361 49.095 42.961 47.191 1.00 17.17 ATOM 2509 C PHE A 361 44.915 47.854 46.253 1.00 19.13 ATOM 2510 O PHE A 361 44.343 48.182 47.285 1.00 21.10 ATOM 2511 N TRP A 362 45.003 48.651 45.190 1.00 20.60 ATOM 2512 CA TRP A 362 44.486 50.013 45.195 1.00 21.41 ATOM 2513 CB TRP A 362 45.496 50.920 44.490 1.00 22.91 ATOM 2514 CG TRP A 362 46.898 50.632 44.933 1.00 26.83 ATOM 2515 CD2 TRP A 362 47.349 50.422 46.281 1.00 28.83 ATOM 2516 CE2 TRP A 362 48.720 50.113 46.218 1.00 29.25 ATOM 2517 CE3 TRP A 362 46.724 50.464 47.534 1.00 30.95 ATOM 2518 CD1 TRP A 362 47.985 50.452 44.136 1.00 26.57 ATOM 2519 NE1 TRP A 362 49.084 50.137 44.898 1.00 28.79 ATOM 2520 CZ2 TRP A 362 49.481 49.845 47.360 1.00 31.64 ATOM 2521 CZ3 TRP A 362 47.483 50.196 48.670 1.00 31.33 ATOM 2522 CH2 TRP A 362 48.844 49.891 48.574 1.00 31.06 ATOM 2523 C TRP A 362 43.103 50.207 44.591 1.00 21.32 ATOM 2524 0 TRP A 362 42.443 51.213 44.856 1.00 21.63 ATOM 2525 N GLY A 363 42.665 49.251 43.782 1.00 20.14 ATOM 2526 CA GLY A 363 41.356 49.364 43.170 1.00 19.06 ATOM 2527 C GLY A 363 41.365 50.224 41.923 1.00 19. 91 ATOM 2528 0 GLY A 363 42.398 50.776 41.545 1.00 20.15

ATOM 2529 N PRO A 364 40.209 50.361 41.262 1.00 19.64 ATOM 2530 CD PRO A 364 38.936 49.783 41.731 1.00 19.35 ATOM 2531 CA PRO A 364 40.006 51.145 40.040 1.00 19.08 ATOM 2532 CB PRO A 364 38.489 51.295 39.980 1.00 18.78 ATOM 2533 CG PRO A 364 38.019 49.989 40.535 1.00 19.83 ATOM 2534 C PRO A 364 40.715 52.497 39.979 1.00 18.77 ATOM 2535 0 PRO. A 364 41.272 52.859 38.951 1.00 21.11 ATOM 2536 N PRO A 365 40.703 53.265 41.079 1.00 20.00 ATOM 2537 CD PRO A 365 40.089 53.024 42.398 1.00 18.27 ATOM 2538 CA PRO A 365 41.370 54.571 41.048 1.00 18.58 ATOM 2539 CB PRO A 365 41.237 55.060 42.491 1.00 19.56 ATOM 2540 CG PRO A 365 39.955 54.429 42.946 1.00 18.79 ATOM 2541 C PRO A 365 42.828 54.538 40.588 1.00 18.76 ATOM 2542 0 PRO A 365 43.366 55.557 40.149 1.00 19.39 ATOM 2543 N VAL A 366 43.472 53.378 40.680 1.00 16.81 ATOM 2544 CA VAL A 366 44.870 53.284 40.278 1.00 15.69 ATOM 2545 CB VAL A 366 45.471 51.900 40.632 1.00 17.04 ATOM 2546 CG1 VAL A 366 45.032 50.854 39.620 1.00 14.83 ATOM 2547 CG2 VAL A 366 46.983 51.999 40.703 1.00 15. 11 ATOM 2548 C VAL A 366 45.062 53.549 38.786 1.00 15.92 ATOM 2549 0 VAL A 366 46.099 54. 056 38.369 1.00 15.23 ATOM 2550 N VAL A 367 44.061 53.218 37.977 1.00 17.40 ATOM 2551 CA VAL A 367 44.173 53.437 36.539 1.00 18.65 ATOM 2552 CB VAL A 367 42.922 52.944 35.798 1.00 18.77 ATOM 2553 CG1 VAL A 367 43.078 53.191 34.309 1.00 18.70 ATOM 2554 CG2 VAL A 367 42.704 51.462 36.081 1.00 18.63 ATOM 2555 C VAL A 367 44.379 54.918 36.227 1.00 18.80 ATOM 2556 0 VAL A 367 45.329 55.292 35.542 1.00 18. 91 ATOM 2557 N GLY A 368 43.488 55.759 36.737 1.00 19.35 ATOM 2558 CA GLY A 368 43.609 57.184 36.501 1.00 19.40 ATOM 2559 C GLY A 368 44.870 57.742 37.131 1.00 20.84 ATOM 2560 0 GLY A 368 45.485 58.671 36.595 1.00 18.86 ATOM 2561 N LYS A 369 45.265 57.169 38.267 1.00 21.29 ATOM 2562 CA LYS A 369 46.463 57.626 38.966 1.00 22.15 ATOM 2563 CB LYS A 369 46.666 56.856 40.276 1.00 22.26 ATOM 2564 CG LYS A 369 47.657 57.537 41.213 1.00 24.45 ATOM 2565 CD LYS A 369 48.206 56.605 42.288 1.00 25.07

ATOM 2566 CE LYS A 369 49.237 55.649 41.706 1.00 25.57 ATOM 2567 NZ LYS A 369 49.956 54.891 42.763 1.00 24.73 ATOM 2568 C LYS A 369 47.688 57.436 38.085 1.00 21.35 ATOM 2569 0 LYS A 369 48.510 58.344 37.937 1.00 21.02 ATOM 2570 N VAL A 370 47.806 56.249 37.499 1.00 20. 37 ATOM 2571 CA VAL A 370 48.935 55.945 36.632 1.00 19.21 ATOM 2572 CB VAL A 370 48.886 54.478 36.144 1.00 18.24 ATOM 2573 CG1 VAL A 370 49.994 54.231 35.133 1.00 15.06 ATOM 2574 CG2 VAL A 370 49.030 53.529 37.336 1.00 15.86 ATOM 2575 C VAL A 370 48.968 56.875 35.425 1.00 20.39 ATOM 2576 0 VAL A 370 50.022 57.409 35.073 1.00 20.38 ATOM 2577 N LYS A 371 47.815 57.078 34.794 1.00 19.77 ATOM 2578 CA LYS A 371 47.754 57.951 33.625 1.00 20.81 ATOM 2579 CB LYS A 371 46.371 57.868 32.963 1.00 20.10 ATOM 2580 CG LYS A 371 46.123 56.531 32.267 1.00 20.41 ATOM 2581 CD LYS A 371 44.848 56.533 31.451 1.00 20.06 ATOM 2582 CE LYS A 371 43. 618 56.701 32.328 1.00 19.96 ATOM 2583 NZ LYS A 371 42.374 56.688 31.510 1.00 18.17 ATOM 2584 C LYS A 371 48.098 59.404 33.944 1.00 21.10 ATOM 2585 O LYS A 371 48.805 60.055 33.176 1.00 20.91 ATOM 2586 N ARG A 372 47.603 59.910 35.071 1.00 21.53 ATOM 2587 CA ARG A 372 47.879 61.288 35.465 1.00 23.57 ATOM 2588 CB ARG A 372 47.065 61.667 36.710 1.00 25.05 ATOM 2589 CG ARG A 372 47.244 63.119 37.135 1.00 29.47 ATOM 2590 CD ARG A 372 46.456 63.480 38.403 1.00 32.48 ATOM 2591 NE ARG A 372 46.958 62.807 39.604 1.00 37.06 ATOM 2592 CZ ARG A 372 46.379 61.755 40.179 1.00 37.86 ATOM 2593 NH1 ARG A 372 45.265 61.242 39.665 1.00 37.52 ATOM 2594 NH2 ARG A 372 46.916 61.215 41.269 1.00 35.72 ATOM 2595 C ARG A 372 49.370 61.503 35.744 1.00 23.58 ATOM 2596 0 ARG A 372 49. 954 62.486 35.284 1.00 23.18 ATOM 2597 N GLU A 373 49.983 60.584 36.490 1.00 22.43 ATOM 2598 CA GLU A 373 51.406 60.694 36.818 1.00 22.21 ATOM 2599 CB GLU A 373 51.798 59.655 37.879 1.00 22.58 ATOM 2600 CG GLU A 373 51.049 59.816 39.203 1.00 21.57 ATOM 2601 CD GLU A 373 51.332 58.689 40.183 1.00 25.08 ATOM 2602 OE1 GLU A 373 51.542 57.547 39.722 1.00 25.29

ATOM 2603 OE2 GLU A 373 51-327 58.936 41.412 1.00 23. 49 ATOM 2604 C GLU A 373 52. 265 60. 509 35.576 1.00 21.94 ATOM 2605 O GLU A 373 53.284 61.178 35.407 1.00 23.16 ATOM 2606 N LEU A 374 51.853 59.601 34.702 1.00 20.39 ATOM 2607 CA LEU A 374 52.601 59.363 33.481 1.00 20.47 ATOM 2608 CB LEU A 374 51.928 58.270 32.648 1.00 18.16 ATOM 2609 CG LEU A 374 52.562 57.989 31.285 1.00 17.79 ATOM 2610 CD1 LEU A 374 54.043 57.696 31.467 1.00 15.43 ATOM 2611 CD2 LEU A 374 51.851 56.817 30.607 1.00 17.19 ATOM 2612 C LEU A 374 52.648 60.661 32.685 1.00 21.91 ATOM 2613 0 LEU A 374 53.711 61.102 32.253 1.00 21.82 ATOM 2614 N GLU A 375 51.482 61.270 32.505 1.00 22.52 ATOM 2615 CA GLU A 375 51.368 62.516 31.760 1.00 25.37 ATOM 2616 CB GLU A 375 49.916 62.995 31.777 1.00 27.60 ATOM 2617 CG GLU A 375 49.635 64.139 30.831 1.00 34.21 ATOM 2618 CD GLU A 375 48.194 64.599 30.906 1.00 37.55 ATOM 2619 OE1 GLU A 375 47.291 63.739 30.809 1.00 39.84 ATOM 2620 OE2 GLU A 375 47.967 65.818 31.056 1.00 39.87 ATOM 2621 C GLU A 375 52.278 63.598 32.339 1.00 23.91 ATOM 2622 0 GLU A 375 53.038 64.232 31.609 1.00 22.96 ATOM 2623 N ALA A 376 52.204 63.798 33.651 1.00 22.62 ATOM 2624 CA ALA A 376 53.030 64.803 34.314 1.00 22.53 ATOM 2625 CB ALA A 376 52.687 64.872 35.811 1.00 17.94 ATOM 2626 C ALA A 376 54.518 64.499 34.121 1.00 22.35 ATOM 2627 0 ALA A 376 55.301 65.400 33.820 1.00 23.58 ATOM 2628 N LEU A 377 54.902 63.232 34.285 1.00 21.82 ATOM 2629 CA LEU A 377 56.298 62.834 34.116 1.00 21.73 ATOM 2630 CB LEU A 377 56.501 61.371 34.528 1.00 19.85 ATOM 2631 CG LEU A 377 56.432 61.109 36.038 1.00 22.75 ATOM 2632 CD1 LEU A 377 56.466 59.608 36.303 1.00 21.26 ATOM 2633 CD2 LEU A 377 57.593 61.816 36.741 1.00 16.51 ATOM 2634 C LEU A 377 56.791 63.041 32.687 1.00 22.19 ATOM 2635 0 LEU A 377 57.945 63.415 32.475 1.00 22.40 ATOM 2636 N LEU A 378 55.934 62.793 31.702 1.00 22.32 ATOM 2637 CA LEU A 378 56.343 62.999 30.315 1.00 22.98 ATOM 2638 CB LEU A 378 55.248 62.525 29.355 1.00 19.93 ATOM 2639 CG LEU A 378 55.048 61.011 29.213 1.00 19.44

ATOM 2640 CD1 LEU A 378 53.777 60.727 28.423 1.00 17.32 ATOM 2641 CD2 LEU A 378 56.256 60.393 28.528 1.00 15.65 ATOM 2642 C LEU A 378 56.637 64.490 30.090 1.00 24.90 ATOM 2643 O LEU A 378 57.625 64.846 29.446 1.00 24.47 ATOM 2644 N LYS A 379 55.781 65.355 30.630 1.00 26.23 ATOM 2645 CA LYS A 379 55.962 66.798 30.491 1.00 30.27 ATOM 2646 CB LYS A 379 54.801 67.558 31.140 1.00 32.19 ATOM 2647 CG LYS A 379 53.431 67.329 30.517 1.00 36.01 ATOM 2648 CD LYS A 379 52.365 68.055 31.337 1.00 38.83 ATOM 2649 CE LYS A 379 50.981 67.944 30.717 1.00 40.37 ATOM 2650 NZ LYS A 379 50.901 68.651 29.410 1.00 42.67 ATOM 2651 C LYS A 379 57.253 67.215 31.182 1.00 30.76 ATOM 2652 O LYS A 379 58.109 67.876 30.600 1.00 31.75 ATOM 2653 N GLU A 380 57.374 66.809 32.438 1.00 31.41 ATOM 2654 CA GLU A 380 58.529 67.125 33.258 1.00 32.37 ATOM 2655 CB GLU A 380 58.332 66.516 34.646 1.00 33.86 ATOM 2656 CG GLU A 380 59.501 66.700 35.586 1.00 40.81 ATOM 2657 CD GLU A 380 59.276 66.017 36.924 1.00 44.51 ATOM 2658 OE1 GLU A 380 60.208 66.025 37.759 1.00 47.77 ATOM 2659 OE2 GLU A 380 58.167 65.476 37.139 1.00 43.32 ATOM 2660 C GLU A 380 59.859 66.658 32.670 1.00 32.10 ATOM 2661 0 GLU A 380 60.904 67.240 32.957 1.00 31.86 ATOM 2662 N GLN A 381 59.830 65.617 31.844 1.00 31.04 ATOM 2663 CA GLN A 381 61.068 65.109 31.265 1.00 30.66 ATOM 2664 CB GLN A 381 61.147 63.588 31.448 1.00 30.50 ATOM 2665 CG GLN A 381 61.526 63.191 32.880 1.00 29.05 ATOM 2666 CD GLN A 381 61.349 61.711 33.165 1.00 30.02 ATOM 2667 OE1 GLN A 381 61.666 60.863 32.331 1.00 30.88 ATOM 2668 NE2 GLN A 381 60.855 61.393 34.359 1.00 27.15 ATOM 2669 C GLN A 381 61.299 65.494 29.810 1.00 30.65 ATOM 2670 O GLN A 381 62.152 64.918 29.135 1.00 30.89 ATOM 2671 N GLY A 382 60.534 66.472 29.336 1.00 29.73 ATOM 2672 CA GLY A 382 60.695 66.958 27.976 1.00 29.28 ATOM 2673 C GLY A 382 60.160 66.145 26.812 1.00 29.75 ATOM 2674 0 GLY A 382 60.547 66.396 25.669 1.00 29.78 ATOM 2675 N PHE A 383 59.281 65.183 27.066 1.00 28.22 ATOM 2676 CA PHE A 383 58.740 64.390 25.968 1.00 28.21

ATOM 2677 CB PHE A 383 58.480 62.949 26.410 1.00 26.99 ATOM 2678 CG PHE A 383 59.718 62.209 26.827 1.00 25.43 ATOM 2679 CD1 PHE A 383 60.001 62.005 28.167 1.00 23.15 ATOM 2680 CD2 PHE A 383 60.592 61.709 25.879 1.00 21.77 ATOM 2681 CE1 PHE A 383 61.131 61.311 28.552 1.00 22.73 ATOM 2682 CE2 PHE A 383 61.722 61.019 26.258 1.00 22.44 ATOM 2683 CZ PHE A 383 61.991 60.818 27.598 1.00 23.36 ATOM 2684 C PHE A 383 57.450 64.988 25.427 1.00 28.57 ATOM 2685 0 PHE A 383 56.561 65.365 26.189 1.00 29.14 ATOM 2686 N GLY A 384 57.356 65.081 24.104 1.00 28.87 ATOM 2687 CA GLY A 384 56.154 65.620 23.497 1.00 29.02 ATOM 2688 C GLY A 384 54.977 64.714 23.799 1.00 29.17 ATOM 2689 O GLY A 384 53.846 65.173 23.949 1.00 30.43 ATOM 2690 N GLY A 385 55.255 63.418 23.895 1.00 28.68 ATOM 2691 CA GLY A 385 54.220 62.444 24.189 1.00 27.39 ATOM 2692 C GLY A 385 54.822 61.072 24.428 1.00 27.16 ATOM 2693 0 GLY A 385 56.034 60.891 24.312 1.00 27.57 ATOM 2694 N VAL A 386 53.975 60.104 24.757 1.00 25.93 ATOM 2695 CA VAL A 386 54.416 58.738 25.018 1.00 25.76 ATOM 2696 CB VAL A 386 53.208 57.784 25.135 1.00 26.31 ATOM 2697 CG1 VAL A 386 53.683 56.337 25.139 1.00 26.62 ATOM 2698 CG2 VAL A 386 52.426 58.093 26.396 1.00 26.19 ATOM 2699 C VAL A 386 55.338 58.198 23.930 1.00 25.24 ATOM 2700 0 VAL A 386 56.382 57.612 24.216 1.00 24.74 ATOM 2701 N THR A 387 54.938 58.403 22.680 1.00 25.11 ATOM 2702 CA THR A 387 55.698 57.930 21.530 1.00 24'. 97 ATOM 2703 CB THR A 387 55.054 58.417 20.211 1.00 26.77 ATOM 2704 OG1 THR A 387 53.687 57.988 20.162 1.00 27.82 ATOM 2705 CG2 THR A 387 55.800 57.856 19.006 1.00 23.16 ATOM 2706 C THR A 387 57.166 58.348 21.542 1.00 24.24 ATOM 2707 0 THR A 387 58.040 57.566 21.171 1.00 24.21 ATOM 2708 N ASP A 388 57.446 59.573 21.970 1.00 24.13 ATOM 2709 CA ASP A 388 58.828 60.049 21.989 1.00 24. 01 ATOM 2710 CB ASP A 388 58.872 61.572 22.140 1.00 28.08 ATOM 2711 CG ASP A 388 57.979 62.282 21.152 1.00 31.47 ATOM 2712 OD1 ASP A 388 56.834 62.614 21.531 1.00 35.57 ATOM 2713 OD2 ASP A 388 58.416 62.498 19.999 1.00 32.91

ATOM 2714 C ASP A 388 59.671 59.428 23.096 1.00 21.44 ATOM 2715 0 ASP A 388 60.894 59.431 23.018 1.00 20.73 ATOM 2716 N ALA A 389 59. 020 58.904 24.128 1. 00 19. 41 ATOM 2717 CA ALA A 389 59.735 58.305 25.249 1.00 18.82 ATOM 2718 CB ALA A 389 58.946 58.528 26.548 1.00 17.68 ATOM 2719 C ALA A 389 60.024 56.816 25.059 1.00 17.88 ATOM 2720 0 ALA A 389 60.871 56.253 25.749 1.00 18.18 ATOM 2721 N ILE A 390 59.320 56.179 24.130 1.00 17.83 ATOM 2722 CA ILE A 390 59.516 54.753 23.875 1.00 16.78 ATOM 2723 CB ILE A 390 58.612 54.264 22.716 1.00 16.58 ATOM 2724 CG2 ILE A 390 58.915 52.808 22.398 1.00 13.38 ATOM 2725 CG1 ILE A 390 57.134 54.435 23.097 1.00 16.11 ATOM 2726 CD1 ILE A 390 56.171 54.247 21.933 1.00 14.39 ATOM 2727 C ILE A 390 60.968 54.425 23.533 1.00 16.91 ATOM 2728 0 ILE A 390 61.451 54.751 22.452 1.00 18.16 ATOM 2729 N GLY A 391 61.661 53.785 24.467 1.00 17.39 ATOM 2730 CA GLY A 391 63.048 53.409 24.242 1.00 16.81 ATOM 2731 C GLY A 391 64.078 54.510 24.445 1.00 16.75 ATOM 2732 0 GLY A 391 65.248 54.322 24.118 1.00 16.88 ATOM 2733 N ALA A 392 63.663 55.641 25.007 1.00 16.78 ATOM 2734 CA ALA A 392 64.573 56.766 25.222 1.00 19.33 ATOM 2735 CB ALA A 392 63.842 57.901 25.930 1.00 17.91 ATOM 2736 C ALA A 392 65.862 56.421 25.977 1.00 19.71 ATOM 2737 0 ALA A 392 66.906 57.011 25.713 1.00 20.84 ATOM 2738 N ASP A 393 65.795 55.475 26.911 1.00 20.21 ATOM 2739 CA ASP A 393 66.982 55.083 27.679 1.00 19.61 ATOM 2740 CB ASP A 393 66.640 53.993 28.700 1.00 18.27 ATOM 2741 CG ASP A 393 65.886 54.521 29.904 1.00 20.38 ATOM 2742 OD1 ASP A 393 65.702 55.753 30.020 1.00 21.42 ATOM 2743 OD2 ASP A 393 65.483 53.690 30.744 1.00 20.13 ATOM 2744 C ASP A 393 68.096 54.551 26.776 1.00 21.69 ATOM 2745 0 ASP A 393 69.277 54.689 27.091 1.00 20.91 ATOM 2746 N HIS A 394 67.712 53.939 25.659 1.00 22.48 ATOM 2747 CA HIS A 394 68.676 53.360 24.730 1.00 24.97 ATOM 2748 CB HIS A 394 67.991 52.297 23.864 1.00 21.33 ATOM 2749 CG HIS A 394 67.382 51.177 24.650 1.00 20. 93 ATOM 2750 CD2 HIS A 394 66.226 51.107 25.354 1.00 19.80

ATOM 2751 ND1 HIS A 394 67.985 49.945 24.782 1.00 18.59 ATOM 2752 CE1 HIS A 394 67.226 49.164 25.531 1.00 18.75 ATOM 2753 NE2 HIS A 394 66.153 49.845 25.891 1.00 18.96 ATOM 2754 C HIS A 394 69.339 54.391 23.825 1.00 27.88 ATOM 2755 0 HIS A 394 70.392 54.130 23.253 1.00 28.20 ATOM 2756 N ARG A 395 68.725 55.560 23.699 1.00 32.23 ATOM 2757 CA ARG A 395 69.262 56.599 22.832 1.00 37.69 ATOM 2758 CB ARG A 395 68.110 57.372 22.176 1.00 36.52 ATOM 2759 CG ARG A 395 67.250 56.510 21.253 1.00 37.79 ATOM 2760 CD ARG A 395 66.316 57.351 20.384 1.00 38.73 ATOM 2761 NE ARG A 395 65.140 57.850 21.097 1.00 39.62 ATOM 2762 CZ ARG A 395 64.091 57.101 21.430 1.00 40.14 ATOM 2763 NH1 ARG A 395 63.064 57.643 22.077 1.00 38.94 ATOM 2764 NH2 ARG A 395 64.064 55.810 21.114 1.00 38.68 ATOM 2765 C ARG A 395 70.222 57.566 23.521 1.00 41.10 ATOM 2766 O ARG A 395 71.015 58.231 22.861 1.00 42.39 ATOM 2767 N ARG A 396 70.163 57.644 24.844 1.00 46.02 ATOM 2768 CA ARG A 396 71.053 58.543 25.568 1.00 50.86 ATOM 2769 CB ARG A 396 70.511 58.820 26.975 1.00 53.12 ATOM 2770 CG ARG A 396 70.485 57.618 27.900 1.00 54.92 ATOM 2771 CD ARG A 396 70.063 58.038 29.297 1.00 58.19 ATOM 2772 NE ARG A 396 70.847 59.180 29.757 1.00 60.28 ATOM 2773 CZ ARG A 396 70.773 59.698 30.978 1.00 61.40 ATOM 2774 NH1 ARG A 396 71.525 60.742 31.302 1.00 61.39 ATOM 2775 NH2 ARG A 396 69.954 59.167 31.876 1.00 62.88 ATOM 2776 C ARG A 396 72.467 57.968 25.661 1.00 52.71 ATOM 2777 O ARG A 396 73.403 58.630 25.164 1.00 54.67 ATOM 2778 OXT ARG A 396 72.626 56.864 26.225 1.00 54.59 TER 1 ARG A 396 END