1. A pharmaceutical composition comprising an effective amount of an agent that specifically binds to a RAGE polypeptide at a site comprising one or more amino acid residues selected from the group consisting of amino acid residues 25, 54, 59, 61, 91, 92, 94, 96, 98, 114, 116, 150, 151, 152, 154, 175, 177, 178, 179, 186, 213, 214, and 216 of the RAGE polypeptide, and a pharmaceutically acceptable excipient. 2. A pharmaceutical composition comprising an effective amount of an agent that inhibits binding of a RAGE ligand to a RAGE polypeptide at a site comprising one or more amino acid residues selected from the group consisting of amino acid residues 25, 54, 59, 61, 91, 92, 94, 96, 98, 114, 116, 150, 151, 152, 154, 175, 177, 178, 179, 186, 213, and 216 of the RAGE

polypeptide, and a pharmaceutically acceptable excipient.

3. The pharmaceutical composition of claim 1 or 2, wherein the agent is an antibody or antigen binding fragment thereof, peptide, polynucleotide, or small molecule compound.

4. The pharmaceutical composition of claim 2, wherein the RAGE ligand is selected from the group consisting of S100A7, S100A8, and S100A9.

5. The pharmaceutical composition of claim 1 or 2, wherein the agent binds at a site comprising one or more amino acid residues selected from the group consisting of amino acid residues 23-54 of the RAGE polypeptide.

6. The pharmaceutical composition of claim 1 or 2, wherein the site comprises each of amino acid residues 25, 54, 59, 61, 92, 94, 96, 114, 116, 150, 151, 152, 175, 177, 179, 186, and 214 of the RAGE polypeptide. 7. The pharmaceutical composition of claim 1 or 2, wherein an effective amount is an amount sufficient to inhibit loss of myosin heavy chain in a cell contacted with the composition.

8. The pharmaceutical composition of claim 1 or 2, wherein an effective amount is an amount sufficient to inhibit cachexia-associated cardiac dysfunction in a subject administered with the composition. 9. A method of inhibiting loss of myosin heavy chain in a cardiomyocyte, the method comprising contacting the cardiomyocyte with an effective amount of an agent that specifically binds to a RAGE polypeptide, thereby inhibiting loss of myosin heavy chain in the

cardiomyocyte. 10. A method of reversing loss of myosin heavy chain in a cardiomyocyte, the method comprising contacting the cardiomyocyte with an effective amount of an agent that specifically binds to a RAGE polypeptide, thereby reversing loss of myosin heavy chain in the cardiomyocyte.

11. A method of preventing and/or inhibiting cardiac dysfunction in a subject, the method comprising administering to the subject an effective amount of an agent that specifically binds to a RAGE polypeptide, thereby preventing or inhibiting cardiac dysfunction in the subject.

12. A method of reversing cardiac dysfunction in a subject, the method comprising

administering to the subject an effective amount of an agent that specifically binds to a RAGE polypeptide, thereby reversing cardiac dysfunction in the subject.

13. A method of treating cardiac dysfunction in a subject, the method comprising

administering to the subject an effective amount of an agent that specifically binds to a RAGE polypeptide, thereby treating cardiac dysfunction in the subject.

14. A method of treating cardiac dysfunction in a selected subject, the method comprising administering to the subject an effective amount of an agent that specifically binds to a RAGE polypeptide, wherein the subject is selected as having an increased level of S100A7, S100A8, or S100A9 polypeptide or polynucleotide in a biological sample obtained from the subject relative to a control level, thereby treating cardiac dysfunction in the subject.

15. The method of any one of claims 11-14, wherein the subject is human.

16. The method of any one of claims 11-15, wherein the cardiac dysfunction is cachexia- associated cardiac dysfunction.

17. The method of any one of claims 11-15, wherein the cardiac dysfunction is heart dysfunction associated with cancer cachexia, cachexia-associated advanced heart failure, heart dysfunction following acute myocardial infarction, cardiac ischemia, or cardiac atrophy.

18. The method of any one of claims 9-17, wherein the agent is an antibody or antigen binding fragment thereof, peptide, polynucleotide, or small molecule compound.

19. The pharmaceutical composition of claim 1 or 2 or method of any one of claims 9-17, wherein the agent is FPS3.

20. The pharmaceutical composition of claim 1 or 2 or method of any one of claims 9-17, wherein the agent is an anti-RAGE antibody.

21. The method of any one of claims 9-10, wherein the cardiomyocyte is in vivo or in vitro.

22. A method for identifying a candidate compound that binds to a site on a RAGE

polypeptide, the method comprising:

(a) providing a three-dimensional structure of a RAGE polypeptide having at least one atomic coordinate, or surrogate thereof, from PDB ID: 4LP4 for each of the amino acid residues 23-54 or for each of the amino acid residues 25, 54, 59, 61, 91, 92, 94, 96, 98, 114, 116, 150, 151, 152, 154, 175, 177, 178, 179, 186, 213, and 216 of the RAGE polypeptide: or atomic coordinates that have a root mean square deviation of the coordinates of less than 3 angstroms; and

(b) producing a structure for a candidate compound wherein the structure defines a molecule having sufficient surface complementary to the RAGE polypeptide to bind the site in an aqueous solution. 23. The method of claim 22, further comprising the step of (c) evaluating the ability of the compound to bind a RAGE polypeptide in an in vitro, in vivo, or ex vivo assay.

24. The method of claim 23, further comprising the step of (d) evaluating the ability of the compound to inhibit cachexia or inhibit loss of myosin heavy chain in a functional assay.

25. The method of any one of claims 22-24, wherein the structure of the candidate compound is designed de novo.

26. The method of any one of claims 22-25, further comprising the step of (e) modifying the candidate compound based upon the positioning, alignment, and interactions between the candidate compound and one or more amino acids comprising the site.

27. The method of claim 23 or 24, wherein the results of the evaluation in step (c) or step (d) provide further structure related binding information such that other candidate compounds are selected for evaluation in step (c) or step (d).

Appendix A: Atomic coordinates provided at PDB ID: 4LP4

HEADER SIGNALING PROTEIN 15-JUL-13 4LP4

TITLE CRYSTAL STRUCTURE OF THE HUMAN RAGE VC1 FRAGMENT IN SPACE GROUP P62

COMPND MOL_ID: 1;

COMPND 2 MOLECULE: ADVANCED GLYCOSYLATION END PRODUCT-SPECIFIC RECEPTOR;

COMPND 3 CHAIN: A, B;

COMPND 4 FRAGMENT: V AND CI DOMAINS (VC1 FRAGMENT), ECTODOMAIN FRAGMENT (UNP

COMPND 5 RESIDUES 23-231) ;

COMPND 6 SYNONYM: RECEPTOR FOR ADVANCED GLYCOSYLATION END PRODUCTS;

COMPND 7 ENGINEERED: YES

SOURCE MOL_ID: 1;

SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;

SOURCE ORGANI SM_COMMON : HUMAN;

SOURCE ORGANISM_TAXID: 9606;

SOURCE GENE: AGER, RAGE;

SOURCE EXPRESSION_SYSTEM: ESCHERICHIA COLI;

SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;

SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SHUFFLE T7 EXPRESS;

SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;

SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PETM11

KEYWDS IMMUNOGLOBULIN FOLD, PATTERN RECOGNITION RECEPTOR, SIGNALING

KEYWDS 2 RECEPTOR, MEMBRANE, SIGNALING PROTEIN

EXPDTA X-RAY DIFFRACTION

AUTHOR L. . YATIME, G. R. .ANDERSEN

REVDAT 4 18-DEC-13 4LP4 1 JRNL

REVDAT 3 27-NOV- 13 4LP4 1 JRNL

REVDAT 2 30-OCT-13 4LP4 1 JRNL

REVDAT 1 16-OCT-13 4LP4 0

JRNL AUTH L. YATIME, G.R.ANDERSEN

JRNL TITL STRUCTURAL INSIGHTS INTO THE OLIGOMERIZATION MODE OF THE

JRNL TITL 2 HUMAN RECEPTOR FOR ADVANCED GLYCATION END-PRODUCTS.

JRNL REF FEBS J. V. 280 6556 2013

JRNL REFN ISSN 1742-464X

JRNL PMID 24119142

JRNL DOI 10.1111/FEBS.12556

REMARK

REMARK RESOLUTION. 2.40 ANGSTROMS.

REMARK

REMARK REFINEMENT.

REMARK PROGRAM PHENIX (PHENIX. REFINE: 1.8.1_1168)

REMARK AUTHORS PAUL ADAMS, PAVEL AFONINE, VICENT CHEN, IAN

REMARK DAVIS, KRESHNA GOPAL, RALF GROSSE-

REMARK KUNSTLEVE, LI-WEI HUNG, ROBERT IMMORMINO,

REMARK TOM IOERGER, AIRLIE MCCOY, ERIK MCKEE, NIGEL

REMARK MORIARTY, REETAL PAI , RANDY READ, JANE

REMARK RICHARDSON, DAVID RICHARDSON, TOD ROMO, JIM

REMARK SACCHETTINI, NICHOLAS SAUTER, JACOB SMITH,

REMARK LAURENT STORONI,TOM TERWILLIGER, PETER

REMARK ZWART

REMARK

REMARK REFINEMENT TARGET ML

REMARK

REMARK DATA USED IN REFINEMENT.

REMARK RESOLUTION RANGE HIGH (ANGSTROMS) 2.40

REMARK RESOLUTION RANGE LOW (ANGSTROMS) 33.39

REMARK MIN (FOBS/ SIGMA FOBS) 2.000 REMARK COMPLETENESS FOR RANGE (%) 99.6

REMARK NUMBER OF REFLECTIONS 23854

REMARK REMARK FIT TO DATA USED IN REFINEMENT.

REMARK R VALUE (WORKING + TEST SET) 0.180

REMARK R VALUE (WORKING SET) 0.178

REMARK FREE R VALUE 0.217

REMARK FREE R VALUE TEST SET SIZE (%) 5.080

REMARK FREE R VALUE TEST SET COUNT 1212

REMARK REMARK FIT TO DATA USED IN REFINEMENT (IN BINS)

REMARK N RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 1 33. .3906 - 4 .9873 0. , 99 2559 133 0 .1674 0 .2231 REMARK 2 4. .9873 - 3 .9606 1. , 00 2535 133 0 .1430 0 .1570 REMARK 3 3. .9606 - 3 .4605 0. , 98 2458 132 0 .1952 0 .2268 REMARK 4 3. .4605 - 3 .1444 1. , 00 2519 136 0 .1840 0 .2246 REMARK 5 3. .1444 - 2 .9192 1. , 00 2506 141 0 .1980 0 .2362 REMARK 6 2. .9192 - 2 .7471 1. , 00 2505 139 0 .1941 0 .2483 REMARK 7 2. .7471 - 2 .6096 1. , 00 2532 135 0 .1873 0 .2329 REMARK 8 2. .6096 - 2 .4961 1. , 00 2493 134 0 .1953 0 .2526 REMARK 9 2. .4961 - 2 .4000 1. , 00 2535 129 0 .2107 0 .2460 REMARK REMARK BULK SOLVENT MODELLING REMARK METHOD USED BULK SOLVENT MODEL REMARK SOLVENT RADIUS REMARK SHRINKAGE RADIUS REMARK K_SOL

REMARK B SOL REMARK REMARK ERROR ESTIMATES.

REMARK COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) 0.250 REMARK PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) 22.460 REMARK REMARK B VALUES.

REMARK FROM WILSON PLOT (A**2) 37.00

REMARK MEAN B VALUE (OVERALL, A**2) 44.43

REMARK OVERALL ANISOTROPIC B VALUE.

REMARK Bll (A**2) NULL

REMARK B22 (A**2) NULL

REMARK B33 (A**2) NULL

REMARK B12 (A**2) NULL

REMARK B13 (A**2) NULL

REMARK B23 (A**2) NULL

REMARK REMARK TWINNING INFORMATION.

REMARK FRACTION: NULL

REMARK OPERATOR: NULL

REMARK REMARK DEVIATIONS FROM IDEAL VALUES REMARK RMSD COUNT REMARK BOND 006 3340

REMARK ANGLE 974 4534

REMARK CHIRALITY 063 486

REMARK PLANARITY 005 602

REMARK DIHEDRAL 12 96 1282

REMARK REMARK TLS DETAILS REMARK NUMBER OF TLS GROUPS REMARK TLS GROUP : 1 REMARK 3 SELECTION: CHAIN A AND (RESID 20: 118 )

REMARK 3 ORIGIN FOR THE GROUP (A) -44 4255 - 11 7844 22.3117

REMARK 3 T TENSOR

REMARK 3 Til 0 3346 T22 0 1939

REMARK 3 T33 0 2709 T12 0 0810

REMARK 3 T13 -0 0289 T23 -0 0287

REMARK 3 L TENSOR

REMARK 3 Lll 3 6848 L22 3 1058

REMARK 3 L33 3 0732 L12 -0 6131

REMARK 3 L13 0 1315 L23 0 1477

REMARK 3 S TENSOR

REMARK 3 Sll -0 2097 S12 -0 4670 S13 0 1060

REMARK 3 S21 0 4580 S22 0 2118 S23 -0 0168

REMARK 3 S31 0 0894 S32 0 0496 S33 0 0320

REMARK 3 TL£ GROUP : 2

REMARK 3 SELECTION: CHAIN A AND (RESID 119 231

REMARK 3 ORIGIN FOR THE GROUP (A) -25 7555 -6 0996 -12.8620

REMARK 3 T TENSOR

REMARK 3 Til 0 2986 T22 0 3588

REMARK 3 T33 0 3621 T12 -0 0411

REMARK 3 T13 0 0314 T23 -0 1219

REMARK 3 L TENSOR

REMARK 3 Lll 4 4625 L22 2 3215

REMARK 3 L33 6 1419 L12 0 9146

REMARK 3 L13 -4 0580 L23 -0 8104

REMARK 3 S TENSOR

REMARK 3 Sll 0 0852 S12 -0 1847 S13 -0 0007

REMARK 3 S21 -0 1855 S22 0 1172 S23 -0 4285

REMARK 3 S31 -0 2356 S32 0 8244 S33 -0 1302

REMARK 3 TL£ GROUP : 3

REMARK 3 SELECTION: CHAIN B AND (RESID 20: 118 )

REMARK 3 ORIGIN FOR THE GROUP (A) -32 4094 - 32 5805 17.7126

REMARK 3 T TENSOR

REMARK 3 Til 0 3066 T22 0 2220

REMARK 3 T33 0 2675 T12 0 0924

REMARK 3 T13 0 0200 T23 0 0084

REMARK 3 L TENSOR

REMARK 3 Lll 3 1428 L22 3 5962

REMARK 3 L33 2 4777 L12 -0 2641

REMARK 3 L13 -0 2974 L23 -0 0455

REMARK 3 S TENSOR

REMARK 3 Sll 0 1237 S12 0 3040 S13 -0 0959

REMARK 3 S21 -0 6026 S22 -0 1027 S23 -0 0478

REMARK 3 S31 -0 0892 S32 -0 0480 S33 -0 0109

REMARK 3 TL£ GROUP : 4

REMARK 3 SELECTION: CHAIN B AND (RESID 119 231

REMARK 3 ORIGIN FOR THE GROUP (A) -18 1587 - 19 2650 52.8930

REMARK 3 T TENSOR

REMARK 3 Til 0 3004 T22 0 3474

REMARK 3 T33 0 3383 T12 -0 0410

REMARK 3 T13 0 0821 T23 -0 0901

REMARK 3 L TENSOR

REMARK 3 Lll 3 4597 L22 2 7773

REMARK 3 L33 4 7269 L12 1 0117

REMARK 3 L13 1 8017 L23 2 1893

REMARK 3 S TENSOR

REMARK 3 Sll 0 0052 S12 -0 1663 S13 0 3429

REMARK 3 S21 -0 0582 S22 0 2251 S23 -0 1990

REMARK 3 S31 -0 5215 S32 0 5405 S33 -0 1130 REMARK 3

REMARK 3 NCS DETAILS

REMARK 3 NUMBER OF NCS GROUPS

REMARK 3 NCS GROUP : 1

REMARK 3 NCS OPERATOR : 1

REMARK 3 REFERENCE SELECTION CHAIN A AND (RESSEQ 20:231 )

REMARK 3 SELECTION CHAIN B AND (RESSEQ 20:231 )

REMARK 3 ATOM PAIRS NUMBER 1626

REMARK 3 RMSD 0.008

REMARK 3

REMARK 3 OTHER REFINEMENT REMARKS: NULL

REMARK 4

REMARK 4 4LP4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-ll

REMARK 100

REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-AUG-13.

REMARK 100 THE RCSB ID CODE IS RCSB080909.

REMARK 200

REMARK 200 EXPERIMENTAL DETAILS

REMARK 200 EXPERIMENT TYPE X-RAY DIFFRACTION

REMARK 200 DATE OF DATA COLLECTION 18-FEB-12

REMARK 200 TEMPERATURE (KELVIN) 100

REMARK 200 PH 7.5

REMARK 200 NUMBER OF CRYSTALS USED 1

REMARK 200

REMARK 200 SYNCHROTRON (Y/N) Y

REMARK 200 RADIATION SOURCE MAX II

REMARK 200 BEAMLINE 1911-2

REMARK 200 X-RAY GENERATOR MODEL NULL

REMARK 200 MONOCHROMATIC OR LAUE (M/L) M

REMARK 200 WAVELENGTH OR RANGE (A) 1.04

REMARK 200 MONOCHROMATOR SI (111)

REMARK 200 OPTICS NULL

REMARK 200

REMARK 200 DETECTOR TYPE CCD

REMARK 200 DETECTOR MANUFACTURER MAR CCD 165 MM

REMARK 200 INTENSITY-INTEGRATION SOFTWARE XDS

REMARK 200 DATA SCALING SOFTWARE XSCALE

REMARK 200

REMARK 200 NUMBER OF UNIQUE REFLECTIONS 23876

REMARK 200 RESOLUTION RANGE HIGH (A) 2.400

REMARK 200 RESOLUTION RANGE LOW (A) 35.000

REMARK 200 REJECTION CRITERIA (SIGMA(I)) 2.000

REMARK 200

REMARK 200 OVERALL .

REMARK 200 COMPLETENESS FOR RANGE (%) 99.7

REMARK 200 DATA REDUNDANCY 9.900

REMARK 200 R MERGE (I) 0.07500

REMARK 200 R SYM (I) NULL

REMARK 200 <I/SIGMA(I)> FOR THE DATA SET 22.7200

REMARK 200

REMARK 200 IN THE HIGHEST RESOLUTION SHELL.

REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) 2.40

REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) 2.50

REMARK 200 COMPLETENESS FOR SHELL (%)

REMARK 200 DATA REDUNDANCY IN SHELL

REMARK 200 R MERGE FOR SHELL (I)

REMARK 200 R SYM FOR SHELL (I)

REMARK 200 <I/SIGMA(I)> FOR SHELL

REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH

REMARK 2 00 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT

REMARK 2 00 SOFTWARE USED: PHASER

REMARK 2 00 STARTING MODEL: PDB ENTRY 303U

REMARK 2 00

REMARK 2 00 REMARK : NULL

REMARK 2 80

REMARK 2 80 CRYSTAL

REMARK 2 80 SOLVENT CONTENT, VS (%) : 63.35

REMARK 2 80 MATTHEWS COEFFICIENT, VM (ANGSTROMS* * 3/DA) : 3.36

REMARK 2 80

REMARK 2 80 CRYSTALLIZATION CONDITIONS: 2.5 M SODIUM ACETATE, PH 7.5, VAPOR

REMARK 2 80 DIFFUSION, HANGING DROP, TEMPERATURE 277K

REMARK 2 90

REMARK 2 90 CRYSTALLOGRAPHIC SYMMETRY

REMARK 2 90 SYMMETRY OPERATORS FOR SPACE GROUP: P 62

REMARK 2 90

REMARK 2 90 SYMOP SYMMETRY

REMARK 2 90 NNNMMM OPERATOR

REMARK 2 90 1555 Χ,Υ,Ζ

REMARK 2 90 2555 -Y,X-Y, Z+2/3

REMARK 2 90 3555 -X+Y, -X, Z+l/3

REMARK 2 90 4555 -X,-Y,Z

REMARK 2 90 5555 Y, -X+Y, Z+2/3

REMARK 2 90 6555 X-Y,X, Z+l/3

REMARK 2 90

REMARK 2 90 WHERE NNN -> OPERATOR NUMBER

REMARK 2 90 MMM -> TRANSLATION VECTOR

REMARK 2 90

REMARK 2 90 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS

REMARK 2 90 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM

REMARK 2 90 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY

REMARK 2 90 RELATED MOLECULES.

REMARK 2 90 SMTRY1 1 1. , 000000 0. , 000000 0. , 000000 0, , 00000

REMARK 2 90 SMTRY2 1 0. , 000000 1. , 000000 0. , 000000 0, , 00000

REMARK 2 90 SMTRY3 1 0. , 000000 0. , 000000 1. , 000000 0, , 00000

REMARK 2 90 SMTRY1 2 -0. , 500000 -0. ,866025 0. , 000000 0, , 00000

REMARK 2 90 SMTRY2 2 0. ,866025 -0. , 500000 0. , 000000 0, , 00000

REMARK 2 90 SMTRY3 2 0. , 000000 0. , 000000 1. , 000000 68 , , 93333

REMARK 2 90 SMTRY1 3 -0. , 500000 0. ,866025 0. , 000000 0, , 00000

REMARK 2 90 SMTRY2 3 -0. ,866025 -0. , 500000 0. , 000000 0, , 00000

REMARK 2 90 SMTRY3 3 0. , 000000 0. , 000000 1. , 000000 34 , ,46667

REMARK 2 90 SMTRY1 4 -1. , 000000 0. , 000000 0. , 000000 0, , 00000

REMARK 2 90 SMTRY2 4 0. , 000000 -1. , 000000 0. , 000000 0, , 00000

REMARK 2 90 SMTRY3 4 0. , 000000 0. , 000000 1. , 000000 0, , 00000

REMARK 2 90 SMTRY1 5 0. , 500000 0. ,866025 0. , 000000 0, , 00000

REMARK 2 90 SMTRY2 5 -0. ,866025 0. , 500000 0. , 000000 0, , 00000

REMARK 2 90 SMTRY3 5 0. , 000000 0. , 000000 1. , 000000 68 , , 93333

REMARK 2 90 SMTRY1 6 0. , 500000 -0. ,866025 0. , 000000 0, , 00000

REMARK 2 90 SMTRY2 6 0. ,866025 0. , 500000 0. , 000000 0, , 00000

REMARK 2 90 SMTRY3 6 0. , 000000 0. , 000000 1. , 000000 34 , ,46667

REMARK 2 90

REMARK 2 90 REMARK : NULL

REMARK 3 00

REMARK 3 00 BIOMOLECULE: 1, 2

REMARK 3 00 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM

REMARK 3 00 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN

REMARK 3 00 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON

REMARK 3 00 BURIED SURFACE AREA. REMARK 350

REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND

REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.

REMARK 350

REMARK 350 BIOMOLECULE: 1

REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC

REMARK 350 APPLY THE FOLLOWING TO CHAINS: A

REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 00000 REMARK 350

REMARK 350 BIOMOLECULE: 2

REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC

REMARK 350 APPLY THE FOLLOWING TO CHAINS: B

REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 00000 REMARK 500

REMARK 500 GEOMETRY AND STEREOCHEMISTRY

REMARK 500 SUBTOPIC: TORSION ANGLES

REMARK 500

REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;

REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE) .

REMARK 500

REMARK 500 STANDARD TABLE:

REMARK 500 FORMAT: ( 1 OX, I 3 , IX, A3 , IX, Al , I 4 , Al , 4X, F7.2 , 3X, F7.2 )

REMARK 500

REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996) . PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500

REMARK 500 M RES CSSEQI PSI PHI

REMARK 500 ALA A 60 -136.53 53.60

REMARK 500 PRO A 151 -179.37 -64.30

REMARK 500 ASN A 167 -3.88 76.17

REMARK 500 ALA B 60 -136.38 53.21

REMARK 500 PRO B 151 -179.44 -63.94

REMARK 500 ASN B 167 -3.64 75.81

REMARK 500

REMARK 500 REMARK : NULL

REMARK 800

REMARK 800 SITE

REMARK 800 SITE_IDENTIFIER: AC1

REMARK 800 EVIDENCE_CODE: SOFTWARE

REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 301

REMARK 800

REMARK 800 SITE_IDENTIFIER: AC2

REMARK 800 EVIDENCE_CODE: SOFTWARE

REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 301

REMARK 800

REMARK 800 SITE_IDENTIFIER: AC3

REMARK 800 EVIDENCE_CODE: SOFTWARE

REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 302

REMARK 800

REMARK 800 SITE_IDENTIFIER: AC4

REMARK 800 EVIDENCE CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION : BINDING SITE FOR RESIDUE NA B 303

REMARK 900

REMARK 900 RELATED ENTRIES

REMARK 900 RELATED ID: 4LP5 RELATED DB: PDB

DBREF 4LP4 A 23 231 UNP Q15109 RAGE HUMAN 23

DBREF 4LP4 B 23 231 UNP Q15109 RAGE HUMAN 23

SEQADV 4LP4 GLY A 20 UNP Q15109 EXPRESSION TAG

SEQADV 4LP4 ALA A 21 UNP Q15109 EXPRESSION TAG

SEQADV 4LP4 MET A 22 UNP Q15109 EXPRESSION TAG

SEQADV 4LP4 GLY B 20 UNP Q15109 EXPRESSION TAG

SEQADV 4LP4 ALA B 21 UNP Q15109 EXPRESSION TAG

SEQADV 4LP4 MET B 22 UNP Q15109 EXPRESSION TAG

SEQRES 1 A 212 GLY ALA MET ALA GLN ASN ILE THR ALA ARG ILE GLY GLU

SEQRES 2 A 212 PRO LEU VAL LEU LYS CYS LYS GLY ALA PRO LYS LYS PRO

SEQRES 3 A 212 PRO GLN ARG LEU GLU TRP LYS LEU ASN THR GLY ARG THR

SEQRES 4 A 212 GLU ALA TRP LYS VAL LEU SER PRO GLN GLY GLY GLY PRO

SEQRES 5 A 212 TRP ASP SER VAL ALA ARG VAL LEU PRO ASN GLY SER LEU

SEQRES 6 A 212 PHE LEU PRO ALA VAL GLY ILE GLN ASP GLU GLY ILE PHE

SEQRES 7 A 212 ARG CYS GLN ALA MET ASN ARG ASN GLY LYS GLU THR LYS

SEQRES 8 A 212 SER ASN TYR ARG VAL ARG VAL TYR GLN ILE PRO GLY LYS

SEQRES 9 A 212 PRO GLU ILE VAL ASP SER ALA SER GLU LEU THR ALA GLY

SEQRES 10 A 212 VAL PRO ASN LYS VAL GLY THR CYS VAL SER GLU GLY SER

SEQRES 11 A 212 TYR PRO ALA GLY THR LEU SER TRP HIS LEU ASP GLY LYS

SEQRES 12 A 212 PRO LEU VAL PRO ASN GLU LYS GLY VAL SER VAL LYS GLU

SEQRES 13 A 212 GLN THR ARG ARG HIS PRO GLU THR GLY LEU PHE THR LEU

SEQRES 14 A 212 GLN SER GLU LEU MET VAL THR PRO ALA ARG GLY GLY ASP

SEQRES 15 A 212 PRO ARG PRO THR PHE SER CYS SER PHE SER PRO GLY LEU

SEQRES 16 A 212 PRO ARG HIS ARG ALA LEU ARG THR ALA PRO ILE GLN PRO

SEQRES 17 A 212 ARG VAL TRP GLU

SEQRES 1 B 212 GLY ALA MET ALA GLN ASN ILE THR ALA ARG ILE GLY GLU

SEQRES 2 B 212 PRO LEU VAL LEU LYS CYS LYS GLY ALA PRO LYS LYS PRO

SEQRES 3 B 212 PRO GLN ARG LEU GLU TRP LYS LEU ASN THR GLY ARG THR

SEQRES 4 B 212 GLU ALA TRP LYS VAL LEU SER PRO GLN GLY GLY GLY PRO

SEQRES 5 B 212 TRP ASP SER VAL ALA ARG VAL LEU PRO ASN GLY SER LEU

SEQRES 6 B 212 PHE LEU PRO ALA VAL GLY ILE GLN ASP GLU GLY ILE PHE

SEQRES 7 B 212 ARG CYS GLN ALA MET ASN ARG ASN GLY LYS GLU THR LYS

SEQRES 8 B 212 SER ASN TYR ARG VAL ARG VAL TYR GLN ILE PRO GLY LYS

SEQRES 9 B 212 PRO GLU ILE VAL ASP SER ALA SER GLU LEU THR ALA GLY

SEQRES 10 B 212 VAL PRO ASN LYS VAL GLY THR CYS VAL SER GLU GLY SER

SEQRES 11 B 212 TYR PRO ALA GLY THR LEU SER TRP HIS LEU ASP GLY LYS

SEQRES 12 B 212 PRO LEU VAL PRO ASN GLU LYS GLY VAL SER VAL LYS GLU

SEQRES 13 B 212 GLN THR ARG ARG HIS PRO GLU THR GLY LEU PHE THR LEU

SEQRES 14 B 212 GLN SER GLU LEU MET VAL THR PRO ALA ARG GLY GLY ASP

SEQRES 15 B 212 PRO ARG PRO THR PHE SER CYS SER PHE SER PRO GLY LEU

SEQRES 16 B 212 PRO ARG HIS ARG ALA LEU ARG THR ALA PRO ILE GLN PRO

SEQRES 17 B 212 ARG VAL TRP GLU

HET NA A . 301 1

HET NA B 301 1

HET NA B 302 1

HET NA B 303 1

HETNAM NA SODIUM ION

FORMUL 3 NA 4 (NA 1+)

FORMUL 7 HOH 245(H2 O)

HELIX 1 1 GLY A 70 VAL A 75 5

HELIX 2 2 GLY A 90 ASP A 93 5

HELIX 3 3 GLY B 70 VAL B 75 5

HELIX 4 4 GLY B 90 ASP B 93 5

SHEET 1 A 5 GLN A 24 ARG A 29 0

SHEET 2 A 5 GLU A 108 TYR A 118 1 O ARG A 114 N ILE A 26 SHEET 3 A 5 GLY A 95 MET A 102 -1 N GLY A 95 O VAL A 115

SHEET 4 A 5 ARG A 48 THR A 55 -1 N LYS A 52 O ARG A 98

SHEET 5 A 5 LYS A 62 LEU A 64 -1 O LEU A 64 N TRP A 51

SHEET 1 B 3 LEU A 34 LEU A 36 0

SHEET 2 B 3 LEU A 84 LEU A 86 -1 O LEU A 86 N LEU A 34

SHEET 3 B 3 ARG A 77 VAL A 78 -1 N ARG A 77 O PHE A 85

SHEET 1 C 4 GLU A 125 VAL A 127 0

SHEET 2 C 4 ASN A 139 SER A 149 -1 O THR A 143 N VAL A 127

SHEET 3 C 4 PHE A 186 VAL A 194 -1 O LEU A 192 N VAL A 141

SHEET 4 C 4 VAL A 171 ARG A 179 -1 N LYS A 174 O GLU A 191

SHEET 1 D 2 GLU A 132 THR A 134 0

SHEET 2 D 2 ARG A 228 TRP A 230 1 O TRP A 230 N LEU A 133

SHEET 1 E 4 LYS A 162 LEU A 164 0

SHEET 2 E 4 THR A 154 LEU A 159 -1 N LEU A 159 O LYS A 162

SHEET 3 E 4 PHE A 206 SER A 211 -1 O SER A 207 N HIS A 158

SHEET 4 E 4 LEU A 220 ARG A 221 -1 O LEU A 220 N PHE A 210

SHEET 1 F 5 GLN B 24 ARG B 29 0

SHEET 2 F 5 GLU B 108 TYR B 118 1 O ARG B 114 N ILE B 26

SHEET 3 F 5 GLY B 95 MET B 102 -1 N GLY B 95 O VAL B 115

SHEET 4 F 5 ARG B 48 THR B 55 -1 N LYS B 52 O ARG B 98

SHEET 5 F 5 LYS B 62 LEU B 64 -1 O LEU B 64 N TRP B 51

SHEET 1 G 3 LEU B 34 LEU B 36 0

SHEET 2 G 3 LEU B 84 LEU B 86 -1 O LEU B 86 N LEU B 34

SHEET 3 G 3 ARG B 77 VAL B 78 -1 N ARG B 77 O PHE B 85

SHEET 1 H 4 GLU B 125 VAL B 127 0

SHEET 2 H 4 ASN B 139 SER B 149 -1 O THR B 143 N VAL B 127

SHEET 3 H 4 PHE B 186 VAL B 194 -1 O LEU B 192 N VAL B 141

SHEET 4 H 4 VAL B 171 ARG B 179 -1 N LYS B 174 O GLU B 191

SHEET 1 I 2 GLU B 132 THR B 134 0

SHEET 2 I 2 ARG B 228 TRP B 230 1 O TRP B 230 N LEU B 133

SHEET 1 J 4 LYS B 162 LEU B 164 0

SHEET 2 J 4 THR B 154 LEU B 159 -1 N LEU B 159 O LYS B 162

SHEET 3 J 4 PHE B 206 SER B 211 -1 O SER B 207 N HIS B 158

SHEET 4 J 4 LEU B 220 ARG B 221 -1 O LEU B 220 N PHE B 210

SSBOND 1 CYS A 38 ) CYS 1 A 99 1555 1555 2 , , 06

SSBOND 2 CYS A 144 CYS 1 A 20 8 1555 1555 2 , , 04

SSBOND 3 CYS B 38 ) CYS 1 B 99 1555 1555 2 , , 06

SSBOND 4 CYS B 144 CYS 1 B 20 8 1555 1555 2 , , 04

LINK NA NA B 301 O HOH B 4 89 1555 1555 3, , 01

LINK NA NA A 301 O HOH A 401 1555 1555 3, , 08

LINK NA NA B 303 O HOH B 401 1555 1555 3, , 11

CISPEP 1 PRO A 45 PRO A 46 0 0, .77

CISPEP 2 TYR A 150 PRO A 151 0 - 11, .05

CISPEP 3 PRO B 45 PRO B 46 0 0, .76

CISPEP 4 TYR B 150 PRO B 151 0 - 11, .28

SITE 1 AC1 3 ALA A 21 ILE A . 96 HOH . A 401

SITE 1 AC 2 3 GLU A 59 ARG B 179 HOH B 48!

SITE 1 AC 3 2 ARG A 179 GLU B 59

SITE 1 AC 4 2 ALA E i 21 ILE B 96

CRYST1 102 ! .000 102. 000 103.400 90. 00 90 .00 : I2C I.00 P 62 12

ORIGXl 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

SCALE 1 0.009804 0, , 005660 0.000000 0. 00000

SCALE2 0.000000 0, , 011321 0.000000 0. 00000

SCALE3 0.000000 0, , 000000 0.009671 0. 00000

ATOM 1 N GLY A 20 -43.410 5, , 450 17 .529 1. ,00 35. , 07

ANISOU 1 N GLY A 20 5059 1799 6466 146 -763

ATOM 2 CA GLY A 20 -43.645 4 , , 374 18 .478 1. ,00 35. ,46 ANISOU 2 CA GLY A 20 5087 2049 6337 252 -773 -766

ATOM 3 C GLY A 20 -42.796 4.534 19.725 1.00 36.84

ANISOU 3 C GLY A 20 5258 2240 6501 219 -860 -1014

ATOM 4 O GLY A 20 -42.143 5.560 19.922 1.00 39.23

ANISOU 4 O GLY A 20 5571 2386 6947 119 -916 -1093

ATOM 5 N ALA A 21 -42.803 3.521 20.580 1.00 37.52

ANISOU 5 N ALA A 21 5333 2515 6408 304 -879 -1137

ATOM 6 CA ALA A 21 -41.994 3.571 21.793 1.00 41.31

ANISOU 6 CA ALA A 21 5813 3050 6834 293 -984 -1374

ATOM 7 C ALA A 21 -40.606 2.995 21.524 1.00 38.94

ANISOU 7 C ALA A 21 5407 2809 6579 141 -1061 -1364

ATOM 8 O ALA A 21 -40.368 2.398 20.476 1.00 35.96

ANISOU 8 O ALA A 21 4967 2449 6246 67 -1011 -1182

ATOM 9 CB ALA A 21 -42. 683 2.818 22.924 1.00 40.16

ANISOU 9 CB ALA A 21 5722 3087 6449 477 -968 -1506

ATOM 10 N MET A 22 -39.697 3.189 22.470 1.00 35.64

ANISOU 10 N MET A 22 4959 2430 6151 99 -1186 -1567

ATOM 11 CA MET A 22 -38. 380 2.579 22.414 1.00 35.55

ANISOU 11 CA MET A 22 4820 2515 6173 -19 -1280 -1596

ATOM 12 C MET A 22 -38. 509 1.064 22.410 1.00 39.66

ANISOU 12 C MET A 22 5332 3229 6507 88 -1259 -1546

ATOM 13 O MET A 22 -39. 216 0.487 23.234 1.00 35.63

ANISOU 13 O MET A 22 4917 2843 5777 263 -1249 -1619

ATOM 14 CB MET A 22 -37.526 3.045 23.594 1.00 38.08

ANISOU 14 CB MET A 22 5113 2878 6479 -48 -1440 -1844

ATOM 15 CG MET A 22 -36.884 4.408 23.380 1.00 40.88

ANISOU 15 CG MET A 22 5423 3028 7083 -230 -1482 -1881

ATOM 16 SD MET A 22 -35.433 4.265 22.310 1.00 41.21

ANISOU 16 SD MET A 22 5244 3058 7357 -486 -1493 -1744

ATOM 17 CE MET A 22 -34.882 5.962 22.259 1.00 45.09

ANISOU 17 CE MET A 22 5726 3290 8116 -684 -1527 -1797

ATOM 18 N ALA A 23 -37.841 0.422 21.461 1.00 31.99

ANISOU 18 N ALA A 23 4240 2333 5582 -13 -1207 -1372

ATOM 19 CA ALA A 23 -37.972 -1.015 21.313 1.00 29.92

ANISOU 19 CA ALA A 23 3961 2301 5107 88 -1127 -1246

ATOM 20 C ALA A 23 -36. 633 -1.648 20.998 1.00 30.05

ANISOU 20 C ALA A 23 3810 2456 5153 1 -1160 -1207

ATOM 21 O ALA A 23 -35. 717 -0.989 20.527 1.00 33.55

ANISOU 21 O ALA A 23 4126 2822 5800 -168 -1193 -1210

ATOM 22 CB ALA A 23 -38.990 -1.349 20.220 1.00 27.99

ANISOU 22 CB ALA A 23 3766 2027 4841 114 -966 -1026

ATOM 23 N GLN A 24 -36.519 -2.934 21.275 1.00 30.32

ANISOU 23 N GLN A 24 3836 2691 4995 120 -1144 -1166

ATOM 24 CA GLN A 24 -35. 381 -3.681 20.792 1.00 33.01

ANISOU 24 CA GLN A 24 4013 3166 5362 76 -1142 -1101

ATOM 25 C GLN A 24 -35. 699 -4.138 19.383 1.00 31.34

ANISOU 25 C GLN A 24 3790 2946 5172 35 -965 -891

ATOM 26 O GLN A 24 -36. 788 -4.660 19.121 1.00 25.74

ANISOU 26 O GLN A 24 3205 2231 4342 122 -872 -798

ATOM 27 CB GLN A 24 -35.092 -4.882 21.680 1.00 38.54

ANISOU 27 CB GLN A 24 4723 4063 5859 243 -1210 -1140

ATOM 28 CG GLN A 24 -33.975 -5.748 21.144 1.00 45.93

ANISOU 28 CG GLN A 24 5489 5135 6829 239 -1198 -1070

ATOM 29 CD GLN A 24 -33.617 -6.867 22.085 1.00 54.22

ANISOU 29 CD GLN A 24 6552 6353 7697 420 -1292 -1102

ATOM 30 OE1 GLN A 24 -33.936 -6.819 23.277 1.00 60.83

ANISOU 30 OE1 GLN A 24 7499 7229 8385 522 -1402 -1203

ATOM 31 NE2 GLN A 24 -32.948 -7.887 21.560 1.00 51.44

ANISOU 31 NE2 GLN A 24 6096 6103 7346 477 -1245 -1012 ATOM 32 N ASN A 25 -34.754 -3.914 18.476 1.00 33.17

ANISOU 32 N ASN A 25 3865 3184 5553 -103 -920 -822

ATOM 33 CA ASN A 25 -34.904 -4.309 17.084 1.00 38.26

ANISOU 33 CA ASN A 25 4494 3848 6193 -144 -753 -636

ATOM 34 C ASN A 25 -34.615 -5.799 16.904 1.00 38.47

ANISOU 34 C ASN A 25 4489 4053 6074 -19 -700 -599

ATOM 35 O ASN A 25 -33.581 -6.300 17.340 1.00 44.63

ANISOU 35 O ASN A 25 5137 4955 6865 20 -765 -670

ATOM 36 CB ASN A 25 -33. 972 -3.474 16.211 1.00 50.22

ANISOU 36 CB ASN A 25 5854 5317 7910 -340 -699 -568

ATOM 37 CG ASN A 25 -34.158 -3.745 14.737 1.00 60.50

ANISOU 37 CG ASN A 25 7162 6651 9173 -382 -518 -371

ATOM 38 OD1 ASN A 25 -35.234 -3.504 14.183 1.00 65.38

ANISOU 38 OD1 ASN A 25 7928 7179 9736 -366 -461 -267

ATOM 39 ND2 ASN A 25 -33.104 -4.237 14.083 1.00 61.11

ANISOU 39 ND2 ASN A 25 7071 6875 9272 -424 -431 -325

ATOM 40 N ILE A 26 -35.551 -6.512 16.298 1.00 31.17

ANISOU 40 N ILE A 26 3686 3134 5023 53 -598 -498

ATOM 41 CA ILE A 26 -35. 373 -7.931 16.029 1.00 28.51

ANISOU 41 CA ILE A 26 3346 2919 4568 168 -541 -468

ATOM 42 C ILE A 26 -35.510 -8.174 14.526 1.00 29.70

ANISOU 42 C ILE A 26 3495 3091 4699 114 -392 -348

ATOM 43 O ILE A 26 -36.497 -7.763 13.906 1.00 28.10

ANISOU 43 O ILE A 26 3396 2811 4469 70 -343 -267

ATOM 44 CB ILE A 26 -36. 442 -8.781 16.750 1.00 27.11

ANISOU 44 CB ILE A 26 3334 2729 4239 306 -562 -476

ATOM 45 CGI ILE A 26 -36.338 -8.641 18.274 1.00 28.59

ANISOU 45 CGI ILE A 26 3548 2930 4385 385 -698 -586

ATOM 46 CG2 ILE A 26 -36.340 -10.235 16.320 1.00 29.22

ANISOU 46 CG2 ILE A 26 3619 3066 4415 406 -494 -434

ATOM 47 CD1 ILE A 26 -35.017 -9.134 18.873 1.00 24.48

ANISOU 47 CD1 ILE A 26 2899 2529 3872 451 -796 -658

ATOM 48 N THR A 27 -34.512 -8.813 13.934 1.00 32.43

ANISOU 48 N THR A 27 3717 3554 5050 131 -323 -342

ATOM 49 CA THR A 27 -34.608 -9.228 12.538 1.00 34.82

ANISOU 49 CA THR A 27 4035 3911 5284 112 -175 -255

ATOM 50 C THR A 27 -34.707 -10.746 12.510 1.00 35.45

ANISOU 50 C THR A 27 4174 4048 5247 270 -151 -300

ATOM 51 O THR A 27 -33.818 -11.445 12.986 1.00 38.13

ANISOU 51 O THR A 27 4418 4459 5610 369 -179 -367

ATOM 52 CB THR A 27 -33.394 -8.785 11.704 1.00 36.62

ANISOU 52 CB THR A 27 4074 4238 5601 11 -71 -213

ATOM 53 OG1 THR A 27 -32. 255 -9.564 12.080 1.00 39.98

ANISOU 53 OG1 THR A 27 4341 4787 6064 105 -82 -302

ATOM 54 CG2 THR A 27 -33.097 -7.302 11.916 1.00 31.66

ANISOU 54 CG2 THR A 27 3367 3521 5142 -162 -111 -178

ATOM 55 N ALA A 28 -35.809 -11.248 11.971 1.00 32.15

ANISOU 55 N ALA A 28 3911 3585 4718 293 -112 -264

ATOM 56 CA ALA A 28 -36.089 -12.670 11.990 1.00 30.06

ANISOU 56 CA ALA A 28 3734 3320 4367 421 -100 -311

ATOM 57 C ALA A 28 -36.194 -13.182 10.560 1.00 28.08

ANISOU 57 C ALA A 28 3519 3127 4024 415 16 -302

ATOM 58 O ALA A 28 -36. 842 -12.565 9.727 1.00 24.61

ANISOU 58 O ALA A 28 3130 2689 3531 321 51 -234

ATOM 59 CB ALA A 28 -37. 390 -12.937 12.749 1.00 27.56

ANISOU 59 CB ALA A 28 3568 2894 4008 447 -170 -303

ATOM 60 N ARG A 29 -35.567 -14.318 10.285 1.00 27.71

ANISOU 60 N ARG A 29 3453 3126 3948 530 68 -376

ATOM 61 CA ARG A 29 -35. 575 -14.875 8.943 1.00 26.64 ANISOU 61 CA ARG A 29 3359 3059 3704 544 180 407

ATOM 62 C ARG A 29 -36.827 -15. .710 8. .719 1. , 00 29. ,28

ANISOU 62 C ARG A 29 3878 3292 3955 562 143 443

ATOM 63 O ARG A 29 -37.182 -16. .553 9. .555 1. , 00 30. , 47

ANISOU 63 O ARG A 29 4102 3327 4147 636 78 481

ATOM 64 CB ARG A 29 -34.324 -15. .716 8. .729 1. , 00 27. ,81

ANISOU 64 CB ARG A 29 3398 3296 3873 678 260 498

ATOM 65 CG ARG A 29 -34.151 -16. .256 7. .333 1. , 00 30. , 13

ANISOU 65 CG ARG A 29 3722 3688 4037 714 397 560

ATOM 66 CD ARG A 29 -32.743 -16. .805 7. .172 1. , 00 33. , 58

ANISOU 66 CD ARG A 29 3994 4242 4523 850 498 642

ATOM 67 NE ARG A 29 -32.544 -17. .405 5. .861 1. , 00 40. , 83

ANISOU 67 NE ARG A 29 4950 5266 5298 913 647 731

ATOM 68 CZ ARG A 29 -31.398 -17. .933 5. .441 1. , 00 45. ,86

ANISOU 68 CZ ARG A 29 5450 6031 5945 1049 776 823

ATOM 69 NH1 ARG A 29 -30.334 -17. .948 6. .232 1. , 00 46. , 33

ANISOU 69 NH1 ARG A 29 5305 6130 6170 1134 759 827

ATOM 70 NH2 ARG A 29 -31.321 -18. .453 4. .226 1. , 00 48. , 36

ANISOU 70 NH2 ARG A 29 5827 6450 6099 1112 918 922

ATOM 71 N ILE A 30 -37.495 -15. .452 7. .596 1. , 00 25. , 17

ANISOU 71 N ILE A 30 3427 2817 3318 485 180 422

ATOM 72 CA ILE A 30 -38.702 -16. .174 7. .195 1. , 00 23. , 66

ANISOU 72 CA ILE A 30 3386 2553 3051 475 132 472

ATOM 73 C ILE A 30 -38.491 -17. .696 7. .183 1. , 00 25. ,78

ANISOU 73 C ILE A 30 3726 2749 3322 592 147 613

ATOM 74 O ILE A 30 -37.493 -18. .186 6. .657 1. , 00 25. , 56

ANISOU 74 O ILE A 30 3654 2795 3262 686 238 696

ATOM 75 CB ILE A 30 -39.169 -15. .704 5. .801 1. , 00 24. , 14

ANISOU 75 CB ILE A 30 3493 2727 2951 400 166 444

ATOM 76 CGI ILE A 30 -39.688 -14. .269 5. .873 1. , 00 26. , 14

ANISOU 76 CGI ILE A 30 3715 2990 3225 292 123 285

ATOM 77 CG2 ILE A 30 -40.232 -16. .642 5. .227 1. , 00 24. , 50

ANISOU 77 CG2 ILE A 30 3673 2725 2909 397 106 546

ATOM 78 CD1 ILE A 30 -39.706 -13. .558 4. .522 1. , 00 27. ,81

ANISOU 78 CD1 ILE A 30 3946 3343 3279 234 180 200

ATOM 79 N GLY A 31 -39.428 -18. .437 7. .775 1. , 00 25. , 01

ANISOU 79 N GLY A 31 3731 2496 3277 588 69 637

ATOM 80 CA GLY A 31 -39.316 -19. .885 7. .839 1. , 00 25. ,88

ANISOU 80 CA GLY A 31 3930 2479 3423 687 74 756

ATOM 81 C GLY A 31 -38.625 -20. .395 9. .097 1. , 00 28. , 64

ANISOU 81 C GLY A 31 4253 2731 3896 808 58 727

ATOM 82 O GLY A 31 -38.727 -21. .577 9. .448 1. , 00 29. , 61

ANISOU 82 O GLY A 31 4474 2691 4085 886 42 778

ATOM 83 N GLU A 32 -37.920 -19. .508 9. .787 1. , 00 26. , 16

ANISOU 83 N GLU A 32 3814 2507 3618 822 51 642

ATOM 84 CA GLU A 32 -37.218 -19. .899 11. .005 1. , 00 32. , 16

ANISOU 84 CA GLU A 32 4539 3212 4468 947 9 610

ATOM 85 C GLU A 32 -37.998 -19. .553 12. .279 1. , 00 32. , 36

ANISOU 85 C GLU A 32 4611 3163 4520 897 -74 501

ATOM 86 O GLU A 32 -38.759 -18. .589 12. .305 1. , 00 31. , 47

ANISOU 86 O GLU A 32 4489 3088 4381 771 -93 447

ATOM 87 CB GLU A 32 -35.822 -19. .280 11. .039 1. , 00 34. , 17

ANISOU 87 CB GLU A 32 4607 3626 4750 1011 36 615

ATOM 88 CG GLU A 32 -34.829 -20. .004 10. .145 1. , 00 43. , 73

ANISOU 88 CG GLU A 32 5760 4900 5957 1138 132 728

ATOM 89 CD GLU A 32 -33.421 -19. .497 10. .335 1. , 00 52. , 95

ANISOU 89 CD GLU A 32 6703 6228 7186 1207 158 727

ATOM 90 OE1 GLU A 32 -33.161 -18. .819 11. .354 1. , 00 54. ,23

ANISOU 90 OE1 GLU A 32 6778 6418 7410 1182 66 655 ATOM 91 OE2 GLU A 32 -32.575 -19.768 9.459 1.00 59.59

ANISOU 91 OE2 GLU A 32 7447 7181 8014 1285 272 -810

ATOM 92 N PRO A 33 -37.812 -20.351 13.339 1.00 30.95

ANISOU 92 N PRO A 33 4489 2883 4388 1012 -118 -464

ATOM 93 CA PRO A 33 -38.518 -20.075 14.590 1.00 27.04

ANISOU 93 CA PRO A 33 4048 2344 3884 981 -176 -358

ATOM 94 C PRO A 33 -38.029 -18.783 15.219 1.00 25.91

ANISOU 94 C PRO A 33 3783 2342 3721 961 -230 -333

ATOM 95 O PRO A 33 -36.913 -18.345 14.956 1.00 24.59

ANISOU 95 O PRO A 33 3480 2285 3578 1000 -237 -381

ATOM 96 CB PRO A 33 -38.126 -21.261 15.481 1.00 28.06

ANISOU 96 CB PRO A 33 4262 2354 4045 1140 -206 -312

ATOM 97 CG PRO A 33 -36.801 -21.709 14.936 1.00 32.38

ANISOU 97 CG PRO A 33 4723 2945 4635 1286 -196 -400

ATOM 98 CD PRO A 33 -36.921 -21.522 13.452 1.00 31.86

ANISOU 98 CD PRO A 33 4624 2925 4555 1195 -113 -509

ATOM 99 N LEU A 34 -38.866 -18.185 16.054 1.00 26.48

ANISOU 99 N LEU A 34 3896 2406 3758 898 -262 -270

ATOM 100 CA LEU A 34 -38.498 -16.983 16.777 1.00 27.79

ANISOU 100 CA LEU A 34 3976 2675 3908 883 -327 -272

ATOM 101 C LEU A 34 -38.994 -17.088 18.216 1.00 32.34

ANISOU 101 C LEU A 34 4642 3231 4415 939 -374 -209

ATOM 102 O LEU A 34 -40.158 -17.402 18.457 1.00 31.72

ANISOU 102 O LEU A 34 4666 3080 4308 895 -324 -148

ATOM 103 CB LEU A 34 -39.094 -15.744 16.102 1.00 23.38

ANISOU 103 CB LEU A 34 3370 2149 3364 735 -302 -284

ATOM 104 CG LEU A 34 -38.873 -14.424 16.851 1.00 26.85

ANISOU 104 CG LEU A 34 3743 2647 3813 703 -371 -303

ATOM 105 CD1 LEU A 34 -37.378 -14.098 16.958 1.00 25.44

ANISOU 105 CD1 LEU A 34 3423 2557 3685 740 -429 -360

ATOM 106 CD2 LEU A 34 -39.635 -13.273 16.192 1.00 19.37

ANISOU 106 CD2 LEU A 34 2780 1683 2897 575 -344 -292

ATOM 107 N VAL A 35 -38.096 -16.841 19.165 1.00 33.36

ANISOU 107 N VAL A 35 4723 3442 4509 1037 -469 -226

ATOM 108 CA VAL A 35 -38.444 -16.809 20.578 1.00 29.84

ANISOU 108 CA VAL A 35 4366 3021 3952 1105 -522 -176

ATOM 109 C VAL A 35 -38.207 -15.396 21.103 1.00 28.41

ANISOU 109 C VAL A 35 4105 2943 3748 1061 -604 -264

ATOM 110 O VAL A 35 -37.114 -14.849 20.963 1.00 29.37

ANISOU 110 O VAL A 35 4091 3139 3930 1062 -687 -347

ATOM 111 CB VAL A 35 -37.584 -17.813 21.400 1.00 24.52

ANISOU 111 CB VAL A 35 3731 2362 3223 1289 -600 -122

ATOM 112 CGI VAL A 35 -37.936 -17.738 22.894 1.00 25.63

ANISOU 112 CGI VAL A 35 3982 2561 3197 1368 -655 -58

ATOM 113 CG2 VAL A 35 -37.755 -19.234 20.875 1.00 24.94

ANISOU 113 CG2 VAL A 35 3878 2268 3331 1342 -522 -45

ATOM 114 N LEU A 36 -39.236 -14.797 21.692 1.00 28.51

ANISOU 114 N LEU A 36 4191 2951 3690 1018 -577 -257

ATOM 115 CA LEU A 36 -39.117 -13.461 22.275 1.00 26.46

ANISOU 115 CA LEU A 36 3886 2757 3411 988 -656 -365

ATOM 116 C LEU A 36 -39.238 -13.568 23.786 1.00 28.42

ANISOU 116 C LEU A 36 4236 3086 3475 1108 -717 -363

ATOM 117 O LEU A 36 -40.188 -14.164 24.292 1.00 27.78

ANISOU 117 O LEU A 36 4278 2988 3289 1146 -625 -263

ATOM 118 CB LEU A 36 -40.204 -12.533 21.721 1.00 23.25

ANISOU 118 CB LEU A 36 3481 2287 3067 868 -577 -383

ATOM 119 CG LEU A 36 -40.145 -12.223 20.219 1.00 24.48

ANISOU 119 CG LEU A 36 3550 2383 3369 749 -527 -375

ATOM 120 CD1 LEU A 36 -41.314 -11.340 19.801 1.00 22.86 ANISOU 120 CD1 LEU A 36 3359 2118 3209 665 -470 -370

ATOM 121 CD2 LEU A 36 -38.819 -11.553 19.838 1.00 25.32

ANISOU 121 CD2 LEU A 36 3521 2526 3572 706 -606 -451

ATOM 122 N LYS A 37 -38.267 -13.017 24.507 1.00 31.49

ANISOU 122 N LYS A 37 4570 3574 3819 1163 -870 -472

ATOM 123 CA LYS A 37 -38.265 -13.109 25.958 1.00 34.86

ANISOU 123 CA LYS A 37 5102 4112 4030 1295 -952 -485

ATOM 124 C LYS A 37 -39.261 -12.134 26.564 1.00 33.14

ANISOU 124 C LYS A 37 4960 3907 3723 1266 -908 -567

ATOM 125 O LYS A 37 -39.408 -11.009 26.091 1.00 34.47

ANISOU 125 O LYS A 37 5058 4018 4021 1160 -913 -686

ATOM 126 CB LYS A 37 -36.877 -12.803 26.514 1.00 46.77

ANISOU 126 CB LYS A 37 6510 5742 5518 1363 -1164 -604

ATOM 127 CG LYS A 37 -35.787 -13.752 26.062 1.00 55.16

ANISOU 127 CG LYS A 37 7473 6821 6663 1435 -1222 -537

ATOM 128 CD LYS A 37 -34.408 -13.187 26.393 1.00 60.41

ANISOU 128 CD LYS A 37 7965 7613 7376 1457 -1435 -685

ATOM 129 CE LYS A 37 -33.304 -14.171 26.054 1.00 62.29

ANISOU 129 CE LYS A 37 8082 7894 7691 1569 -1494 -621

ATOM 130 NZ LYS A 37 -33.332 -15.340 26.974 1.00 65.54

ANISOU 130 NZ LYS A 37 8646 8351 7906 1783 -1542 -480

ATOM 131 N CYS A 38 -39.951 -12.576 27.608 1.00 34.49

ANISOU 131 N CYS A 38 5279 4151 3676 1371 -852 -495

ATOM 132 CA CYS A 38 -40.756 -11.677 28.424 1.00 38.46

ANISOU 132 CA CYS A 38 5857 4711 4047 1392 -818 -601

ATOM 133 C CYS A 38 -39.968 -11.358 29.692 1.00 41.75

ANISOU 133 C CYS A 38 6326 5290 4247 1519 -999 -730

ATOM 134 O CYS A 38 -39.912 -12.166 30.621 1.00 43.20

ANISOU 134 O CYS A 38 6628 5592 4194 1656 -1010 -623

ATOM 135 CB CYS A 38 -42.104 -12.313 28.778 1.00 38.30

ANISOU 135 CB CYS A 38 5951 4695 3906 1422 -611 -443

ATOM 136 SG CYS A 38 -43.204 -11.241 29.750 1.00 52.02

ANISOU 136 SG CYS A 38 7764 6524 5479 1475 -522 -578

ATOM 137 N LYS A 39 -39.338 -10.191 29.718 1.00 43.79

ANISOU 137 N LYS A 39 6500 5550 4589 1469 -1152 -955

ATOM 138 CA LYS A 39 -38.506 -9.804 30.852 1.00 46.82

ANISOU 138 CA LYS A 39 6912 6091 4787 1570 -1366 -1123

ATOM 139 C LYS A 39 -39.342 -9.616 32.116 1.00 46.93

ANISOU 139 C LYS A 39 7109 6236 4487 1699 -1311 -1174

ATOM 140 O LYS A 39 -40.495 -9.179 32.050 1.00 45.57

ANISOU 140 O LYS A 39 6990 6004 4320 1674 -1134 -1186

ATOM 141 CB LYS A 39 -37.737 -8.519 30.535 1.00 51.25

ANISOU 141 CB LYS A 39 7332 6588 5552 1448 -1532 -1371

ATOM 142 CG LYS A 39 -36.876 -8.607 29.276 1.00 54.16

ANISOU 142 CG LYS A 39 7504 6852 6224 1311 -1561 -1320

ATOM 143 CD LYS A 39 -36.213 -7.272 28.953 1.00 57.11

ANISOU 143 CD LYS A 39 7740 7139 6821 1160 -1692 -1538

ATOM 144 CE LYS A 39 -37.255 -6.170 28.782 1.00 59.31

ANISOU 144 CE LYS A 39 8093 7262 7179 1086 -1586 -1634

ATOM 145 NZ LYS A 39 -36.684 -4.885 28.264 1.00 61.29

ANISOU 145 NZ LYS A 39 8221 7360 7705 912 -1683 -1801

ATOM 146 N GLY A 40 -38.764 -9.964 33.264 1.00 46.11

ANISOU 146 N GLY A 40 7096 6327 4096 1852 -1461 -1200

ATOM 147 CA GLY A 40 -39.408 -9.727 34.545 1.00 49.76

ANISOU 147 CA GLY A 40 7741 6957 4209 1991 -1426 -1273

ATOM 148 C GLY A 40 -40.550 -10.669 34.891 1.00 53.36

ANISOU 148 C GLY A 40 8343 7460 4470 2069 -1162 -1009

ATOM 149 O GLY A 40 -41.373 -10.360 35.750 1.00 56.19

ANISOU 149 O GLY A 40 8833 7937 4579 2157 -1047 -1060 ATOM 150 N ALA A 41 -40.614 -11.813 34.217 1.00 53.29

ANISOU 150 N ALA A 41 8309 7354 4585 2032 -1057 -735

ATOM 151 CA ALA A 41 -41.623 -12.821 34.529 1.00 51.35

ANISOU 151 CA ALA A 41 8192 7128 4189 2078 -814 -460

ATOM 152 C ALA A 41 -40.987 -13.963 35.321 1.00 52.02

ANISOU 152 C ALA A 41 8406 7335 4026 2235 -899 -253

ATOM 153 O ALA A 41 -39.815 -14.280 35.120 1.00 52.01

ANISOU 153 O ALA A 41 8337 7326 4098 2274 -1112 -259

ATOM 154 CB ALA A 41 -42.256 -13.346 33.253 1.00 47.07

ANISOU 154 CB ALA A 41 7553 6368 3962 1921 -633 -300

ATOM 155 N PRO A 42 -41.753 -14.574 36.237 1.00 51.47

ANISOU 155 N PRO A 42 8513 7381 3660 2334 -729 -57

ATOM 156 CA PRO A 42 -41.247 -15.738 36.972 1.00 53.75

ANISOU 156 CA PRO A 42 8951 7760 3712 2489 -788 199

ATOM 157 C PRO A 42 -40.845 -16.857 36.014 1.00 51.73

ANISOU 157 C PRO A 42 8631 7280 3742 2433 -785 414

ATOM 158 O PRO A 42 -41.349 -16.904 34.894 1.00 50.55

ANISOU 158 O PRO A 42 8368 6928 3912 2263 -650 422

ATOM 159 CB PRO A 42 -42.451 -16.161 37.819 1.00 54.94

ANISOU 159 CB PRO A 42 9279 8015 3580 2536 -509 408

ATOM 160 CG PRO A 42 -43.238 -14.913 38.007 1.00 48.45

ANISOU 160 CG PRO A 42 8419 7282 2709 2494 -407 147

ATOM 161 CD PRO A 42 -43.087 -14.162 36.709 1.00 53.29

ANISOU 161 CD PRO A 42 8816 7687 3747 2323 -475 -64

ATOM 162 N LYS A 43 -39.945 -17.733 36.451 1.00 53.84

ANISOU 162 N LYS A 43 8967 7585 3904 2579 -936 570

ATOM 163 CA LYS A 43 -39.416 -18.809 35.610 1.00 54.66

ANISOU 163 CA LYS A 43 9018 7476 4276 2566 -958 744

ATOM 164 C LYS A 43 -40.478 -19.775 35.087 1.00 55.33

ANISOU 164 C LYS A 43 9185 7341 4496 2463 -679 1012

ATOM 165 O LYS A 43 -40.365 -20.290 33.976 1.00 54.49

ANISOU 165 O LYS A 43 8984 7009 4711 2364 -647 1042

ATOM 166 CB LYS A 43 -38.354 -19.599 36.375 1.00 56.44

ANISOU 166 CB LYS A 43 9254 7770 4423 2696 -1115 843

ATOM 167 CG LYS A 43 -37.076 -18.832 36.646 1.00 56.04

ANISOU 167 CG LYS A 43 9057 7886 4349 2768 -1415 583

ATOM 168 CD LYS A 43 -36.119 -19.671 37.477 1.00 58.44

ANISOU 168 CD LYS A 43 9383 8272 4552 2911 -1558 712

ATOM 169 CE LYS A 43 -34.772 -18.995 37.613 1.00 58.74

ANISOU 169 CE LYS A 43 9235 8459 4626 2963 -1858 462

ATOM 170 NZ LYS A 43 -33.921 -19.687 38.613 1.00 64.03

ANISOU 170 NZ LYS A 43 9938 9253 5136 3117 -2009 580

ATOM 171 N LYS A 44 -41.503 -20.023 35.893 1.00 58.55

ANISOU 171 N LYS A 44 9734 7816 4694 2451 -463 1180

ATOM 172 CA LYS A 44 -42.545 -20.977 35.536 1.00 62.40

ANISOU 172 CA LYS A 44 10288 8104 5318 2328 -192 1445

ATOM 173 C LYS A 44 -43.889 -20.495 36.075 1.00 66.02

ANISOU 173 C LYS A 44 10800 8687 5598 2259 64 1478

ATOM 174 O LYS A 44 -43. 923 -19.639 36.961 1.00 68.68

ANISOU 174 O LYS A 44 11171 9275 5650 2351 31 1333

ATOM 175 CB LYS A 44 -42. 195 -22.374 36.079 1.00 65.55

ANISOU 175 CB LYS A 44 10774 8409 5722 2370 -182 1710

ATOM 176 CG LYS A 44 -41.768 -22.386 37.532 1.00 71.99

ANISOU 176 CG LYS A 44 11687 9466 6199 2519 -268 1758

ATOM 177 CD LYS A 44 -41.086 -23.695 37.926 1.00 77.12

ANISOU 177 CD LYS A 44 12407 10012 6883 2595 -341 1991

ATOM 178 CE LYS A 44 -42.084 -24.831 38.104 1.00 79.80

ANISOU 178 CE LYS A 44 12863 10179 7279 2481 -83 2313

ATOM 179 NZ LYS A 44 -41.474 -25.993 38.814 1.00 83.50 ANISOU 179 NZ LYS A 44 13439 10595 7694 2581 -161 2553

ATOM 180 N PRO A 45 -45.001 -21.018 35.522 1.00 65.78

ANISOU 180 N PRO A 45 10736 8482 5775 2077 320 1628

ATOM 181 CA PRO A 45 -46.346 -20.694 36.020 1.00 64.59

ANISOU 181 CA PRO A 45 10590 8450 5502 1996 600 1682

ATOM 182 C PRO A 45 -46.485 -20.925 37.526 1.00 67.55

ANISOU 182 C PRO A 45 11121 9051 5495 2121 681 1834

ATOM 183 O PRO A 45 -45.768 -21.762 38.077 1.00 69.58

ANISOU 183 O PRO A 45 11462 9283 5691 2194 569 1981

ATOM 184 CB PRO A 45 -47.237 -21.668 35.248 1.00 64.54

ANISOU 184 CB PRO A 45 10536 8182 5802 1788 812 1894

ATOM 185 CG PRO A 45 -46.522 -21.847 33.945 1.00 62.16

ANISOU 185 CG PRO A 45 10122 7648 5850 1718 627 1762

ATOM 186 CD PRO A 45 -45.054 -21.832 34.290 1.00 62.39

ANISOU 186 CD PRO A 45 10227 7743 5736 1926 348 1701

ATOM 187 N PRO A 46 -47.390 -20.182 38.189 1.00 67.54

ANISOU 187 N PRO A 46 11112 9266 5286 2126 865 1761

ATOM 188 CA PRO A 46 -48.279 -19.170 37.599 1.00 64.71

ANISOU 188 CA PRO A 46 10609 8940 5038 2037 1000 1558

ATOM 189 C PRO A 46 -47.570 -17.843 37.323 1.00 61.75

ANISOU 189 C PRO A 46 10137 8637 4688 2103 748 1158

ATOM 190 O PRO A 46 -46.731 -17.413 38.114 1.00 66.14

ANISOU 190 O PRO A 46 10802 9372 4956 2278 556 1034

ATOM 191 CB PRO A 46 -49.342 -18.979 38.682 1.00 66.60

ANISOU 191 CB PRO A 46 10884 9411 5012 2061 1276 1631

ATOM 192 CG PRO A 46 -48.617 -19.244 39.946 1.00 69.14

ANISOU 192 CG PRO A 46 11345 9894 5030 2204 1143 1677

ATOM 193 CD PRO A 46 -47.626 -20.338 39.635 1.00 69.51

ANISOU 193 CD PRO A 46 11461 9739 5209 2207 956 1862

ATOM 194 N GLN A 47 -47.904 -17.209 36.207 1.00 57.50

ANISOU 194 N GLN A 47 9398 7955 4494 1957 739 966

ATOM 195 CA GLN A 47 -47.302 -15.931 35.844 1.00 56.69

ANISOU 195 CA GLN A 47 9197 7874 4468 1987 523 611

ATOM 196 C GLN A 47 -48.371 -14.912 35.460 1.00 54.48

ANISOU 196 C GLN A 47 8768 7600 4331 1910 670 428

ATOM 197 O GLN A 47 -49.244 -15.196 34.635 1.00 49.86

ANISOU 197 O GLN A 47 8053 6881 4013 1757 826 521

ATOM 198 CB GLN A 47 -46.337 -16.104 34.668 1.00 53.18

ANISOU 198 CB GLN A 47 8651 7215 4340 1903 303 552

ATOM 199 CG GLN A 47 -45.151 -17.013 34.930 1.00 52.82

ANISOU 199 CG GLN A 47 8715 7150 4204 2004 122 691

ATOM 200 CD GLN A 47 -44.796 -17.835 33.706 1.00 48.17

ANISOU 200 CD GLN A 47 8041 6304 3955 1887 81 791

ATOM 201 OE1 GLN A 47 -45.678 -18.245 32.953 1.00 47.57

ANISOU 201 OE1 GLN A 47 7898 6074 4101 1732 255 888

ATOM 202 NE2 GLN A 47 -43.505 -18.071 33.494 1.00 44.92

ANISOU 202 NE2 GLN A 47 7622 5857 3588 1966 -152 751

ATOM 203 N ARG A 48 -48.303 -13.727 36.061 1.00 55.04

ANISOU 203 N ARG A 48 8858 7824 4232 2026 607 157

ATOM 204 CA ARG A 48 -49.146 -12.615 35.634 1.00 51.55

ANISOU 204 CA ARG A 48 8272 7355 3958 1986 696 -57

ATOM 205 C ARG A 48 -48.484 -11.888 34.464 1.00 44.33

ANISOU 205 C ARG A 48 7228 6239 3376 1891 472 -253

ATOM 206 O ARG A 48 -47.848 -10.848 34.644 1.00 42.49

ANISOU 206 O ARG A 48 7007 6023 3114 1956 290 -521

ATOM 207 CB ARG A 48 -49.406 -11.650 36.793 1.00 54.95

ANISOU 207 CB ARG A 48 8793 8012 4071 2163 740 -279

ATOM 208 CG ARG A 48 -50.361 -12.205 37.841 1.00 65.04

ANISOU 208 CG ARG A 48 10165 9513 5037 2247 1040 -88 ATOM 209 CD ARG A 48 -50.242 -11.476 39.178 1.00 72.87

ANISOU 209 CD ARG A 48 11303 10762 5624 2448 1025 -295

ATOM 210 NE ARG A 48 -48.962 -11.737 39.834 1.00 77.21

ANISOU 210 NE ARG A 48 11988 11371 5976 2512 749 -306

ATOM 211 CZ ARG A 48 -48.639 -11.296 41.047 1.00 85.05

ANISOU 211 CZ ARG A 48 13066 12543 6707 2616 656 -446

ATOM 212 NH1 ARG A 48 -49.503 -10.570 41.746 1.00 88.37

ANISOU 212 NH1 ARG A 48 13467 13094 7016 2669 824 -593

ATOM 213 NH2 ARG A 48 -47.451 -11.583 41.564 1.00 87.49

ANISOU 213 NH2 ARG A 48 13469 12904 6868 2671 395 -445

ATOM 214 N LEU A 49 -48.613 -12.447 33.267 1.00 37.65

ANISOU 214 N LEU A 49 6264 5201 2841 1731 486 -119

ATOM 215 CA LEU A 49 -48.064 -11.785 32.098 1.00 40.09

ANISOU 215 CA LEU A 49 6451 5334 3447 1636 310 -272

ATOM 216 C LEU A 49 -49.039 -11.768 30.931 1.00 37.67

ANISOU 216 C LEU A 49 5983 4887 3441 1494 429 -213

ATOM 217 O LEU A 49 -49.953 -12.588 30.847 1.00 38.27

ANISOU 217 O LEU A 49 6026 4966 3549 1429 617 -20

ATOM 218 CB LEU A 49 -46.725 -12.400 31.676 1.00 39.85

ANISOU 218 CB LEU A 49 6445 5221 3476 1607 104 -221

ATOM 219 CG LEU A 49 -46.706 -13.766 30.987 1.00 39.32

ANISOU 219 CG LEU A 49 6368 5032 3541 1512 159 28

ATOM 220 CD1 LEU A 49 -46.830 -13.645 29.484 1.00 35.13

ANISOU 220 CD1 LEU A 49 5687 4318 3342 1357 138 3

ATOM 221 CD2 LEU A 49 -45.432 -14.505 31.353 1.00 40.67

ANISOU 221 CD2 LEU A 49 6633 5222 3597 1596 -7 98

ATOM 222 N GLU A 50 -48.810 -10.841 30.015 1.00 36.69

ANISOU 222 N GLU A 50 5758 4639 3542 1437 308 -372

ATOM 223 CA GLU A 50 -49.677 -10.691 28.869 1.00 39.20

ANISOU 223 CA GLU A 50 5927 4841 4127 1323 381 -333

ATOM 224 C GLU A 50 -48.868 -10.244 27.659 1.00 38.74

ANISOU 224 C GLU A 50 5803 4624 4293 1231 200 -406

ATOM 225 O GLU A 50 -48.071 -9.306 27.756 1.00 40.55

ANISOU 225 O GLU A 50 6053 4826 4529 1269 52 -578

ATOM 226 CB GLU A 50 -50. 749 -9.660 29.193 1.00 40.87

ANISOU 226 CB GLU A 50 6073 5109 4345 1400 496 -458

ATOM 227 CG GLU A 50 -51. 858 -9.601 28.186 1.00 45.51

ANISOU 227 CG GLU A 50 6492 5624 5177 1309 588 -390

ATOM 228 CD GLU A 50 -52. 860 -8.525 28.519 1.00 49.51

ANISOU 228 CD GLU A 50 6920 6184 5708 1421 690 -525

ATOM 229 OE1 GLU A 50 -53.920 -8.857 29.093 1.00 51.43

ANISOU 229 OE1 GLU A 50 7105 6561 5875 1461 900 -451

ATOM 230 OE2 GLU A 50 -52.577 -7.347 28.212 1.00 50.15

ANISOU 230 OE2 GLU A 50 6994 6165 5893 1471 566 -702

ATOM 231 N TRP A 51 -49.064 -10.913 26.526 1.00 26.42

ANISOU 231 N TRP A 51 4164 2963 2911 1104 213 -279

ATOM 232 CA TRP A 51 -48.438 -10.477 25.287 1.00 28.18

ANISOU 232 CA TRP A 51 4320 3058 3329 1017 78 -330

ATOM 233 C TRP A 51 -49. 421 -9.696 24.411 1.00 31.58

ANISOU 233 C TRP A 51 4633 3425 3941 971 113 -355

ATOM 234 O TRP A 51 -50.592 -10.065 24.278 1.00 31.63

ANISOU 234 O TRP A 51 4568 3462 3990 946 238 -270

ATOM 235 CB TRP A 51 -47. 859 -11.661 24.500 1.00 26.24

ANISOU 235 CB TRP A 51 4078 2748 3145 926 45 -204

ATOM 236 CG TRP A 51 -46. 531 -12.146 25.005 1.00 28.16

ANISOU 236 CG TRP A 51 4406 3017 3277 982 -60 -209

ATOM 237 CD1 TRP A 51 -46. 317 -13.110 25.941 1.00 30.82

ANISOU 237 CD1 TRP A 51 4846 3418 3445 1055 -26 -110

ATOM 238 CD2 TRP A 51 -45. 230 -11.692 24.589 1.00 29.97 ANISOU 238 CD2 TRP A 51 4608 3214 3565 974 -218 -306

ATOM 239 NE1 TRP A 51 -44.963 -13.291 26.141 1, 00 31. 10

ANISOU 239 NE1 TRP A 51 4917 3470 3428 1113 -173 -147

ATOM 240 CE2 TRP A 51 -44.275 -12.434 25.326 1, 00 30. 62

ANISOU 240 CE2 TRP A 51 4762 3358 3513 1057 -288 -275

ATOM 241 CE3 TRP A 51 -44.782 -10.731 23.671 1, 00 25.

ANISOU 241 CE3 TRP A 51 4016 2637 3218 903 -302 -400

ATOM 242 CZ2 TRP A 51 -42.896 -12.239 25.179 1, 00 29. 70

ANISOU 242 CZ2 TRP A 51 4605 3250 3429 1072 -443 -355

ATOM 243 CZ3 TRP A 51 -43.416 -10.542 23.516 1, 00 27.

ANISOU 243 CZ3 TRP A 51 4224 2876 3490 896 -433 -468

ATOM 244 CH2 TRP A 51 -42. 485 -11.296 24.271 1, 00 30.

ANISOU 244 CH2 TRP A 51 4586 3272 3684 981 -505 -455

ATOM 245 N LYS A 52 -48. 929 -8.616 23.816 1, 00 32. 07

ANISOU 245 N LYS A 52 4667 3396 4120 960 -4 -461

ATOM 246 CA LYS A 52 -49.709 -7.807 22.891 1, 00 30.

ANISOU 246 CA LYS A 52 4332 3078 4057 933 -4 -466

ATOM 247 C LYS A 52 -48.944 -7.693 21.586 1, 00 29. 13

ANISOU 247 C LYS A 52 4173 2844 4052 825 -115 -42i

ATOM 248 O LYS A 52 -47.764 -7.334 21.570 1, 00 31. 13

ANISOU 248 O LYS A 52 4466 3053 4310 805 -213 -490

ATOM 249 CB LYS A 52 -49.935 -6.394 23.446 1, 00 28. 29

ANISOU 249 CB LYS A 52 4105 2800 3845 1041 -25 -625

ATOM 250 CG LYS A 52 -51.071 -6.264 24.434 1, 00 37.

ANISOU 250 CG LYS A 52 5240 4055 4907 1165 118 -666

ATOM 251 CD LYS A 52 -51.272 -4.798 24.851 1, 00 44. 09

ANISOU 251 CD LYS A 52 6109 4833 5813 1289 88 355

ATOM 252 CE LYS A 52 -52.448 -4.654 25.815 1, 00 50. 56

ANISOU 252 CE LYS A 52 6896 5778 6535 1437 256 -914

ATOM 253 NZ LYS A 52 -52.326 -3.493 26.762 1, 00 52.

ANISOU 253 NZ LYS A 52 7215 5982 6706 1592 235 -1153

ATOM 254 N LEU A 53 -49.604 -7.974 20.477 1, 00 24. 33

ANISOU 254 N LEU A 53 3488 2213 3543 754 -100 -330

ATOM 255 CA LEU A 53 -48.914 -7.814 19.213 1, 00 25. 63

ANISOU 255 CA LEU A 53 3639 2305 3793 664 -188 -290

ATOM 256 C LEU A 53 -49.751 -7.072 18.200 1, 00 26. 08

ANISOU 256 C LEU A 53 3623 2312 3973 652 -214 -243

ATOM 257 O LEU A 53 -50.986 -7.122 18.227 1, 00 31. 16

ANISOU 257 O LEU A 53 4194 2997 4648 689 -162 -215

ATOM 258 CB LEU A 53 -48.385 -9.148 18.667 1, 00 30. 74

ANISOU 258 CB LEU A 53 4303 2984 4393 583 -184 -217

ATOM 259 CG LEU A 53 -49.315 -10.228 18.127 1, 00 33. 90

ANISOU 259 CG LEU A 53 4661 3416 4802 523 -128 -133

ATOM 260 CD1 LEU A 53 -48. 486 -11.315 17.466 1, 00 32. 36

ANISOU 260 CD1 LEU A 53 4508 3207 4579 456 -150 -104

ATOM 261 CD2 LEU A 53 -50. 146 -10.825 19.234 1, 00 36. 45

ANISOU 261 CD2 LEU A 53 4983 3796 5069 562 -22 -112

ATOM 262 N ASN A 54 -49.062 -6.329 17.345 1, 00 24.

ANISOU 262 N ASN A 54 3471 2063 3880 607 -292 -226

ATOM 263 CA ASN A 54 -49.699 -5.634 16.233 1, 00 27. 23

ANISOU 263 CA ASN A 54 3735 2322 4288 599 -336 -145

ATOM 264 C ASN A 54 -48.860 -5.926 15.001 1, 00 25. 67

ANISOU 264 C ASN A 54 3556 2126 4071 493 -378 -63

ATOM 265 O ASN A 54 -47.755 -5.404 14.855 1, 00 22. 90

ANISOU 265 O ASN A 54 3242 1712 3746 449 -404 -71

ATOM 266 CB ASN A 54 -49.785 -4.122 16.495 1, 00 21. 97

ANISOU 266 CB ASN A 54 3086 1522 3738 676 -375 -191

ATOM 267 CG ASN A 54 -50.585 -3.382 15.419 1, 00 27. 99

ANISOU 267 CG ASN A 54 3806 2225 4603 703 -426 ATOM 268 OD1 ASN A 54 -50.947 -3.956 14.397 1.00 32.92

ANISOU 268 OD1 ASN A 54 4389 2927 5191 652 -449 24

ATOM 269 ND2 ASN A 54 -50. 847 -2.107 15.645 1.00 26.43

ANISOU 269 ND2 ASN A 54 3626 1885 4532 794 -457 -112

ATOM 270 N THR A 55 -49. 366 -6.800 14.139 1.00 26.78

ANISOU 270 N THR A 55 3665 2348 4162 446 -378 3

ATOM 271 CA THR A 55 -48. 623 -7.226 12.954 1.00 23.94

ANISOU 271 CA THR A 55 3331 2020 3744 360 -400 61

ATOM 272 C THR A 55 -49. 529 -7.249 11.732 1.00 22.66

ANISOU 272 C THR A 55 3134 1910 3564 344 -455 146

ATOM 273 O THR A 55 -50.696 -6.854 11.804 1.00 22.27

ANISOU 273 O THR A 55 3022 1864 3575 401 -486 168

ATOM 274 CB THR A 55 -48.017 -8.644 13.142 1.00 22.21

ANISOU 274 CB THR A 55 3138 1863 3437 318 -356 12

ATOM 275 OG1 THR A 55 -49.068 -9.614 13.125 1.00 21.66

ANISOU 275 OG1 THR A 55 3037 1844 3348 306 -343 10

ATOM 276 CG2 THR A 55 -47.259 -8.747 14.465 1.00 20.68

ANISOU 276 CG2 THR A 55 2973 1646 3238 358 -323 -65

ATOM 277 N GLY A 56 -48.997 -7.739 10.611 1.00 23.48

ANISOU 277 N GLY A 56 3271 2074 3575 277 -469 185

ATOM 278 CA GLY A 56 -49.788 -7.931 9.410 1.00 20.87

ANISOU 278 CA GLY A 56 2921 1826 3181 259 -539 245

ATOM 279 C GLY A 56 -50.951 -8.894 9.608 1.00 23.05

ANISOU 279 C GLY A 56 3127 2164 3468 249 -563 186

ATOM 280 O GLY A 56 -51.878 -8.912 8.813 1.00 26.42

ANISOU 280 O GLY A 56 3500 2661 3876 246 -650 220

ATOM 281 N ARG A 57 -50.916 -9.693 10.668 1.00 23.21

ANISOU 281 N ARG A 57 3140 2160 3520 239 -489 108

ATOM 282 CA ARG A 57 -52.010 -10.624 10.955 1.00 29.02

ANISOU 282 CA ARG A 57 3798 2934 4294 203 -487 69

ATOM 283 C ARG A 57 -53.148 -9.997 11.753 1.00 28.94

ANISOU 283 C ARG A 57 3675 2929 4393 270 -470 87

ATOM 284 O ARG A 57 -54.245 -10.549 11.797 1.00 33.11

ANISOU 284 O ARG A 57 4094 3512 4977 234 -477 78

ATOM 285 CB ARG A 57 -51.508 -11.842 11.745 1.00 28.53

ANISOU 285 CB ARG A 57 3789 2833 4217 161 -399 8

ATOM 286 CG ARG A 57 -50.396 -12.628 11.084 1.00 26.37

ANISOU 286 CG ARG A 57 3616 2549 3855 120 -398 -33

ATOM 287 CD ARG A 57 -50.142 -13.914 11.837 1.00 25.51

ANISOU 287 CD ARG A 57 3554 2379 3758 96 -329 -79

ATOM 288 NE ARG A 57 -48. 959 -14.609 11.337 1.00 28.86

ANISOU 288 NE ARG A 57 4070 2781 4114 96 -318 -130

ATOM 289 CZ ARG A 57 -48. 965 -15.449 10.307 1.00 31.17

ANISOU 289 CZ ARG A 57 4399 3080 4363 43 -354 -195

ATOM 290 NH1 ARG A 57 -50. 094 -15.710 9.662 1.00 29.04

ANISOU 290 NH1 ARG A 57 4081 2840 4112 -32 -424 -219

ATOM 291 NH2 ARG A 57 -47.839 -16.026 9.922 1.00 34.35

ANISOU 291 NH2 ARG A 57 4878 3467 4706 73 -325 -253

ATOM 292 N THR A 58 -52. 890 -8.869 12.404 1.00 24.54

ANISOU 292 N THR A 58 3134 2313 3877 364 -443 100

ATOM 293 CA THR A 58 -53.858 -8.337 13.363 1.00 26.77

ANISOU 293 CA THR A 58 3321 2598 4251 454 -394 85

ATOM 294 C THR A 58 -54. 624 -7.098 12.904 1.00 23.09

ANISOU 294 C THR A 58 2778 2120 3874 557 -472 135

ATOM 295 O THR A 58 -54. 174 -6.341 12.063 1.00 23.25

ANISOU 295 O THR A 58 2859 2089 3887 572 -554 198

ATOM 296 CB THR A 58 -53. 184 -7.965 14.702 1.00 25.45

ANISOU 296 CB THR A 58 3229 2371 4072 520 -302 23

ATOM 297 OG1 THR A 58 -52. 455 -6.740 14.546 1.00 22.13 ANISOU 297 OG1 THR A 58 2877 1852 3679 574 -353 23

ATOM 298 CG2 THR A 58 -52.252 -9. .075 15. .174 1. ,00 20. .46

ANISOU 298 CG2 THR A 58 2688 1741 3346 450 -246 -7

ATOM 299 N GLU A 59 -55.794 -6. .902 13. .490 1. ,00 24. .20

ANISOU 299 N GLU A 59 2781 2308 4106 634 -434 118

ATOM 300 CA GLU A 59 -56.455 -5. .615 13. .431 1. ,00 25. .55

ANISOU 300 CA GLU A 59 2885 2438 4385 784 -482 144

ATOM 301 C GLU A 59 -56.017 -4. .857 14. .678 1. ,00 30. .45

ANISOU 301 C GLU A 59 3580 2959 5030 887 -385 58

ATOM 302 O GLU A 59 -56.522 -5. .129 15. .770 1. ,00 30. .27

ANISOU 302 O GLU A 59 3496 2996 5010 934 -266 -14

ATOM 303 CB GLU A 59 -57.968 -5. .804 13. .432 1. ,00 31. .10

ANISOU 303 CB GLU A 59 3369 3264 5185 832 -487 152

ATOM 304 CG GLU A 59 -58.744 -4. .502 13. .403 1. ,00 37. .83

ANISOU 304 CG GLU A 59 4129 4077 6169 1024 -536 174

ATOM 305 CD GLU A 59 -58.702 -3. .831 12. .045 1. ,00 40. .41

ANISOU 305 CD GLU A 59 4489 4362 6503 1056 -717 293

ATOM 306 OE1 GLU A 59 -58.581 -4. .548 11. .031 1. ,00 39. .56

ANISOU 306 OE1 GLU A 59 4391 4339 6302 933 -812 347

ATOM 307 OE2 GLU A 59 -58.785 -2. .586 11. .994 1. ,00 44. .85

ANISOU 307 OE2 GLU A 59 5081 4802 7159 1211 -762 333

ATOM 308 N ALA A 60 -55.077 -3. .920 14. .517 1. ,00 28. .31

ANISOU 308 N ALA A 60 3443 2542 4772 913 -433 62

ATOM 309 CA ALA A 60 -54.457 -3. .225 15. .655 1. ,00 25. .42

ANISOU 309 CA ALA A 60 3171 2067 4420 984 -371 -52

ATOM 310 C ALA A 60 -53.895 -4. .240 16. .655 1. ,00 24. .32

ANISOU 310 C ALA A 60 3080 2009 4153 916 -271 ^■134

ATOM 311 O ALA A 60 -53.303 -5. .232 16. .242 1. ,00 23. .08

ANISOU 311 O ALA A 60 2957 1904 3909 790 -278 -91

ATOM 312 CB ALA A 60 -55.438 -2. .275 16. .323 1. ,00 27. .25

ANISOU 312 CB ALA A 60 3329 2258 4767 1170 -337 ^■121

ATOM 313 N TRP A 61 -54.107 -4. .022 17. .956 1. ,00 25. .21

ANISOU 313 N TRP A 61 3201 2138 4241 1016 -178 ^■249

ATOM 314 CA TRP A 61 -53.572 -4. .947 18. .973 1. ,00 24. .41

ANISOU 314 CA TRP A 61 3162 2121 3991 973 -89 ^■305

ATOM 315 C TRP A 61 -54.374 -6. .214 19. .223 1. ,00 27. .07

ANISOU 315 C TRP A 61 3409 2607 4269 923 17 ^■244

ATOM 316 O TRP A 61 -55.602 -6. .196 19. .315 1. ,00 25. .62

ANISOU 316 O TRP A 61 3085 2501 4149 977 84 ^■226

ATOM 317 CB TRP A 61 -53.350 -4. .249 20. .308 1. ,00 33. .43

ANISOU 317 CB TRP A 61 4379 3241 5081 1097 -37 ^■458

ATOM 318 CG TRP A 61 -52.329 -3. .213 20. .213 1. ,00 43. .12

ANISOU 318 CG TRP A 61 5713 4306 6367 1101 -145 ^■536

ATOM 319 CD1 TRP A 61 -52.540 -1. .887 20. .036 1. ,00 51. .65

ANISOU 319 CD1 TRP A 61 6802 5231 7593 1191 -201 ^■592

ATOM 320 CD2 TRP A 61 -50.910 -3. .397 20. .246 1. ,00 42. .54

ANISOU 320 CD2 TRP A 61 5738 4191 6235 1001 -216 ^■562

ATOM 321 NE1 TRP A 61 -51.347 -1. .228 19. .969 1. ,00 52. .60

ANISOU 321 NE1 TRP A 61 7026 5202 7757 1130 -296 ^■649

ATOM 322 CE2 TRP A 61 -50.326 -2. .129 20. .101 1. ,00 48. .96

ANISOU 322 CE2 TRP A 61 6606 4824 7171 1012 -308 ^■636

ATOM 323 CE3 TRP A 61 -50.079 -4. .505 20. .392 1. ,00 38. .27

ANISOU 323 CE3 TRP A 61 5234 3740 5568 909 -212 ^■528

ATOM 324 CZ2 TRP A 61 -48.948 -1. .934 20. .098 1. ,00 45. .17

ANISOU 324 CZ2 TRP A 61 6193 4273 6697 913 -391 ^■681

ATOM 325 CZ3 TRP A 61 -48.711 -4. .310 20. .386 1. ,00 38. .22

ANISOU 325 CZ3 TRP A 61 5291 3673 5557 842 -300 ^■576

ATOM 326 CH2 TRP A 61 -48.160 -3. .036 20. .242 1. ,00 37. .94

ANISOU 326 CH2 TRP A 61 5285 3480 5650 834 -386 ^■653 ATOM 327 N LYS A 62 -53.639 -7.313 19.359 1.00 25.60

ANISOU 327 N LYS A 62 3298 2452 3976 819 35 -210

ATOM 328 CA LYS A 62 -54. 209 -8.605 19.689 1.00 23.59

ANISOU 328 CA LYS A 62 2994 2295 3672 749 140 -142

ATOM 329 C LYS A 62 -53.518 -9.135 20.942 1.00 28.00

ANISOU 329 C LYS A 62 3677 2891 4071 778 221 -168

ATOM 330 O LYS A 62 -52.291 -9.171 21.010 1.00 28.60

ANISOU 330 O LYS A 62 3873 2915 4079 768 146 -200

ATOM 331 CB LYS A 62 -54.020 -9.565 18.510 1.00 22.60

ANISOU 331 CB LYS A 62 2859 2148 3581 601 67 -63

ATOM 332 CG LYS A 62 -54. 142 -11.042 18.862 1.00 26.06

ANISOU 332 CG LYS A 62 3311 2619 3971 502 155 0

ATOM 333 CD LYS A 62 -55.566 -11.410 19.259 1.00 27.40

ANISOU 333 CD LYS A 62 3326 2877 4207 480 275 46

ATOM 334 CE LYS A 62 -55.596 -12.793 19.895 1.00 29.23

ANISOU 334 CE LYS A 62 3603 3114 4390 385 392 127

ATOM 335 NZ LYS A 62 -56.969 -13.190 20.256 1.00 34.07

ANISOU 335 NZ LYS A 62 4044 3814 5087 331 528 189

ATOM 336 N VAL A 63 -54.309 -9.530 21.936 1.00 31.78

ANISOU 336 N VAL A 63 4117 3472 4484 819 375 -146

ATOM 337 CA VAL A 63 -53.788 -10.056 23.200 1.00 29.70

ANISOU 337 CA VAL A 63 3980 3271 4033 864 461 -143

ATOM 338 C VAL A 63 -53.599 -11.582 23.188 1.00 30.53

ANISOU 338 C VAL A 63 4132 3371 4097 745 509 -3

ATOM 339 O VAL A 63 -54.513 -12.322 22.843 1.00 34.81

ANISOU 339 O VAL A 63 4568 3927 4731 644 588 93

ATOM 340 CB VAL A 63 -54.727 -9.679 24.370 1.00 31.37

ANISOU 340 CB VAL A 63 4147 3615 4159 986 633 -178

ATOM 341 CGI VAL A 63 -54.279 -10.345 25.668 1.00 30.02

ANISOU 341 CGI VAL A 63 4118 3537 3752 1032 733 -141

ATOM 342 CG2 VAL A 63 -54.799 -8.162 24.534 1.00 29.97

ANISOU 342 CG2 VAL A 63 3959 3412 4015 1134 583 -347

ATOM 343 N LEU A 64 -52.411 -12.043 23.571 1.00 31.53

ANISOU 343 N LEU A 64 4410 3468 4103 759 451 3

ATOM 344 CA LEU A 64 -52.140 -13.474 23.758 1.00 33.91

ANISOU 344 CA LEU A 64 4788 3741 4354 687 499 138

ATOM 345 C LEU A 64 -51.814 -13.785 25.226 1.00 40.39

ANISOU 345 C LEU A 64 5740 4653 4951 792 585 185

ATOM 346 O LEU A 64 -51.007 -13.093 25.853 1.00 43.43

ANISOU 346 O LEU A 64 6212 5088 5203 910 506 79

ATOM 347 CB LEU A 64 -50.977 -13.928 22.875 1.00 27.70

ANISOU 347 CB LEU A 64 4065 2841 3616 635 352 128

ATOM 348 CG LEU A 64 -51.212 -13.848 21.372 1.00 23.81

ANISOU 348 CG LEU A 64 3475 2274 3297 527 271 103

ATOM 349 CD1 LEU A 64 -49.934 -14.158 20.623 1.00 21.95

ANISOU 349 CD1 LEU A 64 3309 1961 3071 509 150 72

ATOM 350 CD2 LEU A 64 -52.312 -14.814 20.984 1.00 23.67

ANISOU 350 CD2 LEU A 64 3379 2232 3383 402 355 195

ATOM 351 N SER A 65 -52.433 -14.833 25.764 1.00 41.12

ANISOU 351 N SER A 65 5852 4770 5001 743 740 347

ATOM 352 CA SER A 65 -52.271 -15.195 27.170 1.00 41.20

ANISOU 352 CA SER A 65 5996 4888 4770 844 846 434

ATOM 353 C SER A 65 -51.542 -16.528 27.312 1.00 40.91

ANISOU 353 C SER A 65 6101 4754 4689 813 824 596

ATOM 354 O SER A 65 -51.491 -17.302 26.357 1.00 39.70

ANISOU 354 O SER A 65 5920 4446 4718 689 781 648

ATOM 355 CB SER A 65 -53.644 -15.278 27.838 1.00 44.14

ANISOU 355 CB SER A 65 6281 5382 5109 828 1086 526

ATOM 356 OG SER A 65 -54.428 -16.291 27.234 1.00 49.58 ANISOU 356 OG SER A 65 6874 5978 5987 647 1179 676

ATOM 357 N PRO A 66 -50. 975 -16.804 28 507 1, 00 42. 94

ANISOU 357 N PRO A 66 6520 5101 4696 940 845 670

ATOM 358 CA PRO A 66 -50. 308 -18.092 28 754 1, 00 42. 22

ANISOU 358 CA PRO A 66 6576 4910 4556 944 826 853

ATOM 359 C PRO A 66 -51.157 -19.332 28 426 1, 00 46. 73

ANISOU 359 C PRO A 66 7128 5337 5289 777 980 1061

ATOM 360 O PRO A 66 -50. 600 -20.340 27 979 1, 00 47. i

ANISOU 360 O PRO A 66 7365 5315 5549 735 914 1149

ATOM 361 CB PRO A 66 -49. 990 -18.039 30 256 1, 00 38. 46

ANISOU 361 CB PRO A 66 6258 4611 3745 1114 870 923

ATOM 362 CG PRO A 66 -49.788 -16.595 30 526 1, 00 41. 09

ANISOU 362 CG PRO A 66 6545 5093 3973 1221 782 676

ATOM 363 CD PRO A 66 -50.785 -15.870 29 635 1, 00 41. 13

ANISOU 363 CD PRO A 66 6356 5062 4208 1109 847 563

ATOM 364 N GLN A 67 -52.469 -19.269 28 642 1, 00 46. 5

ANISOU 364 N GLN A 67 7030 5421 5343 685 1181 1128

ATOM 365 CA GLN A 67 -53.335 -20.419 28 365 1, 00 51. 03 5

ANISOU 365 CA GLN A 67 7518 5813 6056 494 1331 1320

ATOM 366 C GLN A 67 -53.562 -20.650 26 866 1, 00 48. )

ANISOU 366 C GLN A 67 7109 5362 6092 325 1223 1218

ATOM 367 O GLN A 67 -53.813 -21.775 26 437 1, 00 50. 91

ANISOU 367 O GLN A 67 7386 5433 6525 173 1257 1334

ATOM 368 CB GLN A 67 -54.672 -20.304 29 108 1, 00 59. i

ANISOU 368 CB GLN A 67 8454 7015 7055 438 1596 1431

ATOM 369 CG GLN A 67 -55.391 -18.972 28 934 1, 00 68. 34 I

ANISOU 369 CG GLN A 67 9404 8339 8224 481 1619 1233

ATOM 370 CD GLN A 67 -54.909 -17.890 29 902 1, 00 75. 84 I

ANISOU 370 CD GLN A 67 10444 9493 8877 712 1601 1106

ATOM 371 OE1 GLN A 67 -53.802 -17.965 30 442 1, 00 77. 99 )

ANISOU 371 OE1 GLN A 67 10912 9774 8947 842 1486 1106

ATOM 372 NE2 GLN A 67 -55.747 -16.880 30 124 1, 00 76. i

ANISOU 372 NE2 GLN A 67 10429 9792 8992 771 1704 984

ATOM 373 N GLY A 68 -53.466 -19.584 26 076 1, 00 43. 79

ANISOU 373 N GLY A 68 6349 4776 5514 353 1089 1001

ATOM 374 CA GLY A 68 -53.603 -19.690 24 635 1, 00 40. 21

ANISOU 374 CA GLY A 68 5785 4194 5300 220 968 894

ATOM 375 C GLY A 68 -54.974 -20.166 24 204 1, 00 39. 56

ANISOU 375 C GLY A 68 5530 4077 5422 21 1082 955

ATOM 376 O GLY A 68 -55.986 -19.770 24 778 1, 00 41. 51

ANISOU 376 O GLY A 68 5646 4469 5655 7 1239 1001

ATOM 377 N GLY A 69 -55.005 -21.026 23 191 1, 00 37. i

ANISOU 377 N GLY A 69 5306 3681 5404 -132 1002 942

ATOM 378 CA GLY A 69 -56.255 -21.504 22 629 1, 00 37. 73

ANISOU 378 CA GLY A 69 5105 3618 5611 -346 1063 965

ATOM 379 C GLY A 69 -56.528 -20.873 21 273 1, 00 38. 51

ANISOU 379 C GLY A 69 5050 3745 5836 -395 890 773

ATOM 380 O GLY A 69 -56.063 -19.762 20 992 1, 00 33.

ANISOU 380 O GLY A 69 4452 3264 5153 -254 785 651

ATOM 381 N GLY A 70 -57.276 -21.587 20 433 1, 00 41. 01

ANISOU 381 N GLY A 70 5252 3962 6367 -598 854 750

ATOM 382 CA GLY A 70 -57.729 -21.064 19 155 1, 00 38. 49

ANISOU 382 CA GLY A 70 4772 3697 6157 -656 689 587

ATOM 383 C GLY A 70 -56.675 -21.108 18 064 1, 00 36. 79

ANISOU 383 C GLY A 70 4692 3387 5900 -609 491 445

ATOM 384 O GLY A 70 -55. 601 -21.685 18 256 1, 00 36. 02

ANISOU 384 O GLY A 70 4800 3159 5728 -546 481 465

ATOM 385 N PRO A 71 -56. 976 -20.482 16 913 1, 00 36. 43

ANISOU 385 N PRO A 71 4527 3421 5892 -626 335 309 ATOM 386 CA PRO A 71 -56.110 -20.467 15.722 1.00 31.11

ANISOU 386 CA PRO A 71 3958 2697 5166 -593 159 172

ATOM 387 C PRO A 71 -54.726 -19.893 16.018 1.00 28.33

ANISOU 387 C PRO A 71 3772 2356 4637 -402 149 166

ATOM 388 O PRO A 71 -53.755 -20.278 15.375 1.00 29.04

ANISOU 388 O PRO A 71 3991 2363 4681 -372 69 92

ATOM 389 CB PRO A 71 -56.854 -19.535 14.755 1.00 33.88

ANISOU 389 CB PRO A 71 4127 3202 5542 -602 29 84

ATOM 390 CG PRO A 71 -58.282 -19.531 15.230 1.00 39.10

ANISOU 390 CG PRO A 71 4561 3946 6351 -705 113 150

ATOM 391 CD PRO A 71 -58.216 -19.704 16.716 1.00 37.51

ANISOU 391 CD PRO A 71 4410 3727 6115 -660 328 293

ATOM 392 N TRP A 72 -54.634 -18.977 16.977 1.00 27.10

ANISOU 392 N TRP A 72 3600 2309 4388 -274 228 229

ATOM 393 CA TRP A 72 -53.353 -18.352 17.280 1.00 24.18

ANISOU 393 CA TRP A 72 3360 1959 3870 -111 199 207

ATOM 394 C TRP A 72 -52.268 -19.316 17.782 1.00 26.10

ANISOU 394 C TRP A 72 3784 2076 4057 -65 228 250

ATOM 395 O TRP A 72 -51.084 -19.033 17.625 1.00 28.49

ANISOU 395 O TRP A 72 4173 2379 4273 41 161 199

ATOM 396 CB TRP A 72 -53.532 -17.165 18.230 1.00 23.87

ANISOU 396 CB TRP A 72 3270 2050 3749 12 263 233

ATOM 397 CG TRP A 72 -53.880 -15.921 17.488 1.00 27.54

ANISOU 397 CG TRP A 72 3620 2605 4238 49 173 158

ATOM 398 CD1 TRP A 72 -55.134 -15.426 17.248 1.00 24.05

ANISOU 398 CD1 TRP A 72 3000 2247 3891 17 178 159

ATOM 399 CD2 TRP A 72 -52.964 -15.030 16.836 1.00 21.76

ANISOU 399 CD2 TRP A 72 2938 1881 3450 127 60 89

ATOM 400 NE1 TRP A 72 -55.050 -14.272 16.510 1.00 24.63

ANISOU 400 NE1 TRP A 72 3030 2366 3961 88 66 102

ATOM 401 CE2 TRP A 72 -53.731 -14.008 16.243 1.00 26.70

ANISOU 401 CE2 TRP A 72 3436 2577 4133 144 1 66

ATOM 402 CE3 TRP A 72 -51.573 -14.995 16.704 1.00 20.69

ANISOU 402 CE3 TRP A 72 2927 1701 3233 183 8 54

ATOM 403 CZ2 TRP A 72 -53.149 -12.962 15.521 1.00 24.89

ANISOU 403 CZ2 TRP A 72 3228 2353 3877 204 -101 29

ATOM 404 CZ3 TRP A 72 -50.995 -13.948 15.992 1.00 19.82

ANISOU 404 CZ3 TRP A 72 2812 1615 3104 227 -81 6

ATOM 405 CH2 TRP A 72 -51.784 -12.948 15.415 1.00 20.01

ANISOU 405 CH2 TRP A 72 2735 1688 3182 233 -130 4

ATOM 406 N ASP A 73 -52.668 -20.447 18.363 1.00 27.02

ANISOU 406 N ASP A 73 3949 2083 4236 -145 325 353

ATOM 407 CA ASP A 73 -51.700 -21.431 18.864 1.00 33.78

ANISOU 407 CA ASP A 73 4985 2796 5053 -84 347 418

ATOM 408 C ASP A 73 -50.759 -21.951 17.778 1.00 37.33

ANISOU 408 C ASP A 73 5517 3132 5534 -67 229 298

ATOM 409 O ASP A 73 -49.626 -22.324 18.069 1.00 39.70

ANISOU 409 O ASP A 73 5941 3371 5771 56 209 311

ATOM 410 CB ASP A 73 -52.404 -22.612 19.545 1.00 36.52

ANISOU 410 CB ASP A 73 5375 3006 5493 -197 476 573

ATOM 411 CG ASP A 73 -52.933 -22.261 20.921 1.00 41.10

ANISOU 411 CG ASP A 73 5936 3708 5974 -154 631 727

ATOM 412 OD1 ASP A 73 -52.475 -21.252 21.491 1.00 39.26

ANISOU 412 OD1 ASP A 73 5708 3635 5574 0 621 702

ATOM 413 OD2 ASP A 73 -53.801 -22.998 21.439 1.00 48.62

ANISOU 413 OD2 ASP A 73 6867 4595 7010 -278 770 870

ATOM 414 N SER A 74 -51.237 -21.971 16.535 1.00 38.24

ANISOU 414 N SER A 74 5556 3239 5736 -179 149 177

ATOM 415 CA SER A 74 -50.444 -22.432 15.399 1.00 38.61 ANISOU 415 CA SER A 74 5674 3205 5789 -163 50 39

ATOM 416 C SER A 74 -49.361 -21. .435 15. .041 1. , 00 38. , 62

ANISOU 416 C SER A 74 5674 3342 5657 -21 -10 -28

ATOM 417 O SER A 74 -48.364 -21. .793 14. .417 1. , 00 43. , 96

ANISOU 417 O SER A 74 6422 3975 6304 47 -53 -115

ATOM 418 CB SER A 74 -51.329 -22. .620 14. .168 1. , 00 37. , 01

ANISOU 418 CB SER A 74 5389 2999 5676 -319 -31 -83

ATOM 419 OG SER A 74 -52.389 -23. .515 14. .425 1. , 00 45. , 15

ANISOU 419 OG SER A 74 6388 3902 6866 -486 15 -35

ATOM 420 N VAL A 75 -49.564 -20. .182 15. .432 1. , 00 32. , 18

ANISOU 420 N VAL A 75 4768 2683 4775 20 -5 7

ATOM 421 CA VAL A 75 -48.748 -19. .085 14. .936 1. , 00 31. , 11

ANISOU 421 CA VAL A 75 4604 2667 4551 105 -67 -54

ATOM 422 C VAL A 75 -47.818 -18. .510 15. .993 1. , 00 32. , 14

ANISOU 422 C VAL A 75 4765 2847 4599 238 -46 -9

ATOM 423 O VAL A 75 -46.629 -18. .309 15. .743 1. , 00 33. , 53

ANISOU 423 O VAL A 75 4964 3046 4729 319 -85 -56

ATOM 424 CB VAL A 75 -49.648 -17. .948 14. .427 1. , 00 30. , 10

ANISOU 424 CB VAL A 75 4351 2657 4428 55 - 106 -66

ATOM 425 CGI VAL A 75 -48.804 -16. .765 13. .973 1. , 00 26. , 56

ANISOU 425 CGI VAL A 75 3886 2300 3905 130 - 157 -98

ATOM 426 CG2 VAL A 75 -50.556 -18. .457 13. .307 1. , 00 30. ,40

ANISOU 426 CG2 VAL A 75 4340 2680 4530 -73 - 165 -126

ATOM 427 N ALA A 76 -48.382 -18. .211 17. .162 1. , 00 28. , 75

ANISOU 427 N ALA A 76 4324 2453 4148 259 15 73

ATOM 428 CA ALA A 76 -47.628 -17. .647 18. .272 1. , 00 24. , 14

ANISOU 428 CA ALA A 76 3775 1932 3463 384 19 98

ATOM 429 C ALA A 76 -48.191 -18. .181 19. .580 1. , 00 30. ,21

ANISOU 429 C ALA A 76 4600 2691 4187 406 116 213

ATOM 430 O ALA A 76 -49.391 -18. .072 19. .854 1. , 00 34. , 09

ANISOU 430 O ALA A 76 5032 3212 4710 337 197 261

ATOM 431 CB ALA A 76 -47.680 -16. .138 18. .249 1. , 00 19. , 84

ANISOU 431 CB ALA A 76 3149 1495 2894 409 -19 42

ATOM 432 N ARG A 77 -47.311 -18. .753 20. .389 1. , 00 27. , 30

ANISOU 432 N ARG A 77 4338 2296 3738 510 112 268

ATOM 433 CA ARG A 77 -47.718 -19. .468 21. .579 1. , 00 29. , 83

ANISOU 433 CA ARG A 77 4748 2595 3992 539 209 413

ATOM 434 C ARG A 77 -46.838 -19. .006 22. .729 1. , 00 31. , 65

ANISOU 434 C ARG A 77 5044 2937 4047 701 166 424

ATOM 435 O ARG A 77 -45.642 -18. .768 22. .539 1. , 00 27. , 57

ANISOU 435 O ARG A 77 4529 2441 3507 788 50 344

ATOM 436 CB ARG A 77 -47.536 -20. .969 21. .337 1. , 00 33. ,86

ANISOU 436 CB ARG A 77 5360 2918 4588 509 229 496

ATOM 437 CG ARG A 77 -47.983 -21. .862 22. .454 1. , 00 40. ,29

ANISOU 437 CG ARG A 77 6283 3668 5357 516 343 690

ATOM 438 CD ARG A 77 -49.503 -21. .913 22. .575 1. , 00 44. ,88

ANISOU 438 CD ARG A 77 6786 4256 6010 355 482 764

ATOM 439 NE ARG A 77 -49.918 -22. .795 23. .668 1. , 00 53. , 04

ANISOU 439 NE ARG A 77 7927 5230 6996 347 622 982

ATOM 440 CZ ARG A 77 -50.141 -22. .386 24. .914 1. , 00 59. , 33

ANISOU 440 CZ ARG A 77 8757 6182 7604 432 719 1089

ATOM 441 NH1 ARG A 77 -49.998 -21. .101 25. .229 1. , 00 58. , 95

ANISOU 441 NH1 ARG A 77 8643 6340 7416 530 678 968

ATOM 442 NH2 ARG A 77 -50.515 -23. .256 25. .845 1. , 00 63. , 35

ANISOU 442 NH2 ARG A 77 9376 6635 8058 418 861 1316

ATOM 443 N VAL A 78 -47.428 -18. .871 23. .916 1. , 00 31. , 01

ANISOU 443 N VAL A 78 5005 2943 3834 741 259 514

ATOM 444 CA VAL A 78 -46.670 -18. .537 25. .116 1. , 00 29. , 84

ANISOU 444 CA VAL A 78 4941 2916 3480 902 210 523 ATOM 445 C VAL A 78 -46.029 -19.788 25.740 1.00 30.15

ANISOU 445 C VAL A 78 5129 2881 3445 995 202 684

ATOM 446 O VAL A 78 -46.714 -20.754 26.041 1.00 35.06

ANISOU 446 O VAL A 78 5827 3410 4083 943 328 857

ATOM 447 CB VAL A 78 -47.566 -17.831 26.149 1.00 32.98

ANISOU 447 CB VAL A 78 5338 3466 3729 931 321 538

ATOM 448 CGI VAL A 78 -46.795 -17.551 27.439 1.00 32.20

ANISOU 448 CGI VAL A 78 5350 3509 3376 1104 257 534

ATOM 449 CG2 VAL A 78 -48.150 -16.541 25.558 1.00 26.22

ANISOU 449 CG2 VAL A 78 4338 2662 2962 874 313 376

ATOM 450 N LEU A 79 -44.713 -19.761 25.935 1.00 28.24

ANISOU 450 N LEU A 79 4920 2674 3135 1132 51 634

ATOM 451 CA LEU A 79 -43.976 -20.902 26.504 1.00 30.01

ANISOU 451 CA LEU A 79 5279 2828 3294 1261 11 785

ATOM 452 C LEU A 79 -44.046 -20.913 28.040 1.00 32.18

ANISOU 452 C LEU A 79 5684 3248 3297 1390 36 918

ATOM 453 O LEU A 79 -44.449 -19.913 28.640 1.00 33.19

ANISOU 453 O LEU A 79 5783 3549 3279 1398 60 837

ATOM 454 CB LEU A 79 -42.518 -20.852 26.031 1.00 34.97

ANISOU 454 CB LEU A 79 5852 3460 3975 1369 -169 668

ATOM 455 CG LEU A 79 -42.299 -20.941 24.518 1.00 31.89

ANISOU 455 CG LEU A 79 5353 2949 3814 1270 -183 547

ATOM 456 CD1 LEU A 79 -40.819 -20.890 24.197 1.00 29.01

ANISOU 456 CD1 LEU A 79 4916 2625 3483 1394 -334 446

ATOM 457 CD2 LEU A 79 -42.926 -22.222 23.963 1.00 28.42

ANISOU 457 CD2 LEU A 79 4996 2284 3517 1191 -78 658

ATOM 458 N PRO A 80 -43.670 -22.039 28.679 1.00 34.34

ANISOU 458 N PRO A 80 6110 3447 3491 1503 34 1123

ATOM 459 CA PRO A 80 -43.721 -22.109 30.146 1.00 36.83

ANISOU 459 CA PRO A 80 6572 3918 3505 1640 58 1277

ATOM 460 C PRO A 80 -42.928 -21.009 30.856 1.00 54.27

ANISOU 460 C PRO A 80 8749 6379 5492 1782 -114 1105

ATOM 461 O PRO A 80 -43.333 -20.586 31.938 1.00 38.54

ANISOU 461 O PRO A 80 6837 4570 3234 1845 -63 1138

ATOM 462 CB PRO A 80 -43.113 -23.485 30.454 1.00 39.02

ANISOU 462 CB PRO A 80 7007 4041 3779 1765 21 1509

ATOM 463 CG PRO A 80 -43.451 -24.305 29.270 1.00 38.07

ANISOU 463 CG PRO A 80 6853 3637 3974 1618 96 1528

ATOM 464 CD PRO A 80 -43.378 -23.362 28.087 1.00 34.99

ANISOU 464 CD PRO A 80 6261 3279 3756 1503 38 1244

ATOM 465 N ASN A 81 -41.827 -20.550 30.268 1.00 35.67

ANISOU 465 N ASN A 81 6272 4038 3241 1825 -309 915

ATOM 466 CA ASN A 81 -41.056 -19.476 30.884 1.00 42.23

ANISOU 466 CA ASN A 81 7051 5090 3905 1926 -491 726

ATOM 467 C ASN A 81 -41.607 -18.088 30.531 1.00 39.62

ANISOU 467 C ASN A 81 6597 4825 3630 1795 -457 497

ATOM 468 O ASN A 81 -41.014 -17.066 30.865 1.00 34.37

ANISOU 468 O ASN A 81 5872 4300 2889 1839 -607 298

ATOM 469 CB ASN A 81 -39.560 -19.597 30.546 1.00 36.08

ANISOU 469 CB ASN A 81 6177 4316 3215 2034 -720 637

ATOM 470 CG ASN A 81 -39.227 -19.122 29.131 1.00 33.50

ANISOU 470 CG ASN A 81 5654 3888 3185 1896 -740 458

ATOM 471 OD1 ASN A 81 -40.095 -19.045 28.253 1.00 31.69

ANISOU 471 OD1 ASN A 81 5388 3534 3117 1732 -588 448

ATOM 472 ND2 ASN A 81 -37.961 -18.794 28.912 1.00 33.61

ANISOU 472 ND2 ASN A 81 5533 3973 3265 1963 -929 323

ATOM 473 N GLY A 82 -42.740 -18.061 29.840 1.00 32.79

ANISOU 473 N GLY A 82 5693 3848 2916 1636 -271 523

ATOM 474 CA GLY A 82 -43.387 -16.805 29.503 1.00 33.57 ANISOU 474 CA GLY A 82 5686 3991 3079 1533 -227

ATOM 475 C GLY A 82 -42.990 -16.204 28.165 1.00 31.95

ANISOU 475 C GLY A 82 5318 3684 3138 1418 -303

ATOM 476 O GLY A 82 -43.600 -15.248 27.709 1.00 35.03

ANISOU 476 O GLY A 82 5624 4066 3618 1326 -259

ATOM 477 N SER A 83 -41.963 -16.760 27.538 1.00 28.60

ANISOU 477 N SER A 83 4850 3187 2829 1437 -410

ATOM 478 CA SER A 83 -41.539 -16.306 26.222 1.00 30.59

ANISOU 478 CA SER A 83 4955 3358 3309 1331 -456

ATOM 479 C SER A 83 -42.593 -16.600 25.161 1.00 30.87

ANISOU 479 C SER A 83 4964 3260 3507 1184 -307

ATOM 480 O SER A 83 -43.344 -17.574 25.264 1.00 30.20

ANISOU 480 O SER A 83 4961 3097 3416 1164 -189

ATOM 481 CB SER A 83 -40.218 -16.969 25.819 1.00 30.95

ANISOU 481 CB SER A 83 4953 3377 3430 1405 -574

ATOM 482 OG SER A 83 -39.137 -16.479 26.594 1.00 32.94

ANISOU 482 OG SER A 83 5167 3771 3578 1517 -751

ATOM 483 N LEU A 84 -42.640 -15.748 24.141 1.00 23.77

ANISOU 483 N LEU A 84 3947 2333 2753 1078 -321

ATOM 484 CA LEU A 84 -43.519 -15.964 23.007 1.00 24.10

ANISOU 484 CA LEU A 84 3947 2270 2938 947 -222

ATOM 485 C LEU A 84 -42.758 -16.720 21.926 1.00 27.03

ANISOU 485 C LEU A 84 4288 2556 3427 928 -254

ATOM 486 O LEU A 84 -41.632 -16.352 21.568 1.00 28.06

ANISOU 486 O LEU A 84 4343 2724 3593 959 -346

ATOM 487 CB LEU A 84 -44.032 -14.632 22.449 1.00 22.74

ANISOU 487 CB LEU A 84 3680 2118 2842 861 -222

ATOM 488 CG LEU A 84 -45.210 -14.774 21.468 1.00 24.39

ANISOU 488 CG LEU A 84 3847 2256 3163 742 -129

ATOM 489 CD1 LEU A 84 -46.466 -15.249 22.205 1.00 21.70

ANISOU 489 CD1 LEU A 84 3549 1926 2769 734 -5

ATOM 490 CD2 LEU A 84 -45.485 -13.465 20.707 1.00 20.58

ANISOU 490 CD2 LEU A 84 3271 1779 2771 680 -160

ATOM 491 N PHE A 85 -43.380 -17.773 21.410 1.00 24.21

ANISOU 491 N PHE A 85 3980 2084 3136 874 -172

ATOM 492 CA PHE A 85 -42.743 -18.646 20.447 1.00 22.20

ANISOU 492 CA PHE A 85 3724 1733 2977 877 -188

ATOM 493 C PHE A 85 -43.514 -18.693 19.135 1.00 26.55

ANISOU 493 C PHE A 85 4233 2218 3636 736 -138

ATOM 494 O PHE A 85 -44.704 -19.026 19.105 1.00 24.69

ANISOU 494 O PHE A 85 4024 1925 3434 642 -67

ATOM 495 CB PHE A 85 -42.634 -20.053 21.023 1.00 24.44

ANISOU 495 CB PHE A 85 4136 1903 3248 960 -161

ATOM 496 CG PHE A 85 -42.128 -21.073 20.049 1.00 29.41

ANISOU 496 CG PHE A 85 4786 2396 3992 975 -164

ATOM 497 CD1 PHE A 85 -40.854 -20.966 19.509 1.00 29.63

ANISOU 497 CD1 PHE A 85 4737 2473 4047 1066 -236

ATOM 498 CD2 PHE A 85 -42.918 -22.156 19.686 1.00 35.21

ANISOU 498 CD2 PHE A 85 5609 2952 4817 899 -90

ATOM 499 CE1 PHE A 85 -40.379 -21.915 18.618 1.00 29.12

ANISOU 499 CE1 PHE A 85 4694 2293 4078 1107 -223

ATOM 500 CE2 PHE A 85 -42.449 -23.113 18.793 1.00 34.71

ANISOU 500 CE2 PHE A 85 5583 2745 4859 926 -97

ATOM 501 CZ PHE A 85 -41.175 -22.992 18.266 1.00 32.23

ANISOU 501 CZ PHE A 85 5202 2493 4551 1044 -158

ATOM 502 N LEU A 86 -42.822 -18.364 18.052 1.00 26.07

ANISOU 502 N LEU A 86 4099 2184 3623 719 -176

ATOM 503 CA LEU A 86 -43.365 -18.512 16.708 1.00 24.38

ANISOU 503 CA LEU A 86 3862 1928 3474 610 -149 ATOM 504 C LEU A 86 -42.530 -19.568 15.984 1.00 25.80

ANISOU 504 C LEU A 86 4078 2033 3690 669 -150 -145

ATOM 505 O LEU A 86 -41.359 -19.338 15.688 1.00 28.27

ANISOU 505 O LEU A 86 4331 2414 3995 746 -176 -201

ATOM 506 CB LEU A 86 -43.299 -17.185 15.945 1.00 19.34

ANISOU 506 CB LEU A 86 3122 1394 2832 549 -176 -147

ATOM 507 CG LEU A 86 -44.230 -16.023 16.309 1.00 27.65

ANISOU 507 CG LEU A 86 4131 2497 3879 493 -178 -122

ATOM 508 CD1 LEU A 86 -43.766 -15.303 17.558 1.00 18.85

ANISOU 508 CD1 LEU A 86 3010 1436 2717 570 -208 -120

ATOM 509 CD2 LEU A 86 -44.365 -15.027 15.134 1.00 22.56

ANISOU 509 CD2 LEU A 86 3415 1900 3257 418 -199 -153

ATOM 510 N PRO A 87 -43.129 -20.730 15.697 1.00 26.73

ANISOU 510 N PRO A 87 4285 2005 3864 631 -116 -138

ATOM 511 CA PRO A 87 -42.392 -21.851 15.096 1.00 26.80

ANISOU 511 CA PRO A 87 4356 1907 3922 709 -113 -207

ATOM 512 C PRO A 87 -41.841 -21.557 13.695 1.00 29.02

ANISOU 512 C PRO A 87 4572 2272 4182 700 -113 -345

ATOM 513 O PRO A 87 -40.802 -22.107 13.328 1.00 30.96

ANISOU 513 O PRO A 87 4820 2504 4440 818 -103 -416

ATOM 514 CB PRO A 87 -43.438 -22.974 15.040 1.00 26.42

ANISOU 514 CB PRO A 87 4416 1664 3958 619 -81 -182

ATOM 515 CG PRO A 87 -44.758 -22.280 15.088 1.00 26.14

ANISOU 515 CG PRO A 87 4324 1690 3918 460 -68 -140

ATOM 516 CD PRO A 87 -44.544 -21.058 15.936 1.00 27.20

ANISOU 516 CD PRO A 87 4383 1985 3966 509 -77 -74

ATOM 517 N ALA A 88 -42.517 -20.706 12.930 1.00 24.73

ANISOU 517 N ALA A 88 3971 1825 3599 576 -118 -372

ATOM 518 CA ALA A 88 -42.080 -20.409 11.565 1.00 25.17

ANISOU 518 CA ALA A 88 3986 1980 3599 561 -106 -477

ATOM 519 C ALA A 88 -42.533 -19.017 11.136 1.00 24.26

ANISOU 519 C ALA A 88 3787 2007 3426 464 -124 -437

ATOM 520 O ALA A 88 -43.669 -18.830 10.708 1.00 24.24

ANISOU 520 O ALA A 88 3793 2003 3413 359 -152 -430

ATOM 521 CB ALA A 88 -42.596 -21.481 10.583 1.00 23.39

ANISOU 521 CB ALA A 88 3852 1652 3382 519 -105 -593

ATOM 522 N VAL A 89 -41.631 -18.048 11.264 1.00 24.30

ANISOU 522 N VAL A 89 3702 2122 3410 501 -114 -406

ATOM 523 CA VAL A 89 -41.917 -16.655 10.960 1.00 26.96

ANISOU 523 CA VAL A 89 3969 2556 3718 421 -129 -349

ATOM 524 C VAL A 89 -42.268 -16.452 9.487 1.00 30.56

ANISOU 524 C VAL A 89 4435 3087 4088 354 -118 -376

ATOM 525 O VAL A 89 -41.638 -17.052 8.599 1.00 29.82

ANISOU 525 O VAL A 89 4362 3037 3931 391 -72 -457

ATOM 526 CB VAL A 89 -40.716 -15.762 11.334 1.00 30.71

ANISOU 526 CB VAL A 89 4343 3108 4216 457 -119 -325

ATOM 527 CGI VAL A 89 -40.767 -14.443 10.590 1.00 32.89

ANISOU 527 CGI VAL A 89 4562 3463 4471 369 -111 -270

ATOM 528 CG2 VAL A 89 -40.679 -15.527 12.828 1.00 31.02

ANISOU 528 CG2 VAL A 89 4374 3106 4308 501 -167 -291

ATOM 529 N GLY A 90 -43.284 -15.618 9.239 1.00 27.45

ANISOU 529 N GLY A 90 4032 2718 3682 273 -164 -313

ATOM 530 CA GLY A 90 -43.659 -15.225 7.892 1.00 24.61

ANISOU 530 CA GLY A 90 3682 2452 3216 219 -178 -306

ATOM 531 C GLY A 90 -43.683 -13.713 7.733 1.00 25.82

ANISOU 531 C GLY A 90 3781 2661 3369 183 -188 -184

ATOM 532 O GLY A 90 -43.579 -12.969 8.723 1.00 22.57

ANISOU 532 O GLY A 90 3324 2196 3057 189 -196 -131

ATOM 533 N ILE A 91 -43.825 -13.258 6.488 1.00 24.71 ANISOU 533 N ILE A 91 3659 2621 3111 149 -192

ATOM 534 CA ILE A 91 -43.912 -11.832 6.180 1.00 23.70

ANISOU 534 CA ILE A 91 3501 2520 2984 114 -204

ATOM 535 C ILE A 91 -44.951 -11.093 7.049 1.00 23.88

ANISOU 535 C ILE A 91 3496 2447 3132 111 -284

ATOM 536 O ILE A 91 -44.698 -9.986 7.524 1.00 23.05

ANISOU 536 O ILE A 91 3356 2284 3117 106 -279

ATOM 537 CB ILE A 91 -44.228 -11.608 4.683 1.00 25.60

ANISOU 537 CB ILE A 91 3793 2889 3046 92 -221

ATOM 538 CGI ILE A 91 -43. 073 -12.119 3.816 1.00 26.82

ANISOU 538 CGI ILE A 91 3969 3163 3059 108 -106

ATOM 539 CG2 ILE A 91 -44.515 -10.117 4.388 1.00 23.53

ANISOU 539 CG2 ILE A 91 3520 2621 2801 66 -251

ATOM 540 CD1 ILE A 91 -43. 343 -12.059 2.312 1.00 25.97

ANISOU 540 CD1 ILE A 91 3937 3216 2716 100 -113

ATOM 541 N GLN A 92 -46.103 -11.717 7.279 1.00 24.00

ANISOU 541 N GLN A 92 3515 2439 3164 111 -350

ATOM 542 CA GLN A 92 -47.178 -11.060 8.017 1.00 28.31

ANISOU 542 CA GLN A 92 4014 2924 3819 123 -408

ATOM 543 C GLN A 92 -46.905 -10.930 9.522 1.00 29.75

ANISOU 543 C GLN A 92 4172 3014 4118 158 -365

ATOM 544 O GLN A 92 -47.702 -10.348 10.252 1.00 31.55

ANISOU 544 O GLN A 92 4362 3197 4429 186 -389

ATOM 545 CB GLN A 92 -48.524 -11.746 7.761 1.00 31.47

ANISOU 545 CB GLN A 92 4391 3352 4214 99 -484

ATOM 546 CG GLN A 92 -48. 982 -11.709 6.295 1.00 41.21

ANISOU 546 CG GLN A 92 5645 4699 5314 75 -569

ATOM 547 CD GLN A 92 -48. 989 -10.295 5.695 1.00 50.98

ANISOU 547 CD GLN A 92 6882 5969 6518 107 -605

ATOM 548 OE1 GLN A 92 -48.495 -10.076 4.586 1.00 52.85

ANISOU 548 OE1 GLN A 92 7179 6297 6605 100 -604

ATOM 549 NE2 GLN A 92 -49.558 -9.337 6.426 1.00 52.30

ANISOU 549 NE2 GLN A 92 6992 6059 6823 150 -628

ATOM 550 N ASP A 93 -45.777 -11.457 9.982 1.00 27.47

ANISOU 550 N ASP A 93 3901 2711 3824 173 -307

ATOM 551 CA ASP A 93 -45.422 -11.330 11.389 1.00 23.73

ANISOU 551 CA ASP A 93 3415 2177 3425 217 -288

ATOM 552 C ASP A 93 -44.596 -10.079 11.668 1.00 22.20

ANISOU 552 C ASP A 93 3190 1956 3287 217 -291

ATOM 553 O ASP A 93 -44.186 -9.858 12.801 1.00 21.02

ANISOU 553 O ASP A 93 3031 1770 3184 254 -296

ATOM 554 CB ASP A 93 -44.684 -12.577 11.880 1.00 24.12

ANISOU 554 CB ASP A 93 3495 2219 3451 251 -250

ATOM 555 CG ASP A 93 -45.542 -13.817 11.815 1.00 28.18

ANISOU 555 CG ASP A 93 4051 2706 3952 236 -247

ATOM 556 OD1 ASP A 93 -46.674 -13.781 12.343 1.00 29.53

ANISOU 556 OD1 ASP A 93 4206 2853 4163 220 -257

ATOM 557 OD2 ASP A 93 -45.091 -14.827 11.229 1.00 32.49

ANISOU 557 OD2 ASP A 93 4638 3249 4459 238 -229

ATOM 558 N GLU A 94 -44.346 -9.266 10.640 1.00 24.16

ANISOU 558 N GLU A 94 3429 2222 3528 171 -291

ATOM 559 CA GLU A 94 -43.691 -7.978 10.849 1.00 25.94

ANISOU 559 CA GLU A 94 3626 2384 3846 143 -296

ATOM 560 C GLU A 94 -44.572 -7.083 11.696 1.00 25.41

ANISOU 560 C GLU A 94 3565 2216 3873 184 -348

ATOM 561 O GLU A 94 -45.787 -7.044 11.505 1.00 26.38

ANISOU 561 O GLU A 94 3698 2337 3988 217 -376

ATOM 562 CB GLU A 94 -43.393 -7.278 9.527 1.00 34.77

ANISOU 562 CB GLU A 94 4749 3528 4936 79 -271 ATOM 563 CG GLU A 94 -42.345 -7.983 8.716 1.00 45.82

ANISOU 563 CG GLU A 94 6129 5042 6239 47 -192 211

ATOM 564 CD GLU A 94 -41. 698 -7.085 7.689 1.00 50.16

ANISOU 564 CD GLU A 94 6664 5616 6776 -30 -132 346

ATOM 565 OE1 GLU A 94 -42.380 -6.707 6.697 1.00 51.23

ANISOU 565 OE1 GLU A 94 6859 5780 6826 -39 -146 463

ATOM 566 OE2 GLU A 94 -40.502 -6.766 7.882 1.00 48.38

ANISOU 566 OE2 GLU A 94 6363 5392 6629 -84 -73 344

ATOM 567 N GLY A 95 -43.963 -6.354 12.624 1.00 22.11

ANISOU 567 N GLY A 95 3132 1721 3548 186 -365 32

ATOM 568 CA GLY A 95 -44.726 -5.473 13.489 1.00 21.84

ANISOU 568 CA GLY A 95 3114 1585 3598 244 -406 -8

ATOM 569 C GLY A 95 -44.165 -5.361 14.890 1.00 23.49

ANISOU 569 C GLY A 95 3323 1769 3833 280 -430 -144

ATOM 570 O GLY A 95 -42.954 -5.438 15.096 1.00 21.77

ANISOU 570 O GLY A 95 3074 1571 3628 234 -442 -189

ATOM 571 N ILE A 96 -45.056 -5.191 15.860 1.00 27.94

ANISOU 571 N ILE A 96 3914 2311 4392 370 -437 -214

ATOM 572 CA ILE A 96 -44.657 -4.898 17.232 1.00 30.05

ANISOU 572 CA ILE A 96 4203 2562 4654 423 -471 -356

ATOM 573 C ILE A 96 -45.169 -5.961 18.208 1.00 30.44

ANISOU 573 C ILE A 96 4280 2723 4564 510 -429 -398

ATOM 574 O ILE A 96 -46.327 -6.385 18.136 1.00 27.08

ANISOU 574 O ILE A 96 3851 2333 4104 550 -370 -347

ATOM 575 CB ILE A 96 -45.139 -3.491 17.640 1.00 33.32

ANISOU 575 CB ILE A 96 4644 2831 5185 466 -509 -424

ATOM 576 CGI ILE A 96 -44.576 -2.454 16.666 1.00 33.50

ANISOU 576 CGI ILE A 96 4654 2712 5363 364 -544 -349

ATOM 577 CG2 ILE A 96 -44.722 -3.158 19.067 1.00 32.41

ANISOU 577 CG2 ILE A 96 4566 2710 5039 525 -557 -608

ATOM 578 CD1 ILE A 96 -45.290 -1.133 16.708 1.00 39.56

ANISOU 578 CD1 ILE A 96 5460 3297 6274 415 -574 -363

ATOM 579 N PHE A 97 -44.283 -6.401 19.101 1.00 27.81

ANISOU 579 N PHE A 97 3964 2450 4153 534 -461 -477

ATOM 580 CA PHE A 97 -44.593 -7.441 20.075 1.00 22.98

ANISOU 580 CA PHE A 97 3398 1941 3391 618 -420 -486

ATOM 581 C PHE A 97 -44.264 -6.908 21.459 1.00 27.57

ANISOU 581 C PHE A 97 4028 2549 3898 700 -477 -628

ATOM 582 O PHE A 97 -43.127 -6.504 21.717 1.00 29.41

ANISOU 582 O PHE A 97 4243 2776 4157 676 -578 -717

ATOM 583 CB PHE A 97 -43.768 -8.710 19.807 1.00 22.16

ANISOU 583 CB PHE A 97 3288 1902 3228 598 -419 -426

ATOM 584 CG PHE A 97 -44.127 -9.434 18.516 1.00 25.21

ANISOU 584 CG PHE A 97 3650 2278 3652 531 -362 -317

ATOM 585 CD1 PHE A 97 -44.701 -10.693 18.553 1.00 22.33

ANISOU 585 CD1 PHE A 97 3321 1942 3222 548 -299 -252

ATOM 586 CD2 PHE A 97 -43.867 -8.862 17.274 1.00 27.68

ANISOU 586 CD2 PHE A 97 3913 2549 4056 448 -374 -282

ATOM 587 CE1 PHE A 97 -45.013 -11.374 17.386 1.00 22.26

ANISOU 587 CE1 PHE A 97 3297 1918 3243 483 -267 -191

ATOM 588 CE2 PHE A 97 -44.184 -9.534 16.099 1.00 27.36

ANISOU 588 CE2 PHE A 97 3864 2523 4010 398 -333 -205

ATOM 589 CZ PHE A 97 -44.758 -10.791 16.155 1.00 24.56

ANISOU 589 CZ PHE A 97 3543 2194 3594 416 -289 -177

ATOM 590 N ARG A 98 -45.255 -6.896 22.347 1.00 29.80

ANISOU 590 N ARG A 98 4362 2877 4084 795 -412 -659

ATOM 591 CA ARG A 98 -45.058 -6.368 23.696 1.00 30.22

ANISOU 591 CA ARG A 98 4481 2977 4023 893 -458 -815

ATOM 592 C ARG A 98 -45.466 -7.355 24.775 1.00 30.38 ANISOU 592 C ARG A 98 4575 3146 3822 994 -380 -775

ATOM 593 O ARG A 98 -46.537 -7.970 24.708 1, 00 27. 84

ANISOU 593 O ARG A 98 4248 2860 3469 1008 -245 -662

ATOM 594 CB ARG A 98 -45.857 -5.090 23.899 1, 00 33. 79

ANISOU 594 CB ARG A 98 4943 3341 4554 944 -443 -929

ATOM 595 CG ARG A 98 -45.375 -3.931 23.087 1, 00 40. 95

ANISOU 595 CG ARG A 98 5810 4073 5675 857 -533 -977

ATOM 596 CD ARG A 98 -46.146 -2.686 23.442 1, 00 41. 43

ANISOU 596 CD ARG A 98 5904 4021 5817 940 -526 -1105

ATOM 597 NE ARG A 98 -45.640 -1.529 22.724 1, 00 40.

ANISOU 597 NE ARG A 98 5818 3745 5973 851 -616 -113?

ATOM 598 CZ ARG A 98 -46.142 -0.308 22.853 1, 00 44.

ANISOU 598 CZ ARG A 98 6360 4122 6607 895 -621 -1225

ATOM 599 NH1 ARG A 98 -47.172 -0.099 23.666 1, 00 42. 10

ANISOU 599 NH1 ARG A 98 6029 3812 6155 1046 -542 -1314

ATOM 600 NH2 ARG A 98 -45.618 0.700 22.171 1, 00 51. 59

ANISOU 600 NH2 ARG A 98 7178 4793 7631 777 -678 -1191

ATOM 601 N CYS A 99 -44.615 -7.494 25.780 1, 00 29. 24

ANISOU 601 N CYS A 99 4493 3091 3524 1061 -469 -860

ATOM 602 CA CYS A 99 -44.986 -8.268 26.947 1, 00 33. 93

ANISOU 602 CA CYS A 99 5185 3835 3873 1176 -397

ATOM 603 C CYS A 99 -45.090 -7.351 28.151 1, 00 34. 20

ANISOU 603 C CYS A 99 5297 3942 3755 1291 -435 -1017

ATOM 604 O CYS A 99 -44. 353 -6.370 28.276 1, 00 36. 93

ANISOU 604 O CYS A 99 5634 4234 4162 1279 -585 -1205

ATOM 605 CB CYS A 99 -43. 990 -9.401 27.220 1, 00 32. 07

ANISOU 605 CB CYS A 99 4983 3674 3526 1198 -469 -724

ATOM 606 SG CYS A 99 -44.623 -10.628 28.391 1, 00 43. 97

ANISOU 606 SG CYS A 99 6624 5330 4752 1318 -336 -563

ATOM 607 N GLN A 100 -46.025 -7.669 29.030 1, 00 32. 24

ANISOU 607 N GLN A 100 5122 3816 3312 1396 -290 -981

ATOM 608 CA GLN A 100 -46.150 -6.963 30.287 1, 00 34.

ANISOU 608 CA GLN A 100 5556 4263 3436 1534 -304 -1174

ATOM 609 C GLN A 100 -46.317 -8. 025 31.358 1, 00 39. 21

ANISOU 609 C GLN A 100 6217 5013 3669 1639 -211 -1045

ATOM 610 O GLN A 100 -47.183 -8. 886 31.241 1, 00 39. 92

ANISOU 610 O GLN A 100 6295 5136 3739 1622 -23 337

ATOM 611 CB GLN A 100 -47. 354 -6.030 30.257 1, 00 38. 92

ANISOU 611 CB GLN A 100 6036 4725 4028 1583 -173 -1274

ATOM 612 CG GLN A 100 -47. 470 -5.134 31.479 1, 00 52. 95

ANISOU 612 CG GLN A 100 7919 6594 5606 1738 -191 -1530

ATOM 613 CD GLN A 100 -48.513 -4.052 31.300 1, 00 61. 26

ANISOU 613 CD GLN A 100 8924 7548 6803 1799 -90 -1663

ATOM 614 OE1 GLN A 100 -49.282 -4.069 30.336 1, 00 63. 23

ANISOU 614 OE1 GLN A 100 9056 7695 7274 1736 8 -1531

ATOM 615 NE2 GLN A 100 -48.542 -3.099 32.223 1, 00 66. 17

ANISOU 615 NE2 GLN A 100 9640 8200 7302 1934 -125 -1937

ATOM 616 N ALA A 101 -45.479 -7.968 32.390 1, 00 41. 61

ANISOU 616 N ALA A 101 6629 5451 3731 1740 -352 -1160

ATOM 617 CA ALA A 101 -45.437 -9.007 33.414 1, 00 40. 51

ANISOU 617 CA ALA A 101 6619 5508 3266 1851 -297 -1008

ATOM 618 C ALA A 101 -45.186 -8.421 34.789 1, 00 42. 75

ANISOU 618 C ALA A 101 7042 5986 3217 2014 -381 -1219

ATOM 619 O ALA A 101 -44.634 -7.333 34.917 1, 00 42. 97

ANISOU 619 O ALA A 101 7060 5976 3291 2022 -559 -1501

ATOM 620 CB ALA A 101 -44.356 -10. 026 33.083 1, 00 36. 66

ANISOU 620 CB ALA A 101 6123 4998 2809 1812 -434 -846

ATOM 621 N MET A 102 -45.600 -9. 157 35.814 1, 00 49. 30

ANISOU 621 N MET A 102 8008 7020 3706 2139 -251 -1078 ATOM 622 CA MET A 102 -45.252 -8.848 37.198 1.00 56.51

ANISOU 622 CA MET A 102 9084 8167 4219 2316 -343 -1240

ATOM 623 C MET A 102 -44.492 -10.015 37.808 1.00 60.73

ANISOU 623 C MET A 102 9732 8847 4495 2394 -436 -1022

ATOM 624 O MET A 102 -44.792 -11.173 37.518 1.00 58.79

ANISOU 624 O MET A 102 9491 8563 4284 2353 -292 -699

ATOM 625 CB MET A 102 -46.507 -8.588 38.024 1.00 59.93

ANISOU 625 CB MET A 102 9586 8751 4435 2417 -77 -1256

ATOM 626 CG MET A 102 -47.059 -7.180 37.895 1.00 64.70

ANISOU 626 CG MET A 102 10100 9255 5227 2399 -54 -1545

ATOM 627 SD MET A 102 -48. 637 -7.005 38.747 1.00131.45

ANISOU 627 SD MET A 102 18567 17876 13501 2496 295 -1514

ATOM 628 CE MET A 102 -48. 263 -7.810 40.304 1.00 55.19

ANISOU 628 CE MET A 102 9081 8512 3377 2605 295 -1374

ATOM 629 N ASN A 103 -43.509 -9.720 38.653 1.00 68.72

ANISOU 629 N ASN A 103 10778 9979 5353 2461 -677 -1166

ATOM 630 CA ASN A 103 -42.811 -10.777 39.378 1.00 75.10

ANISOU 630 CA ASN A 103 11672 10925 5937 2548 -768 -949

ATOM 631 C ASN A 103 -43.505 -11.111 40.701 1.00 82.55

ANISOU 631 C ASN A 103 12754 12080 6532 2656 -586 -824

ATOM 632 O ASN A 103 -44.578 -10.580 40.995 1.00 82.68

ANISOU 632 O ASN A 103 12787 12142 6486 2663 -369 -897

ATOM 633 CB ASN A 103 -41.338 -10.420 39.597 1.00 77.12

ANISOU 633 CB ASN A 103 11855 11207 6239 2553 -1119 -1131

ATOM 634 CG ASN A 103 -41.151 -9.063 40.250 1.00 81.93

ANISOU 634 CG ASN A 103 12435 11867 6828 2546 -1244 -1485

ATOM 635 OD1 ASN A 103 -42.042 -8.553 40.932 1.00 85.03

ANISOU 635 OD1 ASN A 103 12904 12340 7062 2592 -1081 -1569

ATOM 636 ND2 ASN A 103 -39.983 -8.469 40.042 1.00 82.36

ANISOU 636 ND2 ASN A 103 12369 11868 7057 2481 -1527 -1693

ATOM 637 N ARG A 104 -42.893 -11.989 41.494 1.00 88.91

ANISOU 637 N ARG A 104 13648 13013 7122 2743 -670 -635

ATOM 638 CA ARG A 104 -43.460 -12.386 42.782 1.00 95.96

ANISOU 638 CA ARG A 104 14682 14113 7666 2840 -508 -492

ATOM 639 C ARG A 104 -43.538 -11.191 43.732 1.00 99.57

ANISOU 639 C ARG A 104 15163 14724 7944 2897 -569 -819

ATOM 640 O ARG A 104 -44.345 -11.176 44.665 1.00103.20

ANISOU 640 O ARG A 104 15721 15350 8140 2962 -371 -776

ATOM 641 CB ARG A 104 -42.633 -13.507 43.429 1.00100.47

ANISOU 641 CB ARG A 104 15342 14771 8062 2925 -632 -242

ATOM 642 CG ARG A 104 -42.291 -14.685 42.517 1.00100.44

ANISOU 642 CG ARG A 104 15310 14581 8270 2880 -634 52

ATOM 643 CD ARG A 104 -43.529 -15.419 42.013 1.00100.73

ANISOU 643 CD ARG A 104 15381 14504 8387 2798 -291 338

ATOM 644 NE ARG A 104 -43.184 -16.623 41.255 1.00 99.90

ANISOU 644 NE ARG A 104 15270 14203 8483 2755 -296 624

ATOM 645 CZ ARG A 104 -44.045 -17.320 40.515 1.00 98.84

ANISOU 645 CZ ARG A 104 15134 13897 8523 2647 -52 860

ATOM 646 NH1 ARG A 104 -45.309 -16.931 40.416 1.00 98.19

ANISOU 646 NH1 ARG A 104 15035 13836 8437 2572 223 853

ATOM 647 NH2 ARG A 104 -43.639 -18.402 39.861 1.00 97.82

ANISOU 647 NH2 ARG A 104 15002 13565 8598 2608 -83 1091

ATOM 648 N ASN A 105 -42.695 -10.191 43.482 1.00 97.16

ANISOU 648 N ASN A 105 14764 14355 7798 2862 -838 -1144

ATOM 649 CA ASN A 105 -42.618 -8.999 44.325 1.00 97.08

ANISOU 649 CA ASN A 105 14774 14447 7664 2899 -937 -1483

ATOM 650 C ASN A 105 -43. 638 -7.921 43.964 1.00 91.14

ANISOU 650 C ASN A 105 13972 13591 7067 2847 -762 -1698

ATOM 651 O ASN A 105 -43. 814 -6.948 44.700 1.00 93.25 ANISOU 651 O ASN A 105 14275 13930 7225 2887 -784 -1964

ATOM 652 CB ASN A 105 -41.204 -8.414 44.286 1.00 97.51

ANISOU 652 CB ASN A 105 14739 14466 7844 2864 -1309 -1727

ATOM 653 CG ASN A 105 -40.195 -9.278 45.016 1.00 99.53

ANISOU 653 CG ASN A 105 15048 14886 7881 2956 -1502 -1577

ATOM 654 OD1 ASN A 105 -40.461 -10.440 45.324 1.00100.09

ANISOU 654 OD1 ASN A 105 15220 15043 7766 3031 -1369 -1248

ATOM 655 ND2 ASN A 105 -39.027 -8.713 45.297 1.00100.85

ANISOU 655 ND2 ASN A 105 15142 15088 8088 2944 -1816 -1810

ATOM 656 N GLY A 106 -44.302 -8.094 42.827 1.00 84.33

ANISOU 656 N GLY A 106 13026 12552 6462 2763 -594 -1587

ATOM 657 CA GLY A 106 -45.313 -7.151 42.385 1.00 82.25

ANISOU 657 CA GLY A 106 12697 12174 6381 2721 -419 -1757

ATOM 658 C GLY A 106 -44.779 -6.061 41.475 1.00 78.75

ANISOU 658 C GLY A 106 12126 11491 6305 2608 -616 -2029

ATOM 659 O GLY A 106 -45.520 -5.172 41.064 1.00 76.34

ANISOU 659 O GLY A 106 11759 11053 6195 2572 -506 -2181

ATOM 660 N LYS A 107 -43.488 -6.123 41.164 1.00 79.32

ANISOU 660 N LYS A 107 12146 11501 6489 2548 -903 -2076

ATOM 661 CA LYS A 107 -42.884 -5.153 40.259 1.00 79.31

ANISOU 661 CA LYS A 107 12010 11263 6861 2410 -1087 -2297

ATOM 662 C LYS A 107 -43.285 -5.439 38.813 1.00 72.58

ANISOU 662 C LYS A 107 11063 10204 6311 2310 -976 -2156

ATOM 663 O LYS A 107 -43.339 -6.592 38.383 1.00 69.06

ANISOU 663 O LYS A 107 10636 9789 5815 2323 -898 -1893

ATOM 664 CB LYS A 107 -41.358 -5.153 40.393 1.00 83.09

ANISOU 664 CB LYS A 107 12431 11761 7377 2366 -1414 -2384

ATOM 665 CG LYS A 107 -40.677 -4.017 39.634 1.00 83.03

ANISOU 665 CG LYS A 107 12278 11521 7750 2202 -1599 -2625

ATOM 666 CD LYS A 107 -39. 176 -4.236 39.494 1.00 83.07

ANISOU 666 CD LYS A 107 12172 11540 7850 2134 -1888 -2650

ATOM 667 CE LYS A 107 -38. 864 -5.414 38.585 1.00 78.30

ANISOU 667 CE LYS A 107 11506 10914 7329 2118 -1876 -2382

ATOM 668 NZ LYS A 107 -37.415 -5.495 38.252 1.00 77.11

ANISOU 668 NZ LYS A 107 11196 10749 7352 2035 -2142 -2425

ATOM 669 N GLU A 108 -43.560 -4.380 38.065 1.00 69.89

ANISOU 669 N GLU A 108 10628 9641 6288 2209 -970 -2326

ATOM 670 CA GLU A 108 -44.001 -4.518 36.688 1.00 64.74

ANISOU 670 CA GLU A 108 9883 8785 5931 2114 -865 -2211

ATOM 671 C GLU A 108 -42.859 -4.251 35.709 1.00 59.44

ANISOU 671 C GLU A 108 9089 7927 5569 1959 -1093 -2267

ATOM 672 O GLU A 108 -42.073 -3.325 35.897 1.00 64.43

ANISOU 672 O GLU A 108 9666 8489 6327 1884 -1285 -2473

ATOM 673 CB GLU A 108 -45. 177 -3.586 36.421 1.00 67.58

ANISOU 673 CB GLU A 108 10206 9014 6458 2111 -681 -2307

ATOM 674 CG GLU A 108 -45. 957 -3.928 35.171 1.00 72.51

ANISOU 674 CG GLU A 108 10748 9487 7315 2057 -512 -2138

ATOM 675 CD GLU A 108 -47.441 -3.686 35.345 1.00 79.07

ANISOU 675 CD GLU A 108 11568 10350 8123 2144 -239 -2115

ATOM 676 OE1 GLU A 108 -47.952 -3.932 36.461 1.00 81.87

ANISOU 676 OE1 GLU A 108 12008 10925 8173 2265 -107 -2107

ATOM 677 OE2 GLU A 108 -48.091 -3.242 34.373 1.00 79.16

ANISOU 677 OE2 GLU A 108 11474 10177 8427 2090 -157 -2096

ATOM 678 N THR A 109 -42.774 -5.077 34.671 1.00 49.49

ANISOU 678 N THR A 109 7783 6590 4431 1906 -1059 -2082

ATOM 679 CA THR A 109 -41.684 -5.018 33.707 1.00 44.41

ANISOU 679 CA THR A 109 6996 5799 4081 1746 -1237 -2072

ATOM 680 C THR A 109 -42.243 -5.154 32.295 1.00 41.00

ANISOU 680 C THR A 109 6443 5163 3972 1608 -1074 -1874 ATOM 681 O THR A 109 -43.040 -6.047 32.024 1.00 38.42

ANISOU 681 O THR A 109 6126 4869 3603 1627 -877 -1635

ATOM 682 CB THR A 109 -40. 681 -6.158 33.949 1.00 46.53

ANISOU 682 CB THR A 109 7252 6220 4208 1777 -1365 -1915

ATOM 683 OG1 THR A 109 -40. 269 -6.155 35.326 1.00 54.39

ANISOU 683 OG1 THR A 109 8363 7440 4864 1922 -1503 -2044

ATOM 684 CG2 THR A 109 -39. 471 -6.012 33.044 1.00 42.56

ANISOU 684 CG2 THR A 109 6569 5596 4006 1623 -1545 -1936

ATOM 685 N LYS A 110 -41. 834 -4.259 31.403 1.00 41.06

ANISOU 685 N LYS A 110 6340 4963 4299 1464 -1161 -1973

ATOM 686 CA LYS A 110 -42.335 -4.245 30.034 1.00 36.34

ANISOU 686 CA LYS A 110 5639 4182 3988 1340 -1030 -1802

ATOM 687 C LYS A 110 -41.235 -4.629 29.060 1.00 36.91

ANISOU 687 C LYS A 110 5576 4192 4257 1195 -1128 -1692

ATOM 688 O LYS A 110 -40.073 -4.279 29.262 1.00 38.87

ANISOU 688 O LYS A 110 5767 4449 4552 1143 -1321 -1828

ATOM 689 CB LYS A 110 -42.874 -2.863 29.673 1.00 38.59

ANISOU 689 CB LYS A 110 5915 4260 4488 1302 -1015 -1963

ATOM 690 CG LYS A 110 -44.107 -2.428 30.465 1.00 45.07

ANISOU 690 CG LYS A 110 6842 5124 5157 1462 -879 -2073

ATOM 691 CD LYS A 110 -44.449 -0.973 30.169 1.00 51.71

ANISOU 691 CD LYS A 110 7639 5762 6248 1395 -877 -2181

ATOM 692 CE LYS A 110 -45.768 -0.554 30.806 1.00 58.20

ANISOU 692 CE LYS A 110 8515 6632 6967 1540 -705 -2237

ATOM 693 NZ LYS A 110 -46.921 -1.312 30.246 1.00 59.21

ANISOU 693 NZ LYS A 110 8611 6796 7091 1607 -503 -2047

ATOM 694 N SER A 111 -41.615 -5.363 28.013 1.00 33.09

ANISOU 694 N SER A 111 5032 3658 3882 1131 -992 -1458

ATOM 695 CA SER A 111 -40.707 -5.740 26.942 1.00 31.61

ANISOU 695 CA SER A 111 4717 3415 3879 1005 -1039 -1348

ATOM 696 C SER A 111 -41.310 -5.276 25.623 1.00 32.24

ANISOU 696 C SER A 111 4735 3321 4193 890 -930 -1253

ATOM 697 O SER A 111 -42.481 -5.508 25.361 1.00 36.66

ANISOU 697 O SER A 111 5334 3862 4733 924 -783 -1151

ATOM 698 CB SER A 111 -40.510 -7.258 26.907 1.00 30.58

ANISOU 698 CB SER A 111 4594 3404 3623 1060 -989 -1154

ATOM 699 OG SER A 111 -40.029 -7.748 28.146 1.00 36.08

ANISOU 699 OG SER A 111 5365 4268 4075 1191 -1089 -1202

ATOM 700 N ASN A 112 -40.504 -4.629 24.793 1.00 29.50

ANISOU 700 N ASN A 112 4284 2860 4065 752 -1003 -1276

ATOM 701 CA ASN A 112 -40.994 -4.025 23.559 1.00 27.69

ANISOU 701 CA ASN A 112 4013 2466 4043 648 -919 -1182

ATOM 702 C ASN A 112 -40.090 -4.402 22.394 1.00 28.31

ANISOU 702 C ASN A 112 3971 2536 4249 521 -916 -1055

ATOM 703 O ASN A 112 -38.911 -4.057 22.385 1.00 30.47

ANISOU 703 O ASN A 112 4151 2807 4620 436 -1020 -1128

ATOM 704 CB ASN A 112 -41. 041 -2.500 23.715 1.00 30.80

ANISOU 704 CB ASN A 112 4424 2682 4596 603 -990 -1344

ATOM 705 CG ASN A 112 -41. 873 -1.825 22.639 1.00 34.63

ANISOU 705 CG ASN A 112 4908 2993 5256 552 -898 -1231

ATOM 706 OD1 ASN A 112 -42. 862 -2.379 22.160 1.00 35.15

ANISOU 706 OD1 ASN A 112 4990 3097 5269 604 -779 -1088

ATOM 707 ND2 ASN A 112 -41. 472 -0.618 22.254 1.00 38.27

ANISOU 707 ND2 ASN A 112 5348 3255 5937 446 -962 -1290

ATOM 708 N TYR A 113 -40. 640 -5.124 21.423 1.00 29.35

ANISOU 708 N TYR A 113 4097 2678 4378 508 -794 -879

ATOM 709 CA TYR A 113 -39. 862 -5.606 20.291 1.00 29.83

ANISOU 709 CA TYR A 113 4059 2759 4517 414 -764 -765

ATOM 710 C TYR A 113 -40. 417 -5.099 18.968 1.00 30.50 ANISOU 710 C TYR A 113 4132 2736 4719 324 -680 -640

ATOM 711 O TYR A 113 -41.628 -5.165 18.721 1.00 27.74

ANISOU 711 O TYR A 113 3848 2358 4335 369 -612 -575

ATOM 712 CB TYR A 113 -39. 856 -7.135 20.259 1.00 28.17

ANISOU 712 CB TYR A 113 3863 2674 4167 491 -710 -675

ATOM 713 CG TYR A 113 -39. 264 -7.790 21.485 1.00 30.79

ANISOU 713 CG TYR A 113 4215 3122 4363 600 -795 -749

ATOM 714 CD1 TYR A 113 -37.894 -7.970 21.609 1.00 24.09

ANISOU 714 CD1 TYR A 113 3258 2347 3548 592 -894 -800

ATOM 715 CD2 TYR A 113 -40.082 -8.247 22.509 1.00 23.29

ANISOU 715 CD2 TYR A 113 3384 2223 3242 719 -773 -753

ATOM 716 CE1 TYR A 113 -37.352 -8.577 22.727 1.00 28.92

ANISOU 716 CE1 TYR A 113 3888 3077 4022 713 -996 -854

ATOM 717 CE2 TYR A 113 -39.554 -8.853 23.632 1.00 25.31

ANISOU 717 CE2 TYR A 113 3679 2596 3341 832 -854 -793

ATOM 718 CZ TYR A 113 -38.192 -9.018 23.738 1.00 28.91

ANISOU 718 CZ TYR A 113 4037 3121 3828 836 -979 -843

ATOM 719 OH TYR A 113 -37.675 -9.624 24.859 1.00 29.83

ANISOU 719 OH TYR A 113 4194 3365 3774 970 -1083 -871

ATOM 720 N ARG A 114 -39.527 -4.600 18.117 1.00 29.64

ANISOU 720 N ARG A 114 3932 2583 4746 198 -683 -598

ATOM 721 CA ARG A 114 -39.884 -4.266 16.744 1.00 30.01

ANISOU 721 CA ARG A 114 3974 2565 4864 116 -598 -445

ATOM 722 C ARG A 114 -39.316 -5.389 15.867 1.00 30.71

ANISOU 722 C ARG A 114 4003 2789 4878 101 -524 -355

ATOM 723 O ARG A 114 -38.104 -5.561 15.770 1.00 35.22

ANISOU 723 O ARG A 114 4465 3425 5491 50 -532 -378

ATOM 724 CB ARG A 114 -39. 326 -2.883 16.366 1.00 32.34

ANISOU 724 CB ARG A 114 4225 2707 5357 -19 -628 -436

ATOM 725 CG ARG A 114 -39.537 -2.426 14.912 1.00 32.70

ANISOU 725 CG ARG A 114 4273 2687 5466 -109 -541 -243

ATOM 726 CD ARG A 114 -41.004 -2.290 14.533 1.00 37.15

ANISOU 726 CD ARG A 114 4943 3195 5979 -24 -516 -159

ATOM 727 NE ARG A 114 -41.179 -1.850 13.143 1.00 43.63

ANISOU 727 NE ARG A 114 5776 3972 6829 -95 -455 38

ATOM 728 CZ ARG A 114 -41.411 -2.666 12.109 1.00 42.31

ANISOU 728 CZ ARG A 114 5612 3942 6521 -86 -387 154

ATOM 729 NH1 ARG A 114 -41.505 -3.981 12.291 1.00 32.79

ANISOU 729 NH1 ARG A 114 4396 2892 5170 -20 -367 91

ATOM 730 NH2 ARG A 114 -41.554 -2.168 10.885 1.00 43.64

ANISOU 730 NH2 ARG A 114 5807 4084 6690 -143 -343 335

ATOM 731 N VAL A 115 -40.202 -6.178 15.269 1.00 25.57

ANISOU 731 N VAL A 115 3414 2182 4121 151 -456 -271

ATOM 732 CA VAL A 115 -39.794 -7.337 14.482 1.00 25.67

ANISOU 732 CA VAL A 115 3397 2307 4048 159 -388 -221

ATOM 733 C VAL A 115 -39. 857 -7.057 12.981 1.00 27.00

ANISOU 733 C VAL A 115 3558 2483 4219 77 -312 -96

ATOM 734 O VAL A 115 -40. 915 -6.719 12.443 1.00 25.91

ANISOU 734 O VAL A 115 3487 2299 4059 75 -306 -21

ATOM 735 CB VAL A 115 -40. 672 -8.571 14.810 1.00 19.50

ANISOU 735 CB VAL A 115 2697 1568 3144 259 -371 -229

ATOM 736 CGI VAL A 115 -40.343 -9.735 13.886 1.00 19.27

ANISOU 736 CGI VAL A 115 2661 1617 3045 268 -305 -197

ATOM 737 CG2 VAL A 115 -40.502 -8.968 16.275 1.00 19.57

ANISOU 737 CG2 VAL A 115 2727 1595 3112 350 -430 -319

ATOM 738 N ARG A 116 -38.716 -7.201 12.315 1.00 27.48

ANISOU 738 N ARG A 116 3527 2621 4293 22 -254 -72

ATOM 739 CA ARG A 116 -38. 627 -7.059 10.865 1.00 27.88

ANISOU 739 CA ARG A 116 3574 2721 4297 -46 -158 50 ATOM 740 C ARG A 116 -38.166 -8.387 10.297 1.00 30.58

ANISOU 740 C ARG A 116 3896 3204 4518 15 -85 14

ATOM 741 O ARG A 116 -37. 241 -9.012 10.831 1.00 30.98

ANISOU 741 O ARG A 116 3863 3313 4594 63 -85 -73

ATOM 742 CB ARG A 116 -37. 626 -5.966 10.488 1.00 31.46

ANISOU 742 CB ARG A 116 3926 3147 4880 -177 -116 121

ATOM 743 CG ARG A 116 -37.854 -4.647 11.208 1.00 38.59

ANISOU 743 CG ARG A 116 4843 3870 5948 -240 -202 116

ATOM 744 CD ARG A 116 -36.695 -3.666 11.007 1.00 43.39

ANISOU 744 CD ARG A 116 5328 4429 6729 -396 -168 163

ATOM 745 NE ARG A 116 -36.777 -2.538 11.939 1.00 46.53

ANISOU 745 NE ARG A 116 5738 4634 7308 -449 -278 92

ATOM 746 CZ ARG A 116 -37.527 -1.459 11.743 1.00 48.88

ANISOU 746 CZ ARG A 116 6135 4742 7693 -484 -301 177

ATOM 747 NH1 ARG A 116 -38.264 -1.353 10.646 1.00 51.41

ANISOU 747 NH1 ARG A 116 6546 5060 7927 -471 -233 357

ATOM 748 NH2 ARG A 116 -37.541 -0.483 12.639 1.00 48.76

ANISOU 748 NH2 ARG A 116 6136 4540 7851 -519 -403 75

ATOM 749 N VAL A 117 -38.811 -8.839 9.226 1.00 29.68

ANISOU 749 N VAL A 117 3861 3144 4272 26 -36 67

ATOM 750 CA VAL A 117 -38. 476 -10.148 8.686 1.00 28.91

ANISOU 750 CA VAL A 117 3771 3155 4059 96 28 -1

ATOM 751 C VAL A 117 -37. 718 -10.043 7.383 1.00 23.70

ANISOU 751 C VAL A 117 3065 2625 3316 53 155 60

ATOM 752 O VAL A 117 -37. 765 -9.026 6.707 1.00 26.26

ANISOU 752 O VAL A 117 3389 2953 3634 -39 193 193

ATOM 753 CB VAL A 117 -39.710 -11.039 8.508 1.00 31.87

ANISOU 753 CB VAL A 117 4270 3507 4331 151 -16 -40

ATOM 754 CGI VAL A 117 -40.570 -10.978 9.761 1.00 29.23

ANISOU 754 CGI VAL A 117 3972 3060 4074 179 -112 -66

ATOM 755 CG2 VAL A 117 -40.498 -10.625 7.269 1.00 31.96

ANISOU 755 CG2 VAL A 117 4350 3563 4229 101 -8 51

ATOM 756 N TYR A 118 -37. 000 -11.097 7.034 1.00 24.30

ANISOU 756 N TYR A 118 3104 2805 3324 129 232 -31

ATOM 757 CA TYR A 118 -36.175 -11.036 5.842 1.00 27.97

ANISOU 757 CA TYR A 118 3507 3424 3694 103 383 12

ATOM 758 C TYR A 118 -35.957 -12.417 5.268 1.00 28.23

ANISOU 758 C TYR A 118 3579 3552 3594 226 449 -122

ATOM 759 O TYR A 118 -36.183 -13.424 5.935 1.00 28.21

ANISOU 759 O TYR A 118 3621 3472 3624 325 379 -244

ATOM 760 CB TYR A 118 -34.824 -10.376 6.150 1.00 27.32

ANISOU 760 CB TYR A 118 3228 3390 3762 41 455 48

ATOM 761 CG TYR A 118 -33. 867 -11.269 6.905 1.00 32.96

ANISOU 761 CG TYR A 118 3816 4144 4562 153 449 -93

ATOM 762 CD1 TYR A 118 -32.894 -12.000 6.235 1.00 33.94

ANISOU 762 CD1 TYR A 118 3838 4426 4631 233 590 -156

ATOM 763 CD2 TYR A 118 -33.946 -11.396 8.289 1.00 35.29

ANISOU 763 CD2 TYR A 118 4099 4329 4981 199 302 -163

ATOM 764 CE1 TYR A 118 -32.022 -12.826 6.918 1.00 33.71

ANISOU 764 CE1 TYR A 118 3686 4429 4694 364 572 -278

ATOM 765 CE2 TYR A 118 -33. 072 -12.218 8.986 1.00 33.27

ANISOU 765 CE2 TYR A 118 3735 4115 4793 322 276 -271

ATOM 766 CZ TYR A 118 -32. 115 -12.928 8.292 1.00 33.24

ANISOU 766 CZ TYR A 118 3620 4253 4757 408 405 -326

ATOM 767 OH TYR A 118 -31. 251 -13.748 8.972 1.00 36.75

ANISOU 767 OH TYR A 118 3949 4735 5281 557 368 -426

ATOM 768 N GLN A 119 -35. 520 -12.456 4.020 1.00 26.59

ANISOU 768 N GLN A 119 3612 3450 3039 778 -371 0

ATOM 769 CA GLN A 119 -35. 073 -13.701 3.424 1.00 27.16 ANISOU 769 CA GLN A 119 3652 3435 3234 998 -320 147

ATOM 770 C GLN A 119 -33.927 -13.413 2.466 1, 00 27. 21

ANISOU 770 C GLN A 119 3501 3572 3267 985 -377 75

ATOM 771 O GLN A 119 -33.908 -12.388 1.783 1, 00 26.

ANISOU 771 O GLN A 119 3459 3530 3261 787 -411 -110

ATOM 772 CB GLN A 119 -36.220 -14.424 2.707 1, 00 25. 92

ANISOU 772 CB GLN A 119 3665 2897 3289 1003 -174 136

ATOM 773 CG GLN A 119 -35.848 -15.807 2.161 1, 00 27. 11

ANISOU 773 CG GLN A 119 3855 2878 3569 1200 -35 259

ATOM 774 CD GLN A 119 -35.358 -16.753 3.247 1, 00 30. 61

ANISOU 774 CD GLN A 119 4295 3408 3929 1473 30 527

ATOM 775 OE1 GLN A 119 -34.177 -16.755 3.610 1, 00 31. 43

ANISOU 775 OE1 GLN A 119 4220 3813 3909 1638 -51 662

ATOM 776 NE2 GLN A 119 -36.270 -17.563 3.775 1, 00 30. 76

ANISOU 776 NE2 GLN A 119 4493 3193 3999 1527 187 627

ATOM 777 N ILE A 120 -32. 965 -14.321 2.436 1, 00 31. 74

ANISOU 777 N ILE A 120 3957 4266 3839 1220 -357 24i

ATOM 778 CA ILE A 120 -31. 786 -14.166 1.606 1, 00 32. 67

ANISOU 778 CA ILE A 120 3894 4541 3977 1243 -392 211

ATOM 779 C ILE A 120 -32.015 -14.813 0.245 1, 00 32. 26

ANISOU 779 C ILE A 120 3960 4139 4159 1289 -240 159

ATOM 780 O ILE A 120 -32.300 -16.010 0.164 1, 00 36. 91

ANISOU 780 O ILE A 120 4671 4488 4864 1477 -72

ATOM 781 CB ILE A 120 -30.567 -14.825 2.286 1, 00 37. 50

ANISOU 781 CB ILE A 120 4272 5520 4457 1516 -428 464

ATOM 782 CGI ILE A 120 -30.342 -14.221 3.674 1, 00 39. 92

ANISOU 782 CGI ILE A 120 4443 6261 4465 1427 -593 507

ATOM 783 CG2 ILE A 120 -29.321 -14.694 1.423 1, 00 35.

ANISOU 783 CG2 ILE A 120 3856 5519 4296 1554 -446 438

ATOM 784 CD1 ILE A 120 -29.127 -14.802 4.409 1, 00 38. 32

ANISOU 784 CD1 ILE A 120 3937 6559 4065 1698 -667 79?

ATOM 785 N PRO A 121 -31.883 -14.032 -0.836 1, 00 29. 95

ANISOU 785 N PRO A 121 3649 3811 3921 1098 -269 -37

ATOM 786 CA PRO A 121 -32.055 -14.634 -2.161 1, 00 27. 27

ANISOU 786 CA PRO A 121 3413 3198 3752 1106 -129 -104

ATOM 787 C PRO A 121 -30.916 -15.603 -2.454 1, 00 31. 76

ANISOU 787 C PRO A 121 3884 3803 4380 1363 -9 31

ATOM 788 O PRO A 121 -29.904 -15.600 -1.749 1, 00 36. 71

ANISOU 788 O PRO A 121 4299 4745 4904 1526 -78 182

ATOM 789 CB PRO A 121 -31. 966 -13.431 -3.099 1, 00 24. 92

ANISOU 789 CB PRO A 121 3078 2949 3444 871 -204 -299

ATOM 790 CG PRO A 121 -31. 058 -12.475 -2.379 1, 00 26. 92

ANISOU 790 CG PRO A 121 3145 3537 3546 808 -336 -311

ATOM 791 CD PRO A 121 -31.423 -12.633 -0.918 1, 00 30. 66

ANISOU 791 CD PRO A 121 3626 4122 3903 871 -393 -197

ATOM 792 N GLY A 122 -31.080 -16.435 -3.473 1, 00 28. 95

ANISOU 792 N GLY A 122 3671 3154 4173 1395 189

ATOM 793 CA GLY A 122 -29.988 -17.278 -3.915 1, 00 31.

ANISOU 793 CA GLY A 122 3898 3434 4552 1643 364 92

ATOM 794 C GLY A 122 -28.955 -16.397 -4.593 1, 00 34. 16

ANISOU 794 C GLY A 122 4047 4063 4870 1560 255

ATOM 795 O GLY A 122 -29.214 -15.218 -4.854 1, 00 35. 12

ANISOU 795 O GLY A 122 4137 4291 4916 1291 88 -176

ATOM 796 N LYS A 123 -27.788 -16.966 -4.869 1, 00 36. 35

ANISOU 796 N LYS A 123 4177 4433 5201 1803 383 11?

ATOM 797 CA LYS A 123 -26.701 -16.249 -5.518 1, 00 41. 69

ANISOU 797 CA LYS A 123 4624 5375 5842 1738 316 39

ATOM 798 C LYS A 123 -27.200 -15.549 -6.781 1, 00 41. 56

ANISOU 798 C LYS A 123 4757 5182 5853 1416 310 -240 ATOM 799 O LYS A 123 -27.933 -16.142 -7.566 1.00 44.31

ANISOU 799 O LYS A 123 5349 5197 6289 1352 469 -341

ATOM 800 CB LYS A 123 -25.585 -17.233 -5.865 1.00 47.75

ANISOU 800 CB LYS A 123 5271 6156 6717 2083 549 217

ATOM 801 CG LYS A 123 -24.227 -16.601 -6.022 1.00 54.72

ANISOU 801 CG LYS A 123 5788 7476 7526 2108 454 245

ATOM 802 CD LYS A 123 -23.165 -17.638 -6.311 1.00 62.82

ANISOU 802 CD LYS A 123 6673 8523 8673 2512 718 470

ATOM 803 CE LYS A 123 -21.810 -16.975 -6.482 1.00 67.94

ANISOU 803 CE LYS A 123 6906 9670 9239 2512 615 495

ATOM 804 NZ LYS A 123 -21.906 -15.821 -7.419 1.00 66.80

ANISOU 804 NZ LYS A 123 6813 9507 9059 2080 509 157

ATOM 805 N PRO A 124 -26.820 -14.275 -6.972 1.00 38.45

ANISOU 805 N PRO A 124 4221 5029 5361 1193 144 -363

ATOM 806 CA PRO A 124 -27.262 -13.558 -8.174 1.00 33.95

ANISOU 806 CA PRO A 124 3785 4315 4799 929 153 -572

ATOM 807 C PRO A 124 -26.561 -14.110 -9.417 1.00 35.44

ANISOU 807 C PRO A 124 3982 4413 5073 988 348 -626

ATOM 808 O PRO A 124 -25.467 -14.658 -9.308 1.00 37.96

ANISOU 808 O PRO A 124 4123 4861 5438 1213 447 -512

ATOM 809 CB PRO A 124 -26.824 -12.117 -7.899 1.00 31.04

ANISOU 809 CB PRO A 124 3264 4215 4316 720 -8 -650

ATOM 810 CG PRO A 124 -25.636 -12.258 -6.986 1.00 32.23

ANISOU 810 CG PRO A 124 3115 4729 4401 866 -66 -523

ATOM 811 CD PRO A 124 -25.920 -13.463 -6.133 1.00 36.30

ANISOU 811 CD PRO A 124 3657 5185 4950 1159 -27 -316

ATOM 812 N GLU A 125 -27.195 -13.988 -10.576 1.00 32.47

ANISOU 812 N GLU A 125 3795 3843 4698 800 415 -783

ATOM 813 CA GLU A 125 -26.640 -14.540 -11.800 1.00 37.26

ANISOU 813 CA GLU A 125 4455 4343 5357 816 626 -869

ATOM 814 C GLU A 125 -26.741 -13.538 -12.933 1.00 39.13

ANISOU 814 C GLU A 125 4729 4632 5505 556 581 -1019

ATOM 815 O GLU A 125 -27.699 -12.770 -13.019 1.00 37.89

ANISOU 815 O GLU A 125 4660 4471 5265 372 447 -1060

ATOM 816 CB GLU A 125 -27.392 -15.808 -12.214 1.00 41.81

ANISOU 816 CB GLU A 125 5290 4598 5999 839 841 -922

ATOM 817 CG GLU A 125 -27.346 -16.940 -11.212 1.00 50.82

ANISOU 817 CG GLU A 125 6461 5600 7248 1121 974 -752

ATOM 818 CD GLU A 125 -28.163 -18.138 -11.663 1.00 58.86

ANISOU 818 CD GLU A 125 7787 6247 8331 1066 1242 -852

ATOM 819 OE1 GLU A 125 -27.967 -18.601 -12.809 1.00 59.38

ANISOU 819 OE1 GLU A 125 7991 6159 8413 970 1474 -1014

ATOM 820 OE2 GLU A 125 -29.009 -18.612 -10.872 1.00 62.60

ANISOU 820 OE2 GLU A 125 8375 6584 8825 1086 1243 -791

ATOM 821 N ILE A 126 -25.754 -13.565 -13.815 1.00 41.40

ANISOU 821 N ILE A 126 4949 4970 5811 568 720 -1075

ATOM 822 CA ILE A 126 -25.800 -12.765 -15.021 1.00 42.56

ANISOU 822 CA ILE A 126 5159 5148 5864 341 727 -1201

ATOM 823 C ILE A 126 -26.275 -13.623 -16.180 1.00 43.28

ANISOU 823 C ILE A 126 5470 5050 5923 258 915 -1330

ATOM 824 O ILE A 126 -25.717 -14.684 -16.444 1.00 47.11

ANISOU 824 O ILE A 126 5998 5404 6497 394 1151 -1359

ATOM 825 CB ILE A 126 -24.428 -12.155 -15.334 1.00 46.23

ANISOU 825 CB ILE A 126 5416 5810 6341 349 776 -1207

ATOM 826 CGI ILE A 126 -24.129 -11.036 -14.338 1.00 45.50

ANISOU 826 CGI ILE A 126 5137 5935 6214 284 588 -1151

ATOM 827 CG2 ILE A 126 -24.387 -11.620 -16.760 1.00 47.76

ANISOU 827 CG2 ILE A 126 5715 5987 6443 152 866 -1327

ATOM 828 CD1 ILE A 126 -22.770 -10.405 -14.515 1.00 51.15 ANISOU 828 CD1 ILE A 126 5613 6895 6927 234 634 -1176

ATOM 829 N VAL A 127 -27.326 -13.167 -16.852 1, 00 43. 11

ANISOU 829 N VAL A 127 5587 5034 5759 32 831 -1401

ATOM 830 CA VAL A 127 -27.837 -13.843 -18.041 1, 00 45. 65

ANISOU 830 CA VAL A 127 6099 5272 5972 -138 982 -1557

ATOM 831 C VAL A 127 -27.732 -12.912 -19.256 1, 00 47. 70

ANISOU 831 C VAL A 127 6363 5699 6061 -320 959 -1603

ATOM 832 O VAL A 127 -27.558 -11.701 -19.106 1, 00 50.

ANISOU 832 O VAL A 127 6659 6229 6439 -323 822 -1499

ATOM 833 CB VAL A 127 -29.296 -14.305 -17.830 1, 00 47. 13

ANISOU 833 CB VAL A 127 6418 5403 6085 -272 909 -1591

ATOM 834 CGI VAL A 127 -29.442 -14.997 -16.473 1, 00 44. 15

ANISOU 834 CGI VAL A 127 6033 4868 5874 -79 911 -1498

ATOM 835 CG2 VAL A 127 -30.249 -13.127 -17.903 1, 00 46. 13

ANISOU 835 CG2 VAL A 127 6237 5477 5812 -398 664 -1501

ATOM 836 N ASP A 128 -27.820 -13.485 -20.451 1, 00 51. 01

ANISOU 836 N ASP A 128 6925 6105 6351 -483 1126 -1763

ATOM 837 CA ASP A 128 -27.757 -12.732 -21.708 1, 00 54.

ANISOU 837 CA ASP A 128 7427 6765 6622 -659 1127 -1797

ATOM 838 C ASP A 128 -26.629 -11.705 -21.760 1, 00 53. 20

ANISOU 838 C ASP A 128 7087 6638 6489 -566 1130 -1706

ATOM 839 O ASP A 128 -26.856 -10.545 -22.109 1, 00 57. 63

ANISOU 839 O ASP A 128 7624 7339 6934 -640 1022 -1603

ATOM 840 CB ASP A 128 -29.094 -12.040 -21.996 1, 00 59.

ANISOU 840 CB ASP A 128 8062 7590 7025 -819 914 -1713

ATOM 841 CG ASP A 128 -30.248 -13.020 -22.115 1, 00 66.

ANISOU 841 CG ASP A 128 8991 8425 7728 -996 913 -1836

ATOM 842 OD1 ASP A 128 -30. 088 -14.050 -22.806 1, 00 68. 39

ANISOU 842 OD1 ASP A 128 9416 J628 7942 -1148 1131 -2056

ATOM 843 OD2 ASP A 128 -31. 310 -12.763 -21.505 1, 00 68. 22

ANISOU 843 OD2 ASP A 128 9195 J766 7961 -1003 725 -1726

ATOM 844 N SER A 129 -25. 420 -12.127 -21.411 1, 00 46. 17

ANISOU 844 N SER A 129 6098 5661 5782 -401 1280 -1727

ATOM 845 CA SER A 129 -24.275 -11.225 -21.426 1, 00 41. 33

ANISOU 845 CA SER A 129 5317 5157 5229 -356 1301 -1670

ATOM 846 C SER A 129 -23.642 -11.145 -22.808 1, 00 43. 54

ANISOU 846 C SER A 129 5661 5485 5397 -472 1503 -1773

ATOM 847 O SER A 129 -23.564 -12.145 -23.527 1, 00 45. 39

ANISOU 847 O SER A 129 6025 5628 5593 -499 1709 -1913

ATOM 848 CB SER A 129 -23.233 -11.657 -20.397 1, 00 38. 32

ANISOU 848 CB SER A 129 4725 4771 5064 -123 1348 -1614

ATOM 849 OG SER A 129 -22.749 -12.951 -20.690 1, 00 39. 51

ANISOU 849 OG SER A 129 4922 4784 5305 18 1600 -1684

ATOM 850 N ALA A 130 -23.197 -9.949 -23.180 1, 00 42. 25

ANISOU 850 N ALA A 130 5432 5444 5175 -558 1480 -1714

ATOM 851 CA ALA A 130 -22.530 -9.756 -24.460 1, 00 44. 24

ANISOU 851 CA ALA A 130 5737 5756 5315 -668 1680 -1792

ATOM 852 C ALA A 130 -21.094 -10.250 -24.376 1, 00 45. 66

ANISOU 852 C ALA A 130 5746 5929 5675 -535 1891 -1853

ATOM 853 O ALA A 130 -20.453 -10.149 -23.333 1, 00 49. 08

ANISOU 853 O ALA A 130 5952 6412 6286 -395 1832 -1782

ATOM 854 CB ALA A 130 -22.564 -8.291 -24.870 1, 00 43. 65

ANISOU 854 CB ALA A 130 5673 5786 5126 -795 1626 -1681

ATOM 855 N SER A 131 -20.588 -10.794 -25.472 1, 00 46. 42

ANISOU 855 N SER A 131 5933 6000 5706 -578 2147 -1978

ATOM 856 CA SER A 131 -19.194 -11.208 -25.513 1, 00 48. il

ANISOU 856 CA SER A 131 6052 6317 6177 -429 2389 -2011

ATOM 857 C SER A 131 -18.333 -10.190 -26.268 1, 00 44. 12

ANISOU 857 C SER A 131 5373 5873 5518 -567 2490 -2014 ATOM 858 O SER A 131 -17.109 -10.182 -26.132 1.00 45.74

ANISOU 858 O SER A 131 5334 6176 5867 -470 2637 -2006

ATOM 859 CB SER A 131 -19.075 -12.597 -26.125 1.00 45.31

ANISOU 859 CB SER A 131 5770 5691 5753 -349 2692 -2155

ATOM 860 OG SER A 131 -19.908 -12.694 -27.258 1.00 47.86

ANISOU 860 OG SER A 131 6389 5984 5810 -604 2742 -2298

ATOM 861 N GLU A 132 -18.977 -9.337 -27.061 1.00 43.58

ANISOU 861 N GLU A 132 5488 5844 5225 -785 2425 -2003

ATOM 862 CA GLU A 132 -18.283 -8.234 -27.726 1.00 52.00

ANISOU 862 CA GLU A 132 6516 7020 6223 -929 2530 -1974

ATOM 863 C GLU A 132 -18.975 -6.896 -27.507 1.00 53.01

ANISOU 863 C GLU A 132 6712 7172 6256 -1052 2345 -1828

ATOM 864 O GLU A 132 -20.194 -6.785 -27.640 1.00 53.51

ANISOU 864 O GLU A 132 6954 7215 6163 -1083 2190 -1752

ATOM 865 CB GLU A 132 -18.138 -8.477 -29.227 1.00 53.86

ANISOU 865 CB GLU A 132 6943 7270 6250 -1054 2770 -2078

ATOM 866 CG GLU A 132 -17.032 -9.444 -29.606 1.00 55.94

ANISOU 866 CG GLU A 132 7120 7499 6636 -949 3080 -2219

ATOM 867 CD GLU A 132 -17.490 -10.874 -29.539 1.00 54.48

ANISOU 867 CD GLU A 132 7067 7144 6491 -831 3117 -2303

ATOM 868 OE1 GLU A 132 -18.705 -11.093 -29.365 1.00 51.11

ANISOU 868 OE1 GLU A 132 6809 6673 5939 -902 2950 -2321

ATOM 869 OE2 GLU A 132 -16.644 -11.778 -29.661 1.00 57.83

ANISOU 869 OE2 GLU A 132 7428 7471 7075 -668 3316 -2329

ATOM 870 N LEU A 133 -18.183 -5.885 -27.160 1.00 52.37

ANISOU 870 N LEU A 133 6483 7142 6273 -1127 2393 -1788

ATOM 871 CA LEU A 133 -18.666 -4.514 -27.096 1.00 48.75

ANISOU 871 CA LEU A 133 6139 6643 5741 -1256 2342 -1656

ATOM 872 C LEU A 133 -17.966 -3.679 -28.160 1.00 50.90

ANISOU 872 C LEU A 133 6484 6940 5915 -1417 2597 -1645

ATOM 873 O LEU A 133 -16.831 -3.970 -28.549 1.00 49.70

ANISOU 873 O LEU A 133 6188 6870 5826 -1454 2789 -1761

ATOM 874 CB LEU A 133 -18.401 -3.911 -25.720 1.00 47.82

ANISOU 874 CB LEU A 133 5844 6522 5804 -1280 2233 -1648

ATOM 875 CG LEU A 133 -18.975 -4.645 -24.508 1.00 46.61

ANISOU 875 CG LEU A 133 5596 6361 5754 -1122 1991 -1644

ATOM 876 CD1 LEU A 133 -18.873 -3.761 -23.289 1.00 43.99

ANISOU 876 CD1 LEU A 133 5156 6038 5521 -1214 1902 -1630

ATOM 877 CD2 LEU A 133 -20.411 -5.079 -24.746 1.00 42.17

ANISOU 877 CD2 LEU A 133 5256 5702 5064 -1032 1842 -1560

ATOM 878 N THR A 134 -18.647 -2.644 -28.635 1.00 52.16

ANISOU 878 N THR A 134 6864 7031 5925 -1490 2625 -1479

ATOM 879 CA THR A 134 -18.027 -1.700 -29.547 1.00 55.64

ANISOU 879 CA THR A 134 7404 7457 6279 -1641 2896 -1428

ATOM 880 C THR A 134 -17.868 -0.359 -28.837 1.00 56.36

ANISOU 880 C THR A 134 7518 7403 6492 -1763 2983 -1356

ATOM 881 O THR A 134 -18.841 0.202 -28.328 1.00 51.63

ANISOU 881 O THR A 134 7055 6678 5885 -1701 2879 -1203

ATOM 882 CB THR A 134 -18.854 -1.525 -30.830 1.00 55.78

ANISOU 882 CB THR A 134 7685 7520 5988 -1621 2940 -1254

ATOM 883 OG1 THR A 134 -19.274 -2.809 -31.305 1.00 54.46

ANISOU 883 OG1 THR A 134 7525 7484 5681 -1555 2826 -1357

ATOM 884 CG2 THR A 134 -18.032 -0.822 -31.905 1.00 51.54

ANISOU 884 CG2 THR A 134 7242 6992 5348 -1761 3257 -1222

ATOM 885 N ALA A 135 -16.635 0.134 -28.789 1.00 59.63

ANISOU 885 N ALA A 135 7798 7837 7021 -1956 3204 -1483

ATOM 886 CA ALA A 135 -16.334 1.393 -28.120 1.00 62.41

ANISOU 886 CA ALA A 135 8182 8046 7485 -2163 3354 -1488

ATOM 887 C ALA A 135 -16.992 2.556 -28.850 1.00 65.03 ANISOU 887 C ALA A 135 8877 8144 7686 -2180 3572 -1246

ATOM 888 O ALA A 135 -17.021 2.582 -30.082 1, 00 65. 71

ANISOU 888 O ALA A 135 9112 8259 7595 -2141 3712 -1124

ATOM 889 CB ALA A 135 -14.827 1.603 -28.040 1, 00 63. 90

ANISOU 889 CB ALA A 135 8119 8371 7791 -2411 3554 -1695

ATOM 890 N GLY A 136 -17.526 3.508 -28.087 1, 00 63. 22

ANISOU 890 N GLY A 136 8798 7687 7535 -2224 3626 -1160

ATOM 891 CA GLY A 136 -18.099 4.714 -28.660 1, 00 63. 65

ANISOU 891 CA GLY A 136 9204 7469 7511 -2191 3882

ATOM 892 C GLY A 136 -19.594 4.657 -28.922 1, 00 63.

ANISOU 892 C GLY A 136 9381 7430 7347 -1880 3740 -564

ATOM 893 O GLY A 136 -20.201 5.663 -29.289 1, 00 65. 01

ANISOU 893 O GLY A 136 9837 7397 7466 -1780 3960 -270

ATOM 894 N VAL A 137 -20.192 3.483 -28.738 1, 00 60. 51

ANISOU 894 N VAL A 137 8828 7264 6898 -1708 3367 -601

ATOM 895 CA VAL A 137 -21.632 3.316 -28.933 1, 00 59. 52

ANISOU 895 CA VAL A 137 8807 7197 6612 -1436 3169 -320

ATOM 896 C VAL A 137 -22.248 2.572 -27.746 1, 00 58. 57

ANISOU 896 C VAL A 137 8527 7117 6611 -1348 2840 -432

ATOM 897 O VAL A 137 -21.536 1.900 -26.998 1, 00 57. 00

ANISOU 897 O VAL A 137 8118 6973 6565 -1457 2724 -716

ATOM 898 CB VAL A 137 -21.945 2.560 -30.244 1, 00 59. 34

ANISOU 898 CB VAL A 137 8785 7470 6292 -1345 3067 -223

ATOM 899 CGI VAL A 137 -21.482 3.367 -31.457 1, 00 59. 94

ANISOU 899 CGI VAL A 137 9046 7521 6205 -1400 3398 -48

ATOM 900 CG2 VAL A 137 -21.304 1.182 -30.232 1, 00 59. 46

ANISOU 900 CG2 VAL A 137 8580 7679 6335 -1431 2892 -552

ATOM 901 N PRO A 138 -23.571 2.703 -27.550 1, 00 58. 31

ANISOU 901 N PRO A 138 8575 7076 6503 -1132 2702 -184

ATOM 902 CA PRO A 138 -24.153 1.977 -26.415 1, 00 56.

ANISOU 902 CA PRO A 138 8174 6851 6359 -1062 2408 -297

ATOM 903 C PRO A 138 -24.159 0.478 -26.677 1, 00 52.

ANISOU 903 C PRO A 138 7554 6675 5827 -1050 2141 -471

ATOM 904 O PRO A 138 -24.430 0.062 -27.803 1, 00 56. 53

ANISOU 904 O PRO A 138 8061 7351 6067 -1023 2116 -394

ATOM 905 CB PRO A 138 -25.590 2.513 -26.345 1, 00 55. 21

ANISOU 905 CB PRO A 138 8161 6677 6138 -824 2366 47

ATOM 906 CG PRO A 138 -25.561 3.806 -27.095 1, 00 59. 55

ANISOU 906 CG PRO A 138 8944 7062 6620 -774 2717 334

ATOM 907 CD PRO A 138 -24.545 3.607 -28.183 1, 00 59.

ANISOU 907 CD PRO A 138 8981 7225 6542 -932 2839 227

ATOM 908 N ASN A 139 -23.837 -0.311 -25.659 1, 00 45. 04

ANISOU 908 N ASN A 139 6401 5694 5017 -1082 1978 -704

ATOM 909 CA ASN A 139 -23.899 -1.761 -25.758 1, 00 42. 95

ANISOU 909 CA ASN A 139 6007 5601 4710 -1047 1783 561

ATOM 910 C ASN A 139 -24.677 -2.327 -24.583 1, 00 42.

ANISOU 910 C ASN A 139 5934 5579 4820 -944 1547 -884

ATOM 911 O ASN A 139 -24.465 -1.916 -23.442 1, 00 41. 91

ANISOU 911 O ASN A 139 5744 5321 4861 -957 1533 -926

ATOM 912 CB ASN A 139 -22.503 -2.377 -25.729 1, 00 42. 53

ANISOU 912 CB ASN A 139 5796 5585 4779 -1144 1872 -1111

ATOM 913 CG ASN A 139 -21.613 -1.879 -26.839 1, 00 47. 73

ANISOU 913 CG ASN A 139 6510 6272 5354 -1265 2127 -1121

ATOM 914 OD1 ASN A 139 -21.437 -2.549 -27.860 1, 00 49. 57

ANISOU 914 OD1 ASN A 139 6770 6626 5441 -1278 2181 -1176

ATOM 915 ND2 ASN A 139 -21.026 -0.706 -26.641 1, 00 47. 92

ANISOU 915 ND2 ASN A 139 6568 6175 5465 -1385 2319 -1090

ATOM 916 N LYS A 140 -25.567 -3.274 -24.855 1, 00 41. 64

ANISOU 916 N LYS A 140 5763 5538 4523 -878 1378 374 ATOM 917 CA LYS A 140 -26.184 -4.033 -23.786 1.00 43.97

ANISOU 917 CA LYS A 140 5979 5805 4924 -800 1180 -932

ATOM 918 C LYS A 140 -25.114 -4.971 -23.232 1.00 45.10

ANISOU 918 C LYS A 140 5982 5915 5238 -809 1196 -1160

ATOM 919 O LYS A 140 -24.606 -5.829 -23.949 1.00 46.44

ANISOU 919 O LYS A 140 6141 6144 5361 -839 1276 -1288

ATOM 920 CB LYS A 140 -27.391 -4.815 -24.309 1.00 49.47

ANISOU 920 CB LYS A 140 6709 6665 5420 -782 1034 -886

ATOM 921 CG LYS A 140 -28.305 -5.383 -23.210 1.00 56.13

ANISOU 921 CG LYS A 140 7499 7471 6357 -704 845 -888

ATOM 922 CD LYS A 140 -29.505 -6.117 -23.821 1.00 61.82

ANISOU 922 CD LYS A 140 8235 8404 6849 -755 721 -865

ATOM 923 CE LYS A 140 -30.315 -6.881 -22.774 1.00 63.97

ANISOU 923 CE LYS A 140 8456 8627 7222 -714 569 -913

ATOM 924 NZ LYS A 140 -29.514 -7.928 -22.070 1.00 64.27

ANISOU 924 NZ LYS A 140 8474 8482 7463 -703 616 -1134

ATOM 925 N VAL A 141 -24.741 -4.784 -21.969 1.00 43.57

ANISOU 925 N VAL A 141 5678 5646 5230 -778 1144 -1196

ATOM 926 CA VAL A 141 -23.692 -5.605 -21.367 1.00 41.08

ANISOU 926 CA VAL A 141 5179 5368 5063 -739 1155 -1345

ATOM 927 C VAL A 141 -24.256 -6.914 -20.837 1.00 39.84

ANISOU 927 C VAL A 141 5001 5188 4949 -605 1032 -1378

ATOM 928 O VAL A 141 -23.703 -7.986 -21.081 1.00 41.80

ANISOU 928 O VAL A 141 5197 5442 5241 -535 1117 -1473

ATOM 929 CB VAL A 141 -22.978 -4.871 -20.230 1.00 40.21

ANISOU 929 CB VAL A 141 4920 5277 5081 -795 1146 -1371

ATOM 930 CGI VAL A 141 -21.924 -5.768 -19.598 1.00 40.23

ANISOU 930 CGI VAL A 141 4669 5418 5200 -712 1133 -1465

ATOM 931 CG2 VAL A 141 -22.345 -3.612 -20.753 1.00 41.80

ANISOU 931 CG2 VAL A 141 5165 5464 5254 -976 1331 -1375

ATOM 932 N GLY A 142 -25.365 -6.827 -20.113 1.00 35.15

ANISOU 932 N GLY A 142 4464 4541 4350 -562 874 -1294

ATOM 933 CA GLY A 142 -25.976 -8.015 -19.567 1.00 31.23

ANISOU 933 CA GLY A 142 3972 4000 3895 -459 782 -1321

ATOM 934 C GLY A 142 -27.124 -7.753 -18.621 1.00 29.30

ANISOU 934 C GLY A 142 3762 3710 3661 -421 617 -1221

ATOM 935 O GLY A 142 -27.485 -6.613 -18.344 1.00 29.64

ANISOU 935 O GLY A 142 3835 3740 3686 -455 584 -1122

ATOM 936 N THR A 143 -27.698 -8.840 -18.125 1.00 30.19

ANISOU 936 N THR A 143 3890 3770 3811 -346 555 -1247

ATOM 937 CA THR A 143 -28.841 -8.777 -17.244 1.00 32.06

ANISOU 937 CA THR A 143 4155 3969 4056 -310 413 -1161

ATOM 938 C THR A 143 -28.522 -9.554 -15.979 1.00 31.95

ANISOU 938 C THR A 143 4062 3893 4184 -178 377 -1175

ATOM 939 O THR A 143 -28.113 -10.710 -16.039 1.00 35.31

ANISOU 939 O THR A 143 4485 4262 4668 -99 468 -1238

ATOM 940 CB THR A 143 -30.082 -9.386 -17.918 1.00 36.33

ANISOU 940 CB THR A 143 4796 4544 4462 -385 377 -1167

ATOM 941 OG1 THR A 143 -30.379 -8.662 -19.118 1.00 39.86

ANISOU 941 OG1 THR A 143 5286 5128 4731 -487 396 -1110

ATOM 942 CG2 THR A 143 -31.276 -9.328 -16.981 1.00 33.35

ANISOU 942 CG2 THR A 143 4419 4147 4104 -343 243 -1070

ATOM 943 N CYS A 144 -28.682 -8.900 -14.837 1.00 30.02

ANISOU 943 N CYS A 144 3765 3654 3985 -145 278 -1105

ATOM 944 CA CYS A 144 -28.452 -9.534 -13.556 1.00 30.35

ANISOU 944 CA CYS A 144 3722 3694 4116 -18 223 -1082

ATOM 945 C CYS A 144 -29.801 -9.897 -12.950 1.00 30.21

ANISOU 945 C CYS A 144 3802 3584 4093 9 138 -1024

ATOM 946 O CYS A 144 -30. 734 -9.095 -12.980 1.00 28.32 ANISOU 946 O CYS A 144 3625 3334 3799 -61 82 -971

ATOM 947 CB CYS A 144 -27. 702 -8.579 -12.631 1.00 31.90

ANISOU 947 CB CYS A 144 3787 4011 4321 -55 175 -1074

ATOM 948 SG CYS A 144 -27.137 -9.317 -11.078 1.00 38.90

ANISOU 948 SG CYS A 144 4501 5030 5251 104 93 -1017

ATOM 949 N VAL A 145 -29. 903 -11.111 -12.415 1.00 30.37

ANISOU 949 N VAL A 145 3833 3530 4176 126 161 -1015

ATOM 950 CA VAL A 145 -31.140 -11.587 -11.803 1.00 30.44

ANISOU 950 CA VAL A 145 3931 3446 4189 136 109 -972

ATOM 951 C VAL A 145 -30. 884 -12.112 -10.388 1.00 33.43

ANISOU 951 C VAL A 145 4254 3810 4637 300 80 -888

ATOM 952 O VAL A 145 -29. 908 -12.827 -10.143 1.00 36.32

ANISOU 952 O VAL A 145 4545 4192 5062 454 158 -856

ATOM 953 CB VAL A 145 -31.786 -12.720 -12.631 1.00 29.78

ANISOU 953 CB VAL A 145 3976 3251 4088 66 218 -1056

ATOM 954 CGI VAL A 145 -33. 149 -13.093 -12.054 1.00 27.49

ANISOU 954 CGI VAL A 145 3757 2903 3786 19 167 -1025

ATOM 955 CG2 VAL A 145 -31. 919 -12.314 -14.082 1.00 29.40

ANISOU 955 CG2 VAL A 145 3962 3290 3918 -103 245 -1137

ATOM 956 N SER A 146 -31.771 -11.750 -9.469 1.00 30.50

ANISOU 956 N SER A 146 3911 3430 4248 288 -16 -828

ATOM 957 CA SER A 146 -31. 723 -12.214 -8.093 1.00 30.05

ANISOU 957 CA SER A 146 3821 3380 4216 426 -51 -734

ATOM 958 C SER A 146 -33. 111 -12.710 -7.683 1.00 29.78

ANISOU 958 C SER A 146 3912 3207 4194 405 -49 -703

ATOM 959 O SER A 146 -34.095 -11.971 -7.808 1.00 25.49

ANISOU 959 O SER A 146 3405 2670 3612 289 -108 -712

ATOM 960 CB SER A 146 -31.283 -11.066 -7.179 1.00 29.02

ANISOU 960 CB SER A 146 3586 3423 4019 386 -159 -718

ATOM 961 OG SER A 146 -31.441 -11.410 -5.818 1.00 29.51

ANISOU 961 OG SER A 146 3626 3534 4054 485 -210 -626

ATOM 962 N GLU A 147 -33.192 -13.952 -7.202 1.00 31.01

ANISOU 962 N GLU A 147 4131 3239 4411 528 48 -649

ATOM 963 CA GLU A 147 -34. 477 -14.549 -6.828 1.00 31.66

ANISOU 963 CA GLU A 147 4338 3180 4511 477 87 -636

ATOM 964 C GLU A 147 -34. 581 -14.904 -5.354 1.00 28.15

ANISOU 964 C GLU A 147 3900 2719 4076 631 76 -496

ATOM 965 O GLU A 147 -33. 724 -15.607 -4.811 1.00 27.55

ANISOU 965 O GLU A 147 3798 2640 4030 836 148 -385

ATOM 966 CB GLU A 147 -34. 734 -15.825 -7.629 1.00 39.58

ANISOU 966 CB GLU A 147 5482 3984 5572 422 288 -723

ATOM 967 CG GLU A 147 -34.802 -15.633 -9.125 1.00 49.78

ANISOU 967 CG GLU A 147 6789 5317 6809 225 314 -881

ATOM 968 CD GLU A 147 -35.018 -16.946 -9.856 1.00 59.35

ANISOU 968 CD GLU A 147 8172 6324 8052 115 557 -1017

ATOM 969 OE1 GLU A 147 -34.319 -17.198 -10.865 1.00 62.38

ANISOU 969 OE1 GLU A 147 8591 6680 8429 76 678 -1123

ATOM 970 OE2 GLU A 147 -35. 885 -17.728 -9.412 1.00 62.50

ANISOU 970 OE2 GLU A 147 8687 6578 8480 43 661 -1034

ATOM 971 N GLY A 148 -35. 648 -14.439 -4.717 1.00 22.47

ANISOU 971 N GLY A 148 3208 2008 3321 552 3 -477

ATOM 972 CA GLY A 148 -36. 035 -14.963 -3.416 1.00 23.04

ANISOU 972 CA GLY A 148 3333 2029 3393 661 30 -357

ATOM 973 C GLY A 148 -35. 738 -14.061 -2.231 1.00 30.08

ANISOU 973 C GLY A 148 4140 3107 4182 711 -102 -286

ATOM 974 O GLY A 148 -35.564 -14.540 -1.109 1.00 33.36

ANISOU 974 O GLY A 148 4562 3562 4554 850 -91 -157

ATOM 975 N SER A 149 -35.679 -12.755 -2.462 1.00 22.86

ANISOU 975 N SER A 149 3162 2309 3213 586 -198 -370 ATOM 976 CA SER A 149 -35.346 -11.844 -1.380 1.00 25.47

ANISOU 976 CA SER A 149 3442 2807 3427 563 -277 -362

ATOM 977 C SER A 149 -36.582 -11.292 -0.674 1.00 21.34

ANISOU 977 C SER A 149 3013 2209 2885 492 -257 -359

ATOM 978 O SER A 149 -37.667 -11.217 -1.249 1.00 22.24

ANISOU 978 O SER A 149 3180 2193 3076 440 -211 -369

ATOM 979 CB SER A 149 -34.483 -10.693 -1.896 1.00 26.43

ANISOU 979 CB SER A 149 3478 3061 3502 444 -321 -472

ATOM 980 OG SER A 149 -35.209 -9.883 -2.800 1.00 24.28

ANISOU 980 OG SER A 149 3272 2666 3288 333 -279 -538

ATOM 981 N TYR A 150 -36.397 -10.930 0.588 1.00 26.38

ANISOU 981 N TYR A 150 3651 2971 3400 488 -286 -340

ATOM 982 CA TYR A 150 -37.325 -10.072 1.308 1.00 21.92

ANISOU 982 CA TYR A 150 3180 2353 2796 397 -236 -373

ATOM 983 C TYR A 150 -36.515 -9.313 2.348 1.00 24.53

ANISOU 983 C TYR A 150 3485 2897 2938 296 -270 -447

ATOM 984 O TYR A 150 -35.678 -9.905 3.026 1.00 26.44

ANISOU 984 O TYR A 150 3632 3363 3050 360 -354 -382

ATOM 985 CB TYR A 150 -38.460 -10.849 1.978 1.00 21.95

ANISOU 985 CB TYR A 150 3267 2242 2834 472 -179 -270

ATOM 986 CG TYR A 150 -39.539 -9.924 2.487 1.00 21.78

ANISOU 986 CG TYR A 150 3328 2138 2809 397 -89 -299

ATOM 987 CD1 TYR A 150 -39.450 -9.343 3.753 1.00 22.84

ANISOU 987 CD1 TYR A 150 3527 2355 2795 340 -55 -336

ATOM 988 CD2 TYR A 150 -40.625 -9.588 1.683 1.00 26.99

ANISOU 988 CD2 TYR A 150 3989 2671 3596 385 -20 -284

ATOM 989 CE1 TYR A 150 -40.425 -8.464 4.210 1.00 23.03

ANISOU 989 CE1 TYR A 150 3653 2264 2832 284 86 -369

ATOM 990 CE2 TYR A 150 -41.611 -8.715 2.134 1.00 27.40

ANISOU 990 CE2 TYR A 150 4099 2648 3663 371 102 -270

ATOM 991 CZ TYR A 150 -41.501 -8.159 3.394 1.00 28.96

ANISOU 991 CZ TYR A 150 4398 2859 3747 327 174 -319

ATOM 992 OH TYR A 150 -42.470 -7.299 3.834 1.00 34.59

ANISOU 992 OH TYR A 150 5193 3458 4491 327 350 -309

ATOM 993 N PRO A 151 -36.679 -7.978 2.411 1.00 27.27

ANISOU 993 N PRO A 151 3907 3199 3255 127 -183 -581

ATOM 994 CA PRO A 151 -37.387 -7.120 1.442 1.00 26.54

ANISOU 994 CA PRO A 151 3892 2884 3307 93 -64 -613

ATOM 995 C PRO A 151 -36.672 -7.147 0.095 1.00 27.30

ANISOU 995 C PRO A 151 3899 2994 3479 96 -113 -632

ATOM 996 O PRO A 151 -35.674 -7.854 -0.027 1.00 29.33

ANISOU 996 O PRO A 151 4039 3410 3694 129 -222 -629

ATOM 997 CB PRO A 151 -37.279 -5.704 2.048 1.00 23.72

ANISOU 997 CB PRO A 151 3658 2492 2864 -93 90 -762

ATOM 998 CG PRO A 151 -36.913 -5.918 3.485 1.00 27.84

ANISOU 998 CG PRO A 151 4183 3219 3178 -180 43 -817

ATOM 999 CD PRO A 151 -36.111 -7.197 3.524 1.00 28.65

ANISOU 999 CD PRO A 151 4104 3563 3220 -55 -165 -708

ATOM 1000 N ALA A 152 -37.174 -6.413 -0.894 1.00 29.36

ANISOU 1000 N ALA A 152 4207 3107 3841 88 -18 -623

ATOM 1001 CA ALA A 152 -36.650 -6.507 -2.259 1.00 27.61

ANISOU 1001 CA ALA A 152 3913 2900 3678 97 -56 -622

ATOM 1002 C ALA A 152 -35.123 -6.439 -2.332 1.00 26.87

ANISOU 1002 C ALA A 152 3731 2968 3510 1 -113 -733

ATOM 1003 O ALA A 152 -34.479 -7.296 -2.942 1.00 28.84

ANISOU 1003 O ALA A 152 3874 3304 3780 66 -199 -714

ATOM 1004 CB ALA A 152 -37.276 -5.434 -3.147 1.00 20.80

ANISOU 1004 CB ALA A 152 3120 1899 2885 98 82 -574

ATOM 1005 N GLY A 153 -34.549 -5.434 -1.686 1.00 25.17 ANISOU 1005 N GLY A 153 3556 2804 3201 -170 -37 -860 N

ATOM 1006 CA GLY A 153 -33.131 -5.165 -1.826 1.00 29.31 C

ANISOU 1006 CA GLY A 153 3966 3528 3642 -317 -71 -984 C

ATOM 1007 C GLY A 153 -32.882 -4.511 -3.174 1.00 29.71 C ANISOU 1007 C GLY A 153 4050 3455 3785 -362 29 -1008 C

ATOM 1008 O GLY A 153 -33.829 -4.088 -3.836 1.00 30.39 O

ANISOU 1008 O GLY A 153 4257 3321 3968 -285 135 -921 O

ATOM 1009 N THR A 154 -31.621 -4.424 -3.583 1.00 29.71 N

ANISOU 1009 N THR A 154 3922 3628 3740 -473 1 -1101 N ATOM 1010 CA THR A 154 -31.265 -3.777 -4.847 1.00 30.93 C

ANISOU 1010 CA THR A 154 4112 3676 3962 -534 115 -1129 C

ATOM 1011 C THR A 154 -30.103 -4.489 -5.558 1.00 31.81 C

ANISOU 1011 C THR A 154 4022 3994 4070 -508 15 -1143 C

ATOM 1012 O THR A 154 -29.270 -5.142 -4.923 1.00 31.48 O ANISOU 1012 O THR A 154 3787 4223 3949 -497 -107 -1162 O

ATOM 1013 CB THR A 154 -30.873 -2.294 -4.638 1.00 35.13 C

ANISOU 1013 CB THR A 154 4777 4121 4451 -809 336 -1292 C

ATOM 1014 OG1 THR A 154 -29.892 -2.204 -3.601 1.00 42.04 O

ANISOU 1014 OG1 THR A 154 5525 5283 5167 -1038 282 -1468 O ATOM 1015 CG2 THR A 154 -32.083 -1.441 -4.244 1.00 34.73 C

ANISOU 1015 CG2 THR A 154 4976 3768 4450 -790 537 -1250 C

ATOM 1016 N LEU A 155 -30.060 -4.355 -6.879 1.00 29.36 N

ANISOU 1016 N LEU A 155 3746 3574 3833 -476 82 -1109 N

ATOM 1017 CA LEU A 155 -28.926 -4.814 -7.672 1.00 33.12 C ANISOU 1017 CA LEU A 155 4061 4209 4314 -477 53 -1144 C

ATOM 1018 C LEU A 155 -28.078 -3.619 -8.124 1.00 36.10 C

ANISOU 1018 C LEU A 155 4453 4597 4665 -718 210 -1275 C

ATOM 1019 O LEU A 155 -28.608 -2.538 -8.371 1.00 34.22 O

ANISOU 1019 O LEU A 155 4417 4136 4449 -813 382 -1282 O ATOM 1020 CB LEU A 155 -29.420 -5.585 -8.899 1.00 30.38 C

ANISOU 1020 CB LEU A 155 3755 3751 4038 -310 41 -1042 C

ATOM 1021 CG LEU A 155 -30.194 -6.878 -8.634 1.00 27.14 C

ANISOU 1021 CG LEU A 155 3345 3306 3660 -120 -62 -947 C

ATOM 1022 CD1 LEU A 155 -30.747 -7.450 -9.935 1.00 22.01 C ANISOU 1022 CD1 LEU A 155 2761 2562 3038 -60 -36 -905 C

ATOM 1023 CD2 LEU A 155 -29.301 -7.891 -7.938 1.00 25.37 C

ANISOU 1023 CD2 LEU A 155 2950 3260 3429 -14 -136 -939 C

ATOM 1024 N SER A 156 -26.765 -3.815 -8.229 1.00 38.80 N

ANISOU 1024 N SER A 156 4581 5196 4965 -808 182 -1362 N ATOM 1025 CA SER A 156 -25.876 -2.787 -8.778 1.00 39.78 C

ANISOU 1025 CA SER A 156 4700 5347 5069 -1065 349 -1499 C

ATOM 1026 C SER A 156 -24.694 -3.395 -9.553 1.00 36.76 C

ANISOU 1026 C SER A 156 4079 5190 4697 -1028 320 -1509 C

ATOM 1027 O SER A 156 -24.342 -4.557 -9.360 1.00 37.23 O ANISOU 1027 O SER A 156 3940 5443 4762 -825 179 -1429 O

ATOM 1028 CB SER A 156 -25.384 -1.844 -7.673 1.00 40.06 C

ANISOU 1028 CB SER A 156 4712 5520 4988 -1392 419 -1690 C

ATOM 1029 OG SER A 156 -24.700 -2.567 -6.664 1.00 42.83 O

ANISOU 1029 OG SER A 156 4773 6281 5219 -1391 222 -1714 O ATOM 1030 N TRP A 157 -24.084 -2.613 -10.434 1.00 36.42 N

ANISOU 1030 N TRP A 157 4070 5102 4666 -1208 492 -1593 N

ATOM 1031 CA TRP A 157 -23.028 -3.150 -11.291 1.00 40.14 C

ANISOU 1031 CA TRP A 157 4335 5758 5159 -1164 503 -1598 C

ATOM 1032 C TRP A 157 -21.645 -2.616 -10.930 1.00 42.04 C ANISOU 1032 C TRP A 157 4314 6339 5320 -1451 555 -1765 C

ATOM 1033 O TRP A 157 -21.512 -1.518 -10.384 1.00 41.18 O

ANISOU 1033 O TRP A 157 4275 6230 5140 -1778 665 -1924 O

ATOM 1034 CB TRP A 157 -23.324 -2.864 -12.763 1.00 31.53 C

ANISOU 1034 CB TRP A 157 3444 4411 4124 -1127 657 -1545 C ATOM 1035 CG TRP A 157 -24.517 -3.590 -13.304 1.00 29.36 C

ANISOU 1035 CG TRP A 157 3335 3934 3885 -869 584 -1390 C

ATOM 1036 CD1 TRP A 157 -25.817 -3.187 -13.244 1.00 28.11 C

ANISOU 1036 CD1 TRP A 157 3405 3549 3727 -813 589 -1292 C ATOM 1037 CD2 TRP A 157 -24.515 -4.844 -14.005 1.00 31.52 C

ANISOU 1037 CD2 TRP A 157 3551 4239 4186 -660 524 -1329 C

ATOM 1038 NE1 TRP A 157 -26.628 -4.111 -13.866 1.00 28.81 N

ANISOU 1038 NE1 TRP A 157 3545 3581 3818 -614 502 -1182 N

ATOM 1039 CE2 TRP A 157 -25.855 -5.135 -14.333 1.00 27.12 C ANISOU 1039 CE2 TRP A 157 3187 3498 3619 -541 476 -1224 C

ATOM 1040 CE3 TRP A 157 -23.513 -5.744 -14.379 1.00 33.39 C

ANISOU 1040 CE3 TRP A 157 3594 4641 4453 -569 540 -1355 C

ATOM 1041 CZ2 TRP A 157 -26.214 -6.291 -15.028 1.00 26.61 C

ANISOU 1041 CZ2 TRP A 157 3147 3409 3554 -399 446 -1191 C ATOM 1042 CZ3 TRP A 157 -23.875 -6.894 -15.067 1.00 33.40 C

ANISOU 1042 CZ3 TRP A 157 3656 4554 4481 -383 546 -1307 C

ATOM 1043 CH2 TRP A 157 -25.215 -7.156 -15.384 1.00 30.72 C

ANISOU 1043 CH2 TRP A 157 3532 4029 4112 -332 499 -1248 C

ATOM 1044 N HIS A 158 -20.618 -3.402 -11.242 1.00 41.38 N ANISOU 1044 N HIS A 158 3925 6552 5243 -1342 504 -1735 N

ATOM 1045 CA HIS A 158 -19.248 -2.982 -10.987 1.00 44.34 C

ANISOU 1045 CA HIS A 158 3975 7342 5531 -1608 541 -1874 C

ATOM 1046 C HIS A 158 -18.361 -3.209 -12.198 1.00 43.94 C

ANISOU 1046 C HIS A 158 3793 7352 5551 -1564 670 -1866 C ATOM 1047 O HIS A 158 -18.509 -4.199 -12.908 1.00 39.23 O

ANISOU 1047 O HIS A 158 3213 6645 5048 -1238 660 -1725 O

ATOM 1048 CB HIS A 158 -18.683 -3.726 -9.779 1.00 48.81 C

ANISOU 1048 CB HIS A 158 4162 8398 5986 -1511 326 -1812 C

ATOM 1049 CG HIS A 158 -19.530 -3.612 -8.555 1.00 50.47 C ANISOU 1049 CG HIS A 158 4493 8579 6105 -1540 197 -1812 C

ATOM 1050 ND1 HIS A 158 -19.237 -2.750 -7.520 1.00 54.21 N

ANISOU 1050 ND1 HIS A 158 4884 9320 6395 -1926 182 -2001 N

ATOM 1051 CD2 HIS A 158 -20.676 -4.247 -8.199 1.00 47.69 C

ANISOU 1051 CD2 HIS A 158 4348 7965 5807 -1262 98 -1665 C ATOM 1052 CE1 HIS A 158 -20.156 -2.860 -6.579 1.00 53.48 C

ANISOU 1052 CE1 HIS A 158 4948 9124 6248 -1860 81 -1960 C

ATOM 1053 NE2 HIS A 158 -21.042 -3.763 -6.970 1.00 50.85 N

ANISOU 1053 NE2 HIS A 158 4784 8470 6067 -1449 25 -1747 N

ATOM 1054 N LEU A 159 -17.439 -2.280 -12.427 1.00 48.37 N ANISOU 1054 N LEU A 159 4239 8080 6059 -1924 823 -2040 N

ATOM 1055 CA LEU A 159 -16.476 -2.396 -13.517 1.00 49.11 C

ANISOU 1055 CA LEU A 159 4176 8278 6207 -1928 970 -2052 C

ATOM 1056 C LEU A 159 -15.068 -2.350 -12.947 1.00 56.59 C

ANISOU 1056 C LEU A 159 4620 9831 7052 -2133 935 -2147 C ATOM 1057 O LEU A 159 -14.681 -1.366 -12.311 1.00 58.87 O

ANISOU 1057 O LEU A 159 4905 10266 7198 -2514 965 -2319 O

ATOM 1058 CB LEU A 159 -16.667 -1.269 -14.534 1.00 46.55 C

ANISOU 1058 CB LEU A 159 4187 7583 5915 -2180 1241 -2153 C

ATOM 1059 CG LEU A 159 -15.599 -1.129 -15.627 1.00 46.37 C ANISOU 1059 CG LEU A 159 4022 7672 5923 -2285 1440 -2207 C

ATOM 1060 CD1 LEU A 159 -15.616 -2.325 -16.549 1.00 45.07 C

ANISOU 1060 CD1 LEU A 159 3829 7452 5844 -1881 1415 -2041 C

ATOM 1061 CD2 LEU A 159 -15.789 0.148 -16.419 1.00 46.89 C

ANISOU 1061 CD2 LEU A 159 4440 7381 5996 -2577 1734 -2298 C ATOM 1062 N ASP A 160 -14.316 -3.425 -13.175 1.00 60.82 N

ANISOU 1062 N ASP A 160 4806 10670 7633 -1821 878 -1997 N

ATOM 1063 CA ASP A 160 -12.949 -3.568 -12.669 1.00 69.57 C

ANISOU 1063 CA ASP A 160 5453 12358 8621 -1865 801 -1970 C

ATOM 1064 C ASP A 160 -12.837 -3.313 -11.163 1.00 73.63 C ANISOU 1064 C ASP A 160 5860 13205 8911 -1998 580 -1976

ATOM 1065 O ASP A 160 -11.894 -2.670 -10 699 1, 00 78. 02

ANISOU 1065 O ASP A 160 6269 14096 9277 -2277 566 -2074

ATOM 1066 CB ASP A 160 -11.967 -2.686 -13 454 1, 00 74. 06

ANISOU 1066 CB ASP A 160 6022 12958 9159 -2180 997 -2120

ATOM 1067 CG ASP A 160 -11.764 -3.168 -14 887 1, 00 76. 65

ANISOU 1067 CG ASP A 160 6363 13092 9669 -1984 1207 -2063

ATOM 1068 OD1 ASP A 160 -12.131 -4.327 -15 185 1, 00 73. 61

ANISOU 1068 OD1 ASP A 160 5915 12641 9412 -1569 1202 -1901

ATOM 1069 OD2 ASP A 160 -11.230 -2.394 -15 714 1, 00 80. 17

ANISOU 1069 OD2 ASP A 160 6912 13435 10115 -2241 1405 -21?

ATOM 1070 N GLY A 161 -13.812 -3.820 -10 414 1, 00 71. 27

ANISOU 1070 N GLY A 161 5644 12820 8617 -1808 426 -1882

ATOM 1071 CA GLY A 161 -13.800 -3.734 -8 965 1, 00 74. 14

ANISOU 1071 CA GLY A 161 5923 13494 8754 -1880 225 -1855

ATOM 1072 C GLY A 161 -14.147 -2.369 -8 398 1, 00 73.

ANISOU 1072 C GLY A 161 6192 13304 8556 -2360 302 -2121

ATOM 1073 O GLY A 161 -13.719 -2.021 -7 299 1, 00 79.

ANISOU 1073 O GLY A 161 6854 14422 9071 -2546 215 -2172

ATOM 1074 N LYS A 162 -14.915 -1.589 -9 147 1, 00 66. 84

ANISOU 1074 N LYS A 162 5701 11887 7808 -2543 507 -2276

ATOM 1075 CA LYS A 162 -15.363 -0.282 -8 684 1, 00 62. 39

ANISOU 1075 CA LYS A 162 5506 11060 7138 -2921 667 -2491

ATOM 1076 C LYS A 162 -16.827 -0.085 -9 064 1, 00 54. 92

ANISOU 1076 C LYS A 162 4981 9510 6376 -2840 762 -247?

ATOM 1077 O LYS A 162 -17.269 -0.578 -10 099 1, 00 50. 60

ANISOU 1077 O LYS A 162 4488 8705 6034 -2640 796 -23?

ATOM 1078 CB LYS A 162 -14.488 0.833 -9 268 1, 00 65. 62

ANISOU 1078 CB LYS A 162 5997 11447 7487 -3283 926 -2692

ATOM 1079 CG LYS A 162 -13.032 0.759 -8 828 1, 00 71. 69

ANISOU 1079 CG LYS A 162 6353 12844 8041 -3419 837 -2730

ATOM 1080 CD LYS A 162 -12.259 2.035 -9 117 1, 00 76.

ANISOU 1080 CD LYS A 162 7047 13402 8494 -3863 1108 -2990

ATOM 1081 CE LYS A 162 -10.845 1.950 -8 541 1, 00 82. 41

ANISOU 1081 CE LYS A 162 7396 14887 9028 -4027 996 -3036

ATOM 1082 NZ LYS A 162 -10.038 3.184 -8 775 1, 00 85.

ANISOU 1082 NZ LYS A 162 7930 15353 9321 -4500 1268 -3323

ATOM 1083 N PRO A 163 -17.588 0.624 -8 217 1, 00 54.

ANISOU 1083 N PRO A 163 5282 9305 6304 -2987 823 -2556

ATOM 1084 CA PRO A 163 -19.019 0.826 -8 479 1, 00 51. 16

ANISOU 1084 CA PRO A 163 5198 8258 5981 -2870 911 -2504

ATOM 1085 C PRO A 163 -19.269 1.545 -9 803 1, 00 49. 46

ANISOU 1085 C PRO A 163 5286 7580 5927 -2925 1198 -2517

ATOM 1086 O PRO A 163 -18.503 2.416 -10 197 1, 00 53. 03

ANISOU 1086 O PRO A 163 5789 8032 6328 -3169 1426 -2637

ATOM 1087 CB PRO A 163 -19.475 1.694 -7 298 1, 00 51. 94

ANISOU 1087 CB PRO A 163 5527 8271 5938 -3067 1012 -2600

ATOM 1088 CG PRO A 163 -18.472 1.427 -6 222 1, 00 53. il

ANISOU 1088 CG PRO A 163 5405 9115 5925 -3198 841 -2659

ATOM 1089 CD PRO A 163 -17.171 1.226 -6 938 1, 00 55. 10

ANISOU 1089 CD PRO A 163 5256 9617 6062 -3252 827 -2683

ATOM 1090 N LEU A 164 -20.340 1.160 -10 481 1, 00 47. 25

ANISOU 1090 N LEU A 164 5219 6923 5812 -2661 1187 -2367

ATOM 1091 CA LEU A 164 -20.695 1.728 -11 769 1, 00 47. 23

ANISOU 1091 CA LEU A 164 5513 6504 5926 -2603 1433 -2281

ATOM 1092 C LEU A 164 -21.979 2.541 -11 591 1, 00 52.

ANISOU 1092 C LEU A 164 6578 6665 6619 -2565 1614 -2212

ATOM 1093 O LEU A 164 -23.055 1.982 -11 373 1, 00 52. 24

ANISOU 1093 O LEU A 164 6662 6537 6651 -2249 1454 -2034 ATOM 1094 CB LEU A 164 -20.895 0.592 -12.770 1.00 43.12

ANISOU 1094 CB LEU A 164 4913 5987 5482 -2190 1272 -2057

ATOM 1095 CG LEU A 164 -20.792 0.827 -14.273 1.00 43.93

ANISOU 1095 CG LEU A 164 5159 5889 5645 -2130 1458 -1970

ATOM 1096 CD1 LEU A 164 -19.542 1.610 -14.636 1.00 48.29

ANISOU 1096 CD1 LEU A 164 5612 6564 6173 -2494 1691 -2156

ATOM 1097 CD2 LEU A 164 -20.790 -0.508 -14.978 1.00 39.61

ANISOU 1097 CD2 LEU A 164 4461 5463 5127 -1791 1273 -1827

ATOM 1098 N VAL A 165 -21.853 3.864 -11.665 1.00 55.67

ANISOU 1098 N VAL A 165 7265 6854 7035 -2804 1963 -2295

ATOM 1099 CA VAL A 165 -22.968 4.774 -11.399 1.00 57.25

ANISOU 1099 CA VAL A 165 7851 6623 7277 -2725 2202 -2192

ATOM 1100 C VAL A 165 -23.825 5.031 -12.640 1.00 58.58

ANISOU 1100 C VAL A 165 8308 6363 7587 -2493 2388 -1954

ATOM 1101 O VAL A 165 -23.321 5.502 -13.662 1.00 61.15

ANISOU 1101 O VAL A 165 8712 6584 7936 -2564 2603 -1927

ATOM 1102 CB VAL A 165 -22.468 6.130 -10.854 1.00 62.51

ANISOU 1102 CB VAL A 165 8681 7230 7839 -3021 2546 -2358

ATOM 1103 CGI VAL A 165 -23.640 7.036 -10.525 1.00 61.68

ANISOU 1103 CGI VAL A 165 8953 6693 7789 -2901 2828 -2237

ATOM 1104 CG2 VAL A 165 -21.593 5.929 -9.627 1.00 63.41

ANISOU 1104 CG2 VAL A 165 8511 7816 7767 -3281 2378 -2584

ATOM 1105 N PRO A 166 -25.132 4.735 -12.548 1.00 57.67

ANISOU 1105 N PRO A 166 8327 6058 7528 -2163 2297 -1731

ATOM 1106 CA PRO A 166 -26.029 4.923 -13.694 1.00 60.05

ANISOU 1106 CA PRO A 166 8819 6112 7886 -1823 2403 -1396

ATOM 1107 C PRO A 166 -26.142 6.389 -14.102 1.00 67.61

ANISOU 1107 C PRO A 166 10146 6633 8908 -1922 2914 -1328

ATOM 1108 O PRO A 166 -25.964 7.269 -13.259 1.00 69.61

ANISOU 1108 O PRO A 166 10514 6807 9128 -2098 3132 -1484

ATOM 1109 CB PRO A 166 -27.377 4.416 -13.171 1.00 57.74

ANISOU 1109 CB PRO A 166 8543 5784 7612 -1501 2209 -1205

ATOM 1110 CG PRO A 166 -27.037 3.516 -12.015 1.00 56.29

ANISOU 1110 CG PRO A 166 8111 5901 7377 -1606 1896 -1415

ATOM 1111 CD PRO A 166 -25.827 4.149 -11.389 1.00 57.65

ANISOU 1111 CD PRO A 166 8251 6152 7502 -2053 2059 -1742

ATOM 1112 N ASN A 167 -26.424 6.625 -15.383 1.00 72.19

ANISOU 1112 N ASN A 167 10838 7096 9496 -1694 3041 -1045

ATOM 1113 CA ASN A 167 -26.691 7.961 -15.934 1.00 79.33

ANISOU 1113 CA ASN A 167 12096 7594 10451 -1637 3527 -864

ATOM 1114 C ASN A 167 -25.466 8.858 -16.146 1.00 81.37

ANISOU 1114 C ASN A 167 12421 7827 10667 -1935 3795 -1118

ATOM 1115 O ASN A 167 -25.584 9.962 -16.677 1.00 84.34

ANISOU 1115 O ASN A 167 13062 7919 11063 -1824 4154 -1000

ATOM 1116 CB ASN A 167 -27.774 8.705 -15.129 1.00 87.87

ANISOU 1116 CB ASN A 167 13376 8438 11574 -1418 3703 -750

ATOM 1117 CG ASN A 167 -29.102 7.967 -15.103 1.00 91.37

ANISOU 1117 CG ASN A 167 13772 8890 12056 -1057 3482 -431

ATOM 1118 OD1 ASN A 167 -29.148 6.749 -14.942 1.00 90.75

ANISOU 1118 OD1 ASN A 167 13402 9164 11916 -1015 3028 -494

ATOM 1119 ND2 ASN A 167 -30.192 8.707 -15.277 1.00 95.45

ANISOU 1119 ND2 ASN A 167 14453 9210 12604 -688 3698 -109

ATOM 1120 N GLU A 168 -24.295 8.379 -15.741 1.00 81.75

ANISOU 1120 N GLU A 168 12213 8194 10655 -2286 3620 -1454

ATOM 1121 CA GLU A 168 -23.056 9.115 -15.957 1.00 87.23

ANISOU 1121 CA GLU A 168 12923 8933 11287 -2593 3842 -1704

ATOM 1122 C GLU A 168 -22.052 8.261 -16.721 1.00 84.70

ANISOU 1122 C GLU A 168 12311 8928 10943 -2727 3635 -1778

ATOM 1123 O GLU A 168 -22.060 7.035 -16.606 1.00 80.86 ANISOU 1123 0 GLU A 168 11534 8725 10464 -2689 3287 -1773 0

ATOM 1124 CB GLU A 168 -22.448 9.537 -14.622 1.00 91.82 C

ANISOU 1124 CB GLU A 168 13431 9693 11762 -2920 3881 -2049 C

ATOM 1125 CG GLU A 168 -23.445 9.565 -13.492 1.00 94.84 C ANISOU 1125 CG GLU A 168 13885 10002 12146 -2806 3839 -2003 C

ATOM 1126 CD GLU A 168 -22.852 10.074 -12.199 1.00100.28 C

ANISOU 1126 CD GLU A 168 14527 10882 12692 -3157 3928 -2318 C

ATOM 1127 OE1 GLU A 168 -21.664 9.789 -11.940 1.00101.94 O

ANISOU 1127 OE1 GLU A 168 14471 11480 12783 -3464 3786 -2567 O ATOM 1128 OE2 GLU A 168 -23.577 10.767 -11.451 1.00102.60 O

ANISOU 1128 OE2 GLU A 168 15043 10962 12979 -3123 4155 -2305 O

ATOM 1129 N LYS A 169 -21.191 8.916 -17.495 1.00 88.47 N

ANISOU 1129 N LYS A 169 12868 9350 11398 -2873 3871 -1853 N

ATOM 1130 CA LYS A 169 -20.122 8.240 -18.239 1.00 88.45 C ANISOU 1130 CA LYS A 169 12586 9656 11366 -3010 3733 -1938 C

ATOM 1131 C LYS A 169 -20.647 7.229 -19.260 1.00 79.69 C

ANISOU 1131 C LYS A 169 11383 8615 10281 -2742 3570 -1644 C

ATOM 1132 O LYS A 169 -20.014 6.204 -19.502 1.00 80.98 O

ANISOU 1132 O LYS A 169 11216 9133 10421 -2794 3353 -1724 O ATOM 1133 CB LYS A 169 -19.127 7.571 -17.274 1.00 91.86 C

ANISOU 1133 CB LYS A 169 12611 10570 11722 -3274 3458 -2251 C

ATOM 1134 CG LYS A 169 -18.355 8.550 -16.396 1.00 97.73 C

ANISOU 1134 CG LYS A 169 13397 11382 12354 -3607 3641 -2557 C

ATOM 1135 CD LYS A 169 -17.810 7.884 -15.138 1.00 98.57 C ANISOU 1135 CD LYS A 169 13127 11982 12344 -3772 3329 -2761 C

ATOM 1136 CE LYS A 169 -16.345 7.496 -15.278 1.00100.79 C

ANISOU 1136 CE LYS A 169 13027 12733 12534 -3995 3202 -2947 C

ATOM 1137 NZ LYS A 169 -15.805 6.947 -14.000 1.00100.99 N

ANISOU 1137 NZ LYS A 169 12686 13274 12410 -4125 2914 -3099 N ATOM 1138 N GLY A 170 -21.802 7.529 -19.853 1.00 72.99 N

ANISOU 1138 N GLY A 170 10812 7477 9445 -2429 3696 -1294 N

ATOM 1139 CA GLY A 170 -22.416 6.663 -20.848 1.00 66.63 C

ANISOU 1139 CA GLY A 170 9930 6832 8555 -2078 3473 -1006 C

ATOM 1140 C GLY A 170 -22.966 5.360 -20.285 1.00 59.43 C ANISOU 1140 C GLY A 170 8753 6212 7615 -1865 2989 -1022 C

ATOM 1141 O GLY A 170 -23.056 4.349 -20.984 1.00 57.78 O

ANISOU 1141 O GLY A 170 8381 6251 7320 -1679 2732 -945 O

ATOM 1142 N VAL A 171 -23.337 5.384 -19.012 1.00 54.93 N

ANISOU 1142 N VAL A 171 8166 5595 7111 -1912 2899 -1135 N ATOM 1143 CA VAL A 171 -23.849 4.198 -18.343 1.00 48.96 C

ANISOU 1143 CA VAL A 171 7183 5079 6339 -1729 2482 -1153 C

ATOM 1144 C VAL A 171 -25.332 4.332 -18.044 1.00 45.80 C

ANISOU 1144 C VAL A 171 6951 4503 5950 -1442 2438 -905 C

ATOM 1145 O VAL A 171 -25.757 5.304 -17.439 1.00 46.67 O ANISOU 1145 O VAL A 171 7286 4320 6128 -1490 2691 -877 O

ATOM 1146 CB VAL A 171 -23.132 3.969 -17.017 1.00 46.25 C

ANISOU 1146 CB VAL A 171 6635 4909 6030 -1989 2364 -1462 C

ATOM 1147 CGI VAL A 171 -23.706 2.743 -16.310 1.00 40.60 C

ANISOU 1147 CGI VAL A 171 5718 4405 5301 -1764 1969 -1438 C ATOM 1148 CG2 VAL A 171 -21.633 3.835 -17.249 1.00 45.54 C

ANISOU 1148 CG2 VAL A 171 6306 5075 5920 -2271 2400 -1692 C

ATOM 1149 N SER A 172 -26.122 3.352 -18.461 1.00 43.74 N

ANISOU 1149 N SER A 172 6578 4422 5619 -1160 2146 -736 N

ATOM 1150 CA SER A 172 -27.543 3.369 -18.150 1.00 43.90 C ANISOU 1150 CA SER A 172 6686 4357 5638 -895 2071 -501 C

ATOM 1151 C SER A 172 -27.983 2.018 -17.596 1.00 38.98 C

ANISOU 1151 C SER A 172 5839 3977 4994 -789 1681 -570 C

ATOM 1152 O SER A 172 -27.465 0.969 -17.987 1.00 35.80 O

ANISOU 1152 O SER A 172 5253 3806 4542 -807 1481 -679 O ATOM 1153 CB SER A 172 -28.360 3.718 -19.391 1.00 47.48 C

ANISOU 1153 CB SER A 172 7258 4798 5983 -642 2166 -139 C

ATOM 1154 OG SER A 172 -28.312 2.655 -20.330 1.00 49.17 O

ANISOU 1154 OG SER A 172 7300 5328 6054 -582 1915 -125 O ATOM 1155 N VAL A 173 -28.944 2.052 -16.681 1.00 37.62 N

ANISOU 1155 N VAL A 173 5703 3721 4869 -673 1618 -501 N

ATOM 1156 CA VAL A 173 -29.454 0.836 -16.073 1.00 38.00 C

ANISOU 1156 CA VAL A 173 5576 3955 4908 -577 1294 -550 C

ATOM 1157 C VAL A 173 -30.974 0.872 -16.105 1.00 38.07 C ANISOU 1157 C VAL A 173 5635 3941 4888 -328 1246 -282 C

ATOM 1158 O VAL A 173 -31.575 1.932 -15.920 1.00 37.29 O

ANISOU 1158 O VAL A 173 5706 3627 4835 -236 1476 -109 O

ATOM 1159 CB VAL A 173 -28.943 0.682 -14.612 1.00 36.37 C

ANISOU 1159 CB VAL A 173 5297 3744 4776 -736 1231 -791 C ATOM 1160 CGI VAL A 173 -29.628 -0.479 -13.897 1.00 27.86 C

ANISOU 1160 CGI VAL A 173 4086 2801 3697 -600 948 -788 C

ATOM 1161 CG2 VAL A 173 -27.438 0.490 -14.598 1.00 34.80 C

ANISOU 1161 CG2 VAL A 173 4953 3694 4575 -966 1232 -1030 C

ATOM 1162 N LYS A 174 -31.582 -0.282 -16.378 1.00 34.09 N ANISOU 1162 N LYS A 174 4982 3665 4307 -226 981 -244 N

ATOM 1163 CA LYS A 174 -33.020 -0.462 -16.230 1.00 29.29 C

ANISOU 1163 CA LYS A 174 4344 3122 3661 -33 882 -33 C

ATOM 1164 C LYS A 174 -33.261 -1.580 -15.231 1.00 29.24 C

ANISOU 1164 C LYS A 174 4221 3187 3703 -58 656 -193 C ATOM 1165 O LYS A 174 -32.548 -2.594 -15.229 1.00 28.02 O

ANISOU 1165 O LYS A 174 3971 3132 3544 -156 521 -388 O

ATOM 1166 CB LYS A 174 -33.693 -0.792 -17.565 1.00 30.60 C

ANISOU 1166 CB LYS A 174 4434 3550 3642 69 794 172 C

ATOM 1167 CG LYS A 174 -33.567 0.300 -18.615 1.00 33.97 C ANISOU 1167 CG LYS A 174 4975 3943 3989 145 1022 404 C

ATOM 1168 CD LYS A 174 -34.268 1.572 -18.175 1.00 40.66 C

ANISOU 1168 CD LYS A 174 5964 4558 4926 341 1276 674 C

ATOM 1169 CE LYS A 174 -33.924 2.748 -19.093 1.00 49.39 C

ANISOU 1169 CE LYS A 174 7243 5529 5994 417 1592 900 C ATOM 1170 NZ LYS A 174 -32.527 3.265 -18.894 1.00 49.94 N

ANISOU 1170 NZ LYS A 174 7473 5320 6182 169 1810 635 N

ATOM 1171 N GLU A 175 -34.271 -1.390 -14.388 1.00 26.32 N

ANISOU 1171 N GLU A 175 3868 2749 3384 54 650 -87 N

ATOM 1172 CA GLU A 175 -34.536 -2.296 -13.284 1.00 28.45 C ANISOU 1172 CA GLU A 175 4062 3042 3706 36 483 -217 C

ATOM 1173 C GLU A 175 -35.966 -2.802 -13.324 1.00 26.78 C

ANISOU 1173 C GLU A 175 3764 2969 3444 169 364 -48 C

ATOM 1174 O GLU A 175 -36.861 -2.165 -13.888 1.00 27.73 O

ANISOU 1174 O GLU A 175 3876 3152 3507 310 436 205 O ATOM 1175 CB GLU A 175 -34.275 -1.596 -11.943 1.00 31.93 C

ANISOU 1175 CB GLU A 175 4606 3275 4251 -20 608 -313 C

ATOM 1176 CG GLU A 175 -32.890 -0.976 -11.851 1.00 41.85 C

ANISOU 1176 CG GLU A 175 5924 4446 5531 -214 745 -499 C

ATOM 1177 CD GLU A 175 -32.637 -0.273 -10.538 1.00 49.88 C ANISOU 1177 CD GLU A 175 7044 5310 6598 -346 879 -639 C

ATOM 1178 OE1 GLU A 175 -33.601 0.232 -9.918 1.00 51.54 O

ANISOU 1178 OE1 GLU A 175 7367 5366 6850 -251 991 -537 O

ATOM 1179 OE2 GLU A 175 -31.460 -0.228 -10.125 1.00 54.80 O

ANISOU 1179 OE2 GLU A 175 7620 5999 7203 -560 883 -857 O ATOM 1180 N GLN A 176 -36.173 -3.945 -12.692 1.00 25.91 N

ANISOU 1180 N GLN A 176 3574 2921 3350 128 199 -172 N

ATOM 1181 CA GLN A 176 -37.462 -4.597 -12.701 1.00 28.32 C

ANISOU 1181 CA GLN A 176 3777 3382 3601 186 84 -67 C

ATOM 1182 C GLN A 176 -37.618 -5.391 -11.410 1.00 24.88 C ANISOU 1182 C GLN A 176 3338 2862 3253 164 9 -191 C

ATOM 1183 0 GLN A 176 -36.675 -6.044 -10.951 1.00 22.56 0

ANISOU 1183 0 GLN A 176 3064 2504 3004 92 -30 -369 0

ATOM 1184 CB GLN A 176 -37.552 -5.525 -13.925 1.00 28.41 C ANISOU 1184 CB GLN A 176 3695 3635 3464 86 -29 -109 C

ATOM 1185 CG GLN A 176 -38.858 -6.278 -14.051 1.00 33.62 C

ANISOU 1185 CG GLN A 176 4224 4522 4027 58 -145 -47 C

ATOM 1186 CD GLN A 176 -38.965 -7.028 -15.372 1.00 40.88 C

ANISOU 1186 CD GLN A 176 5069 5719 4746 -106 -220 -113 C ATOM 1187 OE1 GLN A 176 -38.030 -7.716 -15.785 1.00 44.53 O

ANISOU 1187 OE1 GLN A 176 5602 6117 5202 -232 -203 -320 O

ATOM 1188 NE2 GLN A 176 -40.100 -6.884 -16.046 1.00 41.48 N

ANISOU 1188 NE2 GLN A 176 4987 6136 4640 -108 -288 68 N

ATOM 1189 N THR A 177 -38.806 -5.329 -10.824 1.00 27.54 N ANISOU 1189 N THR A 177 3637 3220 3608 249 3 -66 N

ATOM 1190 CA THR A 177 -39.099 -6.076 -9.604 1.00 29.37 C

ANISOU 1190 CA THR A 177 3873 3380 3906 235 -52 -154 C

ATOM 1191 C THR A 177 -40.358 -6.904 -9.797 1.00 26.32 C

ANISOU 1191 C THR A 177 3365 3171 3464 218 -140 -88 C ATOM 1192 O THR A 177 -41.360 -6.397 -10.291 1.00 27.57 O

ANISOU 1192 O THR A 177 3417 3495 3562 291 -127 104 O

ATOM 1193 CB THR A 177 -39.308 -5.131 -8.401 1.00 32.06 C

ANISOU 1193 CB THR A 177 4309 3541 4331 318 74 -105 C

ATOM 1194 OG1 THR A 177 -38.071 -4.481 -8.084 1.00 33.23 O ANISOU 1194 OG1 THR A 177 4567 3554 4506 249 159 -232 O

ATOM 1195 CG2 THR A 177 -39.779 -5.912 -7.186 1.00 31.41 C

ANISOU 1195 CG2 THR A 177 4225 3425 4286 313 18 -160 C

ATOM 1196 N ARG A 178 -40.298 -8.179 -9.427 1.00 25.55 N

ANISOU 1196 N ARG A 178 3271 3056 3381 119 -206 -234 N ATOM 1197 CA ARG A 178 -41.472 -9.049 -9.499 1.00 25.04 C

ANISOU 1197 CA ARG A 178 3108 3139 3266 33 -255 -223 C

ATOM 1198 C ARG A 178 -41.647 -9.803 -8.196 1.00 23.61 C

ANISOU 1198 C ARG A 178 2996 2795 3180 36 -235 -289 C

ATOM 1199 O ARG A 178 -40.699 -9.957 -7.418 1.00 23.51 O ANISOU 1199 O ARG A 178 3093 2601 3239 89 -212 -363 O

ATOM 1200 CB ARG A 178 -41.365 -10.042 -10.660 1.00 22.88 C

ANISOU 1200 CB ARG A 178 2802 3013 2878 -162 -295 -358 C

ATOM 1201 CG ARG A 178 -41.458 -9.419 -12.039 1.00 44.57 C

ANISOU 1201 CG ARG A 178 5449 6017 5467 -194 -331 -270 C ATOM 1202 CD ARG A 178 -41.364 -10.503 -13.092 1.00 51.67 C

ANISOU 1202 CD ARG A 178 6343 7065 6226 -444 -348 -458 C

ATOM 1203 NE ARG A 178 -40.201 -11.362 -12.863 1.00 54.04 N

ANISOU 1203 NE ARG A 178 6816 7080 6634 -482 -263 -668 N

ATOM 1204 CZ ARG A 178 -39.130 -11.391 -13.648 1.00 56.99 C ANISOU 1204 CZ ARG A 178 7259 7413 6981 -507 -217 -763 C

ATOM 1205 NH1 ARG A 178 -39.082 -10.624 -14.732 1.00 63.14 N

ANISOU 1205 NH1 ARG A 178 7972 8406 7614 -526 -253 -683 N

ATOM 1206 NH2 ARG A 178 -38.113 -12.192 -13.359 1.00 53.37 N

ANISOU 1206 NH2 ARG A 178 6929 6712 6639 -491 -117 -911 N ATOM 1207 N ARG A 179 -42.854 -10.306 -7.975 1.00 24.02 N

ANISOU 1207 N ARG A 179 2962 2952 3211 -27 -241 -250 N

ATOM 1208 CA ARG A 179 -43.189 -10.921 -6.695 1.00 26.91 C

ANISOU 1208 CA ARG A 179 3399 3166 3662 -11 -196 -275 C

ATOM 1209 C ARG A 179 -43.720 -12.330 -6.930 1.00 26.74 C ANISOU 1209 C ARG A 179 3373 3174 3612 -215 -170 -397 C

ATOM 1210 O ARG A 179 -44.540 -12.542 -7.822 1.00 26.48 O

ANISOU 1210 O ARG A 179 3201 3389 3472 -383 -201 -410 O

ATOM 1211 CB ARG A 179 -44.244 -10.057 -5.994 1.00 33.78 C

ANISOU 1211 CB ARG A 179 4188 4088 4558 106 -162 -104 C ATOM 1212 CG ARG A 179 -44.157 -10.035 -4.494 1.00 42.08 C

ANISOU 1212 CG ARG A 179 5364 4933 5691 196 -95 -105 C

ATOM 1213 CD ARG A 179 -44.231 -8.611 -3.956 1.00 44.66 C

ANISOU 1213 CD ARG A 179 5723 5194 6050 354 -11 8 C ATOM 1214 NE ARG A 179 -45.513 -7.970 -4.223 1.00 48.49 N

ANISOU 1214 NE ARG A 179 6057 5828 6538 441 49 195 N

ATOM 1215 CZ ARG A 179 -46.590 -8.108 -3.453 1.00 49.98 C

ANISOU 1215 CZ ARG A 179 6186 6043 6762 475 115 274 C

ATOM 1216 NH1 ARG A 179 -46.541 -8.878 -2.368 1.00 49.36 N ANISOU 1216 NH1 ARG A 179 6216 5829 6709 414 131 172 N

ATOM 1217 NH2 ARG A 179 -47.720 -7.484 -3.771 1.00 46.85 N

ANISOU 1217 NH2 ARG A 179 5605 5830 6367 592 179 482 N

ATOM 1218 N HIS A 180 -43.248 -13.301 -6.155 1.00 25.86 N

ANISOU 1218 N HIS A 180 3416 2829 3579 -213 -90 -483 N ATOM 1219 CA HIS A 180 -43.768 -14.656 -6.287 1.00 24.74 C

ANISOU 1219 CA HIS A 180 3330 2634 3435 -418 15 -607 C

ATOM 1220 C HIS A 180 -45.221 -14.631 -5.811 1.00 25.04 C

ANISOU 1220 C HIS A 180 3245 2813 3455 -507 21 -540 C

ATOM 1221 O HIS A 180 -45.512 -14.131 -4.730 1.00 25.45 O ANISOU 1221 O HIS A 180 3298 2803 3567 -346 23 -415 O

ATOM 1222 CB HIS A 180 -42.941 -15.656 -5.475 1.00 24.17 C

ANISOU 1222 CB HIS A 180 3468 2248 3467 -327 150 -647 C

ATOM 1223 CG HIS A 180 -43.346 -17.086 -5.681 1.00 27.20 C

ANISOU 1223 CG HIS A 180 3979 2485 3872 -539 345 -787 C ATOM 1224 ND1 HIS A 180 -44.511 -17.615 -5.158 1.00 28.93 N

ANISOU 1224 ND1 HIS A 180 4197 2697 4098 -693 433 -799 N

ATOM 1225 CD2 HIS A 180 -42.746 -18.094 -6.358 1.00 27.61 C

ANISOU 1225 CD2 HIS A 180 4185 2363 3944 -644 515 -938 C

ATOM 1226 CE1 HIS A 180 -44.603 -18.889 -5.502 1.00 29.55 C ANISOU 1226 CE1 HIS A 180 4437 2592 4197 -909 657 -964 C

ATOM 1227 NE2 HIS A 180 -43.548 -19.203 -6.232 1.00 29.77 N

ANISOU 1227 NE2 HIS A 180 4574 2500 4236 -876 724 -1052 N

ATOM 1228 N PRO A 181 -46.141 -15.148 -6.629 1.00 26.98 N

ANISOU 1228 N PRO A 181 3367 3286 3598 -784 32 -631 N ATOM 1229 CA PRO A 181 -47.574 -15.035 -6.320 1.00 28.30 C

ANISOU 1229 CA PRO A 181 3336 3691 3725 -883 22 -551 C

ATOM 1230 C PRO A 181 -47.999 -15.709 -5.007 1.00 31.57 C

ANISOU 1230 C PRO A 181 3875 3866 4255 -876 163 -549 C

ATOM 1231 O PRO A 181 -49.024 -15.331 -4.438 1.00 30.77 O ANISOU 1231 O PRO A 181 3621 3911 4160 -850 160 -430 O

ATOM 1232 CB PRO A 181 -48.256 -15.697 -7.535 1.00 30.96 C

ANISOU 1232 CB PRO A 181 3524 4352 3887 -1266 16 -713 C

ATOM 1233 CG PRO A 181 -47.207 -16.534 -8.166 1.00 31.09 C

ANISOU 1233 CG PRO A 181 3776 4137 3902 -1396 114 -931 C ATOM 1234 CD PRO A 181 -45.903 -15.820 -7.915 1.00 28.47 C

ANISOU 1234 CD PRO A 181 3570 3573 3673 -1048 59 -824 C

ATOM 1235 N GLU A 182 -47.224 -16.674 -4.523 1.00 34.08 N

ANISOU 1235 N GLU A 182 4460 3826 4661 -869 307 -648 N

ATOM 1236 CA GLU A 182 -47.600 -17.384 -3.303 1.00 36.20 C ANISOU 1236 CA GLU A 182 4871 3861 5023 -853 467 -620 C

ATOM 1237 C GLU A 182 -46.770 -16.982 -2.083 1.00 35.10 C

ANISOU 1237 C GLU A 182 4874 3500 4961 -514 456 -468 C

ATOM 1238 O GLU A 182 -47.315 -16.778 -0.996 1.00 35.37 O

ANISOU 1238 O GLU A 182 4912 3504 5022 -423 490 -360 O ATOM 1239 CB GLU A 182 -47.519 -18.895 -3.511 1.00 45.43 C

ANISOU 1239 CB GLU A 182 6254 4782 6226 -1095 710 -805 C

ATOM 1240 CG GLU A 182 -48.770 -19.646 -3.086 1.00 58.84 C

ANISOU 1240 CG GLU A 182 7940 6488 7929 -1368 879 -870 C

ATOM 1241 CD GLU A 182 -49.688 -20.005 -4.261 1.00 70.33 C ANISOU 1241 CD GLU A 182 9212 8265 9245 -1824 889 -1082 C

ATOM 1242 OE1 GLU A 182 -49.190 -20.489 -5.307 1.00 71.74 0

ANISOU 1242 OE1 GLU A 182 9475 8425 9358 -2022 944 -1275 O

ATOM 1243 OE2 GLU A 182 -50.915 -19.800 -4.131 1.00 76.69 O ANISOU 1243 OE2 GLU A 182 9773 9379 9986 -1997 849 -1057 O

ATOM 1244 N THR A 183 -45.455 -16.863 -2.256 1.00 31.39 N

ANISOU 1244 N THR A 183 4505 2918 4505 -346 411 -465 N

ATOM 1245 CA THR A 183 -44.565 -16.642 -1.115 1.00 25.61 C

ANISOU 1245 CA THR A 183 3885 2047 3799 -73 399 -339 C ATOM 1246 C THR A 183 -44.326 -15.175 -0.832 1.00 26.10 C

ANISOU 1246 C THR A 183 3836 2266 3814 71 235 -260 C

ATOM 1247 O THR A 183 -43.902 -14.815 0.270 1.00 24.12 O

ANISOU 1247 O THR A 183 3647 1979 3540 226 222 -175 O

ATOM 1248 CB THR A 183 -43.190 -17.292 -1.320 1.00 28.75 C ANISOU 1248 CB THR A 183 4413 2285 4227 53 455 -351 C

ATOM 1249 OG1 THR A 183 -42.540 -16.687 -2.449 1.00 27.36 O

ANISOU 1249 OG1 THR A 183 4143 2235 4020 28 336 -430 O

ATOM 1250 CG2 THR A 183 -43.328 -18.800 -1.534 1.00 27.41 C

ANISOU 1250 CG2 THR A 183 4424 1863 4128 -61 710 -424 C ATOM 1251 N GLY A 184 -44.582 -14.330 -1.830 1.00 25.67 N

ANISOU 1251 N GLY A 184 3633 2391 3729 6 137 -287 N

ATOM 1252 CA GLY A 184 -44.349 -12.905 -1.695 1.00 23.53 C

ANISOU 1252 CA GLY A 184 3299 2210 3433 132 52 -217 C

ATOM 1253 C GLY A 184 -42.899 -12.487 -1.870 1.00 23.55 C ANISOU 1253 C GLY A 184 3354 2179 3414 222 -13 -254 C

ATOM 1254 O GLY A 184 -42.577 -11.312 -1.791 1.00 29.16 O

ANISOU 1254 O GLY A 184 4045 2932 4102 284 -44 -231 O

ATOM 1255 N LEU A 185 -42.010 -13.440 -2.111 1.00 23.93 N

ANISOU 1255 N LEU A 185 3471 2146 3475 226 3 -311 N ATOM 1256 CA LEU A 185 -40.589 -13.109 -2.224 1.00 24.69 C

ANISOU 1256 CA LEU A 185 3573 2260 3548 318 -55 -333 C

ATOM 1257 C LEU A 185 -40.279 -12.415 -3.552 1.00 26.51 C

ANISOU 1257 C LEU A 185 3725 2583 3764 250 -110 -395 C

ATOM 1258 O LEU A 185 -40.884 -12.722 -4.580 1.00 25.36 O ANISOU 1258 O LEU A 185 3539 2484 3614 132 -99 -438 O

ATOM 1259 CB LEU A 185 -39.736 -14.362 -2.078 1.00 23.85 C

ANISOU 1259 CB LEU A 185 3543 2045 3473 402 17 -326 C

ATOM 1260 CG LEU A 185 -39.909 -15.113 -0.760 1.00 27.35 C

ANISOU 1260 CG LEU A 185 4078 2399 3915 512 95 -214 C ATOM 1261 CD1 LEU A 185 -38.958 -16.305 -0.708 1.00 24.11 C

ANISOU 1261 CD1 LEU A 185 3741 1875 3546 665 209 -148 C

ATOM 1262 CD2 LEU A 185 -39.689 -14.166 0.426 1.00 22.27 C

ANISOU 1262 CD2 LEU A 185 3400 1891 3170 584 2 -149 C

ATOM 1263 N PHE A 186 -39.315 -11.501 -3.524 1.00 25.31 N ANISOU 1263 N PHE A 186 3551 2483 3582 299 -160 -406 N

ATOM 1264 CA PHE A 186 -39.009 -10.672 -4.682 1.00 25.97 C

ANISOU 1264 CA PHE A 186 3581 2638 3649 248 -185 -440 C

ATOM 1265 C PHE A 186 -37.984 -11.271 -5.634 1.00 25.76 C

ANISOU 1265 C PHE A 186 3542 2622 3625 228 -187 -520 C ATOM 1266 O PHE A 186 -37.029 -11.921 -5.220 1.00 30.23 O

ANISOU 1266 O PHE A 186 4120 3158 4209 305 -172 -534 O

ATOM 1267 CB PHE A 186 -38.498 -9.306 -4.233 1.00 24.38 C

ANISOU 1267 CB PHE A 186 3390 2453 3420 264 -178 -438 C

ATOM 1268 CG PHE A 186 -39.504 -8.493 -3.486 1.00 26.25 C ANISOU 1268 CG PHE A 186 3666 2647 3662 286 -114 -368 C

ATOM 1269 CD1 PHE A 186 -39.565 -8.540 -2.102 1.00 27.52 C

ANISOU 1269 CD1 PHE A 186 3887 2774 3795 307 -92 -372 C

ATOM 1270 CD2 PHE A 186 -40.374 -7.655 -4.163 1.00 30.26 C

ANISOU 1270 CD2 PHE A 186 4146 3163 4189 308 -52 -276 C ATOM 1271 CE1 PHE A 186 -40.488 -7.762 -1.405 1.00 27.45 C

ANISOU 1271 CE1 PHE A 186 3935 2701 3795 326 11 -321 C

ATOM 1272 CE2 PHE A 186 -41.296 -6.870 -3.475 1.00 29.24 C

ANISOU 1272 CE2 PHE A 186 4054 2971 4085 372 60 -186 C ATOM 1273 CZ PHE A 186 -41.356 -6.931 -2.095 1.00 26.77 C

ANISOU 1273 CZ PHE A 186 3825 2586 3762 370 101 -227 C

ATOM 1274 N THR A 187 -38.193 -11.032 -6.921 1.00 24.54 N

ANISOU 1274 N THR A 187 3351 2534 3439 142 -190 -550 N

ATOM 1275 CA THR A 187 -37.192 -11.331 -7.935 1.00 25.45 C ANISOU 1275 CA THR A 187 3461 2666 3542 110 -170 -635 C

ATOM 1276 C THR A 187 -36.800 -10.008 -8.580 1.00 27.25 C

ANISOU 1276 C THR A 187 3648 2976 3727 95 -190 -613 C

ATOM 1277 O THR A 187 -37.665 -9.233 -8.999 1.00 26.35 O

ANISOU 1277 O THR A 187 3509 2931 3570 75 -197 -528 O ATOM 1278 CB THR A 187 -37.737 -12.288 -8.995 1.00 24.53 C

ANISOU 1278 CB THR A 187 3366 2568 3387 -25 -122 -717 C

ATOM 1279 OG1 THR A 187 -37.975 -13.562 -8.391 1.00 27.07 O

ANISOU 1279 OG1 THR A 187 3772 2745 3770 -24 -34 -754 O

ATOM 1280 CG2 THR A 187 -36.745 -12.454 -10.151 1.00 25.85 C ANISOU 1280 CG2 THR A 187 3543 2756 3524 -70 -74 -815 C

ATOM 1281 N LEU A 188 -35.501 -9.734 -8.620 1.00 28.05 N

ANISOU 1281 N LEU A 188 3736 3081 3842 116 -176 -667 N

ATOM 1282 CA LEU A 188 -35.008 -8.460 -9.135 1.00 25.78 C

ANISOU 1282 CA LEU A 188 3438 2832 3525 77 -148 -662 C ATOM 1283 C LEU A 188 -34.257 -8.703 -10.425 1.00 26.50 C

ANISOU 1283 C LEU A 188 3508 2975 3585 26 -116 -727 C

ATOM 1284 O LEU A 188 -33.578 -9.713 -10.572 1.00 29.63 O

ANISOU 1284 O LEU A 188 3886 3363 4009 47 -97 -802 O

ATOM 1285 CB LEU A 188 -34.070 -7.789 -8.133 1.00 23.41 C ANISOU 1285 CB LEU A 188 3122 2535 3236 71 -137 -704 C

ATOM 1286 CG LEU A 188 -34.605 -7.418 -6.751 1.00 26.97 C

ANISOU 1286 CG LEU A 188 3614 2947 3685 88 -143 -674 C

ATOM 1287 CD1 LEU A 188 -33.506 -6.713 -5.962 1.00 29.09 C

ANISOU 1287 CD1 LEU A 188 3853 3293 3906 -2 -124 -768 C ATOM 1288 CD2 LEU A 188 -35.832 -6.526 -6.847 1.00 26.21 C

ANISOU 1288 CD2 LEU A 188 3599 2760 3601 99 -70 -579 C

ATOM 1289 N GLN A 189 -34.372 -7.763 -11.351 1.00 25.26 N

ANISOU 1289 N GLN A 189 3364 2861 3372 -20 -77 -681 N

ATOM 1290 CA GLN A 189 -33.712 -7.878 -12.637 1.00 26.76 C ANISOU 1290 CA GLN A 189 3546 3117 3506 -82 -34 -736 C

ATOM 1291 C GLN A 189 -33.149 -6.516 -13.018 1.00 33.37 C

ANISOU 1291 C GLN A 189 4407 3944 4328 -109 52 -694 C

ATOM 1292 O GLN A 189 -33.791 -5.483 -12.807 1.00 35.89 O

ANISOU 1292 O GLN A 189 4778 4214 4645 -75 101 -572 O ATOM 1293 CB GLN A 189 -34.702 -8.384 -13.683 1.00 26.15 C

ANISOU 1293 CB GLN A 189 3469 3154 3312 -144 -61 -706 C

ATOM 1294 CG GLN A 189 -34.064 -9.037 -14.877 1.00 37.21 C

ANISOU 1294 CG GLN A 189 4884 4617 4637 -240 -7 -826 C

ATOM 1295 CD GLN A 189 -35.058 -9.817 -15.721 1.00 43.18 C ANISOU 1295 CD GLN A 189 5641 5522 5244 -376 -33 -865 C

ATOM 1296 OE1 GLN A 189 -35.984 -10.436 -15.195 1.00 47.37 O

ANISOU 1296 OE1 GLN A 189 6162 6057 5781 -408 -78 -870 O

ATOM 1297 NE2 GLN A 189 -34.873 -9.783 -17.036 1.00 43.18 N

ANISOU 1297 NE2 GLN A 189 5650 5672 5086 -490 5 -905 N ATOM 1298 N SER A 190 -31.934 -6.513 -13.554 1.00 35.87 N

ANISOU 1298 N SER A 190 4697 4284 4647 -164 111 -790 N

ATOM 1299 CA SER A 190 -31.244 -5.266 -13.859 1.00 35.42 C

ANISOU 1299 CA SER A 190 4675 4196 4587 -231 232 -782 C

ATOM 1300 C SER A 190 -30.446 -5.382 -15.160 1.00 36.82 C ANISOU 1300 C SER A 190 4838 4445 4705 -292 304 -832 C

ATOM 1301 0 SER A 190 -29.617 -6.282 -15.304 1.00 40.87 0

ANISOU 1301 0 SER A 190 5273 5012 5244 -298 296 -950 0

ATOM 1302 CB SER A 190 -30.336 -4.876 -12.689 1.00 31.78 C ANISOU 1302 CB SER A 190 4166 3715 4196 -293 253 -887 C

ATOM 1303 OG SER A 190 -29.514 -3.766 -13.004 1.00 32.39 O

ANISOU 1303 OG SER A 190 4275 3763 4268 -426 404 -935 O

ATOM 1304 N GLU A 191 -30.705 -4.482 -16.107 1.00 32.48 N

ANISOU 1304 N GLU A 191 4369 3895 4076 -312 402 -720 N ATOM 1305 CA GLU A 191 -29.999 -4.510 -17.394 1.00 34.09 C

ANISOU 1305 CA GLU A 191 4579 4178 4197 -380 487 -755 C

ATOM 1306 C GLU A 191 -29.015 -3.354 -17.537 1.00 31.70 C

ANISOU 1306 C GLU A 191 4319 3794 3933 -470 668 -772 C

ATOM 1307 O GLU A 191 -29.394 -2.194 -17.432 1.00 27.88 O ANISOU 1307 O GLU A 191 3948 3189 3456 -461 790 -645 O

ATOM 1308 CB GLU A 191 -30.984 -4.516 -18.562 1.00 39.13 C

ANISOU 1308 CB GLU A 191 5262 4950 4656 -353 466 -604 C

ATOM 1309 CG GLU A 191 -31.889 -5.726 -18.553 1.00 48.30 C

ANISOU 1309 CG GLU A 191 6373 6230 5751 -351 314 -642 C ATOM 1310 CD GLU A 191 -32.851 -5.761 -19.717 1.00 52.96 C

ANISOU 1310 CD GLU A 191 6955 7062 6104 -383 271 -514 C

ATOM 1311 OE1 GLU A 191 -32.861 -4.788 -20.507 1.00 53.89 O

ANISOU 1311 OE1 GLU A 191 7108 7256 6113 -349 354 -338 O

ATOM 1312 OE2 GLU A 191 -33.588 -6.770 -19.835 1.00 51.49 O ANISOU 1312 OE2 GLU A 191 6726 7012 5828 -457 168 -586 O

ATOM 1313 N LEU A 192 -27.751 -3.688 -17.778 1.00 27.69 N

ANISOU 1313 N LEU A 192 3724 3343 3456 -558 720 -928 N

ATOM 1314 CA LEU A 192 -26.696 -2.694 -17.852 1.00 29.02 C

ANISOU 1314 CA LEU A 192 3899 3467 3661 -701 898 -991 C ATOM 1315 C LEU A 192 -26.324 -2.395 -19.292 1.00 36.85 C

ANISOU 1315 C LEU A 192 4958 4488 4555 -747 1045 -947 C

ATOM 1316 O LEU A 192 -26.096 -3.307 -20.085 1.00 38.88 O

ANISOU 1316 O LEU A 192 5164 4861 4746 -723 1009 -998 O

ATOM 1317 CB LEU A 192 -25.461 -3.184 -17.098 1.00 34.62 C ANISOU 1317 CB LEU A 192 4405 4295 4456 -776 864 -1176 C

ATOM 1318 CG LEU A 192 -24.194 -2.332 -17.203 1.00 35.96 C

ANISOU 1318 CG LEU A 192 4511 4507 4647 -985 1042 -1291 C

ATOM 1319 CD1 LEU A 192 -24.386 -0.978 -16.513 1.00 36.38 C

ANISOU 1319 CD1 LEU A 192 4700 4403 4719 -1149 1179 -1303 C ATOM 1320 CD2 LEU A 192 -22.997 -3.072 -16.621 1.00 33.60 C

ANISOU 1320 CD2 LEU A 192 3923 4447 4394 -1010 971 -1429 C

ATOM 1321 N MET A 193 -26.270 -1.111 -19.624 1.00 37.70 N

ANISOU 1321 N MET A 193 5208 4468 4648 -816 1249 -851 N

ATOM 1322 CA MET A 193 -25.764 -0.666 -20.915 1.00 40.60 C ANISOU 1322 CA MET A 193 5652 4853 4923 -876 1431 -799 C

ATOM 1323 C MET A 193 -24.615 0.309 -20.708 1.00 43.54 C

ANISOU 1323 C MET A 193 6043 5117 5383 -1088 1672 -919 C

ATOM 1324 O MET A 193 -24.713 1.219 -19.884 1.00 46.49 O

ANISOU 1324 O MET A 193 6510 5315 5839 -1173 1792 -927 O ATOM 1325 CB MET A 193 -26.867 0.004 -21.730 1.00 41.78 C

ANISOU 1325 CB MET A 193 5978 4962 4936 -740 1504 -505 C

ATOM 1326 CG MET A 193 -27.920 -0.953 -22.252 1.00 42.18 C

ANISOU 1326 CG MET A 193 5974 5225 4828 -605 1281 -402 C

ATOM 1327 SD MET A 193 -29.004 -0.153 -23.443 1.00 64.32 S ANISOU 1327 SD MET A 193 8902 8140 7396 -449 1365 -15 S

ATOM 1328 CE MET A 193 -27.868 0.100 -24.811 1.00 51.66 C

ANISOU 1328 CE MET A 193 7368 6594 5666 -582 1573 -52 C

ATOM 1329 N VAL A 194 -23.521 0.114 -21.437 1.00 41.20 N

ANISOU 1329 N VAL A 194 5661 4927 5066 -1203 1770 -1033 N ATOM 1330 CA VAL A 194 -22.399 1.037 -21.350 1.00 44.80 C

ANISOU 1330 CA VAL A 194 6114 5321 5588 -1453 2019 -1162 C

ATOM 1331 C VAL A 194 -21.941 1.504 -22.728 1.00 49.46 C

ANISOU 1331 C VAL A 194 6820 5885 6087 -1510 2257 -1086 C ATOM 1332 O VAL A 194 -22.078 0.791 -23.725 1.00 48.66 O

ANISOU 1332 O VAL A 194 6707 5913 5867 -1393 2190 -1021 O

ATOM 1333 CB VAL A 194 -21.181 0.427 -20.604 1.00 45.86 C

ANISOU 1333 CB VAL A 194 5939 5680 5808 -1594 1931 -1415 C

ATOM 1334 CGI VAL A 194 -21.587 -0.110 -19.247 1.00 36.78 C ANISOU 1334 CGI VAL A 194 4663 4598 4715 -1522 1691 -1465 C

ATOM 1335 CG2 VAL A 194 -20.533 -0.665 -21.439 1.00 49.19 C

ANISOU 1335 CG2 VAL A 194 6192 6302 6198 -1504 1879 -1461 C

ATOM 1336 N THR A 195 -21.411 2.720 -22.774 1.00 52.23 N

ANISOU 1336 N THR A 195 7307 6058 6481 -1717 2567 -1106 N ATOM 1337 CA THR A 195 -20.747 3.221 -23.963 1.00 52.60 C

ANISOU 1337 CA THR A 195 7450 6076 6459 -1820 2838 -1064 C

ATOM 1338 C THR A 195 -19.265 3.327 -23.637 1.00 55.19 C

ANISOU 1338 C THR A 195 7567 6524 6880 -2134 2962 -1353 C

ATOM 1339 O THR A 195 -18.836 4.283 -22.993 1.00 58.10 O ANISOU 1339 O THR A 195 7991 6756 7329 -2402 3175 -1476 O

ATOM 1340 CB THR A 195 -21.300 4.590 -24.396 1.00 53.60 C

ANISOU 1340 CB THR A 195 7927 5881 6558 -1807 3172 -820 C

ATOM 1341 OG1 THR A 195 -22.681 4.455 -24.756 1.00 55.50 O

ANISOU 1341 OG1 THR A 195 8295 6108 6684 -1481 3039 -505 O ATOM 1342 CG2 THR A 195 -20.514 5.141 -25.593 1.00 50.42 C

ANISOU 1342 CG2 THR A 195 7635 5439 6082 -1935 3490 -776 C

ATOM 1343 N PRO A 196 -18.481 2.321 -24.058 1.00 54.10 N

ANISOU 1343 N PRO A 196 7172 6661 6725 -2113 2848 -1469 N

ATOM 1344 CA PRO A 196 -17.051 2.258 -23.740 1.00 53.15 C ANISOU 1344 CA PRO A 196 6754 6758 6682 -2365 2929 -1715 C

ATOM 1345 C PRO A 196 -16.297 3.404 -24.385 1.00 58.63 C

ANISOU 1345 C PRO A 196 7578 7328 7369 -2660 3319 -1760 C

ATOM 1346 O PRO A 196 -16.505 3.695 -25.565 1.00 62.23 O

ANISOU 1346 O PRO A 196 8263 7647 7734 -2588 3502 -1597 O ATOM 1347 CB PRO A 196 -16.612 0.927 -24.356 1.00 52.17 C

ANISOU 1347 CB PRO A 196 6409 6882 6533 -2174 2792 -1740 C

ATOM 1348 CG PRO A 196 -17.872 0.131 -24.507 1.00 44.52 C

ANISOU 1348 CG PRO A 196 5580 5842 5492 -1870 2559 -1584 C

ATOM 1349 CD PRO A 196 -18.933 1.137 -24.807 1.00 49.58 C ANISOU 1349 CD PRO A 196 6563 6223 6052 -1850 2652 -1382 C

ATOM 1350 N ALA A 197 -15.438 4.053 -23.609 1.00 61.86 N

ANISOU 1350 N ALA A 197 7861 7793 7850 -2965 3394 -1971 N

ATOM 1351 CA ALA A 197 -14.612 5.133 -24.128 1.00 67.14 C

ANISOU 1351 CA ALA A 197 8673 8323 8515 -3189 3644 -2045 C ATOM 1352 C ALA A 197 -13.554 4.567 -25.070 1.00 69.48 C

ANISOU 1352 C ALA A 197 8745 8864 8790 -3190 3674 -2089 C

ATOM 1353 O ALA A 197 -13.104 3.431 -24.905 1.00 69.53 O

ANISOU 1353 O ALA A 197 8395 9209 8815 -3086 3487 -2151 O

ATOM 1354 CB ALA A 197 -13.963 5.894 -22.987 1.00 58.82 C ANISOU 1354 CB ALA A 197 7543 7322 7485 -3498 3657 -2302 C

ATOM 1355 N ARG A 198 -13.165 5.355 -26.065 1.00 71.55 N

ANISOU 1355 N ARG A 198 9226 8939 9022 -3277 3930 -2041 N

ATOM 1356 CA ARG A 198 -12.132 4.929 -26.997 1.00 72.57 C

ANISOU 1356 CA ARG A 198 9172 9271 9131 -3296 3995 -2084 C ATOM 1357 C ARG A 198 -10.785 4.922 -26.287 1.00 73.30 C

ANISOU 1357 C ARG A 198 8884 9688 9278 -3545 3940 -2344 C

ATOM 1358 O ARG A 198 -10.539 5.743 -25.401 1.00 74.05 O

ANISOU 1358 O ARG A 198 8997 9757 9383 -3797 3968 -2505 O

ATOM 1359 CB ARG A 198 -12.110 5.838 -28.224 1.00 75.89 C ANISOU 1359 CB ARG A 198 9939 9403 9491 -3327 4289 -1947 C

ATOM 1360 CG ARG A 198 -13.487 6.020 -28.835 1.00 77.71 C

ANISOU 1360 CG ARG A 198 10537 9365 9625 -3068 4333 -1639 C

ATOM 1361 CD ARG A 198 -13.473 6.887 -30.080 1.00 83.56 C ANISOU 1361 CD ARG A 198 11596 9872 10282 -3047 4612 -1447 C

ATOM 1362 NE ARG A 198 -14.835 7.195 -30.510 1.00 85.51 N

ANISOU 1362 NE ARG A 198 12162 9912 10414 -2774 4638 -1105 N

ATOM 1363 CZ ARG A 198 -15.591 6.382 -31.242 1.00 83.98 C

ANISOU 1363 CZ ARG A 198 11987 9883 10039 -2523 4503 -902 C ATOM 1364 NH1 ARG A 198 -15.118 5.206 -31.634 1.00 84.64 N

ANISOU 1364 NH1 ARG A 198 11830 10272 10059 -2509 4364 -1036 N

ATOM 1365 NH2 ARG A 198 -16.821 6.745 -31.583 1.00 81.49 N

ANISOU 1365 NH2 ARG A 198 11924 9446 9591 -2277 4513 -567 N

ATOM 1366 N GLY A 199 -9.928 3.977 -26.663 1.00 72.29 N ANISOU 1366 N GLY A 199 8412 9890 9164 -3457 3870 -2377 N

ATOM 1367 CA GLY A 199 -8.638 3.818 -26.017 1.00 74.61 C

ANISOU 1367 CA GLY A 199 8273 10586 9488 -3626 3789 -2559 C

ATOM 1368 C GLY A 199 -8.745 3.316 -24.589 1.00 75.28 C

ANISOU 1368 C GLY A 199 8062 10955 9585 -3597 3502 -2625 C ATOM 1369 O GLY A 199 -7.839 3.526 -23.783 1.00 79.37 O

ANISOU 1369 O GLY A 199 8281 11804 10073 -3801 3420 -2774 O

ATOM 1370 N GLY A 200 -9.857 2.656 -24.271 1.00 70.41 N

ANISOU 1370 N GLY A 200 7527 10238 8987 -3348 3348 -2509 N

ATOM 1371 CA GLY A 200 -10.053 2.091 -22.950 1.00 61.38 C ANISOU 1371 CA GLY A 200 6118 9353 7852 -3277 3072 -2540 C

ATOM 1372 C GLY A 200 -9.568 0.656 -22.856 1.00 72.48 C

ANISOU 1372 C GLY A 200 7100 11128 9311 -2965 2906 -2460 C

ATOM 1373 O GLY A 200 -8.929 0.149 -23.774 1.00 71.91 O

ANISOU 1373 O GLY A 200 6921 11130 9273 -2836 3024 -2413 O ATOM 1374 N ASP A 201 -9.875 0.000 -21.740 1.00 73.13 N

ANISOU 1374 N ASP A 201 6961 11423 9403 -2818 2655 -2430 N

ATOM 1375 CA ASP A 201 -9.473 -1.387 -21.516 1.00 72.92 C

ANISOU 1375 CA ASP A 201 6550 11717 9440 -2455 2517 -2313 C

ATOM 1376 C ASP A 201 -10.144 -2.322 -22.523 1.00 67.96 C ANISOU 1376 C ASP A 201 6114 10828 8878 -2127 2632 -2211 C

ATOM 1377 O ASP A 201 -11.366 -2.375 -22.600 1.00 65.37 O

ANISOU 1377 O ASP A 201 6093 10207 8538 -2061 2618 -2188 O

ATOM 1378 CB ASP A 201 -9.817 -1.809 -20.082 1.00 72.65 C

ANISOU 1378 CB ASP A 201 6305 11916 9382 -2356 2232 -2275 C ATOM 1379 CG ASP A 201 -9.248 -3.171 -19.713 1.00 74.60 C

ANISOU 1379 CG ASP A 201 6133 12520 9692 -1951 2106 -2106 C

ATOM 1380 OD1 ASP A 201 -8.368 -3.676 -20.441 1.00 77.51 O

ANISOU 1380 OD1 ASP A 201 6318 13011 10124 -1792 2246 -2036 O

ATOM 1381 OD2 ASP A 201 -9.671 -3.732 -18.679 1.00 73.79 O ANISOU 1381 OD2 ASP A 201 5897 12561 9579 -1770 1889 -2020 O

ATOM 1382 N PRO A 202 -9.339 -3.049 -23.313 1.00 69.28 N

ANISOU 1382 N PRO A 202 6121 11104 9098 -1929 2764 -2156 N

ATOM 1383 CA PRO A 202 -9.900 -3.992 -24.287 1.00 67.94 C

ANISOU 1383 CA PRO A 202 6175 10681 8957 -1637 2898 -2098 C ATOM 1384 C PRO A 202 -10.561 -5.206 -23.641 1.00 66.53 C

ANISOU 1384 C PRO A 202 5932 10501 8847 -1278 2765 -2020 C

ATOM 1385 O PRO A 202 -11.371 -5.875 -24.283 1.00 66.30 O

ANISOU 1385 O PRO A 202 6236 10154 8799 -1085 2792 -1982 O

ATOM 1386 CB PRO A 202 -8.680 -4.416 -25.121 1.00 69.83 C ANISOU 1386 CB PRO A 202 6222 11066 9244 -1534 3091 -2068 C

ATOM 1387 CG PRO A 202 -7.492 -4.084 -24.279 1.00 73.00 C

ANISOU 1387 CG PRO A 202 6165 11901 9671 -1645 2992 -2054 C

ATOM 1388 CD PRO A 202 -7.882 -2.884 -23.474 1.00 72.22 C

ANISOU 1388 CD PRO A 202 6161 11796 9483 -2018 2841 -2165 C ATOM 1389 N ARG A 203 -10.231 -5.488 -22.387 1.00 66.54 N

ANISOU 1389 N ARG A 203 5577 10813 8891 -1180 2561 -1954 N

ATOM 1390 CA ARG A 203 -10.846 -6.617 -21.697 1.00 66.46 C

ANISOU 1390 CA ARG A 203 5567 10744 8942 -803 2398 -1820 C ATOM 1391 C ARG A 203 -11.403 -6.266 -20.311 1.00 61.36 C

ANISOU 1391 C ARG A 203 4860 10209 8244 -880 2093 -1792 C

ATOM 1392 O ARG A 203 -10.913 -6.767 -19.299 1.00 60.96 O

ANISOU 1392 O ARG A 203 4425 10521 8214 -708 1960 -1684 O

ATOM 1393 CB ARG A 203 -9.853 -7.774 -21.594 1.00 72.67 C ANISOU 1393 CB ARG A 203 5957 11805 9848 -423 2517 -1681 C

ATOM 1394 CG ARG A 203 -9.515 -8.415 -22.927 1.00 77.71 C

ANISOU 1394 CG ARG A 203 6767 12213 10546 -259 2828 -1684 C

ATOM 1395 CD ARG A 203 -9.321 -9.906 -22.757 1.00 83.59 C

ANISOU 1395 CD ARG A 203 7413 12918 11429 244 2946 -1505 C ATOM 1396 NE ARG A 203 -10.523 -10.540 -22.219 1.00 85.25 N

ANISOU 1396 NE ARG A 203 7889 12845 11655 409 2818 -1479 N

ATOM 1397 CZ ARG A 203 -11.352 -11.295 -22.932 1.00 86.96 C

ANISOU 1397 CZ ARG A 203 8546 12612 11882 517 2962 -1534 C

ATOM 1398 NH1 ARG A 203 -11.103 -11.525 -24.214 1.00 91.69 N ANISOU 1398 NH1 ARG A 203 9350 13021 12466 482 3256 -1639 N

ATOM 1399 NH2 ARG A 203 -12.423 -11.830 -22.360 1.00 83.27 N

ANISOU 1399 NH2 ARG A 203 8320 11903 11415 630 2810 -1488 N

ATOM 1400 N PRO A 204 -12.446 -5.420 -20.267 1.00 55.87 N

ANISOU 1400 N PRO A 204 4544 9214 7471 -1114 1999 -1865 N ATOM 1401 CA PRO A 204 -13.006 -4.955 -18.995 1.00 53.62 C

ANISOU 1401 CA PRO A 204 4248 8996 7128 -1232 1756 -1869 C

ATOM 1402 C PRO A 204 -13.684 -6.085 -18.240 1.00 52.66 C

ANISOU 1402 C PRO A 204 4134 8823 7050 -862 1566 -1716 C

ATOM 1403 O PRO A 204 -14.040 -7.103 -18.834 1.00 53.09 O ANISOU 1403 O PRO A 204 4344 8651 7177 -562 1643 -1633 O

ATOM 1404 CB PRO A 204 -14.046 -3.924 -19.431 1.00 50.88 C

ANISOU 1404 CB PRO A 204 4371 8242 6721 -1472 1793 -1939 C

ATOM 1405 CG PRO A 204 -14.472 -4.391 -20.782 1.00 49.91 C

ANISOU 1405 CG PRO A 204 4538 7817 6608 -1312 1940 -1893 C ATOM 1406 CD PRO A 204 -13.215 -4.914 -21.417 1.00 52.62 C

ANISOU 1406 CD PRO A 204 4594 8393 7008 -1236 2130 -1914 C

ATOM 1407 N THR A 205 -13.860 -5.900 -16.939 1.00 52.22 N

ANISOU 1407 N THR A 205 3931 8973 6938 -912 1349 -1693 N

ATOM 1408 CA THR A 205 -14.478 -6.915 -16.102 1.00 51.48 C ANISOU 1408 CA THR A 205 3835 8850 6874 -575 1177 -1532 C

ATOM 1409 C THR A 205 -15.696 -6.328 -15.408 1.00 46.66 C

ANISOU 1409 C THR A 205 3523 8008 6196 -725 1008 -1574 C

ATOM 1410 O THR A 205 -15.574 -5.408 -14.605 1.00 45.16 O

ANISOU 1410 O THR A 205 3242 8010 5906 -1020 919 -1673 O ATOM 1411 CB THR A 205 -13.489 -7.450 -15.053 1.00 58.99 C

ANISOU 1411 CB THR A 205 4260 10353 7798 -407 1069 -1399 C

ATOM 1412 OG1 THR A 205 -12.269 -7.838 -15.700 1.00 68.30 O

ANISOU 1412 OG1 THR A 205 5111 11799 9043 -281 1255 -1350 O

ATOM 1413 CG2 THR A 205 -14.068 -8.647 -14.338 1.00 57.16 C ANISOU 1413 CG2 THR A 205 4056 10044 7619 14 961 -1183 C

ATOM 1414 N PHE A 206 -16.872 -6.850 -15.743 1.00 44.96 N

ANISOU 1414 N PHE A 206 3666 7390 6028 -546 990 -1514 N

ATOM 1415 CA PHE A 206 -18.122 -6.394 -15.147 1.00 41.38 C

ANISOU 1415 CA PHE A 206 3490 6706 5527 -633 849 -1522 C ATOM 1416 C PHE A 206 -18.666 -7.438 -14.186 1.00 42.25 C

ANISOU 1416 C PHE A 206 3565 6823 5663 -343 692 -1380 C

ATOM 1417 O PHE A 206 -18.523 -8.639 -14.411 1.00 41.26 O

ANISOU 1417 O PHE A 206 3393 6662 5621 -35 752 -1269 O

ATOM 1418 CB PHE A 206 -19.184 -6.150 -16.215 1.00 37.37 C ANISOU 1418 CB PHE A 206 3389 5789 5021 -665 932 -1537

ATOM 1419 CG PHE A 206 -18.821 -5.099 -17.223 1.00 40.46

ANISOU 1419 CG PHE A 206 3884 6115 5375 -918 1112 -1630

ATOM 1420 CD1 PHE A 206 -19.222 -3.784 -17.045 1.00 39.70

ANISOU 1420 CD1 PHE A 206 3962 5898 5226 -1180 1150 -1685

ATOM 1421 CD2 PHE A 206 -18.116 -5.435 -18.375 1.00 42.09

ANISOU 1421 CD2 PHE A 206 4049 6341 5600 -881 1288 -1653

ATOM 1422 CE1 PHE A 206 -18.910 -2.820 -17.984 1.00 41.36

ANISOU 1422 CE1 PHE A 206 4303 6005 5408 -1391 1362 -1738

ATOM 1423 CE2 PHE A 206 -17.798 -4.479 -19.315 1.00 39.47

ANISOU 1423 CE2 PHE A 206 3829 5943 5223 -1108 1470 -1720

ATOM 1424 CZ PHE A 206 -18.194 -3.170 -19.125 1.00 39.27

ANISOU 1424 CZ PHE A 206 3980 5793 5149 -1358 1510 -1751

ATOM 1425 N SER A 207 -19.320 -6.977 -13.126 1.00 41.69

ANISOU 1425 N SER A 207 3553 6763 5525 -444 534 -1385

ATOM 1426 CA SER A 207 -19.958 -7.886 -12.186 1.00 40.25

ANISOU 1426 CA SER A 207 3379 6559 5354 -190 395 -1246

ATOM 1427 C SER A 207 -21.181 -7.229 -11.563 1.00 41.09

ANISOU 1427 C SER A 207 3746 6458 5408 -333 291 -1285

ATOM 1428 O SER A 207 -21.312 -6.001 -11.568 1.00 43.28

ANISOU 1428 O SER A 207 4128 6689 5628 -629 325 -1412

ATOM 1429 CB SER A 207 -18.975 -8.305 -11.096 1.00 38.81

ANISOU 1429 CB SER A 207 2785 6852 5110 -73 292 -1141

ATOM 1430 OG SER A 207 -18.700 -7.217 -10.232 1.00 40.51

ANISOU 1430 OG SER A 207 2864 7354 5172 -406 185 -1264

ATOM 1431 N CYS A 208 -22.072 -8.058 -11.027 1.00 39.20

ANISOU 1431 N CYS A 208 3623 6072 5199 -117 205 -1171

ATOM 1432 CA CYS A 208 -23.286 -7.588 -10.378 1.00 34.15

ANISOU 1432 CA CYS A 208 3208 5246 4522 -202 116 -1181

ATOM 1433 C CYS A 208 -23.304 -8.034 -8.921 1.00 33.91

ANISOU 1433 C CYS A 208 3032 5428 4425 -95 -30 -1089

ATOM 1434 O CYS A 208 -22.769 -9.085 -8.584 1.00 34.99

ANISOU 1434 O CYS A 208 2978 5736 4583 162 -53 -947

ATOM 1435 CB CYS A 208 -24.519 -8.137 -11.103 1.00 31.55

ANISOU 1435 CB CYS A 208 3163 4559 4264 -81 152 -1132

ATOM 1436 SG CYS A 208 -26.093 -7.741 -10.303 1.00 39.76

ANISOU 1436 SG CYS A 208 4433 5397 5277 -121 56 -1099

ATOM 1437 N SER A 209 -23. 921 -7.242 -8.054 1.00 32.69

ANISOU 1437 N SER A 209 2978 5257 4185 -274 -100 -1150

ATOM 1438 CA SER A 209 -24. 045 -7.644 -6.664 1.00 35.23

ANISOU 1438 CA SER A 209 3193 5784 4411 -190 -237 -1064

ATOM 1439 C SER A 209 -25. 408 -7.297 -6.069 1.00 33.64

ANISOU 1439 C SER A 209 3264 5317 4199 -241 -263 -1076

ATOM 1440 O SER A 209 -26. 034 -6.312 -6.459 1.00 31.92

ANISOU 1440 O SER A 209 3264 4861 4005 -427 -175 -1183

ATOM 1441 CB SER A 209 -22. 922 -7.033 -5.828 1.00 40.08

ANISOU 1441 CB SER A 209 3501 6885 4841 -410 -309 -1149

ATOM 1442 OG SER A 209 -23. 058 -5.630 -5.782 1.00 42.52

ANISOU 1442 OG SER A 209 3953 7122 5083 -801 -231 -1373

ATOM 1443 N PHE A 210 -25.862 -8.120 -5.126 1.00 35.89

ANISOU 1443 N PHE A 210 3537 5645 4455 -48 -357 -939

ATOM 1444 CA PHE A 210 -27.140 -7.894 -4.455 1.00 32.74

ANISOU 1444 CA PHE A 210 3367 5028 4045 -77 -376 -936

ATOM 1445 C PHE A 210 -26.910 -7.283 -3.086 1.00 32.60

ANISOU 1445 C PHE A 210 3263 5293 3831 -259 -452 -1003

ATOM 1446 O PHE A 210 -26.121 -7.798 -2.305 1.00 36.73

ANISOU 1446 O PHE A 210 3533 6203 4220 -183 -561 -917

ATOM 1447 CB PHE A 210 -27.938 -9.198 -4.318 1.00 29.70

ANISOU 1447 CB PHE A 210 3073 4461 3751 216 -391 -760 ATOM 1448 CG PHE A 210 -29.155 -9.070 -3.435 1.00 31.62

ANISOU 1448 CG PHE A 210 3493 4556 3965 198 -417 -737

ATOM 1449 CD1 PHE A 210 -30.369 -8.662 -3.962 1.00 30.28

ANISOU 1449 CD1 PHE A 210 3548 4073 3883 139 -351 -776

ATOM 1450 CD2 PHE A 210 -29.080 -9.348 -2.074 1.00 31.17

ANISOU 1450 CD2 PHE A 210 3355 4716 3773 249 -504 -657

ATOM 1451 CE1 PHE A 210 -31.481 -8.527 -3.150 1.00 32.20

ANISOU 1451 CE1 PHE A 210 3929 4198 4110 134 -353 -746

ATOM 1452 CE2 PHE A 210 -30.188 -9.219 -1.260 1.00 31.52

ANISOU 1452 CE2 PHE A 210 3568 4621 3787 226 -505 -643

ATOM 1453 CZ PHE A 210 -31.390 -8.807 -1.793 1.00 30.87

ANISOU 1453 CZ PHE A 210 3706 4202 3822 170 -422 -693

ATOM 1454 N SER A 211 -27.601 -6.186 -2.799 1.00 34.60

ANISOU 1454 N SER A 211 3724 5371 4052 -495 -374 -1145

ATOM 1455 CA SER A 211 -27.527 -5.550 -1.482 1.00 36.30

ANISOU 1455 CA SER A 211 3922 5808 4062 -723 -401 -1258

ATOM 1456 C SER A 211 -28.853 -5.702 -0.764 1.00 35.38

ANISOU 1456 C SER A 211 4028 5450 3965 -625 -388 -1188

ATOM 1457 O SER A 211 -29.871 -5.168 -1.212 1.00 36.18

ANISOU 1457 O SER A 211 4378 5171 4198 -633 -254 -1210

ATOM 1458 CB SER A 211 -27.195 -4.064 -1.604 1.00 38.78

ANISOU 1458 CB SER A 211 4335 6084 4315 -1123 -236 -1518

ATOM 1459 OG SER A 211 -25.950 -3.878 -2.246 1.00 47.85

ANISOU 1459 OG SER A 211 5265 7476 5439 -1255 -232 -1599

ATOM 1460 N PRO A 212 -28.849 -6.433 0.356 1.00 35.67

ANISOU 1460 N PRO A 212 3959 5733 3862 -512 -516 -1077

ATOM 1461 CA PRO A 212 -30.066 -6.638 1.149 1.00 38.65

ANISOU 1461 CA PRO A 212 4532 5915 4239 -426 -497 -1008

ATOM 1462 C PRO A 212 -30.695 -5.313 1.591 1.00 42.34

ANISOU 1462 C PRO A 212 5231 6201 4655 -714 -334 -1212

ATOM 1463 O PRO A 212 -31.908 -5.245 1.792 1.00 43.47

ANISOU 1463 O PRO A 212 5584 6044 4890 -631 -244 -1165

ATOM 1464 CB PRO A 212 -29.560 -7.417 2.371 1.00 38.33

ANISOU 1464 CB PRO A 212 4292 6294 3976 -329 -652 -877

ATOM 1465 CG PRO A 212 -28.306 -8.072 1.909 1.00 39.76

ANISOU 1465 CG PRO A 212 4171 6794 4142 -188 -751 -766

ATOM 1466 CD PRO A 212 -27.684 -7.130 0.926 1.00 36.53

ANISOU 1466 CD PRO A 212 3735 6351 3795 -432 -675 -973

ATOM 1467 N GLY A 213 -29.879 -4.275 1.743 1.00 46.71

ANISOU 1467 N GLY A 213 5750 6929 5068 -1056 -260 -1441

ATOM 1468 CA GLY A 213 -30.370 -3.002 2.237 1.00 57.26

ANISOU 1468 CA GLY A 213 7343 8066 6347 -1356 -32 -1660

ATOM 1469 C GLY A 213 -30.544 -3.012 3.746 1.00 67.77

ANISOU 1469 C GLY A 213 8691 9637 7422 -1495 -69 -1729

ATOM 1470 O GLY A 213 -30.227 -2.029 4.418 1.00 75.51

ANISOU 1470 O GLY A 213 9759 10726 8207 -1886 73 -1996

ATOM 1471 N LEU A 214 -31.050 -4.124 4.275 1.00 68.64

ANISOU 1471 N LEU A 214 8738 9824 7519 -1198 -230 -1500

ATOM 1472 CA LEU A 214 -31.171 -4.324 5.714 1.00 72.52

ANISOU 1472 CA LEU A 214 9215 10603 7737 -1281 -295 -1509

ATOM 1473 C LEU A 214 -29.792 -4.237 6.377 1.00 76.52

ANISOU 1473 C LEU A 214 9425 11755 7893 -1547 -452 -1622

ATOM 1474 O LEU A 214 -28.832 -4.836 5.891 1.00 80.57

ANISOU 1474 O LEU A 214 9640 12573 8401 -1419 -621 -1497

ATOM 1475 CB LEU A 214 -31.821 -5.679 6.001 1.00 72.73

ANISOU 1475 CB LEU A 214 9202 10599 7834 -876 -432 -1196

ATOM 1476 CG LEU A 214 -32.829 -5.724 7.153 1.00 76.24

ANISOU 1476 CG LEU A 214 9833 10963 8172 -872 -363 -1174

ATOM 1477 CD1 LEU A 214 -34.023 -4.835 6.852 1.00 76.68 ANISOU 1477 CD1 LEU A 214 10202 10499 8434 -936 -97 -1291

ATOM 1478 CD2 LEU A 214 -33.282 -7.147 7.422 1.00 75.49

ANISOU 1478 CD2 LEU A 214 9677 10874 8132 -492 -485 -857

ATOM 1479 N PRO A 215 -29.693 -3.477 7.482 1.00 74.33

ANISOU 1479 N PRO A 215 9217 11677 7349 -1900 -364 -1826

ATOM 1480 CA PRO A 215 -28.445 -3.192 8.204 1.00 78.01

ANISOU 1480 CA PRO A 215 9402 12670 7566 -2147 -429 -1867

ATOM 1481 C PRO A 215 -27.568 -4.413 8.491 1.00 77.72

ANISOU 1481 C PRO A 215 8953 13227 7350 -1887 -739 -1586

ATOM 1482 O PRO A 215 -28.050 -5.424 9.002 1.00 78.49

ANISOU 1482 O PRO A 215 9018 13441 7363 -1582 -891 -1348

ATOM 1483 CB PRO A 215 -28.940 -2.579 9.519 1.00 80.47

ANISOU 1483 CB PRO A 215 9897 12988 7691 -2395 -281 -1997

ATOM 1484 CG PRO A 215 -30.209 -1.907 9.145 1.00 77.82

ANISOU 1484 CG PRO A 215 9979 11985 7603 -2392 -2 -2112

ATOM 1485 CD PRO A 215 -30. 843 -2.780 8.085 1.00 72.72

ANISOU 1485 CD PRO A 215 9376 11074 7181 -2013 -113 -1949

ATOM 1486 N ARG A 216 -26.287 -4.294 8.149 1.00 77.20

ANISOU 1486 N ARG A 216 8583 13513 7238 -1983 -791 -1587

ATOM 1487 CA ARG A 216 -25.263 -5.301 8.445 1.00 76.71

ANISOU 1487 CA ARG A 216 8096 14039 7013 -1736 -1018 -1299

ATOM 1488 C ARG A 216 -25.411 -6.641 7.724 1.00 70.33

ANISOU 1488 C ARG A 216 7171 13170 6380 -1202 -1177 -966

ATOM 1489 O ARG A 216 -24.664 -7.578 8.000 1.00 73.22

ANISOU 1489 O ARG A 216 7224 13942 6654 -903 -1308 -657

ATOM 1490 CB ARG A 216 -25.120 -5.525 9.954 1.00 80.40

ANISOU 1490 CB ARG A 216 8437 14963 7149 -1792 -1094 -1199

ATOM 1491 CG ARG A 216 -24.344 -4.435 10.676 1.00 84.53

ANISOU 1491 CG ARG A 216 8861 15833 7424 -2302 -977 -1461

ATOM 1492 CD ARG A 216 -24.271 -4.736 12.161 1.00 88.21

ANISOU 1492 CD ARG A 216 9191 16777 7548 -2348 -1066 -1351

ATOM 1493 NE ARG A 216 -25.573 -5.151 12.671 1.00 85.96

ANISOU 1493 NE ARG A 216 9203 16160 7298 -2156 -1073 -1269

ATOM 1494 CZ ARG A 216 -26.495 -4.316 13.141 1.00 86.52

ANISOU 1494 CZ ARG A 216 9631 15875 7366 -2441 -885 -1530

ATOM 1495 NH1 ARG A 216 -26.257 -3.010 13.180 1.00 88.78

ANISOU 1495 NH1 ARG A 216 10035 16062 7635 -2924 -654 -1878

ATOM 1496 NH2 ARG A 216 -27.654 -4.789 13.581 1.00 83.56

ANISOU 1496 NH2 ARG A 216 9508 15233 7010 -2232 -891 -1429

ATOM 1497 N HIS A 217 -26.363 -6.739 6.807 1.00 62.75

ANISOU 1497 N HIS A 217 6465 11701 5676 -1068 -1129 -1012

ATOM 1498 CA HIS A 217 -26.463 -7.942 5.987 1.00 62.50

ANISOU 1498 CA HIS A 217 6373 11463 5912 -563 -1175 -698

ATOM 1499 C HIS A 217 -25.479 -7.823 4.828 1.00 65.03

ANISOU 1499 C HIS A 217 6484 11851 6373 -573 -1168 -742

ATOM 1500 O HIS A 217 -25.343 -6.758 4.226 1.00 66.55

ANISOU 1500 O HIS A 217 6775 11887 6623 -924 -1059 -1042

ATOM 1501 CB HIS A 217 -27.894 -8.171 5.487 1.00 52.53

ANISOU 1501 CB HIS A 217 5515 9462 4981 -377 -1018 -667

ATOM 1502 CG HIS A 217 -28.839 -8.647 6.548 1.00 52.26

ANISOU 1502 CG HIS A 217 5646 9355 4856 -247 -1019 -531

ATOM 1503 ND1 HIS A 217 -30.058 -9.218 6.256 1.00 50.41

ANISOU 1503 ND1 HIS A 217 5684 8584 4886 -8 -909 -415

ATOM 1504 CD2 HIS A 217 -28. 742 -8.637 7.898 1.00 56.92

ANISOU 1504 CD2 HIS A 217 6156 10374 5097 -345 -1110 -496

ATOM 1505 CE1 HIS A 217 -30.675 -9.539 7.381 1.00 47.98

ANISOU 1505 CE1 HIS A 217 5468 8338 4423 48 -917 -312

ATOM 1506 NE2 HIS A 217 -29. 897 -9.198 8.389 1.00 54.70

ANISOU 1506 NE2 HIS A 217 6119 9766 4898 -143 -1039 -352 ATOM 1507 N ARG A 218 -24.781 -8.909 4.525 1.00 66.31 N

ANISOU 1507 N ARG A 218 6370 12232 6593 -178 -1247 -433 N

ATOM 1508 CA ARG A 218 -23.716 -8.846 3.532 1.00 70.57 C

ANISOU 1508 CA ARG A 218 6657 12928 7228 -178 -1239 -457 C ATOM 1509 C ARG A 218 -24.202 -9.022 2.093 1.00 63.43 C

ANISOU 1509 C ARG A 218 6011 11367 6720 -26 -1070 -489 C

ATOM 1510 O ARG A 218 -25.203 -9.690 1.832 1.00 60.94 O

ANISOU 1510 O ARG A 218 5974 10562 6619 233 -987 -367 O

ATOM 1511 CB ARG A 218 -22.596 -9.837 3.865 1.00 80.50 C ANISOU 1511 CB ARG A 218 7547 14646 8394 169 -1298 -102 C

ATOM 1512 CG ARG A 218 -23.058 -11.268 4.082 1.00 85.75 C

ANISOU 1512 CG ARG A 218 8253 15152 9175 729 -1282 299 C

ATOM 1513 CD ARG A 218 -22.727 -12.145 2.882 1.00 89.21 C

ANISOU 1513 CD ARG A 218 8640 15333 9924 1122 -1158 479 C ATOM 1514 NE ARG A 218 -21.956 -13.329 3.264 1.00 95.58 N

ANISOU 1514 NE ARG A 218 9282 16315 10719 1546 -1078 881 N

ATOM 1515 CZ ARG A 218 -20.634 -13.434 3.161 1.00 98.38 C

ANISOU 1515 CZ ARG A 218 9329 17058 10991 1591 -1063 988 C

ATOM 1516 NH1 ARG A 218 -19.917 -12.427 2.678 1.00 97.91 N ANISOU 1516 NH1 ARG A 218 9097 17244 10861 1222 -1120 716 N

ATOM 1517 NH2 ARG A 218 -20.027 -14.553 3.535 1.00101.44 N

ANISOU 1517 NH2 ARG A 218 9597 17580 11367 2002 -963 1373 N

ATOM 1518 N ALA A 219 -23.477 -8.400 1.170 1.00 59.93 N

ANISOU 1518 N ALA A 219 5467 10959 6346 -225 -1015 -665 N ATOM 1519 CA ALA A 219 -23.790 -8.469 -0.246 1.00 55.51 C

ANISOU 1519 CA ALA A 219 5115 9874 6103 -128 -863 -708 C

ATOM 1520 C ALA A 219 -23.398 -9.815 -0.852 1.00 56.92 C

ANISOU 1520 C ALA A 219 5164 10009 6453 338 -827 -422 C

ATOM 1521 O ALA A 219 -22.442 -10.451 -0.411 1.00 60.28 O ANISOU 1521 O ALA A 219 5235 10907 6763 554 -901 -205 O

ATOM 1522 CB ALA A 219 -23.096 -7.331 -0.992 1.00 52.08 C

ANISOU 1522 CB ALA A 219 4624 9502 5663 -505 -787 -982 C

ATOM 1523 N LEU A 220 -24.155 -10.241 -1.856 1.00 53.55 N

ANISOU 1523 N LEU A 220 5026 9029 6290 487 -688 -416 N ATOM 1524 CA LEU A 220 -23.800 -11.402 -2.657 1.00 57.04 C

ANISOU 1524 CA LEU A 220 5424 9328 6920 852 -571 -227 C

ATOM 1525 C LEU A 220 -23.313 -10.892 -4.013 1.00 56.16 C

ANISOU 1525 C LEU A 220 5315 9094 6929 700 -467 -403 C

ATOM 1526 O LEU A 220 -23.816 -9.887 -4.511 1.00 50.84 O ANISOU 1526 O LEU A 220 4839 8203 6274 395 -445 -629 O

ATOM 1527 CB LEU A 220 -25.005 -12.329 -2.838 1.00 58.79 C

ANISOU 1527 CB LEU A 220 5979 9039 7318 1072 -460 -130 C

ATOM 1528 CG LEU A 220 -25.604 -13.054 -1.628 1.00 63.69 C

ANISOU 1528 CG LEU A 220 6658 9674 7868 1276 -500 78 C ATOM 1529 CD1 LEU A 220 -26.574 -12.164 -0.864 1.00 61.78 C

ANISOU 1529 CD1 LEU A 220 6586 9381 7505 992 -605 -74 C

ATOM 1530 CD2 LEU A 220 -26.295 -14.343 -2.062 1.00 64.98 C

ANISOU 1530 CD2 LEU A 220 7067 9377 8244 1564 -303 218 C

ATOM 1531 N ARG A 221 -22.342 -11.579 -4.609 1.00 59.22 N ANISOU 1531 N ARG A 221 5491 9613 7397 933 -376 -278 N

ATOM 1532 CA ARG A 221 -21.719 -11.096 -5.840 1.00 61.34 C

ANISOU 1532 CA ARG A 221 5721 9836 7751 785 -271 -437 C

ATOM 1533 C ARG A 221 -21.753 -12.146 -6.949 1.00 60.07 C

ANISOU 1533 C ARG A 221 5700 9320 7805 1067 -57 -356 C ATOM 1534 O ARG A 221 -21.546 -13.332 -6.688 1.00 64.22 O

ANISOU 1534 O ARG A 221 6163 9834 8402 1443 39 -120 O

ATOM 1535 CB ARG A 221 -20.273 -10.691 -5.557 1.00 69.15 C

ANISOU 1535 CB ARG A 221 6254 11427 8594 703 -339 -423 C

ATOM 1536 CG ARG A 221 -19.622 -9.858 -6.643 1.00 74.50 C ANISOU 1536 CG ARG A 221 6883 12113 9312 431 -245 -637 C

ATOM 1537 CD ARG A 221 -19.061 -8.571 -6.055 1.00 80.92 C

ANISOU 1537 CD ARG A 221 7495 13342 9909 -16 -355 -841 C

ATOM 1538 NE ARG A 221 -18.220 -7.843 -7.002 1.00 86.78 N ANISOU 1538 NE ARG A 221 8126 14168 10677 -269 -239 -1018 N

ATOM 1539 CZ ARG A 221 -17.605 -6.696 -6.728 1.00 91.22 C

ANISOU 1539 CZ ARG A 221 8529 15054 11076 -718 -258 -1240 C

ATOM 1540 NH1 ARG A 221 -17.736 -6.138 -5.531 1.00 93.51 N

ANISOU 1540 NH1 ARG A 221 8757 15625 11146 -980 -392 -1334 N ATOM 1541 NH2 ARG A 221 -16.856 -6.106 -7.650 1.00 92.52 N

ANISOU 1541 NH2 ARG A 221 8613 15256 11286 -935 -116 -1389 N

ATOM 1542 N THR A 222 -22.013 -11.718 -8.185 1.00 51.43 N

ANISOU 1542 N THR A 222 4810 7932 6800 884 49 -546 N

ATOM 1543 CA THR A 222 -22.006 -12.648 -9.310 1.00 45.77 C ANISOU 1543 CA THR A 222 4239 6904 6247 1076 273 -525 C

ATOM 1544 C THR A 222 -20.589 -12.935 -9.746 1.00 46.68 C

ANISOU 1544 C THR A 222 4045 7290 6401 1235 397 -449 C

ATOM 1545 O THR A 222 -19.659 -12.212 -9.393 1.00 49.01 O

ANISOU 1545 O THR A 222 4013 8023 6587 1111 290 -462 O ATOM 1546 CB THR A 222 -22.721 -12.100 -10.565 1.00 40.08 C

ANISOU 1546 CB THR A 222 3814 5853 5560 820 342 -740 C

ATOM 1547 OG1 THR A 222 -21.934 -11.049 -11.149 1.00 39.50 O

ANISOU 1547 OG1 THR A 222 3603 5971 5433 588 341 -869 O

ATOM 1548 CG2 THR A 222 -24.118 -11.610 -10.245 1.00 33.37 C ANISOU 1548 CG2 THR A 222 3224 4792 4664 647 222 -806 C

ATOM 1549 N ALA A 223 -20.436 -13.991 -10.534 1.00 48.38 N

ANISOU 1549 N ALA A 223 4368 7247 6768 1486 651 -388 N

ATOM 1550 CA ALA A 223 -19.189 -14.242 -11.230 1.00 53.41 C

ANISOU 1550 CA ALA A 223 4768 8054 7472 1631 835 -344 C ATOM 1551 C ALA A 223 -19.044 -13.175 -12.313 1.00 51.54 C

ANISOU 1551 C ALA A 223 4592 7796 7194 1261 834 -604 C

ATOM 1552 O ALA A 223 -20.034 -12.751 -12.903 1.00 50.26 O

ANISOU 1552 O ALA A 223 4759 7326 7011 1020 812 -777 O

ATOM 1553 CB ALA A 223 -19.204 -15.632 -11.840 1.00 57.54 C ANISOU 1553 CB ALA A 223 5481 8207 8175 1967 1174 -248 C

ATOM 1554 N PRO A 224 -17.810 -12.730 -12.573 1.00 54.63 N

ANISOU 1554 N PRO A 224 4650 8546 7562 1222 869 -609 N

ATOM 1555 CA PRO A 224 -17.577 -11.657 -13.548 1.00 55.86 C

ANISOU 1555 CA PRO A 224 4854 8697 7672 865 895 -837 C ATOM 1556 C PRO A 224 -17.873 -12.049 -15.000 1.00 54.73 C

ANISOU 1556 C PRO A 224 5024 8158 7614 858 1138 -954 C

ATOM 1557 O PRO A 224 -17.922 -13.229 -15.339 1.00 55.67 O

ANISOU 1557 O PRO A 224 5256 8049 7845 1137 1348 -878 O

ATOM 1558 CB PRO A 224 -16.077 -11.385 -13.404 1.00 58.83 C ANISOU 1558 CB PRO A 224 4748 9587 8019 883 919 -778 C

ATOM 1559 CG PRO A 224 -15.507 -12.691 -12.937 1.00 61.58 C

ANISOU 1559 CG PRO A 224 4861 10075 8462 1376 1031 -493 C

ATOM 1560 CD PRO A 224 -16.550 -13.239 -11.999 1.00 58.87 C

ANISOU 1560 CD PRO A 224 4723 9535 8109 1527 908 -375 C ATOM 1561 N ILE A 225 -18.074 -11.047 -15.846 1.00 51.61 N

ANISOU 1561 N ILE A 225 4782 7680 7148 529 1137 -1137 N

ATOM 1562 CA ILE A 225 -18.102 -11.260 -17.282 1.00 52.32 C

ANISOU 1562 CA ILE A 225 5094 7527 7260 478 1363 -1251 C

ATOM 1563 C ILE A 225 -17.010 -10.414 -17.925 1.00 57.00 C ANISOU 1563 C ILE A 225 5484 8350 7822 296 1456 -1333 C

ATOM 1564 O ILE A 225 -16.805 -9.259 -17.550 1.00 58.70 O

ANISOU 1564 O ILE A 225 5584 8761 7959 38 1327 -1388 O

ATOM 1565 CB ILE A 225 -19.468 -10.924 -17.890 1.00 49.00 C

ANISOU 1565 CB ILE A 225 5071 6797 6749 272 1305 -1360 C ATOM 1566 CGI ILE A 225 -19.898 -9.516 -17.485 1.00 45.86 C

ANISOU 1566 CGI ILE A 225 4694 6480 6252 1 1107 -1394 C

ATOM 1567 CG2 ILE A 225 -20.501 -11.963 -17.461 1.00 52.01 C

ANISOU 1567 CG2 ILE A 225 5654 6937 7169 435 1281 -1308 C ATOM 1568 CD1 ILE A 225 -21.317 -9.174 -17.860 1.00 43.20 C

ANISOU 1568 CD1 ILE A 225 4685 5902 5828 -128 1028 -1421 C

ATOM 1569 N GLN A 226 -16.295 -11.001 -18.879 1.00 56.97 N

ANISOU 1569 N GLN A 226 5452 8310 7883 415 1720 -1355 N

ATOM 1570 CA GLN A 226 -15.162 -10.327 -19.494 1.00 59.44 C ANISOU 1570 CA GLN A 226 5542 8860 8183 267 1847 -1420 C

ATOM 1571 C GLN A 226 -15.294 -10.303 -21.007 1.00 56.79 C

ANISOU 1571 C GLN A 226 5496 8276 7806 144 2076 -1557 C

ATOM 1572 O GLN A 226 -14.728 -11.147 -21.695 1.00 57.56 O

ANISOU 1572 O GLN A 226 5581 8309 7978 326 2344 -1561 O ATOM 1573 CB GLN A 226 -13.861 -11.025 -19.109 1.00 67.12 C

ANISOU 1573 CB GLN A 226 6078 10159 9268 565 1975 -1276 C

ATOM 1574 CG GLN A 226 -13.774 -11.402 -17.644 1.00 71.54 C

ANISOU 1574 CG GLN A 226 6351 10987 9844 786 1774 -1081 C

ATOM 1575 CD GLN A 226 -12.366 -11.766 -17.230 1.00 80.11 C ANISOU 1575 CD GLN A 226 6893 12559 10984 1034 1856 -902 C

ATOM 1576 OE1 GLN A 226 -11.413 -11.579 -17.992 1.00 82.14 O

ANISOU 1576 OE1 GLN A 226 6959 12976 11273 991 2051 -951 O

ATOM 1577 NE2 GLN A 226 -12.225 -12.287 -16.015 1.00 83.78 N

ANISOU 1577 NE2 GLN A 226 7082 13302 11446 1309 1713 -672 N ATOM 1578 N PRO A 227 -16.050 -9.334 -21.532 1.00 53.08 N

ANISOU 1578 N PRO A 227 5293 7671 7202 -154 1994 -1652 N

ATOM 1579 CA PRO A 227 -16.239 -9.248 -22.979 1.00 50.77 C

ANISOU 1579 CA PRO A 227 5273 7204 6811 -286 2187 -1757 C

ATOM 1580 C PRO A 227 -15.030 -8.619 -23.640 1.00 53.77 C ANISOU 1580 C PRO A 227 5468 7770 7193 -418 2379 -1810 C

ATOM 1581 O PRO A 227 -14.169 -8.066 -22.953 1.00 58.42 O

ANISOU 1581 O PRO A 227 5724 8633 7839 -474 2331 -1785 O

ATOM 1582 CB PRO A 227 -17.443 -8.319 -23.111 1.00 50.03 C

ANISOU 1582 CB PRO A 227 5461 6980 6570 -509 2011 -1760 C ATOM 1583 CG PRO A 227 -17.346 -7.431 -21.915 1.00 50.06 C

ANISOU 1583 CG PRO A 227 5282 7126 6612 -595 1818 -1709 C

ATOM 1584 CD PRO A 227 -16.824 -8.312 -20.807 1.00 50.97 C

ANISOU 1584 CD PRO A 227 5104 7403 6859 -352 1747 -1642 C

ATOM 1585 N ARG A 228 -14.973 -8.719 -24.963 1.00 50.72 N ANISOU 1585 N ARG A 228 5287 7263 6720 -494 2602 -1896 N

ATOM 1586 CA ARG A 228 -13.924 -8.096 -25.752 1.00 52.31 C

ANISOU 1586 CA ARG A 228 5368 7604 6902 -644 2819 -1953 C

ATOM 1587 C ARG A 228 -14.447 -6.739 -26.213 1.00 51.62 C

ANISOU 1587 C ARG A 228 5501 7457 6655 -952 2761 -1962 C ATOM 1588 O ARG A 228 -15.626 -6.612 -26.545 1.00 49.02 O

ANISOU 1588 O ARG A 228 5487 6952 6188 -999 2655 -1933 O

ATOM 1589 CB ARG A 228 -13.594 -8.977 -26.962 1.00 54.23 C

ANISOU 1589 CB ARG A 228 5750 7736 7121 -553 3132 -2038 C

ATOM 1590 CG ARG A 228 -13.296 -10.431 -26.628 1.00 56.69 C ANISOU 1590 CG ARG A 228 5963 7982 7596 -209 3274 -2014 C

ATOM 1591 CD ARG A 228 -12.804 -11.215 -27.843 1.00 59.34 C

ANISOU 1591 CD ARG A 228 6473 8170 7904 -138 3551 -2057 C

ATOM 1592 NE ARG A 228 -13.865 -11.513 -28.804 1.00 57.74 N

ANISOU 1592 NE ARG A 228 6718 7721 7499 -303 3565 -2172 N ATOM 1593 CZ ARG A 228 -13.711 -12.295 -29.871 1.00 60.26 C

ANISOU 1593 CZ ARG A 228 7261 7881 7754 -302 3774 -2244 C

ATOM 1594 NH1 ARG A 228 -12.539 -12.863 -30.125 1.00 60.53 N

ANISOU 1594 NH1 ARG A 228 7141 7930 7929 -105 4013 -2204 N

ATOM 1595 NH2 ARG A 228 -14.733 -12.510 -30.685 1.00 56.90 N ANISOU 1595 NH2 ARG A 228 7196 7316 7108 -509 3743 -2353

ATOM 1596 N VAL A 229 -13.587 -5.725 -26.223 1, 00 49. 99)

ANISOU 1596 N VAL A 229 5123 7406 6465 -1159 2852 -1987

ATOM 1597 CA VAL A 229 -14.010 -4.384 -26.630 1, 00 53. 15)

ANISOU 1597 CA VAL A 229 5756 7699 6739 -1431 2875 -1969

ATOM 1598 C VAL A 229 -13.345 -3.938 -27.927 1, 00 54. 39

ANISOU 1598 C VAL A 229 5998 7860 6807 -1586 3174 -2012

ATOM 1599 O VAL A 229 -12.123 -3.841 -28.005 1, 00 54. 21

ANISOU 1599 O VAL A 229 5709 8016 6873 -1656 3332 -2076

ATOM 1600 CB VAL A 229 -13.733 -3.333 -25.522 1, 00 55. 30

ANISOU 1600 CB VAL A 229 5858 8072 7081 -1634 2780 -1982

ATOM 1601 CGI VAL A 229 -13.961 -1.924 -26.049 1, 00 50. 14

ANISOU 1601 CGI VAL A 229 5467 7253 6331 -1911 2932 -1963

ATOM 1602 CG2 VAL A 229 -14.617 -3.592 -24.332 1, 00 47. 21

ANISOU 1602 CG2 VAL A 229 4841 7005 6094 -1512 2490 -1926

ATOM 1603 N TRP A 230 -14.151 -3.665 -28.948 1, 00 56. 90

ANISOU 1603 N TRP A 230 6675 8012 6932 -1632 3229 -1951

ATOM 1604 CA TRP A 230 -13.595 -3.259 -30.228 1, 00 63. 80

ANISOU 1604 CA TRP A 230 7670 8884 7689 -1761 3490 -1958

ATOM 1605 C TRP A 230 -13.376 -1.754 -30.309 1, 00 68.

ANISOU 1605 C TRP A 230 8391 9443 8300 -2000 3587 -1885

ATOM 1606 O TRP A 230 -14.282 -0.969 -30.029 1, 00 69. 03

ANISOU 1606 O TRP A 230 8625 9340 8262 -2058 3541 -1776

ATOM 1607 CB TRP A 230 -14.455 -3.725 -31.404 1, 00 66. 99

ANISOU 1607 CB TRP A 230 8399 9208 7845 -1706 3510 -1913

ATOM 1608 CG TRP A 230 -13.632 -3.814 -32.646 1, 00 75. 10

ANISOU 1608 CG TRP A 230 9475 10261 8799 -1754 3711 -1940

ATOM 1609 CD1 TRP A 230 -13.215 -2.779 -33.436 1, 00 77. 56

ANISOU 1609 CD1 TRP A 230 9896 10551 9022 -1914 3865 -1860

ATOM 1610 CD2 TRP A 230 -13.072 -5.001 -33.215 1, 00 78.

ANISOU 1610 CD2 TRP A 230 9877 10739 9279 -1635 3811 -2050

ATOM 1611 NE1 TRP A 230 -12.444 -3.253 -34.470 1, 00 79. 94

ANISOU 1611 NE1 TRP A 230 10201 10895 9277 -1910 4035 -1924

ATOM 1612 CE2 TRP A 230 -12.343 -4.615 -34.357 1, 00 81. S7

ANISOU 1612 CE2 TRP A 230 10352 11162 9593 -1741 4013 -2043

ATOM 1613 CE3 TRP A 230 -13.133 -6.355 -32.878 1, 00 79. 91

ANISOU 1613 CE3 TRP A 230 9962 10866 9532 -1438 3780 -2141

ATOM 1614 CZ2 TRP A 230 -11.676 -5.535 -35.161 1, 00 87. 13

ANISOU 1614 CZ2 TRP A 230 11013 11835 10259 -1666 4180 -2138

ATOM 1615 CZ3 TRP A 230 -12.468 -7.265 -33.669 1, 00 83. 48

ANISOU 1615 CZ3 TRP A 230 10429 11292 9999 -1355 3967 -2222

ATOM 1616 CH2 TRP A 230 -11.747 -6.851 -34.796 1, 00 87.

ANISOU 1616 CH2 TRP A 230 11048 11884 10460 -1473 4162 -2226

ATOM 1617 N GLU A 231 -12.169 -1.364 -30.707 1, 00 73. 11

ANISOU 1617 N GLU A 231 8805 10058 8915 -2124 3747 -1937

ATOM 1618 CA GLU A 231 -11.815 0.044 -30.834 1, 00 79. 06 3

ANISOU 1618 CA GLU A 231 9665 10707 9668 -2370 3882 -1897

ATOM 1619 C GLU A 231 -12.338 0.644 -32.132 1, 00 85. 07i

ANISOU 1619 C GLU A 231 10803 11296 10223 -2388 4035 -1737

ATOM 1620 O GLU A 231 -12.214 0.041 -33.199 1, 00 88. 235

ANISOU 1620 O GLU A 231 11274 11752 10498 -2304 4106 -1727

ATOM 1621 CB GLU A 231 -10.298 0.224 -30.743 1, 00 82. 3

ANISOU 1621 CB GLU A 231 9752 11276 10197 -2515 3990 -2025

ATOM 1622 CG GLU A 231 -9.744 -0.003 -29.349 1, 00 83. 11 L

ANISOU 1622 CG GLU A 231 9476 11627 10474 -2546 3827 -2136

ATOM 1623 CD GLU A 231 -10.396 0.902 -28.320 1, 00 83. 465

ANISOU 1623 CD GLU A 231 9624 11552 10533 -2713 3725 -2144

ATOM 1624 OE1 GLU A 231 -10.496 2.121 -28.582 1, 00 84. 72>

ANISOU 1624 OE1 GLU A 231 10049 11489 10654 -2925 3876 -2124 ATOM 1625 OE2 GLU A 231 -10.817 0.394 -27.256 1.00 81.52

ANISOU 1625 OE2 GLU A 231 9217 11413 10342 -2616 3518 -2165

ATOM 1626 OXT GLU A 231 -12.891 1.747 -32.138 1.00 87.03

ANISOU 1626 OXT GLU A 231 11295 11353 10420 -2472 4100 -1599

TER 1627 GLU A 231

ATOM 1628 N GLY B 20 -16. 985 -40.319 22.502 1.00 32.35

ANISOU 1628 N GLY B 20 2569 3623 6100 1323 844 392

ATOM 1629 CA GLY B 20 -18.030 -39.993 21.546 1.00 37.38

ANISOU 1629 CA GLY B 20 3430 4198 6576 1304 964 308

ATOM 1630 C GLY B 20 -17.464 -39.337 20.302 1.00 37.45

ANISOU 1630 C GLY B 20 3447 4228 6555 1294 1209 237

ATOM 1631 O GLY B 20 -16.249 -39.284 20.112 1.00 39.46

ANISOU 1631 O GLY B 20 3528 4532 6934 1304 1304 245

ATOM 1632 N ALA B 21 -18.342 -38.836 19.444 1.00 37.99

ANISOU 1632 N ALA B 21 3737 4272 6425 1257 1297 172

ATOM 1633 CA ALA B 21 -17. 894 -38.158 18.233 1.00 39.03

ANISOU 1633 CA ALA B 21 3920 4429 6480 1243 1540 127

ATOM 1634 C ALA B 21 -17. 697 -36.665 18.503 1.00 37.93

ANISOU 1634 C ALA B 21 3726 4373 6313 1085 1536 196

ATOM 1635 O ALA B 21 -18. 095 -36.157 19.548 1.00 36.28

ANISOU 1635 O ALA B 21 3485 4197 6103 990 1336 245

ATOM 1636 CB ALA B 21 -18. 895 -38.373 17.106 1.00 36.37

ANISOU 1636 CB ALA B 21 3881 4036 5901 1278 1608 28

ATOM 1637 N MET B 22 -17. 074 -35.976 17.559 1.00 32.84

ANISOU 1637 N MET B 22 3080 3751 5648 1055 1771 196

ATOM 1638 CA MET B 22 -16.958 -34.529 17.617 1.00 35.34

ANISOU 1638 CA MET B 22 3388 4105 5936 898 1800 259

ATOM 1639 C MET B 22 -18.338 -33.887 17.627 1.00 36.06

ANISOU 1639 C MET B 22 3739 4169 5792 836 1665 257

ATOM 1640 O MET B 22 -19.195 -34.211 16.806 1.00 33.76

ANISOU 1640 O MET B 22 3682 3846 5300 904 1692 209

ATOM 1641 CB MET B 22 -16.129 -34.014 16.438 1.00 35.98

ANISOU 1641 CB MET B 22 3458 4197 6016 887 2118 275

ATOM 1642 CG MET B 22 -14.625 -34.150 16.653 1.00 37.21

ANISOU 1642 CG MET B 22 3276 4399 6463 886 2245 304

ATOM 1643 SD MET B 22 -14.032 -32.831 17.745 1.00 37.36

ANISOU 1643 SD MET B 22 3052 4459 6683 669 2120 383

ATOM 1644 CE MET B 22 -12.277 -33.187 17.753 1.00 40.63

ANISOU 1644 CE MET B 22 3124 4939 7373 669 2209 394

ATOM 1645 N ALA B 23 -18.557 -32.985 18.575 1.00 29.66

ANISOU 1645 N ALA B 23 2881 3374 5015 712 1510 299

ATOM 1646 CA ALA B 23 -19.864 -32.380 18.722 1.00 30.86

ANISOU 1646 CA ALA B 23 3246 3499 4982 670 1377 297

ATOM 1647 C ALA B 23 -19.734 -30.906 19.036 1.00 28.06

ANISOU 1647 C ALA B 23 2881 3128 4652 525 1378 343

ATOM 1648 O ALA B 23 -18. 698 -30.449 19.510 1.00 31.77

ANISOU 1648 O ALA B 23 3147 3617 5305 432 1408 365

ATOM 1649 CB ALA B 23 -20. 663 -33.090 19.823 1.00 26.26

ANISOU 1649 CB ALA B 23 2656 2929 4393 699 1135 274

ATOM 1650 N GLN B 24 -20.785 -30.159 18.748 1.00 27.16

ANISOU 1650 N GLN B 24 2980 2968 4370 507 1343 355

ATOM 1651 CA GLN B 24 -20.867 -28.804 19.235 1.00 34.82

ANISOU 1651 CA GLN B 24 3964 3891 5374 381 1306 384

ATOM 1652 C GLN B 24 -21.427 -28.851 20.644 1.00 31.81

ANISOU 1652 C GLN B 24 3530 3539 5017 352 1070 336

ATOM 1653 O GLN B 24 -22.426 -29.533 20.903 1.00 24.39

ANISOU 1653 O GLN B 24 2674 2622 3970 433 948 308

ATOM 1654 CB GLN B 24 -21.754 -27.949 18.343 1.00 39.68

ANISOU 1654 CB GLN B 24 4831 4434 5813 396 1369 429 ATOM 1655 CG GLN B 24 -21.945 -26.551 18.882 1.00 45.38

ANISOU 1655 CG GLN B 24 5586 5070 6585 282 1328 453

ATOM 1656 CD GLN B 24 -22.740 -25.684 17.944 1.00 52.12

ANISOU 1656 CD GLN B 24 6684 5836 7285 317 1397 527

ATOM 1657 OE1 GLN B 24 -22.873 -25.995 16.757 1.00 58.87

ANISOU 1657 OE1 GLN B 24 7672 6705 7991 402 1513 576

ATOM 1658 NE2 GLN B 24 -23.278 -24.586 18.465 1.00 47.62

ANISOU 1658 NE2 GLN B 24 6183 5171 6739 262 1324 533

ATOM 1659 N ASN B 25 -20.758 -28.150 21.554 1.00 31.66

ANISOU 1659 N ASN B 25 3369 3523 5138 228 1012 322

ATOM 1660 CA ASN B 25 -21.174 -28.083 22.946 1.00 37.01

ANISOU 1660 CA ASN B 25 4007 4241 5813 191 800 269

ATOM 1661 C ASN B 25 -22.314 -27.084 23.121 1.00 37.69

ANISOU 1661 C ASN B 25 4284 4254 5783 169 753 245

ATOM 1662 O ASN B 25 -22.223 -25.940 22.682 1.00 44.68

ANISOU 1662 O ASN B 25 5244 5038 6695 97 847 261

ATOM 1663 CB ASN B 25 -19. 985 -27.693 23.820 1.00 49.28

ANISOU 1663 CB ASN B 25 5341 5835 7547 64 737 242

ATOM 1664 CG ASN B 25 -20. 314 -27.716 25.297 1.00 59.39

ANISOU 1664 CG ASN B 25 6591 7184 8789 33 510 181

ATOM 1665 OD1 ASN B 25 -20. 648 -28.766 25.850 1.00 63.19

ANISOU 1665 OD1 ASN B 25 7053 7748 9207 124 399 194

ATOM 1666 ND2 ASN B 25 -20. 212 -26.559 25.950 1.00 61.01

ANISOU 1666 ND2 ASN B 25 6805 7350 9026 -100 448 113

ATOM 1667 N ILE B 26 -23.404 -27.533 23.728 1.00 31.52

ANISOU 1667 N ILE B 26 3578 3511 4886 239 623 216

ATOM 1668 CA ILE B 26 -24.544 -26.668 24.000 1.00 27.46

ANISOU 1668 CA ILE B 26 3217 2939 4278 243 578 185

ATOM 1669 C ILE B 26 -24.821 -26.665 25.497 1.00 27.12

ANISOU 1669 C ILE B 26 3126 2962 4215 208 424 115

ATOM 1670 O ILE B 26 -24.969 -27.725 26.113 1.00 27.35

ANISOU 1670 O ILE B 26 3093 3092 4208 255 334 122

ATOM 1671 CB ILE B 26 -25.813 -27.172 23.285 1.00 27.13

ANISOU 1671 CB ILE B 26 3314 2893 4101 369 579 213

ATOM 1672 CGI ILE B 26 -25.636 -27.150 21.763 1.00 27.67

ANISOU 1672 CGI ILE B 26 3471 2910 4131 416 719 276

ATOM 1673 CG2 ILE B 26 -27.019 -26.353 23.711 1.00 30.34

ANISOU 1673 CG2 ILE B 26 3833 3254 4439 392 520 181

ATOM 1674 CD1 ILE B 26 -25.403 -25.757 21.165 1.00 23.84

ANISOU 1674 CD1 ILE B 26 3083 2307 3667 359 832 322

ATOM 1675 N THR B 27 -24.865 -25.483 26.092 1.00 31.81

ANISOU 1675 N THR B 27 3763 3494 4829 124 401 47

ATOM 1676 CA THR B 27 -25.283 -25.356 27.483 1.00 34.79

ANISOU 1676 CA THR B 27 4143 3936 5140 102 271 -39

ATOM 1677 C THR B 27 -26. 649 -24.682 27.513 1.00 36.84

ANISOU 1677 C THR B 27 4563 4124 5309 169 293 -74

ATOM 1678 O THR B 27 -26. 809 -23.556 27.046 1.00 39.54

ANISOU 1678 O THR B 27 5001 4326 5696 148 366 -91

ATOM 1679 CB THR B 27 -24.294 -24.533 28.320 1.00 35.97

ANISOU 1679 CB THR B 27 4216 4075 5374 -46 206 -133

ATOM 1680 OG1 THR B 27 -24.386 -23.158 27.939 1.00 40.07

ANISOU 1680 OG1 THR B 27 4839 4425 5959 -111 290 -179

ATOM 1681 CG2 THR B 27 -22.872 -25.026 28.112 1.00 32.67

ANISOU 1681 CG2 THR B 27 3605 3713 5095 -114 199 -90

ATOM 1682 N ALA B 28 -27.635 -25.388 28.049 1.00 32.66

ANISOU 1682 N ALA B 28 4054 3684 4671 254 239 -73

ATOM 1683 CA ALA B 28 -29.008 -24.916 28.033 1.00 28.85

ANISOU 1683 CA ALA B 28 3682 3156 4124 340 267 -96

ATOM 1684 C ALA B 28 -29.495 -24.751 29.463 1.00 28.03 ANISOU 1684 C ALA B 28 3592 3126 3932 330 209 -191

ATOM 1685 O ALA B 28 -29.262 -25.611 30.301 1, 00 27. 41

ANISOU 1685 O ALA B 28 3446 3180 3788 313 138 -181

ATOM 1686 CB ALA B 28 -29.892 -25.907 27.278 1, 00 25.

ANISOU 1686 CB ALA B 28 3303 2816 3703 448 276 -11

ATOM 1687 N ARG B 29 -30.179 -23.648 29.736 1, 00 28. 02

ANISOU 1687 N ARG B 29 3689 3036 3923 354 249 -277

ATOM 1688 CA ARG B 29 -30.663 -23.373 31.078 1, 00 25.

ANISOU 1688 CA ARG B 29 3466 2842 3561 353 225 -390

ATOM 1689 C ARG B 29 -32.011 -24.042 31.305 1, 00 27. 50

ANISOU 1689 C ARG B 29 3652 3124 3674 469 257 -349

ATOM 1690 O ARG B 29 -32.918 -23.938 30.469 1, 00 29. 51

ANISOU 1690 O ARG B 29 3919 3314 3979 565 309 -298

ATOM 1691 CB ARG B 29 -30.765 -21.868 31.290 1, 00 27. 80

ANISOU 1691 CB ARG B 29 3808 2916 3839 332 270 -523

ATOM 1692 CG ARG B 29 -31.155 -21.448 32.681 1, 00 31. 13

ANISOU 1692 CG ARG B 29 4292 3394 4142 327 259 -680

ATOM 1693 CD ARG B 29 -30.910 -19.962 32.853 1, 00 33. 36

ANISOU 1693 CD ARG B 29 4686 3487 4503 273 289 336

ATOM 1694 NE ARG B 29 -31.329 -19.492 34.165 1, 00 39. 57

ANISOU 1694 NE ARG B 29 5559 4317 5160 280 292 -1020

ATOM 1695 CZ ARG B 29 -31.214 -18.233 34.579 1, 00 45. 09

ANISOU 1695 CZ ARG B 29 6375 4854 5902 236 316 -1204

ATOM 1696 NH1 ARG B 29 -30.696 -17.311 33.778 1, 00 45. il

ANISOU 1696 NH1 ARG B 29 6504 4717 6186 174 341 -1207

ATOM 1697 NH2 ARG B 29 -31.626 -17.896 35.793 1, 00 47. 435

ANISOU 1697 NH2 ARG B 29 6763 5210 6048 254 327 -1387

ATOM 1698 N ILE B 30 -32.121 -24.745 32.429 1, 00 23. i

ANISOU 1698 N ILE B 30 3164 2818 3092 456 221 -360

ATOM 1699 CA ILE B 30 -33.352 -25.427 32.830 1, 00 25. 44

ANISOU 1699 CA ILE B 30 3337 3109 3218 540 272 -315

ATOM 1700 C ILE B 30 -34.565 -24.483 32.836 1, 00 25. 94

ANISOU 1700 C ILE B 30 3454 3100 3302 637 372 -394

ATOM 1701 O ILE B 30 -34.486 -23.369 33.344 1, 00 24.

ANISOU 1701 O ILE B 30 3421 2909 3161 631 403 -530

ATOM 1702 CB ILE B 30 -33.178 -26.066 34.223 1, 00 23.

ANISOU 1702 CB ILE B 30 3132 3072 2849 499 238 -320

ATOM 1703 CGI ILE B 30 -32.192 -27.232 34.147 1, 00 26. 54

ANISOU 1703 CGI ILE B 30 3397 3488 3200 444 137 -200

ATOM 1704 CG2 ILE B 30 -34.517 -26.523 34.793 1, 00 24. 17

ANISOU 1704 CG2 ILE B 30 3163 3204 2817 575 335 -289

ATOM 1705 CD1 ILE B 30 -31.574 -27.595 35.493 1, 00 28. 02

ANISOU 1705 CD1 ILE B 30 3601 3823 3220 390 53 -207

ATOM 1706 N GLY B 31 -35.679 -24.927 32.255 1, 00 24. 40

ANISOU 1706 N GLY B 31 3195 2912 3163 729 416 -317

ATOM 1707 CA GLY B 31 -36.874 -24.103 32.183 1, 00 24. 66

ANISOU 1707 CA GLY B 31 3240 2882 3247 844 503 -373

ATOM 1708 C GLY B 31 -36.964 -23.247 30.922 1, 00 27. 42

ANISOU 1708 C GLY B 31 3629 3061 3728 909 491 -356

ATOM 1709 O GLY B 31 -38.036 -22.739 30.566 1, 00 29. 12

ANISOU 1709 O GLY B 31 3825 3221 4018 1032 535 -358

ATOM 1710 N GLU B 32 -35.842 -23.083 30.234 1, 00 25. 27

ANISOU 1710 N GLU B 32 3406 2708 3487 832 436 -325

ATOM 1711 CA GLU B 32 -35.831 -22.280 29.018 1, 00 32. 69

ANISOU 1711 CA GLU B 32 4407 3485 4527 885 437 -280

ATOM 1712 C GLU B 32 -35.918 -23.130 27.749 1, 00 33. 53

ANISOU 1712 C GLU B 32 4467 3622 4652 911 381 -145

ATOM 1713 O GLU B 32 -35.468 -24.274 27.732 1, 00 34. 64

ANISOU 1713 O GLU B 32 4543 3868 4752 846 339 -99 ATOM 1714 CB GLU B 32 -34.603 -21.377 28.982 1.00 35.03

ANISOU 1714 CB GLU B 32 4799 3650 4860 783 445 -331

ATOM 1715 CG GLU B 32 -34.735 -20.156 29.874 1.00 42.34

ANISOU 1715 CG GLU B 32 5815 4468 5805 788 500 -484

ATOM 1716 CD GLU B 32 -33.589 -19.191 29.687 1.00 53.05

ANISOU 1716 CD GLU B 32 7260 5655 7242 672 505 -531

ATOM 1717 OE1 GLU B 32 -32.870 -19.307 28.667 1.00 53.20

ANISOU 1717 OE1 GLU B 32 7274 5622 7318 621 494 -418

ATOM 1718 OE2 GLU B 32 -33.399 -18.323 30.565 1.00 60.22

ANISOU 1718 OE2 GLU B 32 8243 6480 8158 626 527 -690

ATOM 1719 N PRO B 33 -36.515 -22.572 26.684 1.00 31.28

ANISOU 1719 N PRO B 33 4224 3239 4421 1016 374 -84

ATOM 1720 CA PRO B 33 -36.631 -23.318 25.432 1.00 25.38

ANISOU 1720 CA PRO B 33 3459 2527 3658 1045 308 24

ATOM 1721 C PRO B 33 -35.270 -23.543 24.800 1.00 23.44

ANISOU 1721 C PRO B 33 3270 2251 3384 944 316 69

ATOM 1722 O PRO B 33 -34.334 -22.804 25.066 1.00 23.95

ANISOU 1722 O PRO B 33 3394 2229 3478 867 370 39

ATOM 1723 CB PRO B 33 -37.459 -22.383 24.542 1.00 27.37

ANISOU 1723 CB PRO B 33 3775 2670 3955 1186 293 78

ATOM 1724 CG PRO B 33 -37.191 -21.017 25.088 1.00 31.19

ANISOU 1724 CG PRO B 33 4354 2998 4501 1192 374 18

ATOM 1725 CD PRO B 33 -37.095 -21.218 26.573 1.00 31.25

ANISOU 1725 CD PRO B 33 4300 3082 4490 1121 418 -111

ATOM 1726 N LEU B 34 -35.173 -24.565 23.961 1.00 23.84

ANISOU 1726 N LEU B 34 3295 2372 3392 943 270 130

ATOM 1727 CA LEU B 34 -33.947 -24.852 23.245 1.00 25.44

ANISOU 1727 CA LEU B 34 3541 2555 3570 871 302 173

ATOM 1728 C LEU B 34 -34.281 -25.225 21.804 1.00 29.90

ANISOU 1728 C LEU B 34 4169 3126 4067 944 265 247

ATOM 1729 O LEU B 34 -35.126 -26.084 21.560 1.00 29.86

ANISOU 1729 O LEU B 34 4110 3200 4033 992 181 240

ATOM 1730 CB LEU B 34 -33.178 -25.990 23.930 1.00 21.76

ANISOU 1730 CB LEU B 34 2974 2188 3105 778 293 143

ATOM 1731 CG LEU B 34 -31.923 -26.449 23.182 1.00 25.49

ANISOU 1731 CG LEU B 34 3456 2654 3575 722 338 182

ATOM 1732 CD1 LEU B 34 -30.904 -25.308 23.075 1.00 23.06

ANISOU 1732 CD1 LEU B 34 3200 2244 3317 653 424 191

ATOM 1733 CD2 LEU B 34 -31.302 -27.697 23.824 1.00 19.06

ANISOU 1733 CD2 LEU B 34 2530 1932 2781 667 312 165

ATOM 1734 N VAL B 35 -33.627 -24.560 20.857 1.00 31.49

ANISOU 1734 N VAL B 35 4488 3239 4236 945 330 315

ATOM 1735 CA VAL B 35 -33.768 -24.882 19.444 1.00 29.88

ANISOU 1735 CA VAL B 35 4380 3052 3921 1011 307 386

ATOM 1736 C VAL B 35 -32.423 -25.385 18.924 1.00 29.36

ANISOU 1736 C VAL B 35 4337 2998 3822 930 410 402

ATOM 1737 O VAL B 35 -31.403 -24.716 19.076 1.00 29.32

ANISOU 1737 O VAL B 35 4345 2918 3876 852 524 427

ATOM 1738 CB VAL B 35 -34.201 -23.643 18.618 1.00 28.02

ANISOU 1738 CB VAL B 35 4293 2709 3646 1105 316 486

ATOM 1739 CGI VAL B 35 -34.316 -23.996 17.130 1.00 28.01

ANISOU 1739 CGI VAL B 35 4416 2749 3477 1177 282 564

ATOM 1740 CG2 VAL B 35 -35.513 -23.060 19.143 1.00 24.23

ANISOU 1740 CG2 VAL B 35 3772 2205 3231 1208 226 470

ATOM 1741 N LEU B 36 -32.417 -26.575 18.333 1.00 28.66

ANISOU 1741 N LEU B 36 4237 2995 3657 947 375 377

ATOM 1742 CA LEU B 36 -31.201 -27.142 17.753 1.00 26.20

ANISOU 1742 CA LEU B 36 3941 2698 3315 899 489 382

ATOM 1743 C LEU B 36 -31.349 -27.195 16.239 1.00 29.38 ANISOU 1743 C LEU B 36 4511 3112 3539 977 509 432

ATOM 1744 O LEU B 36 -32.338 -27.719 15.727 1, 00 30. 56

ANISOU 1744 O LEU B 36 4704 3318 3591 1051 377 402

ATOM 1745 CB LEU B 36 -30.944 -28.546 18.311 1, 00 23. 66

ANISOU 1745 CB LEU B 36 3490 2450 3050 864 453 300

ATOM 1746 CG LEU B 36 -30.644 -28.652 19.814 1, 00 25. 13

ANISOU 1746 CG LEU B 36 3522 2649 3375 789 433 264

ATOM 1747 CD1 LEU B 36 -30.459 -30.102 20.230 1, 00 25.

ANISOU 1747 CD1 LEU B 36 3489 2777 3492 777 393 217

ATOM 1748 CD2 LEU B 36 -29.406 -27.843 20.193 1, 00 28. 01

ANISOU 1748 CD2 LEU B 36 3851 2967 3823 705 542 289

ATOM 1749 N LYS B 37 -30.385 -26.632 15.520 1, 00 33. 26

ANISOU 1749 N LYS B 37 5098 3558 3983 954 671 509

ATOM 1750 CA LYS B 37 -30.465 -26.584 14.069 1, 00 35. 73

ANISOU 1750 CA LYS B 37 5602 3890 4084 1031 712 573

ATOM 1751 C LYS B 37 -30.124 -27.936 13.462 1, 00 34. 01

ANISOU 1751 C LYS B 37 5391 3760 3771 1049 733 479

ATOM 1752 O LYS B 37 -29.222 -28.630 13.934 1, 00 37. 34

ANISOU 1752 O LYS B 37 5686 4192 4310 988 823 418

ATOM 1753 CB LYS B 37 -29.511 -25.533 13.511 1, 00 45. 08

ANISOU 1753 CB LYS B 37 6890 4989 5249 992 917 704

ATOM 1754 CG LYS B 37 -29.792 -24.115 13.961 1, 00 53. 11

ANISOU 1754 CG LYS B 37 7938 5877 6366 976 915 800

ATOM 1755 CD LYS B 37 -28.613 -23.202 13.631 1, 00 58. 34

ANISOU 1755 CD LYS B 37 8652 6430 7082 886 1146 916

ATOM 1756 CE LYS B 37 -28.912 -21.756 13. 975 1, 00 61. 19

ANISOU 1756 CE LYS B 37 9077 6623 7550 872 1149 1010

ATOM 1757 NZ LYS B 37 -29.940 -21.192 13. 057 1, 00 65. 06

ANISOU 1757 NZ LYS B 37 9776 7081 7864 1019 1068 1137

ATOM 1758 N CYS B 38 -30.857 -28.313 12.423 1, 00 32.

ANISOU 1758 N CYS B 38 5395 3673 3416 1138 639 461

ATOM 1759 CA CYS B 38 -30.484 -29.460 11.606 1, 00 36. 77

ANISOU 1759 CA CYS B 38 5958 4233 3780 1165 684 361

ATOM 1760 C CYS B 38 -29.811 -28.938 10.339 1, 00 38. 52

ANISOU 1760 C CYS B 38 6388 4466 3783 1204 869 455

ATOM 1761 O CYS B 38 -30.484 -28.491 9.412 1, 00 40. 64

ANISOU 1761 O CYS B 38 6850 4767 3823 1285 791 520

ATOM 1762 CB CYS B 38 -31.711 -30.305 11.249 1, 00 34. 00

ANISOU 1762 CB CYS B 38 5646 3947 3326 1223 450 249

ATOM 1763 SG CYS B 38 -31.344 -31.803 10.282 1, 00 56. 61

ANISOU 1763 SG CYS B 38 8611 6864 6036 1252 486 77

ATOM 1764 N LYS B 39 -28.483 -28.968 10.316 1, 00 39. 45

ANISOU 1764 N LYS B 39 6458 4560 3970 1150 1115 476

ATOM 1765 CA LYS B 39 -27.732 -28.443 9.176 1, 00 44. 29

ANISOU 1765 CA LYS B 39 7251 5182 4393 1173 1346 583

ATOM 1766 C LYS B 39 -27.987 -29.264 7.910 1, 00 44.

ANISOU 1766 C LYS B 39 7529 5347 4153 1272 1340 494

ATOM 1767 O LYS B 39 -28.188 -30.480 7. 976 1, 00 43. 44

ANISOU 1767 O LYS B 39 7306 5211 3988 1294 1248 316

ATOM 1768 CB LYS B 39 -26.234 -28.414 9. 490 1, 00 48. 90

ANISOU 1768 CB LYS B 39 7686 5732 5163 1086 1619 606

ATOM 1769 CG LYS B 39 -25.876 -27.626 10.747 1, 00 52. 32

ANISOU 1769 CG LYS B 39 7912 6074 5892 971 1614 667

ATOM 1770 CD LYS B 39 -24.388 -27.724 11.072 1, 00 55. 50

ANISOU 1770 CD LYS B 39 8126 6462 6500 880 1847 670

ATOM 1771 CE LYS B 39 -23.954 -29.178 11.243 1, 00 59. 61

ANISOU 1771 CE LYS B 39 8514 7049 7085 920 1853 515

ATOM 1772 NZ LYS B 39 -22.558 -29.321 11.762 1, 00 62. 37

ANISOU 1772 NZ LYS B 39 8621 7391 7686 845 2031 515 ATOM 1773 N GLY B 40 -27.993 -28.591 6.762 1.00 44.62

ANISOU 1773 N GLY B 40 7752 5353 3847 1331 1433 619

ATOM 1774 CA GLY B 40 -28.115 -29.267 5.483 1.00 49.70

ANISOU 1774 CA GLY B 40 8633 6104 4148 1425 1453 536

ATOM 1775 C GLY B 40 -29.502 -29.782 5.137 1.00 54.30

ANISOU 1775 C GLY B 40 9321 6759 4552 1502 1116 423

ATOM 1776 O GLY B 40 -29.647 -30.643 4.274 1.00 57.33

ANISOU 1776 O GLY B 40 9861 7228 4693 1562 1082 276

ATOM 1777 N ALA B 41 -30.524 -29.268 5.815 1.00 54.87

ANISOU 1777 N ALA B 41 9298 6796 4753 1498 868 477

ATOM 1778 CA ALA B 41 -31.903 -29.631 5.500 1.00 53.61

ANISOU 1778 CA ALA B 41 9200 6711 4458 1565 534 391

ATOM 1779 C ALA B 41 -32.573 -28.511 4.706 1.00 54.67

ANISOU 1779 C ALA B 41 9545 6880 4347 1663 428 585

ATOM 17 80 O ALA B 41 -32.266 -27.335 4.908 1.00 54.22

ANISOU 17 80 O ALA B 41 9502 6737 4361 1659 553 793

ATOM 17 81 CB ALA B 41 -32.676 -29.912 6.773 1.00 50.45

ANISOU 17 81 CB ALA B 41 8531 6262 4374 1510 329 316

ATOM 17 82 N PRO B 42 -33.483 -28.872 3.789 1.00 54.02

ANISOU 17 82 N PRO B 42 9631 6915 3979 1752 188 518

ATOM 17 83 CA PRO B 42 -34.238 -27.851 3.056 1.00 57.39

ANISOU 17 83 CA PRO B 42 10248 7385 4172 1868 33 714

ATOM 17 84 C PRO B 42 -35. 009 -26.941 4.014 1.00 55.22

ANISOU 17 84 C PRO B 42 9783 7016 4184 1879 -114 842

ATOM 17 85 O PRO B 42 -35.309 -27.353 5.132 1.00 52.29

ANISOU 17 85 O PRO B 42 9144 6596 4129 1806 -188 724

ATOM 17 86 CB PRO B 42 -35.204 -28.679 2.204 1.00 60.08

ANISOU 17 86 CB PRO B 42 10709 7880 4238 1937 -277 547

ATOM 17 87 CG PRO B 42 -34.518 -29.985 2.012 1.00 47.96

ANISOU 17 87 CG PRO B 42 9189 6375 2658 1871 -148 297

ATOM 17 88 CD PRO B 42 -33.794 -30.233 3.317 1.00 55.13

ANISOU 17 88 CD PRO B 42 9812 7148 3985 1753 48 258

ATOM 17 89 N LYS B 43 -35. 313 -25.722 3.574 1.00 58.30

ANISOU 17 89 N LYS B 43 10320 7371 4460 1978 -141 1083

ATOM 1790 CA LYS B 43 -35.981 -24.724 4.411 1.00 57.09

ANISOU 1790 CA LYS B 43 10008 7101 4581 2007 -242 1211

ATOM 1791 C LYS B 43 -37.349 -25.159 4.935 1.00 56.86

ANISOU 1791 C LYS B 43 9776 7134 4694 2053 -586 1087

ATOM 1792 O LYS B 43 -37.739 -24.801 6.046 1.00 54.84

ANISOU 1792 O LYS B 43 9293 6786 4758 2029 -614 1086

ATOM 1793 CB LYS B 43 -36.136 -23.413 3.640 1.00 57.98

ANISOU 1793 CB LYS B 43 10239 7164 4627 2055 -217 1430

ATOM 1794 CG LYS B 43 -34.834 -22.686 3.377 1.00 57.23

ANISOU 1794 CG LYS B 43 10267 6958 4518 1981 140 1583

ATOM 1795 CD LYS B 43 -35.079 -21.439 2.543 1.00 58.86

ANISOU 1795 CD LYS B 43 10606 7117 4641 2034 134 1804

ATOM 1796 CE LYS B 43 -33.816 -20.613 2.403 1.00 59.74

ANISOU 1796 CE LYS B 43 10803 7092 4804 1941 487 1963

ATOM 1797 NZ LYS B 43 -33.990 -19.524 1.411 1.00 66.27

ANISOU 1797 NZ LYS B 43 11798 7888 5496 1993 488 2185

ATOM 1798 N LYS B 44 -38.078 -25.920 4.128 1.00 60.60

ANISOU 1798 N LYS B 44 10306 7765 4953 2097 -834 964

ATOM 1799 CA LYS B 44 -39.423 -26.348 4.486 1.00 63.61

ANISOU 1799 CA LYS B 44 10480 8218 5470 2129 -1171 848

ATOM 18 00 C LYS B 44 -39.676 -27.754 3.948 1.00 67.53

ANISOU 18 00 C LYS B 44 11005 8856 5798 2085 -1344 600

ATOM 18 01 O LYS B 44 -38.952 -28.210 3.059 1.00 69.85

ANISOU 18 01 O LYS B 44 11526 9207 5807 2069 -1229 543

ATOM 18 02 CB LYS B 44 -40.458 -25.348 3.942 1.00 65.44 ANISOU 1?302 CB LYS B 44 10685 8474 5706 2218 -1359 994

ATOM 1? 303 CG LYS B 44 -40.255 -24.974 2.490 1.00 71.56

ANISOU 1? 303 CG LYS B 44 11722 9325 6143 2260 -1349 1100

ATOM 1? 304 CD LYS B 44 -41.048 -23.731 2.096 1.00 76.20

ANISOU 1? 304 CD LYS B 44 12299 9890 6765 2358 -1470 1311

ATOM 1? 305 CE LYS B 44 -42.529 -24.029 1.922 1.00 79.49

ANISOU 1? 305 CE LYS B 44 12537 10435 7231 2413 -1846 1235

ATOM 1? 306 NZ LYS B 44 -43.231 -22.921 1.211 1.00 85.20

ANISOU 1? 306 NZ LYS B 44 13303 11170 7900 2522 -1976 1451

ATOM 1? 307 N PRO B 45 -40.683 -28.457 4.503 1.00 67.45

ANISOU 1? 307 N PRO B 45 10739 8888 5999 2041 -1589 437

ATOM 1? 308 CA PRO B 45 -41.078 -29.782 4.003 1.00 66.57

ANISOU 1? 308 CA PRO B 45 10628 8886 5780 1976 -1787 183

ATOM 1? 309 C PRO B 45 -41.346 -29.786 2.495 1.00 69.27

ANISOU 1? 309 C PRO B 45 11213 9363 5743 2039 -1941 174

ATOM 1? 310 O PRO B 45 -41.711 -28.748 1.941 1.00 70.17

ANISOU 1? 310 O PRO B 45 11380 9500 5782 2119 -1981 370

ATOM 1? 311 CB PRO B 45 -42.367 -30.069 4.775 1.00 65.86

ANISOU 1? 311 CB PRO B 45 10208 8815 6002 1946 -2052 102

ATOM 1? 312 CG PRO B 45 -42.167 -29.358 6.077 1.00 64.81

ANISOU 1? 312 CG PRO B 45 9873 8547 6205 1927 -1848 230

ATOM 1? 313 CD PRO B 45 -41.414 -28.096 5.736 1.00 64.16

ANISOU 1? 313 CD PRO B 45 10010 8400 5968 2029 -1648 468

ATOM 1? 314 N PRO B 46 -41.155 -30.942 1.834 1.00 69.37

ANISOU 1? 314 N PRO B 46 11344 9446 5567 1973 -1993 -60

ATOM 1? 315 CA PRO B 46 -40.725 -32.218 2.426 1.00 66.04

ANISOU 1? 315 CA PRO B 46 10848 8968 5275 1858 -1926 -308

ATOM 1? 316 C PRO B 46 -39.221 -32.270 2.704 1.00 63.19

ANISOU 1? 316 C PRO B 46 10577 8497 4935 1813 -1499 -277

ATOM 1? 317 O PRO B 46 -38.425 -31.767 1.913 1.00 68.27

ANISOU 1? 317 O PRO B 46 11488 9171 5281 1885 -1310 -167

ATOM 1? 318 CB PRO B 46 -41.089 -33.235 1.341 1.00 67.00

ANISOU 1? 318 CB PRO B 46 11101 9193 5162 1816 -2123 -552

ATOM 1? 319 CG PRO B 46 -40.954 -32.473 0.076 1.00 69.30

ANISOU 1? 319 CG PRO B 46 11628 9580 5124 1897 -2084 -400

ATOM 1? 320 CD PRO B 46 -41.408 -31.069 0.387 1.00 70.36

ANISOU 1? 320 CD PRO B 46 11668 9700 5366 1991 -2114 -103

ATOM 1? 321 N GLN B 47 -38.843 -32.874 3.822 1.00 58.37

ANISOU 1? 321 N GLN B 47 9736 7766 4677 1695 -1351 -363

ATOM 1? 322 CA GLN B 47 -37.435 -32.996 4.181 1.00 57.90

ANISOU 1? 322 CA GLN B 47 9707 7607 4687 1650 -976 -343

ATOM 1? 323 C GLN B 47 -37.087 -34.432 4.566 1.00 55.76

ANISOU 1? 323 C GLN B 47 9338 7263 4584 1544 -920 -589

ATOM 1? 324 O GLN B 47 -37.767 -35.045 5.392 1.00 52.21

ANISOU 1? 324 O GLN B 47 8654 6763 4419 1459 -1067 -682

ATOM 1? 325 CB GLN B 47 -37.095 -32.070 5.355 1.00 55.23

ANISOU 1? 325 CB GLN B 47 9177 7165 4642 1628 -806 -144

ATOM 1? 326 CG GLN B 47 -37.294 -30.588 5.094 1.00 54.17

ANISOU 1? 326 CG GLN B 47 9137 7045 4398 1731 -808 112

ATOM 1? 327 CD GLN B 47 -37.829 -29.871 6.320 1.00 49.84

ANISOU 1? 327 CD GLN B 47 8336 6417 4183 1716 -850 223

ATOM 1? 328 OE1 GLN B 47 -38.621 -30.432 7.075 1.00 48.67

ANISOU 1? 328 OE1 GLN B 47 7958 6267 4265 1662 -1010 114

ATOM 1? 329 NE2 GLN B 47 -37.392 -28.632 6.530 1.00 46.60

ANISOU 1? 329 NE2 GLN B 47 7972 5931 3805 1758 -689 434

ATOM 1? 330 N ARG B 48 -36.030 -34.967 3.963 1.00 55.76

ANISOU 1? 330 N ARG B 48 9517 7250 4418 1554 -694 -685

ATOM 1? 331 CA ARG B 48 -35.488 -36.253 4.389 1.00 52.81

ANISOU 1? 331 CA ARG B 48 9055 6772 4240 1475 -584 -889 ATOM 1?332 C ARG B 48 -34.525 -36.042 5.556 1.00 46.33

ANISOU 1? 332 C ARG B 48 8035 5840 3730 1430 -314 -763

ATOM 1? 333 O ARG B 48 -33. 306 -36.020 5.373 1.00 43.62

ANISOU 1? 333 O ARG B 48 7762 5468 3342 1456 -23 -736

ATOM 1? 334 CB ARG B 48 -34. 782 -36.958 3.230 1.00 57.02

ANISOU 1? 334 CB ARG B 48 9861 7335 4470 1525 -451 -1068

ATOM 1? 335 CG ARG B 48 -35. 737 -37.510 2.178 1.00 66.11

ANISOU 1? 335 CG ARG B 48 11199 8583 5336 1542 -753 -1273

ATOM 1? 336 CD ARG B 48 -35.043 -37.769 0.845 1.00 73.59

ANISOU 1? 336 CD ARG B 48 12494 9609 5859 1628 -602 -1396

ATOM 1? 337 NE ARG B 48 -34.631 -36.530 0.190 1.00 78.24

ANISOU 1? 337 NE ARG B 48 13236 10307 6185 1710 -451 -1137

ATOM 1? 338 CZ ARG B 48 -34.089 -36.469 -1.023 1.00 86.57

ANISOU 1? 338 CZ ARG B 48 14493 11446 6956 1739 -296 -1133

ATOM 1? 339 NH1 ARG B 48 -33.893 -37.581 -1.722 1.00 90.80

ANISOU 1? 339 NH1 ARG B 48 15120 11982 7398 1708 -273 -1393

ATOM 1? 340 NH2 ARG B 48 -33.745 -35.297 -1.541 1.00 88.51

ANISOU 1? 340 NH2 ARG B 48 14848 11765 7016 1796 -157 -870

ATOM 1? 341 N LEU B 49 -35.073 -35.861 6.752 1.00 37.63

ANISOU 1? 341 N LEU B 49 6676 4685 2936 1365 -412 -687

ATOM 1? 342 CA LEU B 49 -34.227 -35.724 7.923 1.00 40.94

ANISOU 1? 342 CA LEU B 49 6907 5012 3638 1316 -200 -587

ATOM 1? 343 C LEU B 49 -34.701 -36.579 9.092 1.00 38.78

ANISOU 1? 343 C LEU B 49 6392 4654 3690 1223 -301 -659

ATOM 1? 344 O LEU B 49 -35.870 -36.957 9.177 1.00 37.54

ANISOU 1? 344 O LEU B 49 6163 4511 3588 1185 -542 -734

ATOM 1? 345 CB LEU B 49 -34.086 -34.257 8.348 1.00 41.03

ANISOU 1? 345 CB LEU B 49 6877 5038 3673 1339 -123 -351

ATOM 1? 346 CG LEU B 49 -35.263 -33.557 9.033 1.00 41.43

ANISOU 1? 346 CG LEU B 49 6784 5105 3852 1331 -330 -257

ATOM 1? 347 CD1 LEU B 49 -35.229 -33.724 10.543 1.00 35.82

ANISOU 1? 347 CD1 LEU B 49 5816 4319 3474 1248 -293 -234

ATOM 1? 348 CD2 LEU B 49 -35.270 -32.086 8.663 1.00 42.48

ANISOU 1? 348 CD2 LEU B 49 7028 5267 3846 1407 -292 -58

ATOM 1? 349 N GLU B 50 -33. 783 -36.849 10.007 1.00 36.88

ANISOU 1? 349 N GLU B 50 6017 4329 3666 1186 -115 -620

ATOM 1? 350 CA GLU B 50 -34. 086 -37.675 11.152 1.00 36.77

ANISOU 1? 350 CA GLU B 50 5797 4231 3944 1105 -175 -657

ATOM 1? 351 C GLU B 50 -33. 296 -37.197 12.364 1.00 36.55

ANISOU 1? 351 C GLU B 50 5606 4169 4112 1079 -18 -507

ATOM 1? 352 O GLU B 50 -32. 087 -36.969 12.267 1.00 38.57

ANISOU 1? 352 O GLU B 50 5890 4413 4350 1110 186 -462

ATOM 1? 353 CB GLU B 50 -33. 729 -39.116 10.827 1.00 38.57

ANISOU 1? 353 CB GLU B 50 6071 4363 4221 1093 -145 -843

ATOM 1? 354 CG GLU B 50 -34.241 -40.109 11.829 1.00 44.68

ANISOU 1? 354 CG GLU B 50 6668 5032 5278 1004 -238 -885

ATOM 1? 355 CD GLU B 50 -33.805 -41.515 11.500 1.00 48.27

ANISOU 1? 355 CD GLU B 50 7183 5351 5805 1002 -190 -1064

ATOM 1? 356 OE1 GLU B 50 -34.621 -42.268 10.927 1.00 50.45

ANISOU 1? 356 OE1 GLU B 50 7527 5587 6054 959 -356 -1236

ATOM 1? 357 OE2 GLU B 50 -32.642 -41.858 11.812 1.00 47.49

ANISOU 1? 357 OE2 GLU B 50 7058 5180 5804 1045 9 -1038

ATOM 1? 358 N TRP B 51 -33. 973 -37.033 13.499 1.00 26.54

ANISOU 1? 358 N TRP B 51 4163 2894 3026 1021 -112 -436

ATOM 1? 359 CA TRP B 51 -33.283 -36.707 14.740 1.00 24.77

ANISOU 1? 359 CA TRP B 51 3791 2646 2976 989 5 -320

ATOM 1? 360 C TRP B 51 -33. 101 -37.944 15.614 1.00 30.91

ANISOU 1? 360 C TRP B 51 4442 3337 3964 938 10 -358

ATOM 1? 361 O TRP B 51 -34. 008 -38.766 15.754 1.00 30.78 ANISOU 1?361 O TRP B 51 4383 3281 4030 891 -119 -427

ATOM 1? 362 CB TRP B 51 -34.021 -35.613 15.528 1.00 24.95

ANISOU 1? 362 CB TRP B 51 3721 2718 3041 970 -64 -207

ATOM 1? 363 CG TRP B 51 -33.777 -34.221 15.025 1.00 28.05

ANISOU 1? 363 CG TRP B 51 4214 3152 3291 1022 -5 -115

ATOM 1? 364 CD1 TRP B 51 -34. 508 -33.549 14.092 1.00 30.41

ANISOU 1? 364 CD1 TRP B 51 4635 3498 3419 1082 -101 -99

ATOM 1? 365 CD2 TRP B 51 -32.730 -33.324 15.436 1.00 29.97

ANISOU 1? 365 CD2 TRP B 51 4444 3380 3563 1013 158 -16

ATOM 1? 366 NE1 TRP B 51 -33.985 -32.288 13.890 1.00 30.03

ANISOU 1? 366 NE1 TRP B 51 4667 3449 3294 1117 9 19

ATOM 1? 367 CE2 TRP B 51 -32. 893 -32.124 14.702 1.00 29.97

ANISOU 1? 367 CE2 TRP B 51 4573 3398 3415 1064 171 63

ATOM 1? 368 CE3 TRP B 51 -31.669 -33.421 16.351 1.00 24.27

ANISOU 1? 368 CE3 TRP B 51 3609 2630 2985 964 279 17

ATOM 1? 369 CZ2 TRP B 51 -32.034 -31.032 14.844 1.00 29.21

ANISOU 1? 369 CZ2 TRP B 51 4498 3270 3329 1051 320 166

ATOM 1? 370 CZ3 TRP B 51 -30.819 -32.335 16.502 1.00 26.54

ANISOU 1? 370 CZ3 TRP B 51 3900 2907 3278 948 405 103

ATOM 1? 371 CH2 TRP B 51 -31. 007 -31.151 15.748 1.00 30.42

ANISOU 1? 371 CH2 TRP B 51 4524 3396 3639 982 434 174

ATOM 1? 372 N LYS B 52 -31. 917 -38.064 16.202 1.00 30.19

ANISOU 1? 372 N LYS B 52 4286 3214 3973 945 155 -302

ATOM 1? 373 CA LYS B 52 -31.611 -39.146 17.129 1.00 27.95

ANISOU 1? 373 CA LYS B 52 3884 2846 3890 916 165 -295

ATOM 1? 374 C LYS B 52 -31.128 -38.543 18.434 1.00 26.53

ANISOU 1? 374 C LYS B 52 3566 2706 3807 887 205 -155

ATOM 1? 375 O LYS B 52 -30.221 -37.708 18.450 1.00 27.57

ANISOU 1? 375 O LYS B 52 3688 2883 3903 906 305 -99

ATOM 1? 376 CB LYS B 52 -30.502 -40.046 16.572 1.00 28.93

ANISOU 1? 376 CB LYS B 52 4053 2889 4051 978 291 -371

ATOM 1? 377 CG LYS B 52 -30.956 -41.093 15.580 1.00 39.16

ANISOU 1? 377 CG LYS B 52 5474 4100 5305 995 242 -543

ATOM 1? 378 CD LYS B 52 -29.788 -42.003 15.171 1.00 45.75

ANISOU 1? 378 CD LYS B 52 6342 4835 6207 1075 396 -622

ATOM 1? 379 CE LYS B 52 -30.250 -43.095 14.210 1.00 52.27

ANISOU 1? 379 CE LYS B 52 7313 5553 6995 1089 347 -827

ATOM 1? 380 NZ LYS B 52 -29.180 -43.583 13.274 1.00 55.28

ANISOU 1? 380 NZ LYS B 52 7803 5883 7317 1198 531 -951

ATOM 1? 381 N LEU B 53 -31.706 -38.966 19.542 1.00 25.42

ANISOU 1? 381 N LEU B 53 3320 2550 3787 834 130 -100

ATOM 1? 382 CA LEU B 53 -31.220 -38.456 20.810 1.00 25.58

ANISOU 1? 382 CA LEU B 53 3232 2621 3867 810 157 18

ATOM 1? 383 C LEU B 53 -30.996 -39.554 21.825 1.00 24.92

ANISOU 1? 383 C LEU B 53 3057 2477 3933 794 143 82

ATOM 1? 384 O LEU B 53 -31.659 -40.595 21.803 1.00 30.41

ANISOU 1? 384 O LEU B 53 3758 3087 4711 771 94 54

ATOM 1? 385 CB LEU B 53 -32. 106 -37.329 21.360 1.00 29.74

ANISOU 1? 385 CB LEU B 53 3737 3233 4329 772 104 63

ATOM 1? 386 CG LEU B 53 -33.507 -37.598 21.899 1.00 32.15

ANISOU 1? 386 CG LEU B 53 3991 3549 4674 726 12 72

ATOM 1? 387 CD1 LEU B 53 -34. 034 -36.343 22.557 1.00 29.74

ANISOU 1? 387 CD1 LEU B 53 3655 3330 4315 716 6 118

ATOM 1? 388 CD2 LEU B 53 -34. 438 -38.021 20.787 1.00 36.31

ANISOU 1? 388 CD2 LEU B 53 4578 4044 5176 729 -69 -27

ATOM 1? 389 N ASN B 54 -30. 008 -39.331 22.679 1.00 25.09

ANISOU 1? 389 N ASN B 54 2998 2537 3997 805 180 170

ATOM 1? 390 CA ASN B 54 -29. 721 -40.227 23.793 1.00 27.99

ANISOU 1? 390 CA ASN B 54 3283 2869 4483 802 153 270 ATOM If 391 C ASN B 54 -29.553 -39.355 25.029 1.00 25.61

ANISOU li 391 C ASN B 54 2915 2688 4127 765 123 364

ATOM li 392 O ASN B 54 -28.541 -38.668 25.185 1.00 22.91

ANISOU 11 392 O ASN B 54 2527 2407 3769 777 147 376

ATOM 11 393 CB ASN B 54 -28.452 -41.055 23.533 1.00 21.92

ANISOU li 393 CB ASN B 54 2477 2021 3830 883 211 274

ATOM 11 394 CG ASN B 54 -28.213 -42.122 24.610 1.00 22.72

ANISOU 11 394 CG ASN B 54 2508 2059 4065 902 167 398

ATOM 11 395 OD1 ASN B 54 -28.890 -42.145 25.633 1.00 30.90

ANISOU 11 395 OD1 ASN B 54 3527 3134 5080 845 105 494

ATOM li 396 ND2 ASN B 54 -27.248 -42.999 24.379 1.00 23.94

ANISOU 11 396 ND2 ASN B 54 2626 2115 4355 992 209 406

ATOM 11 397 N THR B 55 -30.567 -39.350 25.884 1.00 25.67

ANISOU 11 397 N THR B 55 2916 2732 4106 711 77 417

ATOM 11 398 CA THR B 55 -30.569 -38.491 27.067 1.00 23.37

ANISOU li 398 CA THR B 55 2590 2561 3727 676 55 479

ATOM li 399 C THR B 55 -31.046 -39.262 28.285 1.00 22.83

ANISOU li 399 C THR B 55 2495 2505 3674 650 27 599

ATOM 1900 O THR B 55 -31.299 -40.464 28.204 1.00 22.99

ANISOU 1900 O THR B 55 2514 2421 3801 654 26 647

ATOM 1901 CB THR B 55 -31.497 -37.261 26.876 1.00 21.01

ANISOU 1901 CB THR B 55 2332 2324 3326 646 65 409

ATOM 1902 OG1 THR B 55 -32.863 -37.691 26.880 1.00 23.31

ANISOU 1902 OG1 THR B 55 2624 2595 3636 619 53 409

ATOM 1903 CG2 THR B 55 -31.208 -36.558 25.562 1.00 21.29

ANISOU 1903 CG2 THR B 55 2422 2331 3334 674 97 317

ATOM 1904 N GLY B 56 -31.198 -38.560 29.410 1.00 24.56

ANISOU 1904 N GLY B 56 2706 2844 3781 619 13 644

ATOM 1905 CA GLY B 56 -31.761 -39.151 30.611 1.00 21.17

ANISOU 1905 CA GLY B 56 2273 2452 3317 591 11 769

ATOM 1906 C GLY B 56 -33.179 -39.676 30.419 1.00 25.86

ANISOU 1906 C GLY B 56 2867 2988 3969 546 58 775

ATOM 1907 O GLY B 56 -33.664 -40.457 31.224 1.00 28.38

ANISOU 1907 O GLY B 56 3179 3298 4307 515 82 898

ATOM 1908 N ARG B 57 -33.851 -39.254 29.352 1.00 26.26

ANISOU 1908 N ARG B 57 2921 3005 4052 539 68 652

ATOM 1909 CA ARG B 57 -35.204 -39.734 29.070 1.00 30.01

ANISOU 1909 CA ARG B 57 3364 3431 4609 489 87 641

ATOM 1910 C ARG B 57 -35.233 -41.033 28.273 1.00 29.75

ANISOU 1910 C ARG B 57 3332 3235 4735 474 61 630

ATOM 1911 O ARG B 57 -36.258 -41.705 28.231 1.00 33.92

ANISOU 1911 O ARG B 57 3819 3702 5368 408 68 642

ATOM 1912 CB ARG B 57 -36.007 -38.688 28.280 1.00 28.59

ANISOU 1912 CB ARG B 57 3178 3295 4392 499 78 515

ATOM 1913 CG ARG B 57 -36.143 -37.333 28.949 1.00 25.67

ANISOU 1913 CG ARG B 57 2814 3049 3891 520 114 497

ATOM 1914 CD ARG B 57 -37.114 -36.465 28.184 1.00 23.22

ANISOU 1914 CD ARG B 57 2485 2755 3583 545 103 401

ATOM 1915 NE ARG B 57 -37.126 -35.093 28.685 1.00 28.56

ANISOU 1915 NE ARG B 57 3188 3511 4154 582 142 365

ATOM 1916 CZ ARG B 57 -37.863 -34.680 29.712 1.00 31.65

ANISOU 1916 CZ ARG B 57 3540 3983 4502 578 213 383

ATOM 1917 NH1 ARG B 57 -38.649 -35.533 30.355 1.00 29.14

ANISOU 1917 NH1 ARG B 57 3147 3690 4236 531 263 459

ATOM 1918 NH2 ARG B 57 -37.805 -33.417 30.102 1.00 36.99

ANISOU 1918 NH2 ARG B 57 4260 4707 5089 619 249 323

ATOM 1919 N THR B 58 -34.129 -41.374 27.618 1.00 27.33

ANISOU 1919 N THR B 58 3067 2854 4463 532 39 593

ATOM 1920 CA THR B 58 -34.149 -42.476 26.662 1.00 28.28 ANISOU 1920 CA THR B 58 3214 2808 4723 531 20 529

ATOM 1921 C THR B 58 -33.458 -43. ,755 27. ,122 1. , 00 23. , 57

ANISOU 1921 C THR B 58 2622 2077 4258 554 33 637

ATOM 1922 O THR B 58 -32.576 -43. ,738 27. ,968 1. , 00 23. , 69

ANISOU 1922 O THR B 58 2621 2139 4241 602 38 756

ATOM 1923 CB THR B 58 -33.487 -42. ,080 25. ,327 1. , 00 26. , 94

ANISOU 1923 CB THR B 58 3106 2621 4510 596 11 382

ATOM 1924 OG1 THR B 58 -32.063 -42. ,059 25. ,489 1. , 00 21. ,80

ANISOU 1924 OG1 THR B 58 2455 1974 3855 672 44 422

ATOM 1925 CG2 THR B 58 -33.985 -40. ,720 24. ,846 1. , 00 22. , 60

ANISOU 1925 CG2 THR B 58 2572 2194 3822 597 -3 302

ATOM 1926 N GLU B 59 -33.871 -44. ,868 26. ,537 1. , 00 24. , 73

ANISOU 1926 N GLU B 59 2789 2047 4560 522 25 591

ATOM 1927 CA GLU B 59 -33.089 -46. ,085 26. ,591 1. , 00 26. , 06

ANISOU 1927 CA GLU B 59 2984 2037 4882 574 40 650

ATOM 1928 C GLU B 59 -32.211 -46. ,081 25. ,342 1. , 00 30. , 68

ANISOU 1928 C GLU B 59 3623 2565 5469 666 48 485

ATOM 1929 O GLU B 59 -32.699 -46. ,377 24. ,246 1. , 00 31. , 13

ANISOU 1929 O GLU B 59 3737 2534 5558 641 32 318

ATOM 1930 CB GLU B 59 -34.012 -47. ,301 26. ,584 1. , 00 30. , 77

ANISOU 1930 CB GLU B 59 3587 2437 5666 480 39 669

ATOM 1931 CG GLU B 59 -33.273 -48. ,628 26. ,620 1. , 00 37. ,81

ANISOU 1931 CG GLU B 59 4521 3096 6750 541 60 731

ATOM 1932 CD GLU B 59 -32.670 -48. ,926 27. ,981 1. , 00 41. ,23

ANISOU 1932 CD GLU B 59 4929 3547 7190 590 80 990

ATOM 1933 OE1 GLU B 59 -33.227 -48. ,452 28. ,993 1. , 00 39. , 95

ANISOU 1933 OE1 GLU B 59 4731 3530 6919 526 90 1128

ATOM 1934 OE2 GLU B 59 -31.640 -49. ,630 28. ,039 1. , 00 45. ,79

ANISOU 1934 OE2 GLU B 59 5524 4000 7876 704 84 1054

ATOM 1935 N ALA B 60 -30.930 -45. ,734 25. ,504 1. , 00 27. , 54

ANISOU 1935 N ALA B 60 3203 2230 5032 770 74 527

ATOM 1936 CA ALA B 60 -30.017 -45. ,540 24. ,366 1. , 00 25. , 61

ANISOU 1936 CA ALA B 60 2991 1970 4770 861 120 383

ATOM 1937 C ALA B 60 -30.620 -44. ,550 23. ,361 1. , 00 24. , 83

ANISOU 1937 C ALA B 60 2950 1972 4512 820 115 227

ATOM 1938 O ALA B 60 -31.191 -43. ,545 23. ,767 1. , 00 23. , 38

ANISOU 1938 O ALA B 60 2741 1933 4209 763 84 262

ATOM 1939 CB ALA B 60 -29.680 -46. ,867 23. ,696 1. , 00 27. ,40

ANISOU 1939 CB ALA B 60 3271 1968 5172 923 156 306

ATOM 1940 N TRP B 61 -30.535 -44. ,846 22. ,063 1. , 00 25. , 43

ANISOU 1940 N TRP B 61 3115 1969 4578 856 144 58

ATOM 1941 CA TRP B 61 -31.066 -43. ,920 21. ,045 1. , 00 24. , 66

ANISOU 1941 CA TRP B 61 3093 1972 4304 834 127 -71

ATOM 1942 C TRP B 61 -32.562 -43. ,983 20. ,794 1. , 00 26. ,41

ANISOU 1942 C TRP B 61 3340 2189 4505 735 21 -137

ATOM 1943 O TRP B 61 -33.158 -45. ,055 20. ,702 1. , 00 26. , 07

ANISOU 1943 O TRP B 61 3311 2001 4592 684 -25 -189

ATOM 1944 CB TRP B 61 -30.346 -44. ,076 19. ,711 1. , 00 27. , 35

ANISOU 1944 CB TRP B 61 3539 2268 4585 919 206 -225

ATOM 1945 CG TRP B 61 -28.941 -43. ,710 19. ,810 1. , 00 38. ,79

ANISOU 1945 CG TRP B 61 4933 3765 6040 1009 323 -168

ATOM 1946 CD1 TRP B 61 -27.901 -44. ,556 19. ,989 1. , 00 48. , 51

ANISOU 1946 CD1 TRP B 61 6112 4891 7427 1098 399 -145

ATOM 1947 CD2 TRP B 61 -28.391 -42. ,390 19. ,779 1. , 00 39. , 33

ANISOU 1947 CD2 TRP B 61 4971 3989 5983 1016 376 -120

ATOM 1948 NE1 TRP B 61 -26.734 -43. ,854 20. ,061 1. , 00 49. , 66

ANISOU 1948 NE1 TRP B 61 6175 5138 7556 1158 492 -89

ATOM 1949 CE2 TRP B 61 -27.001 -42. ,521 19. ,929 1. , 00 46. , 97

ANISOU 1949 CE2 TRP B 61 5851 4951 7046 1097 483 -76 ATOM 1950 CE3 TRP B 61 -28.934 -41.118 19.629 1.00 35.99

ANISOU 1950 CE3 TRP B 61 4580 3695 5399 963 344 -108

ATOM 1951 CZ2 TRP B 61 -26.143 -41.424 19.934 1.00 44.52

ANISOU 1951 CZ2 TRP B 61 5475 4761 6679 1102 559 -27

ATOM 1952 CZ3 TRP B 61 -28.081 -40.030 19.638 1.00 37.97

ANISOU 1952 CZ3 TRP B 61 4793 4044 5590 976 426 -55

ATOM 1953 CH2 TRP B 61 -26.702 -40.190 19.786 1.00 37.99

ANISOU 1953 CH2 TRP B 61 4699 4040 5694 1033 532 -19

ATOM 1954 N LYS B 62 -33.150 -42.798 20.661 1.00 26.23

ANISOU 1954 N LYS B 62 3315 2317 4336 711 -19 -136

ATOM 1955 CA LYS B 62 -34.557 -42.649 20.332 1.00 24.04

ANISOU 1955 CA LYS B 62 3034 2069 4033 636 -130 -199

ATOM 1956 C LYS B 62 -34.668 -41.778 19.082 1.00 28.92

ANISOU 1956 C LYS B 62 3758 2775 4456 684 -164 -309

ATOM 1957 O LYS B 62 -34.083 -40.694 19.022 1.00 26.21

ANISOU 1957 O LYS B 62 3438 2531 3990 739 -102 -257

ATOM 1958 CB LYS B 62 -35.294 -42.013 21.511 1.00 23.08

ANISOU 1958 CB LYS B 62 2793 2047 3930 580 -148 -66

ATOM 1959 CG LYS B 62 -36. 631 -41.376 21.165 1.00 23.66

ANISOU 1959 CG LYS B 62 2830 2205 3953 538 -246 -114

ATOM 1960 CD LYS B 62 -37. 658 -42.421 20.762 1.00 26.11

ANISOU 1960 CD LYS B 62 3108 2418 4395 450 -346 -205

ATOM 1961 CE LYS B 62 -38.871 -41.749 20.128 1.00 30.17

ANISOU 1961 CE LYS B 62 3582 3033 4850 432 -475 -278

ATOM 1962 NZ LYS B 62 -39.895 -42.741 19.768 1.00 34.25

ANISOU 1962 NZ LYS B 62 4035 3462 5514 324 -593 -377

ATOM 1963 N VAL B 63 -35.403 -42.263 18.084 1.00 32.33

ANISOU 1963 N VAL B 63 4261 3165 4859 659 -267 -456

ATOM 1964 CA VAL B 63 -35.596 -41.550 16.821 1.00 30.30

ANISOU 1964 CA VAL B 63 4130 2996 4388 711 -323 -556

ATOM 1965 C VAL B 63 -36.828 -40.629 16.826 1.00 32.92

ANISOU 1965 C VAL B 63 4399 3449 4661 685 -456 -522

ATOM 1966 O VAL B 63 -37.930 -41.055 17.164 1.00 37.11

ANISOU 1966 O VAL B 63 4819 3964 5319 603 -569 -539

ATOM 1967 CB VAL B 63 -35.738 -42.552 15.653 1.00 32.29

ANISOU 1967 CB VAL B 63 4513 3154 4603 707 -391 -758

ATOM 1968 CGI VAL B 63 -36.095 -41.829 14.354 1.00 30.92

ANISOU 1968 CGI VAL B 63 4485 3094 4169 758 -481 -852

ATOM 1969 CG2 VAL B 63 -34.460 -43.374 15.489 1.00 30.15

ANISOU 1969 CG2 VAL B 63 4318 2758 4380 768 -237 -809

ATOM 1970 N LEU B 64 -36. 632 -39.369 16.449 1.00 32.18

ANISOU 1970 N LEU B 64 4368 3465 4395 759 -433 -468

ATOM 1971 CA LEU B 64 -37. 730 -38.415 16.266 1.00 34.29

ANISOU 1971 CA LEU B 64 4597 3837 4594 774 -560 -437

ATOM 1972 C LEU B 64 -37.838 -37.972 14.799 1.00 39.93

ANISOU 1972 C LEU B 64 5487 4613 5073 848 -647 -514

ATOM 1973 O LEU B 64 -36.836 -37.623 14.171 1.00 42.80

ANISOU 1973 O LEU B 64 6002 4981 5279 914 -530 -507

ATOM 1974 CB LEU B 64 -37.531 -37.186 17.153 1.00 29.86

ANISOU 1974 CB LEU B 64 3969 3337 4038 807 -468 -288

ATOM 1975 CG LEU B 64 -37.603 -37.428 18.657 1.00 26.87

ANISOU 1975 CG LEU B 64 3430 2938 3840 742 -401 -203

ATOM 1976 CD1 LEU B 64 -37.222 -36.169 19.412 1.00 24.66

ANISOU 1976 CD1 LEU B 64 3130 2714 3526 780 -307 -94

ATOM 1977 CD2 LEU B 64 -38.994 -37.877 19.033 1.00 23.46

ANISOU 1977 CD2 LEU B 64 2852 2519 3543 675 -516 -221

ATOM 1978 N SER B 65 -39.055 -37.983 14.262 1.00 41.92

ANISOU 1978 N SER B 65 5711 4919 5299 837 -851 -579

ATOM 1979 CA SER B 65 -39.286 -37.665 12.854 1.00 43.73 ANISOU 1979 CA SER B 65 6116 5220 5278 908 -979 -654

ATOM 1980 C SER B 65 -40.073 -36.366 12.708 1.00 42.83

ANISOU 1980 C SER B 65 5972 5216 5085 988 -1086 -541

ATOM 1981 O SER B 65 -40.719 -35.933 13.660 1.00 42.52

ANISOU 1981 O SER B 65 5745 5192 5220 971 -1098 -453

ATOM 1982 CB SER B 65 -40.048 -38.811 12.186 1.00 46.84

ANISOU 1982 CB SER B 65 6517 5590 5690 837 -1176 -847

ATOM 1983 OG SER B 65 -41.318 -38.974 12.789 1.00 51.90

ANISOU 1983 OG SER B 65 6931 6249 6539 759 -1334 -842

ATOM 1984 N PRO B 66 -40.027 -35.739 11.512 1.00 45.43

ANISOU 1984 N PRO B 66 6496 5620 5147 1086 -1157 -536

ATOM 1985 CA PRO B 66 -40.810 -34.519 11.263 1.00 43.23

ANISOU 1985 CA PRO B 66 6204 5429 4790 1185 -1281 -415

ATOM 1986 C PRO B 66 -42.309 -34.635 11.588 1.00 45.78

ANISOU 1986 C PRO B 66 6299 5807 5288 1160 -1515 -443

ATOM 1987 O PRO B 66 -42.900 -33.649 12.033 1.00 47.61

ANISOU 1987 O PRO B 66 6418 6073 5598 1230 -1541 -319

ATOM 1988 CB PRO B 66 -40.606 -34.273 9.762 1.00 39.94

ANISOU 1988 CB PRO B 66 6057 5085 4035 1276 -1363 -441

ATOM 1989 CG PRO B 66 -39.256 -34.820 9.493 1.00 43.28

ANISOU 1989 CG PRO B 66 6643 5445 4357 1251 -1137 -499

ATOM 1990 CD PRO B 66 -39.128 -36.045 10.379 1.00 42.94

ANISOU 1990 CD PRO B 66 6435 5304 4575 1127 -1086 -616

ATOM 1991 N GLN B 67 -42. 911 -35.802 11.373 1.00 45.14

ANISOU 1991 N GLN B 67 6140 5724 5287 1060 -1674 -608

ATOM 1992 CA GLN B 67 -44. 339 -35.975 11.657 1.00 50.13

ANISOU 1992 CA GLN B 67 6520 6410 6116 1016 -1893 -640

ATOM 1993 C GLN B 67 -44. 650 -36.052 13.157 1.00 48.56

ANISOU 1993 C GLN B 67 6059 6160 6233 939 -1756 -565

ATOM 1994 O GLN B 67 -45. 743 -35.699 13.589 1.00 49.73

ANISOU 1994 O GLN B 67 5981 6368 6547 949 -1856 -521

ATOM 1995 CB GLN B 67 -44. 912 -37.190 10.918 1.00 58.94

ANISOU 1995 CB GLN B 67 7630 7530 7233 910 -2119 -852

ATOM 1996 CG GLN B 67 -44. 116 -38.479 11.087 1.00 67.99

ANISOU 1996 CG GLN B 67 8852 8537 8445 787 -1984 -987

ATOM 1997 CD GLN B 67 -42.937 -38.600 10.119 1.00 73.98

ANISOU 1997 CD GLN B 67 9931 9274 8902 853 -1884 -1057

ATOM 1998 OE1 GLN B 67 -42.449 -37.606 9.579 1.00 75.49

ANISOU 1998 OE1 GLN B 67 10293 9540 8850 984 -1827 -951

ATOM 1999 NE2 GLN B 67 -42.480 -39.830 9.899 1.00 75.11

ANISOU 1999 NE2 GLN B 67 10158 9304 9075 764 -1847 -1233

ATOM 2000 N GLY B 68 -43.681 -36.505 13.947 1.00 46.58

ANISOU 2000 N GLY B 68 5837 5806 6055 873 -1522 -546

ATOM 2001 CA GLY B 68 -43.843 -36.571 15.388 1.00 42.58

ANISOU 2001 CA GLY B 68 5127 5259 5791 808 -1375 -463

ATOM 2002 C GLY B 68 -44.948 -37.516 15.815 1.00 39.82

ANISOU 2002 C GLY B 68 4540 4899 5690 677 -1482 -532

ATOM 2003 O GLY B 68 -45.118 -38.585 15.235 1.00 40.70

ANISOU 2003 O GLY B 68 4673 4961 5832 580 -1603 -672

ATOM 2004 N GLY B 69 -45.707 -37.113 16.828 1.00 38.68

ANISOU 2004 N GLY B 69 4171 4796 5732 668 -1428 -439

ATOM 2005 CA GLY B 69 -46.746 -37.956 17.391 1.00 39.37

ANISOU 2005 CA GLY B 69 4003 4872 6085 531 -1478 -473

ATOM 2006 C GLY B 69 -46.338 -38.512 18.748 1.00 40.74

ANISOU 2006 C GLY B 69 4109 4963 6407 435 -1240 -390

ATOM 2007 O GLY B 69 -45.143 -38.666 19.035 1.00 35.38

ANISOU 2007 O GLY B 69 3601 4210 5629 445 -1090 -356

ATOM 2008 N GLY B 70 -47.331 -38.811 19.583 1.00 42.01

ANISOU 2008 N GLY B 70 4014 5143 6804 346 -1205 -348 ATOM 2009 CA GLY B 70 -47.100 -39.458 20.863 1.00 39.23

ANISOU 2009 CA GLY B 70 3596 4720 6588 242 -992 -255

ATOM 2010 C GLY B 70 -46. 609 -38.524 21.953 1.00 37.49

ANISOU 2010 C GLY B 70 3407 4555 6282 336 -779 -122

ATOM 2011 O GLY B 70 -46.567 -37.305 21.763 1.00 36.79

ANISOU 2011 O GLY B 70 3363 4547 6068 478 -788 -105

ATOM 2012 N PRO B 71 -46.221 -39.099 23.104 1.00 36.58

ANISOU 2012 N PRO B 71 3283 4387 6229 257 -592 -28

ATOM 2013 CA PRO B 71 -45.774 -38.357 24.296 1.00 32.69

ANISOU 2013 CA PRO B 71 2820 3952 5649 322 -393 86

ATOM 2014 C PRO B 71 -44.582 -37.446 24.001 1.00 29.02

ANISOU 2014 C PRO B 71 2573 3493 4959 447 -379 79

ATOM 2015 O PRO B 71 -44.428 -36.412 24.642 1.00 28.43

ANISOU 2015 O PRO B 71 2517 3484 4799 532 -278 124

ATOM 2016 CB PRO B 71 -45.340 -39.468 25.265 1.00 33.53

ANISOU 2016 CB PRO B 71 2939 3975 5828 203 -255 179

ATOM 2017 CG PRO B 71 -46.044 -40.706 24.786 1.00 38.48

ANISOU 2017 CG PRO B 71 3453 4503 6665 58 -351 130

ATOM 2018 CD PRO B 71 -46. 180 -40.562 23.302 1.00 36.58

ANISOU 2018 CD PRO B 71 3260 4256 6384 97 -575 -27

ATOM 2019 N TRP B 72 -43. 740 -37.828 23.046 1.00 27.59

ANISOU 2019 N TRP B 72 2554 3238 4690 453 -468 13

ATOM 2020 CA TRP B 72 -42.562 -37.024 22.738 1.00 25.22

ANISOU 2020 CA TRP B 72 2443 2938 4199 553 -434 15

ATOM 2021 C TRP B 72 -42.857 -35.609 22.227 1.00 26.06

ANISOU 2021 C TRP B 72 2579 3118 4205 679 -481 5

ATOM 2022 O TRP B 72 -42.019 -34.726 22.372 1.00 29.14

ANISOU 2022 O TRP B 72 3088 3510 4475 748 -404 37

ATOM 2023 CB TRP B 72 -41.620 -37.767 21.793 1.00 23.84

ANISOU 2023 CB TRP B 72 2425 2673 3959 540 -487 -53

ATOM 2024 CG TRP B 72 -40.722 -38.691 22.538 1.00 25.23

ANISOU 2024 CG TRP B 72 2635 2765 4184 479 -379 0

ATOM 2025 CD1 TRP B 72 -40.921 -40.027 22.774 1.00 24.23

ANISOU 2025 CD1 TRP B 72 2458 2540 4209 376 -382 0

ATOM 2026 CD2 TRP B 72 -39.493 -38.346 23.190 1.00 21.96

ANISOU 2026 CD2 TRP B 72 2305 2353 3684 519 -262 72

ATOM 2027 NE1 TRP B 72 -39.882 -40.532 23.511 1.00 23.57

ANISOU 2027 NE1 TRP B 72 2431 2395 4130 371 -274 82

ATOM 2028 CE2 TRP B 72 -38.992 -39.520 23.783 1.00 24.82

ANISOU 2028 CE2 TRP B 72 2662 2628 4141 457 -209 123

ATOM 2029 CE3 TRP B 72 -38.765 -37.159 23.320 1.00 23.02

ANISOU 2029 CE3 TRP B 72 2513 2547 3687 597 -205 98

ATOM 2030 CZ2 TRP B 72 -37.796 -39.543 24.503 1.00 22.94

ANISOU 2030 CZ2 TRP B 72 2476 2382 3859 483 -122 203

ATOM 2031 CZ3 TRP B 72 -37.572 -37.182 24.033 1.00 22.10

ANISOU 2031 CZ3 TRP B 72 2442 2420 3536 600 -115 158

ATOM 2032 CH2 TRP B 72 -37. 101 -38.367 24.613 1.00 20.73

ANISOU 2032 CH2 TRP B 72 2248 2181 3447 550 -84 212

ATOM 2033 N ASP B 73 -44. 037 -35.391 21.649 1.00 28.77

ANISOU 2033 N ASP B 73 2805 3512 4614 708 -614 -33

ATOM 2034 CA ASP B 73 -44.409 -34.058 21.153 1.00 35.06

ANISOU 2034 CA ASP B 73 3623 4364 5334 848 -672 -22

ATOM 2035 C ASP B 73 -44.390 -32.981 22.239 1.00 38.38

ANISOU 2035 C ASP B 73 4015 4810 5759 918 -513 44

ATOM 2036 O ASP B 73 -44.152 -31.815 21.947 1.00 39.56

ANISOU 2036 O ASP B 73 4262 4951 5817 1032 -507 64

ATOM 2037 CB ASP B 73 -45.781 -34.077 20.473 1.00 36.24

ANISOU 2037 CB ASP B 73 3607 4576 5584 874 -860 -64

ATOM 2038 CG ASP B 73 -45.740 -34.705 19.096 1.00 43.25 ANISOU 2038 CG ASP B 73 4593 5453 6389 852 -1063 ^■154

ATOM 2039 OD1 ASP B 73 -44.636 -34. ,814 18. ,527 1. ,00 43, , 35

ANISOU 2039 OD1 ASP B 73 4826 5412 6232 861 -1038 ^■174

ATOM 2040 OD2 ASP B 73 -46.812 -35. ,085 18, ,575 1. ,00 49, , 84

ANISOU 2040 OD2 ASP B 73 5277 6336 7325 825 -1247 ^■213

ATOM 2041 N SER B 74 -44.641 -33. ,384 23, ,483 1. ,00 39, , 98

ANISOU 2041 N SER B 74 4097 5034 6061 846 -379 76

ATOM 2042 CA SER B 74 -44.643 -32. ,463 24, ,616 1. ,00 41, , 32

ANISOU 2042 CA SER B 74 4250 5236 6215 903 -217 113

ATOM 2043 C SER B 74 -43.236 -32. ,024 24, ,974 1. ,00 41, , 19

ANISOU 2043 C SER B 74 4431 5172 6048 905 -126 127

ATOM 2044 O SER B 74 -43.049 -30. ,979 25, ,599 1. ,00 47 , , 98

ANISOU 2044 O SER B 74 5337 6035 6857 970 -31 127

ATOM 2045 CB SER B 74 -45.252 -33. ,130 25, ,849 1. ,00 40, , 53

ANISOU 2045 CB SER B 74 3988 5186 6225 816 -85 151

ATOM 2046 OG SER B 74 -46.557 -33. ,596 25, ,591 1. ,00 46, , 93

ANISOU 2046 OG SER B 74 4578 6040 7214 788 -153 141

ATOM 2047 N VAL B 75 -42.252 -32. ,829 24, ,585 1. ,00 31, , 07

ANISOU 2047 N VAL B 75 3254 3841 4710 834 -157 127

ATOM 2048 CA VAL B 75 -40.893 -32. ,671 25, ,082 1. ,00 29, , 87

ANISOU 2048 CA VAL B 75 3236 3659 4455 811 -71 147

ATOM 2049 C VAL B 75 -39.925 -32. ,157 24, ,029 1. ,00 33, ,24

ANISOU 2049 C VAL B 75 3820 4029 4782 855 -114 128

ATOM 2050 O VAL B 75 -39.150 -31. ,235 24, ,282 1. ,00 36, , 08

ANISOU 2050 O VAL B 75 4269 4366 5072 882 -49 134

ATOM 2051 CB VAL B 75 -40.359 -34. ,014 25, ,598 1. ,00 29, , 30

ANISOU 2051 CB VAL B 75 3150 3569 4415 707 -42 183

ATOM 2052 CGI VAL B 75 -38.908 -33. ,875 26, ,048 1. ,00 25, , 00

ANISOU 2052 CGI VAL B 75 2717 3005 3777 694 17 207

ATOM 2053 CG2 VAL B 75 -41.251 -34. ,542 26, ,721 1. ,00 29, , 66

ANISOU 2053 CG2 VAL B 75 3055 3667 4546 651 33 233

ATOM 2054 N ALA B 76 -39.952 -32. ,790 22, ,859 1. ,00 30, , 87

ANISOU 2054 N ALA B 76 3556 3702 4471 852 -216 99

ATOM 2055 CA ALA B 76 -39.090 -32. ,416 21, ,750 1. ,00 26, ,22

ANISOU 2055 CA ALA B 76 3123 3070 3768 894 -237 87

ATOM 2056 C ALA B 76 -39.835 -32. ,639 20, ,444 1. ,00 31, , 37

ANISOU 2056 C ALA B 76 3800 3734 4387 937 -383 45

ATOM 2057 O ALA B 76 -40.345 -33. ,732 20, ,171 1. ,00 34 , , 58

ANISOU 2057 O ALA B 76 4142 4144 4853 882 -468 -6

ATOM 2058 CB ALA B 76 -37.796 -33. ,212 21, ,776 1. ,00 19, ,81

ANISOU 2058 CB ALA B 76 2375 2217 2934 835 -175 84

ATOM 2059 N ARG B 77 -39.886 -31. ,593 19, ,634 1. ,00 28 , ,28

ANISOU 2059 N ARG B 77 3508 3340 3895 1032 -420 69

ATOM 2060 CA ARG B 77 -40.708 -31. ,586 18, ,445 1. ,00 29, , 11

ANISOU 2060 CA ARG B 77 3640 3480 3939 1095 -586 45

ATOM 2061 C ARG B 77 -39.870 -31. ,055 17, ,290 1. ,00 31, , 18

ANISOU 2061 C ARG B 77 4119 3715 4011 1156 -573 73

ATOM 2062 O ARG B 77 -39.069 -30. ,132 17, ,473 1. ,00 26, , 55

ANISOU 2062 O ARG B 77 3623 3080 3384 1181 -446 140

ATOM 2063 CB ARG B 77 -41.913 -30. ,675 18, ,686 1. ,00 32 , , 47

ANISOU 2063 CB ARG B 77 3952 3943 4441 1186 -654 84

ATOM 2064 CG ARG B 77 -42.911 -30. ,619 17, ,564 1. ,00 40, , 52

ANISOU 2064 CG ARG B 77 4958 5018 5417 1265 -864 71

ATOM 2065 CD ARG B 77 -43.722 -31. ,909 17, ,448 1. ,00 46, ,23

ANISOU 2065 CD ARG B 77 5530 5794 6242 1173 -1002 -23

ATOM 2066 NE ARG B 77 -44.693 -31. ,830 16, ,355 1. ,00 53, , 96

ANISOU 2066 NE ARG B 77 6485 6843 7175 1245 -1242 -49

ATOM 2067 CZ ARG B 77 -44.449 -32. ,228 15, ,109 1. ,00 59, , 43

ANISOU 2067 CZ ARG B 77 7340 7555 7686 1251 -1378 ^■105 ATOM 2068 NH1 ARG B 77 -43.264 -32.745 14.793 1.00 57.77

ANISOU 2068 NH1 ARG B 77 7318 7290 7343 1195 -1269 -144

ATOM 2069 NH2 ARG B 77 -45. 389 -32.116 14.179 1.00 64.34

ANISOU 2069 NH2 ARG B 77 7933 8259 8253 1320 -1624 -128

ATOM 2070 N VAL B 78 -40. 046 -31.640 16.107 1.00 31.57

ANISOU 2070 N VAL B 78 4258 3796 3943 1170 -697 17

ATOM 2071 CA VAL B 78 -39.383 -31.147 14.905 1.00 30.04

ANISOU 2071 CA VAL B 78 4285 3596 3531 1238 -682 52

ATOM 2072 C VAL B 78 -40.146 -29.962 14.286 1.00 27.69

ANISOU 2072 C VAL B 78 4046 3326 3148 1368 -793 146

ATOM 2073 O VAL B 78 -41.329 -30.062 14.009 1.00 35.21

ANISOU 2073 O VAL B 78 4908 4344 4128 1415 -989 122

ATOM 2074 CB VAL B 78 -39.220 -32.277 13.872 1.00 30.83

ANISOU 2074 CB VAL B 78 4489 3725 3501 1209 -762 -63

ATOM 2075 CGI VAL B 78 -38.590 -31.748 12.584 1.00 28.66

ANISOU 2075 CGI VAL B 78 4463 3466 2961 1289 -729 -21

ATOM 2076 CG2 VAL B 78 -38. 390 -33.423 14.465 1.00 28.10

ANISOU 2076 CG2 VAL B 78 4094 3321 3260 1103 -638 -142

ATOM 2077 N LEU B 79 -39. 460 -28.843 14.074 1.00 27.87

ANISOU 2077 N LEU B 79 4212 3291 3087 1427 -671 261

ATOM 2078 CA LEU B 79 -40. 077 -27.632 13.512 1.00 29.32

ANISOU 2078 CA LEU B 79 4476 3466 3199 1566 -755 382

ATOM 2079 C LEU B 79 -40. 124 -27.686 11.975 1.00 31.49

ANISOU 2079 C LEU B 79 4959 3803 3203 1642 -875 413

ATOM 2080 O LEU B 79 -39. 461 -28.532 11.372 1.00 33.97

ANISOU 2080 O LEU B 79 5380 4150 3376 1583 -837 334

ATOM 2081 CB LEU B 79 -39. 304 -26.394 13.989 1.00 32.57

ANISOU 2081 CB LEU B 79 4962 3755 3658 1580 -560 496

ATOM 2082 CG LEU B 79 -39.272 -26.162 15.503 1.00 30.62

ANISOU 2082 CG LEU B 79 4544 3452 3638 1519 -453 459

ATOM 2083 CD1 LEU B 79 -38.499 -24.902 15.822 1.00 30.98

ANISOU 2083 CD1 LEU B 79 4688 3364 3718 1525 -285 550

ATOM 2084 CD2 LEU B 79 -40.689 -26.071 16.068 1.00 28.86

ANISOU 2084 CD2 LEU B 79 4132 3272 3560 1589 -588 433

ATOM 2085 N PRO B 80 -40.912 -26.799 11.339 1.00 33.47

ANISOU 2085 N PRO B 80 5274 4072 3373 1786 -1022 526

ATOM 2086 CA PRO B 80 -40.996 -26.807 9.873 1.00 35.94

ANISOU 2086 CA PRO B 80 5807 4463 3386 1871 -1156 571

ATOM 2087 C PRO B 80 -39.644 -26.669 9.164 1.00 41.27

ANISOU 2087 C PRO B 80 6742 5100 3840 1843 -940 631

ATOM 2088 O PRO B 80 -39.476 -27.239 8.089 1.00 40.03

ANISOU 2088 O PRO B 80 6756 5031 3422 1855 -1001 584

ATOM 2089 CB PRO B 80 -41.887 -25.594 9.565 1.00 37.91

ANISOU 2089 CB PRO B 80 6077 4697 3628 2046 -1299 738

ATOM 2090 CG PRO B 80 -42.765 -25.478 10.752 1.00 36.82

ANISOU 2090 CG PRO B 80 5649 4536 3804 2049 -1346 693

ATOM 2091 CD PRO B 80 -41.908 -25.881 11.930 1.00 33.92

ANISOU 2091 CD PRO B 80 5185 4094 3608 1891 -1103 604

ATOM 2092 N ASN B 81 -38.699 -25.940 9.747 1.00 34.91

ANISOU 2092 N ASN B 81 5962 4168 3137 1799 -688 722

ATOM 2093 CA ASN B 81 -37.380 -25.815 9.134 1.00 37.02

ANISOU 2093 CA ASN B 81 6432 4397 3236 1756 -455 783

ATOM 2094 C ASN B 81 -36.453 -26.988 9.497 1.00 35.22

ANISOU 2094 C ASN B 81 6130 4189 3062 1620 -311 621

ATOM 2095 O ASN B 81 -35.270 -26.987 9.170 1.00 33.80

ANISOU 2095 O ASN B 81 6059 3980 2804 1572 -87 650

ATOM 2096 CB ASN B 81 -36.736 -24.459 9.475 1.00 35.29

ANISOU 2096 CB ASN B 81 6274 4023 3111 1760 -253 961

ATOM 2097 CG ASN B 81 -36.164 -24.406 10.895 1.00 33.88 ANISOU 2097 CG ASN B 81 5896 3748 3228 1636 - 102 892

ATOM 2098 OD1 ASN B 81 -36.534 -25. ,196 11. ,772 1. , 00 31. , 01

ANISOU 2098 OD1 ASN B 81 5332 3431 3019 1579 - 177 747

ATOM 2099 ND2 ASN B 81 -35.247 -23. ,470 11. ,120 1. , 00 32. ,81

ANISOU 2099 ND2 ASN B 81 5822 3478 3164 1587 109 1001

ATOM 2100 N GLY B 82 -36.997 -27. ,979 10, ,191 1. , 00 32. ,28

ANISOU 2100 N GLY B 82 5561 3858 2844 1562 - 432 462

ATOM 2101 CA GLY B 82 -36.233 -29. ,168 10, ,523 1. , 00 31. , 01

ANISOU 2101 CA GLY B 82 5332 3702 2748 1454 - 325 316

ATOM 2102 C GLY B 82 -35.516 -29. ,127 11. ,861 1. , 00 33. , 08

ANISOU 2102 C GLY B 82 5419 3882 3266 1357 - 161 315

ATOM 2103 O GLY B 82 -34.995 -30. ,136 12, ,317 1. , 00 36. , 34

ANISOU 2103 O GLY B 82 5740 4294 3774 1279 - 101 208

ATOM 2104 N SER B 83 -35.484 -27. ,960 12, ,490 1. , 00 29. , 69

ANISOU 2104 N SER B 83 4954 3380 2947 1365 -98 430

ATOM 2105 CA SER B 83 -34.879 -27. ,819 13, ,806 1. , 00 29. , 44

ANISOU 2105 CA SER B 83 4766 3283 3137 1273 25 417

ATOM 2106 C SER B 83 -35.660 -28. ,583 14, ,869 1. , 00 29. ,86

ANISOU 2106 C SER B 83 4616 3372 3357 1234 -93 316

ATOM 2107 O SER B 83 -36.877 -28. ,749 14, ,768 1. , 00 31. , 77

ANISOU 2107 O SER B 83 4806 3664 3603 1286 - 268 290

ATOM 2108 CB SER B 83 -34.789 -26. ,343 14, ,204 1. , 00 31. , 17

ANISOU 2108 CB SER B 83 5013 3401 3430 1292 100 539

ATOM 2109 OG SER B 83 -33.829 -25. ,652 13, ,422 1. , 00 32. , 53

ANISOU 2109 OG SER B 83 5351 3513 3497 1289 263 648

ATOM 2110 N LEU B 84 -34.947 -29. ,044 15, ,891 1. , 00 24. , 12

ANISOU 2110 N LEU B 84 3769 2625 2771 1140 5 272

ATOM 2111 CA LEU B 84 -35.577 -29. ,705 17, ,018 1. , 00 24. ,29

ANISOU 2111 CA LEU B 84 3612 2675 2944 1095 -69 206

ATOM 2112 C LEU B 84 -35.853 -28. ,669 18, ,092 1. , 00 27. ,71

ANISOU 2112 C LEU B 84 3970 3072 3487 1096 -38 249

ATOM 2113 O LEU B 84 -34.973 -27. ,872 18, ,442 1. , 00 28. , 60

ANISOU 2113 O LEU B 84 4119 3123 3626 1063 83 290

ATOM 2114 CB LEU B 84 -34.686 -30. ,816 17, ,576 1. , 00 24. , 18

ANISOU 2114 CB LEU B 84 3520 2660 3006 1010 6 149

ATOM 2115 CG LEU B 84 -35.400 -31. ,759 18, ,561 1. , 00 24. ,88

ANISOU 2115 CG LEU B 84 3452 2776 3225 963 -73 98

ATOM 2116 CD1 LEU B 84 -36.441 -32. ,609 17, ,826 1. , 00 21. , 65

ANISOU 2116 CD1 LEU B 84 3041 2398 2787 981 - 221 29

ATOM 2117 CD2 LEU B 84 -34.407 -32. ,656 19, ,322 1. , 00 21. , 43

ANISOU 2117 CD2 LEU B 84 2943 2322 2878 892 10 82

ATOM 2118 N PHE B 85 -37.074 -28. ,689 18, ,612 1. , 00 24. , 30

ANISOU 2118 N PHE B 85 3429 2674 3128 1129 - 140 228

ATOM 2119 CA PHE B 85 -37.514 -27. ,698 19, ,574 1. , 00 23. ,89

ANISOU 2119 CA PHE B 85 3317 2591 3170 1155 - 107 248

ATOM 2120 C PHE B 85 -37.937 -28. ,338 20, ,882 1. , 00 25. , 39

ANISOU 2120 C PHE B 85 3342 2833 3472 1095 - 100 194

ATOM 2121 O PHE B 85 -38.822 -29. ,198 20, ,908 1. , 00 23. ,81

ANISOU 2121 O PHE B 85 3036 2695 3316 1091 - 187 163

ATOM 2122 CB PHE B 85 -38.680 -26. ,897 18, ,998 1. , 00 24. , 85

ANISOU 2122 CB PHE B 85 3454 2705 3281 1283 - 210 292

ATOM 2123 CG PHE B 85 -39.308 -25. ,946 19, ,976 1. , 00 30. , 72

ANISOU 2123 CG PHE B 85 4122 3409 4140 1335 - 172 292

ATOM 2124 CD1 PHE B 85 -38.575 -24. ,901 20, ,521 1. , 00 31. , 10

ANISOU 2124 CD1 PHE B 85 4248 3353 4217 1320 -46 306

ATOM 2125 CD2 PHE B 85 -40.642 -26. ,085 20, ,337 1. , 00 35. ,41

ANISOU 2125 CD2 PHE B 85 4562 4065 4828 1399 - 255 267

ATOM 2126 CE1 PHE B 85 -39.157 -24. ,016 21. ,411 1. , 00 32. , 56

ANISOU 2126 CE1 PHE B 85 4384 3487 4501 1376 -2 279 ATOM 2127 CE2 PHE B 85 -41.233 -25.203 21.233 1.00 35.49 C

ANISOU 2127 CE2 PHE B 85 4503 4038 4944 1466 -193 254 C

ATOM 2128 CZ PHE B 85 -40.491 -24.163 21.763 1.00 34.38 C

ANISOU 2128 CZ PHE B 85 4468 3785 4811 1460 -66 253 C ATOM 2129 N LEU B 86 -37.303 -27.906 21.965 1.00 27.36 N

ANISOU 2129 N LEU B 86 3576 3058 3763 1043 3 184 N

ATOM 2130 CA LEU B 86 -37.704 -28.296 23.315 1.00 25.51 C

ANISOU 2130 CA LEU B 86 3217 2880 3597 1000 30 148 C

ATOM 2131 C LEU B 86 -38.204 -27.043 24.038 1.00 26.05 C ANISOU 2131 C LEU B 86 3284 2913 3700 1058 83 129 C

ATOM 2132 O LEU B 86 -37.420 -26.144 24.338 1.00 27.38 O

ANISOU 2132 O LEU B 86 3538 3011 3856 1039 152 116 O

ATOM 2133 CB LEU B 86 -36.523 -28.902 24.083 1.00 19.08 C

ANISOU 2133 CB LEU B 86 2393 2082 2774 896 90 140 C ATOM 2134 CG LEU B 86 -35.988 -30.292 23.717 1.00 26.74 C

ANISOU 2134 CG LEU B 86 3341 3075 3745 843 61 149 C

ATOM 2135 CD1 LEU B 86 -35.128 -30.257 22.468 1.00 18.72 C

ANISOU 2135 CD1 LEU B 86 2429 2010 2675 855 72 159 C

ATOM 2136 CD2 LEU B 86 -35.201 -30.905 24.887 1.00 22.00 C ANISOU 2136 CD2 LEU B 86 2685 2509 3165 766 102 159 C

ATOM 2137 N PRO B 87 -39.511 -26.978 24.320 1.00 26.35 N

ANISOU 2137 N PRO B 87 3217 2993 3800 1129 58 117 N

ATOM 2138 CA PRO B 87 -40.114 -25.782 24.928 1.00 26.44 C

ANISOU 2138 CA PRO B 87 3225 2962 3860 1216 120 86 C ATOM 2139 C PRO B 87 -39.587 -25.449 26.331 1.00 28.14 C

ANISOU 2139 C PRO B 87 3458 3182 4054 1154 235 19 C

ATOM 2140 O PRO B 87 -39.549 -24.276 26.700 1.00 28.37 O

ANISOU 2140 O PRO B 87 3557 3125 4098 1203 297 -29 O

ATOM 2141 CB PRO B 87 -41.610 -26.128 24.985 1.00 25.15 C ANISOU 2141 CB PRO B 87 2893 2876 3786 1291 76 87 C

ATOM 2142 CG PRO B 87 -41.672 -27.618 24.924 1.00 25.30 C

ANISOU 2142 CG PRO B 87 2820 2986 3808 1190 23 100 C

ATOM 2143 CD PRO B 87 -40.502 -28.041 24.078 1.00 26.93 C

ANISOU 2143 CD PRO B 87 3157 3151 3925 1127 -25 123 C ATOM 2144 N ALA B 88 -39.183 -26.457 27.097 1.00 25.14 N

ANISOU 2144 N ALA B 88 3027 2893 3633 1050 254 14 N

ATOM 2145 CA ALA B 88 -38.705 -26.228 28.461 1.00 23.62 C

ANISOU 2145 CA ALA B 88 2859 2735 3381 993 337 -47 C

ATOM 2146 C ALA B 88 -37.728 -27.321 28.887 1.00 22.74 C ANISOU 2146 C ALA B 88 2740 2693 3208 876 313 -12 C

ATOM 2147 O ALA B 88 -38.135 -28.398 29.313 1.00 23.57 O

ANISOU 2147 O ALA B 88 2759 2884 3311 844 314 33 O

ATOM 2148 CB ALA B 88 -39.893 -26.140 29.443 1.00 22.61 C

ANISOU 2148 CB ALA B 88 2640 2682 3268 1049 423 -86 C ATOM 2149 N VAL B 89 -36.437 -27.028 28.760 1.00 23.18 N

ANISOU 2149 N VAL B 89 2875 2699 3233 814 294 -23 N

ATOM 2150 CA VAL B 89 -35.377 -27.974 29.063 1.00 25.37 C

ANISOU 2150 CA VAL B 89 3133 3030 3475 724 258 16 C

ATOM 2151 C VAL B 89 -35.377 -28.380 30.538 1.00 28.37 C ANISOU 2151 C VAL B 89 3488 3520 3770 681 278 6 C

ATOM 2152 O VAL B 89 -35.592 -27.536 31.425 1.00 28.84 O

ANISOU 2152 O VAL B 89 3593 3599 3765 690 326 -76 O

ATOM 2153 CB VAL B 89 -33.999 -27.388 28.685 1.00 29.04 C

ANISOU 2153 CB VAL B 89 3660 3425 3950 668 243 -4 C ATOM 2154 CGI VAL B 89 -32.884 -28.089 29.436 1.00 29.22 C

ANISOU 2154 CGI VAL B 89 3641 3521 3939 585 203 14 C

ATOM 2155 CG2 VAL B 89 -33.775 -27.485 27.192 1.00 28.61 C

ANISOU 2155 CG2 VAL B 89 3630 3294 3945 696 233 48 C

ATOM 2156 N GLY B 90 -35.151 -29.674 30.785 1.00 23.37 N ANISOU 2156 N GLY B 90 2798 2952 3129 642 247 91

ATOM 2157 CA GLY B 90 -35.006 -30. .199 32. .131 1. , 00 23. , 19

ANISOU 2157 CA GLY B 90 2769 3039 3003 602 255 122

ATOM 2158 C GLY B 90 -33.710 -30. .978 32. .290 1. , 00 25. ,71

ANISOU 2158 C GLY B 90 3075 3380 3312 550 174 188

ATOM 2159 O GLY B 90 -33.010 -31. .256 31. .306 1. , 00 23. ,76

ANISOU 2159 O GLY B 90 2807 3062 3158 547 133 208

ATOM 2160 N ILE B 91 -33.392 -31. .330 33. .533 1. , 00 25. ,79

ANISOU 2160 N ILE B 91 3098 3496 3203 519 152 225

ATOM 2161 CA ILE B 91 -32.202 -32. .116 33. .843 1. , 00 26. , 03

ANISOU 2161 CA ILE B 91 3101 3563 3226 488 56 307

ATOM 2162 C ILE B 91 -32.080 -33. .380 32. .972 1. , 00 25. , 31

ANISOU 2162 C ILE B 91 2945 3396 3276 509 42 414

ATOM 2163 O ILE B 91 -30.996 -33. .706 32. .494 1. , 00 25. , 58

ANISOU 2163 O ILE B 91 2940 3392 3388 508 -17 436

ATOM 2164 CB ILE B 91 -32.172 -32. .501 35. .342 1. , 00 27. , 67

ANISOU 2164 CB ILE B 91 3345 3909 3258 472 33 369

ATOM 2165 CGI ILE B 91 -32.028 -31. .245 36. .207 1. , 00 30. , 04

ANISOU 2165 CGI ILE B 91 3728 4284 3401 446 24 227

ATOM 2166 CG2 ILE B 91 -31.032 -33. .498 35. .642 1. , 00 23. , 62

ANISOU 2166 CG2 ILE B 91 2789 3431 2756 466 -84 494

ATOM 2167 CD1 ILE B 91 -32.113 -31. .511 37. .712 1. , 00 26. , 00

ANISOU 2167 CD1 ILE B 91 3288 3934 2657 437 10 269

ATOM 2168 N GLN B 92 -33.194 -34. .071 32. .745 1. , 00 24. , 31

ANISOU 2168 N GLN B 92 2799 3240 3198 524 103 468

ATOM 2169 CA GLN B 92 -33.159 -35. .328 32. .006 1. , 00 27. , 61

ANISOU 2169 CA GLN B 92 3171 3570 3750 534 88 549

ATOM 2170 C GLN B 92 -32.912 -35. .155 30. .500 1. , 00 27. , 45

ANISOU 2170 C GLN B 92 3146 3446 3840 557 78 473

ATOM 2171 O GLN B 92 -32.804 -36. .137 29. .767 1. , 00 29. , 85

ANISOU 2171 O GLN B 92 3429 3666 4248 570 66 504

ATOM 2172 CB GLN B 92 -34.425 -36. .154 32. .262 1. , 00 31. , 06

ANISOU 2172 CB GLN B 92 3579 3998 4224 517 150 624

ATOM 2173 CG GLN B 92 -34.624 -36. .565 33. .723 1. , 00 41. , 18

ANISOU 2173 CG GLN B 92 4879 5380 5387 495 186 741

ATOM 2174 CD GLN B 92 -33.405 -37. .276 34. .324 1. , 00 50. , 95

ANISOU 2174 CD GLN B 92 6135 6635 6587 503 101 854

ATOM 2175 OE1 GLN B 92 -32.972 -36. .959 35. .436 1. , 00 53. , 45

ANISOU 2175 OE1 GLN B 92 6499 7074 6737 501 71 889

ATOM 2176 NE2 GLN B 92 -32.857 -38. .245 33. .592 1. , 00 51. , 13

ANISOU 2176 NE2 GLN B 92 6122 6539 6764 522 56 907

ATOM 2177 N ASP B 93 -32.811 -33. .914 30. .041 1. , 00 23. , 57

ANISOU 2177 N ASP B 93 2689 2951 3318 566 90 374

ATOM 2178 CA ASP B 93 -32.518 -33. .667 28. .639 1. , 00 21. , 10

ANISOU 2178 CA ASP B 93 2395 2552 3070 591 94 322

ATOM 2179 C ASP B 93 -31.019 -33. .584 28. .362 1. , 00 19. , 93

ANISOU 2179 C ASP B 93 2234 2387 2953 582 79 320

ATOM 2180 O ASP B 93 -30.620 -33. .348 27. .227 1. , 00 21. , 00

ANISOU 2180 O ASP B 93 2392 2460 3127 601 109 285

ATOM 2181 CB ASP B 93 -33.227 -32. .402 28. .149 1. , 00 24. , 61

ANISOU 2181 CB ASP B 93 2889 2978 3483 614 123 245

ATOM 2182 CG ASP B 93 -34.734 -32. .529 28. .199 1. , 00 26. ,79

ANISOU 2182 CG ASP B 93 3140 3270 3768 638 136 244

ATOM 2183 OD1 ASP B 93 -35.261 -33. .534 27. .677 1. , 00 27. , 77

ANISOU 2183 OD1 ASP B 93 3227 3366 3957 638 112 272

ATOM 2184 OD2 ASP B 93 -35.388 -31. .632 28. .771 1. , 00 27. , 99

ANISOU 2184 OD2 ASP B 93 3301 3457 3878 656 172 206

ATOM 2185 N GLU B 94 -30.190 -33. .773 29. .389 1. , 00 21. , 50

ANISOU 2185 N GLU B 94 2388 2649 3131 557 35 363 ATOM 2186 CA GLU B 94 -28.750 -33.854 29.177 1.00 26.22

ANISOU 2186 CA GLU B 94 2925 3241 3797 551 11 372

ATOM 2187 C GLU B 94 -28.412 -35.065 28.329 1.00 25.99

ANISOU 2187 C GLU B 94 2862 3136 3876 605 32 416

ATOM 2188 O GLU B 94 -28.973 -36.145 28.525 1.00 24.93

ANISOU 2188 O GLU B 94 2731 2975 3768 629 18 476

ATOM 2189 CB GLU B 94 -27.996 -33.946 30.499 1.00 35.68

ANISOU 2189 CB GLU B 94 4069 4539 4951 523 -79 418

ATOM 2190 CG GLU B 94 -28.083 -32.684 31.312 1.00 46.10

ANISOU 2190 CG GLU B 94 5431 5927 6159 463 -104 336

ATOM 2191 CD GLU B 94 -26.981 -32.575 32.338 1.00 50.38

ANISOU 2191 CD GLU B 94 5909 6568 6666 422 -221 345

ATOM 2192 OE1 GLU B 94 -27.004 -33.350 33.332 1.00 50.89

ANISOU 2192 OE1 GLU B 94 5968 6719 6648 443 -295 436

ATOM 2193 OE2 GLU B 94 -26.097 -31.708 32.145 1.00 49.94

ANISOU 2193 OE2 GLU B 94 5808 6503 6664 364 -243 268

ATOM 2194 N GLY B 95 -27.484 -34.894 27.394 1.00 23.52

ANISOU 2194 N GLY B 95 2520 2779 3636 620 81 383

ATOM 2195 CA GLY B 95 -27.091 -35.994 26.533 1.00 21.85

ANISOU 2195 CA GLY B 95 2288 2490 3522 684 123 397

ATOM 2196 C GLY B 95 -26.732 -35.562 25.129 1.00 24.28

ANISOU 2196 C GLY B 95 2638 2746 3843 704 227 328

ATOM 2197 O GLY B 95 -26.223 -34.465 24.911 1.00 22.07

ANISOU 2197 O GLY B 95 2353 2488 3546 663 271 302

ATOM 2198 N ILE B 96 -27.014 -36.430 24.165 1.00 28.15

ANISOU 2198 N ILE B 96 3182 3159 4354 760 271 297

ATOM 2199 CA ILE B 96 -26.562 -36.223 22.795 1.00 28.17

ANISOU 2199 CA ILE B 96 3240 3121 4341 796 385 236

ATOM 2200 C ILE B 96 -27.738 -36.140 21.824 1.00 30.03

ANISOU 2200 C ILE B 96 3623 3324 4463 808 382 173

ATOM 2201 O ILE B 96 -28.679 -36.939 21.900 1.00 27.68

ANISOU 2201 O ILE B 96 3357 2992 4169 815 310 154

ATOM 2202 CB ILE B 96 -25.582 -37.342 22.384 1.00 32.90

ANISOU 2202 CB ILE B 96 3775 3665 5060 872 452 230

ATOM 2203 CGI ILE B 96 -24.407 -37.380 23.365 1.00 34.58

ANISOU 2203 CGI ILE B 96 3813 3927 5400 869 426 305

ATOM 2204 CG2 ILE B 96 -25.079 -37.136 20.962 1.00 31.51

ANISOU 2204 CG2 ILE B 96 3668 3462 4844 914 603 161

ATOM 2205 CD1 ILE B 96 -23.618 -38.655 23.315 1.00 41.56

ANISOU 2205 CD1 ILE B 96 4608 4748 6436 967 453 325

ATOM 2206 N PHE B 97 -27.682 -35.152 20.930 1.00 28.55

ANISOU 2206 N PHE B 97 3521 3146 4180 807 453 149

ATOM 2207 CA PHE B 97 -28.739 -34.903 19.954 1.00 24.79

ANISOU 2207 CA PHE B 97 3188 2658 3572 831 429 103

ATOM 2208 C PHE B 97 -28.112 -34.883 18.568 1.00 28.16

ANISOU 2208 C PHE B 97 3717 3066 3917 880 554 64

ATOM 2209 O PHE B 97 -27.196 -34.100 18.309 1.00 29.45

ANISOU 2209 O PHE B 97 3871 3241 4077 867 675 104

ATOM 2210 CB PHE B 97 -29.424 -33.553 20.223 1.00 23.35

ANISOU 2210 CB PHE B 97 3044 2506 3321 798 390 138

ATOM 2211 CG PHE B 97 -30.227 -33.501 21.510 1.00 26.03

ANISOU 2211 CG PHE B 97 3308 2876 3706 761 288 159

ATOM 2212 CD1 PHE B 97 -31.606 -33.357 21.474 1.00 23.05

ANISOU 2212 CD1 PHE B 97 2966 2510 3283 774 203 143

ATOM 2213 CD2 PHE B 97 -29.601 -33.578 22.753 1.00 26.13

ANISOU 2213 CD2 PHE B 97 3211 2919 3799 717 278 195

ATOM 2214 CE1 PHE B 97 -32.351 -33.291 22.640 1.00 21.67

ANISOU 2214 CE1 PHE B 97 2717 2370 3146 745 147 162

ATOM 2215 CE2 PHE B 97 -30.341 -33.519 23.931 1.00 25.86 ANISOU 2215 CE2 PHE B 97 3131 2926 3768 687 207 215

ATOM 2216 CZ PHE B 97 -31.717 -33.375 23. 876 1, 00 23. 36

ANISOU 2216 CZ PHE B 97 2850 2616 3410 701 159 198

ATOM 2217 N ARG B 98 -28.597 -35.742 17. 676 1, 00 29. 16

ANISOU 2217 N ARG B 98 3943 3163 3973 930 533 -19

ATOM 2218 CA ARG B 98 -28.032 -35.832 16.330 1, 00 28. 08

ANISOU 2218 CA ARG B 98 3931 3020 3720 989 664 -72

ATOM 2219 C ARG B 98 -29.087 -35.697 15.250 1, 00 28. 54

ANISOU 2219 C ARG B 98 4172 3096 3576 1020 585 -132

ATOM 2220 O ARG B 98 -30.150 -36.321 15.316 1, 00 27. 92

ANISOU 2220 O ARG B 98 4107 3003 3497 1013 429 -196

ATOM 2221 CB ARG B 98 -27.325 -37.165 16.128 1, 00 32. 21

ANISOU 2221 CB ARG B 98 4420 3483 4336 1041 737 -152

ATOM 2222 CG ARG B 98 -26.080 -37.329 16.938 1, 00 38. 22

ANISOU 2222 CG ARG B 98 4999 4236 5287 1041 827 -90

ATOM 2223 CD ARG B 98 -25.389 -38.617 16.584 1, 00 42. 08

ANISOU 2223 CD ARG B 98 5465 4651 5874 1124 915 -169

ATOM 2224 NE ARG B 98 -24.128 -38.755 17.296 1, 00 42. 40

ANISOU 2224 NE ARG B 98 5307 4694 6110 1144 996 -99

ATOM 2225 CZ ARG B 98 -23.324 -39.802 17.171 1, 00 44. 04

ANISOU 2225 CZ ARG B 98 5443 4833 6457 1236 1085 -142

ATOM 2226 NH1 ARG B 98 -23.661 -40.806 16.368 1, 00 40. 84

ANISOU 2226 NH1 ARG B 98 5171 4335 6012 1308 1115 -271

ATOM 2227 NH2 ARG B 98 -22.190 -39.847 17.851 1, 00 50.

ANISOU 2227 NH2 ARG B 98 6063 5680 7474 1259 1134 -64

ATOM 2228 N CYS B 99 -28.785 -34.890 14.245 1, 00 28. 99

ANISOU 2228 N CYS B 99 4365 3187 3462 1052 689 -103

ATOM 2229 CA CYS B 99 -29. 644 -34.826 13.082 1, 00 33. 47

ANISOU 2229 CA CYS B 99 5128 3787 3801 1101 610 -156

ATOM 2230 C CYS B 99 -28. 902 -35.374 11. 877 1, 00 34. 54

ANISOU 2230 C CYS B 99 5409 3929 3787 1166 766 -241

ATOM 2231 O CYS B 99 -27.685 -35.225 11. 754 1, 00 36. 42

ANISOU 2231 O CYS B 99 5612 4161 4064 1176 983 -203

ATOM 2232 CB CYS B 99 -30.127 -33.396 12.810 1, 00 26. 57

ANISOU 2232 CB CYS B 99 4341 2952 2801 1106 581 -36

ATOM 2233 SG CYS B 99 -31.501 -33.339 11.638 1, 00 43. 05

ANISOU 2233 SG CYS B 99 6629 5098 4628 1175 384 -84

ATOM 2234 N GLN B 100 -29. 645 -36.027 10.997 1, 00 33. 84

ANISOU 2234 N GLN B 100 5472 3854 3530 1207 656 -369

ATOM 2235 CA GLN B 100 -29. 096 -36.485 9.740 1, 00 36. 91

ANISOU 2235 CA GLN B 100 6048 4261 3714 1279 796 -473

ATOM 2236 C GLN B 100 -30.098 -36.094 8.668 1, 00 39. 77

ANISOU 2236 C GLN B 100 6634 4704 3772 1317 645 -501

ATOM 2237 O GLN B 100 -31.275 -36.414 8.778 1, 00 40. 06

ANISOU 2237 O GLN B 100 6663 4747 3813 1294 394 -569

ATOM 2238 CB GLN B 100 -28.891 -37.994 9.769 1, 00 42. 44

ANISOU 2238 CB GLN B 100 6719 4878 4528 1297 800 -657

ATOM 2239 CG GLN B 100 -28.176 -38.544 8.546 1, 00 55. 47

ANISOU 2239 CG GLN B 100 8556 6536 5986 1384 988 -793

ATOM 2240 CD GLN B 100 -27.760 -39.988 8.725 1, 00 63. 60

ANISOU 2240 CD GLN B 100 9529 7443 7193 1415 1036 -963

ATOM 2241 OE1 GLN B 100 -28.157 -40.646 9.689 1, 00 65. 36

ANISOU 2241 OE1 GLN B 100 9598 7573 7663 1364 896 -977

ATOM 2242 NE2 GLN B 100 -26.950 -40.489 7.800 1, 00 68. 55

ANISOU 2242 NE2 GLN B 100 10287 8061 7699 1506 1249 -1088

ATOM 2243 N ALA B 101 -29.629 -35.393 7.641 1, 00 43. 39

ANISOU 2243 N ALA B 101 7284 5230 3972 1374 797 -435

ATOM 2244 CA ALA B 101 -30.508 -34.843 6.614 1, 00 42. 31

ANISOU 2244 CA ALA B 101 7376 5186 3516 1425 651 -414 ATOM 2245 C ALA B 101 -29.872 -34.920 5.241 1.00 43.06 C

ANISOU 2245 C ALA B 101 7737 5349 3277 1505 841 -461 C

ATOM 2246 0 ALA B 101 -28.654 -34.985 5.119 1.00 44.11 0

ANISOU 2246 O ALA B 101 7857 5461 3442 1518 1139 -443 O ATOM 2247 CB ALA B 101 -30.857 -33.393 6.940 1.00 36.27 C

ANISOU 2247 CB ALA B 101 6585 4436 2759 1416 610 -187 C

ATOM 2248 N MET B 102 -30.713 -34.913 4.213 1.00 49.54 N

ANISOU 2248 N MET B 102 8791 6262 3771 1562 663 -521 N

ATOM 2249 CA MET B 102 -30.270 -34.765 2.831 1.00 56.42 C ANISOU 2249 CA MET B 102 9967 7229 4240 1649 821 -532 C

ATOM 2250 C MET B 102 -30.902 -33.522 2.219 1.00 60.34 C

ANISOU 2250 C MET B 102 10641 7817 4468 1698 709 -324 C

ATOM 2251 O MET B 102 -32.055 -33.204 2.508 1.00 59.19 O

ANISOU 2251 O MET B 102 10438 7688 4362 1694 400 -285 O ATOM 2252 CB MET B 102 -30.675 -35.982 2.008 1.00 62.67 C

ANISOU 2252 CB MET B 102 10934 8059 4819 1687 694 -819 C

ATOM 2253 CG MET B 102 -29.734 -37.167 2.138 1.00 67.57 C

ANISOU 2253 CG MET B 102 11493 8587 5592 1688 915 -1021 C

ATOM 2254 SD MET B 102 -30.371 -38.617 1.279 1.00138.04 S ANISOU 2254 SD MET B 102 20578 17513 14358 1691 711 -1374 S

ATOM 2255 CE MET B 102 -30.888 -37.879 -0.270 1.00 54.72 C

ANISOU 2255 CE MET B 102 10304 7157 3329 1723 598 -1299 C

ATOM 2256 N ASN B 103 -30.156 -32.818 1.375 1.00 67.10 N

ANISOU 2256 N ASN B 103 11706 8729 5062 1753 968 -177 N ATOM 2257 CA ASN B 103 -30.723 -31.684 0.649 1.00 73.20 C

ANISOU 2257 CA ASN B 103 12633 9568 5611 1791 854 39 C

ATOM 2258 C ASN B 103 -31.358 -32.117 -0.675 1.00 80.24 C

ANISOU 2258 C ASN B 103 13732 10588 6169 1833 659 -81 C

ATOM 2259 O ASN B 103 -31.434 -33.312 -0.969 1.00 80.37 O ANISOU 2259 O ASN B 103 13772 10631 6134 1823 594 -346 O

ATOM 2260 CB ASN B 103 -29.677 -30.586 0.432 1.00 75.08 C

ANISOU 2260 CB ASN B 103 12888 9765 5874 1764 1186 294 C

ATOM 2261 CG ASN B 103 -28.409 -31.102 -0.225 1.00 78.99 C

ANISOU 2261 CG ASN B 103 13410 10280 6324 1740 1522 218 C ATOM 2262 OD1 ASN B 103 -28.414 -32.125 -0.914 1.00 82.02 O

ANISOU 2262 OD1 ASN B 103 13881 10731 6550 1764 1494 0 O

ATOM 2263 ND2 ASN B 103 -27.309 -30.392 -0.011 1.00 79.04 N

ANISOU 2263 ND2 ASN B 103 13323 10220 6489 1684 1840 392 N

ATOM 2264 N ARG B 104 -31.812 -31.148 -1.468 1.00 86.41 N ANISOU 2264 N ARG B 104 14656 11438 6737 1875 565 112 N

ATOM 2265 CA ARG B 104 -32.439 -31.441 -2.757 1.00 93.36 C

ANISOU 2265 CA ARG B 104 15734 12459 7278 1914 370 23 C

ATOM 2266 C ARG B 104 -31.443 -32.106 -3.707 1.00 96.10 C

ANISOU 2266 C ARG B 104 16222 12862 7430 1903 644 -107 C ATOM 2267 O ARG B 104 -31.834 -32.811 -4.640 1.00 99.80 O

ANISOU 2267 O ARG B 104 16835 13440 7644 1917 504 -290 O

ATOM 2268 CB ARG B 104 -32.995 -30.165 -3.403 1.00 98.16 C

ANISOU 2268 CB ARG B 104 16462 13123 7714 1969 255 292 C

ATOM 2269 CG ARG B 104 -33.843 -29.278 -2.489 1.00 98.45 C ANISOU 2269 CG ARG B 104 16347 13084 7977 1993 45 465 C

ATOM 2270 CD ARG B 104 -35.099 -29.983 -1.986 1.00 98.94 C

ANISOU 2270 CD ARG B 104 16274 13181 8139 1999 -351 279 C

ATOM 2271 NE ARG B 104 -35.968 -29.081 -1.229 1.00 98.23 N

ANISOU 2271 NE ARG B 104 16030 13035 8257 2036 -551 451 N ATOM 2272 CZ ARG B 104 -37.003 -29.477 -0.492 1.00 98.26 C

ANISOU 2272 CZ ARG B 104 15844 13041 8449 2034 -854 340 C

ATOM 2273 NH1 ARG B 104 -37.300 -30.767 -0.395 1.00 97.93 N

ANISOU 2273 NH1 ARG B 104 15748 13042 8417 1984 -1002 55 N

ATOM 2274 NH2 ARG B 104 -37.737 -28.584 0.163 1.00 97.55 N ANISOU 2274 NH2 ARG B 104 15601 12898 8565 2076 -998 507

ATOM 2275 N ASN B 105 -30.156 -31.878 -3.455 1, 00 93. 13

ANISOU 2275 N ASN B 105 15783 12412 7189 1872 1033 -16

ATOM 2276 CA ASN B 105 -29.086 -32.405 -4.298 1, 00 92.

ANISOU 2276 CA ASN B 105 15833 12417 7004 1867 1339 -112

ATOM 2277 C ASN B 105 -28.664 -33.828 -3.940 1, 00 85. 79

ANISOU 2277 C ASN B 105 14839 11485 6273 1845 1409 -418

ATOM 2278 O ASN B 105 -27.911 -34.466 -4.679 1, 00 86. 95

ANISOU 2278 O ASN B 105 15060 11677 6302 1854 1622 -554

ATOM 2279 CB ASN B 105 -27.872 -31.474 -4.258 1, 00 94. 27

ANISOU 2279 CB ASN B 105 15971 12551 7295 1836 1726 133

ATOM 2280 CG ASN B 105 -28.115 -30.167 -4.987 1, 00 97. 45

ANISOU 2280 CG ASN B 105 16540 13002 7485 1858 1716 417

ATOM 2281 OD1 ASN B 105 -29.254 -29.816 -5.295 1, 00 98. 26

ANISOU 2281 OD1 ASN B 105 16753 13163 7420 1905 1397 468

ATOM 2282 ND2 ASN B 105 -27.041 -29.440 -5.270 1, 00 99. 51

ANISOU 2282 ND2 ASN B 105 16803 13234 7773 1823 2062 608

ATOM 2283 N GLY B 106 -29.145 -34.317 -2.802 1, 00 78.

ANISOU 2283 N GLY B 106 13778 10507 5666 1822 1236 -523

ATOM 2284 CA GLY B 106 -28.832 -35.664 -2.361 1, 00 76. 70

ANISOU 2284 CA GLY B 106 13392 10160 5589 1802 1275 502

ATOM 2285 C GLY B 106 -27.622 -35.747 -1.449 1, 00 74. 03

ANISOU 2285 C GLY B 106 12826 9707 5596 1777 1596 -753

ATOM 2286 O GLY B 106 -27.223 -36.833 -1.037 1, 00 71. 90

ANISOU 2286 O GLY B 106 12432 9356 5531 1770 1660 -956

ATOM 2287 N LYS B 107 -27.031 -34.599 -1.136 1, 00 75. 49

ANISOU 2287 N LYS B 107 12940 9875 5866 1758 1789 -482

ATOM 2288 CA LYS B 107 -25.889 -34. 561 -0.233 1, 00 76.

ANISOU 2288 CA LYS B 107 12863 9950 6389 1718 2070 -417

ATOM 2289 C LYS B 107 -26.339 -34. 763 1.213 1, 00 70. 53

ANISOU 2289 C LYS B 107 11856 9043 5897 1693 1910 -445

ATOM 2290 O LYS B 107 -27. 364 -34.233 1.639 1, 00 65. 71

ANISOU 2290 O LYS B 107 11282 8436 5250 1695 1661 -369

ATOM 2291 CB LYS B 107 -25. 127 -33.239 -0.364 1, 00 81. 47

ANISOU 2291 CB LYS B 107 13427 10540 6989 1679 2316 -126

ATOM 2292 CG LYS B 107 -23.802 -33.218 0.394 1, 00 81. 92

ANISOU 2292 CG LYS B 107 13207 10516 7404 1623 2616 -72

ATOM 2293 CD LYS B 107 -23.240 -31.809 0.534 1, 00 81. 67

ANISOU 2293 CD LYS B 107 13119 10454 7459 1551 2796 217

ATOM 2294 CE LYS B 107 -24.106 -30.950 1.447 1, 00 76. 65

ANISOU 2294 CE LYS B 107 12454 9753 6917 1522 2587 362

ATOM 2295 NZ LYS B 107 -23.452 -29.653 1.778 1, 00 74. 48

ANISOU 2295 NZ LYS B 107 12078 9405 6816 1429 2770 615

ATOM 2296 N GLU B 108 -25.559 -35.531 1.963 1, 00 69. 71

ANISOU 2296 N GLU B 108 11528 8851 6106 1677 2052 -547

ATOM 2297 CA GLU B 108 -25.901 -35.847 3.338 1, 00 66. 17

ANISOU 2297 CA GLU B 108 10877 8301 5965 1658 1919 -586

ATOM 2298 C GLU B 108 -25.096 -34.993 4.319 1, 00 63. 34

ANISOU 2298 C GLU B 108 10255 7892 5920 1581 2075 -372

ATOM 2299 O GLU B 108 -23.901 -34.774 4.128 1, 00 67. 05

ANISOU 2299 O GLU B 108 10646 8367 6464 1574 2379 -300

ATOM 2300 CB GLU B 108 -25.682 -37.331 3.602 1, 00 69. 10

ANISOU 2300 CB GLU B 108 11140 8586 6530 1677 1900 332

ATOM 2301 CG GLU B 108 -26.367 -37.837 4.854 1, 00 74.

ANISOU 2301 CG GLU B 108 11652 9208 7572 1616 1636 375

ATOM 2302 CD GLU B 108 -26.900 -39.243 4.678 1, 00 82. 48

ANISOU 2302 CD GLU B 108 12685 10101 8553 1642 1482 -1146

ATOM 2303 OE1 GLU B 108 -27. 365 -39. 562 3.559 1, 00 86. 36

ANISOU 2303 OE1 GLU B 108 13443 10651 8717 1691 1422 -1303 ATOM 2304 OE2 GLU B 108 -26.847 -40.027 5.650 1.00 82.90

ANISOU 2304 OE2 GLU B 108 12527 10031 8939 1609 1416 -1198

ATOM 2305 N THR B 109 -25.767 -34.513 5.363 1.00 55.72

ANISOU 2305 N THR B 109 9125 6881 5166 1501 1837 -276

ATOM 2306 CA THR B 109 -25.174 -33.593 6.324 1.00 39.63

ANISOU 2306 CA THR B 109 6862 4796 3402 1413 1926 -88

ATOM 2307 C THR B 109 -25.570 -34.012 7.732 1.00 40.32

ANISOU 2307 C THR B 109 6693 4810 3816 1350 1706 -128

ATOM 2308 O THR B 109 -26.741 -34.262 8.003 1.00 39.39

ANISOU 2308 O THR B 109 6601 4688 3677 1346 1428 -186

ATOM 2309 CB THR B 109 -25.664 -32.155 6.081 1.00 46.09

ANISOU 2309 CB THR B 109 7804 5634 4074 1384 1880 122

ATOM 2310 OG1 THR B 109 -25.463 -31.801 4.704 1.00 53.13

ANISOU 2310 OG1 THR B 109 8980 6603 4606 1453 2057 178

ATOM 2311 CG2 THR B 109 -24.926 -31.178 6.974 1.00 42.17

ANISOU 2311 CG2 THR B 109 7096 5070 3856 1282 2005 292

ATOM 2312 N LYS B 110 -24.591 -34.103 8.624 1.00 39.70

ANISOU 2312 N LYS B 110 6363 4684 4036 1302 1831 -94

ATOM 2313 CA LYS B 110 -24.832 -34.543 9.992 1.00 33.46

ANISOU 2313 CA LYS B 110 5340 3836 3535 1249 1646 -118

ATOM 2314 C LYS B 110 -24.616 -33.399 10.968 1.00 33.50

ANISOU 2314 C LYS B 110 5186 3827 3717 1149 1628 42

ATOM 2315 O LYS B 110 -23.727 -32.568 10.768 1.00 33.69

ANISOU 2315 O LYS B 110 5177 3855 3767 1109 1832 151

ATOM 2316 CB LYS B 110 -23.909 -35.702 10.354 1.00 34.11

ANISOU 2316 CB LYS B 110 5256 3875 3830 1288 1756 -220

ATOM 2317 CG LYS B 110 -24.144 -36.980 9.556 1.00 41.57

ANISOU 2317 CG LYS B 110 6347 4796 4654 1385 1758 -416

ATOM 2318 CD LYS B 110 -23.062 -38.008 9.860 1.00 48.53

ANISOU 2318 CD LYS B 110 7057 5613 5769 1447 1915 -494

ATOM 2319 CE LYS B 110 -23.357 -39.359 9.219 1.00 55.84

ANISOU 2319 CE LYS B 110 8124 6470 6622 1541 1898 -712

ATOM 2320 NZ LYS B 110 -24.589 -39.983 9.777 1.00 56.77

ANISOU 2320 NZ LYS B 110 8260 6520 6791 1497 1592 -782

ATOM 2321 N SER B 111 -25.445 -33.358 12.013 1.00 29.64

ANISOU 2321 N SER B 111 4602 3314 3346 1102 1393 47

ATOM 2322 CA SER B 111 -25.316 -32.383 13.085 1.00 31.79

ANISOU 2322 CA SER B 111 4727 3565 3788 1010 1350 159

ATOM 2323 C SER B 111 -25.214 -33.139 14.400 1.00 32.79

ANISOU 2323 C SER B 111 4638 3674 4147 979 1231 113

ATOM 2324 O SER B 111 -25.991 -34.048 14.654 1.00 38.41

ANISOU 2324 O SER B 111 5356 4375 4861 1010 1078 33

ATOM 2325 CB SER B 111 -26.526 -31.446 13.123 1.00 29.65

ANISOU 2325 CB SER B 111 4571 3289 3404 998 1186 221

ATOM 2326 OG SER B 111 -26.706 -30.780 11.885 1.00 36.48

ANISOU 2326 OG SER B 111 5658 4171 4031 1044 1268 285

ATOM 2327 N ASN B 112 -24.257 -32.759 15.235 1.00 29.87

ANISOU 2327 N ASN B 112 4078 3300 3972 912 1295 171

ATOM 2328 CA ASN B 112 -23.974 -33.494 16.460 1.00 29.52

ANISOU 2328 CA ASN B 112 3833 3253 4130 894 1191 149

ATOM 2329 C ASN B 112 -23.846 -32.528 17.630 1.00 29.49

ANISOU 2329 C ASN B 112 3705 3258 4241 791 1110 217

ATOM 2330 O ASN B 112 -22.952 -31.688 17.643 1.00 33.41

ANISOU 2330 O ASN B 112 4125 3754 4815 723 1225 270

ATOM 2331 CB ASN B 112 -22.684 -34.310 16.297 1.00 31.68

ANISOU 2331 CB ASN B 112 3965 3526 4544 942 1345 123

ATOM 2332 CG ASN B 112 -22.508 -35.358 17.387 1.00 37.33

ANISOU 2332 CG ASN B 112 4513 4230 5443 966 1219 104

ATOM 2333 OD1 ASN B 112 -23.481 -35.938 17.874 1.00 37.56 ANISOU 2333 OD1 ASN B 112 4590 4235 5447 977 1052 78 0

ATOM 2334 ND2 ASN B 112 -21.263 -35.604 17.776 1.00 40.38 N

ANISOU 2334 ND2 ASN B 112 4691 4630 6021 977 1301 132 N

ATOM 2335 N TYR B 113 -24.749 -32.638 18.600 1.00 27.85 N ANISOU 2335 N TYR B 113 3482 3056 4043 772 922 208 N

ATOM 2336 CA TYR B 113 -24.771 -31.720 19.732 1.00 28.35 C

ANISOU 2336 CA TYR B 113 3464 3131 4176 682 838 245 C

ATOM 2337 C TYR B 113 -24.615 -32.454 21.054 1.00 30.18 C

ANISOU 2337 C TYR B 113 3543 3401 4522 669 709 240 C ATOM 2338 O TYR B 113 -25.277 -33.471 21.294 1.00 29.49 O

ANISOU 2338 O TYR B 113 3470 3314 4419 721 622 221 O

ATOM 2339 CB TYR B 113 -26.089 -30.943 19.769 1.00 27.51 C

ANISOU 2339 CB TYR B 113 3496 3006 3950 678 745 248 C

ATOM 2340 CG TYR B 113 -26.365 -30.106 18.544 1.00 29.62 C ANISOU 2340 CG TYR B 113 3933 3233 4087 703 838 283 C

ATOM 2341 CD1 TYR B 113 -25.838 -28.829 18.418 1.00 23.24 C

ANISOU 2341 CD1 TYR B 113 3147 2375 3307 636 936 343 C

ATOM 2342 CD2 TYR B 113 -27.166 -30.592 17.518 1.00 25.33 C

ANISOU 2342 CD2 TYR B 113 3536 2697 3390 788 817 259 C ATOM 2343 CE1 TYR B 113 -26.094 -28.061 17.297 1.00 25.57 C

ANISOU 2343 CE1 TYR B 113 3616 2623 3475 666 1027 406 C

ATOM 2344 CE2 TYR B 113 -27.428 -29.835 16.401 1.00 27.78 C

ANISOU 2344 CE2 TYR B 113 4020 2986 3551 823 884 309 C

ATOM 2345 CZ TYR B 113 -26.894 -28.571 16.293 1.00 29.25 C ANISOU 2345 CZ TYR B 113 4235 3117 3760 768 995 396 C

ATOM 2346 OH TYR B 113 -27.172 -27.829 15.168 1.00 32.88 O

ANISOU 2346 OH TYR B 113 4887 3548 4060 813 1065 475 O

ATOM 2347 N ARG B 114 -23.746 -31.930 21.912 1.00 30.45 N

ANISOU 2347 N ARG B 114 3435 3466 4668 593 691 262 N ATOM 2348 CA ARG B 114 -23.633 -32.411 23.285 1.00 30.74 C

ANISOU 2348 CA ARG B 114 3349 3559 4772 574 544 272 C

ATOM 2349 C ARG B 114 -24.318 -31.359 24.167 1.00 29.39 C

ANISOU 2349 C ARG B 114 3231 3403 4532 498 450 254 C

ATOM 2350 O ARG B 114 -23.857 -30.226 24.271 1.00 32.64 O ANISOU 2350 O ARG B 114 3627 3797 4976 412 480 239 O

ATOM 2351 CB ARG B 114 -22.154 -32.626 23.658 1.00 31.78 C

ANISOU 2351 CB ARG B 114 3273 3732 5071 552 560 295 C

ATOM 2352 CG ARG B 114 -21.860 -33.034 25.114 1.00 33.10 C

ANISOU 2352 CG ARG B 114 3307 3976 5292 536 384 323 C ATOM 2353 CD ARG B 114 -22.474 -34.372 25.495 1.00 38.04 C

ANISOU 2353 CD ARG B 114 3963 4600 5891 631 304 361 C

ATOM 2354 NE ARG B 114 -22.184 -34.741 26.887 1.00 45.10 N

ANISOU 2354 NE ARG B 114 4754 5574 6807 623 140 417 N

ATOM 2355 CZ ARG B 114 -23.011 -34.539 27.918 1.00 43.19 C ANISOU 2355 CZ ARG B 114 4589 5384 6439 585 25 427 C

ATOM 2356 NH1 ARG B 114 -24.201 -33.972 27.734 1.00 35.46 N

ANISOU 2356 NH1 ARG B 114 3762 4376 5334 557 58 381 N

ATOM 2357 NH2 ARG B 114 -22.650 -34.910 29.141 1.00 42.75 N

ANISOU 2357 NH2 ARG B 114 4453 5415 6375 586 -120 489 N ATOM 2358 N VAL B 115 -25.447 -31.728 24.760 1.00 27.08 N

ANISOU 2358 N VAL B 115 3004 3129 4154 527 352 250 N

ATOM 2359 CA VAL B 115 -26.247 -30.794 25.544 1.00 24.78 C

ANISOU 2359 CA VAL B 115 2778 2851 3787 480 289 220 C

ATOM 2360 C VAL B 115 -26.034 -30.989 27.043 1.00 23.57 C ANISOU 2360 C VAL B 115 2543 2785 3628 441 170 221 C

ATOM 2361 O VAL B 115 -26.273 -32.072 27.577 1.00 23.93 O

ANISOU 2361 O VAL B 115 2556 2876 3661 484 109 269 O

ATOM 2362 CB VAL B 115 -27.757 -30.935 25.225 1.00 20.46 C

ANISOU 2362 CB VAL B 115 2348 2281 3143 540 277 212 C ATOM 2363 CGI VAL B 115 -28.590 -30.060 26.156 1.00 18.96 C

ANISOU 2363 CGI VAL B 115 2203 2111 2891 513 229 177 C

ATOM 2364 CG2 VAL B 115 -28.029 -30.591 23.758 1.00 19.17 C

ANISOU 2364 CG2 VAL B 115 2290 2048 2944 582 363 211 C ATOM 2365 N ARG B 116 -25.583 -29.931 27.708 1.00 23.19 N

ANISOU 2365 N ARG B 116 2476 2752 3583 355 137 170 N

ATOM 2366 CA ARG B 116 -25.419 -29.926 29.161 1.00 28.18 C

ANISOU 2366 CA ARG B 116 3064 3483 4162 312 9 150 C

ATOM 2367 C ARG B 116 -26.342 -28.860 29.725 1.00 29.27 C ANISOU 2367 C ARG B 116 3322 3605 4194 281 7 67 C

ATOM 2368 O ARG B 116 -26.416 -27.748 29.186 1.00 28.21 O

ANISOU 2368 O ARG B 116 3252 3374 4093 245 76 10 O

ATOM 2369 CB ARG B 116 -23.974 -29.609 29.546 1.00 33.07 C

ANISOU 2369 CB ARG B 116 3540 4142 4882 227 -54 130 C ATOM 2370 CG ARG B 116 -22.942 -30.452 28.810 1.00 41.06 C

ANISOU 2370 CG ARG B 116 4409 5152 6041 267 -12 201 C

ATOM 2371 CD ARG B 116 -21.515 -29.946 29.020 1.00 43.67 C

ANISOU 2371 CD ARG B 116 4563 5514 6515 172 -53 174 C

ATOM 2372 NE ARG B 116 -20.579 -30.581 28.089 1.00 45.41 N ANISOU 2372 NE ARG B 116 4642 5712 6897 219 47 232 N

ATOM 2373 CZ ARG B 116 -20.024 -31.774 28.285 1.00 47.47 C

ANISOU 2373 CZ ARG B 116 4773 6031 7232 309 -7 305 C

ATOM 2374 NH1 ARG B 116 -20.306 -32.463 29.382 1.00 48.61 N

ANISOU 2374 NH1 ARG B 116 4920 6258 7294 353 -170 350 N ATOM 2375 NH2 ARG B 116 -19.185 -32.277 27.391 1.00 47.60 N

ANISOU 2375 NH2 ARG B 116 4663 6017 7405 363 113 340 N

ATOM 2376 N VAL B 117 -27.057 -29.190 30.796 1.00 27.40 N

ANISOU 2376 N VAL B 117 3123 3453 3834 303 -56 65 N

ATOM 2377 CA VAL B 117 -28.022 -28.247 31.338 1.00 28.00 C ANISOU 2377 CA VAL B 117 3311 3517 3810 297 -31 -24 C

ATOM 2378 C VAL B 117 -27.546 -27.647 32.637 1.00 23.28 C

ANISOU 2378 C VAL B 117 2724 2998 3122 221 -124 -117 C

ATOM 2379 O VAL B 117 -26.681 -28.196 33.303 1.00 25.81 O

ANISOU 2379 O VAL B 117 2963 3420 3422 187 -236 -86 O ATOM 2380 CB VAL B 117 -29.414 -28.868 31.520 1.00 30.44 C

ANISOU 2380 CB VAL B 117 3670 3859 4036 380 10 22 C

ATOM 2381 CGI VAL B 117 -29.796 -29.645 30.264 1.00 29.00 C

ANISOU 2381 CGI VAL B 117 3467 3613 3940 443 62 101 C

ATOM 2382 CG2 VAL B 117 -29.448 -29.761 32.753 1.00 29.67 C ANISOU 2382 CG2 VAL B 117 3549 3897 3826 381 -59 79 C

ATOM 2383 N TYR B 118 -28.103 -26.500 32.993 1.00 24.24 N

ANISOU 2383 N TYR B 118 2950 3068 3190 201 -87 -240 N

ATOM 2384 CA TYR B 118 -27.639 -25.817 34.186 1.00 26.34 C

ANISOU 2384 CA TYR B 118 3253 3397 3360 118 -178 -370 C ATOM 2385 C TYR B 118 -28.728 -24.940 34.756 1.00 27.57 C

ANISOU 2385 C TYR B 118 3549 3519 3406 152 -105 -494 C

ATOM 2386 O TYR B 118 -29.716 -24.637 34.087 1.00 28.55 O

ANISOU 2386 O TYR B 118 3724 3545 3578 232 14 -482 O

ATOM 2387 CB TYR B 118 -26.395 -24.975 33.878 1.00 28.29 C ANISOU 2387 CB TYR B 118 3440 3559 3749 -5 -228 -448 C

ATOM 2388 CG TYR B 118 -26.689 -23.697 33.123 1.00 32.08 C

ANISOU 2388 CG TYR B 118 4007 3841 4341 -29 -114 -529 C

ATOM 2389 CD1 TYR B 118 -26.839 -22.489 33.796 1.00 33.71 C

ANISOU 2389 CD1 TYR B 118 4323 3972 4515 -90 -121 -705 C ATOM 2390 CD2 TYR B 118 -26.831 -23.701 31.741 1.00 34.49 C

ANISOU 2390 CD2 TYR B 118 4304 4026 4774 18 1 -427 C

ATOM 2391 CE1 TYR B 118 -27.116 -21.320 33.113 1.00 34.52 C

ANISOU 2391 CE1 TYR B 118 4515 3862 4738 -100 -13 -762 C

ATOM 2392 CE2 TYR B 118 -27.102 -22.534 31.046 1.00 35.57 C ANISOU 2392 CE2 TYR B 118 4536 3975 5004 8 102 -468 C

ATOM 2393 CZ TYR B 118 -27.243 -21.349 31.739 1.00 36.38 C

ANISOU 2393 CZ TYR B 118 4738 3984 5101 -49 96 -628 C

ATOM 2394 OH TYR B 118 -27.515 -20.189 31.054 1.00 38.00 O ANISOU 2394 OH TYR B 118 5046 3972 5419 -49 199 -653 O

ATOM 2395 N GLN B 119 -28.542 -24.537 36.002 1.00 26.53 N

ANISOU 2395 N GLN B 119 4013 3168 2898 375 88 272 N

ATOM 2396 CA GLN B 119 -29.395 -23.528 36.603 1.00 28.61 C

ANISOU 2396 CA GLN B 119 4359 3233 3277 484 -18 344 C ATOM 2397 C GLN B 119 -28.573 -22.678 37.561 1.00 28.60 C

ANISOU 2397 C GLN B 119 4398 3151 3318 387 90 356 C

ATOM 2398 O GLN B 119 -27.670 -23.172 38.245 1.00 27.66 O

ANISOU 2398 O GLN B 119 4139 3141 3229 309 234 272 O

ATOM 2399 CB GLN B 119 -30.593 -24.158 37.323 1.00 25.81 C ANISOU 2399 CB GLN B 119 3809 2880 3119 671 -95 258 C

ATOM 2400 CG GLN B 119 -31.604 -23.142 37.863 1.00 26.67 C

ANISOU 2400 CG GLN B 119 3954 2830 3351 823 -218 269 C

ATOM 2401 CD GLN B 119 -32.180 -22.252 36.772 1.00 31.75 C

ANISOU 2401 CD GLN B 119 4826 3335 3904 896 -418 373 C ATOM 2402 OE1 GLN B 119 -31.591 -21.228 36.400 1.00 31.52 O

ANISOU 2402 OE1 GLN B 119 5051 3160 3764 802 -444 494 O

ATOM 2403 NE2 GLN B 119 -33.335 -22.642 36.247 1.00 32.33 N

ANISOU 2403 NE2 GLN B 119 4823 3445 4015 1052 -579 331 N

ATOM 2404 N ILE B 120 -28.884 -21.392 37.592 1.00 29.72 N ANISOU 2404 N ILE B 120 4741 3086 3465 402 -5 450 N

ATOM 2405 CA ILE B 120 -28.157 -20.451 38.421 1.00 31.01 C

ANISOU 2405 CA ILE B 120 4978 3139 3667 299 73 458 C

ATOM 2406 C ILE B 120 -28.832 -20.331 39.782 1.00 29.54 C

ANISOU 2406 C ILE B 120 4636 2891 3696 475 52 350 C ATOM 2407 O ILE B 120 -30.012 -19.991 39.862 1.00 35.34 O

ANISOU 2407 O ILE B 120 5374 3518 4534 672 -100 329 O

ATOM 2408 CB ILE B 120 -28.117 -19.067 37.745 1.00 35.09 C

ANISOU 2408 CB ILE B 120 5840 3417 4077 207 -45 616 C

ATOM 2409 CGI ILE B 120 -27.485 -19.172 36.352 1.00 35.79 C ANISOU 2409 CGI ILE B 120 6100 3604 3895 -16 -12 734 C

ATOM 2410 CG2 ILE B 120 -27.378 -18.057 38.612 1.00 33.60 C

ANISOU 2410 CG2 ILE B 120 5741 3084 3941 82 23 611 C

ATOM 2411 CD1 ILE B 120 -27.379 -17.826 35.625 1.00 37.29 C

ANISOU 2411 CD1 ILE B 120 6694 3544 3931 -172 -138 937 C ATOM 2412 N PRO B 121 -28.089 -20.600 40.863 1.00 26.38 N

ANISOU 2412 N PRO B 121 4088 2583 3352 406 200 261 N

ATOM 2413 CA PRO B 121 -28.696 -20.444 42.190 1.00 25.87 C

ANISOU 2413 CA PRO B 121 3889 2493 3448 539 197 154 C

ATOM 2414 C PRO B 121 -28.972 -18.971 42.485 1.00 27.99 C ANISOU 2414 C PRO B 121 4331 2523 3780 592 101 155 C

ATOM 2415 O PRO B 121 -28.476 -18.087 41.784 1.00 30.12 O

ANISOU 2415 O PRO B 121 4851 2626 3966 478 51 264 O

ATOM 2416 CB PRO B 121 -27.608 -20.964 43.130 1.00 24.03 C

ANISOU 2416 CB PRO B 121 3520 2402 3210 417 356 86 C ATOM 2417 CG PRO B 121 -26.327 -20.654 42.407 1.00 25.51 C

ANISOU 2417 CG PRO B 121 3827 2602 3263 211 430 144 C

ATOM 2418 CD PRO B 121 -26.646 -20.893 40.946 1.00 28.69 C

ANISOU 2418 CD PRO B 121 4338 3009 3552 201 362 239 C

ATOM 2419 N GLY B 122 -29.772 -18.705 43.508 1.00 27.25 N ANISOU 2419 N GLY B 122 4116 2411 3828 754 68 24 N

ATOM 2420 CA GLY B 122 -29.954 -17.340 43.957 1.00 29.11 C

ANISOU 2420 CA GLY B 122 4494 2417 4150 828 -26 -31 C

ATOM 2421 C GLY B 122 -28.668 -16.883 44.622 1.00 36.40 C

ANISOU 2421 C GLY B 122 5478 3317 5035 625 105 -38 C ATOM 2422 O GLY B 122 -27.772 -17.691 44.875 1.00 35.17

ANISOU 2422 O GLY B 122 5201 3356 4804 473 261 -31

ATOM 2423 N LYS B 123 -28. 574 -15.589 44.894 1.00 39.54

ANISOU 2423 N LYS B 123 6064 3466 5496 632 19 -68

ATOM 2424 CA LYS B 123 -27. 410 -15.005 45.545 1.00 42.30

ANISOU 2424 CA LYS B 123 6478 3771 5822 430 123 -97

ATOM 2425 C LYS B 123 -27. 056 -15.789 46.807 1.00 40.33

ANISOU 2425 C LYS B 123 5946 3793 5584 414 289 -238

ATOM 2426 O LYS B 123 -27.937 -16.135 47.587 1.00 41.80

ANISOU 2426 O LYS B 123 5948 4091 5845 590 286 -368

ATOM 2427 CB LYS B 123 -27.709 -13.547 45.893 1.00 48.31

ANISOU 2427 CB LYS B 123 7450 4205 6700 512 -31 -169

ATOM 2428 CG LYS B 123 -26.483 -12.687 46.056 1.00 55.49

ANISOU 2428 CG LYS B 123 8553 4966 7566 241 21 -134

ATOM 2429 CD LYS B 123 -26. 851 -11.248 46.346 1.00 62.46

ANISOU 2429 CD LYS B 123 9683 5466 8583 336 -172 -209

ATOM 2430 CE LYS B 123 -25.600 -10.407 46.509 1.00 67.13

ANISOU 2430 CE LYS B 123 10475 5905 9128 16 -116 -173

ATOM 2431 NZ LYS B 123 -24. 646 -11.062 47.446 1.00 66.46

ANISOU 2431 NZ LYS B 123 10110 6150 8993 -138 120 -290

ATOM 2432 N PRO B 124 -25.764 -16.094 47.002 1.00 36.72

ANISOU 2432 N PRO B 124 5449 3464 5039 193 426 -219

ATOM 2433 CA PRO B 124 -25.366 -16.835 48.204 1.00 33.34

ANISOU 2433 CA PRO B 124 4788 3274 4606 184 540 -336

ATOM 2434 C PRO B 124 -25.493 -15.954 49.447 1.00 36.69

ANISOU 2434 C PRO B 124 5204 3629 5107 232 531 -502

ATOM 2435 O PRO B 124 -25. 411 -14.731 49.341 1.00 39.53

ANISOU 2435 O PRO B 124 5755 3743 5522 204 457 -526

ATOM 2436 CB PRO B 124 -23. 901 -17.182 47.929 1.00 30.17

ANISOU 2436 CB PRO B 124 4364 2995 4103 -45 644 -297

ATOM 2437 CG PRO B 124 -23.425 -16.091 47.013 1.00 31.35

ANISOU 2437 CG PRO B 124 4761 2936 4214 -218 616 -207

ATOM 2438 CD PRO B 124 -24.609 -15.736 46.159 1.00 36.10

ANISOU 2438 CD PRO B 124 5532 3335 4850 -67 473 -106

ATOM 2439 N GLU B 125 -25.713 -16.566 50.603 1.00 32.92

ANISOU 2439 N GLU B 125 4529 3358 4622 293 593 -616

ATOM 2440 CA GLU B 125 -25.909 -15.809 51.828 1.00 37.29

ANISOU 2440 CA GLU B 125 5049 3900 5221 345 596 -805

ATOM 2441 C GLU B 125 -25.090 -16.400 52.959 1.00 38.32

ANISOU 2441 C GLU B 125 5038 4265 5257 237 693 -870

ATOM 2442 O GLU B 125 -24.903 -17.616 53.042 1.00 35.87

ANISOU 2442 O GLU B 125 4611 4150 4867 208 735 -792

ATOM 2443 CB GLU B 125 -27.383 -15.823 52.243 1.00 42.86

ANISOU 2443 CB GLU B 125 5642 4654 5989 563 557 -928

ATOM 2444 CG GLU B 125 -28.341 -15.224 51.236 1.00 51.47

ANISOU 2444 CG GLU B 125 6847 5520 7189 731 413 -904

ATOM 2445 CD GLU B 125 -29.790 -15.327 51.687 1.00 59.70

ANISOU 2445 CD GLU B 125 7705 6679 8297 953 382 -1079

ATOM 2446 OE1 GLU B 125 -30.093 -14.922 52.832 1.00 61.48

ANISOU 2446 OE1 GLU B 125 7815 7005 8541 1013 424 -1304

ATOM 2447 OE2 GLU B 125 -30.625 -15.820 50.898 1.00 62.95

ANISOU 2447 OE2 GLU B 125 8069 7114 8735 1057 322 -1014

ATOM 2448 N ILE B 126 -24.617 -15.532 53.842 1.00 41.65

ANISOU 2448 N ILE B 126 5486 4649 5690 185 701 -1019

ATOM 2449 CA ILE B 126 -23.949 -15.972 55.050 1.00 41.17

ANISOU 2449 CA ILE B 126 5299 4815 5529 105 763 -1107

ATOM 2450 C ILE B 126 -24.932 -15.952 56.205 1.00 42.22

ANISOU 2450 C ILE B 126 5323 5089 5630 221 787 -1271

ATOM 2451 O ILE B 126 -25. 575 -14.939 56.463 1.00 46.58 ANISOU 2451 0 ILE B 126 5911 5520 6267 324 754 -1438 0

ATOM 2452 CB ILE B 126 -22.737 -15.087 55.366 1.00 44.56 C

ANISOU 2452 CB ILE B 126 5801 5166 5966 -55 764 -1195 C

ATOM 2453 CGI ILE B 126 -21.614 -15.389 54.375 1.00 43.75 C ANISOU 2453 CGI ILE B 126 5731 5052 5842 -221 783 -1057 C

ATOM 2454 CG2 ILE B 126 -22.257 -15.315 56.795 1.00 45.99 C

ANISOU 2454 CG2 ILE B 126 5859 5572 6045 -96 795 -1336 C

ATOM 2455 CD1 ILE B 126 -20.393 -14.525 54.549 1.00 48.50 C

ANISOU 2455 CD1 ILE B 126 6384 5598 6448 -428 797 -1146 C ATOM 2456 N VAL B 127 -25.066 -17.090 56.878 1.00 43.40 N

ANISOU 2456 N VAL B 127 5345 5498 5649 197 835 -1230 N

ATOM 2457 CA VAL B 127 -25.905 -17.192 58.068 1.00 44.90 C

ANISOU 2457 CA VAL B 127 5420 5897 5743 238 889 -1380 C

ATOM 2458 C VAL B 127 -25.047 -17.568 59.283 1.00 47.40 C ANISOU 2458 C VAL B 127 5703 6419 5889 110 911 -1416 C

ATOM 2459 O VAL B 127 -23.910 -18.025 59.135 1.00 50.57 O

ANISOU 2459 O VAL B 127 6138 6819 6259 21 868 -1305 O

ATOM 2460 CB VAL B 127 -27.038 -18.221 57.859 1.00 44.50 C

ANISOU 2460 CB VAL B 127 5271 5989 5649 282 922 -1290 C ATOM 2461 CGI VAL B 127 -27.710 -17.997 56.503 1.00 43.41 C

ANISOU 2461 CGI VAL B 127 5173 5649 5673 407 867 -1224 C

ATOM 2462 CG2 VAL B 127 -26.499 -19.635 57.925 1.00 41.73 C

ANISOU 2462 CG2 VAL B 127 4919 5765 5173 164 915 -1085 C

ATOM 2463 N ASP B 128 -25.589 -17.358 60.477 1.00 50.26 N ANISOU 2463 N ASP B 128 5988 6977 6133 107 967 -1592 N

ATOM 2464 CA ASP B 128 -24.906 -17.682 61.732 1.00 54.14 C

ANISOU 2464 CA ASP B 128 6463 7688 6421 -14 973 -1633 C

ATOM 2465 C ASP B 128 -23.454 -17.217 61.787 1.00 53.29 C

ANISOU 2465 C ASP B 128 6420 7483 6346 -82 901 -1655 C ATOM 2466 O ASP B 128 -22.563 -17.993 62.137 1.00 59.22 O

ANISOU 2466 O ASP B 128 7174 8343 6982 -164 842 -1551 O

ATOM 2467 CB ASP B 128 -24.975 -19.186 62.015 1.00 57.16 C

ANISOU 2467 CB ASP B 128 6837 8255 6625 -107 962 -1419 C

ATOM 2468 CG ASP B 128 -26.400 -19.692 62.136 1.00 64.26 C ANISOU 2468 CG ASP B 128 7655 9309 7453 -109 1053 -1413 C

ATOM 2469 OD1 ASP B 128 -27.213 -19.035 62.825 1.00 66.12 O

ANISOU 2469 OD1 ASP B 128 7794 9694 7633 -88 1147 -1642 O

ATOM 2470 OD2 ASP B 128 -26.709 -20.742 61.530 1.00 67.45 O

ANISOU 2470 OD2 ASP B 128 8076 9695 7859 -136 1031 -1207 O ATOM 2471 N SER B 129 -23.214 -15.957 61.442 1.00 45.28 N

ANISOU 2471 N SER B 129 5459 6257 5490 -52 890 -1800 N

ATOM 2472 CA SER B 129 -21.859 -15.419 61.460 1.00 42.03 C

ANISOU 2472 CA SER B 129 5093 5761 5114 -159 837 -1846 C

ATOM 2473 C SER B 129 -21.473 -14.913 62.844 1.00 44.54 C ANISOU 2473 C SER B 129 5377 6240 5305 -217 833 -2070 C

ATOM 2474 O SER B 129 -22.298 -14.348 63.564 1.00 46.41 O

ANISOU 2474 O SER B 129 5589 6539 5504 -152 877 -2268 O

ATOM 2475 CB SER B 129 -21.707 -14.300 60.432 1.00 39.44 C

ANISOU 2475 CB SER B 129 4882 5107 4996 -161 816 -1872 C ATOM 2476 OG SER B 129 -22.579 -13.228 60.730 1.00 41.73 O

ANISOU 2476 OG SER B 129 5217 5264 5372 -53 813 -2076 O

ATOM 2477 N ALA B 130 -20.215 -15.126 63.213 1.00 43.46 N

ANISOU 2477 N ALA B 130 5220 6195 5098 -330 772 -2066 N

ATOM 2478 CA ALA B 130 -19.713 -14.647 64.491 1.00 45.56 C ANISOU 2478 CA ALA B 130 5456 6621 5233 -397 745 -2281 C

ATOM 2479 C ALA B 130 -19.422 -13.157 64.405 1.00 47.06 C

ANISOU 2479 C ALA B 130 5707 6587 5585 -438 743 -2506 C

ATOM 2480 O ALA B 130 -19.018 -12.656 63.358 1.00 49.87 O

ANISOU 2480 O ALA B 130 6135 6691 6124 -490 732 -2444 O ATOM 2481 CB ALA B 130 -18.463 -15.410 64.893 1.00 45.28 C

ANISOU 2481 CB ALA B 130 5366 6761 5076 -483 643 -2213 C

ATOM 2482 N SER B 131 -19.640 -12.443 65.501 1.00 45.44 N

ANISOU 2482 N SER B 131 5492 6473 5302 -432 748 -2770 N ATOM 2483 CA SER B 131 -19.302 -11.029 65.541 1.00 46.03 C

ANISOU 2483 CA SER B 131 5645 6314 5531 -480 717 -3009 C

ATOM 2484 C SER B 131 -17.990 -10.791 66.297 1.00 43.75 C

ANISOU 2484 C SER B 131 5313 6153 5157 -646 652 -3145 C

ATOM 2485 O SER B 131 -17.373 -9.733 66.164 1.00 45.99 O ANISOU 2485 O SER B 131 5666 6229 5581 -759 613 -3298 O

ATOM 2486 CB SER B 131 -20.446 -10.230 66.157 1.00 44.37 C

ANISOU 2486 CB SER B 131 5444 6075 5337 -335 748 -3280 C

ATOM 2487 OG SER B 131 -20.941 -10.893 67.299 1.00 46.84 O

ANISOU 2487 OG SER B 131 5639 6770 5389 -303 805 -3350 O ATOM 2488 N GLU B 132 -17.574 -11.774 67.093 1.00 45.83 N

ANISOU 2488 N GLU B 132 5475 6749 5188 -671 620 -3089 N

ATOM 2489 CA GLU B 132 -16.271 -11.724 67.758 1.00 49.95 C

ANISOU 2489 CA GLU B 132 5930 7428 5621 -807 524 -3200 C

ATOM 2490 C GLU B 132 -15.462 -12.995 67.541 1.00 52.81 C ANISOU 2490 C GLU B 132 6205 7967 5893 -822 443 -2976 C

ATOM 2491 O GLU B 132 -15.979 -14.105 67.676 1.00 54.48 O

ANISOU 2491 O GLU B 132 6417 8320 5962 -730 433 -2783 O

ATOM 2492 CB GLU B 132 -16.409 -11.479 69.258 1.00 52.48 C

ANISOU 2492 CB GLU B 132 6224 8002 5713 -807 499 -3446 C ATOM 2493 CG GLU B 132 -16.694 -10.039 69.640 1.00 54.85 C

ANISOU 2493 CG GLU B 132 6577 8118 6147 -802 515 -3689 C

ATOM 2494 CD GLU B 132 -18.162 -9.723 69.570 1.00 53.80 C

ANISOU 2494 CD GLU B 132 6485 7888 6068 -635 605 -3713 C

ATOM 2495 OE1 GLU B 132 -18.958 -10.666 69.396 1.00 50.31 O ANISOU 2495 OE1 GLU B 132 6012 7584 5518 -554 673 -3557 O

ATOM 2496 OE2 GLU B 132 -18.521 -8.539 69.687 1.00 57.92 O

ANISOU 2496 OE2 GLU B 132 7064 8198 6743 -581 592 -3893 O

ATOM 2497 N LEU B 133 -14.190 -12.817 67.196 1.00 52.52 N

ANISOU 2497 N LEU B 133 6091 7918 5948 -945 376 -3021 N ATOM 2498 CA LEU B 133 -13.245 -13.923 67.135 1.00 49.57 C

ANISOU 2498 CA LEU B 133 5594 7740 5502 -934 256 -2902 C

ATOM 2499 C LEU B 133 -12.171 -13.734 68.198 1.00 53.49 C

ANISOU 2499 C LEU B 133 5985 8463 5874 -1013 116 -3121 C

ATOM 2500 O LEU B 133 -11.856 -12.605 68.590 1.00 52.65 O ANISOU 2500 O LEU B 133 5879 8310 5815 -1140 135 -3366 O

ATOM 2501 CB LEU B 133 -12.591 -14.001 65.759 1.00 47.89 C

ANISOU 2501 CB LEU B 133 5313 7392 5489 -1003 293 -2805 C

ATOM 2502 CG LEU B 133 -13.515 -14.119 64.549 1.00 46.11 C

ANISOU 2502 CG LEU B 133 5193 6933 5393 -944 415 -2595 C ATOM 2503 CD1 LEU B 133 -12.697 -14.473 63.328 1.00 44.34 C

ANISOU 2503 CD1 LEU B 133 4872 6684 5291 -1017 431 -2505 C

ATOM 2504 CD2 LEU B 133 -14.609 -15.142 64.794 1.00 38.60 C

ANISOU 2504 CD2 LEU B 133 4301 6045 4318 -762 411 -2406 C

ATOM 2505 N THR B 134 -11.613 -14.842 68.670 1.00 53.54 N ANISOU 2505 N THR B 134 5915 8701 5727 -930 -52 -3038 N

ATOM 2506 CA THR B 134 -10.487 -14.776 69.583 1.00 53.76 C

ANISOU 2506 CA THR B 134 5822 8961 5643 -981 -230 -3239 C

ATOM 2507 C THR B 134 -9.250 -15.309 68.873 1.00 53.69 C

ANISOU 2507 C THR B 134 5611 9024 5764 -979 -342 -3244 C ATOM 2508 O THR B 134 -9.252 -16.431 68.360 1.00 49.94 O

ANISOU 2508 O THR B 134 5117 8560 5297 -836 -416 -3045 O

ATOM 2509 CB THR B 134 -10.747 -15.581 70.864 1.00 54.24 C

ANISOU 2509 CB THR B 134 5963 9258 5387 -880 -392 -3176 C

ATOM 2510 OG1 THR B 134 -12.066 -15.298 71.344 1.00 55.08 O ANISOU 2510 OG1 THR B 134 6232 9334 5362 -877 -246 -3145 0

ATOM 2511 CG2 THR B 134 -9.726 -15.226 71.938 1.00 52.37 C

ANISOU 2511 CG2 THR B 134 5632 9241 5026 -937 -568 -3412 C

ATOM 2512 N ALA B 135 -8.204 -14.489 68.831 1.00 56.47 N ANISOU 2512 N ALA B 135 5802 9431 6222 -1147 -351 -3498 N

ATOM 2513 CA ALA B 135 -6.963 -14.857 68.160 1.00 58.59 C

ANISOU 2513 CA ALA B 135 5818 9826 6617 -1179 -431 -3580 C

ATOM 2514 C ALA B 135 -6.286 -16.010 68.888 1.00 60.28 C

ANISOU 2514 C ALA B 135 5925 10284 6695 -964 -714 -3554 C ATOM 2515 O ALA B 135 -6.279 -16.050 70.121 1.00 58.42 O

ANISOU 2515 O ALA B 135 5765 10157 6274 -902 -854 -3573 O

ATOM 2516 CB ALA B 135 -6.025 -13.657 68.078 1.00 59.14 C

ANISOU 2516 CB ALA B 135 5763 9873 6832 -1407 -335 -3770 C

ATOM 2517 N GLY B 136 -5.731 -16.950 68.122 1.00 59.09 N ANISOU 2517 N GLY B 136 5613 10202 6636 -842 -808 -3509 N

ATOM 2518 CA GLY B 136 -4.973 -18.051 68.691 1.00 60.67 C

ANISOU 2518 CA GLY B 136 5715 10576 6759 -602 -1110 -3491 C

ATOM 2519 C GLY B 136 -5.769 -19.318 68.953 1.00 61.10 C

ANISOU 2519 C GLY B 136 5970 10597 6648 -380 -1304 -3251 C ATOM 2520 O GLY B 136 -5.200 -20.348 69.320 1.00 63.13 O

ANISOU 2520 O GLY B 136 6196 10932 6857 -158 -1593 -3198 O

ATOM 2521 N VAL B 137 -7.086 -19.248 68.772 1.00 57.70 N

ANISOU 2521 N VAL B 137 5794 9958 6170 -416 -1103 -3010 N

ATOM 2522 CA VAL B 137 -7.950 -20.410 68.968 1.00 57.42 C ANISOU 2522 CA VAL B 137 5993 9829 5995 -249 -1211 -2701 C

ATOM 2523 C VAL B 137 -8.903 -20.569 67.782 1.00 58.79 C

ANISOU 2523 C VAL B 137 6252 9771 6315 -255 -972 -2498 C

ATOM 2524 O VAL B 137 -9.127 -19.616 67.035 1.00 59.55 O

ANISOU 2524 O VAL B 137 6298 9764 6564 -403 -711 -2571 O ATOM 2525 CB VAL B 137 -8.759 -20.301 70.278 1.00 58.96 C

ANISOU 2525 CB VAL B 137 6434 10080 5890 -301 -1239 -2608 C

ATOM 2526 CGI VAL B 137 -7.830 -20.306 71.488 1.00 60.18 C

ANISOU 2526 CGI VAL B 137 6536 10474 5856 -275 -1525 -2779 C

ATOM 2527 CG2 VAL B 137 -9.633 -19.056 70.266 1.00 59.28 C ANISOU 2527 CG2 VAL B 137 6538 10037 5948 -487 -918 -2682 C

ATOM 2528 N PRO B 138 -9.454 -21.780 67.585 1.00 57.23 N

ANISOU 2528 N PRO B 138 6200 9474 6071 -101 -1081 -2241 N

ATOM 2529 CA PRO B 138 -10.368 -21.919 66.446 1.00 53.63 C

ANISOU 2529 CA PRO B 138 5812 8813 5753 -111 -861 -2068 C ATOM 2530 C PRO B 138 -11.669 -21.175 66.706 1.00 52.09 C

ANISOU 2530 C PRO B 138 5791 8530 5472 -247 -614 -1983 C

ATOM 2531 O PRO B 138 -12.166 -21.200 67.833 1.00 57.61 O

ANISOU 2531 O PRO B 138 6634 9317 5940 -282 -661 -1938 O

ATOM 2532 CB PRO B 138 -10.627 -23.429 66.379 1.00 52.85 C ANISOU 2532 CB PRO B 138 5846 8633 5600 75 -1079 -1832 C

ATOM 2533 CG PRO B 138 -9.491 -24.053 67.133 1.00 56.81 C

ANISOU 2533 CG PRO B 138 6279 9281 6025 221 -1440 -1933 C

ATOM 2534 CD PRO B 138 -9.166 -23.076 68.222 1.00 57.44 C

ANISOU 2534 CD PRO B 138 6329 9542 5953 87 -1432 -2110 C ATOM 2535 N ASN B 139 -12.191 -20.503 65.687 1.00 43.07 N

ANISOU 2535 N ASN B 139 4628 7233 4503 -322 -366 -1981 N

ATOM 2536 CA ASN B 139 -13.476 -19.830 65.790 1.00 42.43 C

ANISOU 2536 CA ASN B 139 4686 7050 4384 -400 -156 -1927 C

ATOM 2537 C ASN B 139 -14.353 -20.216 64.615 1.00 41.86 C ANISOU 2537 C ASN B 139 4670 6793 4441 -352 -28 -1739 C

ATOM 2538 O ASN B 139 -13.889 -20.238 63.475 1.00 40.30 O

ANISOU 2538 O ASN B 139 4380 6510 4422 -342 10 -1742 O

ATOM 2539 CB ASN B 139 -13.309 -18.312 65.766 1.00 38.73 C

ANISOU 2539 CB ASN B 139 4167 6536 4014 -541 -2 -2153 C ATOM 2540 CG ASN B 139 -12.437 -17.794 66.881 1.00 47.49 C

ANISOU 2540 CG ASN B 139 5206 7827 5011 -610 -116 -2378 C

ATOM 2541 OD1 ASN B 139 -12.934 -17.312 67.900 1.00 49.94 O

ANISOU 2541 OD1 ASN B 139 5599 8212 5163 -651 -93 -2465 O ATOM 2542 ND2 ASN B 139 -11.125 -17.870 66.688 1.00 47.01 N

ANISOU 2542 ND2 ASN B 139 4970 7866 5028 -628 -237 -2506 N

ATOM 2543 N LYS B 140 -15.618 -20.512 64.887 1.00 42.07 N

ANISOU 2543 N LYS B 140 4835 6787 4364 -340 45 -1594 N

ATOM 2544 CA LYS B 140 -16.584 -20.672 63.818 1.00 43.80 C ANISOU 2544 CA LYS B 140 5097 6838 4707 -307 181 -1453 C

ATOM 2545 C LYS B 140 -16.864 -19.274 63.261 1.00 44.54 C

ANISOU 2545 C LYS B 140 5170 6798 4954 -371 359 -1593 C

ATOM 2546 O LYS B 140 -17.357 -18.404 63.976 1.00 47.56 O

ANISOU 2546 O LYS B 140 5587 7203 5279 -416 434 -1727 O ATOM 2547 CB LYS B 140 -17.862 -21.331 64.342 1.00 48.00 C

ANISOU 2547 CB LYS B 140 5751 7410 5075 -305 212 -1294 C

ATOM 2548 CG LYS B 140 -18.813 -21.836 63.242 1.00 54.31 C

ANISOU 2548 CG LYS B 140 6583 8061 5993 -257 299 -1128 C

ATOM 2549 CD LYS B 140 -20.051 -22.506 63.852 1.00 59.50 C ANISOU 2549 CD LYS B 140 7336 8802 6470 -303 337 -992 C

ATOM 2550 CE LYS B 140 -21.120 -22.822 62.805 1.00 62.27 C

ANISOU 2550 CE LYS B 140 7690 9026 6945 -269 440 -875 C

ATOM 2551 NZ LYS B 140 -21.622 -21.603 62.098 1.00 62.91 N

ANISOU 2551 NZ LYS B 140 7703 8999 7200 -230 597 -1016 N ATOM 2552 N VAL B 141 -16.515 -19.045 61.999 1.00 42.44 N

ANISOU 2552 N VAL B 141 4863 6390 4873 -381 412 -1574 N

ATOM 2553 CA VAL B 141 -16.698 -17.727 61.399 1.00 39.81 C

ANISOU 2553 CA VAL B 141 4565 5882 4679 -463 540 -1672 C

ATOM 2554 C VAL B 141 -18.116 -17.559 60.872 1.00 40.22 C ANISOU 2554 C VAL B 141 4717 5778 4786 -389 638 -1573 C

ATOM 2555 O VAL B 141 -18.769 -16.548 61.128 1.00 41.72 O

ANISOU 2555 O VAL B 141 4970 5869 5013 -391 700 -1687 O

ATOM 2556 CB VAL B 141 -15.710 -17.478 60.257 1.00 36.86 C

ANISOU 2556 CB VAL B 141 4125 5439 4440 -557 563 -1687 C ATOM 2557 CGI VAL B 141 -15.957 -16.117 59.628 1.00 37.57 C

ANISOU 2557 CGI VAL B 141 4321 5303 4652 -674 670 -1743 C

ATOM 2558 CG2 VAL B 141 -14.303 -17.566 60.771 1.00 38.93 C

ANISOU 2558 CG2 VAL B 141 4237 5889 4665 -629 468 -1839 C

ATOM 2559 N GLY B 142 -18.594 -18.560 60.141 1.00 35.03 N ANISOU 2559 N GLY B 142 4066 5101 4143 -310 631 -1387 N

ATOM 2560 CA GLY B 142 -19.932 -18.497 59.600 1.00 30.63 C

ANISOU 2560 CA GLY B 142 3575 4426 3640 -234 705 -1303 C

ATOM 2561 C GLY B 142 -20.280 -19.622 58.651 1.00 27.98 C

ANISOU 2561 C GLY B 142 3236 4061 3332 -168 686 -1108 C ATOM 2562 O GLY B 142 -19.477 -20.513 58.379 1.00 27.77 O

ANISOU 2562 O GLY B 142 3163 4095 3292 -164 608 -1041 O

ATOM 2563 N THR B 143 -21.505 -19.572 58.149 1.00 26.78 N

ANISOU 2563 N THR B 143 3125 3820 3230 -101 742 -1047 N

ATOM 2564 CA THR B 143 -22.020 -20.598 57.272 1.00 29.69 C ANISOU 2564 CA THR B 143 3495 4159 3625 -43 724 -879 C

ATOM 2565 C THR B 143 -22.528 -19.928 56.010 1.00 31.11 C

ANISOU 2565 C THR B 143 3729 4150 3941 -4 766 -853 C

ATOM 2566 O THR B 143 -23.322 -18.993 56.075 1.00 33.33 O

ANISOU 2566 O THR B 143 4048 4340 4276 40 801 -934 O ATOM 2567 CB THR B 143 -23.168 -21.365 57.940 1.00 35.12 C

ANISOU 2567 CB THR B 143 4173 4962 4211 -19 735 -820 C

ATOM 2568 OG1 THR B 143 -22.692 -21.993 59.137 1.00 40.79 O

ANISOU 2568 OG1 THR B 143 4891 5845 4764 -81 674 -812 O

ATOM 2569 CG2 THR B 143 -23.709 -22.421 57.002 1.00 32.77 C ANISOU 2569 CG2 THR B 143 3882 4614 3954 23 707 -657 C

ATOM 2570 N CYS B 144 -22.036 -20.389 54.866 1.00 29.21 N

ANISOU 2570 N CYS B 144 3495 3854 3748 -14 746 -755 N

ATOM 2571 CA CYS B 144 -22.478 -19.883 53.585 1.00 31.21 C ANISOU 2571 CA CYS B 144 3828 3941 4089 5 767 -696 C

ATOM 2572 C CYS B 144 -23.475 -20.869 52.986 1.00 31.97 C

ANISOU 2572 C CYS B 144 3908 4047 4194 101 744 -579 C

ATOM 2573 O CYS B 144 -23.250 -22.076 53.017 1.00 28.57 O

ANISOU 2573 O CYS B 144 3421 3713 3719 111 705 -515 O ATOM 2574 CB CYS B 144 -21.284 -19.717 52.651 1.00 31.62 C

ANISOU 2574 CB CYS B 144 3894 3968 4153 -107 781 -681 C

ATOM 2575 SG CYS B 144 -21.658 -18.864 51.105 1.00 40.37 S

ANISOU 2575 SG CYS B 144 5164 4863 5313 -150 798 -590 S

ATOM 2576 N VAL B 145 -24.579 -20.348 52.458 1.00 32.99 N ANISOU 2576 N VAL B 145 4087 4061 4385 180 744 -566 N

ATOM 2577 CA VAL B 145 -25.605 -21.175 51.832 1.00 31.96 C

ANISOU 2577 CA VAL B 145 3927 3945 4271 262 717 -479 C

ATOM 2578 C VAL B 145 -25.924 -20.693 50.413 1.00 31.92 C

ANISOU 2578 C VAL B 145 4021 3778 4328 305 680 -413 C ATOM 2579 O VAL B 145 -26.057 -19.494 50.164 1.00 35.90 O

ANISOU 2579 O VAL B 145 4633 4125 4884 324 657 -449 O

ATOM 2580 CB VAL B 145 -26.914 -21.173 52.655 1.00 31.78 C

ANISOU 2580 CB VAL B 145 3824 4006 4246 333 737 -553 C

ATOM 2581 CGI VAL B 145 -27.913 -22.168 52.069 1.00 28.38 C ANISOU 2581 CGI VAL B 145 3335 3622 3825 377 713 -471 C

ATOM 2582 CG2 VAL B 145 -26.633 -21.499 54.107 1.00 30.73 C

ANISOU 2582 CG2 VAL B 145 3628 4043 4005 258 778 -613 C

ATOM 2583 N SER B 146 -26.045 -21.641 49.493 1.00 27.47 N

ANISOU 2583 N SER B 146 3442 3242 3752 319 653 -316 N ATOM 2584 CA SER B 146 -26.430 -21.370 48.121 1.00 27.81 C

ANISOU 2584 CA SER B 146 3581 3169 3816 355 605 -242 C

ATOM 2585 C SER B 146 -27.562 -22.320 47.712 1.00 27.43 C

ANISOU 2585 C SER B 146 3459 3176 3789 450 556 -203 C

ATOM 2586 O SER B 146 -27.427 -23.539 47.851 1.00 27.28 O ANISOU 2586 O SER B 146 3359 3265 3743 424 561 -177 O

ATOM 2587 CB SER B 146 -25.220 -21.566 47.205 1.00 27.55 C

ANISOU 2587 CB SER B 146 3599 3153 3718 237 632 -190 C

ATOM 2588 OG SER B 146 -25.606 -21.525 45.850 1.00 29.20 O

ANISOU 2588 OG SER B 146 3903 3291 3900 252 586 -105 O ATOM 2589 N GLU B 147 -28.674 -21.769 47.226 1.00 28.58 N

ANISOU 2589 N GLU B 147 3635 3236 3991 563 488 -212 N

ATOM 2590 CA GLU B 147 -29.835 -22.584 46.855 1.00 30.26 C

ANISOU 2590 CA GLU B 147 3747 3519 4230 644 438 -205 C

ATOM 2591 C GLU B 147 -30.188 -22.500 45.379 1.00 27.13 C ANISOU 2591 C GLU B 147 3448 3031 3831 703 339 -130 C

ATOM 2592 O GLU B 147 -30.343 -21.410 44.831 1.00 27.79 O

ANISOU 2592 O GLU B 147 3670 2958 3930 765 260 -114 O

ATOM 2593 CB GLU B 147 -31.069 -22.169 47.652 1.00 38.15 C

ANISOU 2593 CB GLU B 147 4624 4572 5298 748 430 -334 C ATOM 2594 CG GLU B 147 -30.939 -22.329 49.150 1.00 49.95 C

ANISOU 2594 CG GLU B 147 6013 6209 6758 673 535 -420 C

ATOM 2595 CD GLU B 147 -32.181 -21.859 49.882 1.00 61.20 C

ANISOU 2595 CD GLU B 147 7285 7739 8231 768 549 -595 C

ATOM 2596 OE1 GLU B 147 -32.044 -21.131 50.892 1.00 65.00 O ANISOU 2596 OE1 GLU B 147 7740 8252 8704 773 602 -721 O

ATOM 2597 OE2 GLU B 147 -33.294 -22.215 49.439 1.00 65.10 O

ANISOU 2597 OE2 GLU B 147 7663 8304 8769 838 505 -634 O

ATOM 2598 N GLY B 148 -30.329 -23.657 44.744 1.00 21.89 N

ANISOU 2598 N GLY B 148 2732 2448 3139 682 321 -84 N ATOM 2599 CA GLY B 148 -30.978 -23.734 43.444 1.00 24.66 C

ANISOU 2599 CA GLY B 148 3135 2757 3478 755 213 -40 C

ATOM 2600 C GLY B 148 -30.049 -23.931 42.259 1.00 28.30 C

ANISOU 2600 C GLY B 148 3725 3199 3828 672 211 45 C ATOM 2601 O GLY B 148 -30.377 -23.544 41.136 1.00 32.22 O

ANISOU 2601 O GLY B 148 4341 3631 4271 709 117 102 O

ATOM 2602 N SER B 149 -28.885 -24.529 42.493 1.00 24.39 N

ANISOU 2602 N SER B 149 3202 2779 3286 561 306 36 N

ATOM 2603 CA SER B 149 -27.926 -24.697 41.410 1.00 28.04 C ANISOU 2603 CA SER B 149 3741 3281 3630 470 332 64 C

ATOM 2604 C SER B 149 -28.060 -26.042 40.703 1.00 24.13 C

ANISOU 2604 C SER B 149 3167 2884 3117 496 294 28 C

ATOM 2605 O SER B 149 -28.522 -27.022 41.282 1.00 21.74 O

ANISOU 2605 O SER B 149 2751 2609 2900 543 265 -10 O ATOM 2606 CB SER B 149 -26.494 -24.516 41.919 1.00 28.11 C

ANISOU 2606 CB SER B 149 3734 3346 3600 347 445 22 C

ATOM 2607 OG SER B 149 -26.145 -25.540 42.829 1.00 24.30 O

ANISOU 2607 OG SER B 149 3106 2945 3181 371 464 -50 O

ATOM 2608 N TYR B 150 -27.667 -26.058 39.436 1.00 26.38 N ANISOU 2608 N TYR B 150 3531 3217 3275 446 289 40 N

ATOM 2609 CA TYR B 150 -27.387 -27.290 38.719 1.00 23.22 C

ANISOU 2609 CA TYR B 150 3054 2931 2837 454 273 -43 C

ATOM 2610 C TYR B 150 -26.326 -26.969 37.678 1.00 26.00 C

ANISOU 2610 C TYR B 150 3473 3399 3008 328 353 -69 C ATOM 2611 O TYR B 150 -26.427 -25.949 37.000 1.00 26.65 O

ANISOU 2611 O TYR B 150 3720 3442 2964 248 353 34 O

ATOM 2612 CB TYR B 150 -28.627 -27.887 38.052 1.00 22.56 C

ANISOU 2612 CB TYR B 150 2963 2831 2778 546 149 -35 C

ATOM 2613 CG TYR B 150 -28.362 -29.283 37.542 1.00 22.59 C ANISOU 2613 CG TYR B 150 2880 2921 2783 565 118 -152 C

ATOM 2614 CD1 TYR B 150 -27.816 -29.494 36.274 1.00 23.70 C

ANISOU 2614 CD1 TYR B 150 3055 3179 2770 525 130 -218 C

ATOM 2615 CD2 TYR B 150 -28.617 -30.393 38.344 1.00 26.08 C

ANISOU 2615 CD2 TYR B 150 3219 3322 3368 608 70 -204 C ATOM 2616 CE1 TYR B 150 -27.541 -30.780 35.811 1.00 24.04 C

ANISOU 2616 CE1 TYR B 150 3009 3295 2829 568 88 -372 C

ATOM 2617 CE2 TYR B 150 -28.355 -31.685 37.889 1.00 27.41 C

ANISOU 2617 CE2 TYR B 150 3336 3518 3561 639 5 -323 C

ATOM 2618 CZ TYR B 150 -27.816 -31.866 36.624 1.00 29.45 C ANISOU 2618 CZ TYR B 150 3608 3891 3692 638 12 -424 C

ATOM 2619 OH TYR B 150 -27.553 -33.134 36.175 1.00 33.89 O

ANISOU 2619 OH TYR B 150 4111 4473 4291 694 -65 -584 O

ATOM 2620 N PRO B 151 -25.249 -27.781 37.613 1.00 28.83 N

ANISOU 2620 N PRO B 151 3706 3902 3346 300 418 -217 N ATOM 2621 CA PRO B 151 -24.857 -28.819 38.583 1.00 26.90 C

ANISOU 2621 CA PRO B 151 3309 3661 3251 388 393 -328 C

ATOM 2622 C PRO B 151 -24.525 -28.188 39.932 1.00 28.38 C

ANISOU 2622 C PRO B 151 3482 3782 3518 363 439 -283 C

ATOM 2623 O PRO B 151 -24.645 -26.973 40.057 1.00 29.20 O ANISOU 2623 O PRO B 151 3687 3829 3580 285 491 -186 O

ATOM 2624 CB PRO B 151 -23.575 -29.431 37.979 1.00 25.94 C

ANISOU 2624 CB PRO B 151 3070 3732 3054 362 449 -525 C

ATOM 2625 CG PRO B 151 -23.574 -29.010 36.541 1.00 28.95 C

ANISOU 2625 CG PRO B 151 3533 4238 3230 255 505 -521 C ATOM 2626 CD PRO B 151 -24.289 -27.681 36.499 1.00 31.20 C

ANISOU 2626 CD PRO B 151 4013 4390 3450 169 512 -300 C

ATOM 2627 N ALA B 152 -24.140 -28.990 40.920 1.00 30.01 N

ANISOU 2627 N ALA B 152 3589 3980 3834 429 398 -352 N

ATOM 2628 CA ALA B 152 -23.959 -28.491 42.282 1.00 30.11 C ANISOU 2628 CA ALA B 152 3593 3939 3908 411 421 -310

ATOM 2629 C ALA B 152 -23.128 -27.204 42.356 1, 00 29. 67

ANISOU 2629 C ALA B 152 3562 3934 3776 285 542 -313

ATOM 2630 O ALA B 152 -23.542 -26.215 42.968 1, 00 29. 54

ANISOU 2630 O ALA B 152 3623 3825 3774 247 570 -227

ATOM 2631 CB ALA B 152 -23.351 -29.576 43.169 1, 00 20. 75

ANISOU 2631 CB ALA B 152 2318 2760 2806 486 337 -394

ATOM 2632 N GLY B 153 -21.971 -27.213 41.709 1, 00 27. 65

ANISOU 2632 N GLY B 153 3236 3834 3438 208 612 -434

ATOM 2633 CA GLY B 153 -21.029 -26.117 41.849 1, 00 30. 35

ANISOU 2633 CA GLY B 153 3578 4246 3705 41 732 -460

ATOM 2634 C GLY B 153 -20.344 -26.230 43.198 1, 00 29. 35

ANISOU 2634 C GLY B 153 3341 4140 3670 77 713 -540

ATOM 2635 O GLY B 153 -20.455 -27.260 43.856 1, 00 31. 19

ANISOU 2635 O GLY B 153 3504 4349 3996 225 601 -577

ATOM 2636 N THR B 154 -19.640 -25.183 43.615 1, 00 30. 50

ANISOU 2636 N THR B 154 3490 4318 3780 -72 804 -559

ATOM 2637 CA THR B 154 -18.904 -25.202 44.881 1, 00 31. 33

ANISOU 2637 CA THR B 154 3484 4469 3951 -51 779 -652

ATOM 2638 C THR B 154 -18.936 -23.839 45.590 1, 00 31. 95

ANISOU 2638 C THR B 154 3666 4451 4024 -183 842

ATOM 2639 O THR B 154 -19.103 -22.792 44.955 1, 00 31. 01

ANISOU 2639 O THR B 154 3687 4255 3839 -335 918 -506

ATOM 2640 CB THR B 154 -17.424 -25.605 44.676 1, 00 34. 07

ANISOU 2640 CB THR B 154 3611 5061 4271 -90 813 -880

ATOM 2641 OG1 THR B 154 -16.851 -24.798 43.643 1, 00 41. 10

ANISOU 2641 OG1 THR B 154 4504 6080 5031 -322 971 -916

ATOM 2642 CG2 THR B 154 -17.293 -27.077 44.277 1, 00 32. 69

ANISOU 2642 CG2 THR B 154 3314 4960 4147 105 698 -1002

ATOM 2643 N LEU B 155 -18.775 -23.868 46.909 1, 00 28. 84

ANISOU 2643 N LEU B 155 3222 4046 3691 -125 789 -626

ATOM 2644 CA LEU B 155 -18.621 -22.655 47.700 1, 00 34. 53

ANISOU 2644 CA LEU B 155 4007 4702 4414 -241 838 -626

ATOM 2645 C LEU B 155 -17.165 -22.517 48.151 1, 00 39. 01

ANISOU 2645 C LEU B 155 4407 5450 4964 -346 869 503

ATOM 2646 O LEU B 155 -16.493 -23.515 48.397 1, 00 37. 52

ANISOU 2646 O LEU B 155 4048 5412 4797 -239 795 -923

ATOM 2647 CB LEU B 155 -19.539 -22.696 48.927 1, 00 31. 15

ANISOU 2647 CB LEU B 155 3632 4167 4038 -119 766 -566

ATOM 2648 CG LEU B 155 -21.047 -22. 696 48.663 1, 00 29. 11

ANISOU 2648 CG LEU B 155 3494 3759 3806 -23 740 -435

ATOM 2649 CD1 LEU B 155 -21.827 -22. 889 49.959 1, 00 21. 49

ANISOU 2649 CD1 LEU B 155 2524 2778 2864 65 694 -424

ATOM 2650 CD2 LEU B 155 -21.461 -21.405 47.977 1, 00 23. 60

ANISOU 2650 CD2 LEU B 155 2954 2909 3104 -107 787 -377

ATOM 2651 N SER B 156 -16.681 -21.282 48.256 1, 00 41. 60

ANISOU 2651 N SER B 156 4786 5756 5263 -550 958 333

ATOM 2652 CA SER B 156 -15.348 -21.024 48.811 1, 00 41. 92

ANISOU 2652 CA SER B 156 4653 5980 5294 -674 988 -1020

ATOM 2653 C SER B 156 -15.288 -19. 697 49.585 1, 00 37. 30

ANISOU 2653 C SER B 156 4180 5273 4721 -829 1022 -1025

ATOM 2654 O SER B 156 -16.122 -18. 815 49.394 1, 00 37. 36

ANISOU 2654 O SER B 156 4411 5048 4736 -880 1042 -894

ATOM 2655 CB SER B 156 -14.280 -21.063 47.712 1, 00 41. 80

ANISOU 2655 CB SER B 156 4493 6187 5203 -858 1100 -1146

ATOM 2656 OG SER B 156 -14.571 -20.122 46.693 1, 00 44. 44

ANISOU 2656 OG SER B 156 5024 6411 5451 -1087 1217 -1018

ATOM 2657 N TRP B 157 -14.302 -19.558 50.461 1, 00 36. 51

ANISOU 2657 N TRP B 157 3922 5321 4630 1006 -1195 ATOM 2658 CA TRP B 157 -14.239 -18.376 51.319 1.00 38.26 C

ANISOU 2658 CA TRP B 157 4240 5429 4870 -1018 1018 -1232 C

ATOM 2659 C TRP B 157 -13.085 -17.448 50.961 1.00 39.26 C

ANISOU 2659 C TRP B 157 4311 5648 4960 -1347 1129 -1356 C ATOM 2660 O TRP B 157 -12.064 -17.883 50.425 1.00 36.97 O

ANISOU 2660 O TRP B 157 3803 5618 4627 -1449 1187 -1490 O

ATOM 2661 CB TRP B 157 -14.140 -18.778 52.790 1.00 30.03 C

ANISOU 2661 CB TRP B 157 3099 4463 3847 -857 900 -1326 C

ATOM 2662 CG TRP B 157 -15.367 -19.446 53.333 1.00 28.20 C ANISOU 2662 CG TRP B 157 2965 4127 3624 -616 812 -1194 C

ATOM 2663 CD1 TRP B 157 -15.665 -20.769 53.278 1.00 28.85 C

ANISOU 2663 CD1 TRP B 157 2989 4273 3701 -424 723 -1132 C

ATOM 2664 CD2 TRP B 157 -16.448 -18.819 54.034 1.00 29.35 C

ANISOU 2664 CD2 TRP B 157 3271 4099 3779 -563 806 -1133 C ATOM 2665 NE1 TRP B 157 -16.867 -21.014 53.899 1.00 28.42 N

ANISOU 2665 NE1 TRP B 157 3054 4109 3636 -296 679 -1014 N

ATOM 2666 CE2 TRP B 157 -17.371 -19.829 54.369 1.00 27.94 C

ANISOU 2666 CE2 TRP B 157 3106 3928 3582 -369 737 -1030 C

ATOM 2667 CE3 TRP B 157 -16.730 -17.499 54.409 1.00 31.25 C ANISOU 2667 CE3 TRP B 157 3643 4182 4048 -663 845 -1178 C

ATOM 2668 CZ2 TRP B 157 -18.551 -19.567 55.063 1.00 27.61 C

ANISOU 2668 CZ2 TRP B 157 3164 3797 3530 -288 734 -987 C

ATOM 2669 CZ3 TRP B 157 -17.907 -17.238 55.099 1.00 31.17 C

ANISOU 2669 CZ3 TRP B 157 3734 4061 4049 -534 820 -1155 C ATOM 2670 CH2 TRP B 157 -18.799 -18.267 55.420 1.00 29.47 C

ANISOU 2670 CH2 TRP B 157 3490 3911 3796 -357 779 -1068 C

ATOM 2671 N HIS B 158 -13.253 -16.164 51.267 1.00 39.07 N

ANISOU 2671 N HIS B 158 4477 5415 4954 -1520 1155 -1332 N

ATOM 2672 CA HIS B 158 -12.206 -15.188 51.018 1.00 42.14 C ANISOU 2672 CA HIS B 158 4851 5854 5306 -1886 1255 -1437 C

ATOM 2673 C HIS B 158 -11.960 -14.308 52.230 1.00 42.37 C

ANISOU 2673 C HIS B 158 4911 5798 5391 -1957 1205 -1564 C

ATOM 2674 O HIS B 158 -12.895 -13.949 52.942 1.00 42.00 O

ANISOU 2674 O HIS B 158 5032 5524 5402 -1789 1121 -1510 O ATOM 2675 CB HIS B 158 -12.564 -14.325 49.811 1.00 46.43 C

ANISOU 2675 CB HIS B 158 5679 6169 5792 -2130 1337 -1254 C

ATOM 2676 CG HIS B 158 -12.889 -15.115 48.585 1.00 48.72 C

ANISOU 2676 CG HIS B 158 5967 6540 6004 -2069 1383 -1129 C

ATOM 2677 ND1 HIS B 158 -11.994 -15.293 47.552 1.00 52.48 N ANISOU 2677 ND1 HIS B 158 6318 7267 6354 -2328 1522 -1184 N

ATOM 2678 CD2 HIS B 158 -14.013 -15.788 48.228 1.00 47.22 C

ANISOU 2678 CD2 HIS B 158 5870 6238 5835 -1787 1311 -976 C

ATOM 2679 CE1 HIS B 158 -12.550 -16.032 46.609 1.00 53.05 C

ANISOU 2679 CE1 HIS B 158 6421 7368 6369 -2196 1528 -1069 C ATOM 2680 NE2 HIS B 158 -13.777 -16.345 46.999 1.00 51.15 N

ANISOU 2680 NE2 HIS B 158 6314 6897 6222 -1869 1394 -937 N

ATOM 2681 N LEU B 159 -10.695 -13.971 52.459 1.00 45.44 N

ANISOU 2681 N LEU B 159 5111 6396 5757 -2209 1259 -1762 N

ATOM 2682 CA LEU B 159 -10.309 -13.086 53.552 1.00 48.15 C ANISOU 2682 CA LEU B 159 5467 6681 6145 -2325 1214 -1916 C

ATOM 2683 C LEU B 159 -9.562 -11.889 52.982 1.00 54.69 C

ANISOU 2683 C LEU B 159 6397 7435 6948 -2789 1328 -1953 C

ATOM 2684 O LEU B 159 -8.519 -12.049 52.340 1.00 54.90 O

ANISOU 2684 O LEU B 159 6215 7741 6903 -3050 1445 -2056 O ATOM 2685 CB LEU B 159 -9.424 -13.820 54.563 1.00 45.98 C

ANISOU 2685 CB LEU B 159 4853 6749 5868 -2201 1134 -2152 C

ATOM 2686 CG LEU B 159 -8.773 -12.963 55.656 1.00 47.43 C

ANISOU 2686 CG LEU B 159 4987 6957 6076 -2360 1090 -2362 C

ATOM 2687 CD1 LEU B 159 -9.820 -12.382 56.590 1.00 45.12 C ANISOU 2687 CD1 LEU B 159 4945 6374 5825 -2200 1000 -2307

ATOM 2688 CD2 LEU B 159 -7.751 -13. 758 56. 442 1 , 00 44. 20 )

ANISOU 2688 CD2 LEU B 159 4217 6931 5647 -2251 993 -2601

ATOM 2689 N ASP B 160 -10. 115 -10. 700 53. 214 1 , 00 58. 3

ANISOU 2689 N ASP B 160 7186 7524 7471 -2898 1287 -1883

ATOM 2690 CA ASP B 160 -9. 558 -9. 444 52. 706 1 , 00 66. 11

ANISOU 2690 CA ASP B 160 8364 8324 8432 -3364 1360 -1874

ATOM 2691 C ASP B 160 -9.283 -9. 473 51. 198 1 , 00 69. 435

ANISOU 2691 C ASP B 160 8863 8797 8721 -3630 1494 -1700

ATOM 2692 O ASP B 160 -8.257 -8. 976 50. 733 1 , 00 73. i

ANISOU 2692 O ASP B 160 9298 9425 9080 -3908 1577 -1721

ATOM 2693 CB ASP B 160 -8.304 -9. 035 53. 491 1 , 00 70. 35 )

ANISOU 2693 CB ASP B 160 8672 9092 8965 -3574 1377 -2131

ATOM 2694 CG ASP B 160 -8.622 -8. 620 54. 927 1 , 00 72. 777

ANISOU 2694 CG ASP B 160 9006 9260 9383 -3425 1241 -2304

ATOM 2695 OD1 ASP B 160 -9.810 -8. 364 55. 224 1 , 00 68. 39 )

ANISOU 2695 OD1 ASP B 160 8708 8381 8898 -3167 1141 -2194

ATOM 2696 OD2 ASP B 160 -7.685 -8. 542 55. 755 1 , 00 76. 477

ANISOU 2696 OD2 ASP B 160 9240 9973 9840 -3464 1218 -2516

ATOM 2697 N GLY B 161 -10.210 -10. 064 50. 449 1 , 00 67. 16 )

ANISOU 2697 N GLY B 161 8695 8415 8409 -3420 1483 -1497

ATOM 2698 CA GLY B 161 -10.127 -10. 099 49. 001 1 , 00 70.

ANISOU 2698 CA GLY B 161 9281 8913 8727 -3645 1591 -1314

ATOM 2699 C GLY B 161 -9. 116 -11. 079 48. 434 1 , 00 70. 735

ANISOU 2699 C GLY B 161 8886 9412 8578 -3666 1719 -1447

ATOM 2700 O GLY B 161 -8. 595 -10. 880 47. 336 1 , 00 74. 80 )

ANISOU 2700 O GLY B 161 9458 10046 8915 -3886 1809 -1373

ATOM 2701 N LYS B 162 -8.829 -12. 136 49. 183 1 , 00 64.

ANISOU 2701 N LYS B 162 7755 8961 7907 -3419 1701 -1663

ATOM 2702 CA LYS B 162 -7. 920 -13. 178 48. 720 1 , 00 60. 67

ANISOU 2702 CA LYS B 162 6867 J893 7291 -3336 1764 -1832

ATOM 2703 C LYS B 162 -8. 480 -14. 543 49. 100 1 , 00 55. 40 )

ANISOU 2703 C LYS B 162 5981 J342 6725 -2928 1682 -1879

ATOM 2704 O LYS B 162 -9. 132 -14. 678 50. 134 1 , 00 50. 52

ANISOU 2704 O LYS B 162 5434 7546 6217 -2626 1529 -1846

ATOM 2705 CB LYS B 162 -6. 517 -12. 977 49. 304 1 , 00 63. 79

ANISOU 2705 CB LYS B 162 6989 9587 7660 -3448 1777 -2110

ATOM 2706 CG LYS B 162 -5. 855 -11. 676 48. 868 1 , 00 69. 55 j

ANISOU 2706 CG LYS B 162 7914 10242 8269 -3864 1868 -2069

ATOM 2707 CD LYS B 162 -4.363 -11. 647 49. 155 1 , 00 75. 03

ANISOU 2707 CD LYS B 162 8292 11317 8898 -3993 1919 -2365

ATOM 2708 CE LYS B 162 -3.729 -10. 382 48. 577 1 , 00 81. 55 j

ANISOU 2708 CE LYS B 162 9323 12083 9581 -4447 2029 -2304

ATOM 2709 NZ LYS B 162 -2.255 -10. 303 48. 808 1 , 00 86. 083

ANISOU 2709 NZ LYS B 162 9583 13046 10079 -4610 2101 -2608

ATOM 2710 N PRO B 163 -8.247 -15. 557 48. 253 1 , 00 56. 06 )

ANISOU 2710 N PRO B 163 5888 8679 6735 -2799 1717 -1921

ATOM 2711 CA PRO B 163 -8.792 -16. 896 48. 513 1 , 00 50.

ANISOU 2711 CA PRO B 163 5085 8082 6161 -2364 1597 -1933

ATOM 2712 C PRO B 163 -8.294 -17. 475 49. 836 1 , 00 46. 52

ANISOU 2712 C PRO B 163 4279 7677 5719 -2109 1439 -2142

ATOM 2713 O PRO B 163 -7.158 -17. 247 50. 232 1 , 00 47. 741

ANISOU 2713 O PRO B 163 4196 8074 5869 -2251 1452 -2383

ATOM 2714 CB PRO B 163 -8.270 -17. 724 47. 334 1 , 00 51. 99 )

ANISOU 2714 CB PRO B 163 5058 8499 6197 -2342 1655 -2022

ATOM 2715 CG PRO B 163 -7.997 -16. 721 46. 260 1 , 00 55. 77

ANISOU 2715 CG PRO B 163 5751 8935 6502 -2733 1798 -1915

ATOM 2716 CD PRO B 163 -7. 518 -15. 497 46. 974 1 , 00 56. i

ANISOU 2716 CD PRO B 163 5983 8974 6654 -3005 1823 -1943 ATOM 2717 N LEU B 164 -9.162 -18.212 50.512 1.00 45.09 N

ANISOU 2717 N LEU B 164 4183 7335 5614 -1730 1268 -2032 N

ATOM 2718 CA LEU B 164 -8.851 -18.801 51.801 1.00 47.23 C

ANISOU 2718 CA LEU B 164 4292 7700 5955 -1480 1084 -2169 C ATOM 2719 C LEU B 164 -8.788 -20.319 51.626 1.00 50.95 C

ANISOU 2719 C LEU B 164 4585 8315 6458 -1147 949 -2230 C

ATOM 2720 O LEU B 164 -9.808 -20.971 51.403 1.00 50.78 O

ANISOU 2720 O LEU B 164 4734 8110 6450 -937 889 -2035 O

ATOM 2721 CB LEU B 164 -9.935 -18.404 52.800 1.00 46.17 C ANISOU 2721 CB LEU B 164 4432 7260 5851 -1351 992 -1988 C

ATOM 2722 CG LEU B 164 -9.678 -18.434 54.303 1.00 47.94 C

ANISOU 2722 CG LEU B 164 4588 7532 6094 -1228 838 -2100 C

ATOM 2723 CD1 LEU B 164 -8.375 -17.740 54.656 1.00 52.67 C

ANISOU 2723 CD1 LEU B 164 4974 8348 6691 -1472 870 -2360 C ATOM 2724 CD2 LEU B 164 -10.838 -17.770 55.017 1.00 43.85 C

ANISOU 2724 CD2 LEU B 164 4358 6725 5577 -1186 822 -1936 C

ATOM 2725 N VAL B 165 -7.581 -20.872 51.704 1.00 54.40 N

ANISOU 2725 N VAL B 165 4674 9079 6918 -1100 888 -2522 N

ATOM 2726 CA VAL B 165 -7.353 -22.292 51.434 1.00 55.61 C ANISOU 2726 CA VAL B 165 4638 9369 7121 -781 735 -2638 C

ATOM 2727 C VAL B 165 -7.559 -23.162 52.675 1.00 57.78 C

ANISOU 2727 C VAL B 165 4948 9546 7459 -432 439 -2610 C

ATOM 2728 O VAL B 165 -6.897 -22.962 53.697 1.00 60.96 O

ANISOU 2728 O VAL B 165 5233 10056 7873 -414 317 -2752 O ATOM 2729 CB VAL B 165 -5.928 -22.538 50.889 1.00 59.45 C

ANISOU 2729 CB VAL B 165 4859 10159 7569 -828 732 -2944 C

ATOM 2730 CGI VAL B 165 -5.730 -24.006 50.561 1.00 56.72 C

ANISOU 2730 CGI VAL B 165 4405 9869 7277 -473 533 -3055 C

ATOM 2731 CG2 VAL B 165 -5.659 -21.677 49.663 1.00 60.41 C ANISOU 2731 CG2 VAL B 165 5051 10342 7562 -1200 988 -2923 C

ATOM 2732 N PRO B 166 -8.470 -24.143 52.583 1.00 57.43 N

ANISOU 2732 N PRO B 166 5078 9302 7440 -175 313 -2422 N

ATOM 2733 CA PRO B 166 -8.755 -25.018 53.726 1.00 59.59 C

ANISOU 2733 CA PRO B 166 5448 9453 7739 111 27 -2343 C ATOM 2734 C PRO B 166 -7.540 -25.849 54.133 1.00 67.65 C

ANISOU 2734 C PRO B 166 6179 10698 8827 337 -226 -2637 C

ATOM 2735 O PRO B 166 -6.690 -26.130 53.286 1.00 68.24 O

ANISOU 2735 O PRO B 166 5964 11009 8954 357 -189 -2904 O

ATOM 2736 CB PRO B 166 -9.869 -25.928 53.201 1.00 57.31 C ANISOU 2736 CB PRO B 166 5370 8936 7468 276 -20 -2117 C

ATOM 2737 CG PRO B 166 -10.471 -25.192 52.044 1.00 55.63 C

ANISOU 2737 CG PRO B 166 5249 8668 7220 54 258 -2007 C

ATOM 2738 CD PRO B 166 -9.324 -24.449 51.423 1.00 57.28 C

ANISOU 2738 CD PRO B 166 5201 9152 7409 -174 429 -2257 C ATOM 2739 N ASN B 167 -7.475 -26.213 55.415 1.00 74.34 N

ANISOU 2739 N ASN B 167 7104 11484 9658 502 -486 -2600 N

ATOM 2740 CA ASN B 167 -6.454 -27.114 55.975 1.00 80.75 C

ANISOU 2740 CA ASN B 167 7706 12441 10534 785 -821 -2840 C

ATOM 2741 C ASN B 167 -5.066 -26.498 56.180 1.00 81.67 C ANISOU 2741 C ASN B 167 7504 12868 10658 688 -794 -3179 C

ATOM 2742 O ASN B 167 -4.167 -27.148 56.707 1.00 84.38 O

ANISOU 2742 O ASN B 167 7779 13258 11022 916 -1032 -3340 O

ATOM 2743 CB ASN B 167 -6.354 -28.421 55.167 1.00 88.51 C

ANISOU 2743 CB ASN B 167 8616 13389 11626 1070 -985 -2928 C ATOM 2744 CG ASN B 167 -7.656 -29.201 55.144 1.00 91.79 C

ANISOU 2744 CG ASN B 167 9397 13454 12025 1179 -1066 -2582 C

ATOM 2745 OD1 ASN B 167 -8.734 -28.631 54.982 1.00 90.42 O

ANISOU 2745 OD1 ASN B 167 9457 13122 11776 977 -838 -2313 O

ATOM 2746 ND2 ASN B 167 -7.559 -30.515 55.322 1.00 96.12 N ANISOU 2746 ND2 ASN B 167 10002 13871 12650 1500 -1411 -2599 N

ATOM 2747 N GLU B 168 -4.896 -25.248 55.769 1.00 82.00 N

ANISOU 2747 N GLU B 168 7461 13038 10658 334 -478 -3235 N

ATOM 2748 CA GLU B 168 -3.638 -24.543 55.988 1.00 87.31 C ANISOU 2748 CA GLU B 168 7946 13934 11294 180 -400 -3493 C

ATOM 2749 C GLU B 168 -3.872 -23.245 56.753 1.00 86.23 C

ANISOU 2749 C GLU B 168 7867 13794 11102 -113 -282 -3430 C

ATOM 2750 O GLU B 168 -4.935 -22.636 56.638 1.00 84.04 O

ANISOU 2750 O GLU B 168 7793 13337 10800 -292 -131 -3204 O ATOM 2751 CB GLU B 168 -2.963 -24.228 54.657 1.00 91.51 C

ANISOU 2751 CB GLU B 168 8347 14631 11793 -25 -137 -3661 C

ATOM 2752 CG GLU B 168 -3.428 -25.113 53.527 1.00 94.88 C

ANISOU 2752 CG GLU B 168 8828 14979 12244 104 -122 -3599 C

ATOM 2753 CD GLU B 168 -2.697 -24.850 52.233 1.00 99.40 C ANISOU 2753 CD GLU B 168 9278 15752 12739 -112 99 -3782 C

ATOM 2754 OE1 GLU B 168 -2.341 -23.679 51.969 1.00101.63 O

ANISOU 2754 OE1 GLU B 168 9536 16146 12931 -478 338 -3812 O

ATOM 2755 OE2 GLU B 168 -2.464 -25.828 51.490 1.00100.41 O

ANISOU 2755 OE2 GLU B 168 9345 15920 12885 74 16 -3902 O ATOM 2756 N LYS B 169 -2.873 -22.825 57.526 1.00 89.15 N

ANISOU 2756 N LYS B 169 8110 14317 11446 -146 -344 -3624 N

ATOM 2757 CA LYS B 169 -2.931 -21.563 58.273 1.00 88.62 C

ANISOU 2757 CA LYS B 169 8100 14245 11325 -430 -242 -3612 C

ATOM 2758 C LYS B 169 -4.073 -21.513 59.288 1.00 79.28 C ANISOU 2758 C LYS B 169 7154 12875 10094 -382 -395 -3404 C

ATOM 2759 O LYS B 169 -4.645 -20.450 59.530 1.00 80.82 O

ANISOU 2759 O LYS B 169 7551 12918 10237 -624 -219 -3285 O

ATOM 2760 CB LYS B 169 -3.009 -20.363 57.313 1.00 92.39 C

ANISOU 2760 CB LYS B 169 8616 14706 11782 -847 117 -3590 C ATOM 2761 CG LYS B 169 -1.775 -20.186 56.434 1.00 98.14 C

ANISOU 2761 CG LYS B 169 9143 15664 12480 -984 277 -3821 C

ATOM 2762 CD LYS B 169 -2.078 -19.381 55.174 1.00 99.32 C

ANISOU 2762 CD LYS B 169 9414 15749 12574 -1346 588 -3712 C

ATOM 2763 CE LYS B 169 -1.679 -17.919 55.315 1.00101.24 C ANISOU 2763 CE LYS B 169 9717 15986 12762 -1751 775 -3742 C

ATOM 2764 NZ LYS B 169 -1.886 -17.177 54.038 1.00101.10 N

ANISOU 2764 NZ LYS B 169 9861 15889 12664 -2102 1040 -3614 N

ATOM 2765 N GLY B 170 -4.388 -22.663 59.881 1.00 71.44 N

ANISOU 2765 N GLY B 170 6270 11797 9077 -40 -685 -3290 N ATOM 2766 CA GLY B 170 -5.443 -22.764 60.877 1.00 64.84 C

ANISOU 2766 CA GLY B 170 5795 10724 8120 37 -780 -3003 C

ATOM 2767 C GLY B 170 -6.844 -22.583 60.318 1.00 57.79 C

ANISOU 2767 C GLY B 170 5206 9545 7205 -46 -556 -2690 C

ATOM 2768 O GLY B 170 -7.763 -22.156 61.020 1.00 57.40 O ANISOU 2768 O GLY B 170 5414 9341 7055 -108 -508 -2508 O

ATOM 2769 N VAL B 171 -7.010 -22.914 59.044 1.00 53.14 N

ANISOU 2769 N VAL B 171 4570 8914 6706 -41 -424 -2654 N

ATOM 2770 CA VAL B 171 -8.292 -22.766 58.374 1.00 48.02 C

ANISOU 2770 CA VAL B 171 4179 8016 6052 -108 -228 -2382 C ATOM 2771 C VAL B 171 -8.917 -24.118 58.076 1.00 46.69 C

ANISOU 2771 C VAL B 171 4126 7715 5900 150 -376 -2208 C

ATOM 2772 O VAL B 171 -8.283 -24.976 57.482 1.00 49.40 O

ANISOU 2772 O VAL B 171 4291 8155 6324 311 -493 -2339 O

ATOM 2773 CB VAL B 171 -8.129 -22.030 57.048 1.00 45.14 C ANISOU 2773 CB VAL B 171 3723 7678 5749 -342 49 -2440 C

ATOM 2774 CGI VAL B 171 -9.470 -21.913 56.342 1.00 38.58 C

ANISOU 2774 CGI VAL B 171 3163 6585 4911 -374 206 -2162 C

ATOM 2775 CG2 VAL B 171 -7.496 -20.666 57.281 1.00 39.56 C

ANISOU 2775 CG2 VAL B 171 2933 7067 5030 -646 194 -2602 C ATOM 2776 N SER B 172 -10.164 -24.307 58.483 1.00 44.15 N

ANISOU 2776 N SER B 172 4092 7179 5505 180 -373 -1938 N

ATOM 2777 CA SER B 172 -10.859 -25.547 58.181 1.00 42.77 C

ANISOU 2777 CA SER B 172 4056 6852 5342 370 -499 -1753 C ATOM 2778 C SER B 172 -12.249 -25.256 57.630 1.00 37.75 C

ANISOU 2778 C SER B 172 3628 6022 4694 270 -288 -1522 C

ATOM 2779 O SER B 172 -12.900 -24.288 58.025 1.00 33.80 O

ANISOU 2779 O SER B 172 3241 5469 4135 120 -133 -1455 O

ATOM 2780 CB SER B 172 -10.958 -26.426 59.427 1.00 46.51 C ANISOU 2780 CB SER B 172 4680 7281 5711 529 -795 -1647 C

ATOM 2781 OG SER B 172 -11.861 -25.860 60.363 1.00 48.82 O

ANISOU 2781 OG SER B 172 5182 7513 5855 395 -712 -1486 O

ATOM 2782 N VAL B 173 -12.699 -26.103 56.713 1.00 36.25 N

ANISOU 2782 N VAL B 173 3477 5730 4568 373 -300 -1429 N ATOM 2783 CA VAL B 173 -14.007 -25.935 56.104 1.00 36.16 C

ANISOU 2783 CA VAL B 173 3634 5550 4554 303 -131 -1230 C

ATOM 2784 C VAL B 173 -14.736 -27.266 56.135 1.00 35.92 C

ANISOU 2784 C VAL B 173 3751 5378 4518 451 -294 -1056 C

ATOM 2785 O VAL B 173 -14.118 -28.316 55.949 1.00 37.53 O ANISOU 2785 O VAL B 173 3895 5585 4780 621 -500 -1122 O

ATOM 2786 CB VAL B 173 -13.881 -25.415 54.642 1.00 39.04 C

ANISOU 2786 CB VAL B 173 3901 5934 4997 208 71 -1297 C

ATOM 2787 CGI VAL B 173 -15.227 -25.428 53.917 1.00 26.64 C

ANISOU 2787 CGI VAL B 173 2501 4188 3433 186 188 -1097 C ATOM 2788 CG2 VAL B 173 -13.294 -24.020 54.631 1.00 36.59 C

ANISOU 2788 CG2 VAL B 173 3509 5717 4677 -3 239 -1425 C

ATOM 2789 N LYS B 174 -16.039 -27.215 56.411 1.00 33.17 N

ANISOU 2789 N LYS B 174 3590 4909 4104 382 -215 -854 N

ATOM 2790 CA LYS B 174 -16.911 -28.372 56.265 1.00 29.56 C ANISOU 2790 CA LYS B 174 3283 4307 3642 453 -320 -674 C

ATOM 2791 C LYS B 174 -17.997 -28.026 55.262 1.00 27.28 C

ANISOU 2791 C LYS B 174 3029 3936 3402 384 -118 -589 C

ATOM 2792 O LYS B 174 -18.522 -26.903 55.257 1.00 25.77 O

ANISOU 2792 O LYS B 174 2841 3760 3189 272 71 -590 O ATOM 2793 CB LYS B 174 -17.536 -28.782 57.602 1.00 30.61 C

ANISOU 2793 CB LYS B 174 3602 4409 3618 402 -427 -510 C

ATOM 2794 CG LYS B 174 -16.529 -29.230 58.650 1.00 36.03 C

ANISOU 2794 CG LYS B 174 4304 5156 4228 482 -682 -559 C

ATOM 2795 CD LYS B 174 -15.786 -30.476 58.209 1.00 43.08 C ANISOU 2795 CD LYS B 174 5185 5957 5228 688 -959 -599 C

ATOM 2796 CE LYS B 174 -14.587 -30.769 59.122 1.00 51.24 C

ANISOU 2796 CE LYS B 174 6183 7067 6219 816 -1242 -710 C

ATOM 2797 NZ LYS B 174 -13.443 -29.815 58.924 1.00 51.24 N

ANISOU 2797 NZ LYS B 174 5896 7281 6291 832 -1154 -994 N ATOM 2798 N GLU B 175 -18.333 -28.996 54.419 1.00 25.60 N

ANISOU 2798 N GLU B 175 2847 3621 3257 467 -186 -531 N

ATOM 2799 CA GLU B 175 -19.253 -28.773 53.313 1.00 27.25 C

ANISOU 2799 CA GLU B 175 3070 3765 3517 427 -31 -473 C

ATOM 2800 C GLU B 175 -20.405 -29.755 53.350 1.00 25.74 C ANISOU 2800 C GLU B 175 3019 3447 3312 428 -102 -302 C

ATOM 2801 O GLU B 175 -20.299 -30.850 53.912 1.00 29.17 O

ANISOU 2801 O GLU B 175 3550 3807 3725 477 -302 -232 O

ATOM 2802 CB GLU B 175 -18.517 -28.896 51.973 1.00 29.68 C

ANISOU 2802 CB GLU B 175 3248 4114 3916 494 -9 -612 C ATOM 2803 CG GLU B 175 -17.294 -28.005 51.882 1.00 39.35 C

ANISOU 2803 CG GLU B 175 4312 5497 5142 445 70 -798 C

ATOM 2804 CD GLU B 175 -16.556 -28.137 50.571 1.00 46.22 C

ANISOU 2804 CD GLU B 175 5032 6468 6062 468 121 -956 C

ATOM 2805 OE1 GLU B 175 -16.592 -29.226 49.953 1.00 46.05 O ANISOU 2805 OE1 GLU B 175 4994 6408 6094 602 10 -985 0

ATOM 2806 OE2 GLU B 175 -15.937 -27.137 50.156 1.00 51.65 0

ANISOU 2806 OE2 GLU B 175 5622 7278 6725 331 276 -1060 O

ATOM 2807 N GLN B 176 -21.497 -29.362 52.715 1.00 24.99 N ANISOU 2807 N GLN B 176 2944 3318 3234 368 43 -238 N

ATOM 2808 CA GLN B 176 -22.714 -30.146 52.725 1.00 28.03 C

ANISOU 2808 CA GLN B 176 3430 3618 3604 326 13 -96 C

ATOM 2809 C GLN B 176 -23.480 -29.885 51.433 1.00 24.95 C

ANISOU 2809 C GLN B 176 2999 3194 3286 336 121 -100 C ATOM 2810 O GLN B 176 -23.576 -28.744 50.969 1.00 20.63 O

ANISOU 2810 O GLN B 176 2399 2687 2750 322 260 -154 O

ATOM 2811 CB GLN B 176 -23.562 -29.757 53.948 1.00 26.37 C

ANISOU 2811 CB GLN B 176 3277 3473 3272 193 86 -14 C

ATOM 2812 CG GLN B 176 -24.865 -30.516 54.074 1.00 31.21 C ANISOU 2812 CG GLN B 176 3967 4049 3843 90 83 118 C

ATOM 2813 CD GLN B 176 -25.573 -30.232 55.394 1.00 37.59 C

ANISOU 2813 CD GLN B 176 4810 4984 4489 -69 162 169 C

ATOM 2814 OE1 GLN B 176 -25.707 -29.077 55.802 1.00 42.19 O

ANISOU 2814 OE1 GLN B 176 5310 5682 5037 -82 303 70 O ATOM 2815 NE2 GLN B 176 -26.011 -31.287 56.073 1.00 36.57 N

ANISOU 2815 NE2 GLN B 176 4814 4832 4248 -206 66 315 N

ATOM 2816 N THR B 177 -24.019 -30.944 50.849 1.00 26.13 N

ANISOU 2816 N THR B 177 3196 3252 3479 359 32 -42 N

ATOM 2817 CA THR B 177 -24.816 -30.826 49.632 1.00 27.60 C ANISOU 2817 CA THR B 177 3352 3415 3721 372 103 -45 C

ATOM 2818 C THR B 177 -26.165 -31.503 49.825 1.00 26.41 C

ANISOU 2818 C THR B 177 3256 3220 3560 285 82 65 C

ATOM 2819 O THR B 177 -26.231 -32.635 50.307 1.00 27.22 O

ANISOU 2819 O THR B 177 3451 3240 3651 241 -53 141 O ATOM 2820 CB THR B 177 -24.103 -31.480 48.433 1.00 29.47 C

ANISOU 2820 CB THR B 177 3555 3615 4026 481 22 -136 C

ATOM 2821 OG1 THR B 177 -22.922 -30.736 48.120 1.00 32.16 O

ANISOU 2821 OG1 THR B 177 3808 4053 4359 517 85 -262 O

ATOM 2822 CG2 THR B 177 -25.013 -31.494 47.217 1.00 27.02 C ANISOU 2822 CG2 THR B 177 3238 3284 3744 484 68 -126 C

ATOM 2823 N ARG B 178 -27.239 -30.806 49.469 1.00 25.00 N

ANISOU 2823 N ARG B 178 3022 3091 3385 253 199 66 N

ATOM 2824 CA ARG B 178 -28.575 -31.396 49.530 1.00 25.88 C

ANISOU 2824 CA ARG B 178 3132 3208 3495 156 197 129 C ATOM 2825 C ARG B 178 -29.307 -31.170 48.222 1.00 23.89 C

ANISOU 2825 C ARG B 178 2817 2948 3312 222 218 84 C

ATOM 2826 O ARG B 178 -28.946 -30.286 47.442 1.00 22.05 O

ANISOU 2826 O ARG B 178 2560 2718 3099 320 261 27 O

ATOM 2827 CB ARG B 178 -29.389 -30.816 50.689 1.00 26.66 C ANISOU 2827 CB ARG B 178 3184 3438 3509 39 310 138 C

ATOM 2828 CG ARG B 178 -28.892 -31.206 52.071 1.00 36.46 C

ANISOU 2828 CG ARG B 178 4512 4707 4633 -73 277 207 C

ATOM 2829 CD ARG B 178 -29.777 -30.579 53.131 1.00 47.01 C

ANISOU 2829 CD ARG B 178 5776 6226 5859 -202 418 178 C ATOM 2830 NE ARG B 178 -29.939 -29.144 52.898 1.00 52.53 N

ANISOU 2830 NE ARG B 178 6355 6994 6611 -82 535 36 N

ATOM 2831 CZ ARG B 178 -29.430 -28.200 53.680 1.00 56.54 C

ANISOU 2831 CZ ARG B 178 6850 7566 7066 -61 598 -40 C

ATOM 2832 NH1 ARG B 178 -28.743 -28.544 54.764 1.00 63.32 N ANISOU 2832 NH1 ARG B 178 7791 8466 7800 -152 563 12 N

ATOM 2833 NH2 ARG B 178 -29.616 -26.919 53.388 1.00 53.93 N

ANISOU 2833 NH2 ARG B 178 6444 7243 6805 51 672 -169 N

ATOM 2834 N ARG B 179 -30.351 -31.955 47.996 1.00 25.65 N

ANISOU 2834 N ARG B 179 3024 3164 3556 146 179 117 N ATOM 2835 CA ARG B 179 -31.051 -31.939 46.716 1.00 28.33 C

ANISOU 2835 CA ARG B 179 3309 3499 3957 212 159 70 C

ATOM 2836 C ARG B 179 -32.538 -31.702 46.952 1.00 28.13 C

ANISOU 2836 C ARG B 179 3163 3589 3935 135 218 46 C ATOM 2837 O ARG B 179 -33.134 -32.320 47.835 1.00 28.41 O

ANISOU 2837 O ARG B 179 3182 3684 3930 -36 238 86 O

ATOM 2838 CB ARG B 179 -30.827 -33.285 46.019 1.00 34.08 C

ANISOU 2838 CB ARG B 179 4108 4110 4732 208 20 82 C

ATOM 2839 CG ARG B 179 -30.768 -33.225 44.520 1.00 43.48 C ANISOU 2839 CG ARG B 179 5280 5285 5957 328 -19 7 C

ATOM 2840 CD ARG B 179 -29.575 -34.004 43.980 1.00 46.57 C

ANISOU 2840 CD ARG B 179 5738 5588 6369 409 -118 -49 C

ATOM 2841 NE ARG B 179 -29.663 -35.435 44.246 1.00 49.85 N

ANISOU 2841 NE ARG B 179 6232 5867 6841 352 -266 -28 N ATOM 2842 CZ ARG B 179 -30.321 -36.299 43.476 1.00 50.43 C

ANISOU 2842 CZ ARG B 179 6319 5876 6968 330 -362 -63 C

ATOM 2843 NH1 ARG B 179 -30.962 -35.870 42.392 1.00 50.43 N

ANISOU 2843 NH1 ARG B 179 6240 5963 6956 371 -323 -122 N

ATOM 2844 NH2 ARG B 179 -30.346 -37.592 43.793 1.00 45.77 N ANISOU 2844 NH2 ARG B 179 5839 5114 6437 262 -519 -36 N

ATOM 2845 N HIS B 180 -33.143 -30.801 46.186 1.00 26.57 N

ANISOU 2845 N HIS B 180 2883 3439 3775 252 238 -28 N

ATOM 2846 CA HIS B 180 -34.580 -30.580 46.312 1.00 25.78 C

ANISOU 2846 CA HIS B 180 2621 3473 3700 220 269 -103 C ATOM 2847 C HIS B 180 -35.281 -31.844 45.831 1.00 25.98 C

ANISOU 2847 C HIS B 180 2618 3498 3753 103 193 -89 C

ATOM 2848 O HIS B 180 -34.988 -32.339 44.745 1.00 23.63 O

ANISOU 2848 O HIS B 180 2391 3098 3490 168 93 -77 O

ATOM 2849 CB HIS B 180 -35.032 -29.362 45.501 1.00 25.40 C ANISOU 2849 CB HIS B 180 2516 3433 3701 414 242 -190 C

ATOM 2850 CG HIS B 180 -36.472 -28.998 45.708 1.00 29.63 C

ANISOU 2850 CG HIS B 180 2846 4130 4283 435 255 -322 C

ATOM 2851 ND1 HIS B 180 -37.510 -29.740 45.184 1.00 30.87 N

ANISOU 2851 ND1 HIS B 180 2878 4374 4478 380 197 -373 N ATOM 2852 CD2 HIS B 180 -37.041 -27.972 46.384 1.00 25.90 C

ANISOU 2852 CD2 HIS B 180 2245 3764 3831 513 312 -451 C

ATOM 2853 CE1 HIS B 180 -38.660 -29.178 45.525 1.00 29.28 C

ANISOU 2853 CE1 HIS B 180 2456 4351 4318 423 224 -534 C

ATOM 2854 NE2 HIS B 180 -38.402 -28.111 46.255 1.00 27.66 N ANISOU 2854 NE2 HIS B 180 2245 4159 4106 516 291 -592 N

ATOM 2855 N PRO B 181 -36.188 -32.389 46.651 1.00 25.50 N

ANISOU 2855 N PRO B 181 2459 3565 3666 -98 248 -99 N

ATOM 2856 CA PRO B 181 -36.808 -33.685 46.344 1.00 28.76 C

ANISOU 2856 CA PRO B 181 2872 3956 4100 -275 176 -70 C ATOM 2857 C PRO B 181 -37.610 -33.715 45.034 1.00 31.54 C

ANISOU 2857 C PRO B 181 3113 4333 4536 -173 87 -171 C

ATOM 2858 O PRO B 181 -37.796 -34.795 44.465 1.00 27.70 O

ANISOU 2858 O PRO B 181 2676 3764 4084 -270 -11 -152 O

ATOM 2859 CB PRO B 181 -37.719 -33.944 47.558 1.00 28.64 C ANISOU 2859 CB PRO B 181 2739 4137 4005 -546 294 -80 C

ATOM 2860 CG PRO B 181 -37.921 -32.612 48.185 1.00 28.58 C

ANISOU 2860 CG PRO B 181 2584 4307 3968 -434 422 -193 C

ATOM 2861 CD PRO B 181 -36.649 -31.847 47.936 1.00 26.48 C

ANISOU 2861 CD PRO B 181 2470 3873 3719 -203 387 -147 C ATOM 2862 N GLU B 182 -38.063 -32.560 44.553 1.00 33.93 N

ANISOU 2862 N GLU B 182 3289 4731 4874 26 93 -280 N

ATOM 2863 CA GLU B 182 -38.858 -32.529 43.325 1.00 35.92 C

ANISOU 2863 CA GLU B 182 3442 5016 5188 140 -22 -375 C

ATOM 2864 C GLU B 182 -38.085 -32.014 42.107 1.00 35.68 C ANISOU 2864 C GLU B 182 3563 4843 5150 364 -124 -342 C

ATOM 2865 0 GLU B 182 -38.174 -32.593 41.021 1.00 37.24 0

ANISOU 2865 0 GLU B 182 3799 4994 5355 391 -237 -355 0

ATOM 2866 CB GLU B 182 -40.126 -31.703 43.523 1.00 41.89 C ANISOU 2866 CB GLU B 182 3937 5991 5988 210 2 -545 C

ATOM 2867 CG GLU B 182 -41.401 -32.412 43.095 1.00 54.93 C

ANISOU 2867 CG GLU B 182 5381 7798 7691 99 -56 -666 C

ATOM 2868 CD GLU B 182 -42.165 -33.036 44.266 1.00 66.04 C

ANISOU 2868 CD GLU B 182 6611 9416 9067 -214 88 -719 C ATOM 2869 OE1 GLU B 182 -42.345 -32.365 45.311 1.00 67.82 O

ANISOU 2869 OE1 GLU B 182 6718 9798 9251 -235 226 -788 O

ATOM 2870 OE2 GLU B 182 -42.591 -34.204 44.137 1.00 71.61 O

ANISOU 2870 OE2 GLU B 182 7302 10133 9773 -460 65 -698 O

ATOM 2871 N THR B 183 -37.329 -30.931 42.279 1.00 33.16 N ANISOU 2871 N THR B 183 3336 4465 4799 497 -80 -304 N

ATOM 2872 CA THR B 183 -36.691 -30.274 41.136 1.00 24.83 C

ANISOU 2872 CA THR B 183 2427 3305 3703 663 -161 -268 C

ATOM 2873 C THR B 183 -35.304 -30.806 40.854 1.00 26.67 C

ANISOU 2873 C THR B 183 2832 3428 3875 620 -139 -185 C ATOM 2874 O THR B 183 -34.787 -30.628 39.754 1.00 24.28 O

ANISOU 2874 O THR B 183 2636 3081 3508 695 -196 -170 O

ATOM 2875 CB THR B 183 -36.565 -28.758 41.339 1.00 29.97 C

ANISOU 2875 CB THR B 183 3116 3922 4348 810 -146 -272 C

ATOM 2876 OG1 THR B 183 -35.707 -28.497 42.461 1.00 25.42 O ANISOU 2876 OG1 THR B 183 2588 3318 3753 739 -14 -229 O

ATOM 2877 CG2 THR B 183 -37.944 -28.121 41.558 1.00 26.63 C

ANISOU 2877 CG2 THR B 183 2499 3611 4007 918 -201 -408 C

ATOM 2878 N GLY B 184 -34.696 -31.445 41.853 1.00 25.36 N

ANISOU 2878 N GLY B 184 2688 3234 3715 500 -66 -145 N ATOM 2879 CA GLY B 184 -33.348 -31.959 41.716 1.00 23.44 C

ANISOU 2879 CA GLY B 184 2570 2899 3435 490 -65 -108 C

ATOM 2880 C GLY B 184 -32.259 -30.912 41.896 1.00 25.01 C

ANISOU 2880 C GLY B 184 2845 3080 3579 549 14 -80 C

ATOM 2881 O GLY B 184 -31.079 -31.224 41.823 1.00 29.29 O ANISOU 2881 O GLY B 184 3451 3588 4090 547 26 -84 O

ATOM 2882 N LEU B 185 -32.640 -29.667 42.137 1.00 25.99 N

ANISOU 2882 N LEU B 185 2953 3226 3698 603 57 -75 N

ATOM 2883 CA LEU B 185 -31.647 -28.600 42.250 1.00 26.23 C

ANISOU 2883 CA LEU B 185 3075 3215 3677 630 122 -48 C ATOM 2884 C LEU B 185 -30.895 -28.677 43.579 1.00 27.01 C

ANISOU 2884 C LEU B 185 3163 3320 3781 558 208 -40 C

ATOM 2885 O LEU B 185 -31.464 -29.053 44.606 1.00 26.64 O

ANISOU 2885 O LEU B 185 3041 3316 3763 500 231 -44 O

ATOM 2886 CB LEU B 185 -32.314 -27.237 42.100 1.00 27.01 C ANISOU 2886 CB LEU B 185 3196 3283 3786 723 100 -51 C

ATOM 2887 CG LEU B 185 -33.042 -27.008 40.780 1.00 28.08 C

ANISOU 2887 CG LEU B 185 3373 3398 3897 815 -25 -46 C

ATOM 2888 CD1 LEU B 185 -33.584 -25.581 40.721 1.00 23.88 C

ANISOU 2888 CD1 LEU B 185 2904 2783 3388 937 -94 -46 C ATOM 2889 CD2 LEU B 185 -32.116 -27.296 39.601 1.00 22.63 C

ANISOU 2889 CD2 LEU B 185 2811 2699 3089 772 -37 0 C

ATOM 2890 N PHE B 186 -29.624 -28.296 43.553 1.00 25.59 N

ANISOU 2890 N PHE B 186 3051 3119 3552 544 254 -36 N

ATOM 2891 CA PHE B 186 -28.749 -28.453 44.709 1.00 26.98 C ANISOU 2891 CA PHE B 186 3216 3309 3725 489 304 -42 C

ATOM 2892 C PHE B 186 -28.755 -27.265 45.660 1.00 25.71 C

ANISOU 2892 C PHE B 186 3057 3151 3561 478 379 -51 C

ATOM 2893 O PHE B 186 -28.836 -26.114 45.244 1.00 28.58 O

ANISOU 2893 O PHE B 186 3474 3467 3919 513 397 -55 O ATOM 2894 CB PHE B 186 -27.311 -28.688 44.254 1.00 25.09 C

ANISOU 2894 CB PHE B 186 3003 3085 3447 482 310 -82 C

ATOM 2895 CG PHE B 186 -27.107 -29.967 43.510 1.00 26.87 C

ANISOU 2895 CG PHE B 186 3212 3311 3685 514 225 -125 C ATOM 2896 CD1 PHE B 186 -27.183 -29.999 42.127 1.00 26.98 C

ANISOU 2896 CD1 PHE B 186 3245 3352 3656 541 209 -158 C

ATOM 2897 CD2 PHE B 186 -26.803 -31.136 44.188 1.00 28.68 C

ANISOU 2897 CD2 PHE B 186 3430 3504 3965 520 140 -140 C

ATOM 2898 CE1 PHE B 186 -26.964 -31.187 41.432 1.00 26.33 C ANISOU 2898 CE1 PHE B 186 3139 3277 3588 582 126 -239 C

ATOM 2899 CE2 PHE B 186 -26.585 -32.330 43.502 1.00 27.80 C

ANISOU 2899 CE2 PHE B 186 3318 3356 3889 573 30 -208 C

ATOM 2900 CZ PHE B 186 -26.673 -32.352 42.123 1.00 24.97 C

ANISOU 2900 CZ PHE B 186 2948 3042 3497 609 32 -274 C ATOM 2901 N THR B 187 -28.658 -27.566 46.947 1.00 25.54 N

ANISOU 2901 N THR B 187 2998 3174 3533 423 406 -54 N

ATOM 2902 CA THR B 187 -28.409 -26.552 47.961 1.00 26.79 C

ANISOU 2902 CA THR B 187 3154 3353 3672 405 478 -93 C

ATOM 2903 C THR B 187 -27.068 -26.869 48.607 1.00 26.92 C ANISOU 2903 C THR B 187 3189 3391 3647 355 478 -99 C

ATOM 2904 O THR B 187 -26.834 -28.000 49.040 1.00 26.60 O

ANISOU 2904 O THR B 187 3149 3368 3590 326 415 -65 O

ATOM 2905 CB THR B 187 -29.514 -26.540 49.022 1.00 25.75 C

ANISOU 2905 CB THR B 187 2942 3309 3533 373 516 -123 C ATOM 2906 OG1 THR B 187 -30.733 -26.106 48.415 1.00 25.23 O

ANISOU 2906 OG1 THR B 187 2817 3244 3524 451 502 -166 O

ATOM 2907 CG2 THR B 187 -29.162 -25.600 50.181 1.00 27.63 C

ANISOU 2907 CG2 THR B 187 3174 3590 3735 352 588 -194 C

ATOM 2908 N LEU B 188 -26.179 -25.884 48.639 1.00 28.31 N ANISOU 2908 N LEU B 188 3391 3554 3810 343 526 -146 N

ATOM 2909 CA LEU B 188 -24.833 -26.093 49.165 1.00 25.09 C

ANISOU 2909 CA LEU B 188 2967 3194 3370 305 517 -188 C

ATOM 2910 C LEU B 188 -24.673 -25.328 50.458 1.00 26.21 C

ANISOU 2910 C LEU B 188 3105 3375 3480 261 563 -234 C ATOM 2911 O LEU B 188 -25.210 -24.235 50.610 1.00 28.66 O

ANISOU 2911 O LEU B 188 3437 3648 3806 262 621 -269 O

ATOM 2912 CB LEU B 188 -23.770 -25.618 48.172 1.00 23.09 C

ANISOU 2912 CB LEU B 188 2719 2945 3111 278 551 -237 C

ATOM 2913 CG LEU B 188 -23.722 -26.264 46.789 1.00 28.34 C ANISOU 2913 CG LEU B 188 3381 3612 3773 307 523 -228 C

ATOM 2914 CD1 LEU B 188 -22.570 -25.664 45.996 1.00 30.99 C

ANISOU 2914 CD1 LEU B 188 3707 4013 4057 222 594 -298 C

ATOM 2915 CD2 LEU B 188 -23.570 -27.774 46.880 1.00 30.14 C

ANISOU 2915 CD2 LEU B 188 3557 3863 4030 377 417 -245 C ATOM 2916 N GLN B 189 -23.915 -25.900 51.382 1.00 25.80 N

ANISOU 2916 N GLN B 189 3030 3390 3382 238 512 -251 N

ATOM 2917 CA GLN B 189 -23.678 -25.268 52.663 1.00 27.46 C

ANISOU 2917 CA GLN B 189 3236 3663 3533 188 542 -306 C

ATOM 2918 C GLN B 189 -22.215 -25.458 53.042 1.00 33.37 C ANISOU 2918 C GLN B 189 3949 4472 4259 178 479 -372 C

ATOM 2919 O GLN B 189 -21.638 -26.527 52.832 1.00 35.50 O

ANISOU 2919 O GLN B 189 4201 4750 4539 229 367 -356 O

ATOM 2920 CB GLN B 189 -24.614 -25.866 53.708 1.00 26.75 C

ANISOU 2920 CB GLN B 189 3161 3639 3364 151 528 -248 C ATOM 2921 CG GLN B 189 -24.868 -24.979 54.898 1.00 37.59 C

ANISOU 2921 CG GLN B 189 4519 5101 4660 99 603 -332 C

ATOM 2922 CD GLN B 189 -26.035 -25.461 55.750 1.00 43.02 C

ANISOU 2922 CD GLN B 189 5199 5903 5245 26 637 -295 C

ATOM 2923 OE1 GLN B 189 -27.038 -25.949 55.228 1.00 47.76 O ANISOU 2923 OE1 GLN B 189 5777 6493 5877 23 652 -240 0

ATOM 2924 NE2 GLN B 189 -25.905 -25.329 57.065 1.00 40.59 N

ANISOU 2924 NE2 GLN B 189 4900 5727 4795 -57 655 -334 N

ATOM 2925 N SER B 190 -21.608 -24.408 53.579 1.00 35.71 N ANISOU 2925 N SER B 190 4225 4805 4537 123 532 -471 N

ATOM 2926 CA SER B 190 -20.186 -24.434 53.890 1.00 35.72 C

ANISOU 2926 CA SER B 190 4155 4892 4525 104 477 -571 C

ATOM 2927 C SER B 190 -19.894 -23.683 55.190 1.00 37.10 C

ANISOU 2927 C SER B 190 4328 5137 4631 44 488 -656 C ATOM 2928 O SER B 190 -20.259 -22.514 55.330 1.00 39.67 O

ANISOU 2928 O SER B 190 4686 5417 4970 -13 587 -710 O

ATOM 2929 CB SER B 190 -19.389 -23.841 52.722 1.00 31.70 C

ANISOU 2929 CB SER B 190 3593 4379 4075 51 549 -647 C

ATOM 2930 OG SER B 190 -18.017 -23.685 53.044 1.00 30.23 O ANISOU 2930 OG SER B 190 3292 4315 3879 5 521 -789 O

ATOM 2931 N GLU B 191 -19.249 -24.357 56.140 1.00 33.35 N

ANISOU 2931 N GLU B 191 3830 4759 4082 67 361 -675 N

ATOM 2932 CA GLU B 191 -18.911 -23.731 57.426 1.00 33.08 C

ANISOU 2932 CA GLU B 191 3794 4821 3954 8 351 -765 C ATOM 2933 C GLU B 191 -17.416 -23.460 57.569 1.00 32.29 C

ANISOU 2933 C GLU B 191 3577 4817 3873 -10 286 -921 C

ATOM 2934 O GLU B 191 -16.598 -24.370 57.458 1.00 27.05 O

ANISOU 2934 O GLU B 191 2844 4210 3224 75 140 -943 O

ATOM 2935 CB GLU B 191 -19.408 -24.582 58.594 1.00 38.25 C ANISOU 2935 CB GLU B 191 4535 5540 4458 14 247 -665 C

ATOM 2936 CG GLU B 191 -20.908 -24.775 58.577 1.00 48.12 C

ANISOU 2936 CG GLU B 191 5861 6753 5670 -16 339 -548 C

ATOM 2937 CD GLU B 191 -21.421 -25.583 59.749 1.00 53.44 C

ANISOU 2937 CD GLU B 191 6634 7519 6152 -83 264 -439 C ATOM 2938 OE1 GLU B 191 -20.586 -26.069 60.544 1.00 54.03 O

ANISOU 2938 OE1 GLU B 191 6754 7653 6123 -82 103 -426 O

ATOM 2939 OE2 GLU B 191 -22.663 -25.717 59.869 1.00 52.43 O

ANISOU 2939 OE2 GLU B 191 6538 7417 5967 -149 360 -371 O

ATOM 2940 N LEU B 192 -17.072 -22.199 57.811 1.00 27.10 N ANISOU 2940 N LEU B 192 2891 4178 3227 -116 382 -1053 N

ATOM 2941 CA LEU B 192 -15.684 -21.782 57.883 1.00 30.14 C

ANISOU 2941 CA LEU B 192 3141 4673 3638 -180 349 -1228 C

ATOM 2942 C LEU B 192 -15.238 -21.607 59.326 1.00 35.29 C

ANISOU 2942 C LEU B 192 3778 5453 4179 -195 249 -1328 C ATOM 2943 O LEU B 192 -15.911 -20.951 60.119 1.00 36.84 O

ANISOU 2943 O LEU B 192 4064 5631 4301 -243 307 -1339 O

ATOM 2944 CB LEU B 192 -15.489 -20.469 57.129 1.00 32.27 C

ANISOU 2944 CB LEU B 192 3410 4862 3990 -339 510 -1308 C

ATOM 2945 CG LEU B 192 -14.117 -19.798 57.237 1.00 36.08 C ANISOU 2945 CG LEU B 192 3750 5467 4491 -484 517 -1509 C

ATOM 2946 CD1 LEU B 192 -13.040 -20.641 56.557 1.00 37.18 C

ANISOU 2946 CD1 LEU B 192 3692 5770 4663 -448 457 -1590 C

ATOM 2947 CD2 LEU B 192 -14.161 -18.398 56.639 1.00 34.99 C

ANISOU 2947 CD2 LEU B 192 3698 5185 4412 -688 669 -1544 C ATOM 2948 N MET B 193 -14.098 -22.205 59.656 1.00 36.56 N

ANISOU 2948 N MET B 193 3814 5756 4323 -138 85 -1425 N

ATOM 2949 CA MET B 193 -13.459 -21.996 60.944 1.00 40.27 C

ANISOU 2949 CA MET B 193 4249 6370 4683 -155 -38 -1547 C

ATOM 2950 C MET B 193 -12.042 -21.485 60.740 1.00 43.76 C ANISOU 2950 C MET B 193 4473 6953 5202 -226 -59 -1785 C

ATOM 2951 O MET B 193 -11.298 -22.019 59.916 1.00 46.62 O

ANISOU 2951 O MET B 193 4678 7379 5658 -170 -102 -1852 O

ATOM 2952 CB MET B 193 -13.433 -23.288 61.757 1.00 41.42 C

ANISOU 2952 CB MET B 193 4463 6569 4705 -5 -285 -1439 C ATOM 2953 CG MET B 193 -14.792 -23.715 62.282 1.00 41.53 C

ANISOU 2953 CG MET B 193 4694 6503 4584 -11 -259 -1221 C

ATOM 2954 SD MET B 193 -14.648 -25.051 63.480 1.00 64.61 S

ANISOU 2954 SD MET B 193 7765 9484 7298 81 -572 -1079 S ATOM 2955 CE MET B 193 -13.860 -24.190 64.846 1.00 47.98 C

ANISOU 2955 CE MET B 193 5609 7588 5035 6 -644 -1276 C

ATOM 2956 N VAL B 194 -11.669 -20.440 61.473 1.00 42.44 N

ANISOU 2956 N VAL B 194 4278 6853 4995 -362 -20 -1941 N

ATOM 2957 CA VAL B 194 -10.307 -19.925 61.388 1.00 46.15 C ANISOU 2957 CA VAL B 194 4523 7485 5528 -470 -40 -2189 C

ATOM 2958 C VAL B 194 -9.668 -19.767 62.764 1.00 49.06 C

ANISOU 2958 C VAL B 194 4836 8024 5781 -464 -211 -2346 C

ATOM 2959 O VAL B 194 -10.348 -19.531 63.765 1.00 49.28 O

ANISOU 2959 O VAL B 194 5027 8023 5675 -463 -230 -2291 O ATOM 2960 CB VAL B 194 -10.225 -18.568 60.643 1.00 48.16 C

ANISOU 2960 CB VAL B 194 4775 7643 5879 -726 191 -2273 C

ATOM 2961 CGI VAL B 194 -10.887 -18.650 59.282 1.00 35.71 C

ANISOU 2961 CGI VAL B 194 3284 5898 4385 -744 345 -2106 C

ATOM 2962 CG2 VAL B 194 -10.846 -17.460 61.475 1.00 50.25 C ANISOU 2962 CG2 VAL B 194 5204 7792 6095 -830 258 -2302 C

ATOM 2963 N THR B 195 -8.351 -19.918 62.804 1.00 50.66 N

ANISOU 2963 N THR B 195 4789 8435 6026 -459 -338 -2564 N

ATOM 2964 CA THR B 195 -7.584 -19.595 63.993 1.00 52.38 C

ANISOU 2964 CA THR B 195 4915 8837 6150 -483 -499 -2761 C ATOM 2965 C THR B 195 -6.752 -18.364 63.668 1.00 53.40 C

ANISOU 2965 C THR B 195 4863 9049 6378 -753 -346 -3014 C

ATOM 2966 O THR B 195 -5.709 -18.471 63.026 1.00 55.80 O

ANISOU 2966 O THR B 195 4896 9523 6782 -803 -352 -3196 O

ATOM 2967 CB THR B 195 -6.676 -20.758 64.428 1.00 52.52 C ANISOU 2967 CB THR B 195 4774 9046 6135 -246 -825 -2845 C

ATOM 2968 OG1 THR B 195 -7.488 -21.883 64.793 1.00 53.46 O

ANISOU 2968 OG1 THR B 195 5124 9043 6145 -36 -986 -2579 O

ATOM 2969 CG2 THR B 195 -5.806 -20.353 65.624 1.00 49.95 C

ANISOU 2969 CG2 THR B 195 4333 8936 5709 -277 -1010 -3074 C ATOM 2970 N PRO B 196 -7.233 -17.182 64.088 1.00 51.11 N

ANISOU 2970 N PRO B 196 4722 8637 6061 -942 -206 -3040 N

ATOM 2971 CA PRO B 196 -6.571 -15.912 63.773 1.00 50.24 C

ANISOU 2971 CA PRO B 196 4512 8530 6045 -1247 -58 -3249 C

ATOM 2972 C PRO B 196 -5.204 -15.834 64.418 1.00 54.36 C ANISOU 2972 C PRO B 196 4749 9354 6552 -1307 -216 -3552 C

ATOM 2973 O PRO B 196 -5.059 -16.160 65.597 1.00 57.06 O

ANISOU 2973 O PRO B 196 5096 9817 6769 -1156 -420 -3599 O

ATOM 2974 CB PRO B 196 -7.502 -14.867 64.392 1.00 49.86 C

ANISOU 2974 CB PRO B 196 4724 8266 5955 -1342 36 -3220 C ATOM 2975 CG PRO B 196 -8.825 -15.559 64.531 1.00 47.13 C

ANISOU 2975 CG PRO B 196 4595 7785 5528 -1117 33 -2958 C

ATOM 2976 CD PRO B 196 -8.485 -16.981 64.835 1.00 46.80 C

ANISOU 2976 CD PRO B 196 4453 7933 5396 -885 -177 -2885 C

ATOM 2977 N ALA B 197 -4.210 -15.417 63.643 1.00 57.64 N ANISOU 2977 N ALA B 197 4959 9859 7081 -1490 -90 -3673 N

ATOM 2978 CA ALA B 197 -2.864 -15.238 64.164 1.00 61.78 C

ANISOU 2978 CA ALA B 197 5247 10616 7613 -1505 -163 -3876 C

ATOM 2979 C ALA B 197 -2.826 -14.038 65.108 1.00 66.47 C

ANISOU 2979 C ALA B 197 5950 11136 8170 -1685 -138 -3969 C ATOM 2980 O ALA B 197 -3.584 -13.081 64.944 1.00 65.83 O

ANISOU 2980 O ALA B 197 6095 10803 8114 -1880 11 -3907 O

ATOM 2981 CB ALA B 197 -1.876 -15.057 63.024 1.00 60.05 C

ANISOU 2981 CB ALA B 197 4808 10521 7487 -1676 15 -3979 C

ATOM 2982 N ARG B 198 -1.948 -14.096 66.102 1.00 70.71 N ANISOU 2982 N ARG B 198 6338 11875 8655 -1600 -303 -4127 N

ATOM 2983 CA ARG B 198 -1.799 -12.989 67.034 1.00 73.44 C

ANISOU 2983 CA ARG B 198 6759 12178 8966 -1762 -296 -4244 C

ATOM 2984 C ARG B 198 -1.132 -11.819 66.325 1.00 74.94 C ANISOU 2984 C ARG B 198 6889 12314 9272 -2114 -76 -4351 C

ATOM 2985 O ARG B 198 -0.296 -12.015 65.442 1.00 75.92 O

ANISOU 2985 O ARG B 198 6806 12584 9458 -2198 18 -4412 O

ATOM 2986 CB ARG B 198 -1.000 -13.425 68.261 1.00 77.21 C

ANISOU 2986 CB ARG B 198 7090 12899 9345 -1576 -549 -4380 C ATOM 2987 CG ARG B 198 -1.529 -14.710 68.872 1.00 78.61 C

ANISOU 2987 CG ARG B 198 7354 13131 9385 -1239 -796 -4237 C

ATOM 2988 CD ARG B 198 -0.773 -15.131 70.118 1.00 83.27 C

ANISOU 2988 CD ARG B 198 7857 13926 9856 -1061 -1077 -4339 C

ATOM 2989 NE ARG B 198 -1.189 -16.464 70.547 1.00 84.85 N ANISOU 2989 NE ARG B 198 8170 14149 9920 -754 -1336 -4163 N

ATOM 2990 CZ ARG B 198 -2.273 -16.712 71.277 1.00 84.61 C

ANISOU 2990 CZ ARG B 198 8425 14030 9692 -688 -1412 -3988 C

ATOM 2991 NH1 ARG B 198 -3.054 -15.715 71.671 1.00 85.21 N

ANISOU 2991 NH1 ARG B 198 8676 14000 9700 -872 -1241 -3998 N ATOM 2992 NH2 ARG B 198 -2.577 -17.959 71.616 1.00 83.18 N

ANISOU 2992 NH2 ARG B 198 8368 13861 9375 -441 -1657 -3805 N

ATOM 2993 N GLY B 199 -1.521 -10.604 66.700 1.00 73.69 N

ANISOU 2993 N GLY B 199 6931 11939 9127 -2321 2 -4374 N

ATOM 2994 CA GLY B 199 -1.013 -9.407 66.057 1.00 74.81 C ANISOU 2994 CA GLY B 199 7099 11958 9366 -2683 187 -4434 C

ATOM 2995 C GLY B 199 -1.503 -9.249 64.630 1.00 75.21 C

ANISOU 2995 C GLY B 199 7289 11802 9487 -2851 385 -4254 C

ATOM 2996 O GLY B 199 -0.869 -8.569 63.824 1.00 79.71 O

ANISOU 2996 O GLY B 199 7838 12346 10102 -3152 541 -4271 O ATOM 2997 N GLY B 200 -2.628 -9.884 64.311 1.00 69.76 N

ANISOU 2997 N GLY B 200 6749 10970 8785 -2669 377 -4075 N

ATOM 2998 CA GLY B 200 -3.215 -9.770 62.990 1.00 67.35 C

ANISOU 2998 CA GLY B 200 6603 10449 8536 -2804 545 -3888 C

ATOM 2999 C GLY B 200 -4.216 -8.634 62.897 1.00 69.73 C ANISOU 2999 C GLY B 200 7275 10320 8897 -2950 608 -3784 C

ATOM 3000 O GLY B 200 -4.337 -7.827 63.817 1.00 71.97 O

ANISOU 3000 O GLY B 200 7673 10482 9189 -2973 539 -3888 O

ATOM 3001 N ASP B 201 -4.937 -8.572 61.780 1.00 71.33 N

ANISOU 3001 N ASP B 201 7673 10285 9145 -3026 722 -3588 N ATOM 3002 CA ASP B 201 -5.936 -7.530 61.554 1.00 72.25 C

ANISOU 3002 CA ASP B 201 8170 9947 9337 -3121 752 -3474 C

ATOM 3003 C ASP B 201 -7.079 -7.640 62.564 1.00 68.96 C

ANISOU 3003 C ASP B 201 7890 9405 8908 -2829 638 -3517 C

ATOM 3004 O ASP B 201 -7.736 -8.673 62.649 1.00 67.20 O ANISOU 3004 O ASP B 201 7618 9289 8627 -2579 605 -3462 O

ATOM 3005 CB ASP B 201 -6.473 -7.617 60.119 1.00 70.60 C

ANISOU 3005 CB ASP B 201 8132 9536 9157 -3221 874 -3236 C

ATOM 3006 CG ASP B 201 -7.365 -6.441 59.747 1.00 71.87 C

ANISOU 3006 CG ASP B 201 8709 9190 9407 -3327 874 -3104 C ATOM 3007 OD1 ASP B 201 -7.366 -5.427 60.478 1.00 75.52 O

ANISOU 3007 OD1 ASP B 201 9312 9458 9925 -3380 794 -3213 O

ATOM 3008 OD2 ASP B 201 -8.057 -6.525 58.711 1.00 70.09 O

ANISOU 3008 OD2 ASP B 201 8678 8752 9201 -3341 931 -2893 O

ATOM 3009 N PRO B 202 -7.305 -6.576 63.349 1.00 70.36 N ANISOU 3009 N PRO B 202 8237 9373 9125 -2857 577 -3627 N

ATOM 3010 CA PRO B 202 -8.403 -6.593 64.323 1.00 69.55 C

ANISOU 3010 CA PRO B 202 8255 9184 8987 -2576 492 -3695 C

ATOM 3011 C PRO B 202 -9.786 -6.559 63.675 1.00 66.97 C

ANISOU 3011 C PRO B 202 8184 8536 8725 -2436 533 -3548 C ATOM 3012 O PRO B 202 -10.772 -6.926 64.317 1.00 65.86

ANISOU 3012 O PRO B 202 8082 8417 8525 -2164 498 -3581

ATOM 3013 CB PRO B 202 -8.161 -5.326 65.160 1.00 72.38

ANISOU 3013 CB PRO B 202 8722 9388 9393 -2676 423 -3871

ATOM 3014 CG PRO B 202 -7.271 -4.461 64.322 1.00 75.30

ANISOU 3014 CG PRO B 202 9151 9597 9861 -3034 478 -3827

ATOM 3015 CD PRO B 202 -6.430 -5.401 63.514 1.00 74.15

ANISOU 3015 CD PRO B 202 8753 9760 9660 -3138 573 -3733

ATOM 3016 N ARG B 203 -9.863 -6.133 62.421 1.00 66.14

ANISOU 3016 N ARG B 203 8252 8154 8722 -2619 606 -3379

ATOM 3017 CA ARG B 203 -11.148 -6.098 61.733 1.00 65.72

ANISOU 3017 CA ARG B 203 8448 7783 8741 -2469 625 -3227

ATOM 3018 C ARG B 203 -11.124 -6.755 60.348 1.00 60.61

ANISOU 3018 C ARG B 203 7798 7146 8083 -2522 719 -2938

ATOM 3019 O ARG B 203 -11.312 -6.080 59.337 1.00 60.77

ANISOU 3019 O ARG B 203 8068 6841 8182 -2697 745 -2790

ATOM 3020 CB ARG B 203 -11.655 -4.660 61.631 1.00 71.04

ANISOU 3020 CB ARG B 203 9455 7981 9556 -2522 549 -3236

ATOM 3021 CG ARG B 203 -12.041 -4.048 62.962 1.00 77.03

ANISOU 3021 CG ARG B 203 10233 8710 10323 -2336 442 -3475

ATOM 3022 CD ARG B 203 -13.235 -3.133 62.793 1.00 83.08

ANISOU 3022 CD ARG B 203 11312 9022 11232 -2159 345 -3476

ATOM 3023 NE ARG B 203 -14.384 -3.857 62.256 1.00 84.67

ANISOU 3023 NE ARG B 203 11545 9185 11441 -1903 389 -3353

ATOM 3024 CZ ARG B 203 -15.454 -4.194 62.969 1.00 86.06

ANISOU 3024 CZ ARG B 203 11651 9465 11581 -1562 375 -3467

ATOM 3025 NH1 ARG B 203 -15.529 -3.860 64.251 1.00 89.91

ANISOU 3025 NH1 ARG B 203 12051 10104 12006 -1442 323 -3697

ATOM 3026 NH2 ARG B 203 -16.453 -4.855 62.399 1.00 82.61

ANISOU 3026 NH2 ARG B 203 11220 9022 11146 -1333 410 -3302

ATOM 3027 N PRO B 204 -10.913 -8.082 60.304 1.00 55.25

ANISOU 3027 N PRO B 204 6862 6830 7300 -2363 752 -2858

ATOM 3028 CA PRO B 204 -10.790 -8.799 59.030 1.00 52.38

ANISOU 3028 CA PRO B 204 6454 6533 6916 -2405 841 -2634

ATOM 3029 C PRO B 204 -12.109 -8.821 58.275 1.00 52.44

ANISOU 3029 C PRO B 204 6707 6248 6968 -2213 845 -2397

ATOM 3030 O PRO B 204 -13.169 -8.615 58.867 1.00 52.46

ANISOU 3030 O PRO B 204 6832 6094 7007 -1967 777 -2417

ATOM 3031 CB PRO B 204 -10.421 -10.217 59.465 1.00 49.45

ANISOU 3031 CB PRO B 204 5770 6576 6442 -2192 814 -2657

ATOM 3032 CG PRO B 204 -11.037 -10.353 60.816 1.00 48.80

ANISOU 3032 CG PRO B 204 5689 6541 6310 -1939 712 -2760

ATOM 3033 CD PRO B 204 -10.861 -9.002 61.453 1.00 51.75

ANISOU 3033 CD PRO B 204 6190 6728 6744 -2120 683 -2969

ATOM 3034 N THR B 205 -12.037 -9.073 56.974 1.00 52.90

ANISOU 3034 N THR B 205 6818 6267 7015 -2327 923 -2197

ATOM 3035 CA THR B 205 -13.224 -9.096 56.136 1.00 52.18

ANISOU 3035 CA THR B 205 6957 5909 6959 -2161 909 -1968

ATOM 3036 C THR B 205 -13.328 -10.446 55.443 1.00 49.35

ANISOU 3036 C THR B 205 6428 5798 6524 -2012 966 -1815

ATOM 3037 O THR B 205 -12.475 -10.800 54.634 1.00 49.86

ANISOU 3037 O THR B 205 6375 6041 6527 -2215 1055 -1779

ATOM 3038 CB THR B 205 -13.190 -7.968 55.087 1.00 57.91

ANISOU 3038 CB THR B 205 8006 6268 7730 -2458 917 -1840

ATOM 3039 OG1 THR B 205 -12.922 -6.718 55.735 1.00 65.99

ANISOU 3039 OG1 THR B 205 9191 7046 8836 -2638 849 -2004

ATOM 3040 CG2 THR B 205 -14.514 -7.868 54.372 1.00 56.55

ANISOU 3040 CG2 THR B 205 8094 5784 7607 -2237 845 -1632

ATOM 3041 N PHE B 206 -14.367 -11.203 55.780 1.00 46.86 ANISOU 3041 N PHE B 206 6086 5509 6207 -1670 917 -1749

ATOM 3042 CA PHE B 206 -14.598 -12.512 55.182 1, 00 42. 57

ANISOU 3042 CA PHE B 206 5410 5156 5607 -1507 944 -1607

ATOM 3043 C PHE B 206 -15.772 -12.461 54. 220 1, 00 44.

ANISOU 3043 C PHE B 206 5913 5203 5935 -1387 934 -1402

ATOM 3044 O PHE B 206 -16.736 -11.738 54.442 1, 00 36. 36

ANISOU 3044 O PHE B 206 5023 3862 4931 -1273 868 -1396

ATOM 3045 CB PHE B 206 -14.917 -13.555 56.248 1, 00 37. 27

ANISOU 3045 CB PHE B 206 4563 4710 4889 -1239 883 -1662

ATOM 3046 CG PHE B 206 -13.827 -13.765 57.254 1, 00 41. 20

ANISOU 3046 CG PHE B 206 4853 5468 5333 -1300 846 -1855

ATOM 3047 CD1 PHE B 206 -12.889 -14.767 57.076 1, 00 41. 50

ANISOU 3047 CD1 PHE B 206 4659 5786 5322 -1299 832 -1886

ATOM 3048 CD2 PHE B 206 -13.763 -12.984 58.405 1, 00 42. 31

ANISOU 3048 CD2 PHE B 206 5022 5580 5473 -1331 801 -2030

ATOM 3049 CE1 PHE B 206 -11.898 -14.976 58.017 1, 00 44. 94

ANISOU 3049 CE1 PHE B 206 4898 6465 5714 -1321 757 -2077

ATOM 3050 CE2 PHE B 206 -12.779 -13.187 59. 342 1, 00 38. 41

ANISOU 3050 CE2 PHE B 206 4340 5338 4916 -1378 744 -2211

ATOM 3051 CZ PHE B 206 -11.843 -14.183 59.153 1, 00 38. 17

ANISOU 3051 CZ PHE B 206 4081 5582 4841 -1369 712 -2229

ATOM 3052 N SER B 207 -15.701 -13.257 53.160 1, 00 44. 36

ANISOU 3052 N SER B 207 5797 5240 5819 -1390 983 -1261

ATOM 3053 CA SER B 207 -16.807 -13.353 52. 221 1, 00 42. 13

ANISOU 3053 CA SER B 207 5689 4766 5554 -1261 958 -1069

ATOM 3054 C SER B 207 -16.851 -14.744 51.599 1, 00 42. 48

ANISOU 3054 C SER B 207 5568 5034 5536 -1139 988 -981

ATOM 3055 O SER B 207 -15.854 -15.471 51.599 1, 00 43. 15

ANISOU 3055 O SER B 207 5437 5390 5569 -1206 1034 -1062

ATOM 3056 CB SER B 207 -16.673 -12.294 51.130 1, 00 39. 75

ANISOU 3056 CB SER B 207 5655 4202 5244 -1515 970 -952

ATOM 3057 OG SER B 207 -15.614 -12.626 50.251 1, 00 40. 08

ANISOU 3057 OG SER B 207 5602 4450 5178 -1776 1085 -924

ATOM 3058 N CYS B 208 -18.015 -15.102 51.064 1, 00 39. 42

ANISOU 3058 N CYS B 208 5278 4532 5170 -949 944 -841

ATOM 3059 CA CYS B 208 -18.214 -16.388 50.410 1, 00 33. 21

ANISOU 3059 CA CYS B 208 4371 3909 4338 -827 955 -757

ATOM 3060 C CYS B 208 -18.602 -16.175 48.955 1, 00 35. 17

ANISOU 3060 C CYS B 208 4792 4023 4547 -896 966 -595

ATOM 3061 O CYS B 208 -19.238 -15.180 48.619 1, 00 39. 48

ANISOU 3061 O CYS B 208 5578 4297 5126 -919 912 -512

ATOM 3062 CB CYS B 208 -19.313 -17.179 51.130 1, 00 30. 13

ANISOU 3062 CB CYS B 208 3918 3544 3985 -551 887 -741

ATOM 3063 SG CYS B 208 -19.766 -18.751 50. 343 1, 00 41. 74

ANISOU 3063 SG CYS B 208 5288 5146 5425 -398 868 -631

ATOM 3064 N SER B 209 -18.230 -17.107 48. 086 1, 00 33. 52

ANISOU 3064 N SER B 209 4473 3999 4264 -916 1014 -561

ATOM 3065 CA SER B 209 -18.644 -17.013 46.696 1, 00 35. 21

ANISOU 3065 CA SER B 209 4848 4122 4406 -976 1020 -408

ATOM 3066 C SER B 209 -19.018 -18.367 46.105 1, 00 35. 05

ANISOU 3066 C SER B 209 4698 4260 4360 -803 1007 -379

ATOM 3067 O SER B 209 -18.466 -19.398 46.491 1, 00 33.

ANISOU 3067 O SER B 209 4244 4255 4145 -725 1020 -493

ATOM 3068 CB SER B 209 -17.558 -16.348 45.853 1, 00 39. 53

ANISOU 3068 CB SER B 209 5466 4725 4828 -1329 1129 -401

ATOM 3069 OG SER B 209 -16.410 -17.165 45.798 1, 00 43. 67

ANISOU 3069 OG SER B 209 5707 5591 5294 -1412 1230 -558

ATOM 3070 N PHE B 210 -19.965 -18.352 45.167 1, 00 36. 60

ANISOU 3070 N PHE B 210 5054 4324 4529 -735 953 -235 ATOM 3071 CA PHE B 210 -20.403 -19.567 44.484 1.00 33.92

ANISOU 3071 CA PHE B 210 4618 4106 4163 -588 930 -209

ATOM 3072 C PHE B 210 -19.761 -19.672 43.111 1.00 34.01

ANISOU 3072 C PHE B 210 4659 4249 4014 -779 1010 -183

ATOM 3073 O PHE B 210 -19.812 -18.730 42.328 1.00 36.58

ANISOU 3073 O PHE B 210 5214 4446 4238 -962 1020 -62

ATOM 3074 CB PHE B 210 -21.930 -19.607 44.344 1.00 31.29

ANISOU 3074 CB PHE B 210 4400 3591 3897 -376 809 -99

ATOM 3075 CG PHE B 210 -22.425 -20.726 43.461 1.00 32.93

ANISOU 3075 CG PHE B 210 4548 3898 4068 -266 777 -63

ATOM 3076 CD1 PHE B 210 -22.675 -21.985 43.988 1.00 32.04

ANISOU 3076 CD1 PHE B 210 4250 3899 4025 -105 748 -130

ATOM 3077 CD2 PHE B 210 -22.630 -20.524 42.102 1.00 32.13

ANISOU 3077 CD2 PHE B 210 4596 3765 3848 -342 761 40

ATOM 3078 CE1 PHE B 210 -23.113 -23.018 43.175 1.00 30.70

ANISOU 3078 CE1 PHE B 210 4035 3797 3833 -16 705 -114

ATOM 3079 CE2 PHE B 210 -23.069 -21.550 41.285 1.00 29.98

ANISOU 3079 CE2 PHE B 210 4262 3592 3536 -245 726 47

ATOM 3080 CZ PHE B 210 -23.309 -22.799 41.816 1.00 28.39

ANISOU 3080 CZ PHE B 210 3865 3491 3429 -78 698 -40

ATOM 3081 N SER B 211 -19.161 -20.820 42.822 1.00 35.56

ANISOU 3081 N SER B 211 4635 4698 4177 -741 1056 -305

ATOM 3082 CA SER B 211 -18.566 -21.072 41.510 1.00 36.57

ANISOU 3082 CA SER B 211 4740 5019 4135 -906 1149 -334

ATOM 3083 C SER B 211 -19.360 -22.147 40.794 1.00 36.64

ANISOU 3083 C SER B 211 4725 5056 4140 -706 1072 -311

ATOM 3084 O SER B 211 -19.413 -23.293 41.249 1.00 36.12

ANISOU 3084 O SER B 211 4477 5067 4181 -499 1012 -419

ATOM 3085 CB SER B 211 -17.114 -21.528 41.639 1.00 38.51

ANISOU 3085 CB SER B 211 4708 5580 4345 -1019 1263 -570

ATOM 3086 OG SER B 211 -16.326 -20.537 42.269 1.00 46.04

ANISOU 3086 OG SER B 211 5665 6533 5297 -1235 1338 -611

ATOM 3087 N PRO B 212 -19.989 -21.780 39.671 1.00 35.98

ANISOU 3087 N PRO B 212 4848 4893 3928 -775 1051 -164

ATOM 3088 CA PRO B 212 -20.778 -22.730 38.878 1.00 36.72

ANISOU 3088 CA PRO B 212 4932 5019 4002 -608 972 -148

ATOM 3089 C PRO B 212 -19.945 -23.936 38.436 1.00 39.59

ANISOU 3089 C PRO B 212 5045 5678 4321 -583 1038 -366

ATOM 3090 O PRO B 212 -20.489 -25.024 38.235 1.00 41.56

ANISOU 3090 O PRO B 212 5213 5941 4635 -382 948 -418

ATOM 3091 CB PRO B 212 -21.197 -21.902 37.658 1.00 37.24

ANISOU 3091 CB PRO B 212 5276 5002 3873 -771 958 31

ATOM 3092 CG PRO B 212 -21.136 -20.486 38.122 1.00 39.46

ANISOU 3092 CG PRO B 212 5771 5061 4161 -924 953 161

ATOM 3093 CD PRO B 212 -20.004 -20.422 39.101 1.00 35.59

ANISOU 3093 CD PRO B 212 5085 4695 3742 -1022 1074 4

ATOM 3094 N GLY B 213 -18.640 -23.747 38.285 1.00 42.34

ANISOU 3094 N GLY B 213 5259 6263 4566 -787 1185 -516

ATOM 3095 CA GLY B 213 -17.783 -24.808 37.791 1.00 54.35

ANISOU 3095 CA GLY B 213 6515 8094 6041 -753 1244 -778

ATOM 3096 C GLY B 213 -17.875 -24.952 36.282 1.00 64.90

ANISOU 3096 C GLY B 213 7918 9596 7145 -877 1309 -784

ATOM 3097 O GLY B 213 -16.866 -25.171 35.613 1.00 70.73

ANISOU 3097 O GLY B 213 8481 10665 7729 -1033 1452 -996

ATOM 3098 N LEU B 214 -19.091 -24.831 35.752 1.00 67.34

ANISOU 3098 N LEU B 214 8464 9703 7420 -808 1201 -573

ATOM 3099 CA LEU B 214 -19.324 -24.839 34.315 1.00 70.24

ANISOU 3099 CA LEU B 214 8955 10197 7536 -936 1233 -533

ATOM 3100 C LEU B 214 -18.559 -23.689 33.652 1.00 74.67 ANISOU 3100 C LEU B 214 9661 10894 7815 -1343 1404 -454 C

ATOM 3101 0 LEU B 214 -18.599 -22.557 34.136 1.00 77.57 0

ANISOU 3101 0 LEU B 214 10225 11052 8195 -1491 1403 -266 0

ATOM 3102 CB LEU B 214 -20.822 -24.722 34.031 1.00 69.63 C ANISOU 3102 CB LEU B 214 9123 9840 7492 -783 1050 -299 C

ATOM 3103 CG LEU B 214 -21.364 -25.572 32.880 1.00 73.09 C

ANISOU 3103 CG LEU B 214 9564 10396 7811 -697 986 -355 C

ATOM 3104 CD1 LEU B 214 -21.193 -27.050 33.183 1.00 74.09 C

ANISOU 3104 CD1 LEU B 214 9404 10632 8116 -453 946 -619 C ATOM 3105 CD2 LEU B 214 -22.821 -25.250 32.613 1.00 72.90 C

ANISOU 3105 CD2 LEU B 214 9781 10105 7811 -572 795 -122 C

ATOM 3106 N PRO B 215 -17.852 -23.984 32.547 1.00 74.94 N

ANISOU 3106 N PRO B 215 9602 11285 7586 -1543 1553 -610 N

ATOM 3107 CA PRO B 215 -16.978 -23.047 31.827 1.00 78.27 C ANISOU 3107 CA PRO B 215 10123 11911 7705 -1988 1741 -571 C

ATOM 3108 C PRO B 215 -17.594 -21.676 31.537 1.00 78.57 C

ANISOU 3108 C PRO B 215 10622 11650 7580 -2234 1685 -187 C

ATOM 3109 O PRO B 215 -18.708 -21.589 31.021 1.00 79.69 O

ANISOU 3109 O PRO B 215 11029 11572 7675 -2114 1513 26 O ATOM 3110 CB PRO B 215 -16.692 -23.782 30.515 1.00 79.87 C

ANISOU 3110 CB PRO B 215 10206 12410 7732 -2011 1766 -740 C

ATOM 3111 CG PRO B 215 -16.749 -25.215 30.889 1.00 77.73 C

ANISOU 3111 CG PRO B 215 9617 12248 7669 -1640 1710 -1032 C

ATOM 3112 CD PRO B 215 -17.823 -25.329 31.943 1.00 73.62 C ANISOU 3112 CD PRO B 215 9204 11356 7412 -1346 1538 -870 C

ATOM 3113 N ARG B 216 -16.853 -20.626 31.886 1.00 77.39 N

ANISOU 3113 N ARG B 216 10542 11425 7438 -2497 1741 -121 N

ATOM 3114 CA ARG B 216 -17.212 -19.236 31.589 1.00 76.48 C

ANISOU 3114 CA ARG B 216 10867 10996 7198 -2747 1654 212 C ATOM 3115 C ARG B 216 -18.446 -18.694 32.313 1.00 70.18 C

ANISOU 3115 C ARG B 216 10382 9736 6548 -2556 1467 478 C

ATOM 3116 O ARG B 216 -18.886 -17.577 32.040 1.00 72.89 O

ANISOU 3116 O ARG B 216 11123 9759 6813 -2697 1332 754 O

ATOM 3117 CB ARG B 216 -17.335 -18.999 30.079 1.00 79.70 C ANISOU 3117 CB ARG B 216 11491 11483 7306 -2945 1619 337 C

ATOM 3118 CG ARG B 216 -16.004 -18.873 29.356 1.00 83.19 C

ANISOU 3118 CG ARG B 216 11756 12275 7577 -3277 1785 155 C

ATOM 3119 CD ARG B 216 -16.228 -18.658 27.871 1.00 86.25 C

ANISOU 3119 CD ARG B 216 12381 12739 7652 -3478 1750 292 C ATOM 3120 NE ARG B 216 -17.238 -19.577 27.361 1.00 84.67 N

ANISOU 3120 NE ARG B 216 12195 12560 7415 -3188 1653 307 N

ATOM 3121 CZ ARG B 216 -16.977 -20.793 26.892 1.00 85.68 C

ANISOU 3121 CZ ARG B 216 11997 13040 7516 -3052 1740 24 C

ATOM 3122 NH1 ARG B 216 -15.727 -21.241 26.853 1.00 88.14 N ANISOU 3122 NH1 ARG B 216 11935 13707 7847 -3162 1911 -298 N

ATOM 3123 NH2 ARG B 216 -17.967 -21.561 26.454 1.00 82.77 N

ANISOU 3123 NH2 ARG B 216 11679 12661 7109 -2797 1630 43 N

ATOM 3124 N HIS B 217 -19.007 -19.473 33.228 1.00 62.72 N

ANISOU 3124 N HIS B 217 9206 8698 5928 -2129 1359 354 N ATOM 3125 CA HIS B 217 -20.098 -18.959 34.048 1.00 62.85 C

ANISOU 3125 CA HIS B 217 9400 8284 6196 -1860 1136 517 C

ATOM 3126 C HIS B 217 -19.505 -18.166 35.207 1.00 64.59 C

ANISOU 3126 C HIS B 217 9601 8369 6573 -1961 1188 491 C

ATOM 3127 O HIS B 217 -18.515 -18.581 35.807 1.00 65.71 O ANISOU 3127 O HIS B 217 9436 8755 6776 -2018 1347 270 O

ATOM 3128 CB HIS B 217 -21.012 -20.084 34.547 1.00 54.69 C

ANISOU 3128 CB HIS B 217 8147 7223 5411 -1417 1010 409 C

ATOM 3129 CG HIS B 217 -21.897 -20.661 33.485 1.00 53.17 C

ANISOU 3129 CG HIS B 217 8039 7058 5104 -1287 893 472 C ATOM 3130 ND1 HIS B 217 -23.006 -21.428 33.775 1.00 51.38

ANISOU 3130 ND1 HIS B 217 7715 6730 5079 -931 734 442

ATOM 3131 CD2 HIS B 217 -21.838 -20.585 32.135 1.00 55.66

ANISOU 3131 CD2 HIS B 217 8527 7509 5109 -1486 911 555

ATOM 3132 CE1 HIS B 217 -23.591 -21.800 32.651 1.00 49.34

ANISOU 3132 CE1 HIS B 217 7553 6535 4660 -900 648 493

ATOM 3133 NE2 HIS B 217 -22.902 -21.302 31.640 1.00 53.92

ANISOU 3133 NE2 HIS B 217 8306 7260 4922 -1224 749 565

ATOM 3134 N ARG B 218 -20.097 -17.018 35.511 1.00 64.84

ANISOU 3134 N ARG B 218 9957 8009 6670 -1971 1035 695

ATOM 3135 CA ARG B 218 -19. 509 -16.125 36.500 1.00 67.65

ANISOU 3135 CA ARG B 218 10344 8216 7144 -2115 1077 672

ATOM 3136 C ARG B 218 -19. 905 -16.458 37.937 1.00 62.28

ANISOU 3136 C ARG B 218 9435 7441 6787 -1765 1011 527

ATOM 3137 O ARG B 218 -20.988 -16.985 38.197 1.00 61.02

ANISOU 3137 O ARG B 218 9225 7181 6780 -1411 869 530

ATOM 3138 CB ARG B 218 -19.807 -14.658 36.164 1.00 76.43

ANISOU 3138 CB ARG B 218 11939 8933 8169 -2329 936 935

ATOM 3139 CG ARG B 218 -21.276 -14.340 35.944 1.00 81.86

ANISOU 3139 CG ARG B 218 12900 9251 8950 -2012 640 1112

ATOM 3140 CD ARG B 218 -21.871 -13.614 37.143 1.00 86.34

ANISOU 3140 CD ARG B 218 13529 9461 9815 -1771 478 1084

ATOM 3141 NE ARG B 218 -22. 510 -12.354 36.762 1.00 91.72

ANISOU 3141 NE ARG B 218 14688 9684 10479 -1798 221 1310

ATOM 3142 CZ ARG B 218 -21. 940 -11.156 36.870 1.00 94.42

ANISOU 3142 CZ ARG B 218 15333 9764 10778 -2100 193 1412

ATOM 3143 NH1 ARG B 218 -20.711 -11.041 37.356 1.00 94.27

ANISOU 3143 NH1 ARG B 218 15149 9941 10727 -2412 428 1292

ATOM 3144 NH2 ARG B 218 -22.605 -10.071 36.496 1.00 96.54

ANISOU 3144 NH2 ARG B 218 15923 9674 11082 -2001 -96 1548

ATOM 3145 N ALA B 219 -19.003 -16.146 38.861 1.00 58.84

ANISOU 3145 N ALA B 219 8857 7066 6433 -1896 1121 394

ATOM 3146 CA ALA B 219 -19.222 -16.376 40.280 1.00 55.37

ANISOU 3146 CA ALA B 219 8218 6567 6252 -1627 1074 256

ATOM 3147 C ALA B 219 -20.190 -15.362 40.887 1.00 55.60

ANISOU 3147 C ALA B 219 8503 6186 6435 -1479 890 364

ATOM 3148 O ALA B 219 -20.263 -14.215 40.449 1.00 58.83

ANISOU 3148 O ALA B 219 9254 6325 6775 -1667 813 520

ATOM 3149 CB ALA B 219 -17.893 -16.349 41.028 1.00 53.56

ANISOU 3149 CB ALA B 219 7754 6558 6039 -1821 1234 62

ATOM 3150 N LEU B 220 -20.937 -15.804 41.892 1.00 52.99

ANISOU 3150 N LEU B 220 8014 5814 6307 -1146 811 269

ATOM 3151 CA LEU B 220 -21.768 -14.916 42.689 1.00 54.67

ANISOU 3151 CA LEU B 220 8376 5709 6687 -977 660 279

ATOM 3152 C LEU B 220 -21.084 -14.747 44.043 1.00 52.83

ANISOU 3152 C LEU B 220 7968 5545 6562 -1008 741 102

ATOM 3153 O LEU B 220 -20.457 -15.679 44.535 1.00 47.59

ANISOU 3153 O LEU B 220 7015 5170 5896 -993 854 -28

ATOM 3154 CB LEU B 220 -23.173 -15.497 42.869 1.00 56.70

ANISOU 3154 CB LEU B 220 8556 5919 7068 -604 527 270

ATOM 3155 CG LEU B 220 -24.102 -15.650 41.659 1.00 61.01

ANISOU 3155 CG LEU B 220 9259 6378 7544 -499 394 419

ATOM 3156 CD1 LEU B 220 -23.814 -16.935 40.893 1.00 59.99

ANISOU 3156 CD1 LEU B 220 8951 6554 7288 -531 498 417

ATOM 3157 CD2 LEU B 220 -25.564 -15.603 42.093 1.00 60.66

ANISOU 3157 CD2 LEU B 220 9191 6184 7673 -149 218 377

ATOM 3158 N ARG B 221 -21.199 -13.566 44.643 1.00 56.26

ANISOU 3158 N ARG B 221 8585 5702 7087 -1039 660 85

ATOM 3159 CA ARG B 221 -20.465 -13.268 45.872 1.00 58.50 ANISOU 3159 CA ARG B 221 8732 6047 7447 -1112 731 -89 C

ATOM 3160 C ARG B 221 -21.393 -12.775 46.980 1.00 57.11 C

ANISOU 3160 C ARG B 221 8571 5681 7448 -844 609 -200 C

ATOM 3161 O ARG B 221 -22.320 -12.007 46.717 1.00 61.80 O ANISOU 3161 O ARG B 221 9397 5967 8118 -711 445 -141 O

ATOM 3162 CB ARG B 221 -19.390 -12.219 45.586 1.00 66.18 C

ANISOU 3162 CB ARG B 221 9896 6911 8338 -1506 786 -58 C

ATOM 3163 CG ARG B 221 -18.341 -12.071 46.672 1.00 72.59 C

ANISOU 3163 CG ARG B 221 10513 7878 9189 -1650 890 -255 C ATOM 3164 CD ARG B 221 -16.946 -12.232 46.085 1.00 79.19 C

ANISOU 3164 CD ARG B 221 11241 8983 9865 -2029 1066 -278 C

ATOM 3165 NE ARG B 221 -15.896 -11.870 47.032 1.00 85.49 N

ANISOU 3165 NE ARG B 221 11883 9900 10700 -2212 1141 -471 N

ATOM 3166 CZ ARG B 221 -14.594 -11.911 46.759 1.00 90.06 C ANISOU 3166 CZ ARG B 221 12304 10748 11165 -2551 1296 -564 C

ATOM 3167 NH1 ARG B 221 -14.175 -12.305 45.562 1.00 91.19 N

ANISOU 3167 NH1 ARG B 221 12424 11087 11138 -2751 1411 -487 N

ATOM 3168 NH2 ARG B 221 -13.708 -11.559 47.682 1.00 92.05 N

ANISOU 3168 NH2 ARG B 221 12403 11107 11466 -2695 1339 -759 N ATOM 3169 N THR B 222 -21.151 -13.214 48.217 1.00 48.51 N

ANISOU 3169 N THR B 222 7232 4785 6414 -757 674 -377 N

ATOM 3170 CA THR B 222 -21.952 -12.742 49.342 1.00 44.76 C

ANISOU 3170 CA THR B 222 6741 4193 6072 -537 590 -522 C

ATOM 3171 C THR B 222 -21.494 -11.370 49.779 1.00 45.71 C ANISOU 3171 C THR B 222 7056 4056 6254 -688 538 -606 C

ATOM 3172 O THR B 222 -20.401 -10.926 49.431 1.00 48.49 O

ANISOU 3172 O THR B 222 7501 4385 6537 -1000 600 -566 O

ATOM 3173 CB THR B 222 -21.835 -13.636 50.597 1.00 41.71 C

ANISOU 3173 CB THR B 222 6054 4110 5682 -428 671 -676 C ATOM 3174 OG1 THR B 222 -20.537 -13.474 51.187 1.00 40.18 O

ANISOU 3174 OG1 THR B 222 5780 4042 5445 -644 753 -775 O

ATOM 3175 CG2 THR B 222 -22.102 -15.099 50.274 1.00 37.54 C

ANISOU 3175 CG2 THR B 222 5340 3831 5094 -321 717 -599 C

ATOM 3176 N ALA B 223 -22.335 -10.706 50.560 1.00 47.34 N ANISOU 3176 N ALA B 223 7311 4086 6591 -474 427 -750 N

ATOM 3177 CA ALA B 223 -21.926 -9.503 51.263 1.00 52.53 C

ANISOU 3177 CA ALA B 223 8109 4521 7329 -576 371 -897 C

ATOM 3178 C ALA B 223 -20.930 -9.912 52.347 1.00 51.25 C

ANISOU 3178 C ALA B 223 7698 4667 7107 -707 514 -1054 C ATOM 3179 O ALA B 223 -21.059 -10.984 52.938 1.00 47.48 O

ANISOU 3179 O ALA B 223 6953 4512 6575 -579 596 -1106 O

ATOM 3180 CB ALA B 223 -23.135 -8.818 51.872 1.00 55.89 C

ANISOU 3180 CB ALA B 223 8593 4731 7912 -261 213 -1070 C

ATOM 3181 N PRO B 224 -19.928 -9.065 52.608 1.00 54.52 N ANISOU 3181 N PRO B 224 8214 4974 7525 -976 527 -1127 N

ATOM 3182 CA PRO B 224 -18.878 -9.401 53.580 1.00 56.67 C

ANISOU 3182 CA PRO B 224 8250 5545 7736 -1115 639 -1287 C

ATOM 3183 C PRO B 224 -19.365 -9.461 55.031 1.00 55.72 C

ANISOU 3183 C PRO B 224 7970 5550 7653 -889 617 -1521 C ATOM 3184 O PRO B 224 -20.414 -8.917 55.367 1.00 56.83 O

ANISOU 3184 O PRO B 224 8200 5502 7891 -666 520 -1619 O

ATOM 3185 CB PRO B 224 -17.894 -8.238 53.434 1.00 59.68 C

ANISOU 3185 CB PRO B 224 8826 5710 8138 -1463 627 -1321 C

ATOM 3186 CG PRO B 224 -18.741 -7.092 52.974 1.00 61.03 C ANISOU 3186 CG PRO B 224 9361 5396 8430 -1395 455 -1265 C

ATOM 3187 CD PRO B 224 -19.737 -7.722 52.034 1.00 58.29 C

ANISOU 3187 CD PRO B 224 9053 5028 8066 -1174 414 -1067 C

ATOM 3188 N ILE B 225 -18.595 -10.134 55.879 1.00 51.63 N

ANISOU 3188 N ILE B 225 7209 5367 7041 -947 699 -1625 N ATOM 3189 CA ILE B 225 -18.797 -10.055 57.314 1.00 52.68

ANISOU 3189 CA ILE B 225 7219 5638 7159 -822 684 -1855

ATOM 3190 C ILE B 225 -17.521 -9.534 57.959 1.00 57.22

ANISOU 3190 C ILE B 225 7749 6283 7709 -1068 698 -2016

ATOM 3191 O ILE B 225 -16.418 -9.934 57.585 1.00 60.28

ANISOU 3191 O ILE B 225 8035 6833 8036 -1276 755 -1958

ATOM 3192 CB ILE B 225 -19.192 -11.408 57.922 1.00 48.96

ANISOU 3192 CB ILE B 225 6516 5518 6569 -643 731 -1832

ATOM 3193 CGI ILE B 225 -18.186 -12.485 57.522 1.00 45.71

ANISOU 3193 CGI ILE B 225 5954 5350 6063 -762 783 -1705

ATOM 3194 CG2 ILE B 225 -20.610 -11.782 57.492 1.00 50.49

ANISOU 3194 CG2 ILE B 225 6736 5649 6799 -404 715 -1737

ATOM 3195 CD1 ILE B 225 -18.606 -13.881 57.899 1.00 45.38

ANISOU 3195 CD1 ILE B 225 5753 5572 5919 -595 790 -1627

ATOM 3196 N GLN B 226 -17.671 -8.621 58.912 1.00 57.38

ANISOU 3196 N GLN B 226 7827 6193 7780 -1043 640 -2248

ATOM 3197 CA GLN B 226 -16.519 -7.977 59.528 1.00 59.43

ANISOU 3197 CA GLN B 226 8065 6485 8032 -1288 634 -2428

ATOM 3198 C GLN B 226 -16.566 -8.104 61.040 1.00 56.56

ANISOU 3198 C GLN B 226 7540 6369 7582 -1171 618 -2677

ATOM 3199 O GLN B 226 -17.019 -7.195 61.726 1.00 56.02

ANISOU 3199 O GLN B 226 7567 6142 7578 -1100 557 -2897

ATOM 3200 CB GLN B 226 -16.473 -6.500 59.145 1.00 66.29

ANISOU 3200 CB GLN B 226 9228 6907 9052 -1450 551 -2489

ATOM 3201 CG GLN B 226 -16.759 -6.236 57.681 1.00 70.55

ANISOU 3201 CG GLN B 226 10009 7137 9658 -1529 530 -2227

ATOM 3202 CD GLN B 226 -16.369 -4.836 57.265 1.00 77.64

ANISOU 3202 CD GLN B 226 11232 7600 10669 -1799 438 -2244

ATOM 3203 OE1 GLN B 226 -15.730 -4.103 58.026 1.00 79.49

ANISOU 3203 OE1 GLN B 226 11481 7782 10938 -1966 409 -2460

ATOM 3204 NE2 GLN B 226 -16.749 -4.454 56.049 1.00 80.06

ANISOU 3204 NE2 GLN B 226 11822 7575 11021 -1860 376 -2010

ATOM 3205 N PRO B 227 -16.102 -9.242 61.565 1.00 54.25

ANISOU 3205 N PRO B 227 7016 6463 7133 -1143 656 -2651

ATOM 3206 CA PRO B 227 -16.126 -9.451 63.012 1.00 52.76

ANISOU 3206 CA PRO B 227 6696 6540 6808 -1054 630 -2854

ATOM 3207 C PRO B 227 -14.976 -8.718 63.676 1.00 55.73

ANISOU 3207 C PRO B 227 7036 6958 7180 -1270 586 -3082

ATOM 3208 O PRO B 227 -14.064 -8.247 62.993 1.00 60.75

ANISOU 3208 O PRO B 227 7707 7471 7905 -1512 592 -3061

ATOM 3209 CB PRO B 227 -15.926 -10.958 63.143 1.00 51.32

ANISOU 3209 CB PRO B 227 6334 6697 6466 -975 643 -2691

ATOM 3210 CG PRO B 227 -15.108 -11.318 61.947 1.00 51.28

ANISOU 3210 CG PRO B 227 6298 6658 6529 -1113 667 -2518

ATOM 3211 CD PRO B 227 -15.602 -10.423 60.840 1.00 51.89

ANISOU 3211 CD PRO B 227 6585 6364 6768 -1171 700 -2434

ATOM 3212 N ARG B 228 -15.038 -8.618 64.998 1.00 52.17

ANISOU 3212 N ARG B 228 6513 6699 6610 -1205 547 -3307

ATOM 3213 CA ARG B 228 -13.975 -8.025 65.790 1.00 53.89

ANISOU 3213 CA ARG B 228 6668 7012 6796 -1391 488 -3552

ATOM 3214 C ARG B 228 -13.057 -9.154 66.254 1.00 53.49

ANISOU 3214 C ARG B 228 6394 7361 6568 -1413 447 -3504

ATOM 3215 O ARG B 228 -13.533 -10.236 66.600 1.00 50.38

ANISOU 3215 O ARG B 228 5935 7188 6021 -1235 439 -3374

ATOM 3216 CB ARG B 228 -14.576 -7.302 67.001 1.00 56.17

ANISOU 3216 CB ARG B 228 6998 7310 7033 -1271 447 -3790

ATOM 3217 CG ARG B 228 -15.682 -6.314 66.664 1.00 57.74

ANISOU 3217 CG ARG B 228 7396 7139 7405 -1140 445 -3838

ATOM 3218 CD ARG B 228 -16.114 -5.495 67.874 1.00 59.27 ANISOU 3218 CD ARG B 228 7601 7359 7560 -1021 390 -4069

ATOM 3219 NE ARG B 228 -16.900 -6.264 68.839 1, 00 57. 49 )

ANISOU 3219 NE ARG B 228 7236 7492 7118 -833 439 -4100

ATOM 3220 CZ ARG B 228 -17.502 -5.738 69.903 1, 00 56. 79 )

ANISOU 3220 CZ ARG B 228 7122 7499 6957 -710 426 -4293

ATOM 3221 NH1 ARG B 228 -17.415 -4.438 70.149 1, 00 59. 777

ANISOU 3221 NH1 ARG B 228 7612 7619 7478 -717 346 -4492

ATOM 3222 NH2 ARG B 228 -18.196 -6.513 70.722 1, 00 56. 441

ANISOU 3222 NH2 ARG B 228 6949 7807 6688 -598 490 -4287

ATOM 3223 N VAL B 229 -11.749 -8.916 66.255 1, 00 49. 3

ANISOU 3223 N VAL B 229 5825 6992 6134 -1632 403 -3614

ATOM 3224 CA VAL B 229 -10.800 -9.952 66.663 1, 00 49. 61 L

ANISOU 3224 CA VAL B 229 5562 7328 5958 -1622 319 -3605

ATOM 3225 C VAL B 229 -10.087 -9.599 67.963 1, 00 52. 12 >

ANISOU 3225 C VAL B 229 5783 7852 6169 -1657 210 -3814

ATOM 3226 O VAL B 229 -9.388 -8.591 68.042 1, 00 54. 441

ANISOU 3226 O VAL B 229 6072 8046 6567 -1837 209 -3941

ATOM 3227 CB VAL B 229 -9.752 -10.240 65.555 1, 00 49. 39 )

ANISOU 3227 CB VAL B 229 5394 7334 6035 -1790 348 -3520

ATOM 3228 CGI VAL B 229 -8.642 -11.135 66.083 1, 00 50. 033

ANISOU 3228 CGI VAL B 229 5209 7795 6003 -1762 215 -3606

ATOM 3229 CG2 VAL B 229 -10.417 -10.885 64.367 1, 00 46. il

ANISOU 3229 CG2 VAL B 229 5139 6876 5771 -1685 437 -3230

ATOM 3230 N TRP B 230 -10.257 -10.434 68.982 1, 00 63. 041

ANISOU 3230 N TRP B 230 7109 9512 7332 -1489 112 -3807

ATOM 3231 CA TRP B 230 -9.623 -10.160 70.263 1, 00 65. 59 )

ANISOU 3231 CA TRP B 230 7356 10034 7529 -1499 -2 -3962

ATOM 3232 C TRP B 230 -8.209 -10.722 70.343 1, 00 67. 60 )

ANISOU 3232 C TRP B 230 7389 10534 7762 -1547 -137 -3992

ATOM 3233 O TRP B 230 -7.982 -11.900 70.064 1, 00 66. 3

ANISOU 3233 O TRP B 230 7115 10517 7515 -1438 -223 -3869

ATOM 3234 CB TRP B 230 -10.457 -10.673 71.438 1, 00 68. 177

ANISOU 3234 CB TRP B 230 7756 10547 7597 -1327 -50 -3939

ATOM 3235 CG TRP B 230 -10.121 -9.913 72.681 1, 00 76. 733

ANISOU 3235 CG TRP B 230 8831 11730 8591 -1365 -114 -4136

ATOM 3236 CD1 TRP B 230 -9.015 -10.070 73.471 1, 00 78. 541

ANISOU 3236 CD1 TRP B 230 8935 12190 8718 -1402 -269 -4225

ATOM 3237 CD2 TRP B 230 -10.869 -8.835 73.249 1, 00 80. 19 )

ANISOU 3237 CD2 TRP B 230 9385 12032 9051 -1359 -38 -4290

ATOM 3238 NE1 TRP B 230 -9.040 -9.165 74.503 1, 00 81. 21 L

ANISOU 3238 NE1 TRP B 230 9313 12549 8996 -1438 -281 -4418

ATOM 3239 CE2 TRP B 230 -10.168 -8.397 74.392 1, 00 83. 15

ANISOU 3239 CE2 TRP B 230 9702 12573 9317 -1410 -141 -4468

ATOM 3240 CE3 TRP B 230 -12.072 -8.210 72.913 1, 00 80. 70 )

ANISOU 3240 CE3 TRP B 230 9587 11855 9222 -1291 89 -4308

ATOM 3241 CZ2 TRP B 230 -10.632 -7.358 75.195 1, 00 87. 3

ANISOU 3241 CZ2 TRP B 230 10314 13043 9842 -1406 -Ill -4669

ATOM 3242 CZ3 TRP B 230 -12.526 -7.177 73.705 1, 00 83. 433

ANISOU 3242 CZ3 TRP B 230 9998 12132 9571 -1265 104 -4513

ATOM 3243 CH2 TRP B 230 -11.806 -6.760 74.830 1, 00 87. 741

ANISOU 3243 CH2 TRP B 230 10486 12848 10003 -1329 10 -4694

ATOM 3244 N GLU B 231 -7.268 -9.872 70.741 1, 00 72. 61 L

ANISOU 3244 N GLU B 231 7936 11192 8461 -1695 -170 -4170

ATOM 3245 CA GLU B 231 -5.872 -10.270 70.870 1, 00 78. 733

ANISOU 3245 CA GLU B 231 8467 12211 9234 -1734 -293 -4242

ATOM 3246 C GLU B 231 -5.617 -11.025 72.168 1, 00 83. 99 )

ANISOU 3246 C GLU B 231 9084 13165 9665 -1557 -503 -4265

ATOM 3247 O GLU B 231 -6.077 -10.617 73.236 1, 00 86. 3

ANISOU 3247 O GLU B 231 9491 13480 9810 -1528 -532 -4336 ATOM 3248 CB GLU B 231 -4.957 -9..047 70..782 1., 00 82..15

ANISOU 3248 CB GLU B 231 8829 12564 98 18 -1984 238 -

ATOM 3249 CG GLU B 231 -4. 876 -8. .454 69. .389 1. , 00 82. .41

ANISOU 3249 CG GLU B 231 8900 12353 10060 -2203 -63 -

ATOM 3250 CD GLU B 231 -4. 420 -9. .470 68. .362 1. , 00 82. .29

ANISOU 3250 CD GLU B 231 8707 12476 100 82 -2173 -39 -

ATOM 3251 OE1 GLU B 231 -3. 418 -10. .171 68. .628 1. , 00 82. .58

ANISOU 3251 OE1 GLU B 231 8495 12 811 10072 -2097 - 156 -

ATOM 3252 OE2 GLU B 231 -5. 068 -9. .577 67. .297 1. , 00 82. .02

ANISOU 3252 OE2 GLU B 231 8784 12253 10126 -2207 84 -

ATOM 3253 OXT GLU B 231 -4. 940 -12. .056 72. .173 1. , 00 85. .86

ANISOU 3253 OXT GLU B 231 9173 13607 98 46 -1436 - 659 -

TER 3254 GLU B 231

HETATM 3255 NA NA A 301 -43. 298 0. .548 19. .243 1. , 00 41. .75

HETATM 3256 NA NA B 301 -30. 560 -34. .495 50. .085 1. , 00 14. .53

HETATM 3257 NA NA B 302 -36. 417 -44. .625 24. .437 1. , 00 16. .80

HETATM 3258 NA NA B 303 -21. 173 -37. .785 20. .778 1. , 00 48. .38

HETATM 3259 O HOH A 401 -46. 064 1. .867 19. .579 1. , 00 26. .00

HETATM 3260 O HOH A 402 -39. 244 -23. .434 11. .374 1. , 00 31. .82

HETATM 3261 O HOH A 403 -52. 071 -4. .971 12. .373 1. , 00 22. .12

HETATM 3262 O HOH A 404 -53. 697 -3. .033 12. .172 1. , 00 32. .82

HETATM 3263 O HOH A 405 -54. 761 -11. .978 9. .458 1. , 00 26. .16

HETATM 3264 O HOH A 406 -56. 324 -15. .719 21. .473 1. , 00 41. .89

HETATM 3265 O HOH A 407 -45. 245 -19. .277 13. .428 1. , 00 28. .27

HETATM 3266 O HOH A 408 -39. 041 -16. .625 -5. .601 1. , 00 37. .81

HETATM 3267 O HOH A 409 -35. 194 -2. .876 -0. .344 1. , 00 35. .37

HETATM 3268 O HOH A 410 -39. 992 -23. .323 7. .671 1. , 00 34. .29

HETATM 3269 O HOH A 411 -35. 876 -12. .018 23. .167 1. , 00 36. .99

HETATM 3270 O HOH A 412 -36. 672 -17. .699 26. .517 1. , 00 35. .08

HETATM 3271 O HOH A 413 -50. 830 -4. .011 10. .832 1. , 00 46. .10

HETATM 3272 O HOH A 414 -57. 525 -7. .808 18. .479 1. , 00 34. .19

HETATM 3273 O HOH A 415 -45. 913 -17. .399 11. .467 0. , 97 28. .62

HETATM 3274 O HOH A 416 -44. 040 -15. .384 4. .475 1. , 00 28. .01

HETATM 3275 O HOH A 417 -48. 128 -12. .108 13. .831 0. , 93 26. .44

HETATM 3276 O HOH A 418 -30. 879 -15. .528 -7. .410 1. , 00 32. .43

HETATM 3277 O HOH A 419 -39. 598 -14. .025 -6. .331 1. , 00 32. .79

HETATM 3278 O HOH A 420 -33. 399 -7. .557 1. .102 1. , 00 22. .65

HETATM 3279 O HOH A 421 -29. 866 4. .526 -15. .956 1. , 00 39. .64

HETATM 3280 O HOH A 422 -29. 605 -1. .982 -10. .781 0. , 67 20. .39

HETATM 3281 O HOH A 423 -33. 944 -15. .616 12. .372 1. , 00 29. .39

HETATM 3282 O HOH A 424 -33. 962 -10. .918 -5. .080 1. , 00 22. .24

HETATM 3283 0 HOH A 425 -30. 315 -0. .791 -19. .805 1. , 00 37. .52

HETATM 3284 0 HOH A 426 -40. 728 -3. .569 -12. .018 1. , 00 28. .80

HETATM 3285 0 HOH A 427 -41. 984 -7. .745 30. .262 1. , 00 29. .40

HETATM 3286 0 HOH A 428 -40. 436 -18. .005 -3. .593 1. , 00 33. .15

HETATM 3287 0 HOH A 429 -42. 457 -15. .862 2. .417 1. , 00 31. .95

HETATM 3288 0 HOH A 430 -28. 941 -12. .321 -5. .040 1. , 00 37. .52

HETATM 3289 0 HOH A 431 -30. 579 1. .635 -20. .030 1. , 00 31. .88

HETATM 3290 0 HOH A 432 -56. 794 -17. .774 19. .079 1. , 00 40. .60

HETATM 3291 0 HOH A 433 -38. 601 -18. .356 2. .438 1. , 00 34. .40

HETATM 3292 0 HOH A 434 -32. 291 -9. .953 2. .021 1. , 00 30. .01

HETATM 3293 0 HOH A 435 -42. 095 -22. .849 6. .794 1. , 00 39. .39

HETATM 3294 0 HOH A 436 -50. 469 -18. .514 24. .015 1. , 00 30. .10

HETATM 3295 0 HOH A 437 -51. 584 -18. .667 21. .473 1. , 00 31. .63

HETATM 3296 0 HOH A 438 -35. 989 1. .032 -9. .828 1. , 00 42. .49

HETATM 3297 0 HOH A 439 -40. 262 -13. .627 -11. .594 1. , 00 41. .21

HETATM 3298 0 HOH A 440 -44. 195 -9. .355 -0. .579 1. , 00 35. .93

HETATM 3299 0 HOH A 441 -39. 628 -15. .431 29. .085 1. , 00 32. .80

HETATM 3300 0 HOH A 442 -31. 704 -18. .431 38. .416 1. , 00 41. .48 HETATM 3301 0 HOH A 443 -54..283 -17..755 21..578 1., 00 46..05

HETATM 3302 0 HOH A 444 -46. .598 -5. .022 9. .938 1. , 00 40. .93

HETATM 3303 0 HOH A 445 -37. .401 -16. .144 12. .374 1. , 00 44. .34

HETATM 3304 0 HOH A 446 -36. .294 -2. .913 -9. .480 1. , 00 49. .06

HETATM 3305 0 HOH A 447 -33. .899 -4. .240 -10. .080 1. , 00 40. .68

HETATM 3306 0 HOH A 448 -39. .336 -16. .120 32. .724 1. , 00 36. .49

HETATM 3307 0 HOH A 449 -45. .402 5. .302 22. .028 1. , 00 50. .95

HETATM 3308 0 HOH A 450 -54. .405 -16. .056 24. .070 1. , 00 46. .33

HETATM 3309 0 HOH A 451 -24. .976 -0. .131 -10. .570 1. , 00 40. .61

HETATM 3310 0 HOH A 452 -42. .817 -18. .638 6. .955 1. , 00 42. .71

HETATM 3311 0 HOH A 453 -34. .081 -12. .899 15. .131 1. , 00 52. .67

HETATM 3312 0 HOH A 454 -38. .544 -6. .327 6. .719 1. , 00 46. .81

HETATM 3313 0 HOH A 455 -27. .655 0. .472 -10. .750 1. , 00 43. .94

HETATM 3314 0 HOH A 456 -39. .436 -4. .444 -0. .043 1. , 00 35. .40

HETATM 3315 0 HOH A 457 -40. .965 -20. .816 -4. .276 1. , 00 43. .16

HETATM 3316 0 HOH A 458 -44. .494 -17. .754 5. .441 1. , 00 40. .91

HETATM 3317 0 HOH A 459 -35. .014 -17. .346 -0. .957 1. , 00 44. .72

HETATM 3318 0 HOH A 460 -48. .356 -3. .529 11. .885 1. , 00 47. .12

HETATM 3319 0 HOH A 461 -32. .095 -2. .943 -8. .435 1. , 00 45. .07

HETATM 3320 0 HOH A 462 -46. .314 -10. .284 0. .591 1. , 00 42. .68

HETATM 3321 0 HOH A 463 -33. .065 -1. .429 -0. .146 1. , 00 41. .47

HETATM 3322 0 HOH A 464 -47. .376 -2. .952 13. .774 1. , 00 37. .81

HETATM 3323 0 HOH A 465 -38. .068 -1. .149 -10. .822 1. , 00 43. .07

HETATM 3324 0 HOH A 466 -28. .293 -18. .587 -8. .127 1. , 00 49. .73

HETATM 3325 0 HOH A 467 -47. .437 -12. .075 2. .511 1. , 00 47. .30

HETATM 3326 0 HOH A 468 -38. .568 -15. .298 -10. .082 1. , 00 45. .25

HETATM 3327 0 HOH A 469 -38. .089 -3. .129 -5. .895 1. , 00 35. .96

HETATM 3328 0 HOH A 470 -27. .142 -4. .116 3. .629 1. , 00 50. .34

HETATM 3329 0 HOH A 471 -23. .396 -15. .742 -13. .546 1. , 00 44. .81

HETATM 3330 0 HOH A 472 -41. .047 -18. .240 1. .893 1. , 00 32. .55

HETATM 3331 0 HOH A 473 -40. .840 -4. .743 9. .488 1. , 00 42. .30

HETATM 3332 0 HOH A 474 -47. .233 -14. .288 6. .037 1. , 00 35. .07

HETATM 3333 0 HOH A 475 -26. .654 -3. .412 -5. .001 1. , 00 45. .50

HETATM 3334 0 HOH A 476 -24. .506 3. .414 -22. .744 1. , 00 51. .47

HETATM 3335 0 HOH A 477 -10. .993 -9. .172 -18. .491 1. , 00 60. .17

HETATM 3336 0 HOH A 478 -39. .644 -17. .435 -8. .148 1. , 00 51. .58

HETATM 3337 0 HOH A 479 -34. .661 -1. .926 -7. .395 1. , 00 55. .86

HETATM 3338 0 HOH A 480 -34. .649 -22. .328 39. .391 1. , 00 57. .18

HETATM 3339 0 HOH A 481 -17. .618 -13. .485 -19. .919 1. , 00 49. .03

HETATM 3340 0 HOH A 482 -32. .322 2. .975 -13. .703 1. , 00 43. .85

HETATM 3341 0 HOH A 483 -33. .542 -12. .914 17. .818 1. , 00 45. .43

HETATM 3342 0 HOH A 484 -33. .804 0. .893 -7. .005 1. , 00 60. .63

HETATM 3343 0 HOH A 485 -45. .239 -1. .752 12. .267 1. , 00 52. .89

HETATM 3344 0 HOH A 486 -30. .982 0. .390 -7. .337 1. , 00 49. .56

HETATM 3345 0 HOH A 487 -35. .223 -16. .464 28. .778 1. , 00 50. .05

HETATM 3346 0 HOH A 488 -48. .727 -6. .500 26. .806 1. , 00 39. .10

HETATM 3347 0 HOH A 489 -44. .157 0. .347 13. .692 1. , 00 43. .95

HETATM 3348 0 HOH A 490 -27. .600 -18. .584 5. .912 1. , 00 44. .63

HETATM 3349 0 HOH A 491 -21. .409 -6. .912 2. .359 1. , 00 53. .87

HETATM 3350 0 HOH A 492 -40. .486 -1. .442 31. .936 1. , 00 53. .55

HETATM 3351 0 HOH A 493 -45. .212 -3. .035 10. .094 1. , 00 52. .80

HETATM 3352 0 HOH A 494 -34. .867 -9. .425 25. .725 1. , 00 52. .45

HETATM 3353 0 HOH A 495 -19. .625 5. .206 -12. .967 1. , 00 47. .67

HETATM 3354 0 HOH A 496 -46. .307 -12. .995 37. .728 1. , 00 55. .77

HETATM 3355 0 HOH A 497 -36. .046 -1. .119 15. .456 1. , 00 40. .08

HETATM 3356 0 HOH A 498 -35. .346 -16. .397 18. .397 1. , 00 36. .02

HETATM 3357 0 HOH A 499 -50. .747 -5. .645 28. .370 1. , 00 58. .27

HETATM 3358 0 HOH A 500 -44. .945 -7. .404 6. .391 1. , 00 38. .66

HETATM 3359 0 HOH A 501 -46. .160 -19. .442 30. .767 1. , 00 41. .39 HETATM 3360 0 HOH A 502 -44..892 -12..366 -10..523 1., 00 35..65

HETATM 3361 0 HOH A 503 -47. .169 -16. .511 2. .173 1. , 00 58. .80

HETATM 3362 0 HOH A 504 -45. .840 -18. .556 1. .997 1. , 00 56. .64

HETATM 3363 0 HOH A 505 -43. .180 -13. .401 -11. .997 1. , 00 47. .47

HETATM 3364 0 HOH A 506 -39. .352 -3. .190 8. .609 1. , 00 52. .21

HETATM 3365 0 HOH A 507 -30. .689 -2. .395 -1. .168 1. , 00 51. .85

HETATM 3366 0 HOH A 508 -41. .411 -14. .155 -9. .099 1. , 00 45. .41

HETATM 3367 0 HOH A 509 -48. .666 -18. .337 33. .871 1. , 00 52. .58

HETATM 3368 0 HOH A 510 -22. .567 -0. .109 -8. .028 1. , 00 51. .88

HETATM 3369 0 HOH A 511 -34. .738 -17. .845 24. .471 1. , 00 48. .23

HETATM 3370 0 HOH A 512 -31. .966 -9. .596 25. .123 1. , 00 54. .46

HETATM 3371 0 HOH A 513 -12. .276 -0. .299 -17. .588 1. , 00 46. .98

HETATM 3372 0 HOH A 514 -51. .996 -0. .985 12. .900 1. , 00 50. .80

HETATM 3373 0 HOH A 515 -37. .076 -14. .822 29. .978 1. , 00 55. .04

HETATM 3374 0 HOH A 516 -59. .012 -16. .409 18. .102 1. , 00 47. .52

HETATM 3375 0 HOH A 517 -46. .284 -14. .645 3. .452 1. , 00 45. .66

HETATM 3376 0 HOH A 518 -39. .152 -17. .161 39. .218 1. , 00 46. .23

HETATM 3377 0 HOH A 519 -38. .141 1. .031 16. .496 1. , 00 43. .69

HETATM 3378 0 HOH A 520 -49. .830 -8. .102 33. .217 1. , 00 53. .54

HETATM 3379 0 HOH A 521 -37. .868 -3. .840 26. .055 1. , 00 35. .17

HETATM 3380 0 HOH A 522 -46. .303 3. .578 23. .397 1. , 00 39. .48

HETATM 3381 0 HOH A 523 -40. .325 -3. .376 -3. .518 1. , 00 55. .32

HETATM 3382 0 HOH A 524 -38. .266 -13. .193 32. .769 1. , 00 59. .70

HETATM 3383 0 HOH A 525 -36. .542 -5. .509 25. .204 1. , 00 61. .52

HETATM 3384 0 HOH A 526 -41. .084 -10. .089 -16. .186 1. , 00 50. .03

HETATM 3385 0 HOH A 527 -31. .769 -2. .903 -21. .186 1. , 00 42. .92

HETATM 3386 0 HOH A 528 -35. .889 -2. .712 -5. .507 1. , 00 39. .37

HETATM 3387 0 HOH B 401 -21. .413 -40. .861 20. .429 1. , 00 24. .68

HETATM 3388 0 HOH B 402 -31. .969 -22. .306 21. .648 1. , 00 34. .79

HETATM 3389 0 HOH B 403 -30. .374 -42. .628 27. .626 1. , 00 19. .39

HETATM 3390 0 HOH B 404 -37. .783 -41. .395 30. .517 1. , 00 28. .32

HETATM 3391 0 HOH B 405 -41. .721 -40. .850 18. .614 1. , 00 44. .22

HETATM 3392 0 HOH B 406 -33. .765 -25. .497 45. .633 1. , 00 34. .78

HETATM 3393 0 HOH B 407 -20. .274 -29. .050 40. .327 1. , 00 35. .17

HETATM 3394 0 HOH B 408 -28. .358 -25. .042 16. .827 1. , 00 38. .14

HETATM 3395 0 HOH B 409 -15. .506 -42. .319 21. .526 1. , 00 29. .46

HETATM 3396 0 HOH B 410 -29. .569 -45. .077 27. .889 1. , 00 28. .23

HETATM 3397 0 HOH B 411 -33. .640 -22. .944 13. .484 1. , 00 34. .10

HETATM 3398 0 HOH B 412 -34. .660 -35. .583 26. .159 0. , 92 27. .21

HETATM 3399 0 HOH B 413 -28. .953 -18. .980 47. .419 1. , 00 36. .66

HETATM 3400 0 HOH B 414 -23. .308 -25. .108 38. .916 1. , 00 24. .13

HETATM 3401 0 HOH B 415 -10. .913 -28. .083 55. .957 1. , 00 36. .36

HETATM 3402 0 HOH B 416 -31. .962 -27. .334 46. .344 1. , 00 29. .62

HETATM 3403 0 HOH B 417 -23. .428 -33. .534 52. .016 1. , 00 29. .42

HETATM 3404 0 HOH B 418 -31. .742 -18. .247 1. .604 1. , 00 44. .69

HETATM 3405 0 HOH B 419 -40. .225 -23. .035 32. .351 1. , 00 33. .46

HETATM 3406 0 HOH B 420 -40. .893 -25. .162 33. .124 1. , 00 37. .92

HETATM 3407 0 HOH B 421 -30. .458 -21. .554 27. .688 1. , 00 30. .00

HETATM 3408 0 HOH B 422 -26. .397 -23. .982 45. .131 1. , 00 23. .69

HETATM 3409 0 HOH B 423 -40. .031 -35. .617 37. .335 1. , 00 54. .63

HETATM 3410 0 HOH B 424 -35. .342 -30. .431 35. .547 1. , 00 27. .24

HETATM 3411 0 HOH B 425 -27. .726 -32. .409 9. .813 1. , 00 27. .08

HETATM 3412 0 HOH B 426 -24. .761 -22. .969 37. .937 1. , 00 30. .26

HETATM 3413 0 HOH B 427 -37. .986 -31. .100 28. .462 1. , 00 34. .23

HETATM 3414 0 HOH B 428 -35. .679 -25. .937 43. .607 1. , 00 31. .74

HETATM 3415 0 HOH B 429 -43. .865 -40. .245 21. .052 1. , 00 42. .09

HETATM 3416 0 HOH B 430 -34. .954 -28. .772 37. .613 1. , 00 28. .41

HETATM 3417 0 HOH B 431 -25. .135 -18. .947 44. .996 1. , 00 38. .53

HETATM 3418 0 HOH B 432 -41. .916 -35. .302 18. .540 1. , 00 33. .74 HETATM 3419 0 HOH B 433 -16..386 -24..554 50..838 1., 00 35..14

HETATM 3420 0 HOH B 434 -41. .303 -34. .444 16. .097 1. , 00 29. .18

HETATM 3421 0 HOH B 435 -42. .465 -38. .145 18. .379 1. , 00 47. .72

HETATM 3422 0 HOH B 436 -41. .115 -38. .954 15. .882 1. , 00 41. .22

HETATM 3423 0 HOH B 437 -31. .940 -28. .100 51. .646 1. , 00 47. .68

HETATM 3424 0 HOH B 438 -16. .310 -21. .040 45. .062 1. , 00 49. .07

HETATM 3425 0 HOH B 439 -32. .664 -24. .173 27. .608 1. , 00 42. .74

HETATM 3426 0 HOH B 440 -30. .026 -38. .910 13. .258 1. , 00 42. .20

HETATM 3427 0 HOH B 441 -20. .774 -30. .147 49. .489 1. , 00 48. .20

HETATM 3428 0 HOH B 442 -30. .334 -33. .617 40. .677 1. , 00 35. .39

HETATM 3429 0 HOH B 443 -39. .721 -33. .574 36. .252 1. , 00 55. .08

HETATM 3430 0 HOH B 444 -35. .767 -32. .854 36. .462 1. , 00 48. .40

HETATM 3431 0 HOH B 445 -13. .892 -27. .243 60. .062 1. , 00 35. .63

HETATM 3432 0 HOH B 446 -20. .609 -27. .309 50. .091 1. , 00 40. .42

HETATM 3433 0 HOH B 447 -27. .607 -37. .933 29. .925 1. , 00 39. .60

HETATM 3434 0 HOH B 448 -33. .122 -26. .540 10. .942 1. , 00 31. .00

HETATM 3435 0 HOH B 449 -33. .633 -25. .954 7. .322 1. , 00 41. .54

HETATM 3436 0 HOH B 450 -23. .570 -31. .888 40. .132 1. , 00 35. .48

HETATM 3437 0 HOH B 451 -34. .655 -25. .495 0. .726 1. , 00 42. .09

HETATM 3438 0 HOH B 452 -28. .933 -35. .325 33. .591 1. , 00 34. .70

HETATM 3439 0 HOH B 453 -30. .058 -15. .070 48. .008 1. , 00 43. .19

HETATM 3440 0 HOH B 454 -32. .053 -35. .052 39. .294 1. , 00 46. .08

HETATM 3441 0 HOH B 455 -37. .795 -29. .787 34. .755 1. , 00 41. .49

HETATM 3442 0 HOH B 456 -21. .168 -31. .671 39. .359 1. , 00 50. .32

HETATM 3443 0 HOH B 457 -39. .780 -30. .305 9. .259 1. , 00 40. .93

HETATM 3444 0 HOH B 458 -37. .740 -27. .813 33. .034 1. , 00 43. .39

HETATM 3445 0 HOH B 459 -18. .446 -26. .397 48. .386 1. , 00 41. .77

HETATM 3446 0 HOH B 460 -32. .574 -25. .719 50. .117 1. , 00 43. .59

HETATM 3447 0 HOH B 461 -28. .199 -23. .000 24. .936 1. , 00 49. .25

HETATM 3448 0 HOH B 462 -25. .105 -11. .854 51. .085 1. , 00 51. .76

HETATM 3449 0 HOH B 463 -16. .654 -15. .132 37. .723 1. , 00 52. .00

HETATM 3450 0 HOH B 464 -37. .272 -23. .382 35. .850 1. , 00 39. .85

HETATM 3451 0 HOH B 465 -39. .905 -22. .278 28. .614 1. , 00 28. .92

HETATM 3452 0 HOH B 466 -32. .721 -46. .364 17. .967 1. , 00 49. .77

HETATM 3453 0 HOH B 467 -24. .506 -32. .969 30. .490 1. , 00 46. .28

HETATM 3454 0 HOH B 468 -15. .934 -25. .767 59. .913 1. , 00 45. .33

HETATM 3455 0 HOH B 469 -25. .370 -12. .375 53. .529 1. , 00 40. .76

HETATM 3456 0 HOH B 470 -34. .266 -35. .025 37. .492 1. , 00 45. .95

HETATM 3457 0 HOH B 471 -41. .506 -37. .147 38. .183 1. , 00 56. .46

HETATM 3458 0 HOH B 472 -9. .344 -22. .989 62. .755 1. , 00 51. .28

HETATM 3459 0 HOH B 473 -27. .776 -19. .946 28. .548 1. , 00 48. .84

HETATM 3460 0 HOH B 474 -27. .172 -40. .285 28. .103 1. , 00 52. .54

HETATM 3461 0 HOH B 475 -38. .319 -31. .935 33. .025 1. , 00 43. .04

HETATM 3462 0 HOH B 476 -27. .684 -22. .576 22. .310 1. , 00 46. .34

HETATM 3463 0 HOH B 477 -33. .315 -30. .827 51. .832 1. , 00 45. .20

HETATM 3464 0 HOH B 478 -32. .885 -28. .747 49. .158 1. , 00 45. .16

HETATM 3465 0 HOH B 479 -19. .583 -14. .115 67. .667 1. , 00 53. .69

HETATM 3466 0 HOH B 480 -5. .156 -19. .886 53. .224 1. , 00 48. .41

HETATM 3467 0 HOH B 481 -13. .884 -29. .305 53. .585 1. , 00 44. .52

HETATM 3468 0 HOH B 482 -22. .205 -30. .729 13. .958 1. , 00 39. .84

HETATM 3469 0 HOH B 483 -23. .208 -28. .973 14. .976 1. , 00 60. .65

HETATM 3470 0 HOH B 484 -30. .774 -46. .306 16. .557 1. , 00 40. .99

HETATM 3471 0 HOH B 485 -22. .432 -32. .332 31. .419 1. , 00 49. .56

HETATM 3472 0 HOH B 486 -13. .422 -24. .222 50. .675 1. , 00 39. .66

HETATM 3473 0 HOH B 487 -36. .239 -26. .505 38. .139 1. , 00 33. .60

HETATM 3474 0 HOH B 488 -30. .255 -41. .125 11. .635 1. , 00 56. .79

HETATM 3475 0 HOH B 489 -33. .105 -32. .942 50. .457 1. , 00 43. .29

HETATM 3476 0 HOH B 490 -12. .624 -21. .481 50. .633 1. , 00 38. .70

HETATM 3477 0 HOH B 491 -37. .633 -32. .712 37. .791 1. , 00 61. .43 HETATM 3478 O HOH B 492 -36.098 -33..837 33..906 1., 00 38.38

HETATM 3479 O HOH B 493 -17. 871 -28. .013 40. .231 1. , 00 39 .45

HETATM 3480 O HOH B 494 -26. 218 -39. .507 26. .191 1. , 00 40 .78

HETATM 3481 O HOH B 495 -14. 464 -14. .800 70. .478 1. , 00 41 .80

HETATM 3482 O HOH B 496 -40. 193 -32. .994 6. .211 1. , 00 52 .52

HETATM 3483 O HOH B 497 -33. 042 -21. .220 15. .369 1. , 00 44 .55

HETATM 3484 O HOH B 498 -32. 562 -21. .608 40. .973 1. , 00 38 .87

HETATM 3485 O HOH B 499 -13. 113 -4. .900 58. .296 1. , 00 60 .72

HETATM 3486 O HOH B 500 -43. 862 -42. .913 21. .833 1. , 00 45 .27

HETATM 3487 O HOH B 501 -31. 378 -24. .705 10. .406 1. , 00 57 .08

HETATM 3488 O HOH B 502 -24. 221 -38. .346 27. .740 1. , 00 49 .59

HETATM 3489 O HOH B 503 -35. 252 -24. .241 37. .538 1. , 00 31 .51

HETATM 3490 O HOH B 504 -31. 960 -22. .218 11. .228 1. , 00 50 .64

HETATM 3491 O HOH B 505 -29. 273 -49. .906 26. .299 1. , 00 43 .43

HETATM 3492 O HOH B 506 -39. 373 -29. .480 26. .607 1. , 00 29 .39

HETATM 3493 O HOH B 507 -18. 435 -26. .028 61. .171 1. , 00 40 .05

HETATM 3494 O HOH B 508 -29. 076 -42. .101 29. .396 1. , 00 46 .31

HETATM 3495 O HOH B 509 -25. 187 -37. .622 29. .831 1. , 00 53 .44

HETATM 3496 O HOH B 510 -34. 469 -33. .591 2. .208 1. , 00 56 .76

HETATM 3497 O HOH B 511 -33. 177 -18. .898 -1. .538 1. , 00 59 .02

HETATM 3498 O HOH B 512 -30. 911 -46. .038 30. .038 1. , 00 55 .03

HETATM 3499 O HOH B 513 -31. 975 -39. .052 6. .784 1. , 00 51 .49

HETATM 3500 O HOH B 514 -36. 213 -37. .145 38. .091 1. , 00 48 .14

HETATM 3501 O HOH B 515 -37. 040 -38. .370 36. .426 1. , 00 47 .36

HETATM 3502 O HOH B 516 -38. 830 -30. .735 38. .108 1. , 00 52 .97

HETATM 3503 O HOH B 517 -30. 384 -26. .303 6. .997 1. , 00 58 .10

CONECT 136 606

CONECT 606 136

CONECT 948 1436

CONECT 1436 948

CONECT 1763 2233

CONECT 2233 1763

CONECT 2575 3063

CONECT 3063 2575

CONECT 3255 3259

CONECT 3256 3475

CONECT 3258 3387

CONECT 3259 3255

CONECT 3387 3258

CONECT 3475 3256

MASTER 320 0 4 4 36 0 4 6 3501 2 14

END