Browse entries in the PDBbind-CN Database
HEADER APOPTOSIS 27-MAY-13 4BPK TITLE BCL-XL BOUND TO ALPHA BETA PUMA BH3 PEPTIDE 5 COMPND MOL_ID: 1; COMPND 2 MOLECULE: BCL-2-LIKE PROTEIN 1; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: RESIDUES 1-26,83-209; COMPND 5 SYNONYM: BCL2-L-1, APOPTOSIS REGULATOR BCL-X, BCL-XL; COMPND 6 ENGINEERED: YES; COMPND 7 OTHER_DETAILS: BCL-XL WITHOUT C-TERMINAL DOMAIN OR LOOP BETWEEN ALPHA COMPND 8 1 AND ALPHA 2 HELICES; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: ALPHA BETA BH3-PEPTIDE; COMPND 11 CHAIN: C, D; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX6P3; SOURCE 10 MOL_ID: 2; SOURCE 11 SYNTHETIC: YES; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_COMMON: HUMAN; SOURCE 14 ORGANISM_TAXID: 9606 KEYWDS APOPTOSIS EXPDTA X-RAY DIFFRACTION AUTHOR B.J.SMITH,E.F.LEE,J.W.CHECCO,S.H.GELLMAN,W.D.FAIRLIE REVDAT 5 10-JUL-19 4BPK 1 REMARK REVDAT 4 24-APR-19 4BPK 1 REMARK SEQRES REVDAT 3 20-JUN-18 4BPK 1 LINK ATOM REVDAT 2 10-MAY-17 4BPK 1 REMARK REVDAT 1 09-APR-14 4BPK 0 JRNL AUTH B.J.SMITH,E.F.LEE,J.W.CHECCO,M.EVANGELISTA,S.H.GELLMAN, JRNL AUTH 2 W.D.FAIRLIE JRNL TITL STRUCTURE-GUIDED RATIONAL DESIGN OF ALPHA/BETA-PEPTIDE JRNL TITL 2 FOLDAMERS WITH HIGH AFFINITY FOR BCL-2 FAMILY PROSURVIVAL JRNL TITL 3 PROTEINS. JRNL REF CHEMBIOCHEM V. 14 1564 2013 JRNL REFN ISSN 1439-4227 JRNL PMID 23929624 JRNL DOI 10.1002/CBIC.201300351 REMARK 2 REMARK 2 RESOLUTION. 1.76 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.76 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.07 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 3 NUMBER OF REFLECTIONS : 38364 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.221 REMARK 3 R VALUE (WORKING SET) : 0.219 REMARK 3 FREE R VALUE : 0.252 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 3620 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 36.0741 - 5.1984 0.94 2528 131 0.2372 0.2477 REMARK 3 2 5.1984 - 4.1280 1.00 2661 142 0.1776 0.1582 REMARK 3 3 4.1280 - 3.6068 1.00 2633 137 0.1707 0.2442 REMARK 3 4 3.6068 - 3.2772 1.00 2696 146 0.2056 0.2227 REMARK 3 5 3.2772 - 3.0425 1.00 2688 137 0.2187 0.2817 REMARK 3 6 3.0425 - 2.8632 1.00 2640 141 0.2083 0.2793 REMARK 3 7 2.8632 - 2.7198 1.00 2680 145 0.2175 0.2713 REMARK 3 8 2.7198 - 2.6015 1.00 2673 144 0.2156 0.2352 REMARK 3 9 2.6015 - 2.5014 1.00 2681 143 0.2232 0.2692 REMARK 3 10 2.5014 - 2.4151 1.00 2652 140 0.2137 0.2450 REMARK 3 11 2.4151 - 2.3396 1.00 2711 144 0.2176 0.2764 REMARK 3 12 2.3396 - 2.2727 1.00 2684 138 0.2237 0.2364 REMARK 3 13 2.2727 - 2.2129 1.00 2646 142 0.2355 0.2903 REMARK 3 14 2.2129 - 2.1589 1.00 2657 136 0.2286 0.2705 REMARK 3 15 2.1589 - 2.1098 1.00 2666 136 0.2503 0.2801 REMARK 3 16 2.1098 - 2.0649 1.00 2696 138 0.2473 0.2484 REMARK 3 17 2.0649 - 2.0236 1.00 2701 148 0.2519 0.3258 REMARK 3 18 2.0236 - 1.9854 1.00 2652 137 0.2611 0.3066 REMARK 3 19 1.9854 - 1.9500 1.00 2666 139 0.2737 0.3296 REMARK 3 20 1.9500 - 1.9169 1.00 2665 142 0.2834 0.3671 REMARK 3 21 1.9169 - 1.8860 1.00 2711 143 0.2667 0.2527 REMARK 3 22 1.8860 - 1.8570 1.00 2646 139 0.2858 0.2823 REMARK 3 23 1.8570 - 1.8297 1.00 2651 142 0.2897 0.3698 REMARK 3 24 1.8297 - 1.8039 0.99 2618 136 0.3116 0.3482 REMARK 3 25 1.8039 - 1.7795 0.98 2668 142 0.3363 0.3245 REMARK 3 26 1.7795 - 1.7564 0.85 2272 112 0.3523 0.3741 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.260 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.920 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.010 2933 REMARK 3 ANGLE : 1.058 3939 REMARK 3 CHIRALITY : 0.064 399 REMARK 3 PLANARITY : 0.004 520 REMARK 3 DIHEDRAL : 16.030 1085 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): 18.3088 -27.8496 -12.7689 REMARK 3 T TENSOR REMARK 3 T11: 0.1376 T22: 0.3573 REMARK 3 T33: 0.1263 T12: 0.0291 REMARK 3 T13: -0.0422 T23: -0.1274 REMARK 3 L TENSOR REMARK 3 L11: 4.1447 L22: 9.5458 REMARK 3 L33: 1.1506 L12: -4.4369 REMARK 3 L13: 0.8859 L23: -2.0407 REMARK 3 S TENSOR REMARK 3 S11: -0.2501 S12: -0.4170 S13: 0.4348 REMARK 3 S21: 0.4352 S22: 0.3343 S23: -0.4398 REMARK 3 S31: -0.1077 S32: -0.1191 S33: -0.0167 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 4BPK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-MAY-13. REMARK 100 THE DEPOSITION ID IS D_1290056945. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-AUG-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 : AUSTRALIAN SYNCHROTRON REMARK 200 BEAMLINE : MX2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 198352 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.760 REMARK 200 RESOLUTION RANGE LOW (A) : 3.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : 7.000 REMARK 200 R MERGE (I) : 0.05000 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.7400 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.76 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4 REMARK 200 DATA REDUNDANCY IN SHELL : 9.35 REMARK 200 R MERGE FOR SHELL (I) : 0.71000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.390 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 2P1L REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 55.60 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.79 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, PH7.5 1M SODIUM ACETATE REMARK 280 50MM CADMIUM SULPHATE REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 32.58750 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.28950 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.06650 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.28950 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.58750 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.06650 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 10810 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 14890 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -121.5 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A -3 REMARK 465 PRO A -2 REMARK 465 LEU A -1 REMARK 465 GLY A 0 REMARK 465 GLY A 196 REMARK 465 ASN A 197 REMARK 465 ASN A 198 REMARK 465 ALA A 199 REMARK 465 ALA A 200 REMARK 465 ALA A 201 REMARK 465 GLU A 202 REMARK 465 SER A 203 REMARK 465 ARG A 204 REMARK 465 LYS A 205 REMARK 465 GLY A 206 REMARK 465 GLN A 207 REMARK 465 GLU A 208 REMARK 465 ARG A 209 REMARK 465 GLY B -3 REMARK 465 PRO B -2 REMARK 465 LEU B -1 REMARK 465 GLY B 0 REMARK 465 MET B 1 REMARK 465 GLY B 196 REMARK 465 ASN B 197 REMARK 465 ASN B 198 REMARK 465 ALA B 199 REMARK 465 ALA B 200 REMARK 465 ALA B 201 REMARK 465 GLU B 202 REMARK 465 SER B 203 REMARK 465 ARG B 204 REMARK 465 LYS B 205 REMARK 465 GLY B 206 REMARK 465 GLN B 207 REMARK 465 GLU B 208 REMARK 465 ARG B 209 REMARK 465 ACE C -1 REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 GLN A 3 CG CD OE1 NE2 REMARK 480 GLN A 121 OE1 NE2 REMARK 480 ARG B 102 CG CD NE REMARK 480 GLN B 121 CD OE1 NE2 REMARK 480 GLU B 153 CG CD OE1 OE2 REMARK 480 LYS B 157 CB CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OF1 B3E D 4 O HOH D 2001 2.11 REMARK 500 OD1 ASN A 175 ND2 ASN B 5 2.12 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ACE D -1 O - C - N ANGL. DEV. = -16.5 DEGREES REMARK 500 REMARK 500 REMARK: NULL 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:(10X,I3,1X,A3,1X,A1,I4,A1,4X,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 HIS A 177 -0.13 -140.05 REMARK 500 HR7 C 11 -69.79 -24.62 REMARK 500 B3A D 18 -80.21 -19.06 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH C2002 DISTANCE = 6.16 ANGSTROMS REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CD A1197 CD REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 92 OE2 REMARK 620 2 HOH A2023 O 96.1 REMARK 620 3 HOH A2043 O 99.7 73.6 REMARK 620 4 HOH A2042 O 81.4 173.3 100.6 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CD A1196 CD REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 129 OE1 REMARK 620 2 GLU A 129 OE2 52.5 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CD A1196 CD REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 129 OE2 REMARK 620 2 HOH A2059 O 93.0 REMARK 620 3 GLU A 158 OE2 44.9 48.6 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CD A1199 CD REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 153 OE1 REMARK 620 2 GLU A 153 OE2 55.3 REMARK 620 3 HOH A2066 O 155.1 103.0 REMARK 620 4 HOH A2051 O 89.9 80.8 98.8 REMARK 620 5 HOH A2064 O 89.5 117.7 91.6 156.2 REMARK 620 6 HOH A2065 O 78.6 133.1 123.9 92.3 64.3 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CD A1201 CD REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 179 OE2 REMARK 620 2 HOH A2068 O 107.4 REMARK 620 3 HOH A2069 O 63.8 165.2 REMARK 620 4 GLU B 124 OE1 114.0 132.2 51.5 REMARK 620 5 GLU B 124 OE2 116.6 129.6 54.2 2.8 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CD B1199 CD REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU B 92 OE2 REMARK 620 2 HOH B2026 O 75.1 REMARK 620 3 HOH B2012 O 84.0 71.5 REMARK 620 4 HOH B2075 O 158.6 100.1 114.7 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CD B1201 CD REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU B 153 OE1 REMARK 620 2 ASP B 156 OD2 82.7 REMARK 620 3 HOH B2053 O 121.2 117.9 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CD B1197 CD REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 176 OD1 REMARK 620 2 ASP B 176 OD2 50.5 REMARK 620 3 HOH B2058 O 61.5 96.5 REMARK 620 4 HOH B2073 O 116.8 156.7 61.7 REMARK 620 5 HOH B2074 O 96.3 116.6 112.8 81.8 REMARK 620 6 GLY A 186 O 111.0 118.4 127.2 83.5 17.3 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CD B1198 CD REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS B 177 NE2 REMARK 620 2 HOH B2059 O 96.6 REMARK 620 3 HOH B2060 O 106.4 83.1 REMARK 620 4 HOH B2063 O 70.5 161.4 87.7 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CD B1196 CD REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLY B 186 O REMARK 620 2 ASP B 189 OD1 70.3 REMARK 620 3 ASP B 189 OD2 80.4 54.9 REMARK 620 N 1 2 REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED. REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 1196 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 1197 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 1198 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1196 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1197 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1198 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1199 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 1199 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 1200 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1200 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 1202 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 1203 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 1204 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1205 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1202 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4BPI RELATED DB: PDB REMARK 900 MCL-1 BOUND TO ALPHA BETA PUMA BH3 PEPTIDE 2 REMARK 900 RELATED ID: 4BPJ RELATED DB: PDB REMARK 900 MCL-1 BOUND TO ALPHA BETA PUMA BH3 PEPTIDE 3 REMARK 999 REMARK 999 SEQUENCE REMARK 999 DELETION MUTANT CONTAINING RESIDUES 1-40 AND 81-209 REMARK 999 DELETION REMOVES 41-80 AND 210-233 DBREF 4BPK A 1 26 UNP Q07817 B2CL1_HUMAN 1 26 DBREF 4BPK A 83 209 UNP Q07817 B2CL1_HUMAN 83 209 DBREF 4BPK B 1 26 UNP Q07817 B2CL1_HUMAN 1 26 DBREF 4BPK B 83 209 UNP Q07817 B2CL1_HUMAN 83 209 DBREF 4BPK C -1 21 PDB 4BPK 4BPK -1 21 DBREF 4BPK D -1 21 PDB 4BPK 4BPK -1 21 SEQADV 4BPK GLY A -3 UNP Q07817 EXPRESSION TAG SEQADV 4BPK PRO A -2 UNP Q07817 EXPRESSION TAG SEQADV 4BPK LEU A -1 UNP Q07817 EXPRESSION TAG SEQADV 4BPK GLY A 0 UNP Q07817 EXPRESSION TAG SEQADV 4BPK GLY B -3 UNP Q07817 EXPRESSION TAG SEQADV 4BPK PRO B -2 UNP Q07817 EXPRESSION TAG SEQADV 4BPK LEU B -1 UNP Q07817 EXPRESSION TAG SEQADV 4BPK GLY B 0 UNP Q07817 EXPRESSION TAG SEQRES 1 A 157 GLY PRO LEU GLY MET SER GLN SER ASN ARG GLU LEU VAL SEQRES 2 A 157 VAL ASP PHE LEU SER TYR LYS LEU SER GLN LYS GLY TYR SEQRES 3 A 157 SER TRP SER GLN MET ALA ALA VAL LYS GLN ALA LEU ARG SEQRES 4 A 157 GLU ALA GLY ASP GLU PHE GLU LEU ARG TYR ARG ARG ALA SEQRES 5 A 157 PHE SER ASP LEU THR SER GLN LEU HIS ILE THR PRO GLY SEQRES 6 A 157 THR ALA TYR GLN SER PHE GLU GLN VAL VAL ASN GLU LEU SEQRES 7 A 157 PHE ARG ASP GLY VAL ASN TRP GLY ARG ILE VAL ALA PHE SEQRES 8 A 157 PHE SER PHE GLY GLY ALA LEU CYS VAL GLU SER VAL ASP SEQRES 9 A 157 LYS GLU MET GLN VAL LEU VAL SER ARG ILE ALA ALA TRP SEQRES 10 A 157 MET ALA THR TYR LEU ASN ASP HIS LEU GLU PRO TRP ILE SEQRES 11 A 157 GLN GLU ASN GLY GLY TRP ASP THR PHE VAL GLU LEU TYR SEQRES 12 A 157 GLY ASN ASN ALA ALA ALA GLU SER ARG LYS GLY GLN GLU SEQRES 13 A 157 ARG SEQRES 1 B 157 GLY PRO LEU GLY MET SER GLN SER ASN ARG GLU LEU VAL SEQRES 2 B 157 VAL ASP PHE LEU SER TYR LYS LEU SER GLN LYS GLY TYR SEQRES 3 B 157 SER TRP SER GLN MET ALA ALA VAL LYS GLN ALA LEU ARG SEQRES 4 B 157 GLU ALA GLY ASP GLU PHE GLU LEU ARG TYR ARG ARG ALA SEQRES 5 B 157 PHE SER ASP LEU THR SER GLN LEU HIS ILE THR PRO GLY SEQRES 6 B 157 THR ALA TYR GLN SER PHE GLU GLN VAL VAL ASN GLU LEU SEQRES 7 B 157 PHE ARG ASP GLY VAL ASN TRP GLY ARG ILE VAL ALA PHE SEQRES 8 B 157 PHE SER PHE GLY GLY ALA LEU CYS VAL GLU SER VAL ASP SEQRES 9 B 157 LYS GLU MET GLN VAL LEU VAL SER ARG ILE ALA ALA TRP SEQRES 10 B 157 MET ALA THR TYR LEU ASN ASP HIS LEU GLU PRO TRP ILE SEQRES 11 B 157 GLN GLU ASN GLY GLY TRP ASP THR PHE VAL GLU LEU TYR SEQRES 12 B 157 GLY ASN ASN ALA ALA ALA GLU SER ARG LYS GLY GLN GLU SEQRES 13 B 157 ARG SEQRES 1 C 22 ACE HT7 ALA ARG B3E ILE GLY ALA B3Q AHP ARG HR7 MET SEQRES 2 C 22 ALA ASP B3D LEU ASN B3A GLN TYR NH2 SEQRES 1 D 22 ACE HT7 ALA ARG B3E ILE GLY ALA B3Q AHP ARG HR7 MET SEQRES 2 D 22 ALA ASP B3D LEU ASN B3A GLN TYR NH2 MODRES 4BPK HT7 C 1 TRP MODRES 4BPK B3E C 4 GLU (3S)-3-AMINOHEXANEDIOIC ACID MODRES 4BPK AHP C 9 ALA 2-AMINO-HEPTANOIC ACID MODRES 4BPK HR7 C 11 ARG MODRES 4BPK B3D C 15 ASP 3-AMINOPENTANEDIOIC ACID MODRES 4BPK B3A C 18 ALA (3S)-3-AMINOBUTANOIC ACID MODRES 4BPK HT7 D 1 TRP MODRES 4BPK B3E D 4 GLU (3S)-3-AMINOHEXANEDIOIC ACID MODRES 4BPK AHP D 9 ALA 2-AMINO-HEPTANOIC ACID MODRES 4BPK HR7 D 11 ARG MODRES 4BPK B3D D 15 ASP 3-AMINOPENTANEDIOIC ACID MODRES 4BPK B3A D 18 ALA (3S)-3-AMINOBUTANOIC ACID HET HT7 C 1 15 HET B3E C 4 10 HET B3Q C 8 17 HET AHP C 9 9 HET HR7 C 11 12 HET B3D C 15 8 HET B3A C 18 6 HET NH2 C 21 1 HET ACE D -1 3 HET HT7 D 1 15 HET B3E D 4 10 HET B3Q D 8 10 HET AHP D 9 9 HET HR7 D 11 12 HET B3D D 15 8 HET B3A D 18 6 HET NH2 D 21 1 HET CD A1196 2 HET CD A1197 1 HET CD A1198 1 HET CD A1199 1 HET CD A1200 2 HET CD A1201 1 HET EDO A1202 4 HET CD B1196 1 HET CD B1197 1 HET CD B1198 1 HET CD B1199 1 HET CD B1200 2 HET CD B1201 1 HET CD B1202 1 HET CD B1203 1 HET CD B1204 2 HET EDO B1205 4 HETNAM HT7 (3S)-3-AMINO-4-(1H-INDOL-3-YL)BUTANOIC ACID HETNAM B3E (3S)-3-AMINOHEXANEDIOIC ACID HETNAM B3Q (3S)-3,6-DIAMINO-6-OXOHEXANOIC ACID HETNAM AHP 2-AMINO-HEPTANOIC ACID HETNAM HR7 (3S)-3-AMINO-6-[(DIAMINOMETHYLIDENE)AMINO]HEXANOIC ACID HETNAM B3D 3-AMINOPENTANEDIOIC ACID HETNAM B3A (3S)-3-AMINOBUTANOIC ACID HETNAM NH2 AMINO GROUP HETNAM ACE ACETYL GROUP HETNAM CD CADMIUM ION HETNAM EDO 1,2-ETHANEDIOL HETSYN HT7 BETA-HOMOTRYPTOPHAN HETSYN B3Q (S)-BETA-3-HOMOGLUTAMINE HETSYN HR7 BETA-HOMOARGININE HETSYN B3D BETA-HOMOASPARTATE HETSYN EDO ETHYLENE GLYCOL FORMUL 3 HT7 2(C12 H14 N2 O2) FORMUL 3 B3E 2(C6 H11 N O4) FORMUL 3 B3Q 2(C6 H12 N2 O3) FORMUL 3 AHP 2(C7 H15 N O2) FORMUL 3 HR7 2(C7 H16 N4 O2) FORMUL 3 B3D 2(C5 H9 N O4) FORMUL 3 B3A 2(C4 H9 N O2) FORMUL 3 NH2 2(H2 N) FORMUL 4 ACE C2 H4 O FORMUL 5 CD 15(CD 2+) FORMUL 11 EDO 2(C2 H6 O2) FORMUL 22 HOH *151(H2 O) HELIX 1 1 MET A 1 LYS A 20 1 20 HELIX 2 2 SER A 25 TYR A 101 1 21 HELIX 3 3 TYR A 101 SER A 110 1 10 HELIX 4 4 THR A 118 PHE A 131 1 14 HELIX 5 5 ASN A 136 LYS A 157 1 22 HELIX 6 6 VAL A 161 LEU A 178 1 18 HELIX 7 7 LEU A 178 ASN A 185 1 8 HELIX 8 8 GLY A 187 TYR A 195 1 9 HELIX 9 9 SER B 2 LYS B 20 1 19 HELIX 10 10 SER B 25 TYR B 101 1 21 HELIX 11 11 TYR B 101 SER B 110 1 10 HELIX 12 12 THR B 118 PHE B 131 1 14 HELIX 13 13 ASN B 136 LYS B 157 1 22 HELIX 14 14 VAL B 161 LEU B 178 1 18 HELIX 15 15 LEU B 178 ASN B 185 1 8 HELIX 16 16 GLY B 186 TYR B 195 1 10 HELIX 17 17 HT7 C 1 ARG C 10 1 10 HELIX 18 18 MET C 12 ASN C 17 1 6 HELIX 19 19 HT7 D 1 ARG D 10 1 10 HELIX 20 20 MET D 12 ASN D 17 1 6 LINK OE2 GLU A 92 CD CD A1197 1555 1555 2.36 LINK OE1 GLU A 129 CD B CD A1196 1555 1555 2.54 LINK OE2 GLU A 129 CD A CD A1196 1555 1555 2.41 LINK OE2 GLU A 129 CD B CD A1196 1555 1555 2.39 LINK OE1 GLU A 153 CD CD A1199 1555 1555 2.32 LINK OE2 GLU A 153 CD CD A1199 1555 1555 2.40 LINK OE2 GLU A 179 CD CD A1201 1555 1555 2.37 LINK OE2 GLU B 92 CD CD B1199 1555 1555 2.31 LINK OE2 GLU B 129 CD B CD B1200 1555 1555 2.65 LINK OE1 GLU B 153 CD CD B1201 1555 1555 2.40 LINK OD2 ASP B 156 CD CD B1201 1555 1555 2.53 LINK OD1 ASP B 176 CD CD B1197 1555 1555 2.55 LINK OD2 ASP B 176 CD CD B1197 1555 1555 2.55 LINK NE2 HIS B 177 CD CD B1198 1555 1555 2.37 LINK O GLY B 186 CD CD B1196 1555 1555 2.58 LINK OD1 ASP B 189 CD CD B1196 1555 1555 2.38 LINK OD2 ASP B 189 CD CD B1196 1555 1555 2.39 LINK C HT7 C 1 N ALA C 2 1555 1555 1.33 LINK C ARG C 3 N B3E C 4 1555 1555 1.33 LINK C B3E C 4 N ILE C 5 1555 1555 1.33 LINK C ALA C 7 N B3Q C 8 1555 1555 1.33 LINK C B3Q C 8 N AHP C 9 1555 1555 1.34 LINK C AHP C 9 N ARG C 10 1555 1555 1.33 LINK C ARG C 10 N HR7 C 11 1555 1555 1.33 LINK C HR7 C 11 N MET C 12 1555 1555 1.34 LINK C ASP C 14 N B3D C 15 1555 1555 1.33 LINK C B3D C 15 N LEU C 16 1555 1555 1.33 LINK C ASN C 17 N B3A C 18 1555 1555 1.33 LINK C B3A C 18 N GLN C 19 1555 1555 1.33 LINK C TYR C 20 N NH2 C 21 1555 1555 1.33 LINK C ACE D -1 N HT7 D 1 1555 1555 1.33 LINK C HT7 D 1 N ALA D 2 1555 1555 1.33 LINK C ARG D 3 N B3E D 4 1555 1555 1.33 LINK OF2 B3E D 4 CD A CD B1200 1555 1555 2.68 LINK C B3E D 4 N ILE D 5 1555 1555 1.33 LINK C ALA D 7 N B3Q D 8 1555 1555 1.33 LINK C B3Q D 8 N AHP D 9 1555 1555 1.34 LINK C AHP D 9 N ARG D 10 1555 1555 1.33 LINK C ARG D 10 N HR7 D 11 1555 1555 1.33 LINK C HR7 D 11 N MET D 12 1555 1555 1.33 LINK C ASP D 14 N B3D D 15 1555 1555 1.33 LINK C B3D D 15 N LEU D 16 1555 1555 1.34 LINK C ASN D 17 N B3A D 18 1555 1555 1.33 LINK C B3A D 18 N GLN D 19 1555 1555 1.33 LINK C TYR D 20 N NH2 D 21 1555 1555 1.33 LINK CD A CD A1196 O HOH A2059 1555 1555 2.52 LINK CD CD A1197 O HOH A2023 1555 1555 2.45 LINK CD CD A1197 O HOH A2043 1555 1555 2.39 LINK CD CD A1197 O HOH A2042 1555 1555 2.34 LINK CD CD A1199 O HOH A2066 1555 1555 2.59 LINK CD CD A1199 O HOH A2051 1555 1555 2.39 LINK CD CD A1199 O HOH A2064 1555 1555 2.40 LINK CD CD A1199 O HOH A2065 1555 1555 2.39 LINK CD CD A1201 O HOH A2068 1555 1555 2.25 LINK CD CD A1201 O HOH A2069 1555 1555 2.24 LINK CD CD B1197 O HOH B2058 1555 1555 2.33 LINK CD CD B1197 O HOH B2073 1555 1555 2.33 LINK CD CD B1197 O HOH B2074 1555 1555 2.44 LINK CD CD B1198 O HOH B2059 1555 1555 2.37 LINK CD CD B1198 O HOH B2060 1555 1555 2.48 LINK CD CD B1198 O HOH B2063 1555 1555 2.48 LINK CD CD B1199 O HOH B2026 1555 1555 2.38 LINK CD CD B1199 O HOH B2012 1555 1555 2.38 LINK CD CD B1199 O HOH B2075 1555 1555 2.69 LINK CD CD B1201 O HOH B2053 1555 1555 2.40 LINK CD A CD B1204 O HOH B2076 1555 1555 2.46 LINK CD B CD B1204 O HOH B2076 1555 1555 2.46 LINK OE2 GLU A 158 CD A CD A1196 1555 3544 2.44 LINK O GLY A 186 CD CD B1197 1555 3654 2.33 LINK OE1 GLU B 124 CD CD A1201 1555 3644 2.47 LINK OE2 GLU B 124 CD CD A1201 1555 3644 2.40 SITE 1 AC1 3 GLY B 186 ASP B 189 HOH B2069 SITE 1 AC2 6 GLY A 186 ASP A 189 ASP B 176 HOH B2058 SITE 2 AC2 6 HOH B2073 HOH B2074 SITE 1 AC3 4 HIS B 177 HOH B2059 HOH B2060 HOH B2063 SITE 1 AC4 3 GLU A 129 GLU A 158 HOH A2059 SITE 1 AC5 4 GLU A 92 HOH A2023 HOH A2042 HOH A2043 SITE 1 AC6 1 HIS A 113 SITE 1 AC7 5 GLU A 153 HOH A2051 HOH A2064 HOH A2065 SITE 2 AC7 5 HOH A2066 SITE 1 AC8 5 GLN B 88 GLU B 92 HOH B2012 HOH B2026 SITE 2 AC8 5 HOH B2075 SITE 1 AC9 3 GLU B 129 ARG D 3 B3E D 4 SITE 1 BC1 3 ASP B 156 HOH B2052 HOH B2053 SITE 1 BC2 1 HIS A 177 SITE 1 BC3 2 HIS B 113 B3D C 15 SITE 1 BC4 2 HIS B 113 B3D C 15 SITE 1 BC5 2 GLU B 158 HOH B2076 SITE 1 BC6 4 GLU A 179 HOH A2068 HOH A2069 GLU B 124 SITE 1 BC7 4 ASN B 136 HOH B2047 HOH B2077 HOH B2078 SITE 1 BC8 4 GLN A 88 ARG A 91 ASP B 11 ARG B 91 CRYST1 65.175 72.133 80.579 90.00 90.00 90.00 P 21 21 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.015343 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013863 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012410 0.00000 ATOM 1 N MET A 1 22.626 -42.431 -26.465 1.00 75.82 N ANISOU 1 N MET A 1 11891 9407 7511 1685 -375 -797 N ATOM 2 CA MET A 1 22.652 -42.995 -25.118 1.00 71.68 C ANISOU 2 CA MET A 1 11022 9003 7208 1393 -442 -861 C ATOM 3 C MET A 1 23.761 -42.395 -24.251 1.00 65.88 C ANISOU 3 C MET A 1 10006 8453 6570 1297 -61 -765 C ATOM 4 O MET A 1 23.537 -42.063 -23.084 1.00 61.05 O ANISOU 4 O MET A 1 9071 8000 6126 1044 -99 -791 O ATOM 5 CB MET A 1 22.802 -44.517 -25.183 1.00 74.72 C ANISOU 5 CB MET A 1 11569 9239 7582 1479 -635 -950 C ATOM 6 CG MET A 1 23.159 -45.176 -23.859 1.00 72.62 C ANISOU 6 CG MET A 1 11004 9084 7504 1259 -627 -982 C ATOM 7 SD MET A 1 24.656 -46.178 -24.002 1.00101.09 S ANISOU 7 SD MET A 1 14775 12624 11011 1484 -364 -955 S ATOM 8 CE MET A 1 24.442 -46.839 -25.656 1.00 64.51 C ANISOU 8 CE MET A 1 10681 7715 6113 1851 -539 -986 C ATOM 9 N SER A 2 24.954 -42.254 -24.822 1.00 62.92 N ANISOU 9 N SER A 2 9754 8031 6120 1527 301 -632 N ATOM 10 CA SER A 2 26.098 -41.759 -24.065 1.00 59.04 C ANISOU 10 CA SER A 2 8959 7647 5827 1472 664 -520 C ATOM 11 C SER A 2 25.968 -40.279 -23.719 1.00 54.14 C ANISOU 11 C SER A 2 8092 7140 5340 1348 791 -457 C ATOM 12 O SER A 2 26.330 -39.862 -22.618 1.00 49.24 O ANISOU 12 O SER A 2 7124 6646 4940 1190 869 -466 O ATOM 13 CB SER A 2 27.404 -42.000 -24.826 1.00 64.60 C ANISOU 13 CB SER A 2 9803 8217 6525 1752 1050 -326 C ATOM 14 OG SER A 2 28.519 -41.561 -24.066 1.00 63.75 O ANISOU 14 OG SER A 2 9310 8157 6754 1680 1374 -192 O ATOM 15 N GLN A 3 25.470 -39.491 -24.670 1.00 51.16 N ANISOU 15 N GLN A 3 7906 6702 4829 1458 799 -394 N ATOM 16 CA GLN A 3 25.292 -38.066 -24.456 1.00 49.92 C ANISOU 16 CA GLN A 3 7549 6626 4792 1364 914 -332 C ATOM 17 C GLN A 3 24.226 -37.847 -23.387 1.00 44.88 C ANISOU 17 C GLN A 3 6697 6145 4211 1072 600 -503 C ATOM 18 O GLN A 3 24.369 -36.981 -22.530 1.00 43.60 O ANISOU 18 O GLN A 3 6243 6099 4223 942 683 -502 O ATOM 19 CB GLN A 3 24.898 -37.362 -25.759 1.00 49.60 C ANISOU 19 CB GLN A 3 7809 6474 4562 1582 966 -225 C ATOM 20 CG GLN A 3 25.882 -37.557 -26.899 0.00 51.81 C ANISOU 20 CG GLN A 3 8372 6574 4741 1936 1291 -2 C ATOM 21 CD GLN A 3 25.408 -36.920 -28.191 0.00 53.37 C ANISOU 21 CD GLN A 3 8936 6648 4695 2217 1316 103 C ATOM 22 OE1 GLN A 3 24.748 -35.881 -28.180 0.00 51.86 O ANISOU 22 OE1 GLN A 3 8666 6512 4527 2134 1261 95 O ATOM 23 NE2 GLN A 3 25.738 -37.547 -29.315 0.00 56.94 N ANISOU 23 NE2 GLN A 3 9820 6920 4893 2588 1396 204 N ATOM 24 N SER A 4 23.161 -38.642 -23.449 1.00 42.75 N ANISOU 24 N SER A 4 6554 5847 3843 994 241 -624 N ATOM 25 CA SER A 4 22.079 -38.574 -22.477 1.00 40.39 C ANISOU 25 CA SER A 4 6043 5647 3657 730 -36 -710 C ATOM 26 C SER A 4 22.603 -38.889 -21.089 1.00 32.45 C ANISOU 26 C SER A 4 4755 4775 2798 589 -14 -735 C ATOM 27 O SER A 4 22.272 -38.213 -20.131 1.00 28.91 O ANISOU 27 O SER A 4 4059 4450 2474 442 -62 -738 O ATOM 28 CB SER A 4 20.978 -39.580 -22.826 1.00 44.69 C ANISOU 28 CB SER A 4 6720 6074 4187 700 -381 -782 C ATOM 29 OG SER A 4 20.469 -39.333 -24.115 1.00 55.83 O ANISOU 29 OG SER A 4 8410 7346 5457 885 -468 -784 O ATOM 30 N ASN A 5 23.409 -39.941 -20.987 1.00 33.17 N ANISOU 30 N ASN A 5 4889 4839 2877 669 39 -752 N ATOM 31 CA ASN A 5 23.916 -40.360 -19.687 1.00 31.88 C ANISOU 31 CA ASN A 5 4450 4823 2841 569 18 -789 C ATOM 32 C ASN A 5 24.812 -39.305 -19.101 1.00 30.21 C ANISOU 32 C ASN A 5 3949 4696 2834 539 227 -732 C ATOM 33 O ASN A 5 24.720 -38.992 -17.926 1.00 27.21 O ANISOU 33 O ASN A 5 3309 4427 2601 383 103 -756 O ATOM 34 CB ASN A 5 24.658 -41.690 -19.803 1.00 32.41 C ANISOU 34 CB ASN A 5 4628 4814 2874 683 48 -809 C ATOM 35 CG ASN A 5 23.713 -42.858 -19.898 1.00 41.11 C ANISOU 35 CG ASN A 5 5870 5808 3943 618 -267 -865 C ATOM 36 OD1 ASN A 5 22.548 -42.765 -19.474 1.00 42.73 O ANISOU 36 OD1 ASN A 5 5962 6029 4243 445 -487 -854 O ATOM 37 ND2 ASN A 5 24.197 -43.971 -20.451 1.00 38.04 N ANISOU 37 ND2 ASN A 5 5703 5274 3477 771 -270 -900 N ATOM 38 N ARG A 6 25.689 -38.769 -19.941 1.00 28.41 N ANISOU 38 N ARG A 6 3773 4359 2660 711 544 -626 N ATOM 39 CA ARG A 6 26.569 -37.684 -19.560 1.00 32.24 C ANISOU 39 CA ARG A 6 3936 4817 3499 675 729 -526 C ATOM 40 C ARG A 6 25.755 -36.491 -19.035 1.00 29.85 C ANISOU 40 C ARG A 6 3497 4615 3231 524 567 -595 C ATOM 41 O ARG A 6 26.071 -35.944 -17.984 1.00 28.65 O ANISOU 41 O ARG A 6 3055 4495 3337 398 443 -637 O ATOM 42 CB ARG A 6 27.413 -37.279 -20.769 1.00 45.45 C ANISOU 42 CB ARG A 6 5713 6319 5238 930 1165 -330 C ATOM 43 CG ARG A 6 28.037 -35.900 -20.674 1.00 52.34 C ANISOU 43 CG ARG A 6 6254 7101 6534 903 1367 -186 C ATOM 44 CD ARG A 6 29.307 -35.908 -19.852 1.00 52.37 C ANISOU 44 CD ARG A 6 5817 6987 7093 821 1389 -108 C ATOM 45 NE ARG A 6 29.881 -34.569 -19.746 1.00 54.47 N ANISOU 45 NE ARG A 6 5746 7097 7853 762 1464 17 N ATOM 46 CZ ARG A 6 31.002 -34.286 -19.093 1.00 57.28 C ANISOU 46 CZ ARG A 6 5739 7273 8753 660 1359 89 C ATOM 47 NH1 ARG A 6 31.685 -35.254 -18.495 1.00 60.63 N ANISOU 47 NH1 ARG A 6 6043 7676 9318 639 1247 60 N ATOM 48 NH2 ARG A 6 31.440 -33.037 -19.042 1.00 60.41 N ANISOU 48 NH2 ARG A 6 5922 7477 9555 583 1335 189 N ATOM 49 N GLU A 7 24.694 -36.117 -19.753 1.00 29.70 N ANISOU 49 N GLU A 7 3715 4626 2945 564 528 -624 N ATOM 50 CA GLU A 7 23.854 -34.983 -19.347 1.00 30.72 C ANISOU 50 CA GLU A 7 3732 4840 3102 444 403 -676 C ATOM 51 C GLU A 7 23.202 -35.218 -18.002 1.00 24.07 C ANISOU 51 C GLU A 7 2735 4141 2268 271 122 -787 C ATOM 52 O GLU A 7 23.025 -34.292 -17.227 1.00 21.01 O ANISOU 52 O GLU A 7 2175 3809 1997 197 48 -833 O ATOM 53 CB GLU A 7 22.727 -34.736 -20.353 1.00 40.66 C ANISOU 53 CB GLU A 7 5283 6072 4093 512 348 -673 C ATOM 54 CG GLU A 7 23.149 -34.236 -21.710 1.00 52.50 C ANISOU 54 CG GLU A 7 7007 7422 5519 722 626 -536 C ATOM 55 CD GLU A 7 21.949 -33.762 -22.508 1.00 60.24 C ANISOU 55 CD GLU A 7 8206 8351 6330 727 466 -537 C ATOM 56 OE1 GLU A 7 20.961 -33.324 -21.872 1.00 61.34 O ANISOU 56 OE1 GLU A 7 8219 8574 6514 568 252 -608 O ATOM 57 OE2 GLU A 7 21.982 -33.833 -23.756 1.00 66.32 O ANISOU 57 OE2 GLU A 7 9258 8993 6949 917 540 -452 O ATOM 58 N LEU A 8 22.786 -36.462 -17.755 1.00 21.86 N ANISOU 58 N LEU A 8 2547 3877 1881 240 -22 -796 N ATOM 59 CA LEU A 8 22.156 -36.804 -16.503 1.00 19.04 C ANISOU 59 CA LEU A 8 2069 3552 1611 133 -177 -761 C ATOM 60 C LEU A 8 23.127 -36.680 -15.324 1.00 17.33 C ANISOU 60 C LEU A 8 1665 3433 1485 131 -208 -832 C ATOM 61 O LEU A 8 22.786 -36.134 -14.277 1.00 18.62 O ANISOU 61 O LEU A 8 1773 3597 1706 122 -259 -814 O ATOM 62 CB LEU A 8 21.569 -38.209 -16.588 1.00 20.54 C ANISOU 62 CB LEU A 8 2372 3665 1768 114 -272 -704 C ATOM 63 CG LEU A 8 20.808 -38.627 -15.346 1.00 23.88 C ANISOU 63 CG LEU A 8 2689 4134 2250 57 -337 -635 C ATOM 64 CD1 LEU A 8 19.620 -37.666 -15.133 1.00 28.89 C ANISOU 64 CD1 LEU A 8 3282 4788 2905 31 -337 -598 C ATOM 65 CD2 LEU A 8 20.320 -40.064 -15.571 1.00 30.00 C ANISOU 65 CD2 LEU A 8 3525 4854 3020 32 -462 -606 C ATOM 66 N VAL A 9 24.325 -37.230 -15.483 1.00 18.94 N ANISOU 66 N VAL A 9 1820 3606 1771 173 -155 -853 N ATOM 67 CA VAL A 9 25.376 -37.066 -14.481 1.00 18.14 C ANISOU 67 CA VAL A 9 1522 3482 1887 177 -247 -890 C ATOM 68 C VAL A 9 25.664 -35.582 -14.183 1.00 18.82 C ANISOU 68 C VAL A 9 1452 3511 2187 168 -302 -956 C ATOM 69 O VAL A 9 25.682 -35.162 -13.030 1.00 21.31 O ANISOU 69 O VAL A 9 1743 3830 2522 181 -503 -1039 O ATOM 70 CB VAL A 9 26.689 -37.771 -14.907 1.00 20.56 C ANISOU 70 CB VAL A 9 1752 3647 2414 231 -122 -815 C ATOM 71 CG1 VAL A 9 27.812 -37.417 -13.933 1.00 20.25 C ANISOU 71 CG1 VAL A 9 1458 3522 2714 230 -288 -858 C ATOM 72 CG2 VAL A 9 26.500 -39.293 -14.943 1.00 19.74 C ANISOU 72 CG2 VAL A 9 1794 3580 2127 247 -135 -784 C ATOM 73 N VAL A 10 25.888 -34.800 -15.226 1.00 21.37 N ANISOU 73 N VAL A 10 1737 3717 2666 181 -101 -884 N ATOM 74 CA VAL A 10 26.210 -33.382 -15.042 1.00 25.41 C ANISOU 74 CA VAL A 10 2058 4117 3478 164 -146 -922 C ATOM 75 C VAL A 10 25.061 -32.650 -14.354 1.00 23.34 C ANISOU 75 C VAL A 10 1883 3992 2992 137 -327 -1053 C ATOM 76 O VAL A 10 25.275 -31.825 -13.481 1.00 23.52 O ANISOU 76 O VAL A 10 1854 3924 3159 148 -516 -1147 O ATOM 77 CB VAL A 10 26.570 -32.680 -16.380 1.00 24.23 C ANISOU 77 CB VAL A 10 1862 3808 3537 215 184 -752 C ATOM 78 CG1 VAL A 10 26.699 -31.145 -16.185 1.00 25.08 C ANISOU 78 CG1 VAL A 10 1756 3782 3993 179 122 -779 C ATOM 79 CG2 VAL A 10 27.856 -33.239 -16.937 1.00 29.18 C ANISOU 79 CG2 VAL A 10 2359 4257 4470 297 424 -581 C ATOM 80 N ASP A 11 23.836 -32.983 -14.730 1.00 23.71 N ANISOU 80 N ASP A 11 2126 4184 2698 126 -259 -1023 N ATOM 81 CA ASP A 11 22.688 -32.366 -14.098 1.00 21.83 C ANISOU 81 CA ASP A 11 1995 3974 2327 136 -303 -1016 C ATOM 82 C ASP A 11 22.665 -32.636 -12.599 1.00 22.61 C ANISOU 82 C ASP A 11 2170 4030 2392 203 -406 -998 C ATOM 83 O ASP A 11 22.513 -31.716 -11.796 1.00 20.76 O ANISOU 83 O ASP A 11 1961 3750 2176 264 -496 -1060 O ATOM 84 CB ASP A 11 21.363 -32.823 -14.726 1.00 17.26 C ANISOU 84 CB ASP A 11 1550 3416 1592 110 -209 -874 C ATOM 85 CG ASP A 11 20.174 -32.158 -14.048 1.00 22.76 C ANISOU 85 CG ASP A 11 2275 4110 2261 127 -217 -827 C ATOM 86 OD1 ASP A 11 19.824 -31.047 -14.488 1.00 23.96 O ANISOU 86 OD1 ASP A 11 2400 4265 2439 121 -200 -865 O ATOM 87 OD2 ASP A 11 19.662 -32.671 -13.032 1.00 23.56 O ANISOU 87 OD2 ASP A 11 2407 4243 2301 167 -237 -778 O ATOM 88 N PHE A 12 22.859 -33.895 -12.216 1.00 21.33 N ANISOU 88 N PHE A 12 2054 3890 2159 214 -411 -935 N ATOM 89 CA PHE A 12 22.759 -34.273 -10.817 1.00 22.16 C ANISOU 89 CA PHE A 12 2249 4004 2167 306 -498 -919 C ATOM 90 C PHE A 12 23.903 -33.670 -9.997 1.00 22.01 C ANISOU 90 C PHE A 12 2216 3880 2267 378 -705 -1055 C ATOM 91 O PHE A 12 23.691 -33.101 -8.914 1.00 22.80 O ANISOU 91 O PHE A 12 2424 3960 2279 497 -818 -1112 O ATOM 92 CB PHE A 12 22.745 -35.807 -10.694 1.00 22.57 C ANISOU 92 CB PHE A 12 2330 4109 2137 299 -461 -824 C ATOM 93 CG PHE A 12 22.520 -36.294 -9.292 1.00 22.25 C ANISOU 93 CG PHE A 12 2387 4127 1941 428 -520 -793 C ATOM 94 CD1 PHE A 12 23.587 -36.450 -8.413 1.00 25.92 C ANISOU 94 CD1 PHE A 12 2896 4541 2410 517 -683 -869 C ATOM 95 CD2 PHE A 12 21.251 -36.624 -8.858 1.00 25.52 C ANISOU 95 CD2 PHE A 12 2841 4659 2195 491 -421 -683 C ATOM 96 CE1 PHE A 12 23.382 -36.893 -7.130 1.00 26.92 C ANISOU 96 CE1 PHE A 12 3162 4729 2337 687 -733 -839 C ATOM 97 CE2 PHE A 12 21.044 -37.086 -7.563 1.00 23.36 C ANISOU 97 CE2 PHE A 12 2678 4474 1722 679 -429 -627 C ATOM 98 CZ PHE A 12 22.106 -37.209 -6.694 1.00 27.68 C ANISOU 98 CZ PHE A 12 3327 4960 2231 787 -581 -709 C ATOM 99 N LEU A 13 25.113 -33.781 -10.536 1.00 23.79 N ANISOU 99 N LEU A 13 2295 4019 2727 321 -777 -1110 N ATOM 100 CA LEU A 13 26.267 -33.166 -9.908 1.00 23.01 C ANISOU 100 CA LEU A 13 2115 3739 2890 361 -1019 -1221 C ATOM 101 C LEU A 13 26.131 -31.655 -9.755 1.00 28.16 C ANISOU 101 C LEU A 13 2749 4276 3676 387 -1121 -1322 C ATOM 102 O LEU A 13 26.489 -31.126 -8.715 1.00 28.78 O ANISOU 102 O LEU A 13 2903 4235 3798 497 -1354 -1432 O ATOM 103 CB LEU A 13 27.573 -33.536 -10.631 1.00 26.69 C ANISOU 103 CB LEU A 13 2330 4078 3734 284 -1038 -1199 C ATOM 104 CG LEU A 13 27.895 -35.038 -10.668 1.00 26.07 C ANISOU 104 CG LEU A 13 2256 4090 3561 285 -986 -1126 C ATOM 105 CD1 LEU A 13 29.203 -35.253 -11.362 1.00 26.49 C ANISOU 105 CD1 LEU A 13 2017 3979 4071 241 -957 -1069 C ATOM 106 CD2 LEU A 13 27.929 -35.643 -9.268 1.00 24.61 C ANISOU 106 CD2 LEU A 13 2261 3924 3166 390 -1160 -1145 C ATOM 107 N SER A 14 25.626 -30.974 -10.784 1.00 28.23 N ANISOU 107 N SER A 14 2666 4311 3750 307 -966 -1301 N ATOM 108 CA SER A 14 25.354 -29.536 -10.686 1.00 25.85 C ANISOU 108 CA SER A 14 2346 3905 3570 330 -1046 -1390 C ATOM 109 C SER A 14 24.465 -29.241 -9.485 1.00 31.23 C ANISOU 109 C SER A 14 3268 4662 3937 481 -1123 -1444 C ATOM 110 O SER A 14 24.736 -28.314 -8.719 1.00 31.33 O ANISOU 110 O SER A 14 3323 4529 4051 588 -1345 -1580 O ATOM 111 CB SER A 14 24.658 -29.017 -11.963 1.00 26.99 C ANISOU 111 CB SER A 14 2397 4127 3730 239 -826 -1337 C ATOM 112 OG SER A 14 25.509 -29.109 -13.104 1.00 30.00 O ANISOU 112 OG SER A 14 2521 4415 4462 148 -698 -1253 O ATOM 113 N TYR A 15 23.395 -30.025 -9.336 1.00 25.06 N ANISOU 113 N TYR A 15 2622 4077 2823 507 -941 -1325 N ATOM 114 CA TYR A 15 22.441 -29.838 -8.248 1.00 26.47 C ANISOU 114 CA TYR A 15 2991 4333 2732 669 -946 -1322 C ATOM 115 C TYR A 15 23.075 -29.988 -6.868 1.00 30.74 C ANISOU 115 C TYR A 15 3689 4803 3189 858 -1177 -1423 C ATOM 116 O TYR A 15 22.928 -29.119 -6.001 1.00 32.44 O ANISOU 116 O TYR A 15 4043 4953 3330 1041 -1333 -1544 O ATOM 117 CB TYR A 15 21.286 -30.821 -8.412 1.00 25.27 C ANISOU 117 CB TYR A 15 2878 4355 2366 647 -711 -1138 C ATOM 118 CG TYR A 15 20.193 -30.742 -7.380 1.00 27.34 C ANISOU 118 CG TYR A 15 3300 4715 2371 834 -655 -1090 C ATOM 119 CD1 TYR A 15 19.538 -29.536 -7.117 1.00 31.75 C ANISOU 119 CD1 TYR A 15 3920 5266 2878 934 -667 -1154 C ATOM 120 CD2 TYR A 15 19.766 -31.882 -6.705 1.00 27.23 C ANISOU 120 CD2 TYR A 15 3374 4809 2163 938 -561 -963 C ATOM 121 CE1 TYR A 15 18.521 -29.468 -6.190 1.00 34.11 C ANISOU 121 CE1 TYR A 15 4382 5655 2923 1151 -571 -1086 C ATOM 122 CE2 TYR A 15 18.738 -31.830 -5.775 1.00 30.37 C ANISOU 122 CE2 TYR A 15 3921 5302 2317 1163 -447 -875 C ATOM 123 CZ TYR A 15 18.117 -30.610 -5.526 1.00 35.74 C ANISOU 123 CZ TYR A 15 4677 5966 2938 1274 -442 -932 C ATOM 124 OH TYR A 15 17.099 -30.538 -4.603 1.00 38.08 O ANISOU 124 OH TYR A 15 5139 6339 2990 1540 -280 -812 O ATOM 125 N ALYS A 16 23.762 -31.101 -6.660 0.68 31.90 N ANISOU 125 N ALYS A 16 3834 4956 3330 844 -1211 -1382 N ATOM 126 N BLYS A 16 23.801 -31.089 -6.680 0.32 31.43 N ANISOU 126 N BLYS A 16 3770 4892 3282 840 -1216 -1385 N ATOM 127 CA ALYS A 16 24.353 -31.396 -5.368 0.68 33.36 C ANISOU 127 CA ALYS A 16 4188 5080 3408 1047 -1435 -1470 C ATOM 128 CA BLYS A 16 24.471 -31.404 -5.418 0.32 33.12 C ANISOU 128 CA BLYS A 16 4140 5035 3407 1034 -1449 -1476 C ATOM 129 C ALYS A 16 25.452 -30.415 -5.005 0.68 34.25 C ANISOU 129 C ALYS A 16 4271 4942 3801 1116 -1784 -1680 C ATOM 130 C BLYS A 16 25.374 -30.290 -4.929 0.32 34.16 C ANISOU 130 C BLYS A 16 4279 4927 3773 1137 -1793 -1692 C ATOM 131 O ALYS A 16 25.606 -30.050 -3.842 0.68 35.46 O ANISOU 131 O ALYS A 16 4633 5003 3839 1366 -2026 -1815 O ATOM 132 O BLYS A 16 25.247 -29.824 -3.796 0.32 35.57 O ANISOU 132 O BLYS A 16 4685 5047 3784 1396 -1985 -1811 O ATOM 133 CB ALYS A 16 24.871 -32.830 -5.350 0.68 33.31 C ANISOU 133 CB ALYS A 16 4156 5130 3369 998 -1397 -1373 C ATOM 134 CB BLYS A 16 25.328 -32.660 -5.572 0.32 28.29 C ANISOU 134 CB BLYS A 16 3451 4427 2872 951 -1465 -1414 C ATOM 135 CG ALYS A 16 23.740 -33.838 -5.297 0.68 30.17 C ANISOU 135 CG ALYS A 16 3832 4935 2696 1018 -1125 -1184 C ATOM 136 CG BLYS A 16 24.565 -33.915 -5.913 0.32 29.10 C ANISOU 136 CG BLYS A 16 3558 4719 2780 885 -1194 -1220 C ATOM 137 CD ALYS A 16 23.096 -33.809 -3.928 0.68 34.27 C ANISOU 137 CD ALYS A 16 4612 5517 2893 1318 -1136 -1176 C ATOM 138 CD BLYS A 16 23.509 -34.242 -4.869 0.32 30.58 C ANISOU 138 CD BLYS A 16 3961 5039 2620 1100 -1093 -1140 C ATOM 139 CE ALYS A 16 21.643 -34.212 -3.974 0.68 34.02 C ANISOU 139 CE ALYS A 16 4607 5657 2662 1363 -833 -977 C ATOM 140 CE BLYS A 16 22.126 -34.028 -5.441 0.32 25.34 C ANISOU 140 CE BLYS A 16 3253 4493 1880 1041 -838 -1014 C ATOM 141 NZ ALYS A 16 21.056 -34.231 -2.615 0.68 36.76 N ANISOU 141 NZ ALYS A 16 5224 6058 2686 1719 -786 -924 N ATOM 142 NZ BLYS A 16 21.075 -34.847 -4.775 0.32 36.25 N ANISOU 142 NZ BLYS A 16 4745 6027 3000 1206 -647 -837 N ATOM 143 N ALEU A 17 26.207 -29.972 -6.001 0.68 31.06 N ANISOU 143 N ALEU A 17 3612 4394 3796 926 -1822 -1704 N ATOM 144 N BLEU A 17 26.305 -29.891 -5.788 0.32 31.74 N ANISOU 144 N BLEU A 17 3724 4450 3886 963 -1881 -1735 N ATOM 145 CA ALEU A 17 27.196 -28.933 -5.763 0.68 34.30 C ANISOU 145 CA ALEU A 17 3932 4498 4604 975 -2156 -1881 C ATOM 146 CA BLEU A 17 27.237 -28.820 -5.478 0.32 35.14 C ANISOU 146 CA BLEU A 17 4084 4572 4695 1031 -2227 -1920 C ATOM 147 C ALEU A 17 26.549 -27.631 -5.302 0.68 38.22 C ANISOU 147 C ALEU A 17 4556 4929 5036 1127 -2273 -2013 C ATOM 148 C BLEU A 17 26.501 -27.549 -5.074 0.32 38.48 C ANISOU 148 C BLEU A 17 4638 4953 5030 1177 -2315 -2039 C ATOM 149 O ALEU A 17 27.103 -26.924 -4.460 0.68 39.95 O ANISOU 149 O ALEU A 17 4866 4906 5406 1315 -2637 -2199 O ATOM 150 O BLEU A 17 26.881 -26.882 -4.110 0.32 40.52 O ANISOU 150 O BLEU A 17 5039 5006 5349 1400 -2664 -2224 O ATOM 151 CB ALEU A 17 28.035 -28.683 -7.013 0.68 33.55 C ANISOU 151 CB ALEU A 17 3496 4236 5017 746 -2100 -1821 C ATOM 152 CB BLEU A 17 28.136 -28.543 -6.682 0.32 34.56 C ANISOU 152 CB BLEU A 17 3664 4314 5153 801 -2196 -1870 C ATOM 153 CG ALEU A 17 29.113 -29.737 -7.268 0.68 33.75 C ANISOU 153 CG ALEU A 17 3363 4193 5265 655 -2112 -1737 C ATOM 154 CG BLEU A 17 29.107 -29.668 -7.042 0.32 34.86 C ANISOU 154 CG BLEU A 17 3542 4320 5382 691 -2164 -1766 C ATOM 155 CD1ALEU A 17 29.690 -29.565 -8.656 0.68 32.87 C ANISOU 155 CD1ALEU A 17 2917 3964 5608 453 -1919 -1600 C ATOM 156 CD1BLEU A 17 29.689 -29.438 -8.424 0.32 33.38 C ANISOU 156 CD1BLEU A 17 3016 4005 5663 485 -1981 -1636 C ATOM 157 CD2ALEU A 17 30.207 -29.622 -6.200 0.68 38.13 C ANISOU 157 CD2ALEU A 17 3950 4460 6077 800 -2528 -1888 C ATOM 158 CD2BLEU A 17 30.210 -29.756 -5.992 0.32 38.37 C ANISOU 158 CD2BLEU A 17 4026 4504 6049 832 -2559 -1902 C ATOM 159 N ASER A 18 25.380 -27.319 -5.850 0.68 34.91 N ANISOU 159 N ASER A 18 4151 4702 4413 1065 -1995 -1923 N ATOM 160 N BSER A 18 25.440 -27.232 -5.812 0.32 35.64 N ANISOU 160 N BSER A 18 4242 4771 4529 1074 -2023 -1939 N ATOM 161 CA ASER A 18 24.719 -26.054 -5.515 0.68 36.87 C ANISOU 161 CA ASER A 18 4499 4896 4613 1200 -2083 -2037 C ATOM 162 CA BSER A 18 24.639 -26.042 -5.540 0.32 37.37 C ANISOU 162 CA BSER A 18 4565 4973 4660 1198 -2065 -2030 C ATOM 163 C ASER A 18 24.023 -26.080 -4.156 0.68 40.35 C ANISOU 163 C ASER A 18 5284 5424 4622 1515 -2159 -2090 C ATOM 164 C BSER A 18 24.023 -26.077 -4.150 0.32 40.18 C ANISOU 164 C BSER A 18 5265 5402 4601 1517 -2161 -2091 C ATOM 165 O ASER A 18 23.823 -25.038 -3.529 0.68 40.15 O ANISOU 165 O ASER A 18 5405 5278 4572 1723 -2368 -2241 O ATOM 166 O BSER A 18 23.873 -25.040 -3.502 0.32 42.80 O ANISOU 166 O BSER A 18 5742 5605 4916 1728 -2384 -2248 O ATOM 167 CB ASER A 18 23.751 -25.612 -6.626 0.68 36.97 C ANISOU 167 CB ASER A 18 4387 5050 4610 1032 -1782 -1929 C ATOM 168 CB BSER A 18 23.532 -25.886 -6.585 0.32 36.26 C ANISOU 168 CB BSER A 18 4331 5029 4417 1035 -1716 -1888 C ATOM 169 OG ASER A 18 22.673 -26.517 -6.802 0.68 35.62 O ANISOU 169 OG ASER A 18 4297 5155 4081 997 -1464 -1745 O ATOM 170 OG BSER A 18 24.067 -25.629 -7.869 0.32 35.43 O ANISOU 170 OG BSER A 18 3948 4829 4685 806 -1641 -1851 O ATOM 171 N GLN A 19 23.666 -27.270 -3.692 1.00 36.54 N ANISOU 171 N GLN A 19 4942 5130 3813 1580 -1992 -1959 N ATOM 172 CA GLN A 19 23.030 -27.410 -2.393 1.00 44.76 C ANISOU 172 CA GLN A 19 6322 6243 4440 1924 -2015 -1968 C ATOM 173 C GLN A 19 23.993 -27.109 -1.248 1.00 49.35 C ANISOU 173 C GLN A 19 7120 6587 5043 2218 -2459 -2191 C ATOM 174 O GLN A 19 23.565 -26.820 -0.129 1.00 48.12 O ANISOU 174 O GLN A 19 7303 6417 4564 2589 -2568 -2259 O ATOM 175 CB GLN A 19 22.441 -28.801 -2.235 1.00 43.53 C ANISOU 175 CB GLN A 19 6228 6315 3998 1925 -1712 -1745 C ATOM 176 CG GLN A 19 21.138 -29.018 -2.994 1.00 40.17 C ANISOU 176 CG GLN A 19 5692 6093 3479 1773 -1320 -1530 C ATOM 177 CD GLN A 19 20.658 -30.427 -2.828 1.00 45.14 C ANISOU 177 CD GLN A 19 6346 6887 3917 1786 -1074 -1313 C ATOM 178 OE1 GLN A 19 21.467 -31.351 -2.765 1.00 42.02 O ANISOU 178 OE1 GLN A 19 5918 6476 3570 1732 -1148 -1306 O ATOM 179 NE2 GLN A 19 19.346 -30.609 -2.727 1.00 43.01 N ANISOU 179 NE2 GLN A 19 6124 6761 3456 1876 -783 -1124 N ATOM 180 N LYS A 20 25.286 -27.186 -1.542 1.00 48.45 N ANISOU 180 N LYS A 20 6821 6263 5324 2081 -2721 -2295 N ATOM 181 CA LYS A 20 26.324 -26.921 -0.555 1.00 56.22 C ANISOU 181 CA LYS A 20 7970 6952 6438 2339 -3214 -2520 C ATOM 182 C LYS A 20 26.955 -25.566 -0.814 1.00 59.58 C ANISOU 182 C LYS A 20 8244 7044 7349 2317 -3568 -2716 C ATOM 183 O LYS A 20 27.870 -25.160 -0.107 1.00 60.22 O ANISOU 183 O LYS A 20 8416 6793 7671 2519 -4052 -2925 O ATOM 184 CB LYS A 20 27.395 -28.014 -0.592 1.00 51.95 C ANISOU 184 CB LYS A 20 7316 6349 6075 2227 -3306 -2492 C ATOM 185 CG LYS A 20 26.850 -29.401 -0.371 1.00 47.95 C ANISOU 185 CG LYS A 20 6928 6141 5150 2240 -2979 -2293 C ATOM 186 CD LYS A 20 26.086 -29.463 0.940 1.00 54.37 C ANISOU 186 CD LYS A 20 8178 7037 5444 2670 -2991 -2313 C ATOM 187 CE LYS A 20 25.669 -30.892 1.270 1.00 56.74 C ANISOU 187 CE LYS A 20 8586 7576 5395 2725 -2695 -2103 C ATOM 188 NZ LYS A 20 25.128 -30.990 2.658 1.00 62.99 N ANISOU 188 NZ LYS A 20 9838 8391 5705 3224 -2726 -2114 N ATOM 189 N GLY A 21 26.471 -24.872 -1.839 1.00 58.13 N ANISOU 189 N GLY A 21 7824 6916 7346 2084 -3347 -2646 N ATOM 190 CA GLY A 21 26.941 -23.528 -2.124 1.00 58.24 C ANISOU 190 CA GLY A 21 7674 6610 7846 2068 -3643 -2802 C ATOM 191 C GLY A 21 27.978 -23.384 -3.226 1.00 56.02 C ANISOU 191 C GLY A 21 6961 6092 8232 1754 -3660 -2750 C ATOM 192 O GLY A 21 28.505 -22.294 -3.435 1.00 58.27 O ANISOU 192 O GLY A 21 7067 6037 9035 1748 -3926 -2856 O ATOM 193 N ATYR A 22 28.254 -24.486 -3.927 0.80 48.28 N ANISOU 193 N ATYR A 22 5814 5272 7261 1516 -3368 -2566 N ATOM 194 N BTYR A 22 28.285 -24.460 -3.942 0.20 49.31 N ANISOU 194 N BTYR A 22 5935 5390 7412 1512 -3376 -2568 N ATOM 195 CA ATYR A 22 29.236 -24.509 -5.008 0.80 48.00 C ANISOU 195 CA ATYR A 22 5384 5025 7829 1243 -3309 -2460 C ATOM 196 CA BTYR A 22 29.230 -24.341 -5.050 0.20 48.63 C ANISOU 196 CA BTYR A 22 5446 5076 7954 1242 -3323 -2469 C ATOM 197 C ATYR A 22 28.552 -24.533 -6.390 0.80 44.47 C ANISOU 197 C ATYR A 22 4744 4809 7343 979 -2833 -2258 C ATOM 198 C BTYR A 22 28.546 -24.539 -6.401 0.20 45.49 C ANISOU 198 C BTYR A 22 4873 4941 7471 977 -2828 -2256 C ATOM 199 O ATYR A 22 27.327 -24.445 -6.480 0.80 46.70 O ANISOU 199 O ATYR A 22 5182 5380 7181 1000 -2603 -2226 O ATOM 200 O BTYR A 22 27.320 -24.584 -6.482 0.20 44.62 O ANISOU 200 O BTYR A 22 4925 5142 6885 994 -2582 -2213 O ATOM 201 CB ATYR A 22 30.141 -25.742 -4.853 0.80 47.72 C ANISOU 201 CB ATYR A 22 5301 4971 7861 1194 -3346 -2394 C ATOM 202 CB BTYR A 22 30.413 -25.299 -4.884 0.20 50.27 C ANISOU 202 CB BTYR A 22 5553 5135 8413 1199 -3460 -2435 C ATOM 203 CG ATYR A 22 30.763 -25.918 -3.473 0.80 51.86 C ANISOU 203 CG ATYR A 22 6062 5293 8348 1474 -3813 -2590 C ATOM 204 CG BTYR A 22 31.689 -24.793 -5.524 0.20 53.54 C ANISOU 204 CG BTYR A 22 5581 5098 9665 1054 -3609 -2388 C ATOM 205 CD1ATYR A 22 31.223 -24.831 -2.742 0.80 57.16 C ANISOU 205 CD1ATYR A 22 6799 5575 9343 1694 -4308 -2815 C ATOM 206 CD1BTYR A 22 32.151 -23.508 -5.269 0.20 59.53 C ANISOU 206 CD1BTYR A 22 6236 5423 10959 1155 -3978 -2526 C ATOM 207 CD2ATYR A 22 30.879 -27.181 -2.903 0.80 62.44 C ANISOU 207 CD2ATYR A 22 7575 6812 9338 1543 -3785 -2553 C ATOM 208 CD2BTYR A 22 32.432 -25.598 -6.375 0.20 54.87 C ANISOU 208 CD2BTYR A 22 5477 5239 10133 838 -3373 -2178 C ATOM 209 CE1ATYR A 22 31.800 -25.009 -1.481 0.80 64.90 C ANISOU 209 CE1ATYR A 22 8040 6340 10280 1993 -4787 -3013 C ATOM 210 CE1BTYR A 22 33.316 -23.037 -5.848 0.20 63.17 C ANISOU 210 CE1BTYR A 22 6311 5408 12283 1030 -4087 -2429 C ATOM 211 CE2ATYR A 22 31.445 -27.367 -1.649 0.80 56.10 C ANISOU 211 CE2ATYR A 22 7021 5814 8480 1827 -4220 -2734 C ATOM 212 CE2BTYR A 22 33.602 -25.138 -6.952 0.20 58.67 C ANISOU 212 CE2BTYR A 22 5589 5266 11437 723 -3448 -2070 C ATOM 213 CZ ATYR A 22 31.903 -26.281 -0.941 0.80 61.56 C ANISOU 213 CZ ATYR A 22 7804 6111 9473 2061 -4730 -2972 C ATOM 214 CZ BTYR A 22 34.036 -23.855 -6.690 0.20 62.33 C ANISOU 214 CZ BTYR A 22 5935 5276 12472 812 -3794 -2182 C ATOM 215 OH ATYR A 22 32.467 -26.480 0.306 0.80 66.81 O ANISOU 215 OH ATYR A 22 8763 6553 10068 2384 -5210 -3172 O ATOM 216 OH BTYR A 22 35.196 -23.394 -7.268 0.20 64.99 O ANISOU 216 OH BTYR A 22 5876 5104 13713 705 -3840 -2022 O ATOM 217 N SER A 23 29.340 -24.639 -7.461 1.00 43.62 N ANISOU 217 N SER A 23 4306 4545 7724 758 -2687 -2108 N ATOM 218 CA SER A 23 28.784 -24.807 -8.811 1.00 41.64 C ANISOU 218 CA SER A 23 3902 4500 7419 548 -2245 -1905 C ATOM 219 C SER A 23 29.667 -25.651 -9.753 1.00 40.48 C ANISOU 219 C SER A 23 3498 4300 7582 377 -2021 -1689 C ATOM 220 O SER A 23 30.887 -25.692 -9.621 1.00 44.02 O ANISOU 220 O SER A 23 3764 4427 8535 367 -2187 -1661 O ATOM 221 CB SER A 23 28.439 -23.456 -9.458 1.00 46.94 C ANISOU 221 CB SER A 23 4433 5019 8385 496 -2186 -1901 C ATOM 222 OG SER A 23 29.596 -22.731 -9.852 1.00 53.40 O ANISOU 222 OG SER A 23 4943 5384 9964 432 -2293 -1834 O ATOM 223 N TRP A 24 29.022 -26.311 -10.706 1.00 36.59 N ANISOU 223 N TRP A 24 2995 4103 6805 270 -1649 -1530 N ATOM 224 CA TRP A 24 29.668 -27.156 -11.708 1.00 33.86 C ANISOU 224 CA TRP A 24 2444 3761 6661 160 -1365 -1302 C ATOM 225 C TRP A 24 30.386 -26.311 -12.745 1.00 39.56 C ANISOU 225 C TRP A 24 2863 4168 7999 82 -1156 -1092 C ATOM 226 O TRP A 24 31.477 -26.657 -13.199 1.00 38.88 O ANISOU 226 O TRP A 24 2569 3863 8340 50 -1023 -898 O ATOM 227 CB TRP A 24 28.600 -28.038 -12.396 1.00 30.56 C ANISOU 227 CB TRP A 24 2151 3738 5724 132 -1063 -1225 C ATOM 228 CG TRP A 24 29.002 -28.601 -13.739 1.00 34.13 C ANISOU 228 CG TRP A 24 2415 4198 6357 81 -672 -972 C ATOM 229 CD1 TRP A 24 28.676 -28.100 -14.970 1.00 32.91 C ANISOU 229 CD1 TRP A 24 2180 4043 6279 74 -316 -793 C ATOM 230 CD2 TRP A 24 29.771 -29.791 -13.984 1.00 33.78 C ANISOU 230 CD2 TRP A 24 2297 4157 6380 91 -547 -848 C ATOM 231 NE1 TRP A 24 29.220 -28.877 -15.963 1.00 31.03 N ANISOU 231 NE1 TRP A 24 1883 3795 6112 122 52 -555 N ATOM 232 CE2 TRP A 24 29.894 -29.926 -15.385 1.00 31.35 C ANISOU 232 CE2 TRP A 24 1904 3838 6171 123 -85 -592 C ATOM 233 CE3 TRP A 24 30.394 -30.736 -13.156 1.00 34.12 C ANISOU 233 CE3 TRP A 24 2370 4194 6400 110 -759 -914 C ATOM 234 CZ2 TRP A 24 30.598 -30.975 -15.974 1.00 37.06 C ANISOU 234 CZ2 TRP A 24 2593 4541 6948 185 179 -412 C ATOM 235 CZ3 TRP A 24 31.090 -31.779 -13.746 1.00 34.86 C ANISOU 235 CZ3 TRP A 24 2356 4277 6612 125 -530 -742 C ATOM 236 CH2 TRP A 24 31.187 -31.890 -15.141 1.00 34.25 C ANISOU 236 CH2 TRP A 24 2208 4184 6622 169 -56 -497 C ATOM 237 N SER A 25 29.780 -25.183 -13.102 1.00 40.01 N ANISOU 237 N SER A 25 2905 4179 8117 69 -1097 -1100 N ATOM 238 CA SER A 25 30.290 -24.345 -14.174 1.00 39.42 C ANISOU 238 CA SER A 25 2586 3822 8571 17 -814 -840 C ATOM 239 C SER A 25 29.645 -22.980 -14.073 1.00 40.11 C ANISOU 239 C SER A 25 2687 3807 8744 23 -928 -947 C ATOM 240 O SER A 25 28.701 -22.794 -13.300 1.00 38.61 O ANISOU 240 O SER A 25 2715 3822 8132 77 -1163 -1207 O ATOM 241 CB SER A 25 29.947 -24.950 -15.534 1.00 41.93 C ANISOU 241 CB SER A 25 2910 4365 8656 16 -291 -561 C ATOM 242 OG SER A 25 28.543 -24.860 -15.789 1.00 37.47 O ANISOU 242 OG SER A 25 2531 4138 7568 31 -206 -652 O ATOM 243 N GLN A 26 30.156 -22.027 -14.852 1.00 40.76 N ANISOU 243 N GLN A 26 2550 3555 9380 -9 -733 -720 N ATOM 244 CA GLN A 26 29.565 -20.690 -14.910 1.00 42.93 C ANISOU 244 CA GLN A 26 2808 3705 9796 -6 -796 -781 C ATOM 245 C GLN A 26 28.115 -20.755 -15.404 1.00 42.14 C ANISOU 245 C GLN A 26 2902 4038 9071 -6 -579 -806 C ATOM 246 O GLN A 26 27.214 -20.182 -14.790 1.00 44.17 O ANISOU 246 O GLN A 26 3295 4404 9085 25 -808 -1050 O ATOM 247 CB GLN A 26 30.407 -19.756 -15.783 1.00 56.21 C ANISOU 247 CB GLN A 26 4214 4930 12211 -30 -551 -452 C ATOM 248 CG GLN A 26 29.804 -18.376 -15.978 1.00 66.82 C ANISOU 248 CG GLN A 26 5521 6129 13737 -28 -567 -470 C ATOM 249 CD GLN A 26 29.491 -17.677 -14.665 1.00 74.91 C ANISOU 249 CD GLN A 26 6626 7050 14786 36 -1134 -884 C ATOM 250 OE1 GLN A 26 28.386 -17.794 -14.136 1.00 74.20 O ANISOU 250 OE1 GLN A 26 6783 7320 14090 77 -1273 -1143 O ATOM 251 NE2 GLN A 26 30.462 -16.937 -14.138 1.00 80.87 N ANISOU 251 NE2 GLN A 26 7184 7288 16255 92 -1461 -929 N ATOM 252 N MET A 83 27.878 -21.482 -16.536 1.00 37.67 N ANISOU 252 N MET A 83 2373 3703 8238 1 -130 -547 N ATOM 253 CA MET A 83 26.499 -21.674 -17.026 1.00 31.10 C ANISOU 253 CA MET A 83 1731 3255 6830 33 47 -575 C ATOM 254 C MET A 83 25.603 -22.276 -15.957 1.00 37.08 C ANISOU 254 C MET A 83 2684 4319 7086 35 -276 -908 C ATOM 255 O MET A 83 24.462 -21.847 -15.811 1.00 33.43 O ANISOU 255 O MET A 83 2341 4031 6328 52 -334 -1042 O ATOM 256 CB MET A 83 26.484 -22.542 -18.293 1.00 34.98 C ANISOU 256 CB MET A 83 2316 3908 7066 118 515 -291 C ATOM 257 CG MET A 83 25.124 -23.067 -18.736 1.00 33.15 C ANISOU 257 CG MET A 83 2323 4046 6228 183 643 -360 C ATOM 258 SD MET A 83 24.013 -21.772 -19.334 1.00 55.79 S ANISOU 258 SD MET A 83 5249 6925 9021 217 756 -318 S ATOM 259 CE MET A 83 24.777 -21.391 -20.907 1.00 68.68 C ANISOU 259 CE MET A 83 6932 8325 10837 363 1263 141 C ATOM 260 N ALA A 84 26.095 -23.260 -15.199 1.00 31.34 N ANISOU 260 N ALA A 84 2012 3646 6249 40 -467 -1018 N ATOM 261 CA ALA A 84 25.252 -23.839 -14.146 1.00 29.88 C ANISOU 261 CA ALA A 84 2081 3732 5539 88 -718 -1273 C ATOM 262 C ALA A 84 24.998 -22.815 -13.039 1.00 32.59 C ANISOU 262 C ALA A 84 2531 3948 5905 169 -1046 -1503 C ATOM 263 O ALA A 84 23.915 -22.784 -12.424 1.00 31.23 O ANISOU 263 O ALA A 84 2589 3991 5287 258 -1112 -1637 O ATOM 264 CB ALA A 84 25.872 -25.137 -13.576 1.00 32.79 C ANISOU 264 CB ALA A 84 2517 4170 5772 106 -814 -1295 C ATOM 265 N ALA A 85 25.982 -21.959 -12.794 1.00 31.79 N ANISOU 265 N ALA A 85 2266 3468 6343 174 -1230 -1524 N ATOM 266 CA ALA A 85 25.799 -20.891 -11.819 1.00 36.36 C ANISOU 266 CA ALA A 85 2939 3877 6999 300 -1561 -1752 C ATOM 267 C ALA A 85 24.698 -19.914 -12.253 1.00 32.49 C ANISOU 267 C ALA A 85 2468 3465 6411 294 -1449 -1775 C ATOM 268 O ALA A 85 23.886 -19.506 -11.440 1.00 32.57 O ANISOU 268 O ALA A 85 2687 3583 6107 436 -1611 -1962 O ATOM 269 CB ALA A 85 27.086 -20.164 -11.562 1.00 39.82 C ANISOU 269 CB ALA A 85 3169 3838 8123 318 -1812 -1767 C ATOM 270 N AVAL A 86 24.694 -19.557 -13.534 0.50 34.90 N ANISOU 270 N AVAL A 86 2564 3714 6981 161 -1137 -1546 N ATOM 271 N BVAL A 86 24.692 -19.558 -13.534 0.50 34.89 N ANISOU 271 N BVAL A 86 2564 3714 6979 161 -1136 -1547 N ATOM 272 CA AVAL A 86 23.698 -18.641 -14.093 0.50 32.92 C ANISOU 272 CA AVAL A 86 2302 3523 6684 147 -997 -1525 C ATOM 273 CA BVAL A 86 23.696 -18.637 -14.089 0.50 32.92 C ANISOU 273 CA BVAL A 86 2302 3523 6684 147 -998 -1526 C ATOM 274 C AVAL A 86 22.294 -19.236 -14.035 0.50 31.17 C ANISOU 274 C AVAL A 86 2300 3732 5810 187 -901 -1602 C ATOM 275 C BVAL A 86 22.292 -19.234 -14.042 0.50 31.17 C ANISOU 275 C BVAL A 86 2299 3732 5810 186 -900 -1601 C ATOM 276 O AVAL A 86 21.325 -18.563 -13.650 0.50 33.60 O ANISOU 276 O AVAL A 86 2718 4121 5927 261 -987 -1749 O ATOM 277 O BVAL A 86 21.319 -18.559 -13.669 0.50 33.58 O ANISOU 277 O BVAL A 86 2713 4119 5926 259 -983 -1746 O ATOM 278 CB AVAL A 86 24.053 -18.260 -15.549 0.50 34.10 C ANISOU 278 CB AVAL A 86 2226 3532 7198 54 -599 -1170 C ATOM 279 CB BVAL A 86 24.056 -18.240 -15.540 0.50 34.15 C ANISOU 279 CB BVAL A 86 2232 3534 7212 54 -603 -1172 C ATOM 280 CG1AVAL A 86 22.909 -17.515 -16.213 0.50 34.99 C ANISOU 280 CG1AVAL A 86 2366 3771 7159 64 -407 -1109 C ATOM 281 CG1BVAL A 86 22.943 -17.426 -16.173 0.50 35.11 C ANISOU 281 CG1BVAL A 86 2372 3759 7209 64 -425 -1117 C ATOM 282 CG2AVAL A 86 25.327 -17.421 -15.585 0.50 38.97 C ANISOU 282 CG2AVAL A 86 2609 3652 8544 28 -675 -1061 C ATOM 283 CG2BVAL A 86 25.365 -17.456 -15.569 0.50 39.00 C ANISOU 283 CG2BVAL A 86 2612 3654 8552 28 -679 -1061 C ATOM 284 N LYS A 87 22.185 -20.503 -14.414 1.00 28.22 N ANISOU 284 N LYS A 87 1987 3612 5124 154 -724 -1495 N ATOM 285 CA LYS A 87 20.917 -21.196 -14.365 1.00 23.64 C ANISOU 285 CA LYS A 87 1603 3397 3980 190 -640 -1532 C ATOM 286 C LYS A 87 20.353 -21.213 -12.954 1.00 28.05 C ANISOU 286 C LYS A 87 2419 4038 4202 337 -850 -1719 C ATOM 287 O LYS A 87 19.187 -20.919 -12.746 1.00 25.88 O ANISOU 287 O LYS A 87 2266 3919 3650 409 -799 -1748 O ATOM 288 CB LYS A 87 21.071 -22.645 -14.855 1.00 22.99 C ANISOU 288 CB LYS A 87 1574 3501 3662 149 -471 -1395 C ATOM 289 CG LYS A 87 21.271 -22.780 -16.345 1.00 25.34 C ANISOU 289 CG LYS A 87 1832 3752 4045 113 -129 -1121 C ATOM 290 CD LYS A 87 21.768 -24.202 -16.680 1.00 24.21 C ANISOU 290 CD LYS A 87 1764 3700 3736 111 -19 -1024 C ATOM 291 CE LYS A 87 21.674 -24.519 -18.151 1.00 27.93 C ANISOU 291 CE LYS A 87 2361 4173 4077 164 308 -782 C ATOM 292 NZ LYS A 87 22.297 -25.887 -18.417 1.00 28.08 N ANISOU 292 NZ LYS A 87 2466 4237 3967 194 397 -715 N ATOM 293 N GLN A 88 21.175 -21.578 -11.977 1.00 28.98 N ANISOU 293 N GLN A 88 2615 4045 4352 419 -1043 -1790 N ATOM 294 CA GLN A 88 20.695 -21.622 -10.600 1.00 28.62 C ANISOU 294 CA GLN A 88 2821 4071 3983 624 -1184 -1883 C ATOM 295 C GLN A 88 20.328 -20.251 -10.028 1.00 28.20 C ANISOU 295 C GLN A 88 2826 3881 4006 766 -1365 -2045 C ATOM 296 O GLN A 88 19.361 -20.147 -9.280 1.00 32.77 O ANISOU 296 O GLN A 88 3614 4603 4233 932 -1338 -2057 O ATOM 297 CB GLN A 88 21.695 -22.332 -9.675 1.00 32.39 C ANISOU 297 CB GLN A 88 3378 4457 4470 704 -1376 -1920 C ATOM 298 CG GLN A 88 21.162 -22.604 -8.259 1.00 35.72 C ANISOU 298 CG GLN A 88 4091 4982 4499 943 -1467 -1961 C ATOM 299 CD GLN A 88 19.911 -23.496 -8.245 1.00 38.09 C ANISOU 299 CD GLN A 88 4510 5573 4390 953 -1168 -1776 C ATOM 300 OE1 GLN A 88 19.732 -24.351 -9.113 1.00 38.33 O ANISOU 300 OE1 GLN A 88 4433 5726 4405 787 -959 -1624 O ATOM 301 NE2 GLN A 88 19.046 -23.294 -7.249 1.00 36.77 N ANISOU 301 NE2 GLN A 88 4566 5483 3924 1171 -1157 -1779 N ATOM 302 N ALA A 89 21.095 -19.213 -10.364 1.00 30.12 N ANISOU 302 N ALA A 89 2878 3819 4747 713 -1536 -2136 N ATOM 303 CA ALA A 89 20.807 -17.880 -9.855 1.00 33.63 C ANISOU 303 CA ALA A 89 3365 4094 5317 854 -1746 -2299 C ATOM 304 C ALA A 89 19.501 -17.400 -10.473 1.00 31.21 C ANISOU 304 C ALA A 89 3066 3968 4825 819 -1517 -2266 C ATOM 305 O ALA A 89 18.694 -16.730 -9.816 1.00 33.07 O ANISOU 305 O ALA A 89 3476 4243 4845 994 -1582 -2360 O ATOM 306 CB ALA A 89 21.940 -16.897 -10.184 1.00 36.96 C ANISOU 306 CB ALA A 89 3523 4089 6433 785 -1961 -2349 C ATOM 307 N LEU A 90 19.301 -17.737 -11.742 1.00 28.06 N ANISOU 307 N LEU A 90 2486 3670 4507 611 -1253 -2121 N ATOM 308 CA LEU A 90 18.086 -17.334 -12.429 1.00 31.02 C ANISOU 308 CA LEU A 90 2839 4210 4735 569 -1059 -2089 C ATOM 309 C LEU A 90 16.867 -18.061 -11.847 1.00 33.18 C ANISOU 309 C LEU A 90 3371 4799 4435 708 -902 -2032 C ATOM 310 O LEU A 90 15.820 -17.449 -11.633 1.00 31.69 O ANISOU 310 O LEU A 90 3280 4672 4089 824 -824 -2056 O ATOM 311 CB LEU A 90 18.221 -17.570 -13.932 1.00 32.79 C ANISOU 311 CB LEU A 90 2869 4447 5142 376 -745 -1780 C ATOM 312 CG LEU A 90 17.178 -16.869 -14.799 1.00 40.21 C ANISOU 312 CG LEU A 90 3807 5431 6041 358 -512 -1612 C ATOM 313 CD1 LEU A 90 17.285 -15.325 -14.669 1.00 29.32 C ANISOU 313 CD1 LEU A 90 2309 3770 5063 394 -640 -1721 C ATOM 314 CD2 LEU A 90 17.302 -17.326 -16.233 1.00 38.40 C ANISOU 314 CD2 LEU A 90 3518 5237 5836 254 -227 -1313 C ATOM 315 N ARG A 91 16.997 -19.367 -11.595 1.00 28.81 N ANISOU 315 N ARG A 91 2897 4406 3644 699 -818 -1897 N ATOM 316 CA ARG A 91 15.976 -20.138 -10.873 1.00 26.72 C ANISOU 316 CA ARG A 91 2819 4354 2981 824 -671 -1755 C ATOM 317 C ARG A 91 15.585 -19.500 -9.544 1.00 32.22 C ANISOU 317 C ARG A 91 3744 4999 3500 1084 -772 -1841 C ATOM 318 O ARG A 91 14.395 -19.340 -9.238 1.00 33.66 O ANISOU 318 O ARG A 91 4032 5287 3469 1207 -593 -1749 O ATOM 319 CB ARG A 91 16.443 -21.591 -10.628 1.00 28.03 C ANISOU 319 CB ARG A 91 3020 4601 3028 781 -631 -1622 C ATOM 320 CG ARG A 91 16.226 -22.517 -11.793 1.00 22.62 C ANISOU 320 CG ARG A 91 2210 4037 2347 591 -455 -1455 C ATOM 321 CD ARG A 91 16.765 -23.931 -11.525 1.00 22.57 C ANISOU 321 CD ARG A 91 2241 4066 2267 558 -437 -1345 C ATOM 322 NE ARG A 91 16.638 -24.734 -12.723 1.00 23.88 N ANISOU 322 NE ARG A 91 2321 4296 2457 396 -313 -1209 N ATOM 323 CZ ARG A 91 16.307 -26.025 -12.756 1.00 24.40 C ANISOU 323 CZ ARG A 91 2411 4435 2425 359 -243 -1060 C ATOM 324 NH1 ARG A 91 16.125 -26.712 -11.629 1.00 26.43 N ANISOU 324 NH1 ARG A 91 2749 4741 2553 466 -247 -1019 N ATOM 325 NH2 ARG A 91 16.162 -26.614 -13.933 1.00 28.84 N ANISOU 325 NH2 ARG A 91 2940 5005 3013 241 -185 -966 N ATOM 326 N GLU A 92 16.581 -19.117 -8.754 1.00 36.55 N ANISOU 326 N GLU A 92 4375 5359 4153 1190 -1055 -2006 N ATOM 327 CA GLU A 92 16.293 -18.566 -7.442 1.00 34.61 C ANISOU 327 CA GLU A 92 4408 5056 3686 1481 -1188 -2099 C ATOM 328 C GLU A 92 15.726 -17.153 -7.516 1.00 36.65 C ANISOU 328 C GLU A 92 4687 5209 4027 1566 -1240 -2224 C ATOM 329 O GLU A 92 14.865 -16.784 -6.719 1.00 40.07 O ANISOU 329 O GLU A 92 5361 5689 4175 1802 -1160 -2210 O ATOM 330 CB GLU A 92 17.528 -18.615 -6.547 1.00 34.95 C ANISOU 330 CB GLU A 92 4550 4913 3815 1604 -1534 -2249 C ATOM 331 CG GLU A 92 17.866 -20.033 -6.163 1.00 41.38 C ANISOU 331 CG GLU A 92 5429 5847 4446 1600 -1453 -2120 C ATOM 332 CD GLU A 92 19.162 -20.159 -5.396 1.00 46.91 C ANISOU 332 CD GLU A 92 6197 6350 5275 1708 -1803 -2269 C ATOM 333 OE1 GLU A 92 19.629 -19.175 -4.795 1.00 49.90 O ANISOU 333 OE1 GLU A 92 6664 6505 5790 1883 -2144 -2472 O ATOM 334 OE2 GLU A 92 19.700 -21.270 -5.412 1.00 43.96 O ANISOU 334 OE2 GLU A 92 5784 6034 4886 1624 -1754 -2180 O ATOM 335 N ALA A 93 16.212 -16.371 -8.474 1.00 36.52 N ANISOU 335 N ALA A 93 4418 5030 4426 1385 -1348 -2329 N ATOM 336 CA ALA A 93 15.733 -15.006 -8.655 1.00 38.71 C ANISOU 336 CA ALA A 93 4677 5170 4862 1436 -1404 -2448 C ATOM 337 C ALA A 93 14.254 -15.019 -9.038 1.00 37.84 C ANISOU 337 C ALA A 93 4608 5272 4499 1460 -1033 -2296 C ATOM 338 O ALA A 93 13.482 -14.195 -8.551 1.00 39.45 O ANISOU 338 O ALA A 93 4966 5441 4581 1645 -993 -2332 O ATOM 339 CB ALA A 93 16.555 -14.286 -9.700 1.00 37.94 C ANISOU 339 CB ALA A 93 4248 4818 5348 1216 -1536 -2534 C ATOM 340 N GLY A 94 13.874 -15.976 -9.890 1.00 36.44 N ANISOU 340 N GLY A 94 4285 5293 4267 1291 -770 -2109 N ATOM 341 CA GLY A 94 12.490 -16.171 -10.298 1.00 33.45 C ANISOU 341 CA GLY A 94 3878 5099 3733 1307 -430 -1903 C ATOM 342 C GLY A 94 11.580 -16.593 -9.160 1.00 37.14 C ANISOU 342 C GLY A 94 4582 5677 3853 1541 -251 -1746 C ATOM 343 O GLY A 94 10.451 -16.089 -9.017 1.00 32.40 O ANISOU 343 O GLY A 94 4016 5096 3198 1673 -34 -1637 O ATOM 344 N ASP A 95 12.052 -17.526 -8.341 1.00 30.44 N ANISOU 344 N ASP A 95 3882 4877 2808 1610 -306 -1707 N ATOM 345 CA ASP A 95 11.322 -17.871 -7.132 1.00 36.68 C ANISOU 345 CA ASP A 95 4923 5726 3288 1882 -128 -1567 C ATOM 346 C ASP A 95 11.091 -16.640 -6.261 1.00 38.59 C ANISOU 346 C ASP A 95 5411 5838 3413 2158 -216 -1716 C ATOM 347 O ASP A 95 9.971 -16.388 -5.816 1.00 41.20 O ANISOU 347 O ASP A 95 5845 6206 3601 2354 62 -1565 O ATOM 348 CB ASP A 95 12.078 -18.911 -6.322 1.00 41.03 C ANISOU 348 CB ASP A 95 5615 6305 3668 1949 -236 -1550 C ATOM 349 CG ASP A 95 11.959 -20.300 -6.904 1.00 37.94 C ANISOU 349 CG ASP A 95 5041 6056 3317 1753 -63 -1337 C ATOM 350 OD1 ASP A 95 11.021 -20.551 -7.699 1.00 40.59 O ANISOU 350 OD1 ASP A 95 5181 6481 3758 1635 178 -1151 O ATOM 351 OD2 ASP A 95 12.800 -21.140 -6.547 1.00 37.77 O ANISOU 351 OD2 ASP A 95 5067 6039 3245 1733 -189 -1354 O ATOM 352 N GLU A 96 12.162 -15.889 -6.013 1.00 38.50 N ANISOU 352 N GLU A 96 5474 5650 3504 2184 -612 -1998 N ATOM 353 CA GLU A 96 12.103 -14.696 -5.168 1.00 44.90 C ANISOU 353 CA GLU A 96 6537 6302 4222 2458 -799 -2184 C ATOM 354 C GLU A 96 11.096 -13.671 -5.698 1.00 46.78 C ANISOU 354 C GLU A 96 6700 6508 4566 2461 -597 -2163 C ATOM 355 O GLU A 96 10.253 -13.144 -4.940 1.00 45.14 O ANISOU 355 O GLU A 96 6726 6292 4133 2743 -442 -2121 O ATOM 356 CB GLU A 96 13.501 -14.075 -5.056 1.00 48.35 C ANISOU 356 CB GLU A 96 6948 6502 4920 2422 -1316 -2478 C ATOM 357 CG GLU A 96 13.625 -12.900 -4.086 1.00 63.55 C ANISOU 357 CG GLU A 96 9152 8224 6769 2731 -1633 -2706 C ATOM 358 CD GLU A 96 15.081 -12.520 -3.820 1.00 75.45 C ANISOU 358 CD GLU A 96 10607 9467 8591 2727 -2193 -2957 C ATOM 359 OE1 GLU A 96 15.973 -12.953 -4.586 1.00 75.03 O ANISOU 359 OE1 GLU A 96 10237 9360 8910 2441 -2286 -2949 O ATOM 360 OE2 GLU A 96 15.336 -11.797 -2.833 1.00 84.68 O ANISOU 360 OE2 GLU A 96 12050 10462 9662 3036 -2543 -3150 O ATOM 361 N PHE A 97 11.188 -13.401 -6.999 1.00 43.83 N ANISOU 361 N PHE A 97 6003 6107 4544 2174 -585 -2178 N ATOM 362 CA PHE A 97 10.283 -12.486 -7.696 1.00 41.69 C ANISOU 362 CA PHE A 97 5598 5795 4450 2148 -394 -2138 C ATOM 363 C PHE A 97 8.823 -12.891 -7.531 1.00 39.97 C ANISOU 363 C PHE A 97 5396 5741 4049 2272 63 -1831 C ATOM 364 O PHE A 97 7.984 -12.072 -7.175 1.00 40.81 O ANISOU 364 O PHE A 97 5600 5788 4118 2460 216 -1802 O ATOM 365 CB PHE A 97 10.626 -12.451 -9.192 1.00 38.79 C ANISOU 365 CB PHE A 97 4860 5405 4473 1832 -413 -2138 C ATOM 366 CG PHE A 97 9.759 -11.513 -10.007 1.00 37.55 C ANISOU 366 CG PHE A 97 4525 5189 4552 1804 -240 -2071 C ATOM 367 CD1 PHE A 97 9.877 -10.140 -9.865 1.00 38.45 C ANISOU 367 CD1 PHE A 97 4686 5061 4863 1887 -416 -2261 C ATOM 368 CD2 PHE A 97 8.860 -12.013 -10.944 1.00 35.84 C ANISOU 368 CD2 PHE A 97 4070 5139 4409 1684 53 -1799 C ATOM 369 CE1 PHE A 97 9.091 -9.275 -10.626 1.00 38.33 C ANISOU 369 CE1 PHE A 97 4493 4977 5093 1861 -255 -2173 C ATOM 370 CE2 PHE A 97 8.078 -11.158 -11.709 1.00 34.15 C ANISOU 370 CE2 PHE A 97 3669 4863 4443 1659 175 -1702 C ATOM 371 CZ PHE A 97 8.202 -9.792 -11.560 1.00 33.98 C ANISOU 371 CZ PHE A 97 3703 4608 4601 1749 42 -1884 C ATOM 372 N GLU A 98 8.531 -14.159 -7.792 1.00 38.14 N ANISOU 372 N GLU A 98 5037 5688 3767 2160 273 -1588 N ATOM 373 CA GLU A 98 7.160 -14.665 -7.723 1.00 36.94 C ANISOU 373 CA GLU A 98 4792 5644 3598 2231 685 -1247 C ATOM 374 C GLU A 98 6.596 -14.760 -6.296 1.00 41.07 C ANISOU 374 C GLU A 98 5617 6176 3811 2573 872 -1136 C ATOM 375 O GLU A 98 5.384 -14.641 -6.085 1.00 42.96 O ANISOU 375 O GLU A 98 5802 6427 4094 2707 1203 -888 O ATOM 376 CB GLU A 98 7.106 -16.032 -8.403 1.00 34.10 C ANISOU 376 CB GLU A 98 4191 5427 3340 2005 779 -1030 C ATOM 377 CG GLU A 98 7.336 -15.967 -9.910 1.00 34.72 C ANISOU 377 CG GLU A 98 3957 5525 3712 1714 663 -1055 C ATOM 378 CD GLU A 98 7.771 -17.296 -10.504 1.00 38.21 C ANISOU 378 CD GLU A 98 4252 6086 4179 1498 611 -960 C ATOM 379 OE1 GLU A 98 7.468 -18.350 -9.910 1.00 42.42 O ANISOU 379 OE1 GLU A 98 4826 6687 4603 1551 752 -776 O ATOM 380 OE2 GLU A 98 8.442 -17.284 -11.557 1.00 33.27 O ANISOU 380 OE2 GLU A 98 3478 5469 3696 1283 436 -1066 O ATOM 381 N LEU A 99 7.474 -14.981 -5.320 1.00 42.95 N ANISOU 381 N LEU A 99 6163 6399 3759 2736 648 -1295 N ATOM 382 CA LEU A 99 7.064 -15.081 -3.914 1.00 47.60 C ANISOU 382 CA LEU A 99 7100 6997 3991 3131 787 -1191 C ATOM 383 C LEU A 99 6.864 -13.720 -3.248 1.00 54.49 C ANISOU 383 C LEU A 99 8256 7735 4713 3428 697 -1372 C ATOM 384 O LEU A 99 5.856 -13.485 -2.573 1.00 56.32 O ANISOU 384 O LEU A 99 8644 7975 4781 3728 1009 -1173 O ATOM 385 CB LEU A 99 8.081 -15.904 -3.118 1.00 53.57 C ANISOU 385 CB LEU A 99 8082 7778 4494 3233 550 -1271 C ATOM 386 CG LEU A 99 7.983 -15.845 -1.587 1.00 63.55 C ANISOU 386 CG LEU A 99 9804 9014 5329 3723 561 -1240 C ATOM 387 CD1 LEU A 99 6.684 -16.462 -1.079 1.00 63.34 C ANISOU 387 CD1 LEU A 99 9806 9076 5184 3957 1089 -806 C ATOM 388 CD2 LEU A 99 9.191 -16.532 -0.961 1.00 69.02 C ANISOU 388 CD2 LEU A 99 10684 9693 5847 3796 220 -1383 C ATOM 389 N ARG A 100 7.820 -12.819 -3.450 1.00 54.09 N ANISOU 389 N ARG A 100 8259 7539 4754 3355 267 -1733 N ATOM 390 CA ARG A 100 7.748 -11.492 -2.864 1.00 58.21 C ANISOU 390 CA ARG A 100 9045 7898 5174 3621 97 -1950 C ATOM 391 C ARG A 100 6.551 -10.723 -3.403 1.00 61.11 C ANISOU 391 C ARG A 100 9248 8245 5727 3610 440 -1817 C ATOM 392 O ARG A 100 6.011 -9.842 -2.727 1.00 61.11 O ANISOU 392 O ARG A 100 9497 8159 5561 3918 501 -1860 O ATOM 393 CB ARG A 100 9.031 -10.712 -3.138 1.00 61.00 C ANISOU 393 CB ARG A 100 9379 8052 5745 3483 -467 -2334 C ATOM 394 CG ARG A 100 9.114 -9.374 -2.428 1.00 72.10 C ANISOU 394 CG ARG A 100 11079 9249 7065 3773 -755 -2597 C ATOM 395 CD ARG A 100 10.455 -8.713 -2.683 1.00 76.54 C ANISOU 395 CD ARG A 100 11545 9574 7963 3616 -1360 -2939 C ATOM 396 NE ARG A 100 11.564 -9.586 -2.308 1.00 76.88 N ANISOU 396 NE ARG A 100 11615 9626 7967 3591 -1669 -2996 N ATOM 397 CZ ARG A 100 12.843 -9.326 -2.561 1.00 77.01 C ANISOU 397 CZ ARG A 100 11456 9441 8363 3423 -2169 -3218 C ATOM 398 NH1 ARG A 100 13.184 -8.213 -3.198 1.00 75.90 N ANISOU 398 NH1 ARG A 100 11089 9067 8682 3257 -2421 -3395 N ATOM 399 NH2 ARG A 100 13.780 -10.182 -2.178 1.00 79.37 N ANISOU 399 NH2 ARG A 100 11773 9746 8639 3429 -2401 -3236 N ATOM 400 N TYR A 101 6.127 -11.060 -4.617 1.00 55.04 N ANISOU 400 N TYR A 101 8063 7546 5304 3280 650 -1647 N ATOM 401 CA TYR A 101 4.999 -10.365 -5.234 1.00 56.55 C ANISOU 401 CA TYR A 101 8032 7702 5751 3252 943 -1497 C ATOM 402 C TYR A 101 3.893 -11.338 -5.613 1.00 49.34 C ANISOU 402 C TYR A 101 6826 6939 4983 3160 1365 -1075 C ATOM 403 O TYR A 101 3.308 -11.238 -6.689 1.00 46.91 O ANISOU 403 O TYR A 101 6149 6630 5044 2938 1478 -936 O ATOM 404 CB TYR A 101 5.485 -9.560 -6.436 1.00 47.61 C ANISOU 404 CB TYR A 101 6646 6442 5001 2978 709 -1694 C ATOM 405 CG TYR A 101 6.695 -8.731 -6.078 1.00 60.23 C ANISOU 405 CG TYR A 101 8464 7850 6570 3021 222 -2088 C ATOM 406 CD1 TYR A 101 6.641 -7.808 -5.038 1.00 64.82 C ANISOU 406 CD1 TYR A 101 9397 8296 6936 3343 88 -2269 C ATOM 407 CD2 TYR A 101 7.894 -8.883 -6.753 1.00 55.13 C ANISOU 407 CD2 TYR A 101 7655 7140 6151 2754 -130 -2265 C ATOM 408 CE1 TYR A 101 7.747 -7.054 -4.691 1.00 67.24 C ANISOU 408 CE1 TYR A 101 9864 8391 7291 3380 -435 -2622 C ATOM 409 CE2 TYR A 101 9.004 -8.135 -6.416 1.00 57.54 C ANISOU 409 CE2 TYR A 101 8077 7225 6561 2772 -614 -2589 C ATOM 410 CZ TYR A 101 8.929 -7.222 -5.382 1.00 66.50 C ANISOU 410 CZ TYR A 101 9540 8213 7513 3079 -793 -2770 C ATOM 411 OH TYR A 101 10.038 -6.472 -5.041 1.00 70.46 O ANISOU 411 OH TYR A 101 10114 8465 8193 3098 -1342 -3083 O ATOM 412 N AARG A 102 3.597 -12.260 -4.702 0.68 53.54 N ANISOU 412 N AARG A 102 7518 7570 5253 3353 1565 -852 N ATOM 413 N BARG A 102 3.624 -12.275 -4.704 0.32 53.55 N ANISOU 413 N BARG A 102 7521 7572 5253 3350 1558 -856 N ATOM 414 CA AARG A 102 2.672 -13.357 -4.966 0.68 53.10 C ANISOU 414 CA AARG A 102 7174 7614 5386 3257 1906 -430 C ATOM 415 CA BARG A 102 2.655 -13.353 -4.907 0.32 53.39 C ANISOU 415 CA BARG A 102 7227 7651 5408 3275 1914 -425 C ATOM 416 C AARG A 102 1.277 -12.894 -5.386 0.68 52.20 C ANISOU 416 C AARG A 102 6781 7448 5603 3260 2215 -144 C ATOM 417 C BARG A 102 1.299 -12.871 -5.396 0.32 53.78 C ANISOU 417 C BARG A 102 6984 7648 5803 3258 2206 -154 C ATOM 418 O AARG A 102 0.711 -13.416 -6.340 0.68 49.90 O ANISOU 418 O AARG A 102 6083 7173 5704 2991 2283 79 O ATOM 419 O BARG A 102 0.784 -13.357 -6.400 0.32 49.64 O ANISOU 419 O BARG A 102 6049 7138 5673 2977 2257 49 O ATOM 420 CB AARG A 102 2.574 -14.269 -3.742 0.68 57.32 C ANISOU 420 CB AARG A 102 7984 8213 5584 3550 2091 -212 C ATOM 421 CB BARG A 102 2.458 -14.140 -3.607 0.32 57.86 C ANISOU 421 CB BARG A 102 8091 8269 5623 3608 2124 -198 C ATOM 422 CG AARG A 102 1.778 -15.537 -3.975 0.68 58.06 C ANISOU 422 CG AARG A 102 7771 8362 5926 3435 2394 231 C ATOM 423 CG BARG A 102 3.366 -15.344 -3.453 0.32 56.97 C ANISOU 423 CG BARG A 102 8028 8247 5371 3506 1964 -225 C ATOM 424 CD AARG A 102 1.288 -16.118 -2.661 0.68 65.90 C ANISOU 424 CD AARG A 102 9045 9355 6640 3842 2715 557 C ATOM 425 CD BARG A 102 3.145 -16.041 -2.115 0.32 62.84 C ANISOU 425 CD BARG A 102 9097 9017 5763 3901 2184 25 C ATOM 426 NE AARG A 102 0.487 -15.154 -1.910 0.68 73.21 N ANISOU 426 NE AARG A 102 10208 10198 7411 4225 2967 670 N ATOM 427 NE BARG A 102 3.584 -15.226 -0.984 0.32 66.76 N ANISOU 427 NE BARG A 102 10108 9453 5805 4317 2025 -199 N ATOM 428 CZ AARG A 102 0.919 -14.493 -0.839 0.68 75.60 C ANISOU 428 CZ AARG A 102 11024 10476 7224 4630 2876 473 C ATOM 429 CZ BARG A 102 2.769 -14.552 -0.179 0.32 73.02 C ANISOU 429 CZ BARG A 102 11167 10183 6396 4726 2282 -49 C ATOM 430 NH1AARG A 102 2.149 -14.695 -0.382 0.68 74.62 N ANISOU 430 NH1AARG A 102 11204 10389 6758 4689 2506 157 N ATOM 431 NH1BARG A 102 1.458 -14.594 -0.369 0.32 75.68 N ANISOU 431 NH1BARG A 102 11267 10502 6987 4757 2741 354 N ATOM 432 NH2AARG A 102 0.121 -13.630 -0.227 0.68 78.96 N ANISOU 432 NH2AARG A 102 11664 10822 7517 4990 3128 596 N ATOM 433 NH2BARG A 102 3.267 -13.838 0.821 0.32 76.15 N ANISOU 433 NH2BARG A 102 12068 10512 6355 5123 2060 -290 N ATOM 434 N ARG A 103 0.723 -11.918 -4.673 1.00 56.24 N ANISOU 434 N ARG A 103 7519 7882 5970 3575 2365 -146 N ATOM 435 CA ARG A 103 -0.611 -11.436 -4.986 1.00 58.01 C ANISOU 435 CA ARG A 103 7489 8038 6514 3604 2662 145 C ATOM 436 C ARG A 103 -0.642 -10.787 -6.364 1.00 54.24 C ANISOU 436 C ARG A 103 6646 7507 6455 3274 2464 10 C ATOM 437 O ARG A 103 -1.494 -11.107 -7.181 1.00 53.23 O ANISOU 437 O ARG A 103 6123 7365 6739 3071 2561 297 O ATOM 438 CB ARG A 103 -1.109 -10.466 -3.911 1.00 63.47 C ANISOU 438 CB ARG A 103 8546 8651 6918 4044 2861 147 C ATOM 439 CG ARG A 103 -2.613 -10.423 -3.802 1.00 66.98 C ANISOU 439 CG ARG A 103 8793 9035 7624 4179 3310 622 C ATOM 440 CD ARG A 103 -3.047 -9.624 -2.578 1.00 73.21 C ANISOU 440 CD ARG A 103 10027 9757 8033 4692 3559 667 C ATOM 441 NE ARG A 103 -2.563 -8.252 -2.631 1.00 73.25 N ANISOU 441 NE ARG A 103 10236 9687 7910 4762 3283 215 N ATOM 442 CZ ARG A 103 -3.169 -7.283 -3.309 1.00 72.84 C ANISOU 442 CZ ARG A 103 9938 9540 8198 4662 3311 190 C ATOM 443 NH1 ARG A 103 -4.278 -7.545 -3.992 1.00 72.41 N ANISOU 443 NH1 ARG A 103 9432 9463 8619 4485 3572 592 N ATOM 444 NH2 ARG A 103 -2.678 -6.050 -3.306 1.00 79.54 N ANISOU 444 NH2 ARG A 103 10984 10284 8952 4740 3050 -222 N ATOM 445 N ALA A 104 0.299 -9.887 -6.619 1.00 52.65 N ANISOU 445 N ALA A 104 6587 7244 6173 3235 2155 -402 N ATOM 446 CA ALA A 104 0.415 -9.246 -7.923 1.00 54.87 C ANISOU 446 CA ALA A 104 6562 7456 6831 2964 1964 -517 C ATOM 447 C ALA A 104 0.612 -10.279 -9.035 1.00 48.79 C ANISOU 447 C ALA A 104 5451 6778 6307 2615 1853 -381 C ATOM 448 O ALA A 104 0.057 -10.157 -10.130 1.00 45.00 O ANISOU 448 O ALA A 104 4630 6275 6192 2414 1811 -230 O ATOM 449 CB ALA A 104 1.576 -8.269 -7.918 1.00 53.67 C ANISOU 449 CB ALA A 104 6645 7178 6570 2988 1642 -950 C ATOM 450 N PHE A 105 1.402 -11.299 -8.738 1.00 43.94 N ANISOU 450 N PHE A 105 4956 6263 5476 2561 1772 -429 N ATOM 451 CA PHE A 105 1.767 -12.281 -9.747 1.00 43.04 C ANISOU 451 CA PHE A 105 4580 6231 5541 2255 1631 -350 C ATOM 452 C PHE A 105 0.569 -13.123 -10.161 1.00 41.40 C ANISOU 452 C PHE A 105 4043 6044 5643 2133 1789 54 C ATOM 453 O PHE A 105 0.301 -13.301 -11.354 1.00 42.84 O ANISOU 453 O PHE A 105 3925 6208 6143 1887 1635 159 O ATOM 454 CB PHE A 105 2.891 -13.171 -9.233 1.00 43.20 C ANISOU 454 CB PHE A 105 4824 6341 5248 2247 1508 -496 C ATOM 455 CG PHE A 105 3.443 -14.081 -10.273 1.00 42.37 C ANISOU 455 CG PHE A 105 4499 6319 5282 1954 1337 -466 C ATOM 456 CD1 PHE A 105 4.220 -13.575 -11.295 1.00 36.65 C ANISOU 456 CD1 PHE A 105 3687 5577 4662 1787 1085 -656 C ATOM 457 CD2 PHE A 105 3.158 -15.436 -10.252 1.00 43.45 C ANISOU 457 CD2 PHE A 105 4511 6539 5460 1858 1421 -230 C ATOM 458 CE1 PHE A 105 4.727 -14.413 -12.273 1.00 39.77 C ANISOU 458 CE1 PHE A 105 3906 6065 5138 1539 920 -623 C ATOM 459 CE2 PHE A 105 3.660 -16.278 -11.236 1.00 42.79 C ANISOU 459 CE2 PHE A 105 4245 6523 5491 1602 1234 -214 C ATOM 460 CZ PHE A 105 4.443 -15.759 -12.241 1.00 42.05 C ANISOU 460 CZ PHE A 105 4099 6441 5435 1453 987 -411 C ATOM 461 N SER A 106 -0.142 -13.641 -9.166 1.00 45.06 N ANISOU 461 N SER A 106 4587 6511 6024 2321 2068 301 N ATOM 462 CA SER A 106 -1.385 -14.358 -9.393 1.00 52.43 C ANISOU 462 CA SER A 106 5212 7379 7329 2241 2237 730 C ATOM 463 C SER A 106 -2.426 -13.491 -10.098 1.00 54.77 C ANISOU 463 C SER A 106 5257 7548 8006 2181 2243 873 C ATOM 464 O SER A 106 -3.083 -13.955 -11.029 1.00 55.17 O ANISOU 464 O SER A 106 4982 7511 8471 1946 2114 1088 O ATOM 465 CB SER A 106 -1.948 -14.863 -8.069 1.00 61.47 C ANISOU 465 CB SER A 106 6528 8507 8319 2530 2602 1010 C ATOM 466 OG SER A 106 -0.993 -15.668 -7.411 1.00 62.84 O ANISOU 466 OG SER A 106 6955 8792 8130 2599 2568 892 O ATOM 467 N ASP A 107 -2.588 -12.244 -9.642 1.00 48.60 N ANISOU 467 N ASP A 107 4645 6728 7093 2401 2358 749 N ATOM 468 CA ASP A 107 -3.544 -11.329 -10.252 1.00 51.67 C ANISOU 468 CA ASP A 107 4817 6992 7823 2367 2372 876 C ATOM 469 C ASP A 107 -3.271 -11.125 -11.743 1.00 51.48 C ANISOU 469 C ASP A 107 4560 6948 8054 2058 2003 768 C ATOM 470 O ASP A 107 -4.167 -11.254 -12.574 1.00 46.80 O ANISOU 470 O ASP A 107 3676 6240 7865 1886 1908 1013 O ATOM 471 CB ASP A 107 -3.551 -9.967 -9.531 1.00 53.98 C ANISOU 471 CB ASP A 107 5375 7247 7887 2664 2512 685 C ATOM 472 CG ASP A 107 -4.302 -9.998 -8.208 1.00 61.04 C ANISOU 472 CG ASP A 107 6467 8109 8616 3012 2924 930 C ATOM 473 OD1 ASP A 107 -4.608 -11.099 -7.706 1.00 62.66 O ANISOU 473 OD1 ASP A 107 6651 8331 8825 3050 3119 1223 O ATOM 474 OD2 ASP A 107 -4.579 -8.911 -7.659 1.00 67.08 O ANISOU 474 OD2 ASP A 107 7426 8814 9247 3273 3063 845 O ATOM 475 N LEU A 108 -2.027 -10.795 -12.069 1.00 47.05 N ANISOU 475 N LEU A 108 4148 6464 7265 2008 1785 420 N ATOM 476 CA LEU A 108 -1.632 -10.537 -13.446 1.00 45.63 C ANISOU 476 CA LEU A 108 3812 6263 7265 1769 1470 342 C ATOM 477 C LEU A 108 -1.753 -11.784 -14.332 1.00 45.67 C ANISOU 477 C LEU A 108 3613 6282 7458 1505 1262 520 C ATOM 478 O LEU A 108 -2.287 -11.722 -15.439 1.00 49.89 O ANISOU 478 O LEU A 108 3960 6718 8278 1335 1039 651 O ATOM 479 CB LEU A 108 -0.184 -10.032 -13.488 1.00 41.53 C ANISOU 479 CB LEU A 108 3497 5788 6496 1797 1333 -21 C ATOM 480 CG LEU A 108 0.099 -8.611 -12.997 1.00 42.75 C ANISOU 480 CG LEU A 108 3837 5839 6566 2011 1379 -270 C ATOM 481 CD1 LEU A 108 1.599 -8.329 -13.080 1.00 46.24 C ANISOU 481 CD1 LEU A 108 4449 6253 6867 2004 1195 -599 C ATOM 482 CD2 LEU A 108 -0.690 -7.572 -13.792 1.00 41.94 C ANISOU 482 CD2 LEU A 108 3558 5617 6761 1972 1341 -144 C ATOM 483 N THR A 109 -1.260 -12.913 -13.843 1.00 38.91 N ANISOU 483 N THR A 109 2825 5523 6435 1486 1300 512 N ATOM 484 CA THR A 109 -1.189 -14.106 -14.686 1.00 44.87 C ANISOU 484 CA THR A 109 3428 6278 7340 1247 1055 617 C ATOM 485 C THR A 109 -2.552 -14.751 -14.861 1.00 46.68 C ANISOU 485 C THR A 109 3417 6345 7976 1165 1049 956 C ATOM 486 O THR A 109 -2.812 -15.401 -15.871 1.00 44.07 O ANISOU 486 O THR A 109 2944 5915 7886 961 733 1037 O ATOM 487 CB THR A 109 -0.169 -15.147 -14.173 1.00 46.20 C ANISOU 487 CB THR A 109 3736 6588 7230 1239 1076 500 C ATOM 488 OG1 THR A 109 -0.553 -15.621 -12.876 1.00 51.83 O ANISOU 488 OG1 THR A 109 4536 7316 7842 1417 1384 629 O ATOM 489 CG2 THR A 109 1.211 -14.543 -14.116 1.00 49.08 C ANISOU 489 CG2 THR A 109 4317 7056 7274 1295 1028 173 C ATOM 490 N SER A 110 -3.438 -14.537 -13.892 1.00 48.37 N ANISOU 490 N SER A 110 3602 6490 8286 1341 1382 1160 N ATOM 491 CA SER A 110 -4.791 -15.066 -13.981 1.00 45.91 C ANISOU 491 CA SER A 110 3027 5960 8457 1278 1424 1533 C ATOM 492 C SER A 110 -5.574 -14.386 -15.111 1.00 46.70 C ANISOU 492 C SER A 110 2937 5884 8922 1144 1156 1599 C ATOM 493 O SER A 110 -6.675 -14.817 -15.458 1.00 51.70 O ANISOU 493 O SER A 110 3327 6277 10040 1042 1067 1879 O ATOM 494 CB SER A 110 -5.530 -14.873 -12.656 1.00 56.93 C ANISOU 494 CB SER A 110 4458 7308 9864 1543 1903 1782 C ATOM 495 OG SER A 110 -5.923 -13.521 -12.489 1.00 57.63 O ANISOU 495 OG SER A 110 4600 7376 9921 1701 2048 1743 O ATOM 496 N GLN A 111 -5.022 -13.306 -15.660 1.00 44.56 N ANISOU 496 N GLN A 111 2781 5696 8455 1157 1026 1357 N ATOM 497 CA GLN A 111 -5.699 -12.558 -16.722 1.00 48.23 C ANISOU 497 CA GLN A 111 3113 6002 9212 1064 774 1414 C ATOM 498 C GLN A 111 -5.371 -13.106 -18.110 1.00 50.68 C ANISOU 498 C GLN A 111 3416 6260 9580 852 275 1329 C ATOM 499 O GLN A 111 -6.114 -12.869 -19.057 1.00 52.37 O ANISOU 499 O GLN A 111 3521 6288 10089 763 -17 1421 O ATOM 500 CB GLN A 111 -5.348 -11.065 -16.655 1.00 51.21 C ANISOU 500 CB GLN A 111 3621 6449 9388 1206 888 1237 C ATOM 501 CG GLN A 111 -6.031 -10.308 -15.517 1.00 57.48 C ANISOU 501 CG GLN A 111 4427 7212 10200 1441 1304 1345 C ATOM 502 CD GLN A 111 -5.229 -9.099 -15.053 1.00 66.31 C ANISOU 502 CD GLN A 111 5787 8439 10970 1630 1438 1056 C ATOM 503 OE1 GLN A 111 -4.677 -8.353 -15.864 1.00 67.88 O ANISOU 503 OE1 GLN A 111 6027 8633 11131 1565 1225 885 O ATOM 504 NE2 GLN A 111 -5.146 -8.914 -13.739 1.00 69.99 N ANISOU 504 NE2 GLN A 111 6438 8969 11187 1885 1775 1003 N ATOM 505 N LEU A 112 -4.258 -13.832 -18.212 1.00 49.81 N ANISOU 505 N LEU A 112 3453 6302 9169 797 169 1151 N ATOM 506 CA LEU A 112 -3.797 -14.443 -19.467 1.00 52.25 C ANISOU 506 CA LEU A 112 3839 6578 9437 644 -291 1053 C ATOM 507 C LEU A 112 -4.844 -15.341 -20.149 1.00 59.66 C ANISOU 507 C LEU A 112 4640 7254 10776 505 -635 1220 C ATOM 508 O LEU A 112 -5.487 -16.171 -19.496 1.00 58.29 O ANISOU 508 O LEU A 112 4305 6967 10874 470 -505 1402 O ATOM 509 CB LEU A 112 -2.496 -15.227 -19.230 1.00 50.84 C ANISOU 509 CB LEU A 112 3821 6594 8904 621 -274 876 C ATOM 510 CG LEU A 112 -1.240 -14.394 -18.971 1.00 50.74 C ANISOU 510 CG LEU A 112 3971 6771 8536 718 -97 660 C ATOM 511 CD1 LEU A 112 -0.036 -15.272 -18.667 1.00 51.43 C ANISOU 511 CD1 LEU A 112 4179 7018 8344 683 -76 516 C ATOM 512 CD2 LEU A 112 -0.963 -13.510 -20.174 1.00 50.18 C ANISOU 512 CD2 LEU A 112 3977 6638 8451 712 -347 603 C ATOM 513 N AHIS A 113 -5.022 -15.173 -21.460 0.52 62.16 N ANISOU 513 N AHIS A 113 5043 7436 11140 447 -1083 1163 N ATOM 514 N BHIS A 113 -5.000 -15.139 -21.456 0.48 62.06 N ANISOU 514 N BHIS A 113 5033 7429 11118 450 -1076 1160 N ATOM 515 CA AHIS A 113 -5.986 -15.974 -22.229 0.52 64.38 C ANISOU 515 CA AHIS A 113 5251 7411 11799 327 -1501 1258 C ATOM 516 CA BHIS A 113 -5.910 -15.922 -22.283 0.48 66.04 C ANISOU 516 CA BHIS A 113 5483 7636 11975 332 -1511 1242 C ATOM 517 C AHIS A 113 -5.414 -16.379 -23.595 0.52 68.74 C ANISOU 517 C AHIS A 113 6121 7922 12074 306 -2018 1053 C ATOM 518 C BHIS A 113 -5.255 -16.290 -23.593 0.48 69.11 C ANISOU 518 C BHIS A 113 6193 8008 12056 319 -1995 1033 C ATOM 519 O AHIS A 113 -5.688 -15.732 -24.608 0.52 71.35 O ANISOU 519 O AHIS A 113 6583 8150 12376 355 -2323 1011 O ATOM 520 O BHIS A 113 -5.319 -15.540 -24.570 0.48 70.70 O ANISOU 520 O BHIS A 113 6555 8158 12148 387 -2255 974 O ATOM 521 CB AHIS A 113 -7.305 -15.207 -22.405 0.52 60.04 C ANISOU 521 CB AHIS A 113 4485 6623 11704 328 -1540 1448 C ATOM 522 CB BHIS A 113 -7.181 -15.143 -22.561 0.48 62.16 C ANISOU 522 CB BHIS A 113 4798 6910 11911 333 -1586 1413 C ATOM 523 CG AHIS A 113 -8.408 -16.013 -23.028 0.52 62.61 C ANISOU 523 CG AHIS A 113 4680 6564 12546 197 -1955 1566 C ATOM 524 CG BHIS A 113 -7.973 -14.863 -21.333 0.48 57.93 C ANISOU 524 CG BHIS A 113 3974 6331 11704 375 -1110 1662 C ATOM 525 ND1AHIS A 113 -9.155 -16.930 -22.317 0.52 62.27 N ANISOU 525 ND1AHIS A 113 4372 6301 12986 113 -1830 1797 N ATOM 526 ND1BHIS A 113 -8.231 -13.590 -20.882 0.48 52.24 N ANISOU 526 ND1BHIS A 113 3190 5684 10973 498 -790 1723 N ATOM 527 CD2AHIS A 113 -8.897 -16.028 -24.289 0.52 60.00 C ANISOU 527 CD2AHIS A 113 4458 5985 12354 154 -2507 1489 C ATOM 528 CD2BHIS A 113 -8.524 -15.704 -20.430 0.48 56.68 C ANISOU 528 CD2BHIS A 113 3614 6056 11866 345 -871 1883 C ATOM 529 CE1AHIS A 113 -10.049 -17.480 -23.118 0.52 62.95 C ANISOU 529 CE1AHIS A 113 4376 5992 13551 -1 -2306 1853 C ATOM 530 CE1BHIS A 113 -8.929 -13.660 -19.763 0.48 56.17 C ANISOU 530 CE1BHIS A 113 3487 6118 11737 557 -375 1962 C ATOM 531 NE2AHIS A 113 -9.913 -16.954 -24.320 0.52 64.40 N ANISOU 531 NE2AHIS A 113 4803 6157 13511 25 -2740 1644 N ATOM 532 NE2BHIS A 113 -9.130 -14.932 -19.474 0.48 56.20 N ANISOU 532 NE2BHIS A 113 3394 6001 11957 470 -405 2086 N ATOM 533 N ILE A 114 -4.628 -17.456 -23.607 1.00 68.00 N ANISOU 533 N ILE A 114 6186 7903 11748 264 -2100 933 N ATOM 534 CA ILE A 114 -3.889 -17.893 -24.779 1.00 65.90 C ANISOU 534 CA ILE A 114 6307 7631 11100 298 -2498 728 C ATOM 535 C ILE A 114 -4.700 -18.713 -25.769 1.00 62.61 C ANISOU 535 C ILE A 114 6005 6864 10919 247 -3019 691 C ATOM 536 O ILE A 114 -5.453 -19.605 -25.382 1.00 58.30 O ANISOU 536 O ILE A 114 5238 6088 10826 127 -3084 797 O ATOM 537 CB ILE A 114 -2.738 -18.803 -24.368 1.00 69.99 C ANISOU 537 CB ILE A 114 6959 8339 11294 277 -2368 612 C ATOM 538 CG1 ILE A 114 -2.050 -18.292 -23.105 1.00 71.70 C ANISOU 538 CG1 ILE A 114 7003 8843 11396 302 -1850 646 C ATOM 539 CG2 ILE A 114 -1.754 -18.946 -25.504 1.00 72.56 C ANISOU 539 CG2 ILE A 114 7744 8714 11111 378 -2641 416 C ATOM 540 CD1 ILE A 114 -0.908 -19.190 -22.662 1.00 69.51 C ANISOU 540 CD1 ILE A 114 6839 8745 10825 274 -1737 531 C ATOM 541 N THR A 115 -4.522 -18.407 -27.050 1.00 62.15 N ANISOU 541 N THR A 115 6320 6736 10558 364 -3389 546 N ATOM 542 CA THR A 115 -4.880 -19.319 -28.127 1.00 64.14 C ANISOU 542 CA THR A 115 6857 6678 10836 380 -3918 405 C ATOM 543 C THR A 115 -3.656 -19.496 -29.026 1.00 62.51 C ANISOU 543 C THR A 115 7201 6616 9935 562 -4014 194 C ATOM 544 O THR A 115 -2.723 -18.691 -28.969 1.00 56.09 O ANISOU 544 O THR A 115 6522 6091 8699 674 -3727 200 O ATOM 545 CB THR A 115 -6.051 -18.791 -28.961 1.00 63.61 C ANISOU 545 CB THR A 115 6788 6299 11081 410 -4321 429 C ATOM 546 OG1 THR A 115 -5.688 -17.539 -29.555 1.00 60.59 O ANISOU 546 OG1 THR A 115 6630 6096 10294 585 -4273 409 O ATOM 547 CG2 THR A 115 -7.287 -18.620 -28.092 1.00 69.33 C ANISOU 547 CG2 THR A 115 6965 6838 12540 241 -4190 678 C ATOM 548 N PRO A 116 -3.639 -20.563 -29.841 1.00 66.41 N ANISOU 548 N PRO A 116 8025 6871 10337 613 -4398 21 N ATOM 549 CA PRO A 116 -2.544 -20.738 -30.801 1.00 62.76 C ANISOU 549 CA PRO A 116 8145 6500 9201 842 -4453 -164 C ATOM 550 C PRO A 116 -2.376 -19.534 -31.719 1.00 60.04 C ANISOU 550 C PRO A 116 8131 6227 8454 1075 -4477 -164 C ATOM 551 O PRO A 116 -1.256 -19.220 -32.113 1.00 58.03 O ANISOU 551 O PRO A 116 8241 6175 7633 1268 -4241 -193 O ATOM 552 CB PRO A 116 -2.993 -21.960 -31.604 1.00 69.82 C ANISOU 552 CB PRO A 116 9309 6998 10219 888 -4958 -347 C ATOM 553 CG PRO A 116 -3.763 -22.770 -30.615 1.00 69.16 C ANISOU 553 CG PRO A 116 8721 6741 10817 622 -4981 -230 C ATOM 554 CD PRO A 116 -4.495 -21.763 -29.764 1.00 70.55 C ANISOU 554 CD PRO A 116 8391 7020 11397 476 -4726 9 C ATOM 555 N GLY A 117 -3.476 -18.857 -32.033 1.00 58.62 N ANISOU 555 N GLY A 117 7815 5867 8593 1067 -4727 -101 N ATOM 556 CA GLY A 117 -3.453 -17.737 -32.950 1.00 60.26 C ANISOU 556 CA GLY A 117 8337 6106 8453 1303 -4785 -82 C ATOM 557 C GLY A 117 -3.041 -16.412 -32.340 1.00 56.49 C ANISOU 557 C GLY A 117 7635 5928 7900 1315 -4333 123 C ATOM 558 O GLY A 117 -2.702 -15.477 -33.066 1.00 62.93 O ANISOU 558 O GLY A 117 8761 6810 8341 1547 -4267 178 O ATOM 559 N THR A 118 -3.053 -16.330 -31.011 1.00 53.08 N ANISOU 559 N THR A 118 6690 5646 7831 1096 -4008 242 N ATOM 560 CA THR A 118 -2.758 -15.077 -30.316 1.00 49.82 C ANISOU 560 CA THR A 118 6024 5446 7459 1110 -3612 412 C ATOM 561 C THR A 118 -1.648 -15.217 -29.298 1.00 47.74 C ANISOU 561 C THR A 118 5628 5434 7078 1050 -3199 422 C ATOM 562 O THR A 118 -1.316 -14.259 -28.606 1.00 47.34 O ANISOU 562 O THR A 118 5352 5518 7116 1064 -2876 526 O ATOM 563 CB THR A 118 -3.981 -14.553 -29.544 1.00 54.08 C ANISOU 563 CB THR A 118 6023 5893 8633 940 -3558 554 C ATOM 564 OG1 THR A 118 -4.306 -15.470 -28.486 1.00 52.73 O ANISOU 564 OG1 THR A 118 5484 5703 8848 719 -3428 574 O ATOM 565 CG2 THR A 118 -5.165 -14.390 -30.471 1.00 57.85 C ANISOU 565 CG2 THR A 118 6568 6085 9329 973 -4002 551 C ATOM 566 N ALA A 119 -1.084 -16.409 -29.185 1.00 47.39 N ANISOU 566 N ALA A 119 5712 5422 6873 989 -3223 299 N ATOM 567 CA ALA A 119 -0.031 -16.631 -28.208 1.00 45.45 C ANISOU 567 CA ALA A 119 5341 5403 6524 926 -2872 288 C ATOM 568 C ALA A 119 1.175 -15.734 -28.490 1.00 43.81 C ANISOU 568 C ALA A 119 5418 5335 5892 1141 -2629 317 C ATOM 569 O ALA A 119 1.704 -15.066 -27.590 1.00 41.37 O ANISOU 569 O ALA A 119 4875 5183 5662 1028 -2111 340 O ATOM 570 CB ALA A 119 0.375 -18.090 -28.200 1.00 40.30 C ANISOU 570 CB ALA A 119 4832 4737 5743 847 -2958 154 C ATOM 571 N TYR A 120 1.613 -15.709 -29.743 1.00 45.00 N ANISOU 571 N TYR A 120 6110 5422 5567 1382 -2736 300 N ATOM 572 CA TYR A 120 2.768 -14.897 -30.084 1.00 46.99 C ANISOU 572 CA TYR A 120 6644 5772 5436 1566 -2283 385 C ATOM 573 C TYR A 120 2.486 -13.434 -29.848 1.00 42.30 C ANISOU 573 C TYR A 120 5803 5178 5091 1543 -2000 525 C ATOM 574 O TYR A 120 3.320 -12.716 -29.292 1.00 44.87 O ANISOU 574 O TYR A 120 5980 5602 5465 1472 -1484 567 O ATOM 575 CB TYR A 120 3.206 -15.092 -31.532 1.00 56.45 C ANISOU 575 CB TYR A 120 8499 6878 6071 1912 -2400 403 C ATOM 576 CG TYR A 120 4.467 -14.323 -31.807 1.00 57.94 C ANISOU 576 CG TYR A 120 8914 7146 5954 2112 -1814 572 C ATOM 577 CD1 TYR A 120 5.670 -14.715 -31.230 1.00 55.41 C ANISOU 577 CD1 TYR A 120 8505 6955 5592 2002 -1367 547 C ATOM 578 CD2 TYR A 120 4.458 -13.188 -32.607 1.00 63.54 C ANISOU 578 CD2 TYR A 120 9848 7774 6519 2370 -1649 779 C ATOM 579 CE1 TYR A 120 6.828 -14.013 -31.454 1.00 57.15 C ANISOU 579 CE1 TYR A 120 8816 7193 5706 2133 -790 731 C ATOM 580 CE2 TYR A 120 5.618 -12.472 -32.838 1.00 65.72 C ANISOU 580 CE2 TYR A 120 10230 8076 6664 2513 -1023 985 C ATOM 581 CZ TYR A 120 6.803 -12.893 -32.259 1.00 62.75 C ANISOU 581 CZ TYR A 120 9718 7800 6324 2386 -601 965 C ATOM 582 OH TYR A 120 7.968 -12.197 -32.481 1.00 63.86 O ANISOU 582 OH TYR A 120 9884 7907 6471 2519 11 1206 O ATOM 583 N GLN A 121 1.304 -13.001 -30.282 1.00 44.17 N ANISOU 583 N GLN A 121 5987 5265 5528 1610 -2387 590 N ATOM 584 CA GLN A 121 0.885 -11.616 -30.130 1.00 48.81 C ANISOU 584 CA GLN A 121 6347 5822 6376 1609 -2176 728 C ATOM 585 C GLN A 121 0.918 -11.198 -28.665 1.00 46.23 C ANISOU 585 C GLN A 121 5489 5615 6462 1340 -1773 694 C ATOM 586 O GLN A 121 1.409 -10.123 -28.335 1.00 44.30 O ANISOU 586 O GLN A 121 5146 5402 6285 1334 -1363 746 O ATOM 587 CB GLN A 121 -0.521 -11.413 -30.702 1.00 52.65 C ANISOU 587 CB GLN A 121 6787 6110 7106 1694 -2732 792 C ATOM 588 CG GLN A 121 -0.640 -11.682 -32.195 1.00 59.43 C ANISOU 588 CG GLN A 121 8206 6866 7511 1912 -3011 761 C ATOM 589 CD GLN A 121 -2.070 -11.536 -32.709 1.00 62.79 C ANISOU 589 CD GLN A 121 8524 7115 8219 1863 -3421 744 C ATOM 590 OE1 GLN A 121 -2.984 -11.213 -31.951 0.00 62.39 O ANISOU 590 OE1 GLN A 121 7975 7022 8708 1669 -3449 793 O ATOM 591 NE2 GLN A 121 -2.263 -11.782 -33.999 0.00 66.98 N ANISOU 591 NE2 GLN A 121 9536 7521 8393 2060 -3719 665 N ATOM 592 N SER A 122 0.394 -12.050 -27.788 1.00 45.23 N ANISOU 592 N SER A 122 5044 5525 6616 1152 -1897 615 N ATOM 593 CA SER A 122 0.388 -11.747 -26.359 1.00 44.21 C ANISOU 593 CA SER A 122 4499 5507 6791 979 -1514 583 C ATOM 594 C SER A 122 1.805 -11.684 -25.789 1.00 42.61 C ANISOU 594 C SER A 122 4389 5455 6346 931 -1088 469 C ATOM 595 O SER A 122 2.112 -10.790 -25.002 1.00 38.87 O ANISOU 595 O SER A 122 3745 5015 6008 898 -756 437 O ATOM 596 CB SER A 122 -0.469 -12.748 -25.583 1.00 42.39 C ANISOU 596 CB SER A 122 3932 5266 6906 846 -1684 588 C ATOM 597 OG SER A 122 -1.821 -12.690 -26.011 1.00 47.91 O ANISOU 597 OG SER A 122 4446 5773 7986 868 -2062 719 O ATOM 598 N PHE A 123 2.666 -12.622 -26.192 1.00 37.70 N ANISOU 598 N PHE A 123 4039 4888 5396 945 -1133 400 N ATOM 599 CA PHE A 123 4.069 -12.609 -25.765 1.00 32.32 C ANISOU 599 CA PHE A 123 3428 4309 4543 908 -767 317 C ATOM 600 C PHE A 123 4.764 -11.296 -26.124 1.00 35.70 C ANISOU 600 C PHE A 123 3920 4664 4982 1003 -466 405 C ATOM 601 O PHE A 123 5.390 -10.657 -25.276 1.00 32.89 O ANISOU 601 O PHE A 123 3372 4316 4808 923 -188 336 O ATOM 602 CB PHE A 123 4.857 -13.760 -26.395 1.00 32.39 C ANISOU 602 CB PHE A 123 3758 4353 4196 963 -856 277 C ATOM 603 CG PHE A 123 6.318 -13.780 -26.008 1.00 34.47 C ANISOU 603 CG PHE A 123 4051 4688 4360 929 -487 227 C ATOM 604 CD1 PHE A 123 6.733 -14.431 -24.856 1.00 36.56 C ANISOU 604 CD1 PHE A 123 4119 5067 4706 766 -401 82 C ATOM 605 CD2 PHE A 123 7.276 -13.155 -26.797 1.00 40.59 C ANISOU 605 CD2 PHE A 123 5033 5386 5002 1082 -223 357 C ATOM 606 CE1 PHE A 123 8.077 -14.462 -24.491 1.00 32.88 C ANISOU 606 CE1 PHE A 123 3653 4629 4210 734 -132 30 C ATOM 607 CE2 PHE A 123 8.626 -13.182 -26.445 1.00 39.13 C ANISOU 607 CE2 PHE A 123 4798 5211 4856 1044 101 346 C ATOM 608 CZ PHE A 123 9.028 -13.834 -25.289 1.00 31.83 C ANISOU 608 CZ PHE A 123 3667 4392 4035 858 109 163 C ATOM 609 N GLU A 124 4.658 -10.910 -27.390 1.00 35.89 N ANISOU 609 N GLU A 124 4229 4583 4824 1199 -547 563 N ATOM 610 CA GLU A 124 5.406 -9.763 -27.898 1.00 41.81 C ANISOU 610 CA GLU A 124 5061 5232 5594 1326 -215 721 C ATOM 611 C GLU A 124 4.957 -8.451 -27.258 1.00 39.67 C ANISOU 611 C GLU A 124 4465 4883 5724 1251 -90 732 C ATOM 612 O GLU A 124 5.767 -7.569 -26.983 1.00 43.63 O ANISOU 612 O GLU A 124 4843 5297 6438 1234 217 766 O ATOM 613 CB GLU A 124 5.276 -9.686 -29.419 1.00 52.98 C ANISOU 613 CB GLU A 124 6922 6551 6659 1627 -322 922 C ATOM 614 CG GLU A 124 6.261 -8.741 -30.091 1.00 63.85 C ANISOU 614 CG GLU A 124 8440 7811 8009 1819 120 1169 C ATOM 615 CD GLU A 124 5.966 -8.547 -31.573 1.00 73.38 C ANISOU 615 CD GLU A 124 10145 8920 8816 2198 32 1399 C ATOM 616 OE1 GLU A 124 4.868 -8.953 -32.022 1.00 74.88 O ANISOU 616 OE1 GLU A 124 10526 9104 8821 2282 -463 1327 O ATOM 617 OE2 GLU A 124 6.832 -7.991 -32.287 1.00 77.71 O ANISOU 617 OE2 GLU A 124 10896 9370 9262 2437 450 1670 O ATOM 618 N AGLN A 125 3.659 -8.323 -27.012 0.32 39.38 N ANISOU 618 N AGLN A 125 4271 4845 5847 1216 -341 709 N ATOM 619 N BGLN A 125 3.658 -8.337 -27.012 0.68 39.06 N ANISOU 619 N BGLN A 125 4232 4805 5805 1216 -343 708 N ATOM 620 CA AGLN A 125 3.130 -7.082 -26.455 0.32 40.17 C ANISOU 620 CA AGLN A 125 4098 4860 6305 1190 -224 724 C ATOM 621 CA BGLN A 125 3.100 -7.109 -26.453 0.68 40.05 C ANISOU 621 CA BGLN A 125 4082 4847 6287 1189 -233 723 C ATOM 622 C AGLN A 125 3.504 -6.901 -24.984 0.32 38.37 C ANISOU 622 C AGLN A 125 3600 4684 6297 1047 -23 521 C ATOM 623 C BGLN A 125 3.516 -6.908 -24.997 0.68 38.74 C ANISOU 623 C BGLN A 125 3650 4731 6340 1048 -23 523 C ATOM 624 O AGLN A 125 3.711 -5.776 -24.523 0.32 38.90 O ANISOU 624 O AGLN A 125 3525 4640 6616 1055 155 489 O ATOM 625 O BGLN A 125 3.765 -5.777 -24.562 0.68 38.90 O ANISOU 625 O BGLN A 125 3534 4637 6609 1056 160 493 O ATOM 626 CB AGLN A 125 1.615 -6.993 -26.651 0.32 41.90 C ANISOU 626 CB AGLN A 125 4208 5035 6678 1225 -528 797 C ATOM 627 CB BGLN A 125 1.580 -7.107 -26.593 0.68 39.84 C ANISOU 627 CB BGLN A 125 3938 4785 6416 1214 -545 785 C ATOM 628 CG AGLN A 125 1.178 -7.063 -28.107 0.32 47.49 C ANISOU 628 CG AGLN A 125 5232 5648 7165 1414 -830 965 C ATOM 629 CG BGLN A 125 1.113 -7.060 -28.031 0.68 46.53 C ANISOU 629 CG BGLN A 125 5082 5528 7070 1403 -834 959 C ATOM 630 CD AGLN A 125 2.136 -6.356 -29.052 0.32 50.56 C ANISOU 630 CD AGLN A 125 5928 5959 7324 1601 -580 1126 C ATOM 631 CD BGLN A 125 -0.372 -6.790 -28.157 0.68 48.98 C ANISOU 631 CD BGLN A 125 5205 5736 7668 1428 -1163 1039 C ATOM 632 OE1AGLN A 125 2.398 -5.160 -28.918 0.32 49.91 O ANISOU 632 OE1AGLN A 125 5711 5782 7470 1618 -296 1215 O ATOM 633 OE1BGLN A 125 -0.911 -5.900 -27.500 0.68 46.91 O ANISOU 633 OE1BGLN A 125 4636 5430 7759 1385 -1008 1063 O ATOM 634 NE2AGLN A 125 2.667 -7.100 -30.016 0.32 53.61 N ANISOU 634 NE2AGLN A 125 6734 6359 7277 1772 -663 1184 N ATOM 635 NE2BGLN A 125 -1.042 -7.562 -29.002 0.68 52.85 N ANISOU 635 NE2BGLN A 125 5881 6157 8043 1516 -1648 1075 N ATOM 636 N VAL A 126 3.600 -8.010 -24.254 1.00 34.10 N ANISOU 636 N VAL A 126 3020 4286 5649 949 -79 379 N ATOM 637 CA VAL A 126 4.009 -7.961 -22.856 1.00 32.79 C ANISOU 637 CA VAL A 126 2693 4174 5590 878 80 175 C ATOM 638 C VAL A 126 5.504 -7.634 -22.749 1.00 31.34 C ANISOU 638 C VAL A 126 2566 3921 5421 848 248 88 C ATOM 639 O VAL A 126 5.910 -6.762 -21.981 1.00 36.42 O ANISOU 639 O VAL A 126 3094 4455 6290 852 345 -45 O ATOM 640 CB VAL A 126 3.774 -9.307 -22.129 1.00 30.40 C ANISOU 640 CB VAL A 126 2356 4038 5155 809 0 87 C ATOM 641 CG1 VAL A 126 4.393 -9.266 -20.741 1.00 29.67 C ANISOU 641 CG1 VAL A 126 2204 3998 5072 801 160 -128 C ATOM 642 CG2 VAL A 126 2.279 -9.658 -22.052 1.00 30.58 C ANISOU 642 CG2 VAL A 126 2215 4074 5330 829 -144 208 C ATOM 643 N VAL A 127 6.318 -8.348 -23.515 1.00 32.43 N ANISOU 643 N VAL A 127 2875 4088 5357 839 261 165 N ATOM 644 CA AVAL A 127 7.766 -8.180 -23.411 0.36 29.90 C ANISOU 644 CA AVAL A 127 2545 3676 5141 807 437 130 C ATOM 645 CA BVAL A 127 7.768 -8.197 -23.438 0.64 32.82 C ANISOU 645 CA BVAL A 127 2919 4047 5503 809 437 134 C ATOM 646 C VAL A 127 8.249 -6.817 -23.908 1.00 33.70 C ANISOU 646 C VAL A 127 2947 3913 5946 871 617 277 C ATOM 647 O VAL A 127 9.108 -6.213 -23.289 1.00 38.76 O ANISOU 647 O VAL A 127 3416 4392 6921 818 693 176 O ATOM 648 CB AVAL A 127 8.565 -9.336 -24.071 0.36 33.51 C ANISOU 648 CB AVAL A 127 3199 4215 5319 815 471 205 C ATOM 649 CB BVAL A 127 8.477 -9.336 -24.201 0.64 33.28 C ANISOU 649 CB BVAL A 127 3191 4187 5267 829 464 227 C ATOM 650 CG1AVAL A 127 8.225 -10.661 -23.402 0.36 33.03 C ANISOU 650 CG1AVAL A 127 3163 4356 5031 729 294 41 C ATOM 651 CG1BVAL A 127 9.970 -9.088 -24.296 0.64 30.14 C ANISOU 651 CG1BVAL A 127 2738 3645 5067 825 703 286 C ATOM 652 CG2AVAL A 127 8.328 -9.398 -25.577 0.36 32.91 C ANISOU 652 CG2AVAL A 127 3400 4106 4999 986 487 462 C ATOM 653 CG2BVAL A 127 8.212 -10.665 -23.506 0.64 33.25 C ANISOU 653 CG2BVAL A 127 3207 4381 5047 737 294 57 C ATOM 654 N ASN A 128 7.673 -6.322 -25.000 1.00 40.18 N ANISOU 654 N ASN A 128 3885 4676 6706 996 649 515 N ATOM 655 CA ASN A 128 8.059 -5.009 -25.519 1.00 46.72 C ANISOU 655 CA ASN A 128 4630 5256 7867 1077 857 711 C ATOM 656 C ASN A 128 7.728 -3.882 -24.543 1.00 42.77 C ANISOU 656 C ASN A 128 3866 4612 7771 1013 809 538 C ATOM 657 O ASN A 128 8.487 -2.921 -24.403 1.00 47.72 O ANISOU 657 O ASN A 128 4317 4982 8834 1001 937 568 O ATOM 658 CB ASN A 128 7.402 -4.741 -26.872 1.00 50.53 C ANISOU 658 CB ASN A 128 5351 5718 8130 1273 877 1006 C ATOM 659 CG ASN A 128 7.999 -5.573 -27.987 1.00 51.61 C ANISOU 659 CG ASN A 128 5828 5905 7877 1440 992 1213 C ATOM 660 OD1 ASN A 128 9.124 -6.063 -27.880 1.00 51.20 O ANISOU 660 OD1 ASN A 128 5764 5839 7850 1411 1181 1223 O ATOM 661 ND2 ASN A 128 7.247 -5.731 -29.076 1.00 53.37 N ANISOU 661 ND2 ASN A 128 6383 6163 7734 1652 859 1378 N ATOM 662 N GLU A 129 6.600 -4.004 -23.852 1.00 37.33 N ANISOU 662 N GLU A 129 3146 4056 6981 995 627 368 N ATOM 663 CA GLU A 129 6.241 -3.014 -22.849 1.00 38.09 C ANISOU 663 CA GLU A 129 3064 4027 7382 998 594 178 C ATOM 664 C GLU A 129 7.077 -3.192 -21.594 1.00 37.82 C ANISOU 664 C GLU A 129 2963 3957 7450 934 534 -134 C ATOM 665 O GLU A 129 7.387 -2.227 -20.907 1.00 43.30 O ANISOU 665 O GLU A 129 3547 4428 8478 959 491 -306 O ATOM 666 CB GLU A 129 4.743 -3.067 -22.507 1.00 35.65 C ANISOU 666 CB GLU A 129 2737 3849 6959 1055 491 150 C ATOM 667 CG GLU A 129 4.308 -2.108 -21.376 1.00 36.78 C ANISOU 667 CG GLU A 129 2758 3874 7344 1128 499 -57 C ATOM 668 CD GLU A 129 4.266 -0.626 -21.769 1.00 43.64 C ANISOU 668 CD GLU A 129 3528 4468 8585 1190 559 33 C ATOM 669 OE1 GLU A 129 4.347 -0.292 -22.967 1.00 40.28 O ANISOU 669 OE1 GLU A 129 3120 3963 8223 1196 623 311 O ATOM 670 OE2 GLU A 129 4.137 0.215 -20.854 1.00 44.70 O ANISOU 670 OE2 GLU A 129 3611 4458 8915 1259 540 -176 O ATOM 671 N LEU A 130 7.435 -4.429 -21.277 1.00 33.82 N ANISOU 671 N LEU A 130 2544 3647 6658 872 484 -226 N ATOM 672 CA LEU A 130 8.228 -4.665 -20.087 1.00 33.39 C ANISOU 672 CA LEU A 130 2467 3561 6658 842 384 -524 C ATOM 673 C LEU A 130 9.588 -3.985 -20.228 1.00 35.60 C ANISOU 673 C LEU A 130 2606 3534 7387 787 393 -529 C ATOM 674 O LEU A 130 10.144 -3.508 -19.246 1.00 37.83 O ANISOU 674 O LEU A 130 2820 3625 7927 799 219 -804 O ATOM 675 CB LEU A 130 8.418 -6.174 -19.858 1.00 31.26 C ANISOU 675 CB LEU A 130 2311 3552 6015 784 348 -569 C ATOM 676 CG LEU A 130 9.517 -6.576 -18.867 1.00 31.20 C ANISOU 676 CG LEU A 130 2303 3502 6047 751 233 -829 C ATOM 677 CD1 LEU A 130 9.240 -6.029 -17.473 1.00 32.52 C ANISOU 677 CD1 LEU A 130 2517 3603 6236 885 88 -1146 C ATOM 678 CD2 LEU A 130 9.657 -8.087 -18.827 1.00 29.11 C ANISOU 678 CD2 LEU A 130 2146 3494 5419 693 230 -814 C ATOM 679 N PHE A 131 10.108 -3.942 -21.452 1.00 35.60 N ANISOU 679 N PHE A 131 2570 3454 7504 759 586 -209 N ATOM 680 CA PHE A 131 11.413 -3.322 -21.703 1.00 43.74 C ANISOU 680 CA PHE A 131 3392 4148 9079 716 675 -105 C ATOM 681 C PHE A 131 11.295 -2.033 -22.509 1.00 47.06 C ANISOU 681 C PHE A 131 3708 4306 9865 762 841 167 C ATOM 682 O PHE A 131 12.204 -1.691 -23.278 1.00 47.21 O ANISOU 682 O PHE A 131 3638 4112 10188 732 1058 465 O ATOM 683 CB PHE A 131 12.348 -4.278 -22.447 1.00 40.02 C ANISOU 683 CB PHE A 131 2958 3740 8507 690 870 122 C ATOM 684 CG PHE A 131 12.687 -5.514 -21.688 1.00 35.30 C ANISOU 684 CG PHE A 131 2445 3353 7613 617 711 -117 C ATOM 685 CD1 PHE A 131 13.617 -5.478 -20.658 1.00 36.14 C ANISOU 685 CD1 PHE A 131 2388 3283 8059 542 502 -379 C ATOM 686 CD2 PHE A 131 12.101 -6.733 -22.019 1.00 34.26 C ANISOU 686 CD2 PHE A 131 2560 3564 6895 635 729 -80 C ATOM 687 CE1 PHE A 131 13.943 -6.629 -19.970 1.00 34.41 C ANISOU 687 CE1 PHE A 131 2266 3258 7548 497 359 -580 C ATOM 688 CE2 PHE A 131 12.430 -7.883 -21.335 1.00 33.63 C ANISOU 688 CE2 PHE A 131 2545 3662 6571 571 604 -271 C ATOM 689 CZ PHE A 131 13.334 -7.841 -20.306 1.00 31.76 C ANISOU 689 CZ PHE A 131 2163 3285 6619 508 441 -513 C ATOM 690 N AARG A 132 10.176 -1.335 -22.338 0.50 47.54 N ANISOU 690 N AARG A 132 3801 4387 9875 831 766 97 N ATOM 691 N BARG A 132 10.189 -1.323 -22.324 0.50 47.58 N ANISOU 691 N BARG A 132 3804 4387 9886 829 763 94 N ATOM 692 CA AARG A 132 9.885 -0.123 -23.099 0.50 50.07 C ANISOU 692 CA AARG A 132 4065 4499 10462 873 906 355 C ATOM 693 CA BARG A 132 9.891 -0.135 -23.115 0.50 50.07 C ANISOU 693 CA BARG A 132 4065 4500 10458 873 910 360 C ATOM 694 C AARG A 132 10.994 0.922 -23.005 0.50 50.69 C ANISOU 694 C AARG A 132 3926 4175 11158 749 918 405 C ATOM 695 C BARG A 132 10.966 0.950 -23.006 0.50 50.76 C ANISOU 695 C BARG A 132 3935 4183 11169 751 917 405 C ATOM 696 O AARG A 132 11.499 1.391 -24.024 0.50 52.01 O ANISOU 696 O AARG A 132 4020 4172 11569 753 1195 792 O ATOM 697 O BARG A 132 11.421 1.477 -24.020 0.50 51.98 O ANISOU 697 O BARG A 132 4016 4163 11572 757 1190 789 O ATOM 698 CB AARG A 132 8.552 0.488 -22.649 0.50 51.55 C ANISOU 698 CB AARG A 132 4294 4747 10546 948 773 202 C ATOM 699 CB BARG A 132 8.522 0.433 -22.727 0.50 52.48 C ANISOU 699 CB BARG A 132 4420 4881 10640 954 786 224 C ATOM 700 CG AARG A 132 8.258 1.860 -23.250 0.50 57.68 C ANISOU 700 CG AARG A 132 4994 5283 11641 976 873 414 C ATOM 701 CG BARG A 132 7.926 1.381 -23.755 0.50 59.18 C ANISOU 701 CG BARG A 132 5265 5618 11604 1037 946 546 C ATOM 702 CD AARG A 132 6.972 1.855 -24.076 0.50 57.69 C ANISOU 702 CD AARG A 132 5111 5455 11355 1122 951 638 C ATOM 703 CD BARG A 132 7.502 0.638 -25.018 0.50 61.20 C ANISOU 703 CD BARG A 132 5695 6069 11488 1179 1104 883 C ATOM 704 NE AARG A 132 6.851 0.656 -24.903 0.50 60.73 N ANISOU 704 NE AARG A 132 5670 6090 11315 1198 1023 831 N ATOM 705 NE BARG A 132 6.320 -0.193 -24.795 0.50 60.00 N ANISOU 705 NE BARG A 132 5704 6237 10858 1187 910 751 N ATOM 706 CZ AARG A 132 7.553 0.424 -26.010 0.50 60.78 C ANISOU 706 CZ AARG A 132 5786 6057 11252 1270 1244 1159 C ATOM 707 CZ BARG A 132 5.617 -0.768 -25.766 0.50 56.10 C ANISOU 707 CZ BARG A 132 5424 5915 9976 1279 873 956 C ATOM 708 NH1AARG A 132 8.446 1.307 -26.438 0.50 62.40 N ANISOU 708 NH1AARG A 132 5860 5969 11880 1271 1475 1386 N ATOM 709 NH1BARG A 132 5.968 -0.601 -27.034 0.50 58.09 N ANISOU 709 NH1BARG A 132 5843 6086 10140 1420 1042 1294 N ATOM 710 NH2AARG A 132 7.365 -0.699 -26.690 0.50 58.94 N ANISOU 710 NH2AARG A 132 5829 6074 10489 1335 1227 1261 N ATOM 711 NH2BARG A 132 4.560 -1.505 -25.468 0.50 49.88 N ANISOU 711 NH2BARG A 132 4693 5347 8913 1262 657 838 N ATOM 712 N ASP A 133 11.361 1.280 -21.778 1.00 48.45 N ANISOU 712 N ASP A 133 3542 3724 11142 663 610 26 N ATOM 713 CA ASP A 133 12.354 2.327 -21.545 1.00 58.69 C ANISOU 713 CA ASP A 133 4575 4596 13128 525 507 14 C ATOM 714 C ASP A 133 13.733 1.779 -21.173 1.00 56.15 C ANISOU 714 C ASP A 133 4096 4119 13117 387 396 -55 C ATOM 715 O ASP A 133 14.533 2.473 -20.542 1.00 59.20 O ANISOU 715 O ASP A 133 4232 4176 14085 263 126 -228 O ATOM 716 CB ASP A 133 11.851 3.311 -20.478 1.00 66.16 C ANISOU 716 CB ASP A 133 5506 5392 14240 557 163 -371 C ATOM 717 CG ASP A 133 10.938 2.642 -19.460 1.00 71.02 C ANISOU 717 CG ASP A 133 6396 6304 14283 713 -33 -750 C ATOM 718 OD1 ASP A 133 11.216 1.474 -19.105 1.00 69.29 O ANISOU 718 OD1 ASP A 133 6278 6291 13759 722 -78 -868 O ATOM 719 OD2 ASP A 133 9.936 3.264 -19.034 1.00 70.11 O ANISOU 719 OD2 ASP A 133 6395 6219 14023 840 -100 -896 O ATOM 720 N GLY A 134 14.021 0.538 -21.567 1.00 51.43 N ANISOU 720 N GLY A 134 3619 3759 12162 410 571 77 N ATOM 721 CA GLY A 134 15.356 0.001 -21.373 1.00 54.55 C ANISOU 721 CA GLY A 134 3864 3990 12873 282 527 88 C ATOM 722 C GLY A 134 15.382 -1.346 -20.683 1.00 54.83 C ANISOU 722 C GLY A 134 4073 4324 12436 319 357 -191 C ATOM 723 O GLY A 134 14.353 -2.028 -20.588 1.00 46.14 O ANISOU 723 O GLY A 134 3206 3605 10719 441 372 -301 O ATOM 724 N VAL A 135 16.563 -1.723 -20.198 1.00 48.56 N ANISOU 724 N VAL A 135 3136 3334 11978 203 188 -290 N ATOM 725 CA VAL A 135 16.762 -3.030 -19.582 1.00 46.33 C ANISOU 725 CA VAL A 135 2997 3313 11294 229 42 -518 C ATOM 726 C VAL A 135 17.429 -2.870 -18.219 1.00 48.00 C ANISOU 726 C VAL A 135 3105 3282 11851 174 -491 -969 C ATOM 727 O VAL A 135 18.235 -1.962 -18.000 1.00 52.01 O ANISOU 727 O VAL A 135 3350 3398 13016 65 -701 -990 O ATOM 728 CB VAL A 135 17.628 -3.966 -20.476 1.00 47.44 C ANISOU 728 CB VAL A 135 3135 3508 11383 194 388 -150 C ATOM 729 CG1 VAL A 135 17.752 -5.365 -19.869 1.00 46.78 C ANISOU 729 CG1 VAL A 135 3196 3735 10843 211 246 -379 C ATOM 730 CG2 VAL A 135 17.071 -4.043 -21.884 1.00 49.12 C ANISOU 730 CG2 VAL A 135 3480 3916 11268 306 866 289 C ATOM 731 N ASN A 136 17.076 -3.754 -17.301 1.00 45.71 N ANISOU 731 N ASN A 136 3025 3278 11065 284 -730 -1318 N ATOM 732 CA ASN A 136 17.811 -3.920 -16.066 1.00 51.08 C ANISOU 732 CA ASN A 136 3665 3823 11921 287 -1250 -1723 C ATOM 733 C ASN A 136 17.614 -5.354 -15.627 1.00 49.73 C ANISOU 733 C ASN A 136 3751 4018 11126 393 -1244 -1866 C ATOM 734 O ASN A 136 16.782 -6.077 -16.211 1.00 44.05 O ANISOU 734 O ASN A 136 3180 3685 9872 448 -882 -1678 O ATOM 735 CB ASN A 136 17.401 -2.881 -15.003 1.00 54.37 C ANISOU 735 CB ASN A 136 4137 4185 12336 449 -1697 -2080 C ATOM 736 CG ASN A 136 15.928 -2.961 -14.632 1.00 52.29 C ANISOU 736 CG ASN A 136 4300 4217 11349 646 -1587 -2240 C ATOM 737 OD1 ASN A 136 15.403 -4.044 -14.359 1.00 44.97 O ANISOU 737 OD1 ASN A 136 3641 3620 9826 751 -1471 -2312 O ATOM 738 ND2 ASN A 136 15.255 -1.807 -14.607 1.00 52.97 N ANISOU 738 ND2 ASN A 136 4412 4193 11521 710 -1605 -2270 N ATOM 739 N TRP A 137 18.393 -5.803 -14.650 1.00 52.46 N ANISOU 739 N TRP A 137 4097 4341 11494 449 -1641 -2124 N ATOM 740 CA TRP A 137 18.357 -7.225 -14.295 1.00 47.02 C ANISOU 740 CA TRP A 137 3620 3951 10294 512 -1620 -2233 C ATOM 741 C TRP A 137 16.976 -7.611 -13.738 1.00 40.35 C ANISOU 741 C TRP A 137 3208 3499 8623 684 -1543 -2408 C ATOM 742 O TRP A 137 16.492 -8.720 -13.942 1.00 37.16 O ANISOU 742 O TRP A 137 2960 3495 7664 669 -1279 -2263 O ATOM 743 CB TRP A 137 19.483 -7.556 -13.313 1.00 48.95 C ANISOU 743 CB TRP A 137 3888 4099 10612 639 -1999 -2368 C ATOM 744 CG TRP A 137 20.868 -7.438 -13.909 1.00 53.32 C ANISOU 744 CG TRP A 137 4187 4272 11799 503 -1902 -2083 C ATOM 745 CD1 TRP A 137 21.810 -6.486 -13.625 1.00 59.39 C ANISOU 745 CD1 TRP A 137 4739 4682 13146 529 -2176 -2056 C ATOM 746 CD2 TRP A 137 21.461 -8.301 -14.891 1.00 51.50 C ANISOU 746 CD2 TRP A 137 3889 3992 11687 330 -1504 -1765 C ATOM 747 NE1 TRP A 137 22.954 -6.713 -14.362 1.00 58.89 N ANISOU 747 NE1 TRP A 137 4471 4359 13545 389 -1942 -1726 N ATOM 748 CE2 TRP A 137 22.763 -7.819 -15.146 1.00 51.97 C ANISOU 748 CE2 TRP A 137 3695 3671 12379 272 -1521 -1532 C ATOM 749 CE3 TRP A 137 21.018 -9.430 -15.580 1.00 41.99 C ANISOU 749 CE3 TRP A 137 2794 3205 9955 210 -1124 -1571 C ATOM 750 CZ2 TRP A 137 23.622 -8.437 -16.065 1.00 50.11 C ANISOU 750 CZ2 TRP A 137 3335 3316 12388 150 -1154 -1158 C ATOM 751 CZ3 TRP A 137 21.884 -10.051 -16.487 1.00 43.31 C ANISOU 751 CZ3 TRP A 137 2849 3332 10276 103 -783 -1194 C ATOM 752 CH2 TRP A 137 23.160 -9.550 -16.720 1.00 47.34 C ANISOU 752 CH2 TRP A 137 3129 3349 11506 74 -786 -1001 C ATOM 753 N GLY A 138 16.329 -6.668 -13.056 1.00 47.63 N ANISOU 753 N GLY A 138 4298 4384 9414 835 -1727 -2592 N ATOM 754 CA GLY A 138 15.010 -6.919 -12.511 1.00 44.52 C ANISOU 754 CA GLY A 138 4271 4320 8323 1041 -1583 -2682 C ATOM 755 C GLY A 138 14.019 -7.259 -13.603 1.00 37.45 C ANISOU 755 C GLY A 138 3315 3684 7229 965 -1096 -2351 C ATOM 756 O GLY A 138 13.228 -8.189 -13.470 1.00 35.17 O ANISOU 756 O GLY A 138 3206 3760 6397 1021 -891 -2264 O ATOM 757 N ARG A 139 14.076 -6.504 -14.692 1.00 37.63 N ANISOU 757 N ARG A 139 3080 3535 7684 823 -922 -2097 N ATOM 758 CA ARG A 139 13.195 -6.734 -15.817 1.00 35.16 C ANISOU 758 CA ARG A 139 2739 3467 7153 748 -527 -1733 C ATOM 759 C ARG A 139 13.528 -8.059 -16.466 1.00 34.78 C ANISOU 759 C ARG A 139 2692 3665 6858 624 -343 -1513 C ATOM 760 O ARG A 139 12.653 -8.759 -16.949 1.00 30.43 O ANISOU 760 O ARG A 139 2252 3405 5905 620 -146 -1338 O ATOM 761 CB ARG A 139 13.295 -5.593 -16.820 1.00 36.60 C ANISOU 761 CB ARG A 139 2689 3378 7839 678 -390 -1501 C ATOM 762 CG ARG A 139 12.848 -4.237 -16.214 1.00 39.24 C ANISOU 762 CG ARG A 139 3028 3452 8429 809 -578 -1722 C ATOM 763 CD ARG A 139 13.054 -3.105 -17.181 1.00 41.02 C ANISOU 763 CD ARG A 139 3008 3380 9199 717 -444 -1461 C ATOM 764 NE ARG A 139 12.552 -1.840 -16.644 1.00 43.52 N ANISOU 764 NE ARG A 139 3366 3491 9679 802 -618 -1642 N ATOM 765 CZ ARG A 139 12.319 -0.767 -17.389 1.00 50.17 C ANISOU 765 CZ ARG A 139 4062 4144 10856 749 -478 -1416 C ATOM 766 NH1 ARG A 139 12.528 -0.818 -18.698 1.00 47.72 N ANISOU 766 NH1 ARG A 139 3605 3832 10695 641 -146 -988 N ATOM 767 NH2 ARG A 139 11.857 0.346 -16.834 1.00 53.81 N ANISOU 767 NH2 ARG A 139 4568 4436 11441 835 -654 -1603 N ATOM 768 N ILE A 140 14.807 -8.415 -16.466 1.00 36.35 N ANISOU 768 N ILE A 140 2756 3710 7344 532 -437 -1527 N ATOM 769 CA ILE A 140 15.183 -9.697 -17.059 1.00 32.44 C ANISOU 769 CA ILE A 140 2287 3432 6608 443 -255 -1332 C ATOM 770 C ILE A 140 14.617 -10.884 -16.281 1.00 29.12 C ANISOU 770 C ILE A 140 2106 3349 5608 499 -323 -1480 C ATOM 771 O ILE A 140 14.151 -11.858 -16.862 1.00 26.95 O ANISOU 771 O ILE A 140 1924 3331 4985 461 -143 -1299 O ATOM 772 CB ILE A 140 16.705 -9.814 -17.195 1.00 32.81 C ANISOU 772 CB ILE A 140 2098 3214 7153 351 -309 -1284 C ATOM 773 CG1 ILE A 140 17.172 -8.841 -18.273 1.00 35.11 C ANISOU 773 CG1 ILE A 140 2151 3200 7989 302 -73 -965 C ATOM 774 CG2 ILE A 140 17.088 -11.254 -17.534 1.00 30.95 C ANISOU 774 CG2 ILE A 140 1945 3218 6594 301 -162 -1157 C ATOM 775 CD1 ILE A 140 18.693 -8.712 -18.385 1.00 40.13 C ANISOU 775 CD1 ILE A 140 2601 3468 9178 191 -93 -835 C ATOM 776 N VAL A 141 14.638 -10.789 -14.962 1.00 30.76 N ANISOU 776 N VAL A 141 2437 3530 5721 624 -594 -1803 N ATOM 777 CA VAL A 141 14.058 -11.839 -14.137 1.00 30.17 C ANISOU 777 CA VAL A 141 2599 3755 5110 732 -600 -1898 C ATOM 778 C VAL A 141 12.539 -11.928 -14.382 1.00 27.71 C ANISOU 778 C VAL A 141 2374 3678 4479 795 -358 -1731 C ATOM 779 O VAL A 141 12.008 -13.020 -14.588 1.00 25.87 O ANISOU 779 O VAL A 141 2188 3690 3951 760 -215 -1575 O ATOM 780 CB VAL A 141 14.357 -11.622 -12.642 1.00 35.22 C ANISOU 780 CB VAL A 141 3437 4297 5647 949 -927 -2271 C ATOM 781 CG1 VAL A 141 13.594 -12.623 -11.791 1.00 33.24 C ANISOU 781 CG1 VAL A 141 3455 4359 4816 1129 -827 -2293 C ATOM 782 CG2 VAL A 141 15.872 -11.727 -12.388 1.00 32.94 C ANISOU 782 CG2 VAL A 141 3031 3758 5728 872 -1247 -2433 C ATOM 783 N ALA A 142 11.864 -10.776 -14.382 1.00 29.60 N ANISOU 783 N ALA A 142 2599 3800 4850 884 -336 -1755 N ATOM 784 CA ALA A 142 10.440 -10.715 -14.720 1.00 28.77 C ANISOU 784 CA ALA A 142 2503 3854 4573 934 -120 -1563 C ATOM 785 C ALA A 142 10.130 -11.313 -16.093 1.00 26.33 C ANISOU 785 C ALA A 142 2089 3657 4259 755 30 -1251 C ATOM 786 O ALA A 142 9.116 -11.979 -16.271 1.00 25.44 O ANISOU 786 O ALA A 142 1988 3723 3954 763 127 -1094 O ATOM 787 CB ALA A 142 9.920 -9.252 -14.647 1.00 30.31 C ANISOU 787 CB ALA A 142 2670 3855 4993 1046 -129 -1628 C ATOM 788 N PHE A 143 11.018 -11.084 -17.061 1.00 26.21 N ANISOU 788 N PHE A 143 1980 3502 4478 627 39 -1150 N ATOM 789 CA PHE A 143 10.887 -11.690 -18.390 1.00 24.99 C ANISOU 789 CA PHE A 143 1834 3430 4233 536 160 -880 C ATOM 790 C PHE A 143 10.876 -13.240 -18.326 1.00 24.21 C ANISOU 790 C PHE A 143 1831 3548 3819 489 141 -856 C ATOM 791 O PHE A 143 10.026 -13.912 -18.959 1.00 23.36 O ANISOU 791 O PHE A 143 1780 3563 3532 476 147 -703 O ATOM 792 CB PHE A 143 12.021 -11.166 -19.288 1.00 26.13 C ANISOU 792 CB PHE A 143 1892 3360 4678 484 251 -753 C ATOM 793 CG PHE A 143 12.295 -11.995 -20.499 1.00 25.93 C ANISOU 793 CG PHE A 143 1972 3408 4473 467 388 -516 C ATOM 794 CD1 PHE A 143 11.545 -11.824 -21.645 1.00 26.76 C ANISOU 794 CD1 PHE A 143 2192 3534 4439 533 466 -297 C ATOM 795 CD2 PHE A 143 13.358 -12.911 -20.510 1.00 24.84 C ANISOU 795 CD2 PHE A 143 1848 3288 4301 423 421 -518 C ATOM 796 CE1 PHE A 143 11.826 -12.561 -22.786 1.00 27.58 C ANISOU 796 CE1 PHE A 143 2491 3678 4312 595 563 -104 C ATOM 797 CE2 PHE A 143 13.644 -13.657 -21.642 1.00 27.99 C ANISOU 797 CE2 PHE A 143 2402 3734 4498 467 568 -306 C ATOM 798 CZ PHE A 143 12.867 -13.483 -22.790 1.00 26.09 C ANISOU 798 CZ PHE A 143 2343 3514 4058 573 633 -108 C ATOM 799 N PHE A 144 11.800 -13.817 -17.562 1.00 23.04 N ANISOU 799 N PHE A 144 1697 3416 3642 471 72 -1012 N ATOM 800 CA PHE A 144 11.811 -15.280 -17.419 1.00 21.61 C ANISOU 800 CA PHE A 144 1597 3424 3188 433 57 -990 C ATOM 801 C PHE A 144 10.551 -15.773 -16.695 1.00 21.42 C ANISOU 801 C PHE A 144 1606 3568 2966 506 62 -980 C ATOM 802 O PHE A 144 9.898 -16.723 -17.142 1.00 20.64 O ANISOU 802 O PHE A 144 1515 3577 2751 461 66 -833 O ATOM 803 CB PHE A 144 13.086 -15.782 -16.723 1.00 21.63 C ANISOU 803 CB PHE A 144 1600 3396 3221 411 -29 -1148 C ATOM 804 CG PHE A 144 14.268 -15.880 -17.647 1.00 21.77 C ANISOU 804 CG PHE A 144 1553 3282 3435 329 42 -1038 C ATOM 805 CD1 PHE A 144 14.494 -17.030 -18.400 1.00 27.83 C ANISOU 805 CD1 PHE A 144 2408 4154 4011 288 126 -898 C ATOM 806 CD2 PHE A 144 15.138 -14.806 -17.784 1.00 23.52 C ANISOU 806 CD2 PHE A 144 1618 3242 4078 319 45 -1049 C ATOM 807 CE1 PHE A 144 15.572 -17.112 -19.267 1.00 25.91 C ANISOU 807 CE1 PHE A 144 2134 3783 3929 277 271 -755 C ATOM 808 CE2 PHE A 144 16.218 -14.866 -18.647 1.00 24.32 C ANISOU 808 CE2 PHE A 144 1617 3190 4434 280 199 -869 C ATOM 809 CZ PHE A 144 16.440 -16.023 -19.393 1.00 25.04 C ANISOU 809 CZ PHE A 144 1833 3413 4267 278 344 -712 C ATOM 810 N SER A 145 10.222 -15.126 -15.584 1.00 22.64 N ANISOU 810 N SER A 145 1779 3706 3117 650 64 -1123 N ATOM 811 CA SER A 145 8.995 -15.458 -14.836 1.00 23.27 C ANISOU 811 CA SER A 145 1871 3914 3055 786 174 -1048 C ATOM 812 C SER A 145 7.737 -15.394 -15.716 1.00 26.75 C ANISOU 812 C SER A 145 2179 4360 3623 734 236 -803 C ATOM 813 O SER A 145 6.895 -16.288 -15.657 1.00 23.30 O ANISOU 813 O SER A 145 1667 4011 3174 731 284 -633 O ATOM 814 CB SER A 145 8.820 -14.554 -13.605 1.00 29.65 C ANISOU 814 CB SER A 145 2792 4669 3805 1032 204 -1233 C ATOM 815 OG SER A 145 9.835 -14.845 -12.650 1.00 35.49 O ANISOU 815 OG SER A 145 3698 5403 4383 1129 72 -1468 O ATOM 816 N PHE A 146 7.614 -14.340 -16.522 1.00 23.84 N ANISOU 816 N PHE A 146 1764 3866 3428 700 211 -773 N ATOM 817 CA PHE A 146 6.494 -14.240 -17.459 1.00 23.91 C ANISOU 817 CA PHE A 146 1670 3850 3565 661 192 -555 C ATOM 818 C PHE A 146 6.463 -15.414 -18.453 1.00 23.00 C ANISOU 818 C PHE A 146 1582 3775 3382 536 49 -426 C ATOM 819 O PHE A 146 5.423 -16.026 -18.678 1.00 23.62 O ANISOU 819 O PHE A 146 1559 3861 3554 520 -33 -271 O ATOM 820 CB PHE A 146 6.534 -12.935 -18.246 1.00 25.19 C ANISOU 820 CB PHE A 146 1819 3861 3890 663 181 -536 C ATOM 821 CG PHE A 146 5.574 -12.919 -19.395 1.00 25.08 C ANISOU 821 CG PHE A 146 1758 3806 3964 633 85 -324 C ATOM 822 CD1 PHE A 146 4.204 -13.008 -19.167 1.00 26.20 C ANISOU 822 CD1 PHE A 146 1743 3955 4257 681 76 -188 C ATOM 823 CD2 PHE A 146 6.031 -12.853 -20.695 1.00 25.00 C ANISOU 823 CD2 PHE A 146 1872 3726 3900 593 -1 -242 C ATOM 824 CE1 PHE A 146 3.298 -13.021 -20.237 1.00 28.18 C ANISOU 824 CE1 PHE A 146 1939 4124 4645 658 -111 -7 C ATOM 825 CE2 PHE A 146 5.130 -12.852 -21.770 1.00 26.06 C ANISOU 825 CE2 PHE A 146 2038 3802 4063 618 -168 -73 C ATOM 826 CZ PHE A 146 3.768 -12.938 -21.539 1.00 29.69 C ANISOU 826 CZ PHE A 146 2318 4250 4713 633 -269 25 C ATOM 827 N GLY A 147 7.602 -15.712 -19.063 1.00 22.05 N ANISOU 827 N GLY A 147 1594 3640 3142 468 6 -482 N ATOM 828 CA GLY A 147 7.702 -16.851 -19.955 1.00 23.15 C ANISOU 828 CA GLY A 147 1841 3804 3150 405 -133 -402 C ATOM 829 C GLY A 147 7.272 -18.131 -19.248 1.00 22.35 C ANISOU 829 C GLY A 147 1668 3803 3021 368 -185 -387 C ATOM 830 O GLY A 147 6.480 -18.905 -19.793 1.00 23.26 O ANISOU 830 O GLY A 147 1755 3884 3200 334 -369 -274 O ATOM 831 N GLY A 148 7.769 -18.343 -18.034 1.00 20.71 N ANISOU 831 N GLY A 148 1434 3685 2750 395 -51 -495 N ATOM 832 CA GLY A 148 7.350 -19.499 -17.242 1.00 21.74 C ANISOU 832 CA GLY A 148 1490 3905 2865 400 -28 -433 C ATOM 833 C GLY A 148 5.845 -19.580 -17.036 1.00 24.24 C ANISOU 833 C GLY A 148 1597 4187 3428 443 -1 -228 C ATOM 834 O GLY A 148 5.211 -20.635 -17.222 1.00 25.52 O ANISOU 834 O GLY A 148 1638 4314 3746 383 -110 -76 O ATOM 835 N ALA A 149 5.236 -18.449 -16.685 1.00 26.11 N ANISOU 835 N ALA A 149 1759 4390 3773 553 133 -203 N ATOM 836 CA ALA A 149 3.799 -18.406 -16.444 1.00 25.58 C ANISOU 836 CA ALA A 149 1446 4262 4013 622 218 34 C ATOM 837 C ALA A 149 3.009 -18.692 -17.718 1.00 26.33 C ANISOU 837 C ALA A 149 1411 4210 4382 493 -90 178 C ATOM 838 O ALA A 149 1.974 -19.358 -17.687 1.00 28.89 O ANISOU 838 O ALA A 149 1479 4438 5058 474 -154 400 O ATOM 839 CB ALA A 149 3.397 -17.029 -15.875 1.00 26.78 C ANISOU 839 CB ALA A 149 1583 4392 4198 796 430 8 C ATOM 840 N LEU A 150 3.491 -18.179 -18.839 1.00 26.45 N ANISOU 840 N LEU A 150 1607 4176 4269 434 -295 69 N ATOM 841 CA LEU A 150 2.810 -18.395 -20.106 1.00 26.74 C ANISOU 841 CA LEU A 150 1632 4058 4471 377 -655 163 C ATOM 842 C LEU A 150 2.866 -19.891 -20.490 1.00 26.96 C ANISOU 842 C LEU A 150 1693 4036 4512 288 -931 175 C ATOM 843 O LEU A 150 1.906 -20.424 -21.032 1.00 30.97 O ANISOU 843 O LEU A 150 2084 4368 5314 250 -1241 291 O ATOM 844 CB LEU A 150 3.425 -17.508 -21.196 1.00 26.27 C ANISOU 844 CB LEU A 150 1840 3961 4178 410 -746 66 C ATOM 845 CG LEU A 150 2.624 -17.250 -22.477 1.00 32.54 C ANISOU 845 CG LEU A 150 2696 4585 5084 448 -1099 158 C ATOM 846 CD1 LEU A 150 1.326 -16.476 -22.164 1.00 31.97 C ANISOU 846 CD1 LEU A 150 2309 4417 5421 478 -1084 316 C ATOM 847 CD2 LEU A 150 3.490 -16.454 -23.446 1.00 35.30 C ANISOU 847 CD2 LEU A 150 3374 4925 5112 538 -1064 96 C ATOM 848 N CYS A 151 3.982 -20.566 -20.205 1.00 26.04 N ANISOU 848 N CYS A 151 1753 4042 4100 258 -835 45 N ATOM 849 CA CYS A 151 4.086 -22.006 -20.499 1.00 25.42 C ANISOU 849 CA CYS A 151 1716 3909 4033 185 -1080 43 C ATOM 850 C CYS A 151 3.154 -22.811 -19.616 1.00 27.17 C ANISOU 850 C CYS A 151 1600 4074 4648 145 -1023 235 C ATOM 851 O CYS A 151 2.438 -23.715 -20.082 1.00 28.90 O ANISOU 851 O CYS A 151 1824 4094 5060 78 -1254 302 O ATOM 852 CB CYS A 151 5.524 -22.484 -20.272 1.00 23.24 C ANISOU 852 CB CYS A 151 1675 3779 3376 174 -927 -119 C ATOM 853 SG CYS A 151 6.632 -21.950 -21.543 1.00 27.44 S ANISOU 853 SG CYS A 151 2601 4298 3527 243 -978 -254 S ATOM 854 N VAL A 152 3.185 -22.512 -18.326 1.00 26.88 N ANISOU 854 N VAL A 152 1408 4178 4627 217 -620 306 N ATOM 855 CA VAL A 152 2.241 -23.125 -17.392 1.00 33.73 C ANISOU 855 CA VAL A 152 2074 4966 5777 243 -410 519 C ATOM 856 C VAL A 152 0.777 -22.914 -17.813 1.00 35.94 C ANISOU 856 C VAL A 152 2199 4991 6464 213 -530 702 C ATOM 857 O VAL A 152 -0.025 -23.857 -17.780 1.00 38.34 O ANISOU 857 O VAL A 152 2377 5084 7106 145 -616 874 O ATOM 858 CB VAL A 152 2.477 -22.615 -15.954 1.00 30.68 C ANISOU 858 CB VAL A 152 1675 4754 5228 421 66 551 C ATOM 859 CG1 VAL A 152 1.327 -23.022 -15.047 1.00 37.06 C ANISOU 859 CG1 VAL A 152 2333 5431 6316 497 323 829 C ATOM 860 CG2 VAL A 152 3.815 -23.115 -15.426 1.00 26.26 C ANISOU 860 CG2 VAL A 152 1277 4407 4293 453 162 401 C ATOM 861 N GLU A 153 0.425 -21.692 -18.225 1.00 32.48 N ANISOU 861 N GLU A 153 1757 4538 6046 260 -549 682 N ATOM 862 CA GLU A 153 -0.930 -21.402 -18.679 1.00 37.93 C ANISOU 862 CA GLU A 153 2300 4976 7135 231 -687 852 C ATOM 863 C GLU A 153 -1.252 -22.244 -19.902 1.00 38.42 C ANISOU 863 C GLU A 153 2448 4797 7353 106 -1186 813 C ATOM 864 O GLU A 153 -2.353 -22.772 -20.028 1.00 41.48 O ANISOU 864 O GLU A 153 2673 4897 8190 42 -1327 987 O ATOM 865 CB GLU A 153 -1.111 -19.907 -19.007 1.00 35.01 C ANISOU 865 CB GLU A 153 1944 4642 6718 311 -649 811 C ATOM 866 CG GLU A 153 -2.517 -19.539 -19.515 1.00 38.05 C ANISOU 866 CG GLU A 153 2170 4755 7532 281 -810 987 C ATOM 867 CD GLU A 153 -3.585 -19.717 -18.452 1.00 41.01 C ANISOU 867 CD GLU A 153 2293 5004 8286 324 -477 1273 C ATOM 868 OE1 GLU A 153 -3.229 -19.885 -17.269 1.00 49.72 O ANISOU 868 OE1 GLU A 153 3396 6265 9230 429 -77 1322 O ATOM 869 OE2 GLU A 153 -4.785 -19.681 -18.797 1.00 50.97 O ANISOU 869 OE2 GLU A 153 3373 5984 10008 272 -614 1465 O ATOM 870 N SER A 154 -0.280 -22.369 -20.800 1.00 36.07 N ANISOU 870 N SER A 154 2435 4581 6688 94 -1451 589 N ATOM 871 CA SER A 154 -0.460 -23.194 -21.985 1.00 39.90 C ANISOU 871 CA SER A 154 3126 4834 7200 40 -1915 500 C ATOM 872 C SER A 154 -0.762 -24.654 -21.627 1.00 39.74 C ANISOU 872 C SER A 154 3006 4640 7455 -50 -1978 581 C ATOM 873 O SER A 154 -1.700 -25.245 -22.162 1.00 41.67 O ANISOU 873 O SER A 154 3201 4541 8091 -106 -2292 648 O ATOM 874 CB SER A 154 0.774 -23.110 -22.879 1.00 39.49 C ANISOU 874 CB SER A 154 3470 4917 6617 105 -2075 270 C ATOM 875 OG SER A 154 0.976 -21.785 -23.324 1.00 42.43 O ANISOU 875 OG SER A 154 3936 5379 6805 200 -2057 235 O ATOM 876 N VAL A 155 0.039 -25.243 -20.739 1.00 38.74 N ANISOU 876 N VAL A 155 2848 4714 7159 -58 -1708 576 N ATOM 877 CA VAL A 155 -0.219 -26.630 -20.319 1.00 43.65 C ANISOU 877 CA VAL A 155 3355 5166 8063 -131 -1736 687 C ATOM 878 C VAL A 155 -1.559 -26.737 -19.608 1.00 48.65 C ANISOU 878 C VAL A 155 3630 5560 9295 -155 -1581 1008 C ATOM 879 O VAL A 155 -2.295 -27.712 -19.795 1.00 44.38 O ANISOU 879 O VAL A 155 2973 4673 9217 -233 -1800 1139 O ATOM 880 CB VAL A 155 0.878 -27.173 -19.393 1.00 41.75 C ANISOU 880 CB VAL A 155 3135 5197 7530 -116 -1440 648 C ATOM 881 CG1 VAL A 155 0.579 -28.640 -18.996 1.00 36.68 C ANISOU 881 CG1 VAL A 155 2371 4352 7215 -185 -1478 790 C ATOM 882 CG2 VAL A 155 2.218 -27.071 -20.079 1.00 33.49 C ANISOU 882 CG2 VAL A 155 2429 4348 5949 -94 -1568 370 C ATOM 883 N ASP A 156 -1.866 -25.730 -18.794 1.00 42.17 N ANISOU 883 N ASP A 156 2649 4887 8486 -70 -1194 1147 N ATOM 884 CA ASP A 156 -3.140 -25.648 -18.092 1.00 45.37 C ANISOU 884 CA ASP A 156 2746 5068 9424 -46 -963 1493 C ATOM 885 C ASP A 156 -4.301 -25.779 -19.075 1.00 54.08 C ANISOU 885 C ASP A 156 3741 5743 11063 -148 -1394 1576 C ATOM 886 O ASP A 156 -5.285 -26.469 -18.805 1.00 56.14 O ANISOU 886 O ASP A 156 3748 5650 11931 -198 -1409 1861 O ATOM 887 CB ASP A 156 -3.260 -24.312 -17.357 1.00 51.04 C ANISOU 887 CB ASP A 156 3417 5999 9976 101 -545 1558 C ATOM 888 CG ASP A 156 -2.630 -24.331 -15.977 1.00 53.21 C ANISOU 888 CG ASP A 156 3730 6546 9941 255 -36 1615 C ATOM 889 OD1 ASP A 156 -1.992 -25.337 -15.601 1.00 53.86 O ANISOU 889 OD1 ASP A 156 3865 6695 9902 237 2 1598 O ATOM 890 OD2 ASP A 156 -2.759 -23.310 -15.267 1.00 51.95 O ANISOU 890 OD2 ASP A 156 3586 6521 9631 419 316 1660 O ATOM 891 N LYS A 157 -4.170 -25.124 -20.225 1.00 54.45 N ANISOU 891 N LYS A 157 3992 5791 10906 -161 -1756 1339 N ATOM 892 CA LYS A 157 -5.253 -25.071 -21.201 1.00 60.42 C ANISOU 892 CA LYS A 157 4695 6142 12120 -225 -2198 1379 C ATOM 893 C LYS A 157 -5.118 -26.175 -22.245 1.00 64.80 C ANISOU 893 C LYS A 157 5472 6420 12727 -288 -2748 1191 C ATOM 894 O LYS A 157 -5.571 -26.022 -23.383 1.00 66.40 O ANISOU 894 O LYS A 157 5833 6363 13033 -288 -3224 1060 O ATOM 895 CB LYS A 157 -5.292 -23.702 -21.879 1.00 56.74 C ANISOU 895 CB LYS A 157 4356 5793 11411 -161 -2289 1249 C ATOM 896 CG LYS A 157 -5.616 -22.547 -20.933 1.00 56.00 C ANISOU 896 CG LYS A 157 4045 5884 11347 -79 -1793 1434 C ATOM 897 CD LYS A 157 -6.999 -22.725 -20.319 1.00 57.99 C ANISOU 897 CD LYS A 157 3921 5799 12311 -112 -1639 1808 C ATOM 898 CE LYS A 157 -7.322 -21.631 -19.324 1.00 55.64 C ANISOU 898 CE LYS A 157 3468 5674 11997 18 -1099 1998 C ATOM 899 NZ LYS A 157 -8.697 -21.797 -18.774 1.00 64.72 N ANISOU 899 NZ LYS A 157 4266 6462 13862 11 -920 2413 N ATOM 900 N GLU A 158 -4.497 -27.279 -21.835 1.00 61.44 N ANISOU 900 N GLU A 158 5084 6039 12221 -315 -2681 1172 N ATOM 901 CA GLU A 158 -4.193 -28.407 -22.716 1.00 64.66 C ANISOU 901 CA GLU A 158 5747 6210 12609 -340 -3149 972 C ATOM 902 C GLU A 158 -3.608 -27.957 -24.053 1.00 61.63 C ANISOU 902 C GLU A 158 5825 5893 11698 -245 -3512 632 C ATOM 903 O GLU A 158 -4.009 -28.421 -25.120 1.00 60.88 O ANISOU 903 O GLU A 158 5943 5432 11757 -216 -4032 493 O ATOM 904 CB GLU A 158 -5.424 -29.303 -22.907 1.00 71.55 C ANISOU 904 CB GLU A 158 6387 6490 14309 -424 -3505 1162 C ATOM 905 CG GLU A 158 -5.580 -30.349 -21.813 1.00 76.63 C ANISOU 905 CG GLU A 158 6720 7020 15375 -484 -3229 1450 C ATOM 906 CD GLU A 158 -4.505 -31.422 -21.889 1.00 80.68 C ANISOU 906 CD GLU A 158 7477 7650 15526 -476 -3306 1252 C ATOM 907 OE1 GLU A 158 -4.038 -31.696 -23.016 1.00 84.44 O ANISOU 907 OE1 GLU A 158 8337 8050 15696 -429 -3744 929 O ATOM 908 OE2 GLU A 158 -4.121 -31.990 -20.836 1.00 78.02 O ANISOU 908 OE2 GLU A 158 6975 7471 15196 -489 -2919 1424 O ATOM 909 N MET A 159 -2.656 -27.036 -23.978 1.00 56.51 N ANISOU 909 N MET A 159 5346 5682 10443 -167 -3229 513 N ATOM 910 CA MET A 159 -1.955 -26.573 -25.161 1.00 54.30 C ANISOU 910 CA MET A 159 5523 5495 9616 -38 -3461 248 C ATOM 911 C MET A 159 -0.457 -26.718 -24.923 1.00 50.95 C ANISOU 911 C MET A 159 5323 5444 8593 15 -3183 113 C ATOM 912 O MET A 159 0.284 -25.768 -25.130 1.00 44.53 O ANISOU 912 O MET A 159 4682 4897 7339 104 -3020 36 O ATOM 913 CB MET A 159 -2.289 -25.102 -25.449 1.00 59.00 C ANISOU 913 CB MET A 159 6102 6193 10122 22 -3411 275 C ATOM 914 CG MET A 159 -3.751 -24.817 -25.837 1.00 63.62 C ANISOU 914 CG MET A 159 6498 6395 11280 -20 -3721 393 C ATOM 915 SD MET A 159 -4.101 -23.046 -26.085 1.00 63.69 S ANISOU 915 SD MET A 159 6464 6554 11179 57 -3616 444 S ATOM 916 CE MET A 159 -3.428 -22.361 -24.577 1.00 94.67 C ANISOU 916 CE MET A 159 10104 10929 14939 40 -2927 586 C ATOM 917 N AGLN A 160 -0.048 -27.922 -24.523 0.44 50.52 N ANISOU 917 N AGLN A 160 5256 5361 8578 -38 -3154 102 N ATOM 918 N BGLN A 160 0.001 -27.884 -24.468 0.56 50.50 N ANISOU 918 N BGLN A 160 5247 5384 8558 -39 -3126 105 N ATOM 919 CA AGLN A 160 1.343 -28.259 -24.218 0.44 46.97 C ANISOU 919 CA AGLN A 160 4984 5219 7646 -9 -2904 -9 C ATOM 920 CA BGLN A 160 1.431 -28.035 -24.170 0.56 46.01 C ANISOU 920 CA BGLN A 160 4860 5153 7468 -2 -2852 -8 C ATOM 921 C AGLN A 160 2.271 -27.976 -25.393 0.44 46.25 C ANISOU 921 C AGLN A 160 5386 5194 6993 154 -3020 -223 C ATOM 922 C BGLN A 160 2.287 -27.801 -25.417 0.56 45.70 C ANISOU 922 C BGLN A 160 5322 5148 6894 162 -3003 -222 C ATOM 923 O AGLN A 160 3.465 -27.759 -25.217 0.44 44.19 O ANISOU 923 O AGLN A 160 5272 5211 6308 198 -2752 -286 O ATOM 924 O BGLN A 160 3.445 -27.412 -25.317 0.56 45.15 O ANISOU 924 O BGLN A 160 5411 5357 6388 218 -2741 -284 O ATOM 925 CB AGLN A 160 1.458 -29.744 -23.846 0.44 49.69 C ANISOU 925 CB AGLN A 160 5271 5421 8187 -77 -2964 8 C ATOM 926 CB BGLN A 160 1.761 -29.387 -23.516 0.56 47.28 C ANISOU 926 CB BGLN A 160 4925 5283 7754 -79 -2788 23 C ATOM 927 CG AGLN A 160 0.666 -30.178 -22.613 0.44 50.88 C ANISOU 927 CG AGLN A 160 4955 5491 8887 -204 -2773 274 C ATOM 928 CG BGLN A 160 3.277 -29.700 -23.445 0.56 44.85 C ANISOU 928 CG BGLN A 160 4869 5255 6916 -32 -2590 -124 C ATOM 929 CD AGLN A 160 -0.836 -30.252 -22.862 0.44 52.21 C ANISOU 929 CD AGLN A 160 4898 5230 9709 -255 -3051 438 C ATOM 930 CD BGLN A 160 3.776 -30.037 -22.048 0.56 39.06 C ANISOU 930 CD BGLN A 160 3866 4760 6213 -118 -2230 -20 C ATOM 931 OE1AGLN A 160 -1.302 -30.077 -23.990 0.44 50.54 O ANISOU 931 OE1AGLN A 160 4894 4761 9549 -203 -3462 314 O ATOM 932 OE1BGLN A 160 3.030 -30.545 -21.209 0.56 39.50 O ANISOU 932 OE1BGLN A 160 3599 4709 6701 -196 -2156 168 O ATOM 933 NE2AGLN A 160 -1.600 -30.495 -21.803 0.44 47.31 N ANISOU 933 NE2AGLN A 160 3865 4507 9604 -334 -2814 738 N ATOM 934 NE2BGLN A 160 5.050 -29.757 -21.793 0.56 29.26 N ANISOU 934 NE2BGLN A 160 2769 3811 4536 -85 -1998 -122 N ATOM 935 N VAL A 161 1.705 -28.009 -26.593 1.00 46.39 N ANISOU 935 N VAL A 161 5672 4916 7038 265 -3418 -319 N ATOM 936 CA VAL A 161 2.432 -27.775 -27.839 1.00 46.95 C ANISOU 936 CA VAL A 161 6269 4981 6590 491 -3529 -495 C ATOM 937 C VAL A 161 2.968 -26.341 -27.948 1.00 46.59 C ANISOU 937 C VAL A 161 6308 5211 6183 578 -3262 -462 C ATOM 938 O VAL A 161 3.968 -26.086 -28.617 1.00 47.87 O ANISOU 938 O VAL A 161 6851 5475 5861 762 -3133 -539 O ATOM 939 CB VAL A 161 1.521 -28.112 -29.051 1.00 56.74 C ANISOU 939 CB VAL A 161 7782 5787 7990 626 -4069 -610 C ATOM 940 CG1 VAL A 161 0.130 -27.526 -28.838 1.00 60.79 C ANISOU 940 CG1 VAL A 161 7951 6114 9033 503 -4265 -484 C ATOM 941 CG2 VAL A 161 2.127 -27.637 -30.371 1.00 58.01 C ANISOU 941 CG2 VAL A 161 8517 5934 7591 928 -4149 -763 C ATOM 942 N LEU A 162 2.313 -25.399 -27.280 1.00 43.06 N ANISOU 942 N LEU A 162 5503 4858 6002 467 -3154 -323 N ATOM 943 CA LEU A 162 2.823 -24.026 -27.258 1.00 40.25 C ANISOU 943 CA LEU A 162 5185 4739 5369 547 -2913 -280 C ATOM 944 C LEU A 162 4.132 -23.831 -26.493 1.00 36.10 C ANISOU 944 C LEU A 162 4634 4520 4562 529 -2519 -282 C ATOM 945 O LEU A 162 4.880 -22.883 -26.771 1.00 36.72 O ANISOU 945 O LEU A 162 4898 4732 4320 663 -2352 -283 O ATOM 946 CB LEU A 162 1.768 -23.062 -26.714 1.00 40.68 C ANISOU 946 CB LEU A 162 4850 4787 5821 457 -2897 -133 C ATOM 947 CG LEU A 162 0.722 -22.662 -27.753 1.00 49.00 C ANISOU 947 CG LEU A 162 6034 5569 7013 543 -3268 -140 C ATOM 948 CD1 LEU A 162 -0.185 -21.612 -27.165 1.00 47.66 C ANISOU 948 CD1 LEU A 162 5469 5419 7221 464 -3171 26 C ATOM 949 CD2 LEU A 162 1.394 -22.145 -29.019 1.00 48.43 C ANISOU 949 CD2 LEU A 162 6498 5503 6401 797 -3350 -244 C ATOM 950 N VAL A 163 4.404 -24.709 -25.532 1.00 36.39 N ANISOU 950 N VAL A 163 4450 4639 4736 384 -2380 -275 N ATOM 951 CA VAL A 163 5.574 -24.533 -24.655 1.00 34.68 C ANISOU 951 CA VAL A 163 4165 4689 4321 351 -2041 -297 C ATOM 952 C VAL A 163 6.896 -24.432 -25.424 1.00 35.51 C ANISOU 952 C VAL A 163 4698 4858 3935 521 -1914 -392 C ATOM 953 O VAL A 163 7.724 -23.553 -25.164 1.00 32.40 O ANISOU 953 O VAL A 163 4325 4634 3352 591 -1654 -400 O ATOM 954 CB VAL A 163 5.641 -25.652 -23.597 1.00 35.00 C ANISOU 954 CB VAL A 163 3958 4781 4559 200 -1936 -272 C ATOM 955 CG1 VAL A 163 6.902 -25.549 -22.773 1.00 28.88 C ANISOU 955 CG1 VAL A 163 3165 4247 3562 188 -1634 -338 C ATOM 956 CG2 VAL A 163 4.414 -25.594 -22.693 1.00 31.31 C ANISOU 956 CG2 VAL A 163 3056 4265 4575 93 -1910 -114 C ATOM 957 N SER A 164 7.099 -25.327 -26.384 1.00 35.70 N ANISOU 957 N SER A 164 5054 4723 3788 622 -2047 -453 N ATOM 958 CA SER A 164 8.320 -25.275 -27.181 1.00 40.65 C ANISOU 958 CA SER A 164 6085 5375 3985 834 -1846 -488 C ATOM 959 C SER A 164 8.387 -24.006 -28.031 1.00 36.69 C ANISOU 959 C SER A 164 5838 4862 3241 1059 -1774 -424 C ATOM 960 O SER A 164 9.464 -23.493 -28.313 1.00 35.53 O ANISOU 960 O SER A 164 5897 4800 2804 1231 -1439 -363 O ATOM 961 CB SER A 164 8.449 -26.505 -28.078 1.00 44.86 C ANISOU 961 CB SER A 164 6927 5707 4410 955 -2011 -572 C ATOM 962 OG SER A 164 7.423 -26.528 -29.053 1.00 51.32 O ANISOU 962 OG SER A 164 7939 6278 5283 1075 -2380 -619 O ATOM 963 N ARG A 165 7.237 -23.505 -28.459 1.00 34.14 N ANISOU 963 N ARG A 165 5492 4413 3066 1076 -2057 -404 N ATOM 964 CA ARG A 165 7.228 -22.263 -29.212 1.00 39.57 C ANISOU 964 CA ARG A 165 6406 5090 3538 1294 -1987 -315 C ATOM 965 C ARG A 165 7.594 -21.067 -28.322 1.00 37.76 C ANISOU 965 C ARG A 165 5912 5072 3362 1250 -1704 -208 C ATOM 966 O ARG A 165 8.381 -20.202 -28.715 1.00 36.25 O ANISOU 966 O ARG A 165 5867 4910 2996 1399 -1307 -88 O ATOM 967 CB ARG A 165 5.870 -22.060 -29.890 1.00 44.39 C ANISOU 967 CB ARG A 165 7046 5492 4328 1318 -2391 -333 C ATOM 968 CG ARG A 165 5.519 -23.188 -30.868 1.00 55.19 C ANISOU 968 CG ARG A 165 8733 6599 5639 1432 -2712 -478 C ATOM 969 CD ARG A 165 6.737 -23.594 -31.704 1.00 61.62 C ANISOU 969 CD ARG A 165 10024 7397 5991 1717 -2473 -515 C ATOM 970 NE ARG A 165 7.278 -22.463 -32.456 1.00 67.81 N ANISOU 970 NE ARG A 165 11117 8227 6420 2004 -2188 -394 N ATOM 971 CZ ARG A 165 8.520 -22.395 -32.927 1.00 69.86 C ANISOU 971 CZ ARG A 165 11671 8533 6342 2255 -1765 -310 C ATOM 972 NH1 ARG A 165 9.371 -23.393 -32.725 1.00 68.66 N ANISOU 972 NH1 ARG A 165 11545 8398 6146 2244 -1615 -357 N ATOM 973 NH2 ARG A 165 8.913 -21.319 -33.596 1.00 72.37 N ANISOU 973 NH2 ARG A 165 12225 8862 6413 2525 -1457 -146 N ATOM 974 N ILE A 166 7.026 -21.027 -27.124 1.00 31.72 N ANISOU 974 N ILE A 166 4643 4381 3029 964 -1694 -226 N ATOM 975 CA ILE A 166 7.343 -19.961 -26.173 1.00 32.42 C ANISOU 975 CA ILE A 166 4383 4594 3340 826 -1264 -168 C ATOM 976 C ILE A 166 8.839 -19.959 -25.831 1.00 31.75 C ANISOU 976 C ILE A 166 4330 4610 3124 821 -836 -180 C ATOM 977 O ILE A 166 9.485 -18.904 -25.776 1.00 26.70 O ANISOU 977 O ILE A 166 3627 3974 2544 852 -503 -105 O ATOM 978 CB ILE A 166 6.470 -20.076 -24.912 1.00 34.08 C ANISOU 978 CB ILE A 166 4132 4858 3959 603 -1312 -182 C ATOM 979 CG1 ILE A 166 4.990 -19.895 -25.297 1.00 35.10 C ANISOU 979 CG1 ILE A 166 4149 4838 4350 615 -1697 -110 C ATOM 980 CG2 ILE A 166 6.923 -19.086 -23.832 1.00 28.39 C ANISOU 980 CG2 ILE A 166 3145 4254 3385 518 -902 -183 C ATOM 981 CD1 ILE A 166 3.998 -20.300 -24.212 1.00 33.53 C ANISOU 981 CD1 ILE A 166 3497 4633 4609 447 -1752 -51 C ATOM 982 N ALA A 167 9.405 -21.146 -25.654 1.00 28.41 N ANISOU 982 N ALA A 167 3987 4229 2578 790 -870 -262 N ATOM 983 CA ALA A 167 10.840 -21.267 -25.409 1.00 30.84 C ANISOU 983 CA ALA A 167 4316 4597 2805 799 -507 -260 C ATOM 984 C ALA A 167 11.640 -20.641 -26.558 1.00 32.99 C ANISOU 984 C ALA A 167 4901 4778 2857 1058 -238 -106 C ATOM 985 O ALA A 167 12.623 -19.927 -26.337 1.00 31.19 O ANISOU 985 O ALA A 167 4528 4536 2787 1055 142 -12 O ATOM 986 CB ALA A 167 11.224 -22.723 -25.219 1.00 27.76 C ANISOU 986 CB ALA A 167 4013 4243 2293 762 -625 -357 C ATOM 987 N ALA A 168 11.194 -20.898 -27.779 1.00 37.45 N ANISOU 987 N ALA A 168 5897 5246 3087 1311 -449 -66 N ATOM 988 CA ALA A 168 11.834 -20.333 -28.959 1.00 42.83 C ANISOU 988 CA ALA A 168 6960 5831 3481 1650 -159 129 C ATOM 989 C ALA A 168 11.717 -18.807 -28.985 1.00 41.64 C ANISOU 989 C ALA A 168 6618 5638 3564 1651 85 296 C ATOM 990 O ALA A 168 12.697 -18.105 -29.245 1.00 39.46 O ANISOU 990 O ALA A 168 6322 5300 3370 1771 551 502 O ATOM 991 CB ALA A 168 11.242 -20.938 -30.221 1.00 46.81 C ANISOU 991 CB ALA A 168 7998 6206 3583 1944 -509 88 C ATOM 992 N TRP A 169 10.517 -18.300 -28.713 1.00 38.19 N ANISOU 992 N TRP A 169 6007 5205 3298 1523 -221 230 N ATOM 993 CA TRP A 169 10.291 -16.857 -28.688 1.00 39.44 C ANISOU 993 CA TRP A 169 5974 5312 3700 1514 -35 365 C ATOM 994 C TRP A 169 11.190 -16.176 -27.653 1.00 35.94 C ANISOU 994 C TRP A 169 5095 4888 3672 1307 339 378 C ATOM 995 O TRP A 169 11.742 -15.098 -27.913 1.00 33.14 O ANISOU 995 O TRP A 169 4663 4423 3504 1388 669 563 O ATOM 996 CB TRP A 169 8.825 -16.544 -28.391 1.00 33.53 C ANISOU 996 CB TRP A 169 5049 4564 3127 1387 -430 278 C ATOM 997 CG TRP A 169 7.846 -17.189 -29.330 1.00 35.56 C ANISOU 997 CG TRP A 169 5667 4737 3106 1564 -931 237 C ATOM 998 CD1 TRP A 169 8.097 -17.661 -30.584 1.00 45.53 C ANISOU 998 CD1 TRP A 169 7503 5910 3887 1911 -1045 282 C ATOM 999 CD2 TRP A 169 6.456 -17.439 -29.077 1.00 37.60 C ANISOU 999 CD2 TRP A 169 5743 4950 3592 1434 -1423 143 C ATOM 1000 NE1 TRP A 169 6.948 -18.187 -31.131 1.00 51.38 N ANISOU 1000 NE1 TRP A 169 8417 6529 4576 1959 -1627 160 N ATOM 1001 CE2 TRP A 169 5.927 -18.062 -30.225 1.00 44.16 C ANISOU 1001 CE2 TRP A 169 7034 5636 4110 1685 -1906 104 C ATOM 1002 CE3 TRP A 169 5.606 -17.188 -27.994 1.00 34.65 C ANISOU 1002 CE3 TRP A 169 4867 4617 3680 1165 -1492 106 C ATOM 1003 CZ2 TRP A 169 4.594 -18.442 -30.318 1.00 46.77 C ANISOU 1003 CZ2 TRP A 169 7203 5821 4747 1542 -2372 13 C ATOM 1004 CZ3 TRP A 169 4.293 -17.583 -28.082 1.00 37.62 C ANISOU 1004 CZ3 TRP A 169 5131 4880 4285 1121 -1986 81 C ATOM 1005 CH2 TRP A 169 3.795 -18.199 -29.236 1.00 43.68 C ANISOU 1005 CH2 TRP A 169 6278 5471 4849 1299 -2467 38 C ATOM 1006 N MET A 170 11.335 -16.806 -26.484 1.00 29.10 N ANISOU 1006 N MET A 170 3954 4129 2973 1061 256 186 N ATOM 1007 CA MET A 170 12.191 -16.290 -25.412 1.00 27.37 C ANISOU 1007 CA MET A 170 3371 3902 3125 889 483 132 C ATOM 1008 C MET A 170 13.661 -16.270 -25.807 1.00 31.82 C ANISOU 1008 C MET A 170 3962 4359 3769 991 847 288 C ATOM 1009 O MET A 170 14.353 -15.269 -25.619 1.00 32.59 O ANISOU 1009 O MET A 170 3821 4311 4251 970 1089 391 O ATOM 1010 CB MET A 170 12.013 -17.093 -24.102 1.00 23.57 C ANISOU 1010 CB MET A 170 2683 3561 2712 677 296 -99 C ATOM 1011 CG MET A 170 10.675 -16.838 -23.389 1.00 22.84 C ANISOU 1011 CG MET A 170 2427 3535 2715 579 72 -196 C ATOM 1012 SD MET A 170 10.413 -17.983 -22.011 1.00 22.54 S ANISOU 1012 SD MET A 170 2230 3656 2680 429 -67 -372 S ATOM 1013 CE MET A 170 11.460 -17.203 -20.769 1.00 24.42 C ANISOU 1013 CE MET A 170 2259 3869 3150 375 109 -512 C ATOM 1014 N ALA A 171 14.142 -17.385 -26.340 1.00 30.55 N ANISOU 1014 N ALA A 171 4066 4237 3305 1110 883 317 N ATOM 1015 CA ALA A 171 15.525 -17.463 -26.784 1.00 34.30 C ANISOU 1015 CA ALA A 171 4568 4597 3869 1250 1285 517 C ATOM 1016 C ALA A 171 15.784 -16.464 -27.910 1.00 36.96 C ANISOU 1016 C ALA A 171 5057 4761 4225 1527 1649 852 C ATOM 1017 O ALA A 171 16.840 -15.847 -27.950 1.00 39.19 O ANISOU 1017 O ALA A 171 5110 4870 4912 1566 2042 1077 O ATOM 1018 CB ALA A 171 15.878 -18.889 -27.225 1.00 33.89 C ANISOU 1018 CB ALA A 171 4839 4615 3422 1381 1260 487 C ATOM 1019 N THR A 172 14.815 -16.312 -28.814 1.00 35.61 N ANISOU 1019 N THR A 172 5260 4611 3661 1732 1504 906 N ATOM 1020 CA THR A 172 14.908 -15.350 -29.921 1.00 39.85 C ANISOU 1020 CA THR A 172 6012 4994 4134 2049 1835 1242 C ATOM 1021 C THR A 172 14.956 -13.914 -29.392 1.00 41.82 C ANISOU 1021 C THR A 172 5803 5113 4972 1875 1981 1333 C ATOM 1022 O THR A 172 15.784 -13.116 -29.830 1.00 48.27 O ANISOU 1022 O THR A 172 6507 5730 6102 2022 2442 1663 O ATOM 1023 CB THR A 172 13.710 -15.492 -30.902 1.00 54.75 C ANISOU 1023 CB THR A 172 8418 6923 5462 2304 1506 1218 C ATOM 1024 OG1 THR A 172 13.808 -16.732 -31.614 1.00 56.68 O ANISOU 1024 OG1 THR A 172 9179 7207 5149 2567 1387 1165 O ATOM 1025 CG2 THR A 172 13.676 -14.349 -31.904 1.00 58.10 C ANISOU 1025 CG2 THR A 172 9047 7197 5832 2626 1818 1562 C ATOM 1026 N ATYR A 173 14.079 -13.599 -28.444 0.43 40.68 N ANISOU 1026 N ATYR A 173 5390 5055 5011 1585 1607 1060 N ATOM 1027 N BTYR A 173 14.068 -13.581 -28.457 0.57 40.89 N ANISOU 1027 N BTYR A 173 5418 5080 5037 1588 1608 1063 N ATOM 1028 CA ATYR A 173 14.039 -12.261 -27.858 0.43 40.36 C ANISOU 1028 CA ATYR A 173 4950 4879 5505 1431 1672 1081 C ATOM 1029 CA BTYR A 173 14.083 -12.239 -27.869 0.57 40.74 C ANISOU 1029 CA BTYR A 173 4993 4919 5567 1434 1688 1091 C ATOM 1030 C ATYR A 173 15.276 -12.004 -26.995 0.43 39.73 C ANISOU 1030 C ATYR A 173 4438 4649 6007 1253 1854 1064 C ATOM 1031 C BTYR A 173 15.364 -12.022 -27.085 0.57 39.39 C ANISOU 1031 C BTYR A 173 4410 4596 5961 1275 1892 1094 C ATOM 1032 O ATYR A 173 15.739 -10.870 -26.880 0.43 43.17 O ANISOU 1032 O ATYR A 173 4573 4849 6979 1225 2041 1207 O ATOM 1033 O BTYR A 173 15.927 -10.930 -27.087 0.57 43.77 O ANISOU 1033 O BTYR A 173 4681 4904 7047 1273 2128 1279 O ATOM 1034 CB ATYR A 173 12.760 -12.048 -27.041 0.43 36.27 C ANISOU 1034 CB ATYR A 173 4302 4485 4993 1227 1253 796 C ATOM 1035 CB BTYR A 173 12.893 -11.975 -26.943 0.57 36.65 C ANISOU 1035 CB BTYR A 173 4303 4517 5107 1209 1280 795 C ATOM 1036 CG ATYR A 173 12.466 -10.583 -26.771 0.43 37.77 C ANISOU 1036 CG ATYR A 173 4226 4520 5604 1174 1307 845 C ATOM 1037 CG BTYR A 173 12.896 -10.543 -26.416 0.57 38.69 C ANISOU 1037 CG BTYR A 173 4213 4598 5891 1109 1353 810 C ATOM 1038 CD1ATYR A 173 13.001 -9.941 -25.660 0.43 36.09 C ANISOU 1038 CD1ATYR A 173 3618 4187 5906 979 1307 697 C ATOM 1039 CD1BTYR A 173 12.342 -9.514 -27.161 0.57 40.50 C ANISOU 1039 CD1BTYR A 173 4510 4714 6163 1253 1447 1016 C ATOM 1040 CD2ATYR A 173 11.670 -9.841 -27.637 0.43 40.59 C ANISOU 1040 CD2ATYR A 173 4755 4823 5846 1344 1318 1026 C ATOM 1041 CD2BTYR A 173 13.494 -10.218 -25.196 0.57 36.51 C ANISOU 1041 CD2BTYR A 173 3570 4236 6067 902 1297 610 C ATOM 1042 CE1ATYR A 173 12.754 -8.609 -25.417 0.43 38.06 C ANISOU 1042 CE1ATYR A 173 3646 4257 6557 948 1325 717 C ATOM 1043 CE1BTYR A 173 12.355 -8.207 -26.704 0.57 40.64 C ANISOU 1043 CE1BTYR A 173 4212 4540 6690 1169 1503 1028 C ATOM 1044 CE2ATYR A 173 11.412 -8.501 -27.397 0.43 40.27 C ANISOU 1044 CE2ATYR A 173 4465 4624 6212 1299 1375 1077 C ATOM 1045 CE2BTYR A 173 13.518 -8.916 -24.734 0.57 37.21 C ANISOU 1045 CE2BTYR A 173 3377 4114 6647 839 1303 589 C ATOM 1046 CZ ATYR A 173 11.959 -7.894 -26.284 0.43 39.12 C ANISOU 1046 CZ ATYR A 173 3924 4352 6589 1098 1382 917 C ATOM 1047 CZ BTYR A 173 12.946 -7.911 -25.493 0.57 38.68 C ANISOU 1047 CZ BTYR A 173 3608 4189 6899 962 1421 803 C ATOM 1048 OH ATYR A 173 11.719 -6.569 -26.032 0.43 40.25 O ANISOU 1048 OH ATYR A 173 3837 4301 7154 1068 1403 939 O ATOM 1049 OH BTYR A 173 12.954 -6.602 -25.057 0.57 37.87 O ANISOU 1049 OH BTYR A 173 3226 3850 7315 906 1416 781 O ATOM 1050 N LEU A 174 15.802 -13.064 -26.389 1.00 38.06 N ANISOU 1050 N LEU A 174 4188 4544 5731 1137 1755 887 N ATOM 1051 CA LEU A 174 17.025 -12.979 -25.595 1.00 34.79 C ANISOU 1051 CA LEU A 174 3389 3969 5862 989 1850 855 C ATOM 1052 C LEU A 174 18.218 -12.655 -26.504 1.00 46.79 C ANISOU 1052 C LEU A 174 4839 5230 7708 1190 2367 1283 C ATOM 1053 O LEU A 174 19.047 -11.790 -26.192 1.00 47.51 O ANISOU 1053 O LEU A 174 4622 5022 8406 1046 2396 1382 O ATOM 1054 CB LEU A 174 17.262 -14.305 -24.881 1.00 42.13 C ANISOU 1054 CB LEU A 174 4358 5085 6566 867 1636 604 C ATOM 1055 CG LEU A 174 17.491 -14.312 -23.375 1.00 46.62 C ANISOU 1055 CG LEU A 174 4618 5655 7442 623 1324 275 C ATOM 1056 CD1 LEU A 174 17.444 -15.742 -22.870 1.00 46.15 C ANISOU 1056 CD1 LEU A 174 4703 5829 7004 560 1136 77 C ATOM 1057 CD2 LEU A 174 18.817 -13.683 -23.041 1.00 43.04 C ANISOU 1057 CD2 LEU A 174 3775 4884 7693 568 1449 366 C ATOM 1058 N ASN A 175 18.279 -13.341 -27.642 1.00 47.63 N ANISOU 1058 N ASN A 175 5366 5414 7319 1479 2634 1517 N ATOM 1059 CA ASN A 175 19.391 -13.172 -28.578 1.00 54.31 C ANISOU 1059 CA ASN A 175 6317 6000 8318 1662 3031 1941 C ATOM 1060 C ASN A 175 19.428 -11.818 -29.276 1.00 61.41 C ANISOU 1060 C ASN A 175 7168 6634 9530 1797 3315 2306 C ATOM 1061 O ASN A 175 20.502 -11.265 -29.514 1.00 68.87 O ANISOU 1061 O ASN A 175 7928 7236 11002 1810 3574 2627 O ATOM 1062 CB ASN A 175 19.363 -14.273 -29.639 1.00 61.58 C ANISOU 1062 CB ASN A 175 7803 7051 8543 2009 3178 2061 C ATOM 1063 CG ASN A 175 19.811 -15.610 -29.100 1.00 62.65 C ANISOU 1063 CG ASN A 175 7953 7326 8524 1887 3003 1827 C ATOM 1064 OD1 ASN A 175 20.608 -15.677 -28.169 1.00 60.72 O ANISOU 1064 OD1 ASN A 175 7303 6994 8774 1613 2922 1726 O ATOM 1065 ND2 ASN A 175 19.301 -16.688 -29.685 1.00 67.25 N ANISOU 1065 ND2 ASN A 175 9028 8099 8425 2100 2887 1722 N ATOM 1066 N AASP A 176 18.251 -11.289 -29.599 0.36 59.34 N ANISOU 1066 N AASP A 176 7063 6501 8980 1918 3265 2275 N ATOM 1067 N BASP A 176 18.258 -11.282 -29.601 0.64 59.33 N ANISOU 1067 N BASP A 176 7061 6498 8984 1918 3267 2278 N ATOM 1068 CA AASP A 176 18.147 -10.097 -30.433 0.36 62.02 C ANISOU 1068 CA AASP A 176 7452 6625 9487 2118 3566 2656 C ATOM 1069 CA BASP A 176 18.190 -10.122 -30.475 0.64 62.23 C ANISOU 1069 CA BASP A 176 7493 6646 9507 2131 3582 2672 C ATOM 1070 C AASP A 176 17.998 -8.800 -29.643 0.36 59.89 C ANISOU 1070 C AASP A 176 6692 6170 9895 1812 3412 2569 C ATOM 1071 C BASP A 176 17.849 -8.818 -29.753 0.64 60.22 C ANISOU 1071 C BASP A 176 6789 6242 9851 1854 3421 2576 C ATOM 1072 O AASP A 176 18.497 -7.754 -30.061 0.36 64.06 O ANISOU 1072 O AASP A 176 7074 6381 10884 1840 3686 2925 O ATOM 1073 O BASP A 176 17.966 -7.733 -30.334 0.64 63.65 O ANISOU 1073 O BASP A 176 7170 6439 10577 1947 3692 2923 O ATOM 1074 CB AASP A 176 16.973 -10.228 -31.409 0.36 63.80 C ANISOU 1074 CB AASP A 176 8215 7065 8961 2508 3603 2709 C ATOM 1075 CB BASP A 176 17.190 -10.374 -31.609 0.64 65.23 C ANISOU 1075 CB BASP A 176 8473 7219 9091 2572 3667 2773 C ATOM 1076 CG AASP A 176 17.071 -11.463 -32.279 0.36 67.91 C ANISOU 1076 CG AASP A 176 9323 7720 8761 2845 3604 2701 C ATOM 1077 CG BASP A 176 17.513 -11.629 -32.410 0.64 69.51 C ANISOU 1077 CG BASP A 176 9524 7860 9026 2899 3692 2756 C ATOM 1078 OD1AASP A 176 18.170 -12.052 -32.366 0.36 71.18 O ANISOU 1078 OD1AASP A 176 9698 8009 9339 2893 3757 2784 O ATOM 1079 OD1BASP A 176 18.606 -12.208 -32.220 0.64 72.43 O ANISOU 1079 OD1BASP A 176 9766 8111 9642 2839 3797 2810 O ATOM 1080 OD2AASP A 176 16.046 -11.840 -32.886 0.36 69.25 O ANISOU 1080 OD2AASP A 176 9993 8076 8244 3036 3332 2563 O ATOM 1081 OD2BASP A 176 16.674 -12.031 -33.245 0.64 70.79 O ANISOU 1081 OD2BASP A 176 10217 8196 8485 3181 3525 2641 O ATOM 1082 N AHIS A 177 17.305 -8.862 -28.511 0.36 53.62 N ANISOU 1082 N AHIS A 177 5675 5537 9162 1553 2964 2107 N ATOM 1083 N BHIS A 177 17.414 -8.910 -28.500 0.64 53.87 N ANISOU 1083 N BHIS A 177 5700 5558 9212 1545 2974 2115 N ATOM 1084 CA AHIS A 177 16.953 -7.645 -27.785 0.36 51.17 C ANISOU 1084 CA AHIS A 177 5017 5061 9364 1332 2741 1962 C ATOM 1085 CA BHIS A 177 16.943 -7.714 -27.800 0.64 50.55 C ANISOU 1085 CA BHIS A 177 4955 4998 9255 1340 2742 1958 C ATOM 1086 C AHIS A 177 17.577 -7.498 -26.389 0.36 49.36 C ANISOU 1086 C AHIS A 177 4404 4688 9662 982 2386 1620 C ATOM 1087 C BHIS A 177 17.347 -7.600 -26.321 0.64 48.47 C ANISOU 1087 C BHIS A 177 4321 4642 9453 988 2337 1560 C ATOM 1088 O AHIS A 177 17.605 -6.394 -25.846 0.36 51.00 O ANISOU 1088 O AHIS A 177 4352 4652 10375 828 2228 1539 O ATOM 1089 O BHIS A 177 17.000 -6.620 -25.659 0.64 49.20 O ANISOU 1089 O BHIS A 177 4199 4595 9898 845 2105 1385 O ATOM 1090 CB AHIS A 177 15.424 -7.492 -27.699 0.36 49.10 C ANISOU 1090 CB AHIS A 177 4929 5032 8697 1376 2455 1737 C ATOM 1091 CB BHIS A 177 15.420 -7.565 -27.958 0.64 50.14 C ANISOU 1091 CB BHIS A 177 5138 5175 8738 1437 2518 1804 C ATOM 1092 CG AHIS A 177 14.790 -6.964 -28.953 0.36 53.40 C ANISOU 1092 CG AHIS A 177 5800 5562 8928 1672 2674 2067 C ATOM 1093 CG BHIS A 177 14.980 -7.306 -29.369 0.64 56.49 C ANISOU 1093 CG BHIS A 177 6344 5981 9138 1787 2798 2177 C ATOM 1094 ND1AHIS A 177 15.148 -7.398 -30.212 0.36 57.39 N ANISOU 1094 ND1AHIS A 177 6701 6073 9033 2030 3056 2438 N ATOM 1095 ND1BHIS A 177 15.063 -8.260 -30.363 0.64 60.50 N ANISOU 1095 ND1BHIS A 177 7344 6628 9014 2086 2964 2346 N ATOM 1096 CD2AHIS A 177 13.818 -6.042 -29.137 0.36 53.91 C ANISOU 1096 CD2AHIS A 177 5893 5599 8991 1703 2556 2083 C ATOM 1097 CD2BHIS A 177 14.469 -6.201 -29.955 0.64 56.04 C ANISOU 1097 CD2BHIS A 177 6316 5788 9190 1929 2923 2408 C ATOM 1098 CE1AHIS A 177 14.422 -6.766 -31.117 0.36 56.52 C ANISOU 1098 CE1AHIS A 177 6876 5940 8660 2281 3135 2661 C ATOM 1099 CE1BHIS A 177 14.628 -7.750 -31.498 0.64 56.93 C ANISOU 1099 CE1BHIS A 177 7243 6126 8264 2423 3166 2659 C ATOM 1100 NE2AHIS A 177 13.609 -5.935 -30.492 0.36 55.93 N ANISOU 1100 NE2AHIS A 177 6557 5844 8850 2067 2832 2456 N ATOM 1101 NE2BHIS A 177 14.249 -6.505 -31.277 0.64 56.32 N ANISOU 1101 NE2BHIS A 177 6877 5890 8632 2323 3152 2714 N ATOM 1102 N LEU A 178 18.079 -8.589 -25.812 1.00 47.36 N ANISOU 1102 N LEU A 178 4152 4564 9277 890 2240 1413 N ATOM 1103 CA ALEU A 178 18.559 -8.553 -24.427 0.63 46.60 C ANISOU 1103 CA ALEU A 178 3780 4365 9562 630 1842 1045 C ATOM 1104 CA BLEU A 178 18.546 -8.587 -24.419 0.37 46.66 C ANISOU 1104 CA BLEU A 178 3793 4382 9555 630 1839 1039 C ATOM 1105 C LEU A 178 20.044 -8.859 -24.310 1.00 49.85 C ANISOU 1105 C LEU A 178 4038 4511 10393 550 1916 1175 C ATOM 1106 O LEU A 178 20.735 -8.285 -23.463 1.00 51.30 O ANISOU 1106 O LEU A 178 3951 4380 11160 382 1660 1028 O ATOM 1107 CB ALEU A 178 17.760 -9.513 -23.528 0.63 42.73 C ANISOU 1107 CB ALEU A 178 3387 4238 8610 578 1510 624 C ATOM 1108 CB BLEU A 178 17.798 -9.635 -23.584 0.37 42.84 C ANISOU 1108 CB BLEU A 178 3419 4270 8588 587 1530 637 C ATOM 1109 CG ALEU A 178 16.251 -9.300 -23.432 0.63 34.59 C ANISOU 1109 CG ALEU A 178 2506 3439 7198 628 1359 459 C ATOM 1110 CG BLEU A 178 16.513 -9.238 -22.862 0.37 38.87 C ANISOU 1110 CG BLEU A 178 2927 3923 7919 556 1234 325 C ATOM 1111 CD1ALEU A 178 15.599 -10.338 -22.510 0.63 31.38 C ANISOU 1111 CD1ALEU A 178 2267 3349 6307 536 1029 103 C ATOM 1112 CD1BLEU A 178 15.983 -10.401 -22.030 0.37 35.23 C ANISOU 1112 CD1BLEU A 178 2658 3789 6940 484 948 2 C ATOM 1113 CD2ALEU A 178 15.917 -7.890 -22.951 0.63 36.94 C ANISOU 1113 CD2ALEU A 178 2593 3507 7934 576 1217 364 C ATOM 1114 CD2BLEU A 178 16.732 -8.017 -21.983 0.37 36.37 C ANISOU 1114 CD2BLEU A 178 2376 3309 8135 438 982 139 C ATOM 1115 N GLU A 179 20.534 -9.769 -25.146 1.00 43.37 N ANISOU 1115 N GLU A 179 3411 3780 9288 700 2238 1442 N ATOM 1116 CA GLU A 179 21.943 -10.105 -25.135 1.00 55.89 C ANISOU 1116 CA GLU A 179 4859 5093 11282 664 2353 1618 C ATOM 1117 C GLU A 179 22.877 -8.889 -25.288 1.00 50.80 C ANISOU 1117 C GLU A 179 3923 3897 11482 622 2484 1920 C ATOM 1118 O GLU A 179 23.845 -8.786 -24.537 1.00 52.62 O ANISOU 1118 O GLU A 179 3884 3811 12297 477 2264 1823 O ATOM 1119 CB GLU A 179 22.274 -11.179 -26.166 1.00 54.03 C ANISOU 1119 CB GLU A 179 4934 5008 10587 902 2733 1906 C ATOM 1120 CG GLU A 179 23.690 -11.664 -26.003 1.00 54.39 C ANISOU 1120 CG GLU A 179 4821 4794 11049 863 2808 2043 C ATOM 1121 CD GLU A 179 24.044 -12.813 -26.906 1.00 58.52 C ANISOU 1121 CD GLU A 179 5673 5461 11100 1113 3140 2275 C ATOM 1122 OE1 GLU A 179 23.148 -13.606 -27.277 1.00 55.53 O ANISOU 1122 OE1 GLU A 179 5655 5464 9979 1247 3132 2144 O ATOM 1123 OE2 GLU A 179 25.243 -12.916 -27.228 1.00 61.93 O ANISOU 1123 OE2 GLU A 179 6008 5578 11945 1198 3387 2587 O ATOM 1124 N PRO A 180 22.582 -7.974 -26.237 1.00 53.31 N ANISOU 1124 N PRO A 180 4297 4065 11895 773 2820 2288 N ATOM 1125 CA PRO A 180 23.474 -6.811 -26.349 1.00 58.42 C ANISOU 1125 CA PRO A 180 4620 4335 13243 743 2876 2482 C ATOM 1126 C PRO A 180 23.619 -6.076 -25.021 1.00 59.58 C ANISOU 1126 C PRO A 180 4434 4250 13955 474 2340 2079 C ATOM 1127 O PRO A 180 24.746 -5.779 -24.643 1.00 62.27 O ANISOU 1127 O PRO A 180 4494 4319 14849 415 2203 2078 O ATOM 1128 CB PRO A 180 22.779 -5.930 -27.390 1.00 62.12 C ANISOU 1128 CB PRO A 180 5218 4858 13527 929 3198 2775 C ATOM 1129 CG PRO A 180 21.959 -6.872 -28.197 1.00 57.41 C ANISOU 1129 CG PRO A 180 5086 4614 12113 1173 3454 2893 C ATOM 1130 CD PRO A 180 21.501 -7.922 -27.242 1.00 56.17 C ANISOU 1130 CD PRO A 180 4997 4713 11632 1007 3091 2463 C ATOM 1131 N TRP A 181 22.515 -5.831 -24.311 1.00 55.21 N ANISOU 1131 N TRP A 181 3933 3799 13245 355 2023 1726 N ATOM 1132 CA TRP A 181 22.580 -5.111 -23.038 1.00 56.10 C ANISOU 1132 CA TRP A 181 3813 3723 13780 180 1474 1288 C ATOM 1133 C TRP A 181 23.320 -5.904 -21.971 1.00 55.32 C ANISOU 1133 C TRP A 181 3651 3586 13782 98 1088 955 C ATOM 1134 O TRP A 181 24.052 -5.347 -21.163 1.00 58.44 O ANISOU 1134 O TRP A 181 3824 3737 14643 47 712 751 O ATOM 1135 CB TRP A 181 21.175 -4.755 -22.520 1.00 52.59 C ANISOU 1135 CB TRP A 181 3482 3451 13048 128 1232 956 C ATOM 1136 CG TRP A 181 21.196 -4.017 -21.206 1.00 53.77 C ANISOU 1136 CG TRP A 181 3469 3425 13537 26 660 480 C ATOM 1137 CD1 TRP A 181 21.184 -2.661 -21.038 1.00 57.10 C ANISOU 1137 CD1 TRP A 181 3701 3625 14368 3 503 445 C ATOM 1138 CD2 TRP A 181 21.260 -4.580 -19.883 1.00 52.30 C ANISOU 1138 CD2 TRP A 181 3333 3309 13230 -4 156 -25 C ATOM 1139 NE1 TRP A 181 21.220 -2.346 -19.704 1.00 57.88 N ANISOU 1139 NE1 TRP A 181 3753 3652 14588 -22 -73 -50 N ATOM 1140 CE2 TRP A 181 21.259 -3.501 -18.973 1.00 55.06 C ANISOU 1140 CE2 TRP A 181 3559 3486 13876 -1 -291 -340 C ATOM 1141 CE3 TRP A 181 21.293 -5.884 -19.380 1.00 49.23 C ANISOU 1141 CE3 TRP A 181 3106 3189 12412 9 40 -236 C ATOM 1142 CZ2 TRP A 181 21.304 -3.687 -17.598 1.00 59.71 C ANISOU 1142 CZ2 TRP A 181 4223 4121 14342 68 -839 -834 C ATOM 1143 CZ3 TRP A 181 21.340 -6.066 -18.012 1.00 49.13 C ANISOU 1143 CZ3 TRP A 181 3142 3168 12356 39 -493 -734 C ATOM 1144 CH2 TRP A 181 21.341 -4.973 -17.137 1.00 52.17 C ANISOU 1144 CH2 TRP A 181 3446 3400 12979 100 -922 -1013 C ATOM 1145 N ILE A 182 23.099 -7.210 -21.942 1.00 51.61 N ANISOU 1145 N ILE A 182 3393 3423 12796 115 1147 878 N ATOM 1146 CA ILE A 182 23.764 -8.035 -20.945 1.00 51.01 C ANISOU 1146 CA ILE A 182 3280 3346 12755 54 793 570 C ATOM 1147 C ILE A 182 25.288 -7.980 -21.118 1.00 55.62 C ANISOU 1147 C ILE A 182 3628 3581 13924 69 869 825 C ATOM 1148 O ILE A 182 26.033 -7.823 -20.147 1.00 57.93 O ANISOU 1148 O ILE A 182 3749 3686 14574 28 441 570 O ATOM 1149 CB ILE A 182 23.265 -9.476 -21.003 1.00 47.22 C ANISOU 1149 CB ILE A 182 3057 3427 11459 91 876 468 C ATOM 1150 CG1 ILE A 182 21.773 -9.490 -20.632 1.00 42.67 C ANISOU 1150 CG1 ILE A 182 2667 3266 10282 110 711 163 C ATOM 1151 CG2 ILE A 182 24.105 -10.339 -20.084 1.00 46.46 C ANISOU 1151 CG2 ILE A 182 2912 3291 11448 36 571 232 C ATOM 1152 CD1 ILE A 182 21.065 -10.832 -20.838 1.00 38.58 C ANISOU 1152 CD1 ILE A 182 2402 3265 8990 181 821 106 C ATOM 1153 N GLN A 183 25.741 -8.088 -22.359 1.00 59.01 N ANISOU 1153 N GLN A 183 4064 3987 14371 176 1405 1325 N ATOM 1154 CA GLN A 183 27.181 -8.002 -22.648 1.00 63.20 C ANISOU 1154 CA GLN A 183 4347 4242 15422 222 1541 1607 C ATOM 1155 C GLN A 183 27.735 -6.602 -22.360 1.00 67.95 C ANISOU 1155 C GLN A 183 4610 4481 16728 190 1329 1612 C ATOM 1156 O GLN A 183 28.913 -6.464 -22.027 1.00 78.30 O ANISOU 1156 O GLN A 183 5644 5502 18605 183 1181 1656 O ATOM 1157 CB GLN A 183 27.476 -8.417 -24.090 1.00 64.13 C ANISOU 1157 CB GLN A 183 4601 4442 15321 419 2189 2134 C ATOM 1158 CG GLN A 183 27.059 -9.846 -24.426 1.00 59.80 C ANISOU 1158 CG GLN A 183 4402 4225 14096 500 2394 2152 C ATOM 1159 CD GLN A 183 27.741 -10.881 -23.557 1.00 68.63 C ANISOU 1159 CD GLN A 183 5455 5329 15291 393 2114 1917 C ATOM 1160 OE1 GLN A 183 28.965 -10.953 -23.499 1.00 62.50 O ANISOU 1160 OE1 GLN A 183 4452 4325 14972 400 2129 2053 O ATOM 1161 NE2 GLN A 183 26.943 -11.699 -22.878 1.00 53.53 N ANISOU 1161 NE2 GLN A 183 3732 3730 12876 306 1847 1545 N ATOM 1162 N GLU A 184 26.887 -5.576 -22.471 1.00 67.79 N ANISOU 1162 N GLU A 184 4599 4458 16699 181 1301 1569 N ATOM 1163 CA GLU A 184 27.299 -4.200 -22.167 1.00 72.85 C ANISOU 1163 CA GLU A 184 4924 4752 18002 165 1070 1548 C ATOM 1164 C GLU A 184 27.570 -4.067 -20.684 1.00 76.76 C ANISOU 1164 C GLU A 184 5301 5111 18753 91 382 1044 C ATOM 1165 O GLU A 184 28.353 -3.218 -20.256 1.00 79.34 O ANISOU 1165 O GLU A 184 5309 5097 19738 112 101 1013 O ATOM 1166 CB GLU A 184 26.210 -3.187 -22.539 1.00 72.05 C ANISOU 1166 CB GLU A 184 4890 4707 17777 171 1162 1571 C ATOM 1167 CG GLU A 184 26.010 -2.990 -24.014 1.00 73.10 C ANISOU 1167 CG GLU A 184 5117 4917 17743 311 1802 2092 C ATOM 1168 CD GLU A 184 24.745 -2.229 -24.329 1.00 84.46 C ANISOU 1168 CD GLU A 184 6691 6487 18915 308 1873 2078 C ATOM 1169 OE1 GLU A 184 24.365 -1.356 -23.523 1.00 81.49 O ANISOU 1169 OE1 GLU A 184 6186 5981 18796 201 1465 1763 O ATOM 1170 OE2 GLU A 184 24.123 -2.512 -25.376 1.00 85.99 O ANISOU 1170 OE2 GLU A 184 7135 6915 18621 443 2322 2375 O ATOM 1171 N ASN A 185 26.911 -4.913 -19.902 1.00 68.55 N ANISOU 1171 N ASN A 185 4520 4345 17179 49 103 654 N ATOM 1172 CA ASN A 185 26.926 -4.773 -18.457 1.00 73.00 C ANISOU 1172 CA ASN A 185 5073 4858 17804 60 -563 139 C ATOM 1173 C ASN A 185 27.733 -5.881 -17.827 1.00 71.22 C ANISOU 1173 C ASN A 185 4872 4647 17540 64 -773 4 C ATOM 1174 O ASN A 185 27.542 -6.214 -16.659 1.00 69.15 O ANISOU 1174 O ASN A 185 4745 4484 17043 113 -1263 -429 O ATOM 1175 CB ASN A 185 25.498 -4.742 -17.894 1.00 68.87 C ANISOU 1175 CB ASN A 185 4833 4633 16702 68 -772 -243 C ATOM 1176 CG ASN A 185 24.808 -3.412 -18.137 1.00 69.04 C ANISOU 1176 CG ASN A 185 4775 4563 16893 79 -759 -221 C ATOM 1177 OD1 ASN A 185 24.694 -2.585 -17.234 1.00 70.62 O ANISOU 1177 OD1 ASN A 185 4878 4666 17289 159 -1233 -539 O ATOM 1178 ND2 ASN A 185 24.349 -3.196 -19.364 1.00 64.80 N ANISOU 1178 ND2 ASN A 185 4269 4078 16273 31 -226 169 N ATOM 1179 N GLY A 186 28.637 -6.446 -18.623 1.00 70.32 N ANISOU 1179 N GLY A 186 4641 4442 17635 46 -383 398 N ATOM 1180 CA GLY A 186 29.606 -7.394 -18.129 1.00 71.25 C ANISOU 1180 CA GLY A 186 4710 4499 17862 45 -549 342 C ATOM 1181 C GLY A 186 29.255 -8.850 -18.374 1.00 69.83 C ANISOU 1181 C GLY A 186 4807 4661 17063 23 -301 354 C ATOM 1182 O GLY A 186 29.960 -9.733 -17.910 1.00 66.08 O ANISOU 1182 O GLY A 186 4324 4172 16612 22 -450 277 O ATOM 1183 N GLY A 187 28.173 -9.116 -19.096 1.00 63.01 N ANISOU 1183 N GLY A 187 4181 4092 15669 17 61 452 N ATOM 1184 CA GLY A 187 27.773 -10.499 -19.342 1.00 56.67 C ANISOU 1184 CA GLY A 187 3633 3602 14299 16 278 459 C ATOM 1185 C GLY A 187 26.963 -11.085 -18.190 1.00 54.21 C ANISOU 1185 C GLY A 187 3539 3535 13524 1 -168 -64 C ATOM 1186 O GLY A 187 26.695 -10.394 -17.206 1.00 56.74 O ANISOU 1186 O GLY A 187 3853 3807 13898 30 -632 -423 O ATOM 1187 N TRP A 188 26.556 -12.347 -18.312 1.00 51.72 N ANISOU 1187 N TRP A 188 3434 3708 12509 -16 -19 -99 N ATOM 1188 CA TRP A 188 25.778 -13.018 -17.260 1.00 46.85 C ANISOU 1188 CA TRP A 188 3036 3483 11281 -9 -382 -543 C ATOM 1189 C TRP A 188 26.558 -13.148 -15.940 1.00 53.88 C ANISOU 1189 C TRP A 188 3893 4140 12437 47 -914 -869 C ATOM 1190 O TRP A 188 25.958 -13.267 -14.873 1.00 48.92 O ANISOU 1190 O TRP A 188 3458 3707 11420 133 -1290 -1254 O ATOM 1191 CB TRP A 188 25.264 -14.398 -17.725 1.00 40.71 C ANISOU 1191 CB TRP A 188 2457 3225 9787 -10 -103 -467 C ATOM 1192 CG TRP A 188 23.976 -14.331 -18.492 1.00 37.76 C ANISOU 1192 CG TRP A 188 2240 3204 8904 26 181 -377 C ATOM 1193 CD1 TRP A 188 23.820 -14.424 -19.843 1.00 43.13 C ANISOU 1193 CD1 TRP A 188 2980 3970 9437 96 667 2 C ATOM 1194 CD2 TRP A 188 22.668 -14.148 -17.948 1.00 39.49 C ANISOU 1194 CD2 TRP A 188 2606 3703 8696 49 -15 -664 C ATOM 1195 NE1 TRP A 188 22.494 -14.316 -20.177 1.00 42.13 N ANISOU 1195 NE1 TRP A 188 3024 4150 8834 154 750 -47 N ATOM 1196 CE2 TRP A 188 21.762 -14.143 -19.031 1.00 40.69 C ANISOU 1196 CE2 TRP A 188 2866 4089 8507 109 350 -441 C ATOM 1197 CE3 TRP A 188 22.170 -13.983 -16.652 1.00 38.51 C ANISOU 1197 CE3 TRP A 188 2570 3637 8427 73 -455 -1081 C ATOM 1198 CZ2 TRP A 188 20.396 -13.973 -18.859 1.00 37.60 C ANISOU 1198 CZ2 TRP A 188 2607 3962 7719 153 282 -610 C ATOM 1199 CZ3 TRP A 188 20.812 -13.822 -16.481 1.00 35.85 C ANISOU 1199 CZ3 TRP A 188 2374 3587 7660 130 -480 -1236 C ATOM 1200 CH2 TRP A 188 19.936 -13.822 -17.579 1.00 37.99 C ANISOU 1200 CH2 TRP A 188 2692 4068 7673 152 -114 -995 C ATOM 1201 N ASP A 189 27.891 -13.136 -16.016 1.00 51.98 N ANISOU 1201 N ASP A 189 3426 3478 12845 50 -935 -687 N ATOM 1202 CA ASP A 189 28.736 -13.168 -14.816 1.00 62.71 C ANISOU 1202 CA ASP A 189 4728 4594 14503 143 -1466 -953 C ATOM 1203 C ASP A 189 28.327 -12.103 -13.800 1.00 56.43 C ANISOU 1203 C ASP A 189 3982 3738 13720 265 -1963 -1298 C ATOM 1204 O ASP A 189 28.361 -12.333 -12.591 1.00 58.20 O ANISOU 1204 O ASP A 189 4366 4015 13732 414 -2432 -1635 O ATOM 1205 CB ASP A 189 30.207 -12.943 -15.184 1.00 76.47 C ANISOU 1205 CB ASP A 189 6141 5950 16962 95 -1390 -635 C ATOM 1206 CG ASP A 189 30.780 -14.064 -16.021 1.00 88.06 C ANISOU 1206 CG ASP A 189 7574 7467 18416 33 -942 -299 C ATOM 1207 OD1 ASP A 189 30.134 -15.129 -16.115 1.00 87.36 O ANISOU 1207 OD1 ASP A 189 7724 7767 17701 15 -791 -373 O ATOM 1208 OD2 ASP A 189 31.889 -13.881 -16.576 1.00 97.62 O ANISOU 1208 OD2 ASP A 189 8516 8395 20181 11 -736 46 O ATOM 1209 N THR A 190 27.942 -10.939 -14.315 1.00 57.71 N ANISOU 1209 N THR A 190 4025 3786 14116 230 -1841 -1184 N ATOM 1210 CA THR A 190 27.546 -9.794 -13.503 1.00 68.04 C ANISOU 1210 CA THR A 190 5347 5008 15499 349 -2272 -1466 C ATOM 1211 C THR A 190 26.316 -10.084 -12.633 1.00 62.04 C ANISOU 1211 C THR A 190 4941 4622 14009 502 -2505 -1854 C ATOM 1212 O THR A 190 26.269 -9.735 -11.449 1.00 61.39 O ANISOU 1212 O THR A 190 4986 4521 13820 699 -3011 -2171 O ATOM 1213 CB THR A 190 27.245 -8.577 -14.412 1.00 65.16 C ANISOU 1213 CB THR A 190 4788 4486 15483 266 -1998 -1222 C ATOM 1214 OG1 THR A 190 28.399 -8.283 -15.212 1.00 70.51 O ANISOU 1214 OG1 THR A 190 5138 4827 16824 177 -1744 -820 O ATOM 1215 CG2 THR A 190 26.859 -7.356 -13.581 1.00 65.07 C ANISOU 1215 CG2 THR A 190 4761 4368 15595 394 -2461 -1514 C ATOM 1216 N PHE A 191 25.323 -10.713 -13.242 1.00 51.63 N ANISOU 1216 N PHE A 191 3787 3635 12194 437 -2128 -1804 N ATOM 1217 CA PHE A 191 24.073 -11.071 -12.562 1.00 53.66 C ANISOU 1217 CA PHE A 191 4367 4324 11696 559 -2237 -2097 C ATOM 1218 C PHE A 191 24.268 -12.073 -11.427 1.00 52.72 C ANISOU 1218 C PHE A 191 4503 4428 11099 700 -2519 -2310 C ATOM 1219 O PHE A 191 23.663 -11.929 -10.369 1.00 51.11 O ANISOU 1219 O PHE A 191 4561 4402 10457 907 -2813 -2566 O ATOM 1220 CB PHE A 191 23.082 -11.650 -13.567 1.00 47.81 C ANISOU 1220 CB PHE A 191 3717 3967 10483 380 -1740 -1916 C ATOM 1221 CG PHE A 191 21.843 -12.219 -12.938 1.00 48.79 C ANISOU 1221 CG PHE A 191 4153 4562 9821 479 -1788 -2145 C ATOM 1222 CD1 PHE A 191 20.836 -11.377 -12.474 1.00 52.02 C ANISOU 1222 CD1 PHE A 191 4681 5043 10040 613 -1933 -2346 C ATOM 1223 CD2 PHE A 191 21.682 -13.590 -12.808 1.00 44.92 C ANISOU 1223 CD2 PHE A 191 3835 4432 8800 458 -1669 -2128 C ATOM 1224 CE1 PHE A 191 19.692 -11.898 -11.890 1.00 49.72 C ANISOU 1224 CE1 PHE A 191 4703 5159 9028 730 -1915 -2495 C ATOM 1225 CE2 PHE A 191 20.534 -14.120 -12.227 1.00 47.85 C ANISOU 1225 CE2 PHE A 191 4493 5201 8486 573 -1666 -2278 C ATOM 1226 CZ PHE A 191 19.534 -13.269 -11.776 1.00 45.80 C ANISOU 1226 CZ PHE A 191 4373 4995 8036 713 -1764 -2444 C ATOM 1227 N VAL A 192 25.089 -13.099 -11.670 1.00 51.76 N ANISOU 1227 N VAL A 192 4330 4304 11032 595 -2390 -2164 N ATOM 1228 CA VAL A 192 25.428 -14.085 -10.643 1.00 48.65 C ANISOU 1228 CA VAL A 192 4153 4065 10268 721 -2637 -2320 C ATOM 1229 C VAL A 192 26.044 -13.365 -9.450 1.00 58.22 C ANISOU 1229 C VAL A 192 5392 4955 11775 971 -3218 -2559 C ATOM 1230 O VAL A 192 25.682 -13.625 -8.303 1.00 61.74 O ANISOU 1230 O VAL A 192 6161 5586 11711 1191 -3497 -2777 O ATOM 1231 CB VAL A 192 26.383 -15.179 -11.189 1.00 52.29 C ANISOU 1231 CB VAL A 192 4481 4494 10894 559 -2422 -2101 C ATOM 1232 CG1 VAL A 192 27.009 -16.008 -10.056 1.00 49.68 C ANISOU 1232 CG1 VAL A 192 4316 4180 10380 706 -2757 -2262 C ATOM 1233 CG2 VAL A 192 25.638 -16.084 -12.159 1.00 44.07 C ANISOU 1233 CG2 VAL A 192 3499 3870 9376 383 -1930 -1905 C ATOM 1234 N GLU A 193 26.957 -12.443 -9.733 1.00 57.09 N ANISOU 1234 N GLU A 193 4918 4315 12459 955 -3392 -2486 N ATOM 1235 CA GLU A 193 27.515 -11.589 -8.691 1.00 79.27 C ANISOU 1235 CA GLU A 193 7732 6826 15563 1144 -3974 -2694 C ATOM 1236 C GLU A 193 26.423 -10.759 -8.033 1.00 78.42 C ANISOU 1236 C GLU A 193 7859 6867 15069 1364 -4210 -2942 C ATOM 1237 O GLU A 193 26.348 -10.680 -6.808 1.00 80.78 O ANISOU 1237 O GLU A 193 8445 7167 15080 1661 -4675 -3208 O ATOM 1238 CB GLU A 193 28.587 -10.660 -9.261 1.00 84.50 C ANISOU 1238 CB GLU A 193 7974 7018 17116 982 -4017 -2492 C ATOM 1239 CG GLU A 193 29.867 -11.356 -9.692 1.00 89.11 C ANISOU 1239 CG GLU A 193 8314 7374 18171 830 -3887 -2249 C ATOM 1240 CD GLU A 193 30.931 -10.369 -10.127 1.00 97.37 C ANISOU 1240 CD GLU A 193 8933 7938 20123 725 -3955 -2036 C ATOM 1241 OE1 GLU A 193 30.657 -9.149 -10.083 1.00 99.56 O ANISOU 1241 OE1 GLU A 193 9109 8063 20657 765 -4122 -2095 O ATOM 1242 OE2 GLU A 193 32.038 -10.809 -10.510 1.00102.01 O ANISOU 1242 OE2 GLU A 193 9276 8298 21184 614 -3838 -1799 O ATOM 1243 N LEU A 194 25.571 -10.150 -8.852 1.00 60.89 N ANISOU 1243 N LEU A 194 5543 4762 12830 1239 -3883 -2842 N ATOM 1244 CA LEU A 194 24.539 -9.249 -8.342 1.00 78.19 C ANISOU 1244 CA LEU A 194 7910 7066 14732 1427 -4084 -3051 C ATOM 1245 C LEU A 194 23.474 -9.964 -7.520 1.00 78.58 C ANISOU 1245 C LEU A 194 8468 7597 13794 1576 -4024 -3201 C ATOM 1246 O LEU A 194 23.037 -9.450 -6.494 1.00 82.71 O ANISOU 1246 O LEU A 194 9294 8146 13986 1840 -4359 -3423 O ATOM 1247 CB LEU A 194 23.902 -8.428 -9.468 1.00 74.09 C ANISOU 1247 CB LEU A 194 7164 6545 14441 1215 -3711 -2878 C ATOM 1248 CG LEU A 194 24.642 -7.129 -9.800 1.00 77.87 C ANISOU 1248 CG LEU A 194 7296 6580 15712 1115 -3867 -2779 C ATOM 1249 CD1 LEU A 194 23.996 -6.394 -10.959 1.00 74.48 C ANISOU 1249 CD1 LEU A 194 6669 6157 15473 917 -3437 -2558 C ATOM 1250 CD2 LEU A 194 24.722 -6.225 -8.577 1.00 83.99 C ANISOU 1250 CD2 LEU A 194 8194 7166 16551 1390 -4525 -3104 C ATOM 1251 N TYR A 195 23.054 -11.147 -7.959 1.00 75.26 N ANISOU 1251 N TYR A 195 8151 7531 12913 1432 -3587 -3056 N ATOM 1252 CA TYR A 195 22.120 -11.931 -7.156 1.00 74.96 C ANISOU 1252 CA TYR A 195 8558 7911 12014 1594 -3489 -3128 C ATOM 1253 C TYR A 195 22.816 -12.522 -5.930 1.00 79.78 C ANISOU 1253 C TYR A 195 9415 8460 12436 1836 -3848 -3256 C ATOM 1254 O TYR A 195 23.684 -11.893 -5.324 1.00 88.25 O ANISOU 1254 O TYR A 195 10441 9166 13922 1999 -4343 -3412 O ATOM 1255 CB TYR A 195 21.434 -13.043 -7.969 1.00 68.76 C ANISOU 1255 CB TYR A 195 7783 7508 10834 1386 -2955 -2926 C ATOM 1256 CG TYR A 195 20.631 -13.970 -7.078 1.00 70.15 C ANISOU 1256 CG TYR A 195 8365 8054 10235 1568 -2840 -2932 C ATOM 1257 CD1 TYR A 195 19.374 -13.598 -6.599 1.00 69.19 C ANISOU 1257 CD1 TYR A 195 8527 8134 9628 1741 -2730 -2970 C ATOM 1258 CD2 TYR A 195 21.145 -15.201 -6.682 1.00 72.19 C ANISOU 1258 CD2 TYR A 195 8718 8422 10290 1582 -2816 -2869 C ATOM 1259 CE1 TYR A 195 18.649 -14.440 -5.761 1.00 68.86 C ANISOU 1259 CE1 TYR A 195 8834 8375 8953 1933 -2563 -2904 C ATOM 1260 CE2 TYR A 195 20.434 -16.043 -5.847 1.00 71.12 C ANISOU 1260 CE2 TYR A 195 8925 8579 9520 1761 -2681 -2825 C ATOM 1261 CZ TYR A 195 19.192 -15.662 -5.388 1.00 71.47 C ANISOU 1261 CZ TYR A 195 9229 8799 9128 1940 -2542 -2825 C ATOM 1262 OH TYR A 195 18.506 -16.516 -4.554 1.00 73.88 O ANISOU 1262 OH TYR A 195 9847 9346 8879 2136 -2355 -2722 O TER 1263 TYR A 195 ATOM 1264 N SER B 2 22.668 -18.032 -27.826 1.00 68.28 N ANISOU 1264 N SER B 2 8274 7919 9748 1575 2972 1702 N ATOM 1265 CA SER B 2 21.957 -18.641 -28.943 1.00 75.95 C ANISOU 1265 CA SER B 2 9824 9032 10000 1912 3027 1750 C ATOM 1266 C SER B 2 21.663 -20.089 -28.579 1.00 75.11 C ANISOU 1266 C SER B 2 9911 9171 9459 1851 2742 1436 C ATOM 1267 O SER B 2 20.563 -20.412 -28.131 1.00 73.36 O ANISOU 1267 O SER B 2 9774 9185 8914 1743 2416 1131 O ATOM 1268 CB SER B 2 22.797 -18.563 -30.221 1.00 84.46 C ANISOU 1268 CB SER B 2 11173 9845 11071 2308 3444 2183 C ATOM 1269 OG SER B 2 21.980 -18.551 -31.381 1.00 88.02 O ANISOU 1269 OG SER B 2 12155 10343 10946 2698 3469 2241 O ATOM 1270 N GLN B 3 22.655 -20.954 -28.772 1.00 72.82 N ANISOU 1270 N GLN B 3 9677 8791 9199 1931 2869 1535 N ATOM 1271 CA GLN B 3 22.628 -22.286 -28.187 1.00 68.28 C ANISOU 1271 CA GLN B 3 9148 8401 8394 1804 2611 1250 C ATOM 1272 C GLN B 3 22.664 -22.107 -26.670 1.00 54.84 C ANISOU 1272 C GLN B 3 6938 6794 7103 1424 2395 996 C ATOM 1273 O GLN B 3 21.928 -22.762 -25.924 1.00 46.68 O ANISOU 1273 O GLN B 3 5909 5989 5837 1279 2088 681 O ATOM 1274 CB GLN B 3 23.844 -23.084 -28.650 1.00 76.24 C ANISOU 1274 CB GLN B 3 10247 9250 9472 1969 2847 1454 C ATOM 1275 CG GLN B 3 23.990 -24.430 -27.973 1.00 78.58 C ANISOU 1275 CG GLN B 3 10527 9702 9627 1821 2613 1192 C ATOM 1276 CD GLN B 3 22.811 -25.336 -28.244 1.00 82.29 C ANISOU 1276 CD GLN B 3 11406 10370 9492 1882 2255 915 C ATOM 1277 OE1 GLN B 3 22.663 -25.867 -29.346 1.00 87.19 O ANISOU 1277 OE1 GLN B 3 12477 10915 9737 2188 2255 983 O ATOM 1278 NE2 GLN B 3 21.958 -25.514 -27.240 1.00 80.58 N ANISOU 1278 NE2 GLN B 3 11030 10362 9225 1611 1918 604 N ATOM 1279 N ASER B 4 23.529 -21.200 -26.227 0.46 53.65 N ANISOU 1279 N ASER B 4 6367 6425 7594 1290 2522 1140 N ATOM 1280 N BSER B 4 23.529 -21.203 -26.224 0.54 53.67 N ANISOU 1280 N BSER B 4 6369 6428 7597 1290 2521 1139 N ATOM 1281 CA ASER B 4 23.662 -20.865 -24.815 0.46 50.12 C ANISOU 1281 CA ASER B 4 5459 5986 7599 980 2240 890 C ATOM 1282 CA BSER B 4 23.650 -20.875 -24.812 0.54 50.13 C ANISOU 1282 CA BSER B 4 5463 5991 7594 980 2238 887 C ATOM 1283 C ASER B 4 22.368 -20.263 -24.263 0.46 44.82 C ANISOU 1283 C ASER B 4 4739 5489 6801 875 1991 641 C ATOM 1284 C BSER B 4 22.347 -20.284 -24.274 0.54 44.59 C ANISOU 1284 C BSER B 4 4720 5467 6757 878 1991 639 C ATOM 1285 O ASER B 4 21.912 -20.646 -23.188 0.46 42.66 O ANISOU 1285 O ASER B 4 4331 5383 6497 714 1693 334 O ATOM 1286 O BSER B 4 21.870 -20.689 -23.218 0.54 42.77 O ANISOU 1286 O BSER B 4 4363 5407 6479 721 1695 332 O ATOM 1287 CB ASER B 4 24.832 -19.893 -24.619 0.46 53.48 C ANISOU 1287 CB ASER B 4 5513 6045 8763 890 2349 1105 C ATOM 1288 CB BSER B 4 24.792 -19.880 -24.604 0.54 53.46 C ANISOU 1288 CB BSER B 4 5511 6049 8754 887 2341 1097 C ATOM 1289 OG ASER B 4 24.890 -19.396 -23.293 0.46 52.57 O ANISOU 1289 OG ASER B 4 5032 5880 9062 631 1975 830 O ATOM 1290 OG BSER B 4 24.569 -18.699 -25.358 0.54 54.01 O ANISOU 1290 OG BSER B 4 5612 5945 8965 996 2559 1349 O ATOM 1291 N ASN B 5 21.785 -19.319 -24.998 1.00 44.31 N ANISOU 1291 N ASN B 5 4791 5368 6676 991 2132 797 N ATOM 1292 CA ASN B 5 20.541 -18.678 -24.565 1.00 41.77 C ANISOU 1292 CA ASN B 5 4427 5183 6261 917 1921 599 C ATOM 1293 C ASN B 5 19.375 -19.662 -24.521 1.00 35.79 C ANISOU 1293 C ASN B 5 4029 4710 4860 896 1591 359 C ATOM 1294 O ASN B 5 18.597 -19.650 -23.575 1.00 30.21 O ANISOU 1294 O ASN B 5 3225 4133 4120 704 1240 96 O ATOM 1295 CB ASN B 5 20.190 -17.460 -25.425 1.00 51.27 C ANISOU 1295 CB ASN B 5 5693 6246 7543 1056 2133 843 C ATOM 1296 CG ASN B 5 21.106 -16.281 -25.165 1.00 53.72 C ANISOU 1296 CG ASN B 5 5630 6224 8557 933 2206 999 C ATOM 1297 OD1 ASN B 5 21.639 -16.122 -24.068 1.00 53.30 O ANISOU 1297 OD1 ASN B 5 5248 6070 8933 711 1954 805 O ATOM 1298 ND2 ASN B 5 21.295 -15.454 -26.175 1.00 54.60 N ANISOU 1298 ND2 ASN B 5 5830 6131 8785 1104 2523 1354 N ATOM 1299 N ARG B 6 19.278 -20.543 -25.517 1.00 34.94 N ANISOU 1299 N ARG B 6 4333 4664 4277 1121 1701 459 N ATOM 1300 CA ARG B 6 18.204 -21.525 -25.500 1.00 34.71 C ANISOU 1300 CA ARG B 6 4598 4831 3761 1093 1325 236 C ATOM 1301 C ARG B 6 18.362 -22.446 -24.304 1.00 29.62 C ANISOU 1301 C ARG B 6 3753 4305 3197 858 1082 0 C ATOM 1302 O ARG B 6 17.386 -22.819 -23.680 1.00 28.66 O ANISOU 1302 O ARG B 6 3620 4320 2948 714 749 -195 O ATOM 1303 CB ARG B 6 18.126 -22.347 -26.794 1.00 43.90 C ANISOU 1303 CB ARG B 6 6294 5985 4402 1416 1402 340 C ATOM 1304 CG ARG B 6 16.974 -23.361 -26.749 1.00 47.77 C ANISOU 1304 CG ARG B 6 7030 6603 4519 1360 910 92 C ATOM 1305 CD ARG B 6 16.888 -24.260 -27.975 1.00 57.31 C ANISOU 1305 CD ARG B 6 8718 7702 5354 1617 790 123 C ATOM 1306 NE ARG B 6 15.600 -24.952 -28.032 1.00 58.99 N ANISOU 1306 NE ARG B 6 9062 7932 5420 1532 260 -86 N ATOM 1307 CZ ARG B 6 15.352 -26.136 -27.477 1.00 58.51 C ANISOU 1307 CZ ARG B 6 8906 7901 5425 1345 -22 -254 C ATOM 1308 NH1 ARG B 6 16.306 -26.783 -26.817 1.00 57.88 N ANISOU 1308 NH1 ARG B 6 8664 7877 5452 1243 146 -268 N ATOM 1309 NH2 ARG B 6 14.144 -26.679 -27.586 1.00 56.83 N ANISOU 1309 NH2 ARG B 6 8729 7632 5233 1259 -457 -380 N ATOM 1310 N GLU B 7 19.601 -22.812 -23.982 1.00 33.95 N ANISOU 1310 N GLU B 7 4127 4781 3993 842 1270 53 N ATOM 1311 CA AGLU B 7 19.866 -23.678 -22.835 0.50 29.41 C ANISOU 1311 CA AGLU B 7 3378 4305 3490 652 1047 -153 C ATOM 1312 CA BGLU B 7 19.848 -23.682 -22.843 0.50 28.72 C ANISOU 1312 CA BGLU B 7 3295 4219 3396 653 1045 -154 C ATOM 1313 C GLU B 7 19.379 -23.049 -21.533 1.00 26.51 C ANISOU 1313 C GLU B 7 2736 3997 3338 441 777 -358 C ATOM 1314 O GLU B 7 18.810 -23.730 -20.664 1.00 26.22 O ANISOU 1314 O GLU B 7 2702 4116 3146 334 522 -540 O ATOM 1315 CB AGLU B 7 21.362 -24.009 -22.733 0.50 33.99 C ANISOU 1315 CB AGLU B 7 3773 4750 4392 683 1288 -37 C ATOM 1316 CB BGLU B 7 21.330 -24.056 -22.752 0.50 33.35 C ANISOU 1316 CB BGLU B 7 3708 4676 4288 687 1283 -40 C ATOM 1317 CG AGLU B 7 21.843 -25.037 -23.748 0.50 37.08 C ANISOU 1317 CG AGLU B 7 4483 5123 4484 915 1533 115 C ATOM 1318 CG BGLU B 7 21.607 -25.077 -21.680 0.50 31.12 C ANISOU 1318 CG BGLU B 7 3315 4499 4011 535 1042 -239 C ATOM 1319 CD AGLU B 7 23.328 -24.921 -24.037 0.50 48.00 C ANISOU 1319 CD AGLU B 7 5685 6276 6277 974 1837 360 C ATOM 1320 CD BGLU B 7 23.029 -25.565 -21.681 0.50 30.71 C ANISOU 1320 CD BGLU B 7 3102 4308 4259 583 1254 -116 C ATOM 1321 OE1AGLU B 7 24.010 -24.133 -23.346 0.50 49.57 O ANISOU 1321 OE1AGLU B 7 5473 6328 7032 829 1832 389 O ATOM 1322 OE1BGLU B 7 23.543 -25.900 -22.768 0.50 32.16 O ANISOU 1322 OE1BGLU B 7 3471 4403 4345 801 1602 112 O ATOM 1323 OE2AGLU B 7 23.819 -25.614 -24.957 0.50 54.31 O ANISOU 1323 OE2AGLU B 7 6770 7000 6865 1162 2005 522 O ATOM 1324 OE2BGLU B 7 23.637 -25.605 -20.591 0.50 32.25 O ANISOU 1324 OE2BGLU B 7 3003 4463 4787 436 1069 -239 O ATOM 1325 N LEU B 8 19.611 -21.752 -21.388 1.00 25.28 N ANISOU 1325 N LEU B 8 2360 3696 3548 418 851 -312 N ATOM 1326 CA LEU B 8 19.186 -21.035 -20.203 1.00 22.00 C ANISOU 1326 CA LEU B 8 1751 3299 3310 287 596 -521 C ATOM 1327 C LEU B 8 17.664 -20.992 -20.099 1.00 22.74 C ANISOU 1327 C LEU B 8 2003 3568 3071 274 433 -608 C ATOM 1328 O LEU B 8 17.090 -21.178 -19.006 1.00 21.17 O ANISOU 1328 O LEU B 8 1766 3488 2790 211 227 -787 O ATOM 1329 CB LEU B 8 19.729 -19.605 -20.255 1.00 26.28 C ANISOU 1329 CB LEU B 8 2040 3588 4356 288 693 -443 C ATOM 1330 CG LEU B 8 19.463 -18.762 -19.020 1.00 31.05 C ANISOU 1330 CG LEU B 8 2478 4144 5176 203 396 -694 C ATOM 1331 CD1 LEU B 8 19.902 -19.504 -17.762 1.00 33.21 C ANISOU 1331 CD1 LEU B 8 2716 4481 5421 152 122 -934 C ATOM 1332 CD2 LEU B 8 20.216 -17.431 -19.162 1.00 35.67 C ANISOU 1332 CD2 LEU B 8 2773 4394 6386 198 460 -604 C ATOM 1333 N VAL B 9 17.020 -20.715 -21.231 1.00 24.24 N ANISOU 1333 N VAL B 9 2370 3748 3092 369 537 -457 N ATOM 1334 CA VAL B 9 15.553 -20.629 -21.286 1.00 21.71 C ANISOU 1334 CA VAL B 9 2157 3540 2553 362 363 -499 C ATOM 1335 C VAL B 9 14.953 -21.993 -20.929 1.00 20.28 C ANISOU 1335 C VAL B 9 2073 3512 2120 313 169 -586 C ATOM 1336 O VAL B 9 14.072 -22.082 -20.078 1.00 18.43 O ANISOU 1336 O VAL B 9 1744 3372 1885 246 25 -670 O ATOM 1337 CB VAL B 9 15.085 -20.167 -22.686 1.00 27.20 C ANISOU 1337 CB VAL B 9 3069 4161 3104 511 456 -318 C ATOM 1338 CG1 VAL B 9 13.565 -20.353 -22.897 1.00 24.70 C ANISOU 1338 CG1 VAL B 9 2869 3925 2589 510 197 -351 C ATOM 1339 CG2 VAL B 9 15.473 -18.699 -22.888 1.00 23.21 C ANISOU 1339 CG2 VAL B 9 2412 3494 2915 549 657 -204 C ATOM 1340 N VAL B 10 15.469 -23.045 -21.556 1.00 20.59 N ANISOU 1340 N VAL B 10 2292 3550 1982 370 196 -541 N ATOM 1341 CA VAL B 10 14.955 -24.394 -21.304 1.00 23.28 C ANISOU 1341 CA VAL B 10 2713 3986 2148 323 -7 -609 C ATOM 1342 C VAL B 10 15.146 -24.812 -19.857 1.00 21.19 C ANISOU 1342 C VAL B 10 2240 3823 1987 206 -52 -721 C ATOM 1343 O VAL B 10 14.256 -25.418 -19.249 1.00 18.45 O ANISOU 1343 O VAL B 10 1842 3558 1609 153 -193 -744 O ATOM 1344 CB VAL B 10 15.543 -25.423 -22.298 1.00 23.93 C ANISOU 1344 CB VAL B 10 3075 4014 2004 446 21 -560 C ATOM 1345 CG1 VAL B 10 15.153 -26.860 -21.908 1.00 27.49 C ANISOU 1345 CG1 VAL B 10 3559 4523 2361 374 -210 -644 C ATOM 1346 CG2 VAL B 10 15.068 -25.081 -23.704 1.00 26.91 C ANISOU 1346 CG2 VAL B 10 3766 4292 2165 639 -3 -465 C ATOM 1347 N ASP B 11 16.282 -24.456 -19.268 1.00 19.44 N ANISOU 1347 N ASP B 11 1891 3569 1926 190 59 -772 N ATOM 1348 CA ASP B 11 16.488 -24.796 -17.871 1.00 20.12 C ANISOU 1348 CA ASP B 11 1854 3739 2053 139 -31 -899 C ATOM 1349 C ASP B 11 15.434 -24.127 -16.968 1.00 20.68 C ANISOU 1349 C ASP B 11 1855 3879 2123 152 -100 -960 C ATOM 1350 O ASP B 11 14.845 -24.758 -16.070 1.00 18.77 O ANISOU 1350 O ASP B 11 1608 3749 1775 169 -149 -976 O ATOM 1351 CB ASP B 11 17.889 -24.377 -17.410 1.00 21.91 C ANISOU 1351 CB ASP B 11 1947 3855 2521 138 3 -970 C ATOM 1352 CG ASP B 11 18.116 -24.688 -15.961 1.00 23.01 C ANISOU 1352 CG ASP B 11 2036 4063 2645 143 -159 -1130 C ATOM 1353 OD1 ASP B 11 18.560 -25.824 -15.643 1.00 28.45 O ANISOU 1353 OD1 ASP B 11 2759 4815 3238 133 -194 -1137 O ATOM 1354 OD2 ASP B 11 17.829 -23.820 -15.132 1.00 23.47 O ANISOU 1354 OD2 ASP B 11 2061 4106 2752 192 -257 -1252 O ATOM 1355 N PHE B 12 15.198 -22.845 -17.210 1.00 20.11 N ANISOU 1355 N PHE B 12 1734 3725 2182 175 -62 -962 N ATOM 1356 CA PHE B 12 14.267 -22.087 -16.379 1.00 20.15 C ANISOU 1356 CA PHE B 12 1692 3771 2193 229 -93 -1020 C ATOM 1357 C PHE B 12 12.840 -22.606 -16.552 1.00 18.99 C ANISOU 1357 C PHE B 12 1553 3713 1950 228 -98 -890 C ATOM 1358 O PHE B 12 12.113 -22.784 -15.564 1.00 22.01 O ANISOU 1358 O PHE B 12 1898 4179 2287 297 -70 -880 O ATOM 1359 CB PHE B 12 14.301 -20.599 -16.715 1.00 19.16 C ANISOU 1359 CB PHE B 12 1505 3508 2268 251 -60 -1041 C ATOM 1360 CG PHE B 12 13.498 -19.740 -15.747 1.00 19.18 C ANISOU 1360 CG PHE B 12 1487 3526 2274 348 -88 -1137 C ATOM 1361 CD1 PHE B 12 14.067 -19.251 -14.583 1.00 20.41 C ANISOU 1361 CD1 PHE B 12 1663 3627 2466 446 -196 -1346 C ATOM 1362 CD2 PHE B 12 12.161 -19.463 -15.995 1.00 20.72 C ANISOU 1362 CD2 PHE B 12 1666 3768 2437 377 -31 -1021 C ATOM 1363 CE1 PHE B 12 13.340 -18.479 -13.701 1.00 26.61 C ANISOU 1363 CE1 PHE B 12 2509 4415 3188 606 -209 -1447 C ATOM 1364 CE2 PHE B 12 11.419 -18.694 -15.103 1.00 21.08 C ANISOU 1364 CE2 PHE B 12 1705 3822 2481 509 2 -1083 C ATOM 1365 CZ PHE B 12 11.997 -18.217 -13.962 1.00 25.44 C ANISOU 1365 CZ PHE B 12 2336 4334 2997 642 -66 -1297 C ATOM 1366 N LEU B 13 12.438 -22.815 -17.802 1.00 17.74 N ANISOU 1366 N LEU B 13 1448 3504 1787 186 -137 -775 N ATOM 1367 CA LEU B 13 11.090 -23.292 -18.076 1.00 20.55 C ANISOU 1367 CA LEU B 13 1768 3869 2171 172 -237 -653 C ATOM 1368 C LEU B 13 10.858 -24.707 -17.499 1.00 22.51 C ANISOU 1368 C LEU B 13 1974 4180 2400 139 -289 -606 C ATOM 1369 O LEU B 13 9.787 -24.995 -16.959 1.00 21.07 O ANISOU 1369 O LEU B 13 1644 4009 2353 151 -284 -487 O ATOM 1370 CB LEU B 13 10.791 -23.260 -19.567 1.00 18.33 C ANISOU 1370 CB LEU B 13 1624 3481 1860 178 -369 -582 C ATOM 1371 CG LEU B 13 10.781 -21.889 -20.260 1.00 20.94 C ANISOU 1371 CG LEU B 13 1996 3732 2228 237 -302 -557 C ATOM 1372 CD1 LEU B 13 10.523 -22.034 -21.770 1.00 22.42 C ANISOU 1372 CD1 LEU B 13 2420 3813 2285 317 -449 -477 C ATOM 1373 CD2 LEU B 13 9.760 -20.925 -19.599 1.00 20.67 C ANISOU 1373 CD2 LEU B 13 1776 3706 2373 246 -269 -533 C ATOM 1374 N SER B 14 11.867 -25.567 -17.597 1.00 21.00 N ANISOU 1374 N SER B 14 1883 4006 2091 110 -307 -666 N ATOM 1375 CA SER B 14 11.779 -26.915 -17.021 1.00 22.69 C ANISOU 1375 CA SER B 14 2056 4265 2300 82 -345 -619 C ATOM 1376 C SER B 14 11.468 -26.853 -15.538 1.00 19.74 C ANISOU 1376 C SER B 14 1567 3996 1936 160 -193 -586 C ATOM 1377 O SER B 14 10.604 -27.583 -15.053 1.00 26.67 O ANISOU 1377 O SER B 14 2322 4879 2931 175 -160 -424 O ATOM 1378 CB SER B 14 13.091 -27.703 -17.222 1.00 21.55 C ANISOU 1378 CB SER B 14 2060 4072 2055 65 -320 -676 C ATOM 1379 OG SER B 14 13.397 -27.836 -18.581 1.00 26.39 O ANISOU 1379 OG SER B 14 2847 4563 2617 71 -392 -667 O ATOM 1380 N TYR B 15 12.160 -25.962 -14.839 1.00 21.99 N ANISOU 1380 N TYR B 15 1905 4330 2121 243 -106 -724 N ATOM 1381 CA TYR B 15 11.994 -25.729 -13.417 1.00 26.43 C ANISOU 1381 CA TYR B 15 2481 4978 2583 411 16 -744 C ATOM 1382 C TYR B 15 10.576 -25.276 -13.094 1.00 29.08 C ANISOU 1382 C TYR B 15 2710 5316 3022 510 159 -577 C ATOM 1383 O TYR B 15 9.889 -25.890 -12.282 1.00 26.37 O ANISOU 1383 O TYR B 15 2310 5022 2686 628 322 -399 O ATOM 1384 CB TYR B 15 13.028 -24.680 -12.960 1.00 24.06 C ANISOU 1384 CB TYR B 15 2287 4626 2229 480 -49 -964 C ATOM 1385 CG TYR B 15 13.090 -24.366 -11.471 1.00 28.15 C ANISOU 1385 CG TYR B 15 2947 5114 2636 683 -40 -997 C ATOM 1386 CD1 TYR B 15 13.343 -25.360 -10.539 1.00 28.56 C ANISOU 1386 CD1 TYR B 15 3096 5188 2568 771 -24 -924 C ATOM 1387 CD2 TYR B 15 12.912 -23.069 -11.011 1.00 28.29 C ANISOU 1387 CD2 TYR B 15 3036 5065 2646 815 -57 -1110 C ATOM 1388 CE1 TYR B 15 13.420 -25.084 -9.209 1.00 32.36 C ANISOU 1388 CE1 TYR B 15 3773 5630 2894 997 -25 -955 C ATOM 1389 CE2 TYR B 15 12.987 -22.771 -9.665 1.00 31.00 C ANISOU 1389 CE2 TYR B 15 3583 5359 2836 1042 -81 -1158 C ATOM 1390 CZ TYR B 15 13.247 -23.783 -8.769 1.00 31.28 C ANISOU 1390 CZ TYR B 15 3742 5421 2723 1139 -64 -1077 C ATOM 1391 OH TYR B 15 13.317 -23.515 -7.436 1.00 35.13 O ANISOU 1391 OH TYR B 15 4473 5859 3015 1400 -93 -1121 O ATOM 1392 N ALYS B 16 10.158 -24.188 -13.736 0.59 25.79 N ANISOU 1392 N ALYS B 16 2252 4829 2717 480 133 -601 N ATOM 1393 N BLYS B 16 10.117 -24.211 -13.743 0.41 25.91 N ANISOU 1393 N BLYS B 16 2262 4844 2738 479 135 -593 N ATOM 1394 CA ALYS B 16 8.820 -23.642 -13.552 0.59 26.09 C ANISOU 1394 CA ALYS B 16 2159 4843 2913 570 265 -435 C ATOM 1395 CA BLYS B 16 8.797 -23.667 -13.431 0.41 26.37 C ANISOU 1395 CA BLYS B 16 2196 4885 2938 588 284 -429 C ATOM 1396 C ALYS B 16 7.728 -24.673 -13.779 0.59 26.62 C ANISOU 1396 C ALYS B 16 2013 4860 3241 509 281 -155 C ATOM 1397 C BLYS B 16 7.614 -24.541 -13.897 0.41 27.08 C ANISOU 1397 C BLYS B 16 2056 4904 3329 501 271 -149 C ATOM 1398 O ALYS B 16 6.800 -24.788 -12.978 0.59 30.02 O ANISOU 1398 O ALYS B 16 2309 5297 3802 657 512 63 O ATOM 1399 O BLYS B 16 6.506 -24.425 -13.368 0.41 30.30 O ANISOU 1399 O BLYS B 16 2294 5286 3932 620 463 71 O ATOM 1400 CB ALYS B 16 8.606 -22.460 -14.492 0.59 24.57 C ANISOU 1400 CB ALYS B 16 1943 4557 2836 504 177 -492 C ATOM 1401 CB BLYS B 16 8.682 -22.220 -13.924 0.41 26.09 C ANISOU 1401 CB BLYS B 16 2173 4779 2961 592 250 -531 C ATOM 1402 CG ALYS B 16 9.405 -21.260 -14.081 0.59 27.60 C ANISOU 1402 CG ALYS B 16 2457 4927 3102 594 188 -718 C ATOM 1403 CG BLYS B 16 9.618 -21.267 -13.170 0.41 26.83 C ANISOU 1403 CG BLYS B 16 2438 4877 2877 724 251 -787 C ATOM 1404 CD ALYS B 16 8.890 -20.728 -12.743 0.59 28.60 C ANISOU 1404 CD ALYS B 16 2645 5099 3123 856 370 -735 C ATOM 1405 CD BLYS B 16 8.880 -20.526 -12.047 0.41 28.58 C ANISOU 1405 CD BLYS B 16 2729 5108 3019 992 432 -776 C ATOM 1406 CE ALYS B 16 10.026 -20.617 -11.736 0.59 30.99 C ANISOU 1406 CE ALYS B 16 3182 5398 3195 979 284 -967 C ATOM 1407 CE BLYS B 16 9.801 -20.230 -10.854 0.41 31.75 C ANISOU 1407 CE BLYS B 16 3417 5459 3186 1152 340 -979 C ATOM 1408 NZ ALYS B 16 9.519 -20.258 -10.376 0.59 30.46 N ANISOU 1408 NZ ALYS B 16 3316 5294 2963 1247 411 -929 N ATOM 1409 NZ BLYS B 16 11.155 -19.698 -11.208 0.41 33.47 N ANISOU 1409 NZ BLYS B 16 3667 5592 3459 1049 79 -1254 N ATOM 1410 N LEU B 17 7.847 -25.413 -14.878 1.00 22.78 N ANISOU 1410 N LEU B 17 1502 4291 2864 321 34 -149 N ATOM 1411 CA LEU B 17 6.858 -26.416 -15.244 1.00 27.98 C ANISOU 1411 CA LEU B 17 1943 4822 3866 238 -84 78 C ATOM 1412 C LEU B 17 6.829 -27.546 -14.212 1.00 31.18 C ANISOU 1412 C LEU B 17 2256 5273 4319 302 97 243 C ATOM 1413 O LEU B 17 5.742 -28.037 -13.841 1.00 32.58 O ANISOU 1413 O LEU B 17 2163 5342 4872 336 210 538 O ATOM 1414 CB LEU B 17 7.150 -26.994 -16.630 1.00 28.80 C ANISOU 1414 CB LEU B 17 2152 4803 3988 82 -454 -21 C ATOM 1415 CG LEU B 17 6.825 -26.096 -17.828 1.00 24.13 C ANISOU 1415 CG LEU B 17 1641 4110 3419 58 -665 -87 C ATOM 1416 CD1 LEU B 17 7.500 -26.646 -19.072 1.00 27.61 C ANISOU 1416 CD1 LEU B 17 2350 4470 3671 14 -954 -228 C ATOM 1417 CD2 LEU B 17 5.313 -26.014 -18.023 1.00 26.08 C ANISOU 1417 CD2 LEU B 17 1605 4185 4119 43 -801 125 C ATOM 1418 N SER B 18 8.013 -27.971 -13.770 1.00 30.46 N ANISOU 1418 N SER B 18 2369 5304 3900 325 131 84 N ATOM 1419 CA ASER B 18 8.108 -29.037 -12.773 0.26 31.78 C ANISOU 1419 CA ASER B 18 2499 5525 4051 415 307 236 C ATOM 1420 CA BSER B 18 8.108 -29.038 -12.773 0.74 31.44 C ANISOU 1420 CA BSER B 18 2455 5481 4008 414 307 237 C ATOM 1421 C SER B 18 7.489 -28.605 -11.446 1.00 35.33 C ANISOU 1421 C SER B 18 2929 6044 4450 690 692 424 C ATOM 1422 O SER B 18 6.894 -29.416 -10.740 1.00 35.22 O ANISOU 1422 O SER B 18 2842 5934 4605 766 884 694 O ATOM 1423 CB ASER B 18 9.561 -29.457 -12.551 0.26 29.98 C ANISOU 1423 CB ASER B 18 2513 5406 3472 406 238 9 C ATOM 1424 CB BSER B 18 9.563 -29.469 -12.565 0.74 29.99 C ANISOU 1424 CB BSER B 18 2513 5406 3476 403 234 9 C ATOM 1425 OG ASER B 18 10.202 -28.575 -11.649 0.26 29.77 O ANISOU 1425 OG ASER B 18 2684 5506 3122 593 366 -157 O ATOM 1426 OG BSER B 18 9.659 -30.445 -11.546 0.74 31.13 O ANISOU 1426 OG BSER B 18 2651 5609 3568 523 409 163 O ATOM 1427 N GLN B 19 7.631 -27.323 -11.109 1.00 36.01 N ANISOU 1427 N GLN B 19 3199 6181 4304 823 766 258 N ATOM 1428 CA GLN B 19 7.010 -26.786 -9.896 1.00 37.87 C ANISOU 1428 CA GLN B 19 3579 6364 4446 1080 1053 384 C ATOM 1429 C GLN B 19 5.492 -26.934 -9.904 1.00 37.04 C ANISOU 1429 C GLN B 19 3210 6092 4772 1083 1235 736 C ATOM 1430 O GLN B 19 4.865 -27.039 -8.846 1.00 40.66 O ANISOU 1430 O GLN B 19 3742 6494 5213 1298 1516 963 O ATOM 1431 CB GLN B 19 7.390 -25.321 -9.686 1.00 36.03 C ANISOU 1431 CB GLN B 19 3574 6156 3960 1192 1009 121 C ATOM 1432 CG GLN B 19 8.738 -25.120 -9.019 1.00 37.11 C ANISOU 1432 CG GLN B 19 4039 6342 3719 1280 849 -168 C ATOM 1433 CD GLN B 19 9.133 -23.670 -8.993 1.00 37.13 C ANISOU 1433 CD GLN B 19 4196 6297 3615 1336 716 -430 C ATOM 1434 OE1 GLN B 19 8.658 -22.880 -9.807 1.00 34.90 O ANISOU 1434 OE1 GLN B 19 3763 5993 3504 1251 709 -451 O ATOM 1435 NE2 GLN B 19 9.994 -23.302 -8.053 1.00 37.05 N ANISOU 1435 NE2 GLN B 19 4465 6245 3368 1487 578 -621 N ATOM 1436 N LYS B 20 4.904 -26.949 -11.094 1.00 36.24 N ANISOU 1436 N LYS B 20 2827 5879 5063 858 1031 787 N ATOM 1437 CA LYS B 20 3.453 -27.060 -11.232 1.00 41.09 C ANISOU 1437 CA LYS B 20 3186 6268 6157 822 1096 1093 C ATOM 1438 C LYS B 20 2.998 -28.482 -11.540 1.00 46.75 C ANISOU 1438 C LYS B 20 3684 6795 7282 665 970 1318 C ATOM 1439 O LYS B 20 1.850 -28.701 -11.940 1.00 47.85 O ANISOU 1439 O LYS B 20 3596 6680 7906 574 892 1544 O ATOM 1440 CB LYS B 20 2.968 -26.122 -12.334 1.00 39.79 C ANISOU 1440 CB LYS B 20 2898 6026 6194 690 865 996 C ATOM 1441 CG LYS B 20 3.246 -24.672 -12.033 1.00 38.09 C ANISOU 1441 CG LYS B 20 2863 5938 5671 847 999 811 C ATOM 1442 CD LYS B 20 2.332 -24.199 -10.913 1.00 48.57 C ANISOU 1442 CD LYS B 20 4237 7204 7015 1089 1362 1029 C ATOM 1443 CE LYS B 20 2.447 -22.700 -10.688 1.00 49.08 C ANISOU 1443 CE LYS B 20 4480 7334 6835 1241 1441 835 C ATOM 1444 NZ LYS B 20 1.425 -22.222 -9.716 1.00 58.62 N ANISOU 1444 NZ LYS B 20 5730 8456 8086 1485 1772 1075 N ATOM 1445 N GLY B 21 3.901 -29.440 -11.358 1.00 42.11 N ANISOU 1445 N GLY B 21 3176 6300 6525 635 925 1253 N ATOM 1446 CA GLY B 21 3.619 -30.835 -11.648 1.00 47.13 C ANISOU 1446 CA GLY B 21 3637 6739 7533 486 773 1427 C ATOM 1447 C GLY B 21 3.577 -31.155 -13.135 1.00 46.69 C ANISOU 1447 C GLY B 21 3497 6521 7721 221 267 1255 C ATOM 1448 O GLY B 21 2.967 -32.142 -13.544 1.00 44.94 O ANISOU 1448 O GLY B 21 3137 6022 7916 98 64 1397 O ATOM 1449 N TYR B 22 4.226 -30.325 -13.947 1.00 39.17 N ANISOU 1449 N TYR B 22 2683 5706 6495 164 48 953 N ATOM 1450 CA TYR B 22 4.256 -30.534 -15.395 1.00 34.53 C ANISOU 1450 CA TYR B 22 2165 4965 5990 -13 -437 762 C ATOM 1451 C TYR B 22 5.691 -30.870 -15.777 1.00 32.36 C ANISOU 1451 C TYR B 22 2114 4863 5318 -56 -592 501 C ATOM 1452 O TYR B 22 6.553 -30.915 -14.917 1.00 29.28 O ANISOU 1452 O TYR B 22 1761 4707 4656 26 -345 493 O ATOM 1453 CB TYR B 22 3.805 -29.268 -16.135 1.00 38.84 C ANISOU 1453 CB TYR B 22 2745 5492 6522 -13 -560 669 C ATOM 1454 CG TYR B 22 2.372 -28.857 -15.889 1.00 41.22 C ANISOU 1454 CG TYR B 22 2832 5596 7234 21 -443 923 C ATOM 1455 CD1 TYR B 22 1.370 -29.813 -15.713 1.00 42.01 C ANISOU 1455 CD1 TYR B 22 2738 5397 7827 -28 -469 1193 C ATOM 1456 CD2 TYR B 22 2.014 -27.511 -15.846 1.00 37.28 C ANISOU 1456 CD2 TYR B 22 2315 5171 6677 104 -309 915 C ATOM 1457 CE1 TYR B 22 0.054 -29.438 -15.486 1.00 47.18 C ANISOU 1457 CE1 TYR B 22 3178 5829 8918 4 -353 1468 C ATOM 1458 CE2 TYR B 22 0.702 -27.125 -15.627 1.00 40.28 C ANISOU 1458 CE2 TYR B 22 2505 5357 7444 140 -193 1163 C ATOM 1459 CZ TYR B 22 -0.272 -28.094 -15.449 1.00 48.45 C ANISOU 1459 CZ TYR B 22 3340 6091 8979 89 -212 1449 C ATOM 1460 OH TYR B 22 -1.570 -27.719 -15.233 1.00 45.65 O ANISOU 1460 OH TYR B 22 2773 5502 9069 126 -88 1735 O ATOM 1461 N SER B 23 5.967 -31.087 -17.057 1.00 29.32 N ANISOU 1461 N SER B 23 1942 4365 4833 -144 -970 297 N ATOM 1462 CA SER B 23 7.349 -31.364 -17.431 1.00 33.97 C ANISOU 1462 CA SER B 23 2798 5093 5018 -155 -1061 70 C ATOM 1463 C SER B 23 7.701 -30.850 -18.830 1.00 32.20 C ANISOU 1463 C SER B 23 2908 4809 4517 -152 -1285 -120 C ATOM 1464 O SER B 23 6.911 -30.969 -19.763 1.00 31.36 O ANISOU 1464 O SER B 23 2879 4480 4556 -156 -1518 -116 O ATOM 1465 CB SER B 23 7.634 -32.868 -17.294 1.00 41.18 C ANISOU 1465 CB SER B 23 3728 5908 6012 -203 -1134 97 C ATOM 1466 OG SER B 23 8.569 -33.298 -18.260 1.00 48.02 O ANISOU 1466 OG SER B 23 4936 6753 6555 -213 -1311 -111 O ATOM 1467 N TRP B 24 8.895 -30.270 -18.961 1.00 27.50 N ANISOU 1467 N TRP B 24 2551 4343 3555 -109 -1169 -269 N ATOM 1468 CA TRP B 24 9.409 -29.834 -20.259 1.00 25.74 C ANISOU 1468 CA TRP B 24 2676 4042 3061 -56 -1257 -386 C ATOM 1469 C TRP B 24 9.573 -31.002 -21.245 1.00 30.39 C ANISOU 1469 C TRP B 24 3505 4465 3578 -39 -1440 -431 C ATOM 1470 O TRP B 24 9.224 -30.911 -22.434 1.00 27.97 O ANISOU 1470 O TRP B 24 3412 3999 3216 51 -1625 -480 O ATOM 1471 CB TRP B 24 10.751 -29.101 -20.069 1.00 23.09 C ANISOU 1471 CB TRP B 24 2479 3858 2436 16 -972 -502 C ATOM 1472 CG TRP B 24 11.493 -28.911 -21.365 1.00 25.81 C ANISOU 1472 CG TRP B 24 3157 4116 2532 115 -985 -564 C ATOM 1473 CD1 TRP B 24 12.496 -29.687 -21.851 1.00 25.86 C ANISOU 1473 CD1 TRP B 24 3380 4066 2378 163 -921 -593 C ATOM 1474 CD2 TRP B 24 11.264 -27.885 -22.346 1.00 28.36 C ANISOU 1474 CD2 TRP B 24 3633 4407 2735 227 -1032 -576 C ATOM 1475 NE1 TRP B 24 12.903 -29.224 -23.077 1.00 27.09 N ANISOU 1475 NE1 TRP B 24 3814 4160 2318 321 -891 -610 N ATOM 1476 CE2 TRP B 24 12.166 -28.113 -23.403 1.00 27.26 C ANISOU 1476 CE2 TRP B 24 3823 4191 2343 370 -960 -596 C ATOM 1477 CE3 TRP B 24 10.392 -26.793 -22.426 1.00 27.29 C ANISOU 1477 CE3 TRP B 24 3385 4297 2686 248 -1111 -555 C ATOM 1478 CZ2 TRP B 24 12.223 -27.296 -24.525 1.00 26.71 C ANISOU 1478 CZ2 TRP B 24 4011 4063 2075 561 -941 -574 C ATOM 1479 CZ3 TRP B 24 10.444 -25.980 -23.550 1.00 28.13 C ANISOU 1479 CZ3 TRP B 24 3746 4345 2598 410 -1145 -555 C ATOM 1480 CH2 TRP B 24 11.353 -26.238 -24.585 1.00 30.38 C ANISOU 1480 CH2 TRP B 24 4397 4548 2599 576 -1045 -554 C ATOM 1481 N SER B 25 10.124 -32.105 -20.749 1.00 28.67 N ANISOU 1481 N SER B 25 3268 4263 3363 -83 -1394 -430 N ATOM 1482 CA SER B 25 10.442 -33.239 -21.612 1.00 29.56 C ANISOU 1482 CA SER B 25 3613 4213 3405 -27 -1537 -505 C ATOM 1483 C SER B 25 10.666 -34.465 -20.753 1.00 27.82 C ANISOU 1483 C SER B 25 3241 4007 3322 -104 -1520 -465 C ATOM 1484 O SER B 25 10.722 -34.368 -19.520 1.00 28.22 O ANISOU 1484 O SER B 25 3041 4217 3462 -176 -1367 -376 O ATOM 1485 CB SER B 25 11.712 -32.950 -22.425 1.00 28.68 C ANISOU 1485 CB SER B 25 3831 4128 2938 96 -1381 -594 C ATOM 1486 OG SER B 25 12.876 -32.937 -21.585 1.00 25.08 O ANISOU 1486 OG SER B 25 3331 3814 2383 54 -1114 -587 O ATOM 1487 N GLN B 26 10.816 -35.610 -21.407 1.00 27.50 N ANISOU 1487 N GLN B 26 3371 3782 3296 -54 -1690 -530 N ATOM 1488 CA GLN B 26 11.079 -36.846 -20.697 1.00 29.97 C ANISOU 1488 CA GLN B 26 3564 4075 3747 -114 -1696 -496 C ATOM 1489 C GLN B 26 12.434 -36.778 -19.995 1.00 27.59 C ANISOU 1489 C GLN B 26 3292 4008 3184 -131 -1409 -508 C ATOM 1490 O GLN B 26 12.538 -37.188 -18.849 1.00 29.52 O ANISOU 1490 O GLN B 26 3318 4359 3541 -199 -1328 -425 O ATOM 1491 CB GLN B 26 11.003 -38.056 -21.633 1.00 40.87 C ANISOU 1491 CB GLN B 26 5163 5162 5203 -34 -1976 -583 C ATOM 1492 CG GLN B 26 10.871 -39.384 -20.884 1.00 53.55 C ANISOU 1492 CG GLN B 26 6577 6660 7110 -118 -2064 -511 C ATOM 1493 CD GLN B 26 12.171 -40.178 -20.806 1.00 59.59 C ANISOU 1493 CD GLN B 26 7502 7507 7631 -75 -1946 -589 C ATOM 1494 OE1 GLN B 26 13.151 -39.862 -21.484 1.00 65.65 O ANISOU 1494 OE1 GLN B 26 8549 8353 8042 39 -1817 -694 O ATOM 1495 NE2 GLN B 26 12.178 -41.226 -19.981 1.00 56.75 N ANISOU 1495 NE2 GLN B 26 6947 7102 7514 -156 -1976 -506 N ATOM 1496 N MET B 83 13.463 -36.263 -20.675 1.00 27.22 N ANISOU 1496 N MET B 83 3509 3993 2842 -44 -1260 -587 N ATOM 1497 CA MET B 83 14.778 -36.082 -20.042 1.00 28.63 C ANISOU 1497 CA MET B 83 3717 4283 2879 -36 -1000 -589 C ATOM 1498 C MET B 83 14.682 -35.169 -18.824 1.00 25.53 C ANISOU 1498 C MET B 83 3100 4034 2566 -58 -841 -548 C ATOM 1499 O MET B 83 15.282 -35.415 -17.786 1.00 20.47 O ANISOU 1499 O MET B 83 2336 3508 1933 -56 -693 -542 O ATOM 1500 CB MET B 83 15.799 -35.514 -21.044 1.00 31.51 C ANISOU 1500 CB MET B 83 4326 4631 3017 98 -841 -650 C ATOM 1501 CG MET B 83 17.130 -35.069 -20.402 1.00 36.55 C ANISOU 1501 CG MET B 83 4900 5371 3616 134 -572 -651 C ATOM 1502 SD MET B 83 18.002 -36.426 -19.585 1.00 42.24 S ANISOU 1502 SD MET B 83 5549 6115 4384 108 -543 -656 S ATOM 1503 CE MET B 83 18.236 -37.497 -20.998 1.00 37.94 C ANISOU 1503 CE MET B 83 5306 5423 3685 220 -641 -711 C ATOM 1504 N ALA B 84 13.926 -34.081 -18.945 1.00 24.06 N ANISOU 1504 N ALA B 84 2852 3877 2414 -57 -852 -535 N ATOM 1505 CA ALA B 84 13.746 -33.190 -17.820 1.00 20.11 C ANISOU 1505 CA ALA B 84 2133 3556 1952 -56 -677 -520 C ATOM 1506 C ALA B 84 13.071 -33.878 -16.635 1.00 19.99 C ANISOU 1506 C ALA B 84 1859 3658 2077 -94 -685 -426 C ATOM 1507 O ALA B 84 13.402 -33.584 -15.476 1.00 21.00 O ANISOU 1507 O ALA B 84 1880 3988 2110 -48 -499 -422 O ATOM 1508 CB ALA B 84 12.928 -31.920 -18.248 1.00 24.01 C ANISOU 1508 CB ALA B 84 2593 4060 2471 -44 -709 -520 C ATOM 1509 N ALA B 85 12.121 -34.769 -16.924 1.00 21.32 N ANISOU 1509 N ALA B 85 1908 3692 2500 -156 -918 -327 N ATOM 1510 CA ALA B 85 11.423 -35.507 -15.866 1.00 24.26 C ANISOU 1510 CA ALA B 85 1948 4132 3139 -179 -867 -129 C ATOM 1511 C ALA B 85 12.376 -36.481 -15.155 1.00 21.86 C ANISOU 1511 C ALA B 85 1689 3909 2708 -156 -748 -126 C ATOM 1512 O ALA B 85 12.325 -36.628 -13.941 1.00 22.43 O ANISOU 1512 O ALA B 85 1644 4095 2784 -80 -501 30 O ATOM 1513 CB ALA B 85 10.213 -36.270 -16.431 1.00 26.51 C ANISOU 1513 CB ALA B 85 2072 4127 3875 -253 -1137 -3 C ATOM 1514 N VAL B 86 13.212 -37.152 -15.936 1.00 24.90 N ANISOU 1514 N VAL B 86 2297 4188 2975 -178 -901 -275 N ATOM 1515 CA VAL B 86 14.237 -38.024 -15.363 1.00 23.68 C ANISOU 1515 CA VAL B 86 2187 4115 2696 -156 -809 -294 C ATOM 1516 C VAL B 86 15.205 -37.226 -14.481 1.00 20.93 C ANISOU 1516 C VAL B 86 1901 3972 2079 -70 -551 -359 C ATOM 1517 O VAL B 86 15.465 -37.604 -13.349 1.00 22.74 O ANISOU 1517 O VAL B 86 2048 4345 2246 -6 -433 -281 O ATOM 1518 CB VAL B 86 15.003 -38.802 -16.450 1.00 25.65 C ANISOU 1518 CB VAL B 86 2716 4152 2880 -160 -955 -411 C ATOM 1519 CG1 VAL B 86 16.137 -39.627 -15.819 1.00 28.86 C ANISOU 1519 CG1 VAL B 86 3140 4643 3182 -129 -840 -430 C ATOM 1520 CG2 VAL B 86 14.052 -39.703 -17.231 1.00 26.84 C ANISOU 1520 CG2 VAL B 86 2835 4093 3270 -231 -1254 -372 C ATOM 1521 N LYS B 87 15.695 -36.096 -14.978 1.00 23.25 N ANISOU 1521 N LYS B 87 2349 4207 2280 -42 -466 -466 N ATOM 1522 CA LYS B 87 16.624 -35.280 -14.199 1.00 20.31 C ANISOU 1522 CA LYS B 87 1994 3912 1812 30 -306 -528 C ATOM 1523 C LYS B 87 16.045 -34.898 -12.849 1.00 22.81 C ANISOU 1523 C LYS B 87 2192 4455 2018 123 -238 -490 C ATOM 1524 O LYS B 87 16.709 -35.019 -11.826 1.00 22.58 O ANISOU 1524 O LYS B 87 2199 4474 1905 222 -190 -504 O ATOM 1525 CB LYS B 87 17.052 -34.017 -14.972 1.00 22.56 C ANISOU 1525 CB LYS B 87 2346 4100 2126 34 -263 -594 C ATOM 1526 CG LYS B 87 18.033 -34.266 -16.130 1.00 21.05 C ANISOU 1526 CG LYS B 87 2274 3789 1934 31 -271 -626 C ATOM 1527 CD LYS B 87 18.144 -33.005 -17.008 1.00 17.29 C ANISOU 1527 CD LYS B 87 1834 3294 1442 53 -231 -665 C ATOM 1528 CE LYS B 87 19.132 -33.158 -18.138 1.00 24.41 C ANISOU 1528 CE LYS B 87 2867 4150 2258 112 -178 -697 C ATOM 1529 NZ LYS B 87 19.239 -31.890 -18.927 1.00 27.46 N ANISOU 1529 NZ LYS B 87 3289 4552 2592 171 -83 -723 N ATOM 1530 N AGLN B 88 14.806 -34.415 -12.857 0.75 22.32 N ANISOU 1530 N AGLN B 88 2010 4484 1987 130 -235 -407 N ATOM 1531 N BGLN B 88 14.799 -34.442 -12.858 0.25 22.48 N ANISOU 1531 N BGLN B 88 2029 4502 2010 129 -236 -404 N ATOM 1532 CA AGLN B 88 14.157 -33.955 -11.641 0.75 23.49 C ANISOU 1532 CA AGLN B 88 2119 4732 2076 296 -46 -286 C ATOM 1533 CA BGLN B 88 14.156 -33.965 -11.644 0.25 23.40 C ANISOU 1533 CA BGLN B 88 2107 4719 2065 295 -46 -285 C ATOM 1534 C AGLN B 88 13.842 -35.105 -10.677 0.75 23.58 C ANISOU 1534 C AGLN B 88 2071 4766 2124 400 100 -49 C ATOM 1535 C BGLN B 88 13.830 -35.101 -10.676 0.25 24.78 C ANISOU 1535 C BGLN B 88 2221 4918 2277 400 101 -47 C ATOM 1536 O AGLN B 88 14.015 -34.964 -9.470 0.75 27.86 O ANISOU 1536 O AGLN B 88 2724 5423 2437 625 259 -8 O ATOM 1537 O BGLN B 88 13.961 -34.943 -9.464 0.25 27.01 O ANISOU 1537 O BGLN B 88 2612 5315 2336 628 267 0 O ATOM 1538 CB AGLN B 88 12.887 -33.143 -11.968 0.75 24.50 C ANISOU 1538 CB AGLN B 88 2124 4812 2373 288 11 -181 C ATOM 1539 CB BGLN B 88 12.895 -33.158 -11.977 0.25 24.25 C ANISOU 1539 CB BGLN B 88 2093 4779 2342 286 9 -182 C ATOM 1540 CG AGLN B 88 12.138 -32.646 -10.736 0.75 24.48 C ANISOU 1540 CG AGLN B 88 2102 4897 2304 518 280 -19 C ATOM 1541 CG BGLN B 88 12.464 -32.229 -10.857 0.25 25.87 C ANISOU 1541 CG BGLN B 88 2341 5091 2399 511 229 -135 C ATOM 1542 CD AGLN B 88 12.910 -31.598 -9.946 0.75 29.29 C ANISOU 1542 CD AGLN B 88 2942 5620 2567 704 301 -245 C ATOM 1543 CD BGLN B 88 13.538 -31.217 -10.500 0.25 27.54 C ANISOU 1543 CD BGLN B 88 2762 5355 2347 595 143 -419 C ATOM 1544 OE1AGLN B 88 13.803 -30.917 -10.478 0.75 27.59 O ANISOU 1544 OE1AGLN B 88 2812 5321 2349 593 96 -480 O ATOM 1545 OE1BGLN B 88 14.349 -30.833 -11.342 0.25 24.44 O ANISOU 1545 OE1BGLN B 88 2392 4855 2041 442 -29 -583 O ATOM 1546 NE2AGLN B 88 12.586 -31.478 -8.659 0.75 32.00 N ANISOU 1546 NE2AGLN B 88 3432 5932 2794 947 459 -119 N ATOM 1547 NE2BGLN B 88 13.554 -30.788 -9.242 0.25 29.88 N ANISOU 1547 NE2BGLN B 88 3227 5606 2520 811 212 -396 N ATOM 1548 N ALA B 89 13.416 -36.244 -11.213 1.00 27.36 N ANISOU 1548 N ALA B 89 2402 5109 2884 267 25 104 N ATOM 1549 CA ALA B 89 13.132 -37.417 -10.378 1.00 28.65 C ANISOU 1549 CA ALA B 89 2464 5251 3172 352 179 375 C ATOM 1550 C ALA B 89 14.410 -37.889 -9.688 1.00 27.18 C ANISOU 1550 C ALA B 89 2471 5182 2673 452 180 261 C ATOM 1551 O ALA B 89 14.406 -38.235 -8.509 1.00 30.34 O ANISOU 1551 O ALA B 89 2929 5669 2929 670 386 431 O ATOM 1552 CB ALA B 89 12.572 -38.525 -11.218 1.00 31.23 C ANISOU 1552 CB ALA B 89 2590 5348 3930 163 -2 503 C ATOM 1553 N LEU B 90 15.506 -37.918 -10.438 1.00 23.01 N ANISOU 1553 N LEU B 90 2050 4638 2053 324 -39 -4 N ATOM 1554 CA LEU B 90 16.778 -38.342 -9.868 1.00 23.13 C ANISOU 1554 CA LEU B 90 2203 4727 1857 400 -81 -117 C ATOM 1555 C LEU B 90 17.269 -37.353 -8.817 1.00 27.22 C ANISOU 1555 C LEU B 90 2888 5336 2117 605 -48 -236 C ATOM 1556 O LEU B 90 17.772 -37.762 -7.767 1.00 25.08 O ANISOU 1556 O LEU B 90 2737 5059 1735 769 -29 -199 O ATOM 1557 CB LEU B 90 17.836 -38.544 -10.971 1.00 24.26 C ANISOU 1557 CB LEU B 90 2390 4788 2041 240 -270 -328 C ATOM 1558 CG LEU B 90 19.157 -39.185 -10.532 1.00 30.02 C ANISOU 1558 CG LEU B 90 3205 5440 2761 278 -289 -384 C ATOM 1559 CD1 LEU B 90 18.908 -40.524 -9.856 1.00 26.10 C ANISOU 1559 CD1 LEU B 90 2656 5035 2228 344 -262 -192 C ATOM 1560 CD2 LEU B 90 20.046 -39.369 -11.751 1.00 28.21 C ANISOU 1560 CD2 LEU B 90 3024 5007 2688 156 -337 -485 C ATOM 1561 N ARG B 91 17.100 -36.052 -9.077 1.00 28.09 N ANISOU 1561 N ARG B 91 3021 5366 2285 582 -75 -357 N ATOM 1562 CA ARG B 91 17.367 -35.022 -8.069 1.00 26.17 C ANISOU 1562 CA ARG B 91 2936 5050 1957 753 -92 -441 C ATOM 1563 C ARG B 91 16.595 -35.274 -6.779 1.00 29.44 C ANISOU 1563 C ARG B 91 3470 5559 2159 1034 88 -252 C ATOM 1564 O ARG B 91 17.151 -35.192 -5.674 1.00 32.23 O ANISOU 1564 O ARG B 91 4020 5861 2366 1229 36 -301 O ATOM 1565 CB ARG B 91 17.007 -33.614 -8.589 1.00 26.17 C ANISOU 1565 CB ARG B 91 2912 4991 2039 698 -116 -542 C ATOM 1566 CG ARG B 91 18.048 -33.016 -9.520 1.00 27.41 C ANISOU 1566 CG ARG B 91 3028 4985 2400 526 -239 -695 C ATOM 1567 CD ARG B 91 17.669 -31.596 -10.006 1.00 26.73 C ANISOU 1567 CD ARG B 91 2915 4857 2385 498 -243 -767 C ATOM 1568 NE ARG B 91 18.690 -31.082 -10.921 1.00 23.43 N ANISOU 1568 NE ARG B 91 2448 4309 2146 379 -301 -858 N ATOM 1569 CZ ARG B 91 19.040 -29.797 -11.045 1.00 28.09 C ANISOU 1569 CZ ARG B 91 3022 4831 2820 391 -361 -974 C ATOM 1570 NH1 ARG B 91 18.433 -28.846 -10.341 1.00 27.14 N ANISOU 1570 NH1 ARG B 91 2958 4729 2623 507 -393 -1030 N ATOM 1571 NH2 ARG B 91 20.005 -29.465 -11.877 1.00 30.50 N ANISOU 1571 NH2 ARG B 91 3249 5057 3285 310 -390 -1045 N ATOM 1572 N GLU B 92 15.310 -35.577 -6.919 1.00 33.76 N ANISOU 1572 N GLU B 92 3887 6209 2731 1074 330 2 N ATOM 1573 CA GLU B 92 14.453 -35.753 -5.756 1.00 32.86 C ANISOU 1573 CA GLU B 92 3862 6096 2527 1361 607 280 C ATOM 1574 C GLU B 92 14.703 -37.083 -5.044 1.00 35.19 C ANISOU 1574 C GLU B 92 4192 6411 2769 1492 719 489 C ATOM 1575 O GLU B 92 14.614 -37.169 -3.815 1.00 36.36 O ANISOU 1575 O GLU B 92 4545 6526 2743 1793 845 608 O ATOM 1576 CB GLU B 92 12.997 -35.598 -6.152 1.00 36.48 C ANISOU 1576 CB GLU B 92 4092 6544 3226 1336 868 557 C ATOM 1577 CG GLU B 92 12.660 -34.167 -6.529 1.00 33.39 C ANISOU 1577 CG GLU B 92 3731 6130 2826 1301 799 378 C ATOM 1578 CD GLU B 92 11.204 -33.980 -6.842 1.00 38.22 C ANISOU 1578 CD GLU B 92 4100 6680 3743 1284 1040 663 C ATOM 1579 OE1 GLU B 92 10.363 -34.735 -6.314 1.00 41.02 O ANISOU 1579 OE1 GLU B 92 4336 6943 4307 1390 1297 1032 O ATOM 1580 OE2 GLU B 92 10.912 -33.077 -7.633 1.00 34.35 O ANISOU 1580 OE2 GLU B 92 3516 6187 3347 1155 950 532 O ATOM 1581 N ALA B 93 15.025 -38.115 -5.818 1.00 36.50 N ANISOU 1581 N ALA B 93 4166 6630 3072 1289 671 537 N ATOM 1582 CA ALA B 93 15.363 -39.412 -5.246 1.00 33.11 C ANISOU 1582 CA ALA B 93 3749 6212 2620 1387 760 736 C ATOM 1583 C ALA B 93 16.659 -39.328 -4.433 1.00 35.09 C ANISOU 1583 C ALA B 93 4293 6435 2604 1522 527 474 C ATOM 1584 O ALA B 93 16.778 -39.927 -3.353 1.00 36.78 O ANISOU 1584 O ALA B 93 4660 6636 2680 1776 636 626 O ATOM 1585 CB ALA B 93 15.487 -40.450 -6.346 1.00 30.86 C ANISOU 1585 CB ALA B 93 3198 5843 2685 1064 635 774 C ATOM 1586 N GLY B 94 17.633 -38.596 -4.970 1.00 31.91 N ANISOU 1586 N GLY B 94 3932 5975 2219 1347 219 111 N ATOM 1587 CA GLY B 94 18.876 -38.321 -4.273 1.00 31.80 C ANISOU 1587 CA GLY B 94 4112 5858 2111 1429 -15 -121 C ATOM 1588 C GLY B 94 18.650 -37.593 -2.968 1.00 40.35 C ANISOU 1588 C GLY B 94 5456 6906 2969 1756 15 -129 C ATOM 1589 O GLY B 94 19.278 -37.893 -1.949 1.00 38.58 O ANISOU 1589 O GLY B 94 5437 6649 2574 1979 -70 -163 O ATOM 1590 N ASP B 95 17.754 -36.612 -2.992 1.00 40.39 N ANISOU 1590 N ASP B 95 5474 6913 2960 1812 123 -107 N ATOM 1591 CA ASP B 95 17.376 -35.913 -1.768 1.00 41.01 C ANISOU 1591 CA ASP B 95 5822 6958 2800 2172 184 -89 C ATOM 1592 C ASP B 95 16.720 -36.865 -0.785 1.00 37.95 C ANISOU 1592 C ASP B 95 5553 6621 2247 2502 490 246 C ATOM 1593 O ASP B 95 16.994 -36.813 0.404 1.00 41.92 O ANISOU 1593 O ASP B 95 6349 7084 2495 2858 465 230 O ATOM 1594 CB ASP B 95 16.396 -34.768 -2.068 1.00 39.15 C ANISOU 1594 CB ASP B 95 5551 6719 2604 2169 293 -77 C ATOM 1595 CG ASP B 95 17.068 -33.564 -2.694 1.00 40.17 C ANISOU 1595 CG ASP B 95 5644 6762 2858 1964 1 -399 C ATOM 1596 OD1 ASP B 95 18.295 -33.409 -2.539 1.00 42.43 O ANISOU 1596 OD1 ASP B 95 5991 6954 3176 1924 -284 -623 O ATOM 1597 OD2 ASP B 95 16.362 -32.762 -3.344 1.00 43.88 O ANISOU 1597 OD2 ASP B 95 6004 7239 3429 1853 72 -401 O ATOM 1598 N GLU B 96 15.830 -37.722 -1.277 1.00 42.22 N ANISOU 1598 N GLU B 96 5856 7219 2965 2411 787 575 N ATOM 1599 CA GLU B 96 15.035 -38.576 -0.397 1.00 45.59 C ANISOU 1599 CA GLU B 96 6324 7638 3360 2726 1159 990 C ATOM 1600 C GLU B 96 15.913 -39.635 0.252 1.00 48.04 C ANISOU 1600 C GLU B 96 6764 7959 3530 2864 1100 1008 C ATOM 1601 O GLU B 96 15.708 -40.007 1.409 1.00 53.97 O ANISOU 1601 O GLU B 96 7728 8680 4096 3265 1301 1210 O ATOM 1602 CB GLU B 96 13.901 -39.244 -1.175 1.00 50.32 C ANISOU 1602 CB GLU B 96 6550 8221 4348 2539 1462 1373 C ATOM 1603 CG GLU B 96 13.169 -40.331 -0.399 1.00 61.86 C ANISOU 1603 CG GLU B 96 7948 9604 5954 2803 1851 1864 C ATOM 1604 CD GLU B 96 12.037 -40.960 -1.193 1.00 72.24 C ANISOU 1604 CD GLU B 96 8819 10797 7833 2571 2086 2258 C ATOM 1605 OE1 GLU B 96 12.215 -41.185 -2.410 1.00 71.73 O ANISOU 1605 OE1 GLU B 96 8488 10746 8020 2169 1898 2144 O ATOM 1606 OE2 GLU B 96 10.966 -41.221 -0.600 1.00 79.75 O ANISOU 1606 OE2 GLU B 96 9677 11599 9024 2804 2441 2685 O ATOM 1607 N PHE B 97 16.891 -40.108 -0.511 1.00 44.79 N ANISOU 1607 N PHE B 97 6230 7579 3207 2554 834 805 N ATOM 1608 CA PHE B 97 17.852 -41.092 -0.038 1.00 46.51 C ANISOU 1608 CA PHE B 97 6549 7803 3321 2629 726 786 C ATOM 1609 C PHE B 97 18.726 -40.488 1.051 1.00 49.02 C ANISOU 1609 C PHE B 97 7227 8056 3340 2910 475 513 C ATOM 1610 O PHE B 97 18.904 -41.073 2.122 1.00 52.47 O ANISOU 1610 O PHE B 97 7891 8481 3564 3252 558 629 O ATOM 1611 CB PHE B 97 18.714 -41.559 -1.207 1.00 40.02 C ANISOU 1611 CB PHE B 97 5512 7007 2687 2230 475 609 C ATOM 1612 CG PHE B 97 19.864 -42.449 -0.810 1.00 44.98 C ANISOU 1612 CG PHE B 97 6235 7620 3234 2268 299 538 C ATOM 1613 CD1 PHE B 97 19.639 -43.731 -0.328 1.00 50.77 C ANISOU 1613 CD1 PHE B 97 6955 8386 3951 2423 533 871 C ATOM 1614 CD2 PHE B 97 21.171 -42.013 -0.952 1.00 40.62 C ANISOU 1614 CD2 PHE B 97 5747 6991 2696 2136 -88 175 C ATOM 1615 CE1 PHE B 97 20.698 -44.559 0.016 1.00 50.39 C ANISOU 1615 CE1 PHE B 97 6995 8324 3829 2456 361 810 C ATOM 1616 CE2 PHE B 97 22.237 -42.837 -0.605 1.00 43.07 C ANISOU 1616 CE2 PHE B 97 6120 7268 2974 2164 -263 125 C ATOM 1617 CZ PHE B 97 21.996 -44.111 -0.124 1.00 45.69 C ANISOU 1617 CZ PHE B 97 6475 7664 3223 2326 -51 426 C ATOM 1618 N GLU B 98 19.274 -39.313 0.772 1.00 42.46 N ANISOU 1618 N GLU B 98 6444 7162 2526 2780 163 165 N ATOM 1619 CA GLU B 98 20.136 -38.644 1.734 1.00 44.28 C ANISOU 1619 CA GLU B 98 6987 7288 2549 3032 -138 -104 C ATOM 1620 C GLU B 98 19.352 -38.195 2.990 1.00 49.40 C ANISOU 1620 C GLU B 98 7977 7917 2875 3549 55 23 C ATOM 1621 O GLU B 98 19.911 -38.130 4.081 1.00 53.54 O ANISOU 1621 O GLU B 98 8843 8364 3134 3916 -109 -91 O ATOM 1622 CB GLU B 98 20.862 -37.469 1.068 1.00 42.04 C ANISOU 1622 CB GLU B 98 6612 6901 2459 2763 -489 -450 C ATOM 1623 CG GLU B 98 21.804 -37.887 -0.058 1.00 44.70 C ANISOU 1623 CG GLU B 98 6661 7212 3110 2338 -669 -565 C ATOM 1624 CD GLU B 98 22.060 -36.784 -1.074 1.00 48.33 C ANISOU 1624 CD GLU B 98 6928 7590 3845 2037 -818 -758 C ATOM 1625 OE1 GLU B 98 21.781 -35.601 -0.770 1.00 49.25 O ANISOU 1625 OE1 GLU B 98 7154 7646 3912 2157 -889 -873 O ATOM 1626 OE2 GLU B 98 22.521 -37.099 -2.195 1.00 43.73 O ANISOU 1626 OE2 GLU B 98 6093 6995 3526 1708 -847 -778 O ATOM 1627 N LEU B 99 18.057 -37.909 2.842 1.00 53.68 N ANISOU 1627 N LEU B 99 8441 8509 3446 3612 403 273 N ATOM 1628 CA LEU B 99 17.226 -37.545 4.002 1.00 55.32 C ANISOU 1628 CA LEU B 99 8967 8683 3368 4143 659 462 C ATOM 1629 C LEU B 99 16.879 -38.742 4.890 1.00 59.20 C ANISOU 1629 C LEU B 99 9586 9192 3716 4520 1011 828 C ATOM 1630 O LEU B 99 17.056 -38.695 6.112 1.00 64.21 O ANISOU 1630 O LEU B 99 10628 9765 4004 5031 1017 826 O ATOM 1631 CB LEU B 99 15.936 -36.838 3.568 1.00 54.43 C ANISOU 1631 CB LEU B 99 8709 8589 3384 4100 942 652 C ATOM 1632 CG LEU B 99 15.143 -36.241 4.733 1.00 64.91 C ANISOU 1632 CG LEU B 99 10394 9853 4415 4671 1181 821 C ATOM 1633 CD1 LEU B 99 15.983 -35.186 5.434 1.00 68.41 C ANISOU 1633 CD1 LEU B 99 11234 10203 4557 4922 758 417 C ATOM 1634 CD2 LEU B 99 13.803 -35.651 4.276 1.00 59.93 C ANISOU 1634 CD2 LEU B 99 9578 9227 3967 4614 1504 1069 C ATOM 1635 N ARG B 100 16.367 -39.802 4.270 1.00 57.54 N ANISOU 1635 N ARG B 100 9032 9042 3788 4294 1304 1154 N ATOM 1636 CA ARG B 100 15.948 -41.006 4.982 1.00 65.64 C ANISOU 1636 CA ARG B 100 10082 10061 4798 4608 1694 1570 C ATOM 1637 C ARG B 100 17.105 -41.616 5.772 1.00 66.36 C ANISOU 1637 C ARG B 100 10460 10148 4605 4821 1474 1402 C ATOM 1638 O ARG B 100 16.911 -42.148 6.870 1.00 68.11 O ANISOU 1638 O ARG B 100 10941 10335 4601 5315 1734 1635 O ATOM 1639 CB ARG B 100 15.380 -42.041 4.002 1.00 68.04 C ANISOU 1639 CB ARG B 100 9902 10389 5563 4238 1940 1904 C ATOM 1640 CG ARG B 100 14.825 -43.301 4.665 1.00 76.55 C ANISOU 1640 CG ARG B 100 10906 11411 6767 4534 2387 2405 C ATOM 1641 CD ARG B 100 13.382 -43.094 5.116 1.00 83.67 C ANISOU 1641 CD ARG B 100 11743 12202 7846 4858 2878 2860 C ATOM 1642 NE ARG B 100 13.006 -43.994 6.205 1.00 90.54 N ANISOU 1642 NE ARG B 100 12715 12991 8695 5362 3310 3289 N ATOM 1643 CZ ARG B 100 12.906 -43.620 7.478 1.00 97.66 C ANISOU 1643 CZ ARG B 100 14069 13858 9179 5988 3492 3347 C ATOM 1644 NH1 ARG B 100 13.146 -42.360 7.821 1.00 99.49 N ANISOU 1644 NH1 ARG B 100 14683 14113 9005 6163 3243 2997 N ATOM 1645 NH2 ARG B 100 12.558 -44.499 8.407 1.00101.83 N ANISOU 1645 NH2 ARG B 100 14673 14309 9711 6466 3928 3766 N ATOM 1646 N TYR B 101 18.307 -41.522 5.213 1.00 61.32 N ANISOU 1646 N TYR B 101 9776 9525 3997 4470 1005 1011 N ATOM 1647 CA TYR B 101 19.496 -42.076 5.855 1.00 66.51 C ANISOU 1647 CA TYR B 101 10668 10153 4448 4609 729 827 C ATOM 1648 C TYR B 101 20.478 -40.984 6.231 1.00 67.65 C ANISOU 1648 C TYR B 101 11100 10192 4414 4687 215 357 C ATOM 1649 O TYR B 101 21.688 -41.165 6.097 1.00 65.15 O ANISOU 1649 O TYR B 101 10779 9823 4150 4505 -183 89 O ATOM 1650 CB TYR B 101 20.184 -43.070 4.921 1.00 64.63 C ANISOU 1650 CB TYR B 101 10104 9970 4480 4151 603 820 C ATOM 1651 CG TYR B 101 19.294 -44.218 4.539 1.00 67.27 C ANISOU 1651 CG TYR B 101 10139 10367 5054 4072 1058 1288 C ATOM 1652 CD1 TYR B 101 18.409 -44.107 3.476 1.00 66.62 C ANISOU 1652 CD1 TYR B 101 9692 10311 5311 3751 1241 1455 C ATOM 1653 CD2 TYR B 101 19.319 -45.404 5.257 1.00 71.08 C ANISOU 1653 CD2 TYR B 101 10691 10851 5464 4334 1300 1579 C ATOM 1654 CE1 TYR B 101 17.581 -45.145 3.135 1.00 70.01 C ANISOU 1654 CE1 TYR B 101 9808 10733 6061 3678 1621 1904 C ATOM 1655 CE2 TYR B 101 18.497 -46.451 4.920 1.00 73.52 C ANISOU 1655 CE2 TYR B 101 10672 11162 6098 4257 1714 2041 C ATOM 1656 CZ TYR B 101 17.631 -46.315 3.859 1.00 76.76 C ANISOU 1656 CZ TYR B 101 10697 11564 6904 3923 1857 2203 C ATOM 1657 OH TYR B 101 16.807 -47.355 3.519 1.00 82.91 O ANISOU 1657 OH TYR B 101 11105 12274 8122 3833 2222 2674 O ATOM 1658 N ARG B 102 19.948 -39.866 6.715 1.00 70.57 N ANISOU 1658 N ARG B 102 11703 10500 4611 4974 224 285 N ATOM 1659 CA ARG B 102 20.740 -38.665 6.970 1.00 75.08 C ANISOU 1659 CA ARG B 102 12501 10931 5094 5034 -271 -146 C ATOM 1660 C ARG B 102 21.967 -38.925 7.835 1.00 79.09 C ANISOU 1660 C ARG B 102 13336 11313 5403 5290 -676 -398 C ATOM 1661 O ARG B 102 23.063 -38.477 7.503 1.00 78.60 O ANISOU 1661 O ARG B 102 13201 11132 5532 5041 -1160 -741 O ATOM 1662 CB ARG B 102 19.873 -37.568 7.600 1.00 78.89 C ANISOU 1662 CB ARG B 102 13276 11356 5341 5444 -151 -123 C ATOM 1663 CG ARG B 102 20.350 -36.156 7.302 0.00 81.87 C ANISOU 1663 CG ARG B 102 13678 11610 5817 5301 -594 -511 C ATOM 1664 CD ARG B 102 19.726 -35.633 6.019 0.00 79.83 C ANISOU 1664 CD ARG B 102 12986 11443 5903 4801 -453 -460 C ATOM 1665 NE ARG B 102 20.639 -34.786 5.257 0.00 80.26 N ANISOU 1665 NE ARG B 102 12849 11397 6248 4414 -897 -820 N ATOM 1666 CZ ARG B 102 20.317 -34.182 4.118 1.00 79.24 C ANISOU 1666 CZ ARG B 102 12379 11312 6418 3992 -856 -846 C ATOM 1667 NH1 ARG B 102 19.099 -34.323 3.611 1.00 78.47 N ANISOU 1667 NH1 ARG B 102 12103 11351 6362 3890 -438 -563 N ATOM 1668 NH2 ARG B 102 21.211 -33.430 3.487 1.00 77.66 N ANISOU 1668 NH2 ARG B 102 12014 10992 6501 3695 -1227 -1139 N ATOM 1669 N ARG B 103 21.779 -39.652 8.933 1.00 82.80 N ANISOU 1669 N ARG B 103 14154 11786 5522 5802 -467 -207 N ATOM 1670 CA ARG B 103 22.874 -39.955 9.851 1.00 84.32 C ANISOU 1670 CA ARG B 103 14713 11848 5477 6114 -847 -433 C ATOM 1671 C ARG B 103 23.935 -40.847 9.216 1.00 77.80 C ANISOU 1671 C ARG B 103 13582 11047 4930 5658 -1083 -516 C ATOM 1672 O ARG B 103 25.111 -40.488 9.164 1.00 75.47 O ANISOU 1672 O ARG B 103 13303 10596 4775 5518 -1619 -865 O ATOM 1673 CB ARG B 103 22.349 -40.636 11.111 1.00 88.93 C ANISOU 1673 CB ARG B 103 15735 12444 5609 6787 -489 -157 C ATOM 1674 CG ARG B 103 23.462 -41.138 12.018 1.00 94.13 C ANISOU 1674 CG ARG B 103 16774 12980 6010 7105 -862 -364 C ATOM 1675 CD ARG B 103 22.992 -42.290 12.878 1.00 97.06 C ANISOU 1675 CD ARG B 103 17384 13433 6062 7579 -387 16 C ATOM 1676 NE ARG B 103 24.016 -42.722 13.823 1.00101.74 N ANISOU 1676 NE ARG B 103 18406 13901 6351 7945 -754 -191 N ATOM 1677 CZ ARG B 103 24.081 -42.318 15.086 1.00108.70 C ANISOU 1677 CZ ARG B 103 19940 14618 6742 8681 -889 -320 C ATOM 1678 NH1 ARG B 103 23.176 -41.466 15.552 1.00111.81 N ANISOU 1678 NH1 ARG B 103 20629 14959 6895 9132 -664 -243 N ATOM 1679 NH2 ARG B 103 25.047 -42.761 15.882 1.00112.89 N ANISOU 1679 NH2 ARG B 103 20853 15023 7018 8989 -1264 -522 N ATOM 1680 N ALA B 104 23.511 -42.019 8.758 1.00 74.30 N ANISOU 1680 N ALA B 104 12859 10772 4600 5456 -683 -170 N ATOM 1681 CA ALA B 104 24.411 -42.963 8.112 1.00 73.42 C ANISOU 1681 CA ALA B 104 12458 10695 4743 5045 -854 -191 C ATOM 1682 C ALA B 104 25.074 -42.347 6.879 1.00 66.60 C ANISOU 1682 C ALA B 104 11213 9783 4310 4468 -1191 -451 C ATOM 1683 O ALA B 104 26.268 -42.541 6.653 1.00 64.05 O ANISOU 1683 O ALA B 104 10796 9362 4177 4258 -1582 -657 O ATOM 1684 CB ALA B 104 23.668 -44.239 7.741 1.00 73.98 C ANISOU 1684 CB ALA B 104 12274 10934 4901 4935 -342 254 C ATOM 1685 N PHE B 105 24.305 -41.600 6.088 1.00 64.27 N ANISOU 1685 N PHE B 105 10695 9539 4187 4237 -1026 -422 N ATOM 1686 CA PHE B 105 24.867 -40.965 4.897 1.00 63.19 C ANISOU 1686 CA PHE B 105 10209 9348 4451 3734 -1285 -640 C ATOM 1687 C PHE B 105 25.961 -39.979 5.291 1.00 65.60 C ANISOU 1687 C PHE B 105 10670 9426 4827 3810 -1817 -1026 C ATOM 1688 O PHE B 105 27.045 -39.979 4.710 1.00 56.24 O ANISOU 1688 O PHE B 105 9261 8132 3976 3504 -2131 -1194 O ATOM 1689 CB PHE B 105 23.790 -40.269 4.052 1.00 61.76 C ANISOU 1689 CB PHE B 105 9810 9252 4404 3525 -1016 -544 C ATOM 1690 CG PHE B 105 24.326 -39.617 2.810 1.00 56.30 C ANISOU 1690 CG PHE B 105 8783 8502 4106 3052 -1229 -740 C ATOM 1691 CD1 PHE B 105 24.755 -40.385 1.741 1.00 53.28 C ANISOU 1691 CD1 PHE B 105 8075 8165 4006 2661 -1211 -680 C ATOM 1692 CD2 PHE B 105 24.403 -38.234 2.714 1.00 60.38 C ANISOU 1692 CD2 PHE B 105 9326 8901 4714 3035 -1432 -968 C ATOM 1693 CE1 PHE B 105 25.256 -39.793 0.594 1.00 51.18 C ANISOU 1693 CE1 PHE B 105 7524 7826 4094 2284 -1355 -829 C ATOM 1694 CE2 PHE B 105 24.901 -37.631 1.571 1.00 56.16 C ANISOU 1694 CE2 PHE B 105 8480 8298 4561 2634 -1576 -1107 C ATOM 1695 CZ PHE B 105 25.331 -38.415 0.513 1.00 52.01 C ANISOU 1695 CZ PHE B 105 7643 7816 4301 2270 -1520 -1029 C ATOM 1696 N ASER B 106 25.673 -39.146 6.285 0.50 70.48 N ANISOU 1696 N ASER B 106 11673 9945 5159 4250 -1918 -1146 N ATOM 1697 N BSER B 106 25.667 -39.140 6.279 0.50 70.45 N ANISOU 1697 N BSER B 106 11669 9942 5157 4249 -1917 -1146 N ATOM 1698 CA ASER B 106 26.648 -38.183 6.779 0.50 73.87 C ANISOU 1698 CA ASER B 106 12298 10108 5659 4400 -2469 -1518 C ATOM 1699 CA BSER B 106 26.643 -38.185 6.791 0.50 73.92 C ANISOU 1699 CA BSER B 106 12310 10115 5661 4406 -2468 -1517 C ATOM 1700 C ASER B 106 27.790 -38.878 7.527 0.50 76.52 C ANISOU 1700 C ASER B 106 12836 10302 5936 4587 -2831 -1651 C ATOM 1701 C BSER B 106 27.800 -38.907 7.481 0.50 76.29 C ANISOU 1701 C BSER B 106 12787 10278 5921 4565 -2825 -1646 C ATOM 1702 O ASER B 106 28.918 -38.388 7.543 0.50 77.96 O ANISOU 1702 O ASER B 106 12989 10234 6400 4514 -3341 -1941 O ATOM 1703 O BSER B 106 28.946 -38.464 7.412 0.50 77.21 O ANISOU 1703 O BSER B 106 12838 10154 6344 4454 -3321 -1924 O ATOM 1704 CB ASER B 106 25.967 -37.151 7.677 0.50 79.10 C ANISOU 1704 CB ASER B 106 13375 10687 5992 4888 -2494 -1606 C ATOM 1705 CB BSER B 106 25.983 -37.210 7.768 0.50 79.54 C ANISOU 1705 CB BSER B 106 13463 10740 6019 4924 -2497 -1603 C ATOM 1706 OG ASER B 106 24.855 -36.567 7.020 0.50 76.24 O ANISOU 1706 OG ASER B 106 12824 10463 5679 4726 -2140 -1452 O ATOM 1707 OG BSER B 106 25.581 -37.871 8.957 0.50 84.17 O ANISOU 1707 OG BSER B 106 14494 11369 6119 5476 -2313 -1455 O ATOM 1708 N ASP B 107 27.490 -40.020 8.142 1.00 76.48 N ANISOU 1708 N ASP B 107 13021 10435 5603 4835 -2566 -1423 N ATOM 1709 CA ASP B 107 28.500 -40.796 8.863 1.00 80.87 C ANISOU 1709 CA ASP B 107 13780 10881 6066 5023 -2875 -1516 C ATOM 1710 C ASP B 107 29.609 -41.307 7.939 1.00 77.84 C ANISOU 1710 C ASP B 107 12957 10450 6169 4506 -3114 -1572 C ATOM 1711 O ASP B 107 30.791 -41.050 8.170 1.00 74.24 O ANISOU 1711 O ASP B 107 12529 9743 5938 4504 -3636 -1841 O ATOM 1712 CB ASP B 107 27.869 -41.991 9.594 1.00 81.47 C ANISOU 1712 CB ASP B 107 14099 11138 5716 5369 -2454 -1193 C ATOM 1713 CG ASP B 107 27.501 -41.680 11.034 1.00 85.43 C ANISOU 1713 CG ASP B 107 15230 11545 5683 6099 -2463 -1241 C ATOM 1714 OD1 ASP B 107 27.891 -40.606 11.539 1.00 89.33 O ANISOU 1714 OD1 ASP B 107 16015 11804 6123 6353 -2901 -1574 O ATOM 1715 OD2 ASP B 107 26.825 -42.523 11.660 1.00 87.96 O ANISOU 1715 OD2 ASP B 107 15763 12005 5652 6451 -2026 -931 O ATOM 1716 N LEU B 108 29.235 -42.036 6.895 1.00 70.42 N ANISOU 1716 N LEU B 108 11617 9721 5420 4097 -2746 -1312 N ATOM 1717 CA LEU B 108 30.255 -42.637 6.045 1.00 67.54 C ANISOU 1717 CA LEU B 108 10867 9315 5481 3675 -2925 -1322 C ATOM 1718 C LEU B 108 30.868 -41.666 5.040 1.00 63.44 C ANISOU 1718 C LEU B 108 9995 8637 5472 3293 -3159 -1518 C ATOM 1719 O LEU B 108 32.018 -41.838 4.634 1.00 63.14 O ANISOU 1719 O LEU B 108 9717 8442 5833 3071 -3451 -1614 O ATOM 1720 CB LEU B 108 29.771 -43.940 5.394 1.00 64.96 C ANISOU 1720 CB LEU B 108 10301 9225 5154 3457 -2506 -978 C ATOM 1721 CG LEU B 108 28.392 -44.037 4.756 1.00 61.66 C ANISOU 1721 CG LEU B 108 9748 9021 4660 3346 -1991 -716 C ATOM 1722 CD1 LEU B 108 28.503 -43.877 3.255 1.00 62.04 C ANISOU 1722 CD1 LEU B 108 9351 9088 5133 2846 -1952 -720 C ATOM 1723 CD2 LEU B 108 27.735 -45.359 5.105 1.00 59.87 C ANISOU 1723 CD2 LEU B 108 9592 8962 4194 3511 -1606 -361 C ATOM 1724 N THR B 109 30.119 -40.633 4.661 1.00 62.69 N ANISOU 1724 N THR B 109 9864 8565 5391 3241 -3020 -1558 N ATOM 1725 CA THR B 109 30.687 -39.580 3.826 1.00 66.32 C ANISOU 1725 CA THR B 109 10034 8845 6319 2948 -3239 -1739 C ATOM 1726 C THR B 109 31.754 -38.796 4.587 1.00 72.60 C ANISOU 1726 C THR B 109 11000 9289 7297 3159 -3815 -2058 C ATOM 1727 O THR B 109 32.686 -38.267 3.988 1.00 75.96 O ANISOU 1727 O THR B 109 11136 9482 8243 2919 -4087 -2190 O ATOM 1728 CB THR B 109 29.621 -38.607 3.289 1.00 68.86 C ANISOU 1728 CB THR B 109 10296 9262 6604 2866 -2977 -1708 C ATOM 1729 OG1 THR B 109 28.772 -38.185 4.363 1.00 74.52 O ANISOU 1729 OG1 THR B 109 11430 10012 6873 3302 -2919 -1730 O ATOM 1730 CG2 THR B 109 28.787 -39.278 2.213 1.00 64.05 C ANISOU 1730 CG2 THR B 109 9415 8912 6010 2559 -2505 -1435 C ATOM 1731 N SER B 110 31.621 -38.726 5.907 1.00 75.59 N ANISOU 1731 N SER B 110 11858 9592 7269 3641 -4007 -2175 N ATOM 1732 CA SER B 110 32.637 -38.071 6.723 1.00 80.51 C ANISOU 1732 CA SER B 110 12707 9832 8052 3901 -4629 -2503 C ATOM 1733 C SER B 110 33.881 -38.953 6.890 1.00 79.37 C ANISOU 1733 C SER B 110 12468 9532 8158 3831 -4950 -2546 C ATOM 1734 O SER B 110 34.885 -38.511 7.444 1.00 83.40 O ANISOU 1734 O SER B 110 13090 9667 8930 3987 -5522 -2816 O ATOM 1735 CB SER B 110 32.072 -37.674 8.091 1.00 90.07 C ANISOU 1735 CB SER B 110 14529 10985 8710 4512 -4754 -2632 C ATOM 1736 OG SER B 110 31.996 -38.789 8.966 1.00 96.38 O ANISOU 1736 OG SER B 110 15658 11903 9060 4832 -4658 -2519 O ATOM 1737 N GLN B 111 33.812 -40.198 6.419 1.00 73.27 N ANISOU 1737 N GLN B 111 11488 9017 7334 3612 -4611 -2279 N ATOM 1738 CA GLN B 111 34.972 -41.095 6.469 1.00 76.93 C ANISOU 1738 CA GLN B 111 11809 9356 8065 3513 -4875 -2279 C ATOM 1739 C GLN B 111 35.732 -41.124 5.144 1.00 74.21 C ANISOU 1739 C GLN B 111 10879 8931 8384 3010 -4851 -2207 C ATOM 1740 O GLN B 111 36.740 -41.826 5.013 1.00 73.67 O ANISOU 1740 O GLN B 111 10607 8741 8642 2884 -5038 -2179 O ATOM 1741 CB GLN B 111 34.565 -42.522 6.860 1.00 78.03 C ANISOU 1741 CB GLN B 111 12100 9783 7765 3638 -4566 -2022 C ATOM 1742 CG GLN B 111 34.023 -42.673 8.275 1.00 84.79 C ANISOU 1742 CG GLN B 111 13558 10675 7982 4207 -4588 -2061 C ATOM 1743 CD GLN B 111 35.069 -42.429 9.343 1.00 91.36 C ANISOU 1743 CD GLN B 111 14728 11153 8834 4552 -5232 -2375 C ATOM 1744 OE1 GLN B 111 36.268 -42.573 9.106 1.00 91.47 O ANISOU 1744 OE1 GLN B 111 14491 10926 9335 4345 -5632 -2491 O ATOM 1745 NE2 GLN B 111 34.617 -42.053 10.533 1.00 99.21 N ANISOU 1745 NE2 GLN B 111 16303 12080 9312 5112 -5343 -2509 N ATOM 1746 N LEU B 112 35.239 -40.371 4.163 1.00 71.17 N ANISOU 1746 N LEU B 112 10236 8609 8195 2752 -4599 -2162 N ATOM 1747 CA LEU B 112 35.896 -40.272 2.864 1.00 68.95 C ANISOU 1747 CA LEU B 112 9435 8235 8526 2334 -4523 -2082 C ATOM 1748 C LEU B 112 37.271 -39.638 3.022 1.00 74.34 C ANISOU 1748 C LEU B 112 9965 8445 9837 2318 -5057 -2295 C ATOM 1749 O LEU B 112 37.387 -38.511 3.497 1.00 73.15 O ANISOU 1749 O LEU B 112 9964 8021 9809 2481 -5397 -2527 O ATOM 1750 CB LEU B 112 35.066 -39.431 1.888 1.00 61.70 C ANISOU 1750 CB LEU B 112 8343 7443 7657 2130 -4186 -2020 C ATOM 1751 CG LEU B 112 33.651 -39.894 1.524 1.00 58.07 C ANISOU 1751 CG LEU B 112 7964 7387 6715 2092 -3663 -1805 C ATOM 1752 CD1 LEU B 112 33.082 -39.090 0.356 1.00 58.23 C ANISOU 1752 CD1 LEU B 112 7737 7472 6918 1834 -3389 -1752 C ATOM 1753 CD2 LEU B 112 33.635 -41.366 1.206 1.00 57.28 C ANISOU 1753 CD2 LEU B 112 7758 7495 6510 1988 -3420 -1572 C ATOM 1754 N HIS B 113 38.309 -40.362 2.619 1.00 77.16 N ANISOU 1754 N HIS B 113 10010 8670 10636 2133 -5139 -2204 N ATOM 1755 CA HIS B 113 39.666 -39.827 2.649 1.00 80.86 C ANISOU 1755 CA HIS B 113 10249 8634 11840 2076 -5615 -2353 C ATOM 1756 C HIS B 113 40.144 -39.578 1.226 1.00 75.09 C ANISOU 1756 C HIS B 113 8973 7797 11759 1703 -5346 -2174 C ATOM 1757 O HIS B 113 40.591 -40.498 0.543 1.00 70.46 O ANISOU 1757 O HIS B 113 8095 7290 11387 1515 -5107 -1962 O ATOM 1758 CB HIS B 113 40.604 -40.792 3.368 1.00 86.54 C ANISOU 1758 CB HIS B 113 11026 9203 12652 2189 -5950 -2380 C ATOM 1759 CG HIS B 113 42.029 -40.331 3.410 1.00 91.76 C ANISOU 1759 CG HIS B 113 11421 9292 14151 2120 -6458 -2509 C ATOM 1760 ND1 HIS B 113 42.537 -39.578 4.446 1.00 98.33 N ANISOU 1760 ND1 HIS B 113 12522 9690 15148 2392 -7106 -2824 N ATOM 1761 CD2 HIS B 113 43.047 -40.515 2.541 1.00 93.53 C ANISOU 1761 CD2 HIS B 113 11133 9264 15141 1830 -6413 -2352 C ATOM 1762 CE1 HIS B 113 43.810 -39.318 4.210 1.00104.10 C ANISOU 1762 CE1 HIS B 113 12891 9904 16759 2244 -7467 -2853 C ATOM 1763 NE2 HIS B 113 44.147 -39.874 3.062 1.00101.97 N ANISOU 1763 NE2 HIS B 113 12134 9736 16873 1901 -7027 -2552 N ATOM 1764 N ILE B 114 40.046 -38.323 0.791 1.00 77.15 N ANISOU 1764 N ILE B 114 9116 7865 12334 1631 -5373 -2251 N ATOM 1765 CA ILE B 114 40.221 -37.964 -0.614 1.00 65.44 C ANISOU 1765 CA ILE B 114 7181 6337 11346 1322 -5010 -2053 C ATOM 1766 C ILE B 114 41.482 -37.159 -0.903 1.00 70.14 C ANISOU 1766 C ILE B 114 7416 6343 12891 1215 -5315 -2078 C ATOM 1767 O ILE B 114 41.720 -36.125 -0.292 1.00 74.57 O ANISOU 1767 O ILE B 114 8082 6542 13711 1353 -5759 -2300 O ATOM 1768 CB ILE B 114 39.027 -37.130 -1.107 1.00 64.90 C ANISOU 1768 CB ILE B 114 7203 6517 10941 1291 -4698 -2050 C ATOM 1769 CG1 ILE B 114 37.721 -37.862 -0.817 1.00 67.01 C ANISOU 1769 CG1 ILE B 114 7805 7304 10353 1395 -4386 -1995 C ATOM 1770 CG2 ILE B 114 39.170 -36.816 -2.591 1.00 62.63 C ANISOU 1770 CG2 ILE B 114 6490 6201 11107 1006 -4294 -1832 C ATOM 1771 CD1 ILE B 114 36.502 -37.055 -1.143 1.00 65.62 C ANISOU 1771 CD1 ILE B 114 7749 7348 9836 1392 -4123 -2003 C ATOM 1772 N THR B 115 42.272 -37.642 -1.855 1.00 69.56 N ANISOU 1772 N THR B 115 6914 6146 13368 989 -5060 -1828 N ATOM 1773 CA THR B 115 43.448 -36.937 -2.348 1.00 77.15 C ANISOU 1773 CA THR B 115 7456 6530 15327 852 -5206 -1743 C ATOM 1774 C THR B 115 43.454 -37.094 -3.861 1.00 70.27 C ANISOU 1774 C THR B 115 6210 5773 14715 616 -4561 -1399 C ATOM 1775 O THR B 115 42.896 -38.070 -4.375 1.00 65.46 O ANISOU 1775 O THR B 115 5646 5614 13613 572 -4131 -1252 O ATOM 1776 CB THR B 115 44.754 -37.537 -1.782 1.00 79.28 C ANISOU 1776 CB THR B 115 7579 6392 16153 873 -5609 -1750 C ATOM 1777 OG1 THR B 115 44.872 -38.906 -2.192 1.00 76.21 O ANISOU 1777 OG1 THR B 115 7089 6309 15560 789 -5248 -1532 O ATOM 1778 CG2 THR B 115 44.782 -37.452 -0.259 1.00 88.25 C ANISOU 1778 CG2 THR B 115 9140 7395 16995 1158 -6276 -2103 C ATOM 1779 N PRO B 116 44.080 -36.143 -4.583 1.00 73.02 N ANISOU 1779 N PRO B 116 6206 5686 15853 493 -4487 -1257 N ATOM 1780 CA PRO B 116 44.069 -36.184 -6.049 1.00 70.29 C ANISOU 1780 CA PRO B 116 5554 5421 15732 321 -3830 -908 C ATOM 1781 C PRO B 116 44.599 -37.497 -6.609 1.00 69.45 C ANISOU 1781 C PRO B 116 5271 5431 15685 256 -3470 -647 C ATOM 1782 O PRO B 116 44.029 -38.016 -7.574 1.00 64.78 O ANISOU 1782 O PRO B 116 4676 5205 14731 215 -2917 -458 O ATOM 1783 CB PRO B 116 44.987 -35.023 -6.437 1.00 80.58 C ANISOU 1783 CB PRO B 116 6495 6079 18044 242 -3923 -774 C ATOM 1784 CG PRO B 116 44.873 -34.070 -5.293 1.00 82.47 C ANISOU 1784 CG PRO B 116 6949 6062 18324 383 -4586 -1135 C ATOM 1785 CD PRO B 116 44.800 -34.958 -4.082 1.00 84.42 C ANISOU 1785 CD PRO B 116 7536 6507 18034 539 -5003 -1397 C ATOM 1786 N GLY B 117 45.641 -38.043 -5.985 1.00 73.44 N ANISOU 1786 N GLY B 117 5658 5623 16624 272 -3804 -655 N ATOM 1787 CA GLY B 117 46.255 -39.275 -6.448 1.00 73.26 C ANISOU 1787 CA GLY B 117 5450 5655 16731 225 -3493 -405 C ATOM 1788 C GLY B 117 45.469 -40.553 -6.183 1.00 68.22 C ANISOU 1788 C GLY B 117 5107 5594 15220 310 -3374 -482 C ATOM 1789 O GLY B 117 45.680 -41.559 -6.858 1.00 66.62 O ANISOU 1789 O GLY B 117 4780 5535 14999 285 -2969 -253 O ATOM 1790 N THR B 118 44.567 -40.518 -5.206 1.00 66.29 N ANISOU 1790 N THR B 118 5261 5649 14276 435 -3705 -779 N ATOM 1791 CA THR B 118 43.833 -41.713 -4.800 1.00 62.52 C ANISOU 1791 CA THR B 118 5070 5656 13028 534 -3639 -830 C ATOM 1792 C THR B 118 42.322 -41.609 -5.051 1.00 57.02 C ANISOU 1792 C THR B 118 4657 5450 11557 569 -3369 -888 C ATOM 1793 O THR B 118 41.580 -42.546 -4.761 1.00 53.97 O ANISOU 1793 O THR B 118 4506 5444 10555 650 -3283 -900 O ATOM 1794 CB THR B 118 44.025 -41.994 -3.311 1.00 65.59 C ANISOU 1794 CB THR B 118 5741 5990 13192 699 -4221 -1078 C ATOM 1795 OG1 THR B 118 43.426 -40.944 -2.548 1.00 66.64 O ANISOU 1795 OG1 THR B 118 6172 6097 13053 817 -4555 -1345 O ATOM 1796 CG2 THR B 118 45.514 -42.096 -2.964 1.00 73.45 C ANISOU 1796 CG2 THR B 118 6467 6458 14984 669 -4579 -1051 C ATOM 1797 N ALA B 119 41.886 -40.469 -5.576 1.00 56.20 N ANISOU 1797 N ALA B 119 4517 5299 11536 509 -3245 -907 N ATOM 1798 CA ALA B 119 40.459 -40.193 -5.783 1.00 51.62 C ANISOU 1798 CA ALA B 119 4192 5126 10295 534 -3035 -974 C ATOM 1799 C ALA B 119 39.762 -41.264 -6.629 1.00 47.00 C ANISOU 1799 C ALA B 119 3619 4923 9314 506 -2571 -802 C ATOM 1800 O ALA B 119 38.691 -41.756 -6.272 1.00 43.97 O ANISOU 1800 O ALA B 119 3518 4895 8295 576 -2541 -868 O ATOM 1801 CB ALA B 119 40.278 -38.818 -6.401 1.00 51.87 C ANISOU 1801 CB ALA B 119 4109 4993 10608 456 -2936 -975 C ATOM 1802 N TYR B 120 40.375 -41.638 -7.742 1.00 47.02 N ANISOU 1802 N TYR B 120 3332 4813 9722 429 -2199 -568 N ATOM 1803 CA TYR B 120 39.777 -42.652 -8.587 1.00 44.82 C ANISOU 1803 CA TYR B 120 3083 4828 9117 448 -1783 -429 C ATOM 1804 C TYR B 120 39.669 -44.013 -7.890 1.00 42.61 C ANISOU 1804 C TYR B 120 2951 4739 8501 533 -1917 -453 C ATOM 1805 O TYR B 120 38.712 -44.756 -8.096 1.00 39.64 O ANISOU 1805 O TYR B 120 2738 4664 7661 577 -1753 -443 O ATOM 1806 CB TYR B 120 40.538 -42.817 -9.895 1.00 44.49 C ANISOU 1806 CB TYR B 120 2764 4592 9550 417 -1312 -158 C ATOM 1807 CG TYR B 120 39.966 -43.969 -10.670 1.00 41.48 C ANISOU 1807 CG TYR B 120 2476 4470 8817 496 -928 -56 C ATOM 1808 CD1 TYR B 120 38.743 -43.843 -11.313 1.00 38.00 C ANISOU 1808 CD1 TYR B 120 2205 4292 7942 523 -698 -96 C ATOM 1809 CD2 TYR B 120 40.605 -45.210 -10.708 1.00 42.41 C ANISOU 1809 CD2 TYR B 120 2531 4543 9041 559 -831 59 C ATOM 1810 CE1 TYR B 120 38.185 -44.900 -11.989 1.00 35.84 C ANISOU 1810 CE1 TYR B 120 2045 4191 7381 620 -398 -41 C ATOM 1811 CE2 TYR B 120 40.050 -46.280 -11.394 1.00 42.89 C ANISOU 1811 CE2 TYR B 120 2713 4793 8789 661 -505 125 C ATOM 1812 CZ TYR B 120 38.839 -46.113 -12.034 1.00 42.20 C ANISOU 1812 CZ TYR B 120 2806 4928 8299 697 -300 66 C ATOM 1813 OH TYR B 120 38.244 -47.145 -12.721 1.00 36.80 O ANISOU 1813 OH TYR B 120 2279 4366 7338 820 -10 97 O ATOM 1814 N GLN B 121 40.669 -44.338 -7.081 1.00 46.03 N ANISOU 1814 N GLN B 121 3317 4958 9216 561 -2227 -475 N ATOM 1815 CA GLN B 121 40.707 -45.626 -6.409 1.00 49.71 C ANISOU 1815 CA GLN B 121 3904 5565 9419 654 -2353 -469 C ATOM 1816 C GLN B 121 39.591 -45.696 -5.390 1.00 44.28 C ANISOU 1816 C GLN B 121 3599 5170 8054 757 -2575 -626 C ATOM 1817 O GLN B 121 38.937 -46.728 -5.246 1.00 42.62 O ANISOU 1817 O GLN B 121 3544 5211 7438 826 -2476 -567 O ATOM 1818 CB GLN B 121 42.054 -45.826 -5.715 1.00 57.38 C ANISOU 1818 CB GLN B 121 4725 6206 10869 667 -2679 -472 C ATOM 1819 CG GLN B 121 43.247 -45.743 -6.647 1.00 60.99 C ANISOU 1819 CG GLN B 121 4790 6310 12072 568 -2434 -264 C ATOM 1820 CD GLN B 121 44.564 -45.714 -5.891 0.00 64.52 C ANISOU 1820 CD GLN B 121 5067 6357 13091 557 -2834 -285 C ATOM 1821 OE1 GLN B 121 44.696 -46.322 -4.828 0.00 65.35 O ANISOU 1821 OE1 GLN B 121 5336 6506 12986 652 -3205 -405 O ATOM 1822 NE2 GLN B 121 45.542 -44.996 -6.431 0.00 67.60 N ANISOU 1822 NE2 GLN B 121 5129 6322 14233 451 -2762 -152 N ATOM 1823 N SER B 122 39.383 -44.598 -4.677 1.00 45.76 N ANISOU 1823 N SER B 122 3948 5290 8148 789 -2854 -807 N ATOM 1824 CA SER B 122 38.279 -44.517 -3.734 1.00 53.69 C ANISOU 1824 CA SER B 122 5347 6547 8506 922 -2980 -928 C ATOM 1825 C SER B 122 36.948 -44.654 -4.467 1.00 40.26 C ANISOU 1825 C SER B 122 3735 5158 6406 872 -2609 -847 C ATOM 1826 O SER B 122 36.065 -45.376 -4.023 1.00 39.75 O ANISOU 1826 O SER B 122 3908 5335 5859 964 -2541 -801 O ATOM 1827 CB SER B 122 38.319 -43.199 -2.966 1.00 47.59 C ANISOU 1827 CB SER B 122 4730 5595 7758 994 -3307 -1145 C ATOM 1828 OG SER B 122 39.490 -43.141 -2.183 1.00 52.43 O ANISOU 1828 OG SER B 122 5305 5882 8734 1069 -3728 -1251 O ATOM 1829 N PHE B 123 36.828 -43.969 -5.596 1.00 38.57 N ANISOU 1829 N PHE B 123 3325 4901 6428 738 -2370 -814 N ATOM 1830 CA PHE B 123 35.600 -44.030 -6.393 1.00 34.74 C ANISOU 1830 CA PHE B 123 2913 4665 5622 689 -2055 -763 C ATOM 1831 C PHE B 123 35.284 -45.459 -6.814 1.00 41.52 C ANISOU 1831 C PHE B 123 3765 5682 6330 712 -1859 -633 C ATOM 1832 O PHE B 123 34.180 -45.971 -6.584 1.00 31.05 O ANISOU 1832 O PHE B 123 2658 4579 4562 758 -1790 -615 O ATOM 1833 CB PHE B 123 35.726 -43.133 -7.627 1.00 33.94 C ANISOU 1833 CB PHE B 123 2579 4452 5864 571 -1822 -732 C ATOM 1834 CG PHE B 123 34.618 -43.309 -8.617 1.00 32.36 C ANISOU 1834 CG PHE B 123 2423 4466 5408 536 -1507 -691 C ATOM 1835 CD1 PHE B 123 33.415 -42.620 -8.460 1.00 31.79 C ANISOU 1835 CD1 PHE B 123 2567 4562 4950 523 -1501 -781 C ATOM 1836 CD2 PHE B 123 34.776 -44.152 -9.717 1.00 32.60 C ANISOU 1836 CD2 PHE B 123 2294 4496 5597 543 -1204 -575 C ATOM 1837 CE1 PHE B 123 32.383 -42.781 -9.373 1.00 29.98 C ANISOU 1837 CE1 PHE B 123 2384 4511 4497 491 -1247 -767 C ATOM 1838 CE2 PHE B 123 33.735 -44.314 -10.643 1.00 27.94 C ANISOU 1838 CE2 PHE B 123 1834 4064 4717 528 -914 -571 C ATOM 1839 CZ PHE B 123 32.553 -43.635 -10.466 1.00 29.74 C ANISOU 1839 CZ PHE B 123 2258 4468 4572 487 -961 -670 C ATOM 1840 N GLU B 124 36.267 -46.096 -7.436 1.00 35.74 N ANISOU 1840 N GLU B 124 2777 4794 6008 694 -1749 -527 N ATOM 1841 CA GLU B 124 36.101 -47.444 -7.955 1.00 36.51 C ANISOU 1841 CA GLU B 124 2842 4972 6057 739 -1554 -416 C ATOM 1842 C GLU B 124 35.868 -48.489 -6.866 1.00 32.96 C ANISOU 1842 C GLU B 124 2590 4645 5290 842 -1751 -387 C ATOM 1843 O GLU B 124 35.075 -49.400 -7.056 1.00 31.67 O ANISOU 1843 O GLU B 124 2527 4630 4877 887 -1634 -330 O ATOM 1844 CB GLU B 124 37.323 -47.849 -8.765 1.00 45.54 C ANISOU 1844 CB GLU B 124 3697 5873 7731 735 -1344 -283 C ATOM 1845 CG GLU B 124 36.960 -48.470 -10.076 1.00 49.14 C ANISOU 1845 CG GLU B 124 4133 6342 8197 770 -915 -193 C ATOM 1846 CD GLU B 124 38.018 -49.417 -10.576 1.00 48.91 C ANISOU 1846 CD GLU B 124 3930 6112 8543 854 -694 -29 C ATOM 1847 OE1 GLU B 124 38.997 -49.654 -9.836 1.00 47.43 O ANISOU 1847 OE1 GLU B 124 3638 5802 8580 842 -908 10 O ATOM 1848 OE2 GLU B 124 37.843 -49.917 -11.706 1.00 49.55 O ANISOU 1848 OE2 GLU B 124 4160 6160 8508 907 -270 49 O ATOM 1849 N GLN B 125 36.564 -48.367 -5.742 1.00 37.36 N ANISOU 1849 N GLN B 125 3208 5114 5873 901 -2048 -423 N ATOM 1850 CA GLN B 125 36.374 -49.331 -4.654 1.00 42.91 C ANISOU 1850 CA GLN B 125 4125 5925 6254 1043 -2207 -366 C ATOM 1851 C GLN B 125 34.939 -49.251 -4.115 1.00 39.86 C ANISOU 1851 C GLN B 125 4058 5779 5309 1121 -2148 -360 C ATOM 1852 O GLN B 125 34.288 -50.274 -3.885 1.00 34.72 O ANISOU 1852 O GLN B 125 3528 5262 4400 1211 -2048 -220 O ATOM 1853 CB GLN B 125 37.401 -49.126 -3.540 1.00 42.34 C ANISOU 1853 CB GLN B 125 4092 5690 6305 1129 -2562 -442 C ATOM 1854 CG GLN B 125 38.794 -49.619 -3.914 1.00 49.20 C ANISOU 1854 CG GLN B 125 4652 6316 7727 1080 -2599 -380 C ATOM 1855 CD GLN B 125 39.868 -49.212 -2.908 1.00 59.37 C ANISOU 1855 CD GLN B 125 5947 7370 9239 1141 -3011 -497 C ATOM 1856 OE1 GLN B 125 39.569 -48.666 -1.843 1.00 60.87 O ANISOU 1856 OE1 GLN B 125 6422 7588 9117 1263 -3290 -640 O ATOM 1857 NE2 GLN B 125 41.125 -49.476 -3.247 1.00 64.51 N ANISOU 1857 NE2 GLN B 125 6298 7755 10457 1077 -3048 -437 N ATOM 1858 N VAL B 126 34.451 -48.031 -3.923 1.00 36.42 N ANISOU 1858 N VAL B 126 3743 5367 4728 1099 -2180 -485 N ATOM 1859 CA VAL B 126 33.076 -47.841 -3.477 1.00 34.12 C ANISOU 1859 CA VAL B 126 3730 5272 3963 1180 -2054 -458 C ATOM 1860 C VAL B 126 32.087 -48.405 -4.486 1.00 31.05 C ANISOU 1860 C VAL B 126 3274 5027 3498 1094 -1754 -346 C ATOM 1861 O VAL B 126 31.219 -49.204 -4.132 1.00 31.60 O ANISOU 1861 O VAL B 126 3479 5239 3290 1195 -1625 -187 O ATOM 1862 CB VAL B 126 32.754 -46.355 -3.207 1.00 34.57 C ANISOU 1862 CB VAL B 126 3901 5295 3938 1176 -2119 -622 C ATOM 1863 CG1 VAL B 126 31.287 -46.194 -2.860 1.00 33.58 C ANISOU 1863 CG1 VAL B 126 4021 5359 3380 1268 -1913 -558 C ATOM 1864 CG2 VAL B 126 33.628 -45.829 -2.059 1.00 38.50 C ANISOU 1864 CG2 VAL B 126 4524 5630 4474 1322 -2470 -767 C ATOM 1865 N VAL B 127 32.214 -47.984 -5.742 1.00 29.19 N ANISOU 1865 N VAL B 127 2826 4740 3525 933 -1635 -415 N ATOM 1866 CA VAL B 127 31.248 -48.335 -6.779 1.00 29.40 C ANISOU 1866 CA VAL B 127 2836 4861 3474 833 -1352 -355 C ATOM 1867 C VAL B 127 31.229 -49.846 -7.088 1.00 28.65 C ANISOU 1867 C VAL B 127 2741 4708 3437 809 -1187 -191 C ATOM 1868 O VAL B 127 30.164 -50.447 -7.276 1.00 27.15 O ANISOU 1868 O VAL B 127 2646 4563 3107 765 -1019 -74 O ATOM 1869 CB VAL B 127 31.474 -47.468 -8.052 1.00 28.91 C ANISOU 1869 CB VAL B 127 2631 4697 3655 687 -1204 -456 C ATOM 1870 CG1 VAL B 127 30.748 -48.009 -9.254 1.00 24.93 C ANISOU 1870 CG1 VAL B 127 2195 4171 3105 579 -905 -393 C ATOM 1871 CG2 VAL B 127 31.061 -45.997 -7.782 1.00 27.26 C ANISOU 1871 CG2 VAL B 127 2466 4543 3348 680 -1306 -584 C ATOM 1872 N ASN B 128 32.400 -50.469 -7.128 1.00 30.40 N ANISOU 1872 N ASN B 128 2830 4793 3926 840 -1257 -174 N ATOM 1873 CA ASN B 128 32.439 -51.898 -7.465 1.00 32.17 C ANISOU 1873 CA ASN B 128 3061 4933 4229 827 -1110 -37 C ATOM 1874 C ASN B 128 31.811 -52.750 -6.358 1.00 33.79 C ANISOU 1874 C ASN B 128 3400 5238 4200 938 -1162 137 C ATOM 1875 O ASN B 128 31.208 -53.791 -6.616 1.00 33.24 O ANISOU 1875 O ASN B 128 3363 5118 4148 897 -1010 279 O ATOM 1876 CB ASN B 128 33.867 -52.364 -7.795 1.00 32.91 C ANISOU 1876 CB ASN B 128 2968 4842 4695 857 -1129 -35 C ATOM 1877 CG ASN B 128 34.304 -51.965 -9.207 1.00 36.68 C ANISOU 1877 CG ASN B 128 3349 5175 5413 789 -879 -93 C ATOM 1878 OD1 ASN B 128 33.480 -51.574 -10.049 1.00 40.72 O ANISOU 1878 OD1 ASN B 128 3987 5720 5765 721 -706 -145 O ATOM 1879 ND2 ASN B 128 35.597 -52.073 -9.474 1.00 43.13 N ANISOU 1879 ND2 ASN B 128 3949 5815 6623 843 -845 -58 N ATOM 1880 N GLU B 129 31.941 -52.279 -5.126 1.00 30.57 N ANISOU 1880 N GLU B 129 3087 4945 3584 1111 -1383 134 N ATOM 1881 CA GLU B 129 31.337 -52.920 -3.969 1.00 32.97 C ANISOU 1881 CA GLU B 129 3575 5360 3594 1305 -1379 341 C ATOM 1882 C GLU B 129 29.827 -52.650 -3.896 1.00 33.08 C ANISOU 1882 C GLU B 129 3703 5496 3371 1300 -1142 467 C ATOM 1883 O GLU B 129 29.057 -53.537 -3.531 1.00 34.22 O ANISOU 1883 O GLU B 129 3886 5646 3469 1360 -948 737 O ATOM 1884 CB GLU B 129 32.051 -52.440 -2.707 1.00 35.82 C ANISOU 1884 CB GLU B 129 4090 5756 3764 1544 -1708 265 C ATOM 1885 CG GLU B 129 31.653 -53.122 -1.414 1.00 40.89 C ANISOU 1885 CG GLU B 129 4996 6464 4076 1792 -1662 488 C ATOM 1886 CD GLU B 129 31.833 -54.627 -1.435 1.00 41.45 C ANISOU 1886 CD GLU B 129 4977 6500 4273 1859 -1577 744 C ATOM 1887 OE1 GLU B 129 32.774 -55.130 -2.078 1.00 37.77 O ANISOU 1887 OE1 GLU B 129 4294 5884 4171 1721 -1662 672 O ATOM 1888 OE2 GLU B 129 31.003 -55.308 -0.806 1.00 47.09 O ANISOU 1888 OE2 GLU B 129 5830 7280 4782 2016 -1348 1041 O ATOM 1889 N LEU B 130 29.413 -51.431 -4.245 1.00 30.15 N ANISOU 1889 N LEU B 130 3347 5191 2916 1230 -1146 303 N ATOM 1890 CA LEU B 130 27.993 -51.073 -4.304 1.00 32.71 C ANISOU 1890 CA LEU B 130 3730 5605 3093 1206 -919 417 C ATOM 1891 C LEU B 130 27.222 -51.984 -5.275 1.00 30.87 C ANISOU 1891 C LEU B 130 3352 5240 3137 995 -708 557 C ATOM 1892 O LEU B 130 26.096 -52.392 -4.986 1.00 33.19 O ANISOU 1892 O LEU B 130 3637 5536 3439 1024 -519 806 O ATOM 1893 CB LEU B 130 27.827 -49.600 -4.706 1.00 31.01 C ANISOU 1893 CB LEU B 130 3524 5449 2807 1136 -985 183 C ATOM 1894 CG LEU B 130 26.410 -49.065 -4.963 1.00 30.69 C ANISOU 1894 CG LEU B 130 3503 5479 2680 1079 -769 266 C ATOM 1895 CD1 LEU B 130 25.565 -49.261 -3.724 1.00 29.53 C ANISOU 1895 CD1 LEU B 130 3523 5451 2247 1351 -610 534 C ATOM 1896 CD2 LEU B 130 26.490 -47.606 -5.351 1.00 25.91 C ANISOU 1896 CD2 LEU B 130 2906 4915 2025 1020 -874 13 C ATOM 1897 N PHE B 131 27.844 -52.328 -6.401 1.00 28.35 N ANISOU 1897 N PHE B 131 2927 4769 3074 820 -751 410 N ATOM 1898 CA PHE B 131 27.202 -53.180 -7.401 1.00 30.77 C ANISOU 1898 CA PHE B 131 3167 4900 3626 660 -658 468 C ATOM 1899 C PHE B 131 27.765 -54.609 -7.465 1.00 33.44 C ANISOU 1899 C PHE B 131 3459 5071 4175 670 -672 567 C ATOM 1900 O PHE B 131 27.599 -55.293 -8.478 1.00 35.33 O ANISOU 1900 O PHE B 131 3685 5110 4629 560 -678 516 O ATOM 1901 CB PHE B 131 27.295 -52.541 -8.781 1.00 24.85 C ANISOU 1901 CB PHE B 131 2428 4071 2942 519 -673 226 C ATOM 1902 CG PHE B 131 26.551 -51.232 -8.880 1.00 29.91 C ANISOU 1902 CG PHE B 131 3096 4836 3431 482 -650 148 C ATOM 1903 CD1 PHE B 131 25.161 -51.216 -8.914 1.00 27.11 C ANISOU 1903 CD1 PHE B 131 2720 4471 3111 424 -591 274 C ATOM 1904 CD2 PHE B 131 27.238 -50.026 -8.905 1.00 27.78 C ANISOU 1904 CD2 PHE B 131 2837 4661 3058 506 -696 -29 C ATOM 1905 CE1 PHE B 131 24.464 -50.012 -9.000 1.00 24.98 C ANISOU 1905 CE1 PHE B 131 2467 4308 2715 399 -560 212 C ATOM 1906 CE2 PHE B 131 26.540 -48.801 -8.994 1.00 24.33 C ANISOU 1906 CE2 PHE B 131 2426 4325 2492 476 -678 -102 C ATOM 1907 CZ PHE B 131 25.167 -48.798 -9.039 1.00 21.90 C ANISOU 1907 CZ PHE B 131 2126 4033 2161 428 -602 12 C ATOM 1908 N ARG B 132 28.409 -55.046 -6.394 1.00 31.70 N ANISOU 1908 N ARG B 132 3252 4916 3877 830 -709 696 N ATOM 1909 CA ARG B 132 29.136 -56.324 -6.397 1.00 32.53 C ANISOU 1909 CA ARG B 132 3308 4869 4183 856 -735 779 C ATOM 1910 C ARG B 132 28.267 -57.520 -6.826 1.00 39.51 C ANISOU 1910 C ARG B 132 4127 5542 5343 762 -652 953 C ATOM 1911 O ARG B 132 28.703 -58.363 -7.615 1.00 40.95 O ANISOU 1911 O ARG B 132 4292 5516 5750 700 -697 874 O ATOM 1912 CB ARG B 132 29.779 -56.594 -5.034 1.00 37.55 C ANISOU 1912 CB ARG B 132 3995 5613 4660 1079 -810 929 C ATOM 1913 CG ARG B 132 30.677 -57.830 -5.011 1.00 48.52 C ANISOU 1913 CG ARG B 132 5319 6850 6267 1115 -856 1006 C ATOM 1914 CD ARG B 132 31.219 -58.094 -3.608 1.00 57.20 C ANISOU 1914 CD ARG B 132 6509 8052 7172 1374 -966 1171 C ATOM 1915 NE ARG B 132 30.138 -58.220 -2.633 1.00 67.18 N ANISOU 1915 NE ARG B 132 7897 9427 8202 1542 -801 1470 N ATOM 1916 CZ ARG B 132 29.532 -59.364 -2.330 1.00 75.58 C ANISOU 1916 CZ ARG B 132 8911 10386 9419 1586 -605 1806 C ATOM 1917 NH1 ARG B 132 29.906 -60.490 -2.924 1.00 79.06 N ANISOU 1917 NH1 ARG B 132 9207 10608 10224 1458 -612 1836 N ATOM 1918 NH2 ARG B 132 28.556 -59.384 -1.431 1.00 78.69 N ANISOU 1918 NH2 ARG B 132 9398 10869 9631 1782 -378 2137 N ATOM 1919 N ASP B 133 27.037 -57.589 -6.334 1.00 35.04 N ANISOU 1919 N ASP B 133 3515 4989 4810 768 -538 1195 N ATOM 1920 CA ASP B 133 26.185 -58.717 -6.702 1.00 40.60 C ANISOU 1920 CA ASP B 133 4087 5422 5918 667 -511 1385 C ATOM 1921 C ASP B 133 24.950 -58.338 -7.524 1.00 41.08 C ANISOU 1921 C ASP B 133 4076 5354 6180 500 -548 1338 C ATOM 1922 O ASP B 133 23.980 -59.098 -7.569 1.00 45.65 O ANISOU 1922 O ASP B 133 4483 5693 7168 430 -542 1566 O ATOM 1923 CB ASP B 133 25.786 -59.531 -5.470 1.00 45.08 C ANISOU 1923 CB ASP B 133 4568 5982 6580 823 -331 1822 C ATOM 1924 CG ASP B 133 25.292 -58.666 -4.336 1.00 50.89 C ANISOU 1924 CG ASP B 133 5385 6982 6970 1027 -133 2026 C ATOM 1925 OD1 ASP B 133 24.984 -57.487 -4.582 1.00 48.13 O ANISOU 1925 OD1 ASP B 133 5099 6777 6410 989 -150 1842 O ATOM 1926 OD2 ASP B 133 25.211 -59.164 -3.192 1.00 56.82 O ANISOU 1926 OD2 ASP B 133 6168 7788 7632 1264 54 2380 O ATOM 1927 N GLY B 134 24.980 -57.181 -8.182 1.00 34.13 N ANISOU 1927 N GLY B 134 3298 4594 5076 440 -608 1059 N ATOM 1928 CA GLY B 134 23.859 -56.793 -9.013 1.00 34.55 C ANISOU 1928 CA GLY B 134 3306 4515 5305 298 -693 991 C ATOM 1929 C GLY B 134 23.489 -55.328 -9.014 1.00 38.43 C ANISOU 1929 C GLY B 134 3850 5234 5516 295 -632 885 C ATOM 1930 O GLY B 134 24.125 -54.484 -8.360 1.00 33.95 O ANISOU 1930 O GLY B 134 3369 4932 4600 407 -541 833 O ATOM 1931 N VAL B 135 22.449 -55.035 -9.782 1.00 35.70 N ANISOU 1931 N VAL B 135 3452 4747 5364 171 -736 836 N ATOM 1932 CA VAL B 135 21.928 -53.688 -9.907 1.00 30.19 C ANISOU 1932 CA VAL B 135 2784 4219 4465 152 -691 748 C ATOM 1933 C VAL B 135 20.459 -53.650 -9.484 1.00 34.36 C ANISOU 1933 C VAL B 135 3086 4664 5304 117 -602 1051 C ATOM 1934 O VAL B 135 19.691 -54.582 -9.745 1.00 38.92 O ANISOU 1934 O VAL B 135 3476 4936 6377 26 -713 1217 O ATOM 1935 CB VAL B 135 22.047 -53.182 -11.364 1.00 30.07 C ANISOU 1935 CB VAL B 135 2939 4106 4379 67 -895 400 C ATOM 1936 CG1 VAL B 135 21.641 -51.683 -11.482 1.00 33.77 C ANISOU 1936 CG1 VAL B 135 3444 4770 4616 55 -833 304 C ATOM 1937 CG2 VAL B 135 23.457 -53.417 -11.902 1.00 28.91 C ANISOU 1937 CG2 VAL B 135 2983 3963 4038 135 -915 174 C ATOM 1938 N ASN B 136 20.078 -52.574 -8.810 1.00 31.11 N ANISOU 1938 N ASN B 136 2675 4493 4654 205 -403 1138 N ATOM 1939 CA ASN B 136 18.667 -52.229 -8.647 1.00 33.80 C ANISOU 1939 CA ASN B 136 2805 4757 5281 177 -294 1387 C ATOM 1940 C ASN B 136 18.594 -50.711 -8.559 1.00 33.84 C ANISOU 1940 C ASN B 136 2939 5024 4894 235 -209 1231 C ATOM 1941 O ASN B 136 19.633 -50.059 -8.426 1.00 32.49 O ANISOU 1941 O ASN B 136 2986 5071 4286 309 -225 988 O ATOM 1942 CB ASN B 136 18.065 -52.925 -7.418 1.00 36.77 C ANISOU 1942 CB ASN B 136 2981 5098 5892 331 28 1891 C ATOM 1943 CG ASN B 136 18.706 -52.477 -6.115 1.00 33.93 C ANISOU 1943 CG ASN B 136 2837 5071 4984 624 312 1992 C ATOM 1944 OD1 ASN B 136 18.802 -51.283 -5.828 1.00 37.77 O ANISOU 1944 OD1 ASN B 136 3497 5798 5054 734 375 1846 O ATOM 1945 ND2 ASN B 136 19.159 -53.432 -5.332 1.00 38.11 N ANISOU 1945 ND2 ASN B 136 3382 5589 5508 772 440 2224 N ATOM 1946 N TRP B 137 17.400 -50.131 -8.636 1.00 33.01 N ANISOU 1946 N TRP B 137 2675 4868 4998 201 -137 1374 N ATOM 1947 CA TRP B 137 17.300 -48.677 -8.670 1.00 30.81 C ANISOU 1947 CA TRP B 137 2520 4807 4378 243 -84 1201 C ATOM 1948 C TRP B 137 17.837 -47.976 -7.411 1.00 30.95 C ANISOU 1948 C TRP B 137 2730 5133 3897 507 164 1241 C ATOM 1949 O TRP B 137 18.390 -46.870 -7.494 1.00 28.91 O ANISOU 1949 O TRP B 137 2656 5051 3279 540 94 961 O ATOM 1950 CB TRP B 137 15.863 -48.232 -8.948 1.00 30.85 C ANISOU 1950 CB TRP B 137 2293 4677 4751 173 -46 1379 C ATOM 1951 CG TRP B 137 15.351 -48.566 -10.335 1.00 34.95 C ANISOU 1951 CG TRP B 137 2708 4887 5686 -62 -433 1219 C ATOM 1952 CD1 TRP B 137 14.344 -49.432 -10.644 1.00 38.94 C ANISOU 1952 CD1 TRP B 137 2908 5032 6857 -177 -583 1446 C ATOM 1953 CD2 TRP B 137 15.790 -48.005 -11.582 1.00 34.60 C ANISOU 1953 CD2 TRP B 137 2889 4831 5426 -165 -740 805 C ATOM 1954 NE1 TRP B 137 14.141 -49.459 -12.002 1.00 38.73 N ANISOU 1954 NE1 TRP B 137 2949 4765 7000 -335 -1042 1148 N ATOM 1955 CE2 TRP B 137 15.013 -48.593 -12.603 1.00 36.39 C ANISOU 1955 CE2 TRP B 137 3006 4695 6124 -307 -1108 767 C ATOM 1956 CE3 TRP B 137 16.771 -47.074 -11.936 1.00 31.95 C ANISOU 1956 CE3 TRP B 137 2835 4722 4582 -125 -740 488 C ATOM 1957 CZ2 TRP B 137 15.190 -48.283 -13.955 1.00 34.39 C ANISOU 1957 CZ2 TRP B 137 3004 4333 5731 -359 -1461 407 C ATOM 1958 CZ3 TRP B 137 16.944 -46.766 -13.279 1.00 28.89 C ANISOU 1958 CZ3 TRP B 137 2634 4227 4117 -194 -1008 191 C ATOM 1959 CH2 TRP B 137 16.156 -47.364 -14.270 1.00 31.01 C ANISOU 1959 CH2 TRP B 137 2873 4167 4744 -286 -1357 146 C ATOM 1960 N GLY B 138 17.662 -48.611 -6.256 1.00 32.61 N ANISOU 1960 N GLY B 138 2916 5376 4098 723 431 1593 N ATOM 1961 CA GLY B 138 18.181 -48.082 -5.006 1.00 37.43 C ANISOU 1961 CA GLY B 138 3798 6244 4180 1052 608 1622 C ATOM 1962 C GLY B 138 19.694 -47.905 -5.064 1.00 36.59 C ANISOU 1962 C GLY B 138 3922 6251 3730 1050 327 1243 C ATOM 1963 O GLY B 138 20.224 -46.867 -4.673 1.00 28.79 O ANISOU 1963 O GLY B 138 3150 5429 2359 1187 242 1015 O ATOM 1964 N ARG B 139 20.385 -48.916 -5.584 1.00 28.69 N ANISOU 1964 N ARG B 139 2850 5119 2930 896 165 1180 N ATOM 1965 CA ARG B 139 21.832 -48.830 -5.765 1.00 27.13 C ANISOU 1965 CA ARG B 139 2793 4976 2540 875 -80 864 C ATOM 1966 C ARG B 139 22.206 -47.752 -6.793 1.00 24.84 C ANISOU 1966 C ARG B 139 2519 4695 2222 702 -257 508 C ATOM 1967 O ARG B 139 23.191 -47.039 -6.624 1.00 25.02 O ANISOU 1967 O ARG B 139 2652 4805 2051 761 -399 278 O ATOM 1968 CB ARG B 139 22.401 -50.192 -6.172 1.00 31.19 C ANISOU 1968 CB ARG B 139 3215 5321 3313 765 -164 906 C ATOM 1969 CG ARG B 139 22.193 -51.284 -5.129 1.00 30.05 C ANISOU 1969 CG ARG B 139 3051 5153 3214 950 16 1275 C ATOM 1970 CD ARG B 139 22.639 -52.642 -5.642 1.00 30.27 C ANISOU 1970 CD ARG B 139 2961 4971 3568 815 -81 1314 C ATOM 1971 NE ARG B 139 22.516 -53.683 -4.618 1.00 33.13 N ANISOU 1971 NE ARG B 139 3296 5300 3990 1003 104 1692 N ATOM 1972 CZ ARG B 139 23.127 -54.866 -4.653 1.00 36.03 C ANISOU 1972 CZ ARG B 139 3614 5530 4547 978 37 1757 C ATOM 1973 NH1 ARG B 139 23.948 -55.182 -5.651 1.00 35.04 N ANISOU 1973 NH1 ARG B 139 3479 5286 4548 793 -201 1459 N ATOM 1974 NH2 ARG B 139 22.926 -55.735 -3.670 1.00 39.86 N ANISOU 1974 NH2 ARG B 139 4075 5986 5084 1176 246 2149 N ATOM 1975 N ILE B 140 21.417 -47.630 -7.852 1.00 23.57 N ANISOU 1975 N ILE B 140 2244 4416 2297 507 -267 481 N ATOM 1976 CA ILE B 140 21.648 -46.577 -8.826 1.00 23.31 C ANISOU 1976 CA ILE B 140 2253 4392 2214 389 -379 201 C ATOM 1977 C ILE B 140 21.534 -45.193 -8.166 1.00 24.94 C ANISOU 1977 C ILE B 140 2543 4775 2156 514 -335 124 C ATOM 1978 O ILE B 140 22.390 -44.341 -8.369 1.00 21.01 O ANISOU 1978 O ILE B 140 2108 4320 1555 510 -449 -110 O ATOM 1979 CB ILE B 140 20.742 -46.732 -10.099 1.00 27.75 C ANISOU 1979 CB ILE B 140 2736 4770 3036 206 -449 181 C ATOM 1980 CG1 ILE B 140 21.186 -47.946 -10.922 1.00 29.34 C ANISOU 1980 CG1 ILE B 140 2954 4765 3431 123 -584 131 C ATOM 1981 CG2 ILE B 140 20.777 -45.474 -10.980 1.00 21.55 C ANISOU 1981 CG2 ILE B 140 2026 4020 2141 143 -507 -49 C ATOM 1982 CD1 ILE B 140 20.186 -48.322 -11.981 1.00 27.62 C ANISOU 1982 CD1 ILE B 140 2699 4309 3486 0 -750 121 C ATOM 1983 N VAL B 141 20.493 -44.957 -7.372 1.00 26.23 N ANISOU 1983 N VAL B 141 2703 5014 2251 647 -159 337 N ATOM 1984 CA VAL B 141 20.409 -43.676 -6.649 1.00 23.73 C ANISOU 1984 CA VAL B 141 2530 4853 1632 828 -127 247 C ATOM 1985 C VAL B 141 21.609 -43.429 -5.704 1.00 24.82 C ANISOU 1985 C VAL B 141 2871 5054 1505 1025 -281 83 C ATOM 1986 O VAL B 141 22.194 -42.341 -5.679 1.00 27.66 O ANISOU 1986 O VAL B 141 3304 5294 1914 990 -407 -165 O ATOM 1987 CB VAL B 141 19.099 -43.569 -5.835 1.00 25.47 C ANISOU 1987 CB VAL B 141 2747 5129 1800 1021 165 559 C ATOM 1988 CG1 VAL B 141 19.129 -42.338 -4.953 1.00 29.73 C ANISOU 1988 CG1 VAL B 141 3526 5806 1964 1286 185 439 C ATOM 1989 CG2 VAL B 141 17.887 -43.560 -6.787 1.00 28.95 C ANISOU 1989 CG2 VAL B 141 2940 5437 2623 804 242 686 C ATOM 1990 N ALA B 142 21.971 -44.445 -4.934 1.00 26.36 N ANISOU 1990 N ALA B 142 3134 5278 1602 1184 -261 243 N ATOM 1991 CA ALA B 142 23.172 -44.387 -4.096 1.00 29.34 C ANISOU 1991 CA ALA B 142 3680 5556 1910 1302 -446 70 C ATOM 1992 C ALA B 142 24.433 -43.978 -4.883 1.00 26.99 C ANISOU 1992 C ALA B 142 3289 5113 1855 1082 -691 -213 C ATOM 1993 O ALA B 142 25.243 -43.207 -4.394 1.00 27.90 O ANISOU 1993 O ALA B 142 3493 5113 1993 1128 -868 -392 O ATOM 1994 CB ALA B 142 23.387 -45.708 -3.389 1.00 29.08 C ANISOU 1994 CB ALA B 142 3703 5568 1780 1472 -390 304 C ATOM 1995 N PHE B 143 24.579 -44.516 -6.086 1.00 25.60 N ANISOU 1995 N PHE B 143 2926 4923 1877 871 -686 -216 N ATOM 1996 CA PHE B 143 25.718 -44.239 -6.970 1.00 24.48 C ANISOU 1996 CA PHE B 143 2678 4637 1988 707 -807 -402 C ATOM 1997 C PHE B 143 25.796 -42.751 -7.304 1.00 23.81 C ANISOU 1997 C PHE B 143 2594 4457 1996 639 -823 -555 C ATOM 1998 O PHE B 143 26.841 -42.118 -7.184 1.00 24.85 O ANISOU 1998 O PHE B 143 2695 4470 2277 639 -976 -681 O ATOM 1999 CB PHE B 143 25.560 -45.091 -8.224 1.00 24.32 C ANISOU 1999 CB PHE B 143 2521 4621 2100 557 -740 -358 C ATOM 2000 CG PHE B 143 26.393 -44.660 -9.407 1.00 22.82 C ANISOU 2000 CG PHE B 143 2239 4317 2116 439 -750 -510 C ATOM 2001 CD1 PHE B 143 27.725 -45.041 -9.512 1.00 27.92 C ANISOU 2001 CD1 PHE B 143 2795 4858 2955 457 -816 -551 C ATOM 2002 CD2 PHE B 143 25.817 -43.958 -10.452 1.00 21.46 C ANISOU 2002 CD2 PHE B 143 2073 4115 1967 338 -652 -565 C ATOM 2003 CE1 PHE B 143 28.488 -44.688 -10.627 1.00 21.64 C ANISOU 2003 CE1 PHE B 143 1907 3925 2389 398 -719 -612 C ATOM 2004 CE2 PHE B 143 26.564 -43.597 -11.578 1.00 22.58 C ANISOU 2004 CE2 PHE B 143 2173 4138 2269 293 -578 -645 C ATOM 2005 CZ PHE B 143 27.915 -43.966 -11.658 1.00 22.54 C ANISOU 2005 CZ PHE B 143 2068 4022 2475 333 -577 -649 C ATOM 2006 N PHE B 144 24.663 -42.187 -7.682 1.00 20.86 N ANISOU 2006 N PHE B 144 2230 4132 1563 593 -686 -522 N ATOM 2007 CA PHE B 144 24.606 -40.756 -7.931 1.00 22.66 C ANISOU 2007 CA PHE B 144 2465 4282 1865 553 -693 -635 C ATOM 2008 C PHE B 144 24.897 -39.958 -6.664 1.00 22.40 C ANISOU 2008 C PHE B 144 2566 4213 1734 719 -832 -714 C ATOM 2009 O PHE B 144 25.727 -39.048 -6.690 1.00 23.89 O ANISOU 2009 O PHE B 144 2722 4275 2080 698 -982 -851 O ATOM 2010 CB PHE B 144 23.256 -40.374 -8.564 1.00 23.17 C ANISOU 2010 CB PHE B 144 2508 4404 1892 484 -536 -570 C ATOM 2011 CG PHE B 144 23.174 -40.656 -10.028 1.00 21.37 C ANISOU 2011 CG PHE B 144 2198 4122 1798 322 -476 -573 C ATOM 2012 CD1 PHE B 144 23.647 -39.736 -10.965 1.00 21.05 C ANISOU 2012 CD1 PHE B 144 2125 3992 1882 254 -461 -669 C ATOM 2013 CD2 PHE B 144 22.638 -41.860 -10.487 1.00 19.01 C ANISOU 2013 CD2 PHE B 144 1870 3868 1484 270 -459 -478 C ATOM 2014 CE1 PHE B 144 23.554 -40.019 -12.345 1.00 22.56 C ANISOU 2014 CE1 PHE B 144 2311 4146 2112 174 -402 -676 C ATOM 2015 CE2 PHE B 144 22.549 -42.144 -11.846 1.00 21.47 C ANISOU 2015 CE2 PHE B 144 2189 4085 1884 166 -458 -514 C ATOM 2016 CZ PHE B 144 23.004 -41.230 -12.786 1.00 19.34 C ANISOU 2016 CZ PHE B 144 1948 3733 1667 139 -414 -611 C ATOM 2017 N SER B 145 24.238 -40.291 -5.549 1.00 26.17 N ANISOU 2017 N SER B 145 3198 4790 1956 916 -791 -624 N ATOM 2018 CA SER B 145 24.436 -39.547 -4.307 1.00 29.84 C ANISOU 2018 CA SER B 145 3859 5209 2272 1136 -928 -715 C ATOM 2019 C SER B 145 25.886 -39.669 -3.853 1.00 30.57 C ANISOU 2019 C SER B 145 3969 5170 2474 1170 -1207 -847 C ATOM 2020 O SER B 145 26.458 -38.735 -3.311 1.00 30.80 O ANISOU 2020 O SER B 145 4074 5073 2554 1259 -1426 -1010 O ATOM 2021 CB SER B 145 23.481 -39.999 -3.191 1.00 34.38 C ANISOU 2021 CB SER B 145 4631 5912 2521 1416 -773 -552 C ATOM 2022 OG SER B 145 22.123 -39.805 -3.575 1.00 38.05 O ANISOU 2022 OG SER B 145 5037 6482 2937 1402 -520 -404 O ATOM 2023 N PHE B 146 26.495 -40.813 -4.128 1.00 28.12 N ANISOU 2023 N PHE B 146 3567 4872 2244 1101 -1225 -780 N ATOM 2024 CA PHE B 146 27.902 -40.989 -3.788 1.00 29.68 C ANISOU 2024 CA PHE B 146 3732 4933 2614 1119 -1499 -885 C ATOM 2025 C PHE B 146 28.778 -40.062 -4.615 1.00 29.19 C ANISOU 2025 C PHE B 146 3459 4702 2930 949 -1624 -1016 C ATOM 2026 O PHE B 146 29.688 -39.420 -4.073 1.00 31.77 O ANISOU 2026 O PHE B 146 3787 4856 3427 1016 -1899 -1157 O ATOM 2027 CB PHE B 146 28.356 -42.428 -4.010 1.00 31.29 C ANISOU 2027 CB PHE B 146 3847 5182 2858 1080 -1475 -766 C ATOM 2028 CG PHE B 146 29.846 -42.596 -3.939 1.00 30.70 C ANISOU 2028 CG PHE B 146 3651 4944 3070 1054 -1738 -854 C ATOM 2029 CD1 PHE B 146 30.531 -42.267 -2.781 1.00 34.18 C ANISOU 2029 CD1 PHE B 146 4240 5268 3481 1233 -2026 -971 C ATOM 2030 CD2 PHE B 146 30.560 -43.063 -5.031 1.00 29.24 C ANISOU 2030 CD2 PHE B 146 3199 4701 3211 881 -1701 -822 C ATOM 2031 CE1 PHE B 146 31.926 -42.405 -2.698 1.00 36.28 C ANISOU 2031 CE1 PHE B 146 4360 5342 4083 1207 -2297 -1048 C ATOM 2032 CE2 PHE B 146 31.951 -43.219 -4.957 1.00 32.13 C ANISOU 2032 CE2 PHE B 146 3401 4890 3919 870 -1917 -867 C ATOM 2033 CZ PHE B 146 32.631 -42.887 -3.796 1.00 36.42 C ANISOU 2033 CZ PHE B 146 4064 5301 4474 1014 -2223 -975 C ATOM 2034 N GLY B 147 28.515 -40.001 -5.918 1.00 26.48 N ANISOU 2034 N GLY B 147 2937 4387 2735 760 -1431 -966 N ATOM 2035 CA GLY B 147 29.308 -39.174 -6.803 1.00 26.34 C ANISOU 2035 CA GLY B 147 2699 4218 3089 631 -1484 -1042 C ATOM 2036 C GLY B 147 29.109 -37.711 -6.438 1.00 32.00 C ANISOU 2036 C GLY B 147 3478 4843 3837 676 -1591 -1163 C ATOM 2037 O GLY B 147 30.059 -36.935 -6.446 1.00 29.43 O ANISOU 2037 O GLY B 147 3019 4312 3853 660 -1787 -1261 O ATOM 2038 N GLY B 148 27.868 -37.341 -6.106 1.00 30.06 N ANISOU 2038 N GLY B 148 3415 4724 3285 744 -1464 -1144 N ATOM 2039 CA GLY B 148 27.612 -35.988 -5.606 1.00 31.37 C ANISOU 2039 CA GLY B 148 3670 4809 3441 834 -1580 -1268 C ATOM 2040 C GLY B 148 28.409 -35.650 -4.349 1.00 36.40 C ANISOU 2040 C GLY B 148 4440 5287 4103 1033 -1924 -1424 C ATOM 2041 O GLY B 148 29.062 -34.587 -4.253 1.00 36.09 O ANISOU 2041 O GLY B 148 4339 5033 4342 1054 -2162 -1576 O ATOM 2042 N ALA B 149 28.363 -36.552 -3.370 1.00 33.67 N ANISOU 2042 N ALA B 149 4288 5016 3488 1207 -1973 -1393 N ATOM 2043 CA ALA B 149 29.081 -36.343 -2.117 1.00 38.00 C ANISOU 2043 CA ALA B 149 5028 5404 4005 1455 -2325 -1555 C ATOM 2044 C ALA B 149 30.583 -36.298 -2.356 1.00 39.68 C ANISOU 2044 C ALA B 149 5027 5363 4689 1355 -2620 -1653 C ATOM 2045 O ALA B 149 31.299 -35.522 -1.735 1.00 43.43 O ANISOU 2045 O ALA B 149 5554 5577 5369 1486 -2981 -1843 O ATOM 2046 CB ALA B 149 28.726 -37.410 -1.107 1.00 39.44 C ANISOU 2046 CB ALA B 149 5468 5724 3792 1683 -2279 -1470 C ATOM 2047 N LEU B 150 31.059 -37.135 -3.272 1.00 43.24 N ANISOU 2047 N LEU B 150 5226 5852 5352 1142 -2476 -1519 N ATOM 2048 CA LEU B 150 32.472 -37.150 -3.623 1.00 41.90 C ANISOU 2048 CA LEU B 150 4791 5424 5705 1040 -2686 -1556 C ATOM 2049 C LEU B 150 32.902 -35.830 -4.283 1.00 41.79 C ANISOU 2049 C LEU B 150 4555 5166 6157 930 -2761 -1631 C ATOM 2050 O LEU B 150 34.011 -35.351 -4.064 1.00 43.44 O ANISOU 2050 O LEU B 150 4626 5040 6840 944 -3066 -1727 O ATOM 2051 CB LEU B 150 32.771 -38.350 -4.535 1.00 41.04 C ANISOU 2051 CB LEU B 150 4465 5424 5706 873 -2453 -1370 C ATOM 2052 CG LEU B 150 34.211 -38.823 -4.690 1.00 44.01 C ANISOU 2052 CG LEU B 150 4589 5566 6567 818 -2620 -1346 C ATOM 2053 CD1 LEU B 150 34.747 -39.298 -3.355 1.00 44.53 C ANISOU 2053 CD1 LEU B 150 4853 5542 6522 1010 -2964 -1447 C ATOM 2054 CD2 LEU B 150 34.281 -39.935 -5.732 1.00 38.94 C ANISOU 2054 CD2 LEU B 150 3746 5058 5990 687 -2315 -1152 C ATOM 2055 N CYS B 151 32.027 -35.238 -5.096 1.00 38.02 N ANISOU 2055 N CYS B 151 4035 4821 5590 826 -2491 -1575 N ATOM 2056 CA CYS B 151 32.318 -33.931 -5.690 1.00 38.01 C ANISOU 2056 CA CYS B 151 3842 4593 6006 744 -2540 -1630 C ATOM 2057 C CYS B 151 32.357 -32.814 -4.640 1.00 43.48 C ANISOU 2057 C CYS B 151 4714 5076 6731 936 -2903 -1850 C ATOM 2058 O CYS B 151 33.254 -31.972 -4.660 1.00 46.69 O ANISOU 2058 O CYS B 151 4948 5119 7674 927 -3165 -1938 O ATOM 2059 CB CYS B 151 31.304 -33.595 -6.801 1.00 34.24 C ANISOU 2059 CB CYS B 151 3307 4319 5384 611 -2174 -1523 C ATOM 2060 SG CYS B 151 31.597 -34.471 -8.367 1.00 33.07 S ANISOU 2060 SG CYS B 151 2868 4253 5443 417 -1810 -1301 S ATOM 2061 N VAL B 152 31.389 -32.806 -3.723 1.00 41.75 N ANISOU 2061 N VAL B 152 4838 5046 5979 1135 -2918 -1923 N ATOM 2062 CA VAL B 152 31.342 -31.789 -2.669 1.00 45.73 C ANISOU 2062 CA VAL B 152 5571 5359 6446 1389 -3268 -2143 C ATOM 2063 C VAL B 152 32.546 -31.927 -1.752 1.00 56.81 C ANISOU 2063 C VAL B 152 7033 6439 8114 1553 -3742 -2304 C ATOM 2064 O VAL B 152 33.250 -30.953 -1.488 1.00 54.72 O ANISOU 2064 O VAL B 152 6710 5795 8286 1630 -4127 -2475 O ATOM 2065 CB VAL B 152 30.076 -31.902 -1.816 1.00 45.43 C ANISOU 2065 CB VAL B 152 5907 5585 5770 1624 -3141 -2147 C ATOM 2066 CG1 VAL B 152 30.164 -30.988 -0.593 1.00 50.61 C ANISOU 2066 CG1 VAL B 152 6859 6016 6352 1973 -3553 -2389 C ATOM 2067 CG2 VAL B 152 28.853 -31.526 -2.643 1.00 41.42 C ANISOU 2067 CG2 VAL B 152 5341 5316 5081 1483 -2746 -2016 C ATOM 2068 N GLU B 153 32.780 -33.149 -1.279 1.00 50.80 N ANISOU 2068 N GLU B 153 6380 5797 7124 1612 -3737 -2246 N ATOM 2069 CA GLU B 153 33.924 -33.430 -0.403 1.00 55.67 C ANISOU 2069 CA GLU B 153 7068 6112 7970 1772 -4198 -2392 C ATOM 2070 C GLU B 153 35.244 -33.001 -1.044 1.00 57.76 C ANISOU 2070 C GLU B 153 6935 5965 9045 1579 -4424 -2407 C ATOM 2071 O GLU B 153 36.184 -32.613 -0.346 1.00 72.29 O ANISOU 2071 O GLU B 153 8803 7396 11269 1724 -4925 -2589 O ATOM 2072 CB GLU B 153 33.960 -34.913 -0.032 1.00 54.70 C ANISOU 2072 CB GLU B 153 7060 6214 7511 1811 -4080 -2275 C ATOM 2073 CG GLU B 153 32.895 -35.339 0.970 0.00 55.03 C ANISOU 2073 CG GLU B 153 7539 6528 6842 2106 -3967 -2272 C ATOM 2074 CD GLU B 153 33.264 -34.997 2.401 0.00 61.30 C ANISOU 2074 CD GLU B 153 8723 7080 7488 2515 -4450 -2519 C ATOM 2075 OE1 GLU B 153 32.945 -33.877 2.852 0.00 63.98 O ANISOU 2075 OE1 GLU B 153 9254 7273 7781 2723 -4647 -2692 O ATOM 2076 OE2 GLU B 153 33.875 -35.852 3.075 0.00 63.89 O ANISOU 2076 OE2 GLU B 153 9186 7349 7739 2653 -4651 -2546 O ATOM 2077 N ASER B 154 35.312 -33.076 -2.370 0.72 54.10 N ANISOU 2077 N ASER B 154 6109 5574 8874 1277 -4057 -2202 N ATOM 2078 N BSER B 154 35.306 -33.082 -2.370 0.28 54.08 N ANISOU 2078 N BSER B 154 6107 5574 8866 1277 -4054 -2201 N ATOM 2079 CA ASER B 154 36.479 -32.625 -3.117 0.72 56.21 C ANISOU 2079 CA ASER B 154 5962 5438 9957 1096 -4151 -2138 C ATOM 2080 CA BSER B 154 36.464 -32.622 -3.122 0.28 56.16 C ANISOU 2080 CA BSER B 154 5957 5436 9945 1096 -4147 -2137 C ATOM 2081 C ASER B 154 36.599 -31.108 -3.056 0.72 59.41 C ANISOU 2081 C ASER B 154 6309 5487 10778 1152 -4416 -2281 C ATOM 2082 C BSER B 154 36.590 -31.111 -3.024 0.28 59.46 C ANISOU 2082 C BSER B 154 6325 5495 10772 1158 -4424 -2287 C ATOM 2083 O ASER B 154 37.678 -30.580 -2.818 0.72 64.45 O ANISOU 2083 O ASER B 154 6774 5623 12091 1179 -4810 -2361 O ATOM 2084 O BSER B 154 37.663 -30.590 -2.728 0.28 64.62 O ANISOU 2084 O BSER B 154 6822 5646 12083 1199 -4837 -2378 O ATOM 2085 CB ASER B 154 36.411 -33.087 -4.575 0.72 51.86 C ANISOU 2085 CB ASER B 154 5091 5071 9544 823 -3628 -1857 C ATOM 2086 CB BSER B 154 36.354 -33.030 -4.589 0.28 51.76 C ANISOU 2086 CB BSER B 154 5083 5065 9518 823 -3620 -1860 C ATOM 2087 OG ASER B 154 36.474 -34.507 -4.674 0.72 49.64 O ANISOU 2087 OG ASER B 154 4818 5041 9000 782 -3436 -1725 O ATOM 2088 OG BSER B 154 37.399 -32.455 -5.352 0.28 54.29 O ANISOU 2088 OG BSER B 154 5007 4971 10651 678 -3626 -1745 O ATOM 2089 N VAL B 155 35.492 -30.408 -3.283 1.00 56.80 N ANISOU 2089 N VAL B 155 6105 5382 10094 1169 -4212 -2303 N ATOM 2090 CA VAL B 155 35.497 -28.953 -3.175 1.00 59.83 C ANISOU 2090 CA VAL B 155 6456 5448 10827 1248 -4471 -2447 C ATOM 2091 C VAL B 155 35.678 -28.532 -1.706 1.00 65.29 C ANISOU 2091 C VAL B 155 7491 5894 11422 1598 -5061 -2748 C ATOM 2092 O VAL B 155 36.321 -27.524 -1.417 1.00 70.31 O ANISOU 2092 O VAL B 155 8042 6050 12623 1699 -5503 -2899 O ATOM 2093 CB VAL B 155 34.220 -28.335 -3.782 1.00 55.69 C ANISOU 2093 CB VAL B 155 5990 5242 9928 1187 -4102 -2393 C ATOM 2094 CG1 VAL B 155 34.251 -26.815 -3.676 1.00 59.02 C ANISOU 2094 CG1 VAL B 155 6360 5321 10743 1276 -4382 -2538 C ATOM 2095 CG2 VAL B 155 34.061 -28.766 -5.237 1.00 51.03 C ANISOU 2095 CG2 VAL B 155 5106 4860 9423 890 -3568 -2115 C ATOM 2096 N ASP B 156 35.120 -29.323 -0.788 1.00 64.83 N ANISOU 2096 N ASP B 156 7828 6133 10670 1810 -5073 -2819 N ATOM 2097 CA ASP B 156 35.243 -29.081 0.653 1.00 70.41 C ANISOU 2097 CA ASP B 156 8944 6636 11171 2209 -5604 -3093 C ATOM 2098 C ASP B 156 36.715 -29.006 1.077 1.00 76.53 C ANISOU 2098 C ASP B 156 9586 6845 12645 2268 -6186 -3234 C ATOM 2099 O ASP B 156 37.053 -28.356 2.066 1.00 82.66 O ANISOU 2099 O ASP B 156 10612 7252 13541 2590 -6768 -3502 O ATOM 2100 CB ASP B 156 34.559 -30.206 1.447 1.00 69.05 C ANISOU 2100 CB ASP B 156 9171 6863 10203 2407 -5432 -3065 C ATOM 2101 CG ASP B 156 33.117 -29.886 1.847 1.00 67.37 C ANISOU 2101 CG ASP B 156 9307 6993 9299 2615 -5173 -3064 C ATOM 2102 OD1 ASP B 156 32.542 -28.903 1.334 1.00 65.90 O ANISOU 2102 OD1 ASP B 156 9022 6825 9193 2541 -5048 -3061 O ATOM 2103 OD2 ASP B 156 32.559 -30.647 2.685 1.00 67.83 O ANISOU 2103 OD2 ASP B 156 9731 7289 8752 2864 -5079 -3044 O ATOM 2104 N LYS B 157 37.586 -29.685 0.334 1.00 75.33 N ANISOU 2104 N LYS B 157 9051 6600 12973 1980 -6044 -3048 N ATOM 2105 CA LYS B 157 39.009 -29.722 0.654 1.00 82.01 C ANISOU 2105 CA LYS B 157 9711 6886 14562 1997 -6554 -3129 C ATOM 2106 C LYS B 157 39.854 -29.114 -0.466 1.00 81.97 C ANISOU 2106 C LYS B 157 9141 6482 15523 1699 -6472 -2945 C ATOM 2107 O LYS B 157 40.993 -29.523 -0.683 1.00 84.68 O ANISOU 2107 O LYS B 157 9178 6477 16520 1569 -6602 -2840 O ATOM 2108 CB LYS B 157 39.458 -31.164 0.901 0.00 80.97 C ANISOU 2108 CB LYS B 157 9618 6919 14227 1960 -6490 -3042 C ATOM 2109 CG LYS B 157 38.523 -31.985 1.777 0.00 78.83 C ANISOU 2109 CG LYS B 157 9850 7121 12981 2206 -6374 -3108 C ATOM 2110 CD LYS B 157 38.662 -31.623 3.243 0.00 85.29 C ANISOU 2110 CD LYS B 157 11146 7664 13596 2656 -7003 -3435 C ATOM 2111 CE LYS B 157 37.354 -31.103 3.811 0.00 84.40 C ANISOU 2111 CE LYS B 157 11478 7848 12744 2948 -6878 -3534 C ATOM 2112 NZ LYS B 157 36.265 -32.113 3.712 0.00 78.70 N ANISOU 2112 NZ LYS B 157 10921 7740 11242 2915 -6273 -3321 N ATOM 2113 N GLU B 158 39.279 -28.154 -1.186 1.00 79.87 N ANISOU 2113 N GLU B 158 8733 6257 15355 1601 -6223 -2877 N ATOM 2114 CA GLU B 158 39.993 -27.427 -2.237 1.00 81.25 C ANISOU 2114 CA GLU B 158 8396 6023 16452 1365 -6109 -2675 C ATOM 2115 C GLU B 158 40.644 -28.314 -3.305 1.00 82.51 C ANISOU 2115 C GLU B 158 8162 6221 16968 1062 -5642 -2327 C ATOM 2116 O GLU B 158 41.811 -28.134 -3.645 1.00 83.18 O ANISOU 2116 O GLU B 158 7862 5772 17969 959 -5771 -2182 O ATOM 2117 CB GLU B 158 41.043 -26.498 -1.614 1.00 89.59 C ANISOU 2117 CB GLU B 158 9324 6316 18399 1525 -6817 -2850 C ATOM 2118 CG GLU B 158 41.327 -25.258 -2.430 1.00 91.71 C ANISOU 2118 CG GLU B 158 9168 6332 19345 1338 -6699 -2672 C ATOM 2119 CD GLU B 158 42.010 -24.198 -1.607 1.00102.62 C ANISOU 2119 CD GLU B 158 10507 7222 21260 1495 -7389 -2875 C ATOM 2120 OE1 GLU B 158 42.565 -24.558 -0.547 1.00104.80 O ANISOU 2120 OE1 GLU B 158 10994 7275 21548 1697 -7952 -3101 O ATOM 2121 OE2 GLU B 158 41.972 -23.015 -2.005 1.00102.11 O ANISOU 2121 OE2 GLU B 158 10216 6985 21595 1432 -7390 -2820 O ATOM 2122 N MET B 159 39.887 -29.270 -3.837 1.00 78.27 N ANISOU 2122 N MET B 159 7718 6281 15739 944 -5101 -2177 N ATOM 2123 CA MET B 159 40.381 -30.123 -4.918 1.00 72.37 C ANISOU 2123 CA MET B 159 6640 5616 15242 702 -4618 -1843 C ATOM 2124 C MET B 159 39.400 -30.152 -6.089 1.00 68.32 C ANISOU 2124 C MET B 159 6087 5553 14317 550 -3978 -1639 C ATOM 2125 O MET B 159 38.942 -31.216 -6.498 1.00 63.66 O ANISOU 2125 O MET B 159 5570 5403 13217 485 -3607 -1519 O ATOM 2126 CB MET B 159 40.622 -31.543 -4.411 1.00 70.42 C ANISOU 2126 CB MET B 159 6532 5599 14624 736 -4652 -1851 C ATOM 2127 CG MET B 159 41.816 -31.681 -3.495 1.00 75.41 C ANISOU 2127 CG MET B 159 7120 5732 15799 843 -5232 -1982 C ATOM 2128 SD MET B 159 41.977 -33.366 -2.888 1.00 73.96 S ANISOU 2128 SD MET B 159 7132 5872 15097 897 -5245 -1987 S ATOM 2129 CE MET B 159 40.788 -33.341 -1.555 1.00 73.05 C ANISOU 2129 CE MET B 159 7652 6129 13976 1213 -5520 -2321 C ATOM 2130 N GLN B 160 39.107 -28.971 -6.631 1.00 71.78 N ANISOU 2130 N GLN B 160 6407 5841 15024 510 -3881 -1603 N ATOM 2131 CA GLN B 160 38.072 -28.782 -7.654 1.00 66.95 C ANISOU 2131 CA GLN B 160 5809 5619 14013 402 -3355 -1458 C ATOM 2132 C GLN B 160 38.362 -29.435 -9.013 1.00 57.52 C ANISOU 2132 C GLN B 160 4348 4520 12986 230 -2767 -1090 C ATOM 2133 O GLN B 160 37.430 -29.777 -9.742 1.00 54.98 O ANISOU 2133 O GLN B 160 4129 4630 12131 181 -2353 -999 O ATOM 2134 CB GLN B 160 37.756 -27.280 -7.796 1.00 74.76 C ANISOU 2134 CB GLN B 160 6742 6368 15296 427 -3455 -1523 C ATOM 2135 CG GLN B 160 37.241 -26.813 -9.159 1.00 79.65 C ANISOU 2135 CG GLN B 160 7194 7115 15954 279 -2905 -1265 C ATOM 2136 CD GLN B 160 38.327 -26.138 -9.987 1.00 88.49 C ANISOU 2136 CD GLN B 160 7890 7679 18053 187 -2751 -964 C ATOM 2137 OE1 GLN B 160 39.097 -26.805 -10.683 1.00 90.42 O ANISOU 2137 OE1 GLN B 160 7912 7814 18629 103 -2430 -667 O ATOM 2138 NE2 GLN B 160 38.398 -24.810 -9.909 1.00 90.77 N ANISOU 2138 NE2 GLN B 160 8066 7588 18836 227 -2962 -1014 N ATOM 2139 N VAL B 161 39.639 -29.641 -9.335 1.00 64.34 N ANISOU 2139 N VAL B 161 4892 4966 14590 170 -2731 -872 N ATOM 2140 CA VAL B 161 40.025 -30.314 -10.580 1.00 62.94 C ANISOU 2140 CA VAL B 161 4495 4841 14577 70 -2142 -490 C ATOM 2141 C VAL B 161 39.448 -31.741 -10.683 1.00 57.17 C ANISOU 2141 C VAL B 161 3971 4653 13097 84 -1912 -499 C ATOM 2142 O VAL B 161 39.353 -32.306 -11.775 1.00 56.36 O ANISOU 2142 O VAL B 161 3807 4730 12877 57 -1386 -236 O ATOM 2143 CB VAL B 161 41.566 -30.352 -10.770 1.00 69.74 C ANISOU 2143 CB VAL B 161 4982 5113 16404 28 -2152 -230 C ATOM 2144 CG1 VAL B 161 42.206 -31.471 -9.933 1.00 68.92 C ANISOU 2144 CG1 VAL B 161 4913 5002 16272 59 -2459 -341 C ATOM 2145 CG2 VAL B 161 41.924 -30.529 -12.241 1.00 71.31 C ANISOU 2145 CG2 VAL B 161 4959 5253 16881 -25 -1446 239 C ATOM 2146 N ALEU B 162 39.056 -32.300 -9.542 0.40 54.35 N ANISOU 2146 N ALEU B 162 3883 4527 12240 164 -2299 -789 N ATOM 2147 N BLEU B 162 39.060 -32.306 -9.543 0.60 54.11 N ANISOU 2147 N BLEU B 162 3852 4496 12210 163 -2299 -788 N ATOM 2148 CA ALEU B 162 38.535 -33.662 -9.487 0.40 51.05 C ANISOU 2148 CA ALEU B 162 3653 4564 11180 190 -2145 -798 C ATOM 2149 CA BLEU B 162 38.539 -33.670 -9.501 0.60 51.08 C ANISOU 2149 CA BLEU B 162 3655 4568 11186 190 -2140 -794 C ATOM 2150 C ALEU B 162 37.098 -33.768 -9.985 0.40 46.95 C ANISOU 2150 C ALEU B 162 3355 4528 9957 192 -1853 -823 C ATOM 2151 C BLEU B 162 37.096 -33.770 -9.984 0.60 47.09 C ANISOU 2151 C BLEU B 162 3373 4546 9973 192 -1853 -823 C ATOM 2152 O ALEU B 162 36.696 -34.809 -10.490 0.40 41.48 O ANISOU 2152 O ALEU B 162 2719 4140 8902 193 -1565 -723 O ATOM 2153 O BLEU B 162 36.686 -34.810 -10.477 0.60 41.46 O ANISOU 2153 O BLEU B 162 2720 4140 8894 193 -1569 -727 O ATOM 2154 CB ALEU B 162 38.615 -34.210 -8.062 0.40 51.41 C ANISOU 2154 CB ALEU B 162 3933 4656 10946 302 -2634 -1054 C ATOM 2155 CB BLEU B 162 38.636 -34.247 -8.087 0.60 51.31 C ANISOU 2155 CB BLEU B 162 3913 4643 10939 300 -2623 -1045 C ATOM 2156 CG ALEU B 162 40.024 -34.351 -7.475 0.40 56.15 C ANISOU 2156 CG ALEU B 162 4344 4790 12201 318 -2986 -1055 C ATOM 2157 CG BLEU B 162 40.040 -34.607 -7.578 0.60 55.65 C ANISOU 2157 CG BLEU B 162 4270 4778 12097 309 -2919 -1018 C ATOM 2158 CD1ALEU B 162 39.976 -35.124 -6.167 0.40 56.75 C ANISOU 2158 CD1ALEU B 162 4711 4998 11852 460 -3391 -1280 C ATOM 2159 CD1BLEU B 162 39.951 -35.176 -6.173 0.60 56.57 C ANISOU 2159 CD1BLEU B 162 4695 4995 11803 460 -3379 -1277 C ATOM 2160 CD2ALEU B 162 40.940 -35.032 -8.473 0.40 56.98 C ANISOU 2160 CD2ALEU B 162 4113 4744 12793 212 -2599 -723 C ATOM 2161 CD2BLEU B 162 40.708 -35.601 -8.515 0.60 55.19 C ANISOU 2161 CD2BLEU B 162 3957 4717 12295 223 -2502 -711 C ATOM 2162 N VAL B 163 36.332 -32.691 -9.832 1.00 47.05 N ANISOU 2162 N VAL B 163 3486 4573 9818 203 -1951 -960 N ATOM 2163 CA VAL B 163 34.894 -32.711 -10.144 1.00 44.51 C ANISOU 2163 CA VAL B 163 3390 4676 8847 208 -1746 -1010 C ATOM 2164 C VAL B 163 34.551 -33.170 -11.561 1.00 38.25 C ANISOU 2164 C VAL B 163 2496 4066 7970 152 -1226 -772 C ATOM 2165 O VAL B 163 33.644 -33.995 -11.761 1.00 34.86 O ANISOU 2165 O VAL B 163 2236 3990 7020 173 -1079 -789 O ATOM 2166 CB VAL B 163 34.249 -31.317 -9.903 1.00 46.51 C ANISOU 2166 CB VAL B 163 3734 4863 9077 227 -1892 -1157 C ATOM 2167 CG1 VAL B 163 32.768 -31.351 -10.235 1.00 37.84 C ANISOU 2167 CG1 VAL B 163 2852 4171 7356 226 -1678 -1189 C ATOM 2168 CG2 VAL B 163 34.462 -30.859 -8.465 1.00 51.31 C ANISOU 2168 CG2 VAL B 163 4517 5294 9683 361 -2404 -1418 C ATOM 2169 N SER B 164 35.258 -32.637 -12.551 1.00 41.86 N ANISOU 2169 N SER B 164 2707 4253 8947 114 -933 -535 N ATOM 2170 CA SER B 164 34.993 -33.044 -13.925 1.00 44.19 C ANISOU 2170 CA SER B 164 2985 4689 9117 141 -393 -289 C ATOM 2171 C SER B 164 35.490 -34.462 -14.202 1.00 44.14 C ANISOU 2171 C SER B 164 2971 4760 9039 199 -198 -166 C ATOM 2172 O SER B 164 34.938 -35.164 -15.050 1.00 40.08 O ANISOU 2172 O SER B 164 2590 4471 8168 280 155 -76 O ATOM 2173 CB SER B 164 35.619 -32.072 -14.911 1.00 48.29 C ANISOU 2173 CB SER B 164 3316 4877 10155 137 -67 -14 C ATOM 2174 OG SER B 164 37.011 -32.000 -14.713 1.00 57.66 O ANISOU 2174 OG SER B 164 4253 5638 12020 111 -138 133 O ATOM 2175 N ARG B 165 36.539 -34.878 -13.494 1.00 39.54 N ANISOU 2175 N ARG B 165 2256 3961 8808 180 -437 -172 N ATOM 2176 CA ARG B 165 37.021 -36.245 -13.632 1.00 39.39 C ANISOU 2176 CA ARG B 165 2229 4009 8730 236 -292 -73 C ATOM 2177 C ARG B 165 35.966 -37.195 -13.100 1.00 35.53 C ANISOU 2177 C ARG B 165 1980 3923 7599 269 -446 -278 C ATOM 2178 O ARG B 165 35.615 -38.167 -13.758 1.00 33.72 O ANISOU 2178 O ARG B 165 1838 3875 7097 345 -153 -200 O ATOM 2179 CB ARG B 165 38.350 -36.445 -12.896 1.00 43.27 C ANISOU 2179 CB ARG B 165 2518 4160 9761 202 -566 -47 C ATOM 2180 CG ARG B 165 39.415 -35.445 -13.318 1.00 47.93 C ANISOU 2180 CG ARG B 165 2831 4262 11118 156 -464 172 C ATOM 2181 CD ARG B 165 40.813 -35.869 -12.853 1.00 52.29 C ANISOU 2181 CD ARG B 165 3146 4432 12288 133 -635 273 C ATOM 2182 NE ARG B 165 41.775 -34.799 -13.079 1.00 69.98 N ANISOU 2182 NE ARG B 165 5099 6133 15360 78 -629 468 N ATOM 2183 CZ ARG B 165 42.998 -34.775 -12.560 1.00 72.70 C ANISOU 2183 CZ ARG B 165 5189 6011 16422 39 -890 535 C ATOM 2184 NH1 ARG B 165 43.407 -35.767 -11.781 1.00 68.42 N ANISOU 2184 NH1 ARG B 165 4671 5516 15811 50 -1175 410 N ATOM 2185 NH2 ARG B 165 43.807 -33.759 -12.819 1.00 78.19 N ANISOU 2185 NH2 ARG B 165 5601 6163 17943 -6 -874 742 N ATOM 2186 N ILE B 166 35.480 -36.910 -11.898 1.00 34.89 N ANISOU 2186 N ILE B 166 2039 3936 7281 240 -893 -527 N ATOM 2187 CA ILE B 166 34.423 -37.709 -11.294 1.00 31.85 C ANISOU 2187 CA ILE B 166 1916 3897 6290 276 -1033 -683 C ATOM 2188 C ILE B 166 33.215 -37.838 -12.219 1.00 33.74 C ANISOU 2188 C ILE B 166 2262 4395 6162 285 -730 -667 C ATOM 2189 O ILE B 166 32.724 -38.944 -12.431 1.00 29.34 O ANISOU 2189 O ILE B 166 1800 4034 5316 331 -624 -673 O ATOM 2190 CB ILE B 166 34.042 -37.156 -9.906 1.00 32.46 C ANISOU 2190 CB ILE B 166 2214 3999 6121 303 -1459 -904 C ATOM 2191 CG1 ILE B 166 35.264 -37.252 -8.966 1.00 39.56 C ANISOU 2191 CG1 ILE B 166 3039 4624 7369 341 -1793 -954 C ATOM 2192 CG2 ILE B 166 32.879 -37.904 -9.317 1.00 29.86 C ANISOU 2192 CG2 ILE B 166 2194 3996 5157 359 -1499 -986 C ATOM 2193 CD1 ILE B 166 35.016 -36.677 -7.590 1.00 37.90 C ANISOU 2193 CD1 ILE B 166 3083 4379 6936 445 -2199 -1178 C ATOM 2194 N ALA B 167 32.739 -36.727 -12.782 1.00 29.44 N ANISOU 2194 N ALA B 167 1706 3830 5652 254 -604 -661 N ATOM 2195 CA ALA B 167 31.633 -36.788 -13.740 1.00 27.25 C ANISOU 2195 CA ALA B 167 1535 3763 5056 283 -311 -661 C ATOM 2196 C ALA B 167 31.900 -37.754 -14.895 1.00 25.78 C ANISOU 2196 C ALA B 167 1417 3559 4817 382 123 -475 C ATOM 2197 O ALA B 167 31.015 -38.518 -15.326 1.00 25.39 O ANISOU 2197 O ALA B 167 1706 3688 4252 408 229 -499 O ATOM 2198 CB ALA B 167 31.302 -35.400 -14.282 1.00 28.91 C ANISOU 2198 CB ALA B 167 1712 3893 5380 253 -193 -627 C ATOM 2199 N ALA B 168 33.120 -37.730 -15.393 1.00 31.73 N ANISOU 2199 N ALA B 168 1962 4061 6033 442 353 -261 N ATOM 2200 CA ALA B 168 33.495 -38.609 -16.485 1.00 34.58 C ANISOU 2200 CA ALA B 168 2448 4369 6322 603 798 -66 C ATOM 2201 C ALA B 168 33.554 -40.074 -16.036 1.00 30.96 C ANISOU 2201 C ALA B 168 2076 4008 5681 632 688 -139 C ATOM 2202 O ALA B 168 33.103 -40.952 -16.769 1.00 28.49 O ANISOU 2202 O ALA B 168 2104 3774 4947 737 894 -122 O ATOM 2203 CB ALA B 168 34.823 -38.170 -17.097 1.00 36.65 C ANISOU 2203 CB ALA B 168 2570 4317 7038 640 1054 214 C ATOM 2204 N TRP B 169 34.115 -40.343 -14.853 1.00 28.95 N ANISOU 2204 N TRP B 169 1592 3721 5684 546 310 -223 N ATOM 2205 CA TRP B 169 34.171 -41.730 -14.355 1.00 32.78 C ANISOU 2205 CA TRP B 169 2201 4298 5954 564 179 -270 C ATOM 2206 C TRP B 169 32.747 -42.244 -14.163 1.00 25.92 C ANISOU 2206 C TRP B 169 1724 3703 4423 512 52 -421 C ATOM 2207 O TRP B 169 32.434 -43.411 -14.416 1.00 24.68 O ANISOU 2207 O TRP B 169 1787 3605 3987 554 125 -410 O ATOM 2208 CB TRP B 169 34.903 -41.834 -13.016 1.00 29.66 C ANISOU 2208 CB TRP B 169 1595 3836 5838 500 -265 -343 C ATOM 2209 CG TRP B 169 36.284 -41.288 -13.017 1.00 33.53 C ANISOU 2209 CG TRP B 169 1868 4010 6863 468 -250 -193 C ATOM 2210 CD1 TRP B 169 37.134 -41.190 -14.088 1.00 37.29 C ANISOU 2210 CD1 TRP B 169 2232 4259 7676 526 173 54 C ATOM 2211 CD2 TRP B 169 36.998 -40.770 -11.889 1.00 35.44 C ANISOU 2211 CD2 TRP B 169 2014 4079 7375 391 -677 -282 C ATOM 2212 NE1 TRP B 169 38.324 -40.623 -13.694 1.00 39.50 N ANISOU 2212 NE1 TRP B 169 2277 4220 8511 451 22 140 N ATOM 2213 CE2 TRP B 169 38.267 -40.354 -12.351 1.00 39.10 C ANISOU 2213 CE2 TRP B 169 2230 4181 8444 370 -521 -86 C ATOM 2214 CE3 TRP B 169 36.678 -40.588 -10.540 1.00 38.51 C ANISOU 2214 CE3 TRP B 169 2554 4547 7532 372 -1155 -500 C ATOM 2215 CZ2 TRP B 169 39.225 -39.784 -11.507 1.00 42.66 C ANISOU 2215 CZ2 TRP B 169 2526 4321 9363 306 -887 -133 C ATOM 2216 CZ3 TRP B 169 37.632 -40.011 -9.701 1.00 41.28 C ANISOU 2216 CZ3 TRP B 169 2813 4608 8264 351 -1498 -563 C ATOM 2217 CH2 TRP B 169 38.885 -39.614 -10.192 1.00 42.51 C ANISOU 2217 CH2 TRP B 169 2671 4379 9101 306 -1394 -396 C ATOM 2218 N MET B 170 31.879 -41.359 -13.692 1.00 24.07 N ANISOU 2218 N MET B 170 1547 3598 3999 426 -148 -550 N ATOM 2219 CA MET B 170 30.485 -41.754 -13.492 1.00 26.13 C ANISOU 2219 CA MET B 170 2105 4080 3742 381 -238 -640 C ATOM 2220 C MET B 170 29.772 -42.043 -14.798 1.00 22.98 C ANISOU 2220 C MET B 170 1964 3686 3081 421 29 -596 C ATOM 2221 O MET B 170 29.016 -43.023 -14.905 1.00 22.99 O ANISOU 2221 O MET B 170 2177 3754 2806 417 -17 -615 O ATOM 2222 CB MET B 170 29.726 -40.680 -12.716 1.00 21.07 C ANISOU 2222 CB MET B 170 1470 3560 2977 323 -464 -763 C ATOM 2223 CG MET B 170 30.080 -40.617 -11.254 1.00 22.12 C ANISOU 2223 CG MET B 170 1523 3723 3157 353 -826 -860 C ATOM 2224 SD MET B 170 29.260 -39.174 -10.493 1.00 25.58 S ANISOU 2224 SD MET B 170 2131 4172 3417 339 -962 -950 S ATOM 2225 CE MET B 170 27.590 -39.766 -10.311 1.00 27.15 C ANISOU 2225 CE MET B 170 2609 4580 3126 343 -824 -888 C ATOM 2226 N ALA B 171 29.987 -41.177 -15.786 1.00 23.18 N ANISOU 2226 N ALA B 171 1983 3611 3214 482 277 -532 N ATOM 2227 CA ALA B 171 29.297 -41.317 -17.062 1.00 24.40 C ANISOU 2227 CA ALA B 171 2460 3754 3059 583 483 -512 C ATOM 2228 C ALA B 171 29.744 -42.596 -17.751 1.00 26.11 C ANISOU 2228 C ALA B 171 2874 3864 3182 740 644 -458 C ATOM 2229 O ALA B 171 28.933 -43.294 -18.357 1.00 25.30 O ANISOU 2229 O ALA B 171 3101 3767 2746 799 583 -530 O ATOM 2230 CB ALA B 171 29.554 -40.110 -17.963 1.00 28.73 C ANISOU 2230 CB ALA B 171 2982 4202 3730 677 766 -409 C ATOM 2231 N THR B 172 31.036 -42.892 -17.662 1.00 26.50 N ANISOU 2231 N THR B 172 2715 3782 3570 820 818 -335 N ATOM 2232 CA THR B 172 31.565 -44.138 -18.210 1.00 28.87 C ANISOU 2232 CA THR B 172 3190 3970 3809 992 986 -278 C ATOM 2233 C THR B 172 31.016 -45.373 -17.502 1.00 28.87 C ANISOU 2233 C THR B 172 3282 4054 3632 886 667 -399 C ATOM 2234 O THR B 172 30.672 -46.356 -18.163 1.00 26.41 O ANISOU 2234 O THR B 172 3286 3675 3073 1002 677 -447 O ATOM 2235 CB THR B 172 33.095 -44.160 -18.178 1.00 28.46 C ANISOU 2235 CB THR B 172 2821 3738 4254 1098 1256 -81 C ATOM 2236 OG1 THR B 172 33.576 -43.073 -18.980 1.00 36.14 O ANISOU 2236 OG1 THR B 172 3701 4582 5449 1234 1634 100 O ATOM 2237 CG2 THR B 172 33.620 -45.485 -18.708 1.00 30.11 C ANISOU 2237 CG2 THR B 172 3228 3830 4381 1302 1449 -23 C ATOM 2238 N TYR B 173 30.922 -45.327 -16.174 1.00 28.76 N ANISOU 2238 N TYR B 173 3022 4162 3743 700 378 -442 N ATOM 2239 CA TYR B 173 30.379 -46.472 -15.429 1.00 23.92 C ANISOU 2239 CA TYR B 173 2474 3623 2993 622 130 -491 C ATOM 2240 C TYR B 173 28.877 -46.649 -15.753 1.00 27.59 C ANISOU 2240 C TYR B 173 3186 4149 3147 561 -12 -575 C ATOM 2241 O TYR B 173 28.393 -47.771 -15.915 1.00 27.12 O ANISOU 2241 O TYR B 173 3282 4024 3000 570 -117 -594 O ATOM 2242 CB TYR B 173 30.598 -46.337 -13.913 1.00 23.04 C ANISOU 2242 CB TYR B 173 2113 3624 3015 517 -120 -491 C ATOM 2243 CG TYR B 173 30.266 -47.628 -13.177 1.00 25.21 C ANISOU 2243 CG TYR B 173 2441 3941 3195 496 -279 -462 C ATOM 2244 CD1 TYR B 173 31.213 -48.634 -13.051 1.00 30.26 C ANISOU 2244 CD1 TYR B 173 3015 4474 4009 567 -251 -396 C ATOM 2245 CD2 TYR B 173 28.992 -47.867 -12.689 1.00 22.06 C ANISOU 2245 CD2 TYR B 173 2141 3657 2583 422 -415 -462 C ATOM 2246 CE1 TYR B 173 30.914 -49.825 -12.419 1.00 31.50 C ANISOU 2246 CE1 TYR B 173 3216 4647 4105 557 -376 -344 C ATOM 2247 CE2 TYR B 173 28.684 -49.056 -12.052 1.00 24.72 C ANISOU 2247 CE2 TYR B 173 2495 3996 2903 419 -508 -376 C ATOM 2248 CZ TYR B 173 29.652 -50.029 -11.924 1.00 31.64 C ANISOU 2248 CZ TYR B 173 3321 4772 3929 484 -495 -324 C ATOM 2249 OH TYR B 173 29.364 -51.205 -11.294 1.00 34.55 O ANISOU 2249 OH TYR B 173 3697 5124 4305 488 -574 -216 O ATOM 2250 N LEU B 174 28.146 -45.540 -15.848 1.00 24.61 N ANISOU 2250 N LEU B 174 2816 3862 2672 497 -39 -618 N ATOM 2251 CA LEU B 174 26.738 -45.588 -16.246 1.00 26.40 C ANISOU 2251 CA LEU B 174 3232 4107 2692 445 -183 -679 C ATOM 2252 C LEU B 174 26.592 -46.237 -17.628 1.00 29.10 C ANISOU 2252 C LEU B 174 3915 4264 2877 601 -149 -741 C ATOM 2253 O LEU B 174 25.791 -47.163 -17.824 1.00 29.82 O ANISOU 2253 O LEU B 174 4153 4257 2919 583 -371 -795 O ATOM 2254 CB LEU B 174 26.154 -44.158 -16.248 1.00 27.10 C ANISOU 2254 CB LEU B 174 3268 4301 2726 384 -174 -706 C ATOM 2255 CG LEU B 174 24.664 -43.916 -16.450 1.00 33.45 C ANISOU 2255 CG LEU B 174 4172 5138 3399 308 -338 -745 C ATOM 2256 CD1 LEU B 174 23.866 -44.640 -15.374 1.00 30.85 C ANISOU 2256 CD1 LEU B 174 3713 4870 3138 198 -509 -677 C ATOM 2257 CD2 LEU B 174 24.386 -42.404 -16.384 1.00 33.10 C ANISOU 2257 CD2 LEU B 174 4046 5197 3334 270 -279 -761 C ATOM 2258 N ASN B 175 27.382 -45.759 -18.588 1.00 28.08 N ANISOU 2258 N ASN B 175 3925 4052 2691 791 125 -721 N ATOM 2259 CA ASN B 175 27.365 -46.290 -19.940 1.00 35.99 C ANISOU 2259 CA ASN B 175 5356 4871 3449 1047 196 -782 C ATOM 2260 C ASN B 175 27.787 -47.756 -20.059 1.00 36.54 C ANISOU 2260 C ASN B 175 5570 4789 3524 1156 145 -813 C ATOM 2261 O ASN B 175 27.114 -48.544 -20.733 1.00 36.66 O ANISOU 2261 O ASN B 175 5928 4645 3356 1259 -92 -949 O ATOM 2262 CB ASN B 175 28.249 -45.437 -20.845 1.00 47.05 C ANISOU 2262 CB ASN B 175 6862 6215 4800 1291 619 -673 C ATOM 2263 CG ASN B 175 27.445 -44.564 -21.771 1.00 57.22 C ANISOU 2263 CG ASN B 175 8391 7484 5865 1347 586 -692 C ATOM 2264 OD1 ASN B 175 26.768 -43.632 -21.336 1.00 49.18 O ANISOU 2264 OD1 ASN B 175 7211 6599 4876 1179 477 -720 O ATOM 2265 ND2 ASN B 175 27.500 -44.869 -23.063 1.00 67.51 N ANISOU 2265 ND2 ASN B 175 10048 8614 6989 1559 634 -640 N ATOM 2266 N ASP B 176 28.900 -48.124 -19.429 1.00 33.08 N ANISOU 2266 N ASP B 176 4878 4365 3326 1146 323 -700 N ATOM 2267 CA ASP B 176 29.464 -49.455 -19.638 1.00 34.33 C ANISOU 2267 CA ASP B 176 5181 4363 3501 1291 344 -710 C ATOM 2268 C ASP B 176 28.816 -50.524 -18.731 1.00 34.72 C ANISOU 2268 C ASP B 176 5108 4416 3670 1083 -18 -755 C ATOM 2269 O ASP B 176 28.702 -51.692 -19.118 1.00 35.81 O ANISOU 2269 O ASP B 176 5470 4369 3768 1184 -155 -833 O ATOM 2270 CB ASP B 176 31.003 -49.456 -19.485 1.00 37.43 C ANISOU 2270 CB ASP B 176 5351 4718 4154 1411 718 -537 C ATOM 2271 CG ASP B 176 31.728 -48.586 -20.538 1.00 43.67 C ANISOU 2271 CG ASP B 176 6265 5425 4903 1689 1179 -412 C ATOM 2272 OD1 ASP B 176 31.110 -48.095 -21.511 1.00 46.15 O ANISOU 2272 OD1 ASP B 176 6941 5708 4887 1850 1228 -474 O ATOM 2273 OD2 ASP B 176 32.952 -48.376 -20.390 1.00 45.98 O ANISOU 2273 OD2 ASP B 176 6273 5658 5541 1766 1507 -216 O ATOM 2274 N HIS B 177 28.379 -50.139 -17.536 1.00 30.68 N ANISOU 2274 N HIS B 177 4263 4089 3306 831 -161 -694 N ATOM 2275 CA HIS B 177 27.950 -51.135 -16.551 1.00 31.17 C ANISOU 2275 CA HIS B 177 4167 4155 3519 684 -388 -643 C ATOM 2276 C HIS B 177 26.523 -51.025 -16.005 1.00 34.95 C ANISOU 2276 C HIS B 177 4555 4696 4027 501 -633 -624 C ATOM 2277 O HIS B 177 26.041 -51.964 -15.383 1.00 39.40 O ANISOU 2277 O HIS B 177 5016 5200 4754 419 -785 -540 O ATOM 2278 CB HIS B 177 28.932 -51.195 -15.380 1.00 30.12 C ANISOU 2278 CB HIS B 177 3729 4145 3571 638 -299 -515 C ATOM 2279 CG HIS B 177 30.315 -51.595 -15.782 1.00 39.57 C ANISOU 2279 CG HIS B 177 4929 5225 4880 804 -80 -482 C ATOM 2280 ND1 HIS B 177 30.672 -52.911 -16.015 1.00 43.03 N ANISOU 2280 ND1 HIS B 177 5481 5493 5377 904 -88 -477 N ATOM 2281 CD2 HIS B 177 31.427 -50.859 -16.009 1.00 39.49 C ANISOU 2281 CD2 HIS B 177 4794 5209 5001 900 172 -423 C ATOM 2282 CE1 HIS B 177 31.944 -52.964 -16.358 1.00 44.07 C ANISOU 2282 CE1 HIS B 177 5570 5540 5635 1068 176 -415 C ATOM 2283 NE2 HIS B 177 32.428 -51.733 -16.370 1.00 40.89 N ANISOU 2283 NE2 HIS B 177 5000 5223 5313 1067 346 -363 N ATOM 2284 N LEU B 178 25.861 -49.891 -16.204 1.00 27.96 N ANISOU 2284 N LEU B 178 3677 3913 3034 449 -639 -661 N ATOM 2285 CA LEU B 178 24.519 -49.707 -15.644 1.00 29.17 C ANISOU 2285 CA LEU B 178 3698 4117 3268 294 -816 -597 C ATOM 2286 C LEU B 178 23.440 -49.634 -16.722 1.00 32.69 C ANISOU 2286 C LEU B 178 4349 4388 3684 300 -1038 -714 C ATOM 2287 O LEU B 178 22.327 -50.135 -16.537 1.00 29.90 O ANISOU 2287 O LEU B 178 3898 3911 3552 194 -1271 -656 O ATOM 2288 CB LEU B 178 24.465 -48.474 -14.746 1.00 24.92 C ANISOU 2288 CB LEU B 178 2965 3831 2671 228 -697 -530 C ATOM 2289 CG LEU B 178 25.289 -48.509 -13.458 1.00 28.51 C ANISOU 2289 CG LEU B 178 3234 4438 3159 240 -609 -429 C ATOM 2290 CD1 LEU B 178 25.111 -47.223 -12.660 1.00 28.13 C ANISOU 2290 CD1 LEU B 178 3080 4592 3016 223 -573 -420 C ATOM 2291 CD2 LEU B 178 24.947 -49.737 -12.591 1.00 24.68 C ANISOU 2291 CD2 LEU B 178 2655 3915 2806 221 -678 -264 C ATOM 2292 N GLU B 179 23.780 -49.005 -17.842 1.00 33.05 N ANISOU 2292 N GLU B 179 4669 4395 3492 446 -967 -855 N ATOM 2293 CA GLU B 179 22.890 -48.917 -19.000 1.00 38.85 C ANISOU 2293 CA GLU B 179 5700 4940 4120 526 -1224 -1004 C ATOM 2294 C GLU B 179 22.278 -50.260 -19.481 1.00 40.63 C ANISOU 2294 C GLU B 179 6094 4839 4505 558 -1620 -1105 C ATOM 2295 O GLU B 179 21.071 -50.317 -19.764 1.00 38.25 O ANISOU 2295 O GLU B 179 5764 4374 4397 477 -1920 -1111 O ATOM 2296 CB GLU B 179 23.605 -48.192 -20.151 1.00 40.49 C ANISOU 2296 CB GLU B 179 6258 5143 3983 778 -1009 -1104 C ATOM 2297 CG GLU B 179 22.857 -48.178 -21.463 1.00 49.11 C ANISOU 2297 CG GLU B 179 7639 6019 5002 897 -1175 -1145 C ATOM 2298 CD GLU B 179 21.660 -47.256 -21.454 1.00 57.42 C ANISOU 2298 CD GLU B 179 8541 7119 6158 741 -1297 -1099 C ATOM 2299 OE1 GLU B 179 21.458 -46.533 -20.455 1.00 55.93 O ANISOU 2299 OE1 GLU B 179 8042 7143 6067 548 -1203 -1020 O ATOM 2300 OE2 GLU B 179 20.914 -47.253 -22.459 1.00 65.15 O ANISOU 2300 OE2 GLU B 179 9725 7912 7115 844 -1498 -1140 O ATOM 2301 N PRO B 180 23.096 -51.329 -19.589 1.00 42.51 N ANISOU 2301 N PRO B 180 6457 4950 4747 675 -1586 -1139 N ATOM 2302 CA PRO B 180 22.503 -52.610 -19.996 1.00 46.95 C ANISOU 2302 CA PRO B 180 7165 5157 5519 701 -2015 -1250 C ATOM 2303 C PRO B 180 21.376 -53.057 -19.066 1.00 45.68 C ANISOU 2303 C PRO B 180 6575 4917 5864 422 -2260 -1079 C ATOM 2304 O PRO B 180 20.334 -53.481 -19.557 1.00 50.94 O ANISOU 2304 O PRO B 180 7271 5286 6799 394 -2651 -1130 O ATOM 2305 CB PRO B 180 23.690 -53.575 -19.930 1.00 47.86 C ANISOU 2305 CB PRO B 180 7374 5216 5592 839 -1831 -1250 C ATOM 2306 CG PRO B 180 24.856 -52.706 -20.256 1.00 46.17 C ANISOU 2306 CG PRO B 180 7297 5218 5027 1022 -1371 -1235 C ATOM 2307 CD PRO B 180 24.569 -51.419 -19.533 1.00 42.47 C ANISOU 2307 CD PRO B 180 6499 5049 4589 822 -1201 -1098 C ATOM 2308 N TRP B 181 21.573 -52.944 -17.757 1.00 40.03 N ANISOU 2308 N TRP B 181 5460 4450 5300 261 -1969 -823 N ATOM 2309 CA TRP B 181 20.512 -53.255 -16.800 1.00 38.46 C ANISOU 2309 CA TRP B 181 4853 4202 5560 57 -2064 -574 C ATOM 2310 C TRP B 181 19.290 -52.335 -16.928 1.00 35.73 C ANISOU 2310 C TRP B 181 4383 3860 5334 -43 -2195 -538 C ATOM 2311 O TRP B 181 18.150 -52.805 -16.995 1.00 40.86 O ANISOU 2311 O TRP B 181 4845 4223 6458 -148 -2513 -455 O ATOM 2312 CB TRP B 181 21.055 -53.235 -15.365 1.00 35.34 C ANISOU 2312 CB TRP B 181 4165 4096 5167 4 -1686 -307 C ATOM 2313 CG TRP B 181 20.046 -53.677 -14.330 1.00 33.78 C ANISOU 2313 CG TRP B 181 3584 3836 5413 -122 -1674 23 C ATOM 2314 CD1 TRP B 181 19.857 -54.942 -13.847 1.00 36.56 C ANISOU 2314 CD1 TRP B 181 3747 3968 6176 -160 -1739 222 C ATOM 2315 CD2 TRP B 181 19.102 -52.843 -13.647 1.00 34.50 C ANISOU 2315 CD2 TRP B 181 3431 4072 5604 -190 -1530 236 C ATOM 2316 NE1 TRP B 181 18.860 -54.944 -12.902 1.00 34.53 N ANISOU 2316 NE1 TRP B 181 3129 3707 6283 -234 -1604 585 N ATOM 2317 CE2 TRP B 181 18.375 -53.671 -12.766 1.00 34.63 C ANISOU 2317 CE2 TRP B 181 3115 3944 6099 -241 -1467 596 C ATOM 2318 CE3 TRP B 181 18.800 -51.475 -13.698 1.00 31.94 C ANISOU 2318 CE3 TRP B 181 3137 3969 5030 -190 -1422 179 C ATOM 2319 CZ2 TRP B 181 17.356 -53.176 -11.950 1.00 40.92 C ANISOU 2319 CZ2 TRP B 181 3622 4812 7114 -261 -1257 920 C ATOM 2320 CZ3 TRP B 181 17.799 -50.983 -12.875 1.00 33.03 C ANISOU 2320 CZ3 TRP B 181 3002 4186 5362 -226 -1258 457 C ATOM 2321 CH2 TRP B 181 17.091 -51.831 -12.013 1.00 36.61 C ANISOU 2321 CH2 TRP B 181 3141 4496 6275 -246 -1155 832 C ATOM 2322 N ILE B 182 19.520 -51.022 -16.956 1.00 31.26 N ANISOU 2322 N ILE B 182 3883 3584 4412 -12 -1960 -581 N ATOM 2323 CA ILE B 182 18.430 -50.059 -17.069 1.00 29.56 C ANISOU 2323 CA ILE B 182 3556 3394 4281 -92 -2048 -546 C ATOM 2324 C ILE B 182 17.504 -50.374 -18.269 1.00 35.47 C ANISOU 2324 C ILE B 182 4502 3776 5199 -46 -2391 -671 C ATOM 2325 O ILE B 182 16.274 -50.319 -18.156 1.00 36.86 O ANISOU 2325 O ILE B 182 4457 3790 5759 -145 -2524 -534 O ATOM 2326 CB ILE B 182 19.002 -48.627 -17.152 1.00 28.35 C ANISOU 2326 CB ILE B 182 3526 3561 3684 -27 -1755 -625 C ATOM 2327 CG1 ILE B 182 19.758 -48.298 -15.859 1.00 28.40 C ANISOU 2327 CG1 ILE B 182 3329 3879 3584 -46 -1371 -461 C ATOM 2328 CG2 ILE B 182 17.903 -47.602 -17.417 1.00 30.16 C ANISOU 2328 CG2 ILE B 182 3691 3801 3969 -84 -1809 -599 C ATOM 2329 CD1 ILE B 182 20.626 -46.999 -15.953 1.00 30.23 C ANISOU 2329 CD1 ILE B 182 3670 4360 3458 27 -1123 -564 C ATOM 2330 N GLN B 183 18.096 -50.738 -19.402 1.00 37.53 N ANISOU 2330 N GLN B 183 5180 3889 5190 152 -2498 -895 N ATOM 2331 CA GLN B 183 17.328 -51.001 -20.612 1.00 41.60 C ANISOU 2331 CA GLN B 183 5943 4075 5788 288 -2822 -1006 C ATOM 2332 C GLN B 183 16.541 -52.311 -20.531 1.00 45.40 C ANISOU 2332 C GLN B 183 6271 4152 6827 235 -3216 -949 C ATOM 2333 O GLN B 183 15.500 -52.461 -21.170 1.00 47.41 O ANISOU 2333 O GLN B 183 6550 4104 7359 285 -3551 -959 O ATOM 2334 CB GLN B 183 18.232 -50.997 -21.847 1.00 47.61 C ANISOU 2334 CB GLN B 183 7206 4814 6070 589 -2783 -1202 C ATOM 2335 CG GLN B 183 18.738 -49.612 -22.249 1.00 55.08 C ANISOU 2335 CG GLN B 183 8297 6046 6586 676 -2430 -1210 C ATOM 2336 CD GLN B 183 17.626 -48.565 -22.354 1.00 60.92 C ANISOU 2336 CD GLN B 183 8898 6816 7431 579 -2480 -1148 C ATOM 2337 OE1 GLN B 183 17.453 -47.732 -21.458 1.00 59.74 O ANISOU 2337 OE1 GLN B 183 8450 6914 7333 388 -2266 -1034 O ATOM 2338 NE2 GLN B 183 16.879 -48.598 -23.453 1.00 66.26 N ANISOU 2338 NE2 GLN B 183 9812 7233 8130 739 -2784 -1225 N ATOM 2339 N GLU B 184 17.030 -53.256 -19.736 1.00 42.91 N ANISOU 2339 N GLU B 184 5773 3807 6724 144 -3194 -868 N ATOM 2340 CA GLU B 184 16.322 -54.523 -19.556 1.00 50.27 C ANISOU 2340 CA GLU B 184 6491 4338 8272 83 -3526 -757 C ATOM 2341 C GLU B 184 15.264 -54.403 -18.461 1.00 53.37 C ANISOU 2341 C GLU B 184 6341 4699 9238 -154 -3424 -406 C ATOM 2342 O GLU B 184 14.440 -55.304 -18.268 1.00 58.73 O ANISOU 2342 O GLU B 184 6760 5008 10548 -206 -3650 -226 O ATOM 2343 CB GLU B 184 17.313 -55.639 -19.238 1.00 53.11 C ANISOU 2343 CB GLU B 184 6891 4644 8644 108 -3532 -796 C ATOM 2344 CG GLU B 184 18.280 -55.889 -20.384 1.00 65.10 C ANISOU 2344 CG GLU B 184 8964 6137 9635 400 -3610 -1103 C ATOM 2345 CD GLU B 184 19.278 -56.993 -20.103 1.00 73.52 C ANISOU 2345 CD GLU B 184 10098 7128 10708 443 -3603 -1160 C ATOM 2346 OE1 GLU B 184 19.594 -57.234 -18.916 1.00 76.75 O ANISOU 2346 OE1 GLU B 184 10157 7642 11361 233 -3426 -985 O ATOM 2347 OE2 GLU B 184 19.753 -57.616 -21.078 1.00 78.83 O ANISOU 2347 OE2 GLU B 184 11174 7647 11131 704 -3768 -1356 O ATOM 2348 N ASN B 185 15.284 -53.272 -17.762 1.00 45.80 N ANISOU 2348 N ASN B 185 5212 4122 8069 -254 -3062 -280 N ATOM 2349 CA ASN B 185 14.394 -53.045 -16.633 1.00 45.05 C ANISOU 2349 CA ASN B 185 4629 4072 8417 -413 -2839 103 C ATOM 2350 C ASN B 185 13.434 -51.870 -16.817 1.00 44.54 C ANISOU 2350 C ASN B 185 4508 4069 8345 -434 -2787 145 C ATOM 2351 O ASN B 185 12.958 -51.268 -15.855 1.00 43.38 O ANISOU 2351 O ASN B 185 4039 4113 8330 -509 -2473 430 O ATOM 2352 CB ASN B 185 15.208 -52.932 -15.344 1.00 48.61 C ANISOU 2352 CB ASN B 185 4843 4914 8712 -457 -2430 320 C ATOM 2353 CG ASN B 185 15.693 -54.282 -14.851 1.00 47.20 C ANISOU 2353 CG ASN B 185 4526 4578 8829 -472 -2455 458 C ATOM 2354 OD1 ASN B 185 15.016 -54.924 -14.048 1.00 50.46 O ANISOU 2354 OD1 ASN B 185 4573 4819 9780 -531 -2323 835 O ATOM 2355 ND2 ASN B 185 16.857 -54.736 -15.344 1.00 38.36 N ANISOU 2355 ND2 ASN B 185 3721 3490 7363 -387 -2574 178 N ATOM 2356 N GLY B 186 13.151 -51.548 -18.071 1.00 44.62 N ANISOU 2356 N GLY B 186 4851 3916 8188 -326 -3083 -122 N ATOM 2357 CA GLY B 186 12.116 -50.585 -18.379 1.00 44.03 C ANISOU 2357 CA GLY B 186 4719 3805 8204 -340 -3119 -82 C ATOM 2358 C GLY B 186 12.610 -49.171 -18.525 1.00 40.94 C ANISOU 2358 C GLY B 186 4508 3833 7215 -306 -2857 -216 C ATOM 2359 O GLY B 186 11.809 -48.245 -18.575 1.00 40.82 O ANISOU 2359 O GLY B 186 4397 3855 7259 -336 -2817 -151 O ATOM 2360 N GLY B 187 13.927 -48.989 -18.559 1.00 37.35 N ANISOU 2360 N GLY B 187 4290 3673 6229 -236 -2670 -380 N ATOM 2361 CA GLY B 187 14.502 -47.680 -18.818 1.00 32.67 C ANISOU 2361 CA GLY B 187 3889 3422 5104 -173 -2428 -504 C ATOM 2362 C GLY B 187 14.275 -46.641 -17.735 1.00 36.70 C ANISOU 2362 C GLY B 187 4092 4252 5601 -278 -2127 -321 C ATOM 2363 O GLY B 187 13.612 -46.896 -16.730 1.00 35.39 O ANISOU 2363 O GLY B 187 3551 4066 5830 -378 -2048 -54 O ATOM 2364 N TRP B 188 14.854 -45.461 -17.935 1.00 31.94 N ANISOU 2364 N TRP B 188 3651 3927 4558 -220 -1924 -433 N ATOM 2365 CA TRP B 188 14.719 -44.381 -16.965 1.00 28.21 C ANISOU 2365 CA TRP B 188 2944 3750 4026 -271 -1676 -304 C ATOM 2366 C TRP B 188 13.254 -43.948 -16.780 1.00 35.28 C ANISOU 2366 C TRP B 188 3580 4530 5295 -340 -1727 -127 C ATOM 2367 O TRP B 188 12.864 -43.524 -15.692 1.00 32.11 O ANISOU 2367 O TRP B 188 2872 4286 5043 -369 -1517 98 O ATOM 2368 CB TRP B 188 15.601 -43.184 -17.353 1.00 28.06 C ANISOU 2368 CB TRP B 188 3163 3967 3531 -194 -1475 -460 C ATOM 2369 CG TRP B 188 17.037 -43.336 -16.965 1.00 28.05 C ANISOU 2369 CG TRP B 188 3263 4132 3262 -135 -1288 -526 C ATOM 2370 CD1 TRP B 188 18.093 -43.589 -17.795 1.00 30.03 C ANISOU 2370 CD1 TRP B 188 3799 4323 3290 -35 -1229 -656 C ATOM 2371 CD2 TRP B 188 17.575 -43.263 -15.646 1.00 25.03 C ANISOU 2371 CD2 TRP B 188 2689 3985 2837 -131 -1072 -435 C ATOM 2372 NE1 TRP B 188 19.247 -43.662 -17.075 1.00 31.53 N ANISOU 2372 NE1 TRP B 188 3942 4674 3362 1 -1037 -660 N ATOM 2373 CE2 TRP B 188 18.963 -43.466 -15.751 1.00 25.35 C ANISOU 2373 CE2 TRP B 188 2882 4088 2662 -57 -957 -544 C ATOM 2374 CE3 TRP B 188 17.022 -43.023 -14.384 1.00 25.41 C ANISOU 2374 CE3 TRP B 188 2496 4167 2993 -145 -895 -228 C ATOM 2375 CZ2 TRP B 188 19.808 -43.442 -14.642 1.00 21.49 C ANISOU 2375 CZ2 TRP B 188 2292 3775 2099 -27 -765 -486 C ATOM 2376 CZ3 TRP B 188 17.863 -43.012 -13.279 1.00 26.07 C ANISOU 2376 CZ3 TRP B 188 2559 4441 2905 -69 -684 -180 C ATOM 2377 CH2 TRP B 188 19.246 -43.219 -13.419 1.00 23.71 C ANISOU 2377 CH2 TRP B 188 2397 4185 2426 -26 -664 -326 C ATOM 2378 N ASP B 189 12.449 -44.088 -17.835 1.00 34.58 N ANISOU 2378 N ASP B 189 3620 4145 5375 -328 -1994 -203 N ATOM 2379 CA ASP B 189 11.022 -43.790 -17.763 1.00 44.32 C ANISOU 2379 CA ASP B 189 4612 5187 7040 -387 -2083 -31 C ATOM 2380 C ASP B 189 10.320 -44.616 -16.686 1.00 41.77 C ANISOU 2380 C ASP B 189 3882 4713 7275 -469 -1997 303 C ATOM 2381 O ASP B 189 9.421 -44.134 -15.999 1.00 40.92 O ANISOU 2381 O ASP B 189 3481 4610 7456 -495 -1810 563 O ATOM 2382 CB ASP B 189 10.347 -44.033 -19.118 1.00 53.01 C ANISOU 2382 CB ASP B 189 5944 5919 8278 -328 -2474 -177 C ATOM 2383 CG ASP B 189 10.588 -45.436 -19.648 1.00 57.83 C ANISOU 2383 CG ASP B 189 6710 6213 9048 -276 -2769 -268 C ATOM 2384 OD1 ASP B 189 9.796 -46.362 -19.336 1.00 67.07 O ANISOU 2384 OD1 ASP B 189 7635 7052 10798 -342 -2954 -95 O ATOM 2385 OD2 ASP B 189 11.575 -45.610 -20.391 1.00 57.67 O ANISOU 2385 OD2 ASP B 189 7058 6252 8604 -147 -2802 -491 O ATOM 2386 N THR B 190 10.738 -45.864 -16.532 1.00 38.54 N ANISOU 2386 N THR B 190 3461 4155 7026 -483 -2084 333 N ATOM 2387 CA THR B 190 10.200 -46.687 -15.465 1.00 45.82 C ANISOU 2387 CA THR B 190 4005 4937 8467 -533 -1919 706 C ATOM 2388 C THR B 190 10.636 -46.177 -14.093 1.00 42.66 C ANISOU 2388 C THR B 190 3404 4939 7868 -483 -1431 943 C ATOM 2389 O THR B 190 9.849 -46.168 -13.154 1.00 40.91 O ANISOU 2389 O THR B 190 2890 4682 7972 -447 -1127 1320 O ATOM 2390 CB THR B 190 10.585 -48.149 -15.654 1.00 50.99 C ANISOU 2390 CB THR B 190 4701 5321 9352 -549 -2139 682 C ATOM 2391 OG1 THR B 190 10.038 -48.599 -16.898 1.00 49.99 O ANISOU 2391 OG1 THR B 190 4771 4778 9444 -527 -2610 487 O ATOM 2392 CG2 THR B 190 10.029 -48.999 -14.534 1.00 54.70 C ANISOU 2392 CG2 THR B 190 4774 5627 10383 -578 -1912 1126 C ATOM 2393 N PHE B 191 11.884 -45.730 -13.977 1.00 37.80 N ANISOU 2393 N PHE B 191 2977 4682 6705 -431 -1339 742 N ATOM 2394 CA PHE B 191 12.340 -45.126 -12.728 1.00 34.25 C ANISOU 2394 CA PHE B 191 2428 4612 5974 -314 -902 928 C ATOM 2395 C PHE B 191 11.492 -43.913 -12.373 1.00 40.34 C ANISOU 2395 C PHE B 191 3070 5502 6755 -257 -682 1064 C ATOM 2396 O PHE B 191 11.115 -43.726 -11.213 1.00 43.43 O ANISOU 2396 O PHE B 191 3311 6020 7172 -110 -267 1382 O ATOM 2397 CB PHE B 191 13.818 -44.736 -12.820 1.00 34.43 C ANISOU 2397 CB PHE B 191 2834 4912 5337 -246 -848 603 C ATOM 2398 CG PHE B 191 14.293 -43.869 -11.681 1.00 31.51 C ANISOU 2398 CG PHE B 191 2542 4880 4549 -85 -467 655 C ATOM 2399 CD1 PHE B 191 14.639 -44.431 -10.464 1.00 32.71 C ANISOU 2399 CD1 PHE B 191 2668 5144 4614 58 -198 871 C ATOM 2400 CD2 PHE B 191 14.386 -42.488 -11.828 1.00 28.98 C ANISOU 2400 CD2 PHE B 191 2352 4737 3922 -47 -414 481 C ATOM 2401 CE1 PHE B 191 15.062 -43.635 -9.409 1.00 32.40 C ANISOU 2401 CE1 PHE B 191 2779 5380 4150 264 67 878 C ATOM 2402 CE2 PHE B 191 14.829 -41.693 -10.777 1.00 31.17 C ANISOU 2402 CE2 PHE B 191 2736 5272 3836 125 -152 484 C ATOM 2403 CZ PHE B 191 15.164 -42.267 -9.568 1.00 32.43 C ANISOU 2403 CZ PHE B 191 2916 5532 3873 294 62 665 C ATOM 2404 N VAL B 192 11.208 -43.080 -13.371 1.00 38.07 N ANISOU 2404 N VAL B 192 2918 5165 6383 -324 -925 816 N ATOM 2405 CA VAL B 192 10.332 -41.937 -13.164 1.00 40.94 C ANISOU 2405 CA VAL B 192 3176 5589 6789 -280 -753 920 C ATOM 2406 C VAL B 192 8.975 -42.419 -12.647 1.00 39.09 C ANISOU 2406 C VAL B 192 2664 5068 7121 -271 -599 1300 C ATOM 2407 O VAL B 192 8.422 -41.820 -11.738 1.00 45.93 O ANISOU 2407 O VAL B 192 3406 6042 8003 -138 -217 1561 O ATOM 2408 CB VAL B 192 10.195 -41.066 -14.430 1.00 37.56 C ANISOU 2408 CB VAL B 192 2967 5106 6197 -342 -1055 604 C ATOM 2409 CG1 VAL B 192 9.213 -39.915 -14.198 1.00 37.65 C ANISOU 2409 CG1 VAL B 192 2837 5155 6315 -302 -887 733 C ATOM 2410 CG2 VAL B 192 11.555 -40.495 -14.807 1.00 34.36 C ANISOU 2410 CG2 VAL B 192 2861 4965 5230 -312 -1098 297 C ATOM 2411 N GLU B 193 8.482 -43.528 -13.200 1.00 43.56 N ANISOU 2411 N GLU B 193 3169 5243 8138 -378 -886 1344 N ATOM 2412 CA GLU B 193 7.227 -44.152 -12.754 1.00 53.66 C ANISOU 2412 CA GLU B 193 4161 6160 10069 -375 -784 1748 C ATOM 2413 C GLU B 193 7.298 -44.610 -11.291 1.00 58.08 C ANISOU 2413 C GLU B 193 4557 6834 10675 -216 -270 2164 C ATOM 2414 O GLU B 193 6.391 -44.328 -10.501 1.00 61.14 O ANISOU 2414 O GLU B 193 4783 7151 11297 -81 82 2539 O ATOM 2415 CB GLU B 193 6.877 -45.351 -13.646 1.00 60.68 C ANISOU 2415 CB GLU B 193 5042 6576 11438 -493 -1250 1684 C ATOM 2416 CG GLU B 193 6.025 -46.407 -12.947 1.00 75.11 C ANISOU 2416 CG GLU B 193 6547 8025 13968 -469 -1114 2148 C ATOM 2417 CD GLU B 193 6.269 -47.825 -13.450 1.00 82.66 C ANISOU 2417 CD GLU B 193 7520 8629 15260 -539 -1485 2077 C ATOM 2418 OE1 GLU B 193 7.013 -47.999 -14.437 1.00 84.83 O ANISOU 2418 OE1 GLU B 193 8097 8924 15212 -592 -1871 1650 O ATOM 2419 OE2 GLU B 193 5.719 -48.771 -12.849 1.00 86.70 O ANISOU 2419 OE2 GLU B 193 7757 8824 16359 -503 -1373 2467 O ATOM 2420 N LEU B 194 8.381 -45.310 -10.938 1.00 49.51 N ANISOU 2420 N LEU B 194 3559 5917 9337 -190 -217 2110 N ATOM 2421 CA LEU B 194 8.552 -45.862 -9.593 1.00 54.25 C ANISOU 2421 CA LEU B 194 4082 6621 9911 9 252 2496 C ATOM 2422 C LEU B 194 8.721 -44.783 -8.533 1.00 53.78 C ANISOU 2422 C LEU B 194 4162 6949 9321 279 728 2599 C ATOM 2423 O LEU B 194 8.198 -44.912 -7.424 1.00 58.91 O ANISOU 2423 O LEU B 194 4787 7573 10025 529 1150 3000 O ATOM 2424 CB LEU B 194 9.751 -46.820 -9.532 1.00 53.02 C ANISOU 2424 CB LEU B 194 4010 6564 9570 -18 160 2380 C ATOM 2425 CG LEU B 194 9.620 -48.165 -10.244 1.00 54.65 C ANISOU 2425 CG LEU B 194 4118 6347 10301 -199 -228 2358 C ATOM 2426 CD1 LEU B 194 10.966 -48.872 -10.300 1.00 52.59 C ANISOU 2426 CD1 LEU B 194 3993 6245 9743 -220 -345 2155 C ATOM 2427 CD2 LEU B 194 8.570 -49.039 -9.557 1.00 56.95 C ANISOU 2427 CD2 LEU B 194 4131 6262 11244 -122 -10 2878 C ATOM 2428 N TYR B 195 9.468 -43.735 -8.861 1.00 49.21 N ANISOU 2428 N TYR B 195 3779 6701 8216 276 642 2234 N ATOM 2429 CA TYR B 195 9.682 -42.652 -7.909 1.00 53.84 C ANISOU 2429 CA TYR B 195 4580 7623 8255 556 1016 2250 C ATOM 2430 C TYR B 195 8.383 -41.921 -7.588 1.00 57.72 C ANISOU 2430 C TYR B 195 5000 7971 8961 663 1233 2486 C ATOM 2431 O TYR B 195 8.125 -41.588 -6.431 1.00 62.53 O ANISOU 2431 O TYR B 195 5762 8669 9327 982 1623 2716 O ATOM 2432 CB TYR B 195 10.734 -41.640 -8.386 1.00 51.58 C ANISOU 2432 CB TYR B 195 4514 7666 7417 530 836 1800 C ATOM 2433 CG TYR B 195 10.791 -40.459 -7.446 1.00 56.53 C ANISOU 2433 CG TYR B 195 5407 8542 7529 824 1142 1770 C ATOM 2434 CD1 TYR B 195 11.371 -40.584 -6.188 1.00 59.25 C ANISOU 2434 CD1 TYR B 195 6057 9040 7414 1136 1380 1832 C ATOM 2435 CD2 TYR B 195 10.211 -39.234 -7.787 1.00 57.79 C ANISOU 2435 CD2 TYR B 195 5581 8711 7667 808 1122 1656 C ATOM 2436 CE1 TYR B 195 11.397 -39.520 -5.299 1.00 60.92 C ANISOU 2436 CE1 TYR B 195 6607 9364 7177 1421 1508 1732 C ATOM 2437 CE2 TYR B 195 10.234 -38.161 -6.905 1.00 58.94 C ANISOU 2437 CE2 TYR B 195 6026 9003 7365 1082 1327 1589 C ATOM 2438 CZ TYR B 195 10.827 -38.311 -5.661 1.00 61.97 C ANISOU 2438 CZ TYR B 195 6736 9492 7318 1386 1484 1610 C ATOM 2439 OH TYR B 195 10.855 -37.257 -4.773 1.00 63.68 O ANISOU 2439 OH TYR B 195 7281 9770 7144 1664 1559 1495 O TER 2440 TYR B 195 HETATM 2441 N HT7 C 1 -6.311 -6.201 -20.002 1.00 59.81 N ANISOU 2441 N HT7 C 1 4635 7129 10961 1230 312 1186 N HETATM 2442 CB HT7 C 1 -4.957 -6.747 -20.092 1.00 57.41 C ANISOU 2442 CB HT7 C 1 4509 6977 10328 1193 245 987 C HETATM 2443 CG HT7 C 1 -4.971 -8.216 -19.647 1.00 56.32 C ANISOU 2443 CG HT7 C 1 4333 6916 10150 1112 238 1028 C HETATM 2444 CD HT7 C 1 -5.771 -9.169 -20.487 1.00 56.40 C ANISOU 2444 CD HT7 C 1 4209 6792 10429 960 -111 1200 C HETATM 2445 CE2 HT7 C 1 -5.268 -10.176 -21.380 1.00 51.46 C ANISOU 2445 CE2 HT7 C 1 3674 6175 9704 839 -489 1143 C HETATM 2446 CZ3 HT7 C 1 -3.984 -10.584 -21.770 1.00 49.35 C ANISOU 2446 CZ3 HT7 C 1 3605 6045 9100 823 -610 970 C HETATM 2447 CH3 HT7 C 1 -3.851 -11.614 -22.685 1.00 47.22 C ANISOU 2447 CH3 HT7 C 1 3438 5725 8777 731 -1019 955 C HETATM 2448 CT2 HT7 C 1 -4.975 -12.247 -23.227 1.00 51.18 C ANISOU 2448 CT2 HT7 C 1 3853 6015 9577 640 -1341 1073 C HETATM 2449 CH2 HT7 C 1 -6.241 -11.873 -22.869 1.00 56.87 C ANISOU 2449 CH2 HT7 C 1 4328 6572 10707 625 -1239 1253 C HETATM 2450 CZ2 HT7 C 1 -6.381 -10.828 -21.939 1.00 55.10 C ANISOU 2450 CZ2 HT7 C 1 3996 6425 10516 732 -791 1305 C HETATM 2451 NZ1 HT7 C 1 -7.510 -10.264 -21.402 1.00 62.27 N ANISOU 2451 NZ1 HT7 C 1 4688 7200 11772 769 -575 1492 N HETATM 2452 CE1 HT7 C 1 -7.132 -9.269 -20.531 1.00 62.71 C ANISOU 2452 CE1 HT7 C 1 4792 7395 11639 919 -157 1430 C HETATM 2453 CA HT7 C 1 -4.363 -6.554 -21.492 1.00 56.05 C ANISOU 2453 CA HT7 C 1 4428 6762 10106 1131 -98 958 C HETATM 2454 C HT7 C 1 -2.917 -7.005 -21.534 1.00 54.27 C ANISOU 2454 C HT7 C 1 4371 6667 9582 1113 -99 781 C HETATM 2455 O HT7 C 1 -2.244 -7.052 -20.507 1.00 51.99 O ANISOU 2455 O HT7 C 1 4145 6485 9123 1154 162 622 O ATOM 2456 N ALA C 2 -2.429 -7.354 -22.719 1.00 48.84 N ANISOU 2456 N ALA C 2 3784 5954 8818 1081 -410 812 N ATOM 2457 CA ALA C 2 -1.045 -7.768 -22.850 1.00 46.70 C ANISOU 2457 CA ALA C 2 3791 5794 8158 1020 -370 641 C ATOM 2458 C ALA C 2 -0.119 -6.594 -22.526 1.00 47.84 C ANISOU 2458 C ALA C 2 4039 5914 8224 1066 -99 507 C ATOM 2459 O ALA C 2 0.753 -6.726 -21.678 1.00 42.51 O ANISOU 2459 O ALA C 2 3420 5316 7416 1043 80 324 O ATOM 2460 CB ALA C 2 -0.767 -8.326 -24.233 1.00 45.30 C ANISOU 2460 CB ALA C 2 3874 5583 7755 1004 -706 695 C ATOM 2461 N ARG C 3 -0.330 -5.442 -23.169 1.00 47.68 N ANISOU 2461 N ARG C 3 4028 5753 8336 1138 -103 600 N ATOM 2462 CA ARG C 3 0.500 -4.271 -22.882 1.00 48.30 C ANISOU 2462 CA ARG C 3 4149 5738 8464 1175 119 493 C ATOM 2463 C ARG C 3 0.291 -3.851 -21.437 1.00 46.73 C ANISOU 2463 C ARG C 3 3815 5541 8399 1243 320 320 C ATOM 2464 O ARG C 3 1.241 -3.481 -20.739 1.00 39.82 O ANISOU 2464 O ARG C 3 3013 4630 7485 1252 432 106 O ATOM 2465 CB ARG C 3 0.204 -3.120 -23.845 1.00 58.57 C ANISOU 2465 CB ARG C 3 5465 6867 9924 1257 90 666 C ATOM 2466 CG ARG C 3 0.658 -3.410 -25.267 1.00 67.24 C ANISOU 2466 CG ARG C 3 6817 7945 10785 1283 -47 832 C ATOM 2467 CD ARG C 3 0.342 -2.277 -26.226 1.00 75.64 C ANISOU 2467 CD ARG C 3 7934 8836 11971 1414 -54 1042 C ATOM 2468 NE ARG C 3 0.773 -2.596 -27.587 1.00 81.74 N ANISOU 2468 NE ARG C 3 9040 9592 12425 1529 -151 1222 N ATOM 2469 CZ ARG C 3 0.017 -3.220 -28.487 1.00 84.74 C ANISOU 2469 CZ ARG C 3 9611 9986 12603 1630 -504 1328 C ATOM 2470 NH1 ARG C 3 -1.216 -3.599 -28.174 1.00 86.50 N ANISOU 2470 NH1 ARG C 3 9629 10216 13022 1580 -800 1299 N ATOM 2471 NH2 ARG C 3 0.493 -3.468 -29.701 1.00 85.90 N ANISOU 2471 NH2 ARG C 3 10160 10106 12373 1813 -572 1473 N HETATM 2472 N B3E C 4 -0.964 -3.963 -21.000 1.00 48.24 N ANISOU 2472 N B3E C 4 3837 5752 8739 1313 345 421 N HETATM 2473 CB B3E C 4 -1.119 -3.001 -19.921 1.00 51.13 C ANISOU 2473 CB B3E C 4 4230 6058 9137 1431 555 274 C HETATM 2474 CG B3E C 4 -2.145 -1.958 -20.351 1.00 61.06 C ANISOU 2474 CG B3E C 4 5394 7178 10627 1484 551 433 C HETATM 2475 CD B3E C 4 -1.850 -0.544 -19.878 1.00 70.25 C ANISOU 2475 CD B3E C 4 6625 8186 11883 1593 675 280 C HETATM 2476 CE B3E C 4 -2.278 -0.247 -18.451 1.00 77.81 C ANISOU 2476 CE B3E C 4 7643 9163 12758 1785 874 128 C HETATM 2477 OF2 B3E C 4 -1.700 -0.842 -17.514 1.00 78.32 O ANISOU 2477 OF2 B3E C 4 7833 9326 12600 1862 942 -61 O HETATM 2478 OF1 B3E C 4 -3.186 0.601 -18.269 1.00 81.62 O ANISOU 2478 OF1 B3E C 4 8074 9555 13381 1897 966 202 O HETATM 2479 CA B3E C 4 -1.624 -3.710 -18.672 1.00 48.27 C ANISOU 2479 CA B3E C 4 3871 5830 8639 1518 715 228 C HETATM 2480 C B3E C 4 -0.557 -4.626 -18.072 1.00 41.85 C ANISOU 2480 C B3E C 4 3176 5145 7579 1501 735 41 C HETATM 2481 O B3E C 4 0.208 -4.182 -17.219 1.00 46.40 O ANISOU 2481 O B3E C 4 3901 5687 8044 1618 814 -213 O ATOM 2482 N ILE C 5 -0.508 -5.882 -18.510 1.00 41.25 N ANISOU 2482 N ILE C 5 3048 5187 7439 1369 623 146 N ATOM 2483 CA ILE C 5 0.390 -6.859 -17.911 1.00 41.39 C ANISOU 2483 CA ILE C 5 3161 5336 7230 1349 653 -5 C ATOM 2484 C ILE C 5 1.848 -6.421 -18.022 1.00 39.52 C ANISOU 2484 C ILE C 5 3117 5046 6851 1278 571 -248 C ATOM 2485 O ILE C 5 2.555 -6.385 -17.016 1.00 42.18 O ANISOU 2485 O ILE C 5 3591 5394 7043 1367 624 -487 O ATOM 2486 CB ILE C 5 0.222 -8.279 -18.506 1.00 42.13 C ANISOU 2486 CB ILE C 5 3188 5537 7281 1190 492 151 C ATOM 2487 CG1 ILE C 5 -1.149 -8.858 -18.159 1.00 45.64 C ANISOU 2487 CG1 ILE C 5 3480 5993 7870 1208 544 373 C ATOM 2488 CG2 ILE C 5 1.311 -9.213 -17.982 1.00 41.00 C ANISOU 2488 CG2 ILE C 5 3214 5529 6835 1130 498 -23 C ATOM 2489 CD1 ILE C 5 -1.503 -10.093 -18.957 1.00 42.64 C ANISOU 2489 CD1 ILE C 5 3000 5614 7587 1043 280 532 C ATOM 2490 N GLY C 6 2.281 -6.083 -19.239 1.00 35.21 N ANISOU 2490 N GLY C 6 2586 4415 6375 1148 439 -165 N ATOM 2491 CA GLY C 6 3.657 -5.671 -19.481 1.00 36.21 C ANISOU 2491 CA GLY C 6 2820 4443 6495 1077 408 -301 C ATOM 2492 C GLY C 6 4.106 -4.500 -18.619 1.00 34.18 C ANISOU 2492 C GLY C 6 2572 4003 6411 1186 450 -532 C ATOM 2493 O GLY C 6 5.153 -4.577 -17.972 1.00 36.75 O ANISOU 2493 O GLY C 6 2977 4279 6706 1178 390 -759 O ATOM 2494 N ALA C 7 3.310 -3.431 -18.589 1.00 35.92 N ANISOU 2494 N ALA C 7 2717 4095 6836 1302 506 -490 N ATOM 2495 CA ALA C 7 3.621 -2.245 -17.785 1.00 39.39 C ANISOU 2495 CA ALA C 7 3192 4314 7462 1441 499 -732 C ATOM 2496 C ALA C 7 3.436 -2.541 -16.308 1.00 45.08 C ANISOU 2496 C ALA C 7 4070 5111 7949 1655 537 -983 C ATOM 2497 O ALA C 7 4.098 -1.942 -15.451 1.00 40.57 O ANISOU 2497 O ALA C 7 3657 4376 7382 1770 418 -1279 O ATOM 2498 CB ALA C 7 2.765 -1.059 -18.211 1.00 43.70 C ANISOU 2498 CB ALA C 7 3650 4709 8244 1509 556 -593 C HETATM 2499 N B3Q C 8 2.472 -3.420 -16.034 1.00 46.42 N ANISOU 2499 N B3Q C 8 4218 5501 7919 1726 692 -825 N HETATM 2500 CB AB3Q C 8 2.212 -3.190 -14.612 0.54 40.71 C ANISOU 2500 CB AB3Q C 8 3715 4776 6978 2026 797 -1018 C HETATM 2501 CB BB3Q C 8 2.147 -3.230 -14.626 0.46 40.68 C ANISOU 2501 CB BB3Q C 8 3703 4783 6971 2026 809 -1001 C HETATM 2502 CG AB3Q C 8 0.852 -2.506 -14.366 0.54 47.51 C ANISOU 2502 CG AB3Q C 8 4544 5622 7886 2228 1002 -845 C HETATM 2503 CG BB3Q C 8 0.715 -2.697 -14.506 0.46 46.59 C ANISOU 2503 CG BB3Q C 8 4382 5543 7777 2194 1017 -783 C HETATM 2504 CA AB3Q C 8 2.273 -4.524 -13.872 0.54 43.19 C ANISOU 2504 CA AB3Q C 8 4132 5312 6965 2099 891 -1025 C HETATM 2505 CA BB3Q C 8 2.266 -4.546 -13.864 0.46 43.06 C ANISOU 2505 CA BB3Q C 8 4115 5299 6945 2100 894 -1023 C HETATM 2506 C B3Q C 8 3.698 -5.095 -13.787 1.00 41.11 C ANISOU 2506 C B3Q C 8 3980 5060 6578 1959 657 -1265 C HETATM 2507 O B3Q C 8 4.395 -4.847 -12.814 1.00 45.60 O ANISOU 2507 O B3Q C 8 4817 5539 6971 2103 529 -1545 O HETATM 2508 CD AB3Q C 8 0.621 -1.178 -15.081 0.54 47.86 C ANISOU 2508 CD AB3Q C 8 4486 5456 8243 2169 931 -802 C HETATM 2509 CD BB3Q C 8 0.472 -1.767 -13.332 0.46 48.86 C ANISOU 2509 CD BB3Q C 8 4929 5714 7920 2558 1114 -983 C HETATM 2510 CE AB3Q C 8 1.296 0.033 -14.454 0.54 53.13 C ANISOU 2510 CE AB3Q C 8 5356 5862 8968 2316 806 -1119 C HETATM 2511 CE BB3Q C 8 -0.896 -1.119 -13.413 0.46 53.29 C ANISOU 2511 CE BB3Q C 8 5357 6269 8621 2655 1268 -795 C HETATM 2512 NF2AB3Q C 8 1.178 1.183 -15.112 0.54 53.42 N ANISOU 2512 NF2AB3Q C 8 5282 5698 9316 2243 741 -1067 N HETATM 2513 NF2BB3Q C 8 -1.627 -1.411 -14.483 0.46 52.53 N ANISOU 2513 NF2BB3Q C 8 4969 6226 8763 2402 1280 -460 N HETATM 2514 OF1AB3Q C 8 1.913 -0.049 -13.391 0.54 57.77 O ANISOU 2514 OF1AB3Q C 8 6218 6404 9327 2484 735 -1399 O HETATM 2515 OF1BB3Q C 8 -1.290 -0.366 -12.525 0.46 57.92 O ANISOU 2515 OF1BB3Q C 8 6111 6765 9129 2940 1348 -962 O HETATM 2516 N AHP C 9 4.121 -5.861 -14.797 1.00 35.72 N ANISOU 2516 N AHP C 9 3154 4470 5946 1657 575 -1101 N HETATM 2517 CA AHP C 9 5.448 -6.486 -14.797 1.00 34.29 C ANISOU 2517 CA AHP C 9 3051 4304 5676 1509 395 -1255 C HETATM 2518 C AHP C 9 6.575 -5.480 -14.580 1.00 36.97 C ANISOU 2518 C AHP C 9 3444 4364 6240 1514 171 -1536 C HETATM 2519 O AHP C 9 7.444 -5.698 -13.731 1.00 39.94 O ANISOU 2519 O AHP C 9 3977 4687 6512 1591 -9 -1808 O HETATM 2520 CB AHP C 9 5.727 -7.281 -16.081 1.00 36.20 C ANISOU 2520 CB AHP C 9 3157 4640 5959 1229 368 -1018 C HETATM 2521 CG AHP C 9 4.876 -8.524 -16.305 1.00 39.53 C ANISOU 2521 CG AHP C 9 3521 5284 6212 1183 458 -789 C HETATM 2522 CD AHP C 9 5.277 -9.684 -15.414 1.00 42.24 C ANISOU 2522 CD AHP C 9 3978 5787 6284 1224 473 -886 C HETATM 2523 CE AHP C 9 4.475 -10.930 -15.773 1.00 46.88 C ANISOU 2523 CE AHP C 9 4453 6536 6823 1143 530 -629 C HETATM 2524 CZ AHP C 9 4.654 -12.063 -14.780 1.00 46.97 C ANISOU 2524 CZ AHP C 9 4553 6698 6596 1224 610 -666 C ATOM 2525 N ARG C 10 6.570 -4.398 -15.357 1.00 37.75 N ANISOU 2525 N ARG C 10 3397 4253 6694 1438 153 -1458 N ATOM 2526 CA ARG C 10 7.693 -3.464 -15.326 1.00 38.16 C ANISOU 2526 CA ARG C 10 3403 3973 7121 1395 -68 -1657 C ATOM 2527 C ARG C 10 7.684 -2.773 -13.981 1.00 44.95 C ANISOU 2527 C ARG C 10 4501 4681 7897 1647 -251 -2005 C ATOM 2528 O ARG C 10 8.704 -2.707 -13.289 1.00 43.46 O ANISOU 2528 O ARG C 10 4425 4337 7750 1652 -546 -2265 O ATOM 2529 CB ARG C 10 7.616 -2.457 -16.464 1.00 45.67 C ANISOU 2529 CB ARG C 10 4143 4724 8485 1280 5 -1432 C ATOM 2530 CG ARG C 10 8.881 -1.646 -16.630 1.00 47.35 C ANISOU 2530 CG ARG C 10 4218 4567 9206 1178 -178 -1522 C ATOM 2531 CD ARG C 10 8.579 -0.180 -16.823 1.00 57.70 C ANISOU 2531 CD ARG C 10 5458 5607 10857 1198 -198 -1486 C ATOM 2532 NE ARG C 10 7.334 0.025 -17.555 1.00 56.82 N ANISOU 2532 NE ARG C 10 5320 5646 10626 1242 47 -1214 N ATOM 2533 CZ ARG C 10 7.237 -0.157 -18.863 1.00 54.43 C ANISOU 2533 CZ ARG C 10 4895 5405 10382 1130 235 -854 C ATOM 2534 NH1 ARG C 10 8.307 -0.542 -19.550 1.00 60.26 N ANISOU 2534 NH1 ARG C 10 5542 6079 11273 994 279 -703 N ATOM 2535 NH2 ARG C 10 6.084 0.012 -19.475 1.00 43.69 N ANISOU 2535 NH2 ARG C 10 3528 4163 8910 1185 373 -632 N HETATM 2536 N HR7 C 11 6.516 -2.248 -13.625 1.00 50.87 N ANISOU 2536 N HR7 C 11 5354 5477 8495 1844 -89 -1958 N HETATM 2537 CB HR7 C 11 6.668 -1.258 -12.574 1.00 56.84 C ANISOU 2537 CB HR7 C 11 6362 6014 9220 2046 -292 -2241 C HETATM 2538 CG HR7 C 11 5.956 0.049 -12.940 1.00 61.53 C ANISOU 2538 CG HR7 C 11 6872 6423 10086 2098 -213 -2160 C HETATM 2539 CD HR7 C 11 6.301 0.495 -14.352 1.00 68.20 C ANISOU 2539 CD HR7 C 11 7357 7123 11433 1810 -201 -1934 C HETATM 2540 CE HR7 C 11 6.806 1.931 -14.430 1.00 79.26 C ANISOU 2540 CE HR7 C 11 8681 8143 13289 1761 -416 -2040 C HETATM 2541 NZ HR7 C 11 8.249 2.069 -14.202 1.00 84.00 N ANISOU 2541 NZ HR7 C 11 9216 8498 14202 1617 -762 -2236 N HETATM 2542 CH HR7 C 11 9.137 2.546 -15.081 1.00 83.28 C ANISOU 2542 CH HR7 C 11 8811 8156 14675 1367 -821 -2080 C HETATM 2543 NH2 HR7 C 11 8.752 2.937 -16.291 1.00 81.59 N ANISOU 2543 NH2 HR7 C 11 8385 7919 14697 1249 -544 -1721 N HETATM 2544 NH1 HR7 C 11 10.421 2.629 -14.750 1.00 83.90 N ANISOU 2544 NH1 HR7 C 11 8781 8007 15088 1249 -1146 -2242 N HETATM 2545 C HR7 C 11 6.933 -2.849 -10.706 1.00 50.30 C ANISOU 2545 C HR7 C 11 6043 5496 7571 2325 -336 -2453 C HETATM 2546 O HR7 C 11 7.932 -2.445 -10.117 1.00 51.34 O ANISOU 2546 O HR7 C 11 6309 5430 7767 2334 -719 -2726 O HETATM 2547 CA HR7 C 11 6.000 -1.828 -11.342 1.00 56.72 C ANISOU 2547 CA HR7 C 11 6695 6205 8652 2347 -147 -2301 C ATOM 2548 N MET C 12 6.633 -4.143 -10.861 1.00 48.74 N ANISOU 2548 N MET C 12 5797 5591 7130 2281 -109 -2260 N ATOM 2549 CA MET C 12 7.292 -5.210 -10.098 1.00 48.97 C ANISOU 2549 CA MET C 12 6025 5761 6819 2312 -218 -2355 C ATOM 2550 C MET C 12 8.789 -5.360 -10.366 1.00 51.07 C ANISOU 2550 C MET C 12 6185 5882 7337 2093 -605 -2548 C ATOM 2551 O MET C 12 9.569 -5.553 -9.437 1.00 49.43 O ANISOU 2551 O MET C 12 6199 5629 6954 2180 -891 -2747 O ATOM 2552 CB MET C 12 6.631 -6.568 -10.355 1.00 48.99 C ANISOU 2552 CB MET C 12 5931 6082 6602 2267 114 -2063 C ATOM 2553 CG MET C 12 5.112 -6.607 -10.253 1.00 56.89 C ANISOU 2553 CG MET C 12 6895 7205 7517 2422 530 -1771 C ATOM 2554 SD MET C 12 4.467 -8.283 -10.514 1.00 58.36 S ANISOU 2554 SD MET C 12 6899 7693 7584 2313 822 -1411 S ATOM 2555 CE MET C 12 5.087 -8.662 -12.127 1.00 71.04 C ANISOU 2555 CE MET C 12 8145 9351 9496 1954 638 -1368 C ATOM 2556 N ALA C 13 9.176 -5.288 -11.635 1.00 41.02 N ANISOU 2556 N ALA C 13 4556 4526 6503 1823 -595 -2441 N ATOM 2557 CA ALA C 13 10.565 -5.530 -12.043 1.00 40.42 C ANISOU 2557 CA ALA C 13 4301 4290 6767 1600 -852 -2527 C ATOM 2558 C ALA C 13 11.487 -4.419 -11.529 1.00 51.19 C ANISOU 2558 C ALA C 13 5674 5289 8487 1602 -1274 -2771 C ATOM 2559 O ALA C 13 12.595 -4.678 -11.072 1.00 47.73 O ANISOU 2559 O ALA C 13 5232 4745 8159 1552 -1600 -2919 O ATOM 2560 CB ALA C 13 10.650 -5.625 -13.543 1.00 37.87 C ANISOU 2560 CB ALA C 13 3628 3960 6801 1339 -640 -2231 C ATOM 2561 N ASP C 14 11.016 -3.180 -11.614 1.00 46.20 N ANISOU 2561 N ASP C 14 5018 4465 8069 1659 -1286 -2790 N ATOM 2562 CA ASP C 14 11.755 -2.034 -11.090 1.00 56.43 C ANISOU 2562 CA ASP C 14 6305 5417 9719 1680 -1710 -3013 C ATOM 2563 C ASP C 14 11.582 -1.983 -9.581 1.00 61.16 C ANISOU 2563 C ASP C 14 7349 6083 9804 2005 -1945 -3269 C ATOM 2564 O ASP C 14 12.276 -1.248 -8.886 1.00 67.40 O ANISOU 2564 O ASP C 14 8202 6633 10775 2089 -2392 -3497 O ATOM 2565 CB ASP C 14 11.298 -0.746 -11.764 1.00 58.09 C ANISOU 2565 CB ASP C 14 6329 5398 10345 1624 -1619 -2916 C ATOM 2566 CG ASP C 14 11.543 -0.770 -13.260 1.00 53.60 C ANISOU 2566 CG ASP C 14 5352 4749 10266 1336 -1360 -2587 C ATOM 2567 OD1 ASP C 14 12.308 -1.647 -13.711 1.00 47.87 O ANISOU 2567 OD1 ASP C 14 4470 4068 9650 1175 -1323 -2480 O ATOM 2568 OD2 ASP C 14 10.983 0.076 -13.985 1.00 54.33 O ANISOU 2568 OD2 ASP C 14 5301 4736 10607 1295 -1172 -2402 O HETATM 2569 OE1 B3D C 15 8.551 0.535 -6.660 1.00 88.22 O ANISOU 2569 OE1 B3D C 15 11981 9449 12088 3135 -1730 -3613 O HETATM 2570 CD B3D C 15 9.511 -0.231 -6.865 1.00 77.46 C ANISOU 2570 CD B3D C 15 10464 8128 10841 2936 -1941 -3625 C HETATM 2571 OE2 B3D C 15 10.680 0.013 -6.519 1.00 66.37 O ANISOU 2571 OE2 B3D C 15 9020 6519 9679 2890 -2472 -3843 O HETATM 2572 CG B3D C 15 9.251 -1.527 -7.577 1.00 72.59 C ANISOU 2572 CG B3D C 15 9665 7809 10109 2752 -1548 -3350 C HETATM 2573 CB B3D C 15 10.545 -2.318 -7.734 1.00 63.39 C ANISOU 2573 CB B3D C 15 8331 6638 9116 2535 -1856 -3407 C HETATM 2574 N B3D C 15 10.649 -2.801 -9.101 1.00 64.28 N ANISOU 2574 N B3D C 15 8034 6804 9585 2202 -1623 -3185 N HETATM 2575 CA B3D C 15 10.498 -3.473 -6.751 1.00 59.13 C ANISOU 2575 CA B3D C 15 8120 6367 7978 2739 -1793 -3391 C HETATM 2576 C B3D C 15 11.761 -4.304 -6.776 1.00 57.64 C ANISOU 2576 C B3D C 15 7795 6178 7926 2568 -2097 -3442 C ATOM 2577 N LEU C 16 11.852 -5.256 -7.701 1.00 52.48 N ANISOU 2577 N LEU C 16 6876 5688 7377 2309 -1846 -3246 N ATOM 2578 CA LEU C 16 12.965 -6.201 -7.674 1.00 54.19 C ANISOU 2578 CA LEU C 16 6986 5936 7666 2174 -2057 -3260 C ATOM 2579 C LEU C 16 14.332 -5.554 -7.910 1.00 56.96 C ANISOU 2579 C LEU C 16 7040 5938 8664 2009 -2534 -3405 C ATOM 2580 O LEU C 16 15.304 -5.866 -7.212 1.00 58.19 O ANISOU 2580 O LEU C 16 7245 6015 8849 2087 -2902 -3516 O ATOM 2581 CB LEU C 16 12.748 -7.355 -8.675 1.00 50.89 C ANISOU 2581 CB LEU C 16 6351 5758 7226 1942 -1677 -3023 C ATOM 2582 CG LEU C 16 13.800 -8.473 -8.619 1.00 51.23 C ANISOU 2582 CG LEU C 16 6316 5867 7282 1822 -1824 -3011 C ATOM 2583 CD1 LEU C 16 13.792 -9.156 -7.262 1.00 57.97 C ANISOU 2583 CD1 LEU C 16 7550 6877 7598 2096 -1912 -3046 C ATOM 2584 CD2 LEU C 16 13.639 -9.518 -9.733 1.00 40.75 C ANISOU 2584 CD2 LEU C 16 4762 4741 5981 1587 -1479 -2803 C ATOM 2585 N ASN C 17 14.409 -4.669 -8.898 1.00 52.26 N ANISOU 2585 N ASN C 17 6103 5114 8640 1798 -2504 -3355 N ATOM 2586 CA ASN C 17 15.698 -4.169 -9.357 1.00 54.09 C ANISOU 2586 CA ASN C 17 5922 5006 9625 1594 -2831 -3366 C ATOM 2587 C ASN C 17 16.400 -3.314 -8.302 1.00 67.02 C ANISOU 2587 C ASN C 17 7644 6372 11448 1799 -3412 -3617 C ATOM 2588 O ASN C 17 17.619 -3.162 -8.323 1.00 67.28 O ANISOU 2588 O ASN C 17 7370 6143 12052 1723 -3763 -3631 O ATOM 2589 CB ASN C 17 15.548 -3.417 -10.680 1.00 52.77 C ANISOU 2589 CB ASN C 17 5366 4646 10038 1338 -2582 -3171 C ATOM 2590 CG ASN C 17 16.885 -3.035 -11.295 1.00 63.84 C ANISOU 2590 CG ASN C 17 6265 5706 12285 1118 -2774 -3053 C ATOM 2591 OD1 ASN C 17 17.611 -3.884 -11.827 1.00 52.90 O ANISOU 2591 OD1 ASN C 17 4663 4340 11098 967 -2649 -2885 O ATOM 2592 ND2 ASN C 17 17.212 -1.749 -11.237 1.00 67.20 N ANISOU 2592 ND2 ASN C 17 6482 5808 13246 1120 -3045 -3105 N HETATM 2593 CG B3A C 18 15.337 -0.327 -7.162 1.00 75.82 C ANISOU 2593 CG B3A C 18 9127 7047 12634 2224 -3913 -4038 C HETATM 2594 CB B3A C 18 16.242 -1.526 -6.917 1.00 73.94 C ANISOU 2594 CB B3A C 18 8849 6920 12327 2195 -4040 -4002 C HETATM 2595 N B3A C 18 15.621 -2.766 -7.375 1.00 67.31 N ANISOU 2595 N B3A C 18 8096 6454 11024 2095 -3505 -3796 N HETATM 2596 CA B3A C 18 16.557 -1.641 -5.436 1.00 81.27 C ANISOU 2596 CA B3A C 18 10211 7833 12833 2582 -4503 -4255 C HETATM 2597 C B3A C 18 17.788 -2.490 -5.204 1.00 84.50 C ANISOU 2597 C B3A C 18 10468 8184 13453 2555 -4796 -4242 C HETATM 2598 O B3A C 18 18.915 -1.999 -5.295 1.00 88.65 O ANISOU 2598 O B3A C 18 10632 8357 14693 2491 -5242 -4294 O ATOM 2599 N GLN C 19 17.578 -3.774 -4.925 1.00 85.98 N ANISOU 2599 N GLN C 19 10898 8696 13074 2610 -4526 -4145 N ATOM 2600 CA GLN C 19 18.665 -4.656 -4.489 1.00 87.24 C ANISOU 2600 CA GLN C 19 11021 8812 13314 2658 -4799 -4151 C ATOM 2601 C GLN C 19 19.700 -4.988 -5.572 1.00 84.13 C ANISOU 2601 C GLN C 19 10047 8257 13663 2302 -4743 -3964 C ATOM 2602 O GLN C 19 20.829 -5.359 -5.259 1.00 84.54 O ANISOU 2602 O GLN C 19 9968 8112 14041 2348 -5073 -3990 O ATOM 2603 CB GLN C 19 18.105 -5.948 -3.882 1.00 88.55 C ANISOU 2603 CB GLN C 19 11605 9366 12676 2820 -4484 -4067 C ATOM 2604 CG GLN C 19 17.659 -6.984 -4.907 1.00 86.00 C ANISOU 2604 CG GLN C 19 11090 9352 12235 2507 -3883 -3794 C ATOM 2605 CD GLN C 19 17.366 -8.334 -4.278 1.00 85.71 C ANISOU 2605 CD GLN C 19 11374 9638 11556 2650 -3648 -3689 C ATOM 2606 OE1 GLN C 19 16.716 -8.418 -3.235 1.00 89.86 O ANISOU 2606 OE1 GLN C 19 12352 10292 11499 2991 -3624 -3735 O ATOM 2607 NE2 GLN C 19 17.857 -9.399 -4.904 1.00 79.41 N ANISOU 2607 NE2 GLN C 19 10339 8951 10881 2408 -3455 -3526 N ATOM 2608 N TYR C 20 19.315 -4.872 -6.839 1.00 81.00 N ANISOU 2608 N TYR C 20 9322 7917 13538 1983 -4302 -3758 N ATOM 2609 CA TYR C 20 20.256 -5.088 -7.935 1.00 77.74 C ANISOU 2609 CA TYR C 20 8371 7318 13850 1687 -4172 -3530 C ATOM 2610 C TYR C 20 21.013 -3.804 -8.263 1.00 79.39 C ANISOU 2610 C TYR C 20 8136 7066 14964 1632 -4489 -3523 C ATOM 2611 O TYR C 20 22.083 -3.843 -8.873 1.00 75.48 O ANISOU 2611 O TYR C 20 7197 6293 15188 1496 -4490 -3331 O ATOM 2612 CB TYR C 20 19.532 -5.597 -9.185 1.00 75.97 C ANISOU 2612 CB TYR C 20 8014 7336 13513 1411 -3546 -3280 C ATOM 2613 CG TYR C 20 19.023 -7.018 -9.086 1.00 70.75 C ANISOU 2613 CG TYR C 20 7644 7083 12155 1416 -3227 -3223 C ATOM 2614 CD1 TYR C 20 19.544 -7.905 -8.153 1.00 73.84 C ANISOU 2614 CD1 TYR C 20 8266 7566 12224 1582 -3429 -3303 C ATOM 2615 CD2 TYR C 20 18.027 -7.477 -9.936 1.00 64.40 C ANISOU 2615 CD2 TYR C 20 6867 6547 11053 1268 -2734 -3075 C ATOM 2616 CE1 TYR C 20 19.082 -9.209 -8.071 1.00 69.33 C ANISOU 2616 CE1 TYR C 20 7923 7363 11058 1579 -3120 -3214 C ATOM 2617 CE2 TYR C 20 17.559 -8.774 -9.856 1.00 61.67 C ANISOU 2617 CE2 TYR C 20 6742 6561 10126 1281 -2466 -3009 C ATOM 2618 CZ TYR C 20 18.087 -9.635 -8.924 1.00 63.40 C ANISOU 2618 CZ TYR C 20 7165 6883 10041 1425 -2646 -3065 C ATOM 2619 OH TYR C 20 17.622 -10.931 -8.847 1.00 60.03 O ANISOU 2619 OH TYR C 20 6924 6806 9078 1428 -2363 -2959 O HETATM 2620 N NH2 C 21 20.449 -2.666 -7.861 1.00 81.28 N ANISOU 2620 N NH2 C 21 8501 7204 15178 1755 -4718 -3704 N TER 2621 NH2 C 21 HETATM 2622 C ACE D -1 38.689 -49.456 6.867 1.00 73.82 C ANISOU 2622 C ACE D -1 10750 9342 7956 3244 -4897 -1176 C HETATM 2623 O ACE D -1 38.174 -50.238 6.073 1.00 69.12 O ANISOU 2623 O ACE D -1 9917 8973 7372 3047 -4469 -890 O HETATM 2624 CH3 ACE D -1 39.894 -49.796 7.692 1.00 79.48 C ANISOU 2624 CH3 ACE D -1 11570 9802 8826 3416 -5416 -1317 C HETATM 2625 N HT7 D 1 38.660 -48.264 6.285 1.00 72.35 N ANISOU 2625 N HT7 D 1 10407 9031 8052 3067 -4951 -1359 N HETATM 2626 CB HT7 D 1 37.620 -47.848 5.351 1.00 66.95 C ANISOU 2626 CB HT7 D 1 9569 8555 7313 2860 -4498 -1246 C HETATM 2627 CG HT7 D 1 37.096 -46.472 5.754 1.00 68.63 C ANISOU 2627 CG HT7 D 1 10047 8682 7348 3017 -4606 -1489 C HETATM 2628 CD HT7 D 1 36.345 -46.423 7.050 1.00 72.62 C ANISOU 2628 CD HT7 D 1 11125 9273 7195 3487 -4599 -1534 C HETATM 2629 CE2 HT7 D 1 35.009 -46.883 7.289 1.00 71.08 C ANISOU 2629 CE2 HT7 D 1 11161 9387 6458 3665 -4096 -1290 C HETATM 2630 CZ3 HT7 D 1 34.031 -47.488 6.492 1.00 69.68 C ANISOU 2630 CZ3 HT7 D 1 10779 9485 6210 3464 -3558 -978 C HETATM 2631 CH3 HT7 D 1 32.815 -47.814 7.059 1.00 66.67 C ANISOU 2631 CH3 HT7 D 1 10696 9308 5328 3750 -3146 -768 C HETATM 2632 CT2 HT7 D 1 32.541 -47.557 8.402 1.00 72.46 C ANISOU 2632 CT2 HT7 D 1 11949 10002 5581 4266 -3211 -851 C HETATM 2633 CH2 HT7 D 1 33.472 -46.968 9.209 1.00 77.64 C ANISOU 2633 CH2 HT7 D 1 12872 10401 6227 4505 -3755 -1185 C HETATM 2634 CZ2 HT7 D 1 34.713 -46.629 8.636 1.00 76.86 C ANISOU 2634 CZ2 HT7 D 1 12449 10071 6685 4181 -4221 -1409 C HETATM 2635 NZ1 HT7 D 1 35.820 -46.048 9.195 1.00 82.37 N ANISOU 2635 NZ1 HT7 D 1 13276 10434 7586 4311 -4834 -1744 N HETATM 2636 CE1 HT7 D 1 36.793 -45.925 8.236 1.00 79.12 C ANISOU 2636 CE1 HT7 D 1 12365 9858 7839 3874 -5056 -1808 C HETATM 2637 CA HT7 D 1 38.178 -47.826 3.933 1.00 62.87 C ANISOU 2637 CA HT7 D 1 8499 7969 7419 2440 -4385 -1175 C HETATM 2638 C HT7 D 1 37.057 -47.728 2.918 1.00 57.28 C ANISOU 2638 C HT7 D 1 7653 7509 6601 2245 -3895 -1014 C HETATM 2639 O HT7 D 1 35.885 -47.816 3.270 1.00 56.34 O ANISOU 2639 O HT7 D 1 7807 7610 5988 2396 -3632 -920 O ATOM 2640 N ALA D 2 37.428 -47.560 1.652 1.00 54.09 N ANISOU 2640 N ALA D 2 6828 7042 6681 1933 -3763 -973 N ATOM 2641 CA ALA D 2 36.467 -47.324 0.576 1.00 49.26 C ANISOU 2641 CA ALA D 2 6079 6611 6025 1744 -3361 -869 C ATOM 2642 C ALA D 2 35.585 -48.529 0.261 1.00 51.29 C ANISOU 2642 C ALA D 2 6364 7126 5998 1745 -3005 -610 C ATOM 2643 O ALA D 2 34.376 -48.381 0.017 1.00 43.93 O ANISOU 2643 O ALA D 2 5543 6375 4773 1742 -2724 -536 O ATOM 2644 CB ALA D 2 37.186 -46.858 -0.674 1.00 52.09 C ANISOU 2644 CB ALA D 2 6015 6801 6976 1471 -3308 -889 C ATOM 2645 N ARG D 3 36.193 -49.709 0.223 1.00 54.54 N ANISOU 2645 N ARG D 3 6651 7520 6553 1749 -3023 -466 N ATOM 2646 CA AARG D 3 35.458 -50.951 0.016 0.41 55.34 C ANISOU 2646 CA AARG D 3 6779 7801 6446 1784 -2739 -210 C ATOM 2647 CA BARG D 3 35.440 -50.936 0.003 0.59 55.37 C ANISOU 2647 CA BARG D 3 6783 7807 6449 1782 -2735 -211 C ATOM 2648 C ARG D 3 34.397 -51.073 1.100 1.00 52.65 C ANISOU 2648 C ARG D 3 6843 7622 5539 2043 -2634 -118 C ATOM 2649 O ARG D 3 33.244 -51.433 0.828 1.00 46.69 O ANISOU 2649 O ARG D 3 6146 7026 4568 2056 -2306 61 O ATOM 2650 CB AARG D 3 36.418 -52.134 0.090 0.41 59.20 C ANISOU 2650 CB AARG D 3 7118 8200 7177 1810 -2841 -88 C ATOM 2651 CB BARG D 3 36.371 -52.145 -0.013 0.59 59.65 C ANISOU 2651 CB BARG D 3 7157 8262 7246 1795 -2815 -82 C ATOM 2652 CG AARG D 3 36.381 -53.058 -1.110 0.41 60.09 C ANISOU 2652 CG AARG D 3 6941 8319 7571 1664 -2583 70 C ATOM 2653 CG BARG D 3 36.465 -52.829 -1.363 0.59 60.87 C ANISOU 2653 CG BARG D 3 6978 8394 7756 1612 -2575 30 C ATOM 2654 CD AARG D 3 35.482 -54.252 -0.861 0.41 62.35 C ANISOU 2654 CD AARG D 3 7378 8745 7566 1796 -2375 325 C ATOM 2655 CD BARG D 3 37.911 -53.119 -1.745 0.59 63.98 C ANISOU 2655 CD BARG D 3 7064 8564 8679 1532 -2703 1 C ATOM 2656 NE AARG D 3 35.986 -55.446 -1.533 0.41 64.28 N ANISOU 2656 NE AARG D 3 7384 8895 8144 1753 -2291 461 N ATOM 2657 NE BARG D 3 38.008 -53.879 -2.988 0.59 64.18 N ANISOU 2657 NE BARG D 3 6824 8537 9023 1422 -2426 109 N ATOM 2658 CZ AARG D 3 35.363 -56.621 -1.547 0.41 66.18 C ANISOU 2658 CZ AARG D 3 7673 9186 8287 1847 -2103 698 C ATOM 2659 CZ BARG D 3 39.148 -54.146 -3.617 0.59 68.06 C ANISOU 2659 CZ BARG D 3 7023 8816 10018 1346 -2385 122 C ATOM 2660 NH1AARG D 3 34.197 -56.765 -0.931 0.41 64.76 N ANISOU 2660 NH1AARG D 3 7741 9161 7705 1978 -1922 877 N ATOM 2661 NH1BARG D 3 40.298 -53.709 -3.122 0.59 72.92 N ANISOU 2661 NH1BARG D 3 7536 9249 10921 1340 -2639 42 N ATOM 2662 NH2AARG D 3 35.905 -57.652 -2.183 0.41 67.48 N ANISOU 2662 NH2AARG D 3 7635 9200 8805 1763 -1998 782 N ATOM 2663 NH2BARG D 3 39.140 -54.848 -4.743 0.59 67.95 N ANISOU 2663 NH2BARG D 3 6837 8735 10248 1291 -2081 217 N HETATM 2664 N B3E D 4 34.821 -50.752 2.322 1.00 50.51 N ANISOU 2664 N B3E D 4 6848 7279 5062 2278 -2905 -242 N HETATM 2665 CB B3E D 4 33.965 -51.465 3.259 1.00 52.38 C ANISOU 2665 CB B3E D 4 7421 7667 4814 2567 -2700 -33 C HETATM 2666 CG B3E D 4 34.784 -52.533 3.975 1.00 69.45 C ANISOU 2666 CG B3E D 4 9650 9768 6969 2724 -2881 73 C HETATM 2667 CD B3E D 4 33.907 -53.551 4.669 1.00 73.65 C ANISOU 2667 CD B3E D 4 10434 10446 7106 2982 -2556 394 C HETATM 2668 CE B3E D 4 33.376 -54.530 3.648 1.00 72.66 C ANISOU 2668 CE B3E D 4 10020 10384 7201 2782 -2220 681 C HETATM 2669 OF2 B3E D 4 34.086 -54.759 2.640 1.00 66.56 O ANISOU 2669 OF2 B3E D 4 8899 9522 6870 2520 -2337 625 O HETATM 2670 OF1 B3E D 4 32.264 -55.062 3.863 1.00 75.55 O ANISOU 2670 OF1 B3E D 4 10502 10864 7339 2914 -1826 966 O HETATM 2671 CA B3E D 4 33.385 -50.554 4.331 1.00 55.62 C ANISOU 2671 CA B3E D 4 8239 8101 4792 2865 -2727 -169 C HETATM 2672 C B3E D 4 32.355 -49.562 3.793 1.00 52.90 C ANISOU 2672 C B3E D 4 7876 7840 4385 2769 -2487 -221 C HETATM 2673 O B3E D 4 31.162 -49.824 3.882 1.00 52.21 O ANISOU 2673 O B3E D 4 7898 7909 4031 2878 -2098 -4 O ATOM 2674 N ILE D 5 32.813 -48.436 3.252 1.00 51.77 N ANISOU 2674 N ILE D 5 7575 7571 4526 2576 -2701 -480 N ATOM 2675 CA ILE D 5 31.898 -47.413 2.731 1.00 50.84 C ANISOU 2675 CA ILE D 5 7432 7515 4372 2480 -2503 -541 C ATOM 2676 C ILE D 5 30.968 -47.952 1.651 1.00 50.66 C ANISOU 2676 C ILE D 5 7187 7656 4407 2266 -2108 -310 C ATOM 2677 O ILE D 5 29.755 -47.789 1.742 1.00 44.31 O ANISOU 2677 O ILE D 5 6498 6983 3354 2360 -1799 -183 O ATOM 2678 CB ILE D 5 32.654 -46.169 2.218 1.00 48.99 C ANISOU 2678 CB ILE D 5 7015 7085 4514 2288 -2789 -822 C ATOM 2679 CG1 ILE D 5 33.347 -45.473 3.395 1.00 54.28 C ANISOU 2679 CG1 ILE D 5 7967 7551 5104 2565 -3208 -1076 C ATOM 2680 CG2 ILE D 5 31.701 -45.214 1.505 1.00 55.02 C ANISOU 2680 CG2 ILE D 5 7707 7923 5275 2150 -2552 -845 C ATOM 2681 CD1 ILE D 5 34.367 -44.451 2.987 1.00 56.36 C ANISOU 2681 CD1 ILE D 5 8012 7539 5862 2395 -3561 -1324 C ATOM 2682 N GLY D 6 31.541 -48.608 0.648 1.00 42.29 N ANISOU 2682 N GLY D 6 5808 6565 3697 2012 -2121 -252 N ATOM 2683 CA GLY D 6 30.770 -49.174 -0.441 1.00 38.66 C ANISOU 2683 CA GLY D 6 5145 6218 3325 1837 -1817 -73 C ATOM 2684 C GLY D 6 29.780 -50.244 -0.010 1.00 40.27 C ANISOU 2684 C GLY D 6 5475 6564 3262 2015 -1514 249 C ATOM 2685 O GLY D 6 28.645 -50.286 -0.513 1.00 37.53 O ANISOU 2685 O GLY D 6 5067 6325 2867 1968 -1218 409 O ATOM 2686 N ALA D 7 30.214 -51.110 0.905 1.00 42.20 N ANISOU 2686 N ALA D 7 5866 6786 3380 2220 -1576 376 N ATOM 2687 CA ALA D 7 29.372 -52.177 1.450 1.00 43.73 C ANISOU 2687 CA ALA D 7 6171 7071 3372 2423 -1246 742 C ATOM 2688 C ALA D 7 28.368 -51.584 2.425 1.00 59.01 C ANISOU 2688 C ALA D 7 8400 9090 4930 2705 -1005 816 C ATOM 2689 O ALA D 7 27.235 -52.054 2.529 1.00 46.86 O ANISOU 2689 O ALA D 7 6851 7628 3324 2808 -593 1147 O ATOM 2690 CB ALA D 7 30.229 -53.230 2.144 1.00 46.39 C ANISOU 2690 CB ALA D 7 6583 7341 3704 2567 -1386 847 C HETATM 2691 N B3Q D 8 28.829 -50.577 3.162 1.00 48.63 N ANISOU 2691 N B3Q D 8 7325 7723 3430 2852 -1261 526 N HETATM 2692 CB B3Q D 8 27.890 -50.334 4.256 1.00 52.27 C ANISOU 2692 CB B3Q D 8 8105 8252 3505 3233 -980 659 C HETATM 2693 CG B3Q D 8 28.562 -50.555 5.616 1.00 59.92 C ANISOU 2693 CG B3Q D 8 9438 9160 4169 3610 -1173 591 C HETATM 2694 CA B3Q D 8 27.394 -48.902 4.214 1.00 51.88 C ANISOU 2694 CA B3Q D 8 8136 8198 3379 3247 -1000 435 C HETATM 2695 C B3Q D 8 26.444 -48.598 3.050 1.00 47.63 C ANISOU 2695 C B3Q D 8 7307 7737 3054 2963 -743 536 C HETATM 2696 O B3Q D 8 25.232 -48.736 3.212 1.00 48.37 O ANISOU 2696 O B3Q D 8 7407 7912 3059 3103 -330 817 O HETATM 2697 CD B3Q D 8 28.896 -52.002 5.925 1.00 61.30 C ANISOU 2697 CD B3Q D 8 9599 9343 4348 3689 -1086 869 C HETATM 2698 CE B3Q D 8 27.655 -52.854 6.123 1.00 66.92 C ANISOU 2698 CE B3Q D 8 10285 10154 4989 3852 -497 1336 C HETATM 2699 NF2 B3Q D 8 26.581 -52.246 6.624 1.00 64.71 N ANISOU 2699 NF2 B3Q D 8 10166 9930 4491 4112 -159 1430 N HETATM 2700 OF1 B3Q D 8 27.664 -54.051 5.828 1.00 72.33 O ANISOU 2700 OF1 B3Q D 8 10775 10831 5875 3753 -336 1629 O HETATM 2701 N AHP D 9 26.988 -48.172 1.907 1.00 43.78 N ANISOU 2701 N AHP D 9 6558 7204 2874 2594 -972 325 N HETATM 2702 CA AHP D 9 26.179 -47.743 0.762 1.00 40.10 C ANISOU 2702 CA AHP D 9 5849 6796 2589 2337 -794 357 C HETATM 2703 C AHP D 9 25.246 -48.819 0.219 1.00 44.35 C ANISOU 2703 C AHP D 9 6195 7428 3226 2278 -442 742 C HETATM 2704 O AHP D 9 24.074 -48.551 -0.034 1.00 42.57 O ANISOU 2704 O AHP D 9 5896 7266 3012 2276 -155 919 O HETATM 2705 CB AHP D 9 27.069 -47.231 -0.382 1.00 39.56 C ANISOU 2705 CB AHP D 9 5540 6639 2851 1989 -1079 81 C HETATM 2706 CG AHP D 9 27.587 -45.814 -0.205 1.00 44.89 C ANISOU 2706 CG AHP D 9 6289 7197 3571 1968 -1331 -235 C HETATM 2707 CD AHP D 9 26.486 -44.794 -0.458 1.00 50.35 C ANISOU 2707 CD AHP D 9 6996 7943 4192 1952 -1139 -250 C HETATM 2708 CE AHP D 9 26.837 -43.433 0.122 1.00 56.32 C ANISOU 2708 CE AHP D 9 7911 8577 4912 2059 -1367 -509 C HETATM 2709 CZ AHP D 9 28.159 -42.907 -0.402 1.00 56.66 C ANISOU 2709 CZ AHP D 9 7781 8442 5305 1847 -1704 -745 C ATOM 2710 N ARG D 10 25.769 -50.022 0.006 1.00 38.66 N ANISOU 2710 N ARG D 10 5359 6685 2646 2222 -479 893 N ATOM 2711 CA ARG D 10 24.960 -51.100 -0.560 1.00 38.94 C ANISOU 2711 CA ARG D 10 5164 6739 2894 2145 -190 1293 C ATOM 2712 C ARG D 10 23.851 -51.505 0.409 1.00 44.55 C ANISOU 2712 C ARG D 10 5969 7461 3497 2420 246 1694 C ATOM 2713 O ARG D 10 22.694 -51.686 0.009 1.00 41.99 O ANISOU 2713 O ARG D 10 5438 7117 3400 2353 560 2012 O ATOM 2714 CB ARG D 10 25.832 -52.302 -0.926 1.00 39.98 C ANISOU 2714 CB ARG D 10 5149 6792 3250 2053 -341 1365 C ATOM 2715 CG ARG D 10 25.176 -53.239 -1.925 1.00 40.58 C ANISOU 2715 CG ARG D 10 4897 6687 3834 1734 -141 1542 C ATOM 2716 CD ARG D 10 26.080 -54.412 -2.300 1.00 38.98 C ANISOU 2716 CD ARG D 10 4570 6330 3909 1609 -275 1527 C ATOM 2717 NE ARG D 10 26.366 -55.279 -1.164 1.00 41.73 N ANISOU 2717 NE ARG D 10 5054 6701 4100 1907 -204 1815 N ATOM 2718 CZ ARG D 10 27.570 -55.423 -0.613 1.00 41.27 C ANISOU 2718 CZ ARG D 10 5145 6681 3855 2071 -468 1688 C ATOM 2719 NH1 ARG D 10 28.616 -54.771 -1.108 1.00 39.26 N ANISOU 2719 NH1 ARG D 10 4863 6420 3635 1943 -804 1298 N ATOM 2720 NH2 ARG D 10 27.732 -56.233 0.420 1.00 43.18 N ANISOU 2720 NH2 ARG D 10 5538 6917 3951 2336 -383 1945 N HETATM 2721 N HR7 D 11 24.231 -51.662 1.678 1.00 46.80 N ANISOU 2721 N HR7 D 11 6541 7743 3497 2735 260 1689 N HETATM 2722 CB HR7 D 11 23.314 -52.487 2.463 1.00 48.72 C ANISOU 2722 CB HR7 D 11 6785 7964 3761 2991 726 2148 C HETATM 2723 CG HR7 D 11 24.134 -53.598 3.111 1.00 54.08 C ANISOU 2723 CG HR7 D 11 7568 8597 4383 3129 659 2250 C HETATM 2724 CD HR7 D 11 24.280 -54.754 2.146 1.00 57.27 C ANISOU 2724 CD HR7 D 11 7624 8896 5239 2831 649 2470 C HETATM 2725 CE HR7 D 11 23.238 -55.817 2.457 1.00 65.39 C ANISOU 2725 CE HR7 D 11 8444 9814 6587 2915 1139 3007 C HETATM 2726 NZ HR7 D 11 22.210 -55.894 1.425 1.00 66.28 N ANISOU 2726 NZ HR7 D 11 8167 9804 7213 2627 1307 3231 N HETATM 2727 CH HR7 D 11 21.133 -56.669 1.510 1.00 70.65 C ANISOU 2727 CH HR7 D 11 8415 10184 8246 2617 1703 3682 C HETATM 2728 NH2 HR7 D 11 20.941 -57.438 2.576 1.00 70.77 N ANISOU 2728 NH2 HR7 D 11 8471 10173 8246 2909 2029 3974 N HETATM 2729 NH1 HR7 D 11 20.254 -56.675 0.517 1.00 73.58 N ANISOU 2729 NH1 HR7 D 11 8415 10376 9166 2315 1742 3828 N HETATM 2730 C HR7 D 11 21.684 -50.613 3.075 1.00 53.05 C ANISOU 2730 C HR7 D 11 7508 8584 4065 3291 1081 2109 C HETATM 2731 O HR7 D 11 20.536 -50.931 2.774 1.00 55.13 O ANISOU 2731 O HR7 D 11 7500 8804 4642 3249 1461 2480 O HETATM 2732 CA HR7 D 11 22.660 -51.679 3.579 1.00 55.76 C ANISOU 2732 CA HR7 D 11 7960 8901 4327 3378 951 2146 C ATOM 2733 N MET D 12 22.147 -49.366 2.999 1.00 49.47 N ANISOU 2733 N MET D 12 7232 8161 3404 3254 753 1678 N ATOM 2734 CA MET D 12 21.307 -48.221 2.650 1.00 53.37 C ANISOU 2734 CA MET D 12 7677 8672 3927 3207 839 1600 C ATOM 2735 C MET D 12 20.569 -48.348 1.315 1.00 50.71 C ANISOU 2735 C MET D 12 6944 8344 3980 2835 961 1768 C ATOM 2736 O MET D 12 19.377 -48.075 1.236 1.00 50.10 O ANISOU 2736 O MET D 12 6726 8246 4064 2876 1276 2012 O ATOM 2737 CB MET D 12 22.143 -46.941 2.627 1.00 50.18 C ANISOU 2737 CB MET D 12 7467 8251 3348 3147 397 1094 C ATOM 2738 CG MET D 12 22.827 -46.628 3.939 1.00 51.39 C ANISOU 2738 CG MET D 12 8024 8349 3152 3527 208 903 C ATOM 2739 SD MET D 12 24.034 -45.304 3.782 1.00 70.48 S ANISOU 2739 SD MET D 12 10553 10657 5569 3373 -383 347 S ATOM 2740 CE MET D 12 23.039 -43.963 3.157 1.00 65.35 C ANISOU 2740 CE MET D 12 9792 10022 5015 3248 -264 278 C ATOM 2741 N ALA D 13 21.281 -48.750 0.269 1.00 41.09 N ANISOU 2741 N ALA D 13 5545 7132 2935 2495 694 1643 N ATOM 2742 CA ALA D 13 20.696 -48.802 -1.067 1.00 37.95 C ANISOU 2742 CA ALA D 13 4817 6733 2869 2158 725 1757 C ATOM 2743 C ALA D 13 19.646 -49.897 -1.192 1.00 39.65 C ANISOU 2743 C ALA D 13 4733 6818 3514 2118 1097 2299 C ATOM 2744 O ALA D 13 18.584 -49.681 -1.768 1.00 45.34 O ANISOU 2744 O ALA D 13 5188 7433 4607 1944 1254 2436 O ATOM 2745 CB ALA D 13 21.788 -48.976 -2.141 1.00 34.45 C ANISOU 2745 CB ALA D 13 4253 6244 2591 1818 321 1415 C ATOM 2746 N ASP D 14 19.954 -51.072 -0.663 1.00 41.75 N ANISOU 2746 N ASP D 14 4991 7008 3864 2232 1193 2546 N ATOM 2747 CA ASP D 14 19.029 -52.197 -0.701 1.00 48.21 C ANISOU 2747 CA ASP D 14 5472 7611 5235 2178 1525 3061 C ATOM 2748 C ASP D 14 17.844 -51.987 0.247 1.00 54.87 C ANISOU 2748 C ASP D 14 6275 8412 6160 2483 1979 3346 C ATOM 2749 O ASP D 14 16.764 -52.547 0.042 1.00 53.24 O ANISOU 2749 O ASP D 14 5684 7987 6558 2402 2238 3733 O ATOM 2750 CB ASP D 14 19.769 -53.501 -0.425 1.00 47.18 C ANISOU 2750 CB ASP D 14 5331 7388 5209 2204 1470 3194 C ATOM 2751 CG ASP D 14 20.708 -53.874 -1.555 1.00 43.43 C ANISOU 2751 CG ASP D 14 4742 6808 4951 1812 1011 2782 C ATOM 2752 OD1 ASP D 14 20.617 -53.246 -2.635 1.00 40.31 O ANISOU 2752 OD1 ASP D 14 4237 6371 4706 1506 782 2445 O ATOM 2753 OD2 ASP D 14 21.522 -54.793 -1.377 1.00 42.01 O ANISOU 2753 OD2 ASP D 14 4596 6575 4792 1834 903 2799 O HETATM 2754 OE1 B3D D 15 16.381 -52.863 5.476 1.00 90.14 O ANISOU 2754 OE1 B3D D 15 11423 12858 9968 4441 3441 4293 O HETATM 2755 CD B3D D 15 16.113 -52.580 4.288 1.00 82.81 C ANISOU 2755 CD B3D D 15 10187 11878 9397 3987 3246 4211 C HETATM 2756 OE2 B3D D 15 14.937 -52.557 3.863 1.00 86.83 O ANISOU 2756 OE2 B3D D 15 10309 12216 10468 3895 3470 4516 O HETATM 2757 CG B3D D 15 17.269 -52.262 3.351 1.00 68.69 C ANISOU 2757 CG B3D D 15 8507 10211 7380 3569 2704 3737 C HETATM 2758 CB B3D D 15 16.897 -51.444 2.104 1.00 59.20 C ANISOU 2758 CB B3D D 15 7094 8998 6402 3168 2493 3564 C HETATM 2759 N B3D D 15 18.073 -51.183 1.282 1.00 55.69 N ANISOU 2759 N B3D D 15 6769 8670 5720 2852 2015 3139 N HETATM 2760 CA B3D D 15 16.320 -50.101 2.514 1.00 56.08 C ANISOU 2760 CA B3D D 15 6911 8669 5729 3400 2567 3424 C HETATM 2761 C B3D D 15 15.686 -49.349 1.360 1.00 54.19 C ANISOU 2761 C B3D D 15 6415 8390 5784 3042 2452 3347 C ATOM 2762 N LEU D 16 16.452 -48.488 0.672 1.00 48.25 N ANISOU 2762 N LEU D 16 5818 7784 4732 2807 2063 2885 N ATOM 2763 CA LEU D 16 15.875 -47.593 -0.336 1.00 45.97 C ANISOU 2763 CA LEU D 16 5351 7491 4625 2522 1966 2767 C ATOM 2764 C LEU D 16 15.189 -48.360 -1.456 1.00 49.06 C ANISOU 2764 C LEU D 16 5248 7693 5698 2136 2009 3053 C ATOM 2765 O LEU D 16 14.101 -47.978 -1.906 1.00 52.51 O ANISOU 2765 O LEU D 16 5433 7985 6534 2015 2102 3197 O ATOM 2766 CB LEU D 16 16.913 -46.625 -0.927 1.00 44.12 C ANISOU 2766 CB LEU D 16 5331 7427 4005 2342 1538 2219 C ATOM 2767 CG LEU D 16 16.331 -45.706 -2.011 1.00 43.19 C ANISOU 2767 CG LEU D 16 5025 7322 4062 2059 1461 2090 C ATOM 2768 CD1 LEU D 16 15.240 -44.793 -1.441 1.00 46.38 C ANISOU 2768 CD1 LEU D 16 5481 7666 4473 2281 1692 2201 C ATOM 2769 CD2 LEU D 16 17.376 -44.881 -2.717 1.00 34.59 C ANISOU 2769 CD2 LEU D 16 4079 6365 2700 1865 1049 1577 C ATOM 2770 N ASN D 17 15.819 -49.444 -1.898 1.00 48.18 N ANISOU 2770 N ASN D 17 5000 7527 5777 1933 1888 3122 N ATOM 2771 CA ASN D 17 15.246 -50.249 -2.965 1.00 51.88 C ANISOU 2771 CA ASN D 17 5005 7695 7013 1535 1767 3258 C ATOM 2772 C ASN D 17 13.885 -50.805 -2.553 1.00 59.36 C ANISOU 2772 C ASN D 17 5626 8341 8587 1646 2089 3773 C ATOM 2773 O ASN D 17 13.012 -51.021 -3.394 1.00 57.70 O ANISOU 2773 O ASN D 17 5057 7822 9046 1357 1945 3860 O ATOM 2774 CB ASN D 17 16.194 -51.355 -3.428 1.00 45.31 C ANISOU 2774 CB ASN D 17 4153 6743 6318 1330 1444 3083 C ATOM 2775 CG ASN D 17 15.730 -52.000 -4.714 1.00 43.30 C ANISOU 2775 CG ASN D 17 3536 6140 6775 921 1127 3007 C ATOM 2776 OD1 ASN D 17 15.599 -51.329 -5.737 1.00 43.55 O ANISOU 2776 OD1 ASN D 17 3555 6139 6854 689 826 2658 O ATOM 2777 ND2 ASN D 17 15.451 -53.297 -4.665 1.00 49.63 N ANISOU 2777 ND2 ASN D 17 4065 6654 8140 862 1171 3335 N HETATM 2778 CG B3A D 18 13.225 -52.766 0.394 1.00 74.13 C ANISOU 2778 CG B3A D 18 7484 10041 10643 2624 2991 4689 C HETATM 2779 CB B3A D 18 12.692 -51.952 -0.775 1.00 67.66 C ANISOU 2779 CB B3A D 18 6506 9121 10079 2248 2718 4515 C HETATM 2780 N B3A D 18 13.707 -51.024 -1.254 1.00 62.57 N ANISOU 2780 N B3A D 18 6192 8788 8793 2091 2431 4022 N HETATM 2781 CA B3A D 18 11.464 -51.183 -0.326 1.00 72.10 C ANISOU 2781 CA B3A D 18 7028 9588 10780 2497 2993 4738 C HETATM 2782 C B3A D 18 10.765 -50.489 -1.482 1.00 69.69 C ANISOU 2782 C B3A D 18 6522 9122 10835 2112 2729 4609 C HETATM 2783 O B3A D 18 10.205 -51.141 -2.359 1.00 70.36 O ANISOU 2783 O B3A D 18 6235 8855 11645 1778 2505 4720 O ATOM 2784 N GLN D 19 10.813 -49.161 -1.501 1.00 70.24 N ANISOU 2784 N GLN D 19 6859 9424 10404 2159 2704 4329 N ATOM 2785 CA GLN D 19 9.954 -48.377 -2.391 1.00 72.33 C ANISOU 2785 CA GLN D 19 6944 9546 10993 1888 2546 4251 C ATOM 2786 C GLN D 19 10.149 -48.583 -3.905 1.00 66.34 C ANISOU 2786 C GLN D 19 5954 8653 10599 1344 2066 3953 C ATOM 2787 O GLN D 19 9.275 -48.217 -4.693 1.00 67.21 O ANISOU 2787 O GLN D 19 5857 8536 11142 1119 1886 3924 O ATOM 2788 CB GLN D 19 10.015 -46.885 -2.031 1.00 75.05 C ANISOU 2788 CB GLN D 19 7633 10175 10709 2085 2625 3995 C ATOM 2789 CG GLN D 19 11.390 -46.247 -2.189 1.00 72.62 C ANISOU 2789 CG GLN D 19 7681 10237 9673 2034 2380 3475 C ATOM 2790 CD GLN D 19 11.462 -44.867 -1.565 1.00 70.57 C ANISOU 2790 CD GLN D 19 7800 10185 8827 2313 2436 3237 C ATOM 2791 OE1 GLN D 19 11.437 -43.855 -2.268 1.00 68.56 O ANISOU 2791 OE1 GLN D 19 7563 10014 8473 2119 2248 2944 O ATOM 2792 NE2 GLN D 19 11.549 -44.819 -0.237 1.00 69.07 N ANISOU 2792 NE2 GLN D 19 7919 10050 8273 2788 2673 3348 N ATOM 2793 N TYR D 20 11.277 -49.160 -4.313 1.00 58.73 N ANISOU 2793 N TYR D 20 5040 7810 9466 1169 1836 3711 N ATOM 2794 CA TYR D 20 11.506 -49.459 -5.729 1.00 55.11 C ANISOU 2794 CA TYR D 20 4391 7190 9358 729 1337 3383 C ATOM 2795 C TYR D 20 11.267 -50.939 -6.054 1.00 59.80 C ANISOU 2795 C TYR D 20 4725 7362 10633 561 1151 3579 C ATOM 2796 O TYR D 20 11.411 -51.357 -7.206 1.00 60.09 O ANISOU 2796 O TYR D 20 4678 7182 10972 252 667 3279 O ATOM 2797 CB TYR D 20 12.925 -49.057 -6.165 1.00 48.44 C ANISOU 2797 CB TYR D 20 3783 6701 7923 657 1097 2898 C ATOM 2798 CG TYR D 20 13.222 -47.577 -6.047 1.00 53.60 C ANISOU 2798 CG TYR D 20 4753 7678 7935 775 1132 2591 C ATOM 2799 CD1 TYR D 20 12.820 -46.680 -7.033 1.00 54.89 C ANISOU 2799 CD1 TYR D 20 4870 7801 8183 574 876 2317 C ATOM 2800 CD2 TYR D 20 13.910 -47.079 -4.952 1.00 53.63 C ANISOU 2800 CD2 TYR D 20 5120 7994 7262 1108 1376 2565 C ATOM 2801 CE1 TYR D 20 13.087 -45.323 -6.915 1.00 53.22 C ANISOU 2801 CE1 TYR D 20 4922 7855 7442 680 911 2055 C ATOM 2802 CE2 TYR D 20 14.182 -45.737 -4.830 1.00 53.68 C ANISOU 2802 CE2 TYR D 20 5405 8240 6752 1220 1350 2268 C ATOM 2803 CZ TYR D 20 13.772 -44.864 -5.804 1.00 52.50 C ANISOU 2803 CZ TYR D 20 5162 8047 6740 994 1140 2027 C ATOM 2804 OH TYR D 20 14.058 -43.530 -5.659 1.00 53.30 O ANISOU 2804 OH TYR D 20 5522 8359 6372 1106 1117 1746 O HETATM 2805 N NH2 D 21 10.912 -51.729 -5.041 1.00 59.67 N ANISOU 2805 N NH2 D 21 4624 7211 10836 820 1501 4053 N TER 2806 NH2 D 21 HETATM 2807 CD A CD A1196 2.866 2.210 -20.406 0.68 44.39 CD ANISOU 2807 CD A CD A1196 3530 4177 9159 1409 560 -209 CD HETATM 2808 CD B CD A1196 3.564 2.027 -22.304 0.32 45.27 CD ANISOU 2808 CD B CD A1196 3592 4236 9372 1299 640 208 CD HETATM 2809 CD CD A1197 21.300 -22.188 -3.933 1.00 56.44 CD ANISOU 2809 CD CD A1197 7574 7427 6445 1866 -2174 -2315 CD HETATM 2810 CD CD A1198 -10.361 -17.518 -19.467 1.00 68.97 CD ANISOU 2810 CD CD A1198 4653 7030 14522 213 -725 2481 CD HETATM 2811 CD CD A1199 -5.376 -19.528 -16.473 1.00 46.89 CD ANISOU 2811 CD CD A1199 2673 5550 9594 518 266 1836 CD HETATM 2812 CD A CD A1200 13.293 -8.668 -33.556 0.45 62.33 CD ANISOU 2812 CD A CD A1200 9129 7064 7491 3096 2950 2765 CD HETATM 2813 CD B CD A1200 11.955 -8.229 -32.504 0.55 64.09 CD ANISOU 2813 CD B CD A1200 9009 7380 7963 2682 2330 2368 CD HETATM 2814 CD CD A1201 25.149 -14.852 -28.597 1.00 53.81 CD ANISOU 2814 CD CD A1201 5692 4934 9817 1661 3756 2754 CD HETATM 2815 C1 EDO A1202 20.166 -25.813 -12.290 1.00 40.72 C ANISOU 2815 C1 EDO A1202 4384 6155 4933 343 -567 -1367 C HETATM 2816 O1 EDO A1202 19.531 -26.549 -13.357 1.00 39.92 O ANISOU 2816 O1 EDO A1202 4275 6184 4709 249 -380 -1221 O HETATM 2817 C2 EDO A1202 21.515 -26.474 -12.007 1.00 46.67 C ANISOU 2817 C2 EDO A1202 5093 6799 5839 329 -682 -1400 C HETATM 2818 O2 EDO A1202 21.836 -26.326 -10.614 1.00 57.67 O ANISOU 2818 O2 EDO A1202 6605 8110 7197 471 -887 -1493 O HETATM 2819 CD CD B1196 10.826 -47.818 -20.916 1.00 47.47 CD ANISOU 2819 CD CD B1196 5756 4240 8038 -98 -3430 -483 CD HETATM 2820 CD CD B1197 33.152 -46.881 -22.445 1.00 47.68 CD ANISOU 2820 CD CD B1197 6852 5757 5508 2019 1958 23 CD HETATM 2821 CD CD B1198 34.487 -51.223 -17.422 1.00 45.94 CD ANISOU 2821 CD CD B1198 5507 5641 6306 1405 978 -150 CD HETATM 2822 CD CD B1199 9.051 -31.720 -7.814 1.00 54.56 CD ANISOU 2822 CD CD B1199 5898 8607 6226 1208 1179 743 CD HETATM 2823 CD A CD B1200 32.356 -56.357 1.365 0.46 46.20 CD ANISOU 2823 CD A CD B1200 6072 7061 4421 2404 -1640 1158 CD HETATM 2824 CD B CD B1200 32.324 -57.507 -0.142 0.54 88.06 CD ANISOU 2824 CD B CD B1200 10959 12278 10220 2179 -1462 1329 CD HETATM 2825 CD CD B1201 33.027 -32.228 4.599 1.00 74.08 CD ANISOU 2825 CD CD B1201 11140 8078 8928 3400 -5413 -3150 CD HETATM 2826 CD CD B1202 42.325 -36.801 3.989 1.00 97.62 CD ANISOU 2826 CD CD B1202 12306 9046 15739 2378 -7402 -3096 CD HETATM 2827 CD CD B1203 44.623 -38.488 6.859 1.00106.55 CD ANISOU 2827 CD CD B1203 14066 9414 17003 3021 -8937 -3560 CD HETATM 2828 CD A CD B1204 44.376 -22.510 -0.774 0.48118.91 CD ANISOU 2828 CD A CD B1204 11973 8019 25187 1547 -8606 -2979 CD HETATM 2829 CD B CD B1204 45.176 -23.637 -0.289 0.52120.89 CD ANISOU 2829 CD B CD B1204 12260 8142 25532 1567 -8827 -2999 CD HETATM 2830 C1 EDO B1205 18.664 -56.530 -6.608 1.00 50.14 C ANISOU 2830 C1 EDO B1205 4365 6265 8420 374 77 2495 C HETATM 2831 O1 EDO B1205 20.020 -56.978 -6.532 1.00 54.36 O ANISOU 2831 O1 EDO B1205 5132 6911 8612 433 -22 2281 O HETATM 2832 C2 EDO B1205 17.804 -57.596 -7.284 1.00 52.43 C ANISOU 2832 C2 EDO B1205 4318 6068 9535 172 -139 2651 C HETATM 2833 O2 EDO B1205 16.473 -57.092 -7.444 1.00 43.97 O ANISOU 2833 O2 EDO B1205 2971 4847 8888 96 -97 2848 O HETATM 2834 O HOH A2001 25.054 -30.351 -20.123 1.00 60.78 O ANISOU 2834 O HOH A2001 6958 8302 7834 510 984 -351 O HETATM 2835 O HOH A2002 23.327 -29.567 -17.011 1.00 45.08 O ANISOU 2835 O HOH A2002 4741 6627 5759 153 138 -865 O HETATM 2836 O HOH A2003 21.770 -29.234 -21.042 1.00 45.47 O ANISOU 2836 O HOH A2003 5525 6605 5146 504 692 -494 O HETATM 2837 O HOH A2004 20.247 -41.429 -20.310 1.00 49.15 O ANISOU 2837 O HOH A2004 6819 6746 5109 314 -719 -810 O HETATM 2838 O HOH A2005 12.685 -28.488 -5.705 1.00 75.36 O ANISOU 2838 O HOH A2005 9627 11227 7781 1619 446 -382 O HETATM 2839 O HOH A2006 33.771 -34.268 -17.509 1.00 45.23 O ANISOU 2839 O HOH A2006 3531 5238 8418 458 985 221 O HETATM 2840 O HOH A2008 19.565 -26.070 -4.396 1.00 61.76 O ANISOU 2840 O HOH A2008 8244 8785 6437 1625 -1211 -1638 O HETATM 2841 O HOH A2009 23.539 -31.671 -18.168 1.00 47.31 O ANISOU 2841 O HOH A2009 5333 6952 5691 257 333 -731 O HETATM 2842 O AHOH A2010 19.685 -32.157 -23.781 0.45 31.45 O ANISOU 2842 O AHOH A2010 4807 4650 2491 759 198 -525 O HETATM 2843 O BHOH A2010 21.250 -31.942 -24.848 0.26 25.18 O ANISOU 2843 O BHOH A2010 4185 3732 1651 1066 653 -325 O HETATM 2844 O CHOH A2010 20.006 -33.946 -24.809 0.29 28.23 O ANISOU 2844 O CHOH A2010 4745 4073 1910 942 87 -535 O HETATM 2845 O HOH A2013 21.484 -31.442 -20.435 1.00 52.10 O ANISOU 2845 O HOH A2013 6518 7580 5699 434 400 -650 O HETATM 2846 O HOH A2014 34.993 -28.248 -12.781 1.00 61.94 O ANISOU 2846 O HOH A2014 5016 6059 12459 39 -1173 -602 O HETATM 2847 O HOH A2015 20.556 -30.093 -16.819 1.00 34.64 O ANISOU 2847 O HOH A2015 3741 5622 3799 109 -58 -942 O HETATM 2848 O HOH A2016 17.517 -29.676 -13.898 1.00 39.60 O ANISOU 2848 O HOH A2016 4381 6318 4348 166 -183 -820 O HETATM 2849 O HOH A2017 19.668 -35.192 -12.102 1.00 24.89 O ANISOU 2849 O HOH A2017 2616 4485 2358 188 -255 -659 O HETATM 2850 O HOH A2018 26.199 -26.293 -10.175 1.00 32.33 O ANISOU 2850 O HOH A2018 2965 4172 5148 400 -1481 -1656 O HETATM 2851 O AHOH A2019 24.604 -26.048 -16.834 0.54 25.56 O ANISOU 2851 O AHOH A2019 1652 3631 4428 118 123 -841 O HETATM 2852 O BHOH A2019 24.158 -28.044 -15.283 0.46 21.33 O ANISOU 2852 O BHOH A2019 1373 3440 3292 102 -240 -1094 O HETATM 2853 O HOH A2020 14.797 -29.877 -6.622 1.00 48.21 O ANISOU 2853 O HOH A2020 6050 7764 4504 1253 79 -587 O HETATM 2854 O HOH A2021 17.551 -28.298 -2.195 1.00 56.89 O ANISOU 2854 O HOH A2021 8112 8511 4992 2211 -660 -1162 O HETATM 2855 O HOH A2022 25.270 -31.697 -2.065 1.00 43.31 O ANISOU 2855 O HOH A2022 6037 6173 4246 1738 -2007 -1726 O HETATM 2856 O HOH A2023 21.196 -24.471 -4.818 1.00 43.10 O ANISOU 2856 O HOH A2023 5705 6055 4614 1539 -1696 -1973 O HETATM 2857 O HOH A2024 24.874 -24.038 -10.216 1.00 41.82 O ANISOU 2857 O HOH A2024 4215 5304 6369 475 -1526 -1804 O HETATM 2858 O HOH A2025 23.236 -32.021 -0.488 1.00 57.00 O ANISOU 2858 O HOH A2025 8259 8171 5228 2252 -1675 -1538 O HETATM 2859 O HOH A2026 33.328 -26.672 -9.467 1.00 58.57 O ANISOU 2859 O HOH A2026 5251 5751 11252 320 -2393 -1511 O HETATM 2860 O HOH A2027 33.378 -28.982 -14.392 1.00 51.46 O ANISOU 2860 O HOH A2027 3903 5374 10274 51 -473 -413 O HETATM 2861 O HOH A2028 29.334 -28.573 -19.524 1.00 60.67 O ANISOU 2861 O HOH A2028 5876 7422 9752 428 1241 149 O HETATM 2862 O HOH A2029 27.731 -26.325 -18.358 1.00 49.31 O ANISOU 2862 O HOH A2029 4299 6042 8393 223 718 -216 O HETATM 2863 O HOH A2030 29.989 -22.478 -18.311 1.00 42.22 O ANISOU 2863 O HOH A2030 2739 3927 9375 81 604 148 O HETATM 2864 O HOH A2031 30.195 -14.157 -11.987 1.00 63.06 O ANISOU 2864 O HOH A2031 4926 4479 14556 414 -2619 -1583 O HETATM 2865 O HOH A2032 17.861 -28.107 -19.086 1.00 47.64 O ANISOU 2865 O HOH A2032 5650 7224 5227 175 -1 -800 O HETATM 2866 O AHOH A2033 16.572 -25.973 -6.581 0.68 42.97 O ANISOU 2866 O AHOH A2033 5537 6738 4051 1289 -516 -1244 O HETATM 2867 O BHOH A2033 15.216 -24.526 -6.060 0.32 32.45 O ANISOU 2867 O BHOH A2033 4359 5419 2551 1532 -408 -1260 O HETATM 2868 O AHOH A2035 24.180 -19.869 -8.380 0.58 37.38 O ANISOU 2868 O AHOH A2035 3815 4173 6213 921 -2281 -2332 O HETATM 2869 O BHOH A2035 22.530 -19.285 -6.967 0.42 38.59 O ANISOU 2869 O BHOH A2035 4430 4577 5656 1280 -2366 -2485 O HETATM 2870 O HOH A2036 4.943 -19.770 -13.232 1.00 40.57 O ANISOU 2870 O HOH A2036 3609 6462 5345 993 759 -68 O HETATM 2871 O HOH A2037 17.323 -21.124 -15.121 1.00 30.54 O ANISOU 2871 O HOH A2037 2835 4774 3993 250 -296 -1357 O HETATM 2872 O HOH A2038 20.018 -27.329 -17.313 1.00 38.80 O ANISOU 2872 O HOH A2038 4142 6018 4581 124 33 -937 O HETATM 2873 O HOH A2039 17.406 -26.076 -9.017 1.00 33.20 O ANISOU 2873 O HOH A2039 3893 5453 3267 812 -518 -1251 O HETATM 2874 O HOH A2040 15.653 -28.960 -9.595 1.00 32.34 O ANISOU 2874 O HOH A2040 3666 5646 2975 694 -152 -816 O HETATM 2875 O HOH A2041 14.681 -17.778 -4.130 1.00 45.02 O ANISOU 2875 O HOH A2041 6606 6398 4099 2381 -1186 -2134 O HETATM 2876 O HOH A2042 21.144 -20.047 -2.996 1.00 53.84 O ANISOU 2876 O HOH A2042 7477 6799 6181 2240 -2643 -2634 O HETATM 2877 O HOH A2043 19.848 -23.409 -2.479 1.00 55.22 O ANISOU 2877 O HOH A2043 7880 7601 5500 2245 -1837 -2095 O HETATM 2878 O HOH A2044 -4.481 -4.228 -24.897 1.00 44.68 O ANISOU 2878 O HOH A2044 3205 4969 8804 1293 -734 1195 O HETATM 2879 O HOH A2045 18.850 1.204 -14.523 1.00 65.28 O ANISOU 2879 O HOH A2045 4682 4556 15564 467 -2516 -2121 O HETATM 2880 O HOH A2046 7.052 -18.295 -13.848 1.00 27.60 O ANISOU 2880 O HOH A2046 2296 4777 3414 880 447 -602 O HETATM 2881 O HOH A2047 14.627 1.893 -13.338 1.00 79.52 O ANISOU 2881 O HOH A2047 7768 6947 15497 954 -2315 -2711 O HETATM 2882 O HOH A2048 2.215 -8.739 -4.402 1.00 58.35 O ANISOU 2882 O HOH A2048 8349 7833 5987 3806 1674 -1118 O HETATM 2883 O HOH A2049 1.918 -19.485 -13.195 1.00 38.75 O ANISOU 2883 O HOH A2049 2956 5924 5844 1040 1008 500 O HETATM 2884 O HOH A2050 -6.937 -23.440 -15.642 1.00 59.29 O ANISOU 2884 O HOH A2050 3719 6362 12448 305 242 2630 O HETATM 2885 O HOH A2051 -5.167 -17.198 -16.968 1.00 56.49 O ANISOU 2885 O HOH A2051 4031 6942 10491 647 295 1589 O HETATM 2886 O HOH A2052 -10.007 -16.462 -27.945 1.00 58.78 O ANISOU 2886 O HOH A2052 4615 5577 12142 -552 -1532 2071 O HETATM 2887 O HOH A2053 0.446 -17.076 -31.935 1.00 55.98 O ANISOU 2887 O HOH A2053 8149 6403 6718 1529 -3479 63 O HETATM 2888 O HOH A2054 -3.339 -14.537 -35.323 1.00 65.23 O ANISOU 2888 O HOH A2054 9803 6835 8146 2011 -4754 127 O HETATM 2889 O HOH A2055 -3.645 -10.016 -30.118 1.00 60.30 O ANISOU 2889 O HOH A2055 6843 6822 9246 1426 -2994 967 O HETATM 2890 O HOH A2056 -4.007 -8.416 -33.196 1.00 66.91 O ANISOU 2890 O HOH A2056 5136 7591 12697 702 1521 4056 O HETATM 2891 O HOH A2057 3.800 -3.877 -26.719 1.00 53.91 O ANISOU 2891 O HOH A2057 5644 6220 8620 1328 302 956 O HETATM 2892 O HOH A2058 -2.415 -5.219 -25.529 1.00 63.24 O ANISOU 2892 O HOH A2058 5992 7477 10558 1270 -778 1037 O HETATM 2893 O HOH A2059 0.686 0.955 -20.303 1.00 47.22 O ANISOU 2893 O HOH A2059 3858 4931 9150 1516 620 -5 O HETATM 2894 O HOH A2060 19.630 0.372 -17.885 1.00 68.41 O ANISOU 2894 O HOH A2060 4846 4913 16235 29 -1011 -847 O HETATM 2895 O HOH A2061 16.303 0.535 -15.530 1.00 59.77 O ANISOU 2895 O HOH A2061 4566 4370 13773 454 -1710 -1970 O HETATM 2896 O HOH A2062 0.413 -19.347 -15.335 1.00 37.95 O ANISOU 2896 O HOH A2062 2468 5539 6411 732 524 717 O HETATM 2897 O HOH A2063 -1.571 -21.112 -14.521 1.00 42.43 O ANISOU 2897 O HOH A2063 2707 5774 7641 701 708 1300 O HETATM 2898 O HOH A2064 -5.188 -21.513 -15.141 1.00 70.31 O ANISOU 2898 O HOH A2064 5577 8482 12655 549 582 2104 O HETATM 2899 O HOH A2065 -4.087 -19.316 -14.467 1.00 46.08 O ANISOU 2899 O HOH A2065 2863 5882 8764 839 957 1723 O HETATM 2900 O HOH A2066 -7.963 -19.714 -16.517 1.00 57.39 O ANISOU 2900 O HOH A2066 3489 6230 12087 451 278 2466 O HETATM 2901 O HOH A2067 14.694 -19.354 -30.959 1.00 54.19 O ANISOU 2901 O HOH A2067 8949 7029 4613 2409 1154 798 O HETATM 2902 O HOH A2068 23.559 -14.502 -30.150 1.00 52.72 O ANISOU 2902 O HOH A2068 6221 5043 8765 2142 3979 2912 O HETATM 2903 O HOH A2069 26.310 -15.042 -26.692 1.00 50.96 O ANISOU 2903 O HOH A2069 4676 4376 10309 1149 3278 2393 O HETATM 2904 O HOH A2070 27.234 -13.608 -21.171 1.00 56.14 O ANISOU 2904 O HOH A2070 6308 6482 8541 1839 2147 509 O HETATM 2905 O HOH A2071 32.649 -15.530 -18.123 1.00 74.71 O ANISOU 2905 O HOH A2071 5626 5613 17148 11 102 654 O HETATM 2906 O HOH B2001 13.044 -56.234 -9.291 1.00 64.48 O ANISOU 2906 O HOH B2001 5053 6580 12867 -312 -669 2880 O HETATM 2907 O HOH B2002 25.921 -18.418 -19.946 1.00 70.73 O ANISOU 2907 O HOH B2002 6624 7796 12453 152 912 161 O HETATM 2908 O HOH B2003 8.980 -26.021 -5.705 1.00 56.80 O ANISOU 2908 O HOH B2003 7137 8813 5630 1926 1122 30 O HETATM 2909 O HOH B2004 18.815 -26.432 -20.525 1.00 35.95 O ANISOU 2909 O HOH B2004 4196 5531 3934 325 346 -630 O HETATM 2910 O HOH B2005 25.957 -26.232 -23.633 1.00 61.69 O ANISOU 2910 O HOH B2005 7099 7744 8597 949 2040 561 O HETATM 2911 O HOH B2006 25.421 -27.296 -21.567 1.00 48.77 O ANISOU 2911 O HOH B2006 5193 6412 6925 665 1523 62 O HETATM 2912 O HOH B2007 10.516 -29.972 -16.501 1.00 27.02 O ANISOU 2912 O HOH B2007 2387 4725 3153 -17 -550 -338 O HETATM 2913 O HOH B2008 15.856 -29.412 -18.561 1.00 38.02 O ANISOU 2913 O HOH B2008 4467 5957 4024 88 -254 -692 O HETATM 2914 O HOH B2009 5.721 -22.395 -11.933 1.00 36.64 O ANISOU 2914 O HOH B2009 3247 6077 4596 1010 869 63 O HETATM 2915 O HOH B2010 10.415 -28.933 -8.501 1.00 45.55 O ANISOU 2915 O HOH B2010 5113 7550 4645 1149 748 -1 O HETATM 2916 O HOH B2011 9.454 -33.123 -13.428 1.00 35.63 O ANISOU 2916 O HOH B2011 2969 5833 4735 95 -128 297 O HETATM 2917 O HOH B2012 8.565 -33.061 -9.713 1.00 45.61 O ANISOU 2917 O HOH B2012 4205 7334 5792 747 898 894 O HETATM 2918 O HOH B2013 6.442 -27.586 -6.421 1.00 63.36 O ANISOU 2918 O HOH B2013 7313 9544 7218 1787 1676 833 O HETATM 2919 O HOH B2014 6.613 -32.798 -12.718 1.00 49.24 O ANISOU 2919 O HOH B2014 4149 7273 7289 203 191 905 O HETATM 2920 O AHOH B2015 15.569 -32.089 -23.412 0.66 31.14 O ANISOU 2920 O AHOH B2015 4631 4574 2627 418 -654 -648 O HETATM 2921 O BHOH B2015 15.291 -30.378 -24.332 0.34 23.07 O ANISOU 2921 O BHOH B2015 3749 3553 1462 587 -566 -607 O HETATM 2922 O AHOH B2017 13.619 -35.795 -23.792 0.53 26.31 O ANISOU 2922 O AHOH B2017 4074 3568 2354 348 -1446 -754 O HETATM 2923 O BHOH B2017 14.561 -33.378 -23.935 0.47 35.37 O ANISOU 2923 O BHOH B2017 5262 4946 3231 420 -1003 -691 O HETATM 2924 O HOH B2018 10.127 -35.819 -24.350 1.00 48.88 O ANISOU 2924 O HOH B2018 6733 5968 5871 278 -2236 -735 O HETATM 2925 O HOH B2020 13.564 -35.391 0.468 1.00 58.84 O ANISOU 2925 O HOH B2020 8383 9220 4754 3163 1254 834 O HETATM 2926 O HOH B2021 16.382 -31.548 -19.750 1.00 31.70 O ANISOU 2926 O HOH B2021 3976 4974 3097 128 -369 -649 O HETATM 2927 O HOH B2022 11.317 -31.885 -14.672 1.00 33.48 O ANISOU 2927 O HOH B2022 3135 5675 3909 32 -338 -222 O HETATM 2928 O HOH B2023 10.039 -35.886 -12.579 1.00 33.40 O ANISOU 2928 O HOH B2023 2581 5464 4644 71 -97 545 O HETATM 2929 O HOH B2024 14.932 -29.992 -14.754 1.00 47.21 O ANISOU 2929 O HOH B2024 5303 7400 5235 111 -185 -682 O HETATM 2930 O HOH B2025 12.743 -35.647 -2.482 1.00 50.05 O ANISOU 2930 O HOH B2025 6485 8166 4366 2275 1261 890 O HETATM 2931 O HOH B2026 8.211 -33.813 -7.062 1.00 38.71 O ANISOU 2931 O HOH B2026 3649 6427 4632 1278 1482 1335 O HETATM 2932 O HOH B2027 14.741 -42.321 -3.520 1.00 46.96 O ANISOU 2932 O HOH B2027 5389 7841 4614 1764 1330 1621 O HETATM 2933 O HOH B2028 13.978 -32.386 -3.258 1.00 50.17 O ANISOU 2933 O HOH B2028 6731 8119 4211 2045 591 10 O HETATM 2934 O HOH B2029 8.607 -42.539 -1.805 1.00 74.06 O ANISOU 2934 O HOH B2029 8028 10349 9762 2396 2760 3521 O HETATM 2935 O HOH B2030 9.033 -40.684 0.666 1.00 88.20 O ANISOU 2935 O HOH B2030 10778 12432 10300 3378 3062 3306 O HETATM 2936 O HOH B2031 25.059 -36.371 -2.669 1.00 34.91 O ANISOU 2936 O HOH B2031 4816 5568 2879 1476 -1401 -1149 O HETATM 2937 O HOH B2032 27.926 -34.196 0.831 1.00 67.31 O ANISOU 2937 O HOH B2032 9586 8952 7037 2335 -2754 -1920 O HETATM 2938 O HOH B2033 22.054 -39.236 14.617 1.00 54.01 O ANISOU 2938 O HOH B2033 7723 6820 5977 513 -1957 -741 O HETATM 2939 O HOH B2034 19.130 -60.446 -13.237 1.00 74.74 O ANISOU 2939 O HOH B2034 7922 7401 13075 -310 -2401 818 O HETATM 2940 O HOH B2035 19.234 -59.460 -16.029 1.00 74.41 O ANISOU 2940 O HOH B2035 8724 7153 12397 -173 -3147 -128 O HETATM 2941 O HOH B2036 35.363 -47.053 -12.393 1.00 33.66 O ANISOU 2941 O HOH B2036 2497 4485 5806 700 -239 -222 O HETATM 2942 O HOH B2037 35.631 -42.378 -1.013 1.00 61.11 O ANISOU 2942 O HOH B2037 7365 7774 8079 1405 -3348 -1368 O HETATM 2943 O HOH B2038 40.917 -49.273 -8.348 1.00 77.89 O ANISOU 2943 O HOH B2038 9501 7940 12153 2634 4597 3496 O HETATM 2944 O HOH B2039 35.650 -52.671 -4.371 1.00 47.88 O ANISOU 2944 O HOH B2039 4886 6750 6557 1265 -2016 12 O HETATM 2945 O HOH B2040 40.164 -46.977 1.338 1.00 59.68 O ANISOU 2945 O HOH B2040 6992 7074 8611 1730 -4391 -1187 O HETATM 2946 O HOH B2041 31.233 -54.793 -9.136 1.00 38.14 O ANISOU 2946 O HOH B2041 3970 5408 5112 701 -739 167 O HETATM 2947 O HOH B2042 31.463 -52.841 -10.876 1.00 35.70 O ANISOU 2947 O HOH B2042 3695 5085 4786 635 -570 -110 O HETATM 2948 O HOH B2043 37.299 -52.808 -6.564 1.00 43.25 O ANISOU 2948 O HOH B2043 3740 5783 6912 1079 -1686 10 O HETATM 2949 O HOH B2044 33.967 -55.048 -4.494 1.00 47.09 O ANISOU 2949 O HOH B2044 5012 6767 6112 1280 -1534 399 O HETATM 2950 O HOH B2045 27.066 -55.310 -11.029 1.00 49.98 O ANISOU 2950 O HOH B2045 5700 6643 6645 393 -763 178 O HETATM 2951 O HOH B2046 24.385 -57.570 -0.963 1.00 55.17 O ANISOU 2951 O HOH B2046 6356 8059 6547 1887 466 2752 O HETATM 2952 O HOH B2047 16.962 -55.754 -9.634 1.00 55.60 O ANISOU 2952 O HOH B2047 4875 6383 9866 -153 -782 1892 O HETATM 2953 O HOH B2048 14.834 -51.677 -8.213 1.00 48.20 O ANISOU 2953 O HOH B2048 3835 6190 8289 121 63 2251 O HETATM 2954 O HOH B2049 12.388 -51.313 -13.227 1.00 47.47 O ANISOU 2954 O HOH B2049 3821 4903 9312 -540 -1677 1257 O HETATM 2955 O HOH B2050 26.136 -34.412 -1.581 1.00 51.46 O ANISOU 2955 O HOH B2050 7100 7339 5111 1739 -1947 -1534 O HETATM 2956 O HOH B2051 36.214 -34.305 2.030 1.00 87.93 O ANISOU 2956 O HOH B2051 11538 9533 12339 2285 -5346 -2776 O HETATM 2957 O HOH B2052 34.758 -34.443 5.179 1.00 76.58 O ANISOU 2957 O HOH B2052 11429 8280 9390 3370 -5717 -3109 O HETATM 2958 O HOH B2053 35.020 -31.876 5.883 1.00 85.01 O ANISOU 2958 O HOH B2053 12743 8669 10889 3771 -6541 -3596 O HETATM 2959 O HOH B2054 39.982 -21.752 -2.023 1.00105.81 O ANISOU 2959 O HOH B2054 11089 7918 21196 1613 -7196 -3026 O HETATM 2960 O HOH B2055 36.627 -30.069 -12.547 1.00 52.59 O ANISOU 2960 O HOH B2055 3664 4722 11598 47 -1168 -435 O HETATM 2961 O HOH B2056 34.458 -45.583 -14.720 1.00 31.85 O ANISOU 2961 O HOH B2056 2534 4228 5341 764 394 -177 O HETATM 2962 O HOH B2057 33.328 -48.001 -15.641 1.00 32.35 O ANISOU 2962 O HOH B2057 3249 4343 4699 893 499 -249 O HETATM 2963 O HOH B2058 31.912 -48.238 -23.880 1.00 66.23 O ANISOU 2963 O HOH B2058 10069 7988 7109 2282 1613 -224 O HETATM 2964 O HOH B2059 33.771 -51.647 -19.637 1.00 48.84 O ANISOU 2964 O HOH B2059 6697 5808 6051 1833 1257 -285 O HETATM 2965 O HOH B2060 34.337 -48.857 -18.143 1.00 34.82 O ANISOU 2965 O HOH B2060 4006 4301 4922 1415 1262 -81 O HETATM 2966 O HOH B2061 35.922 -49.672 -21.648 1.00 59.22 O ANISOU 2966 O HOH B2061 7935 6920 7646 2215 2297 272 O HETATM 2967 O HOH B2062 29.178 -54.806 -15.827 1.00 37.82 O ANISOU 2967 O HOH B2062 4978 4624 4766 796 -520 -522 O HETATM 2968 O HOH B2063 34.528 -50.406 -15.086 1.00 43.87 O ANISOU 2968 O HOH B2063 4644 5634 6392 1010 464 -145 O HETATM 2969 O HOH B2064 19.420 -45.041 -20.602 1.00 56.26 O ANISOU 2969 O HOH B2064 7891 7209 6278 357 -1365 -936 O HETATM 2970 O HOH B2065 18.371 -57.925 -12.267 1.00 66.20 O ANISOU 2970 O HOH B2065 6683 7019 11449 -316 -1821 1057 O HETATM 2971 O HOH B2066 16.336 -45.312 -20.337 1.00 37.76 O ANISOU 2971 O HOH B2066 5187 4556 4606 110 -1945 -821 O HETATM 2972 O HOH B2067 20.478 -59.502 -18.693 1.00 69.01 O ANISOU 2972 O HOH B2067 9213 6224 10784 292 -3644 -1023 O HETATM 2973 O HOH B2068 17.800 -57.532 -15.502 1.00 57.23 O ANISOU 2973 O HOH B2068 6186 5313 10248 -337 -2923 130 O HETATM 2974 O HOH B2069 12.701 -49.551 -21.830 1.00 58.86 O ANISOU 2974 O HOH B2069 7772 5566 9024 174 -3623 -812 O HETATM 2975 O HOH B2070 7.808 -42.095 -17.821 1.00 43.97 O ANISOU 2975 O HOH B2070 4081 4803 7822 -464 -2169 336 O HETATM 2976 O HOH B2071 7.153 -50.817 -13.445 1.00 64.35 O ANISOU 2976 O HOH B2071 5134 5784 13532 -578 -1848 2155 O HETATM 2977 O HOH B2072 2.988 -46.555 -13.070 1.00 71.30 O ANISOU 2977 O HOH B2072 5476 6578 15035 -448 -1257 2822 O HETATM 2978 O HOH B2073 33.109 -46.343 -24.710 1.00 77.74 O ANISOU 2978 O HOH B2073 11311 9392 8835 2400 2241 244 O HETATM 2979 O HOH B2074 32.236 -44.627 -22.248 1.00 56.21 O ANISOU 2979 O HOH B2074 7698 7010 6650 1786 1888 24 O HETATM 2980 O HOH B2075 7.044 -30.099 -7.037 1.00 62.67 O ANISOU 2980 O HOH B2075 6924 9467 7419 1494 1568 1031 O HETATM 2981 O HOH B2076 46.700 -22.101 -1.462 1.00130.17 O ANISOU 2981 O HOH B2076 12414 8535 28508 1228 -8799 -2549 O HETATM 2982 O HOH B2077 16.167 -58.013 -4.709 1.00 76.35 O ANISOU 2982 O HOH B2077 6854 9098 13056 629 926 3972 O HETATM 2983 O HOH B2078 14.377 -56.012 -7.012 1.00 74.61 O ANISOU 2983 O HOH B2078 6392 8642 13314 129 271 3374 O HETATM 2984 O HOH C2001 17.144 1.757 -9.245 1.00 88.93 O ANISOU 2984 O HOH C2001 9428 7863 16500 1600 -4230 -3756 O HETATM 2985 O HOH C2002 15.327 4.011 -9.866 1.00 81.40 O ANISOU 2985 O HOH C2002 8543 6700 15686 1613 -3905 -3745 O HETATM 2986 O HOH C2003 14.661 0.289 -11.096 1.00 60.90 O ANISOU 2986 O HOH C2003 6144 5012 11983 1369 -2775 -3246 O HETATM 2987 O HOH C2004 13.262 -1.881 -4.470 1.00 70.99 O ANISOU 2987 O HOH C2004 9949 7172 9854 3127 -3475 -4160 O HETATM 2988 O HOH C2005 18.082 3.156 -12.237 1.00 84.31 O ANISOU 2988 O HOH C2005 7475 6735 17824 911 -3621 -2956 O HETATM 2989 O HOH D2001 30.872 -55.253 5.440 1.00 70.53 O ANISOU 2989 O HOH D2001 11379 8101 7319 2297 -3431 -33 O HETATM 2990 O HOH D2002 16.224 -54.057 -1.589 1.00 54.38 O ANISOU 2990 O HOH D2002 5126 7646 7888 1773 2045 4048 O HETATM 2991 O HOH D2003 9.806 -54.189 -5.511 1.00 83.31 O ANISOU 2991 O HOH D2003 7022 9268 15363 635 1190 4533 O CONECT 334 2809 CONECT 669 2808 CONECT 670 2807 2808 CONECT 868 2811 CONECT 869 2811 CONECT 1123 2814 CONECT 1580 2822 CONECT 1888 2824 CONECT 2075 2825 CONECT 2103 2825 CONECT 2272 2820 CONECT 2273 2820 CONECT 2283 2821 CONECT 2359 2819 CONECT 2384 2819 CONECT 2385 2819 CONECT 2441 2442 CONECT 2442 2441 2443 2453 CONECT 2443 2442 2444 CONECT 2444 2443 2445 2452 CONECT 2445 2444 2446 2450 CONECT 2446 2445 2447 CONECT 2447 2446 2448 CONECT 2448 2447 2449 CONECT 2449 2448 2450 CONECT 2450 2445 2449 2451 CONECT 2451 2450 2452 CONECT 2452 2444 2451 CONECT 2453 2442 2454 CONECT 2454 2453 2455 2456 CONECT 2455 2454 CONECT 2456 2454 CONECT 2463 2472 CONECT 2472 2463 2473 CONECT 2473 2472 2474 2479 CONECT 2474 2473 2475 CONECT 2475 2474 2476 CONECT 2476 2475 2477 2478 CONECT 2477 2476 CONECT 2478 2476 CONECT 2479 2473 2480 CONECT 2480 2479 2481 2482 CONECT 2481 2480 CONECT 2482 2480 CONECT 2496 2499 CONECT 2499 2496 2500 2501 CONECT 2500 2499 2502 2504 CONECT 2501 2499 2503 2505 CONECT 2502 2500 2508 CONECT 2503 2501 2509 CONECT 2504 2500 2506 CONECT 2505 2501 2506 CONECT 2506 2504 2505 2507 2516 CONECT 2507 2506 CONECT 2508 2502 2510 CONECT 2509 2503 2511 CONECT 2510 2508 2512 2514 CONECT 2511 2509 2513 2515 CONECT 2512 2510 CONECT 2513 2511 CONECT 2514 2510 CONECT 2515 2511 CONECT 2516 2506 2517 CONECT 2517 2516 2518 2520 CONECT 2518 2517 2519 2525 CONECT 2519 2518 CONECT 2520 2517 2521 CONECT 2521 2520 2522 CONECT 2522 2521 2523 CONECT 2523 2522 2524 CONECT 2524 2523 CONECT 2525 2518 CONECT 2527 2536 CONECT 2536 2527 2537 CONECT 2537 2536 2538 2547 CONECT 2538 2537 2539 CONECT 2539 2538 2540 CONECT 2540 2539 2541 CONECT 2541 2540 2542 CONECT 2542 2541 2543 2544 CONECT 2543 2542 CONECT 2544 2542 CONECT 2545 2546 2547 2548 CONECT 2546 2545 CONECT 2547 2537 2545 CONECT 2548 2545 CONECT 2563 2574 CONECT 2569 2570 CONECT 2570 2569 2571 2572 CONECT 2571 2570 CONECT 2572 2570 2573 CONECT 2573 2572 2574 2575 CONECT 2574 2563 2573 CONECT 2575 2573 2576 CONECT 2576 2575 2577 CONECT 2577 2576 CONECT 2587 2595 CONECT 2593 2594 CONECT 2594 2593 2595 2596 CONECT 2595 2587 2594 CONECT 2596 2594 2597 CONECT 2597 2596 2598 2599 CONECT 2598 2597 CONECT 2599 2597 CONECT 2610 2620 CONECT 2620 2610 CONECT 2622 2623 2624 2625 CONECT 2623 2622 CONECT 2624 2622 CONECT 2625 2622 2626 CONECT 2626 2625 2627 2637 CONECT 2627 2626 2628 CONECT 2628 2627 2629 2636 CONECT 2629 2628 2630 2634 CONECT 2630 2629 2631 CONECT 2631 2630 2632 CONECT 2632 2631 2633 CONECT 2633 2632 2634 CONECT 2634 2629 2633 2635 CONECT 2635 2634 2636 CONECT 2636 2628 2635 CONECT 2637 2626 2638 CONECT 2638 2637 2639 2640 CONECT 2639 2638 CONECT 2640 2638 CONECT 2648 2664 CONECT 2664 2648 2665 CONECT 2665 2664 2666 2671 CONECT 2666 2665 2667 CONECT 2667 2666 2668 CONECT 2668 2667 2669 2670 CONECT 2669 2668 2823 CONECT 2670 2668 CONECT 2671 2665 2672 CONECT 2672 2671 2673 2674 CONECT 2673 2672 CONECT 2674 2672 CONECT 2688 2691 CONECT 2691 2688 2692 CONECT 2692 2691 2693 2694 CONECT 2693 2692 2697 CONECT 2694 2692 2695 CONECT 2695 2694 2696 2701 CONECT 2696 2695 CONECT 2697 2693 2698 CONECT 2698 2697 2699 2700 CONECT 2699 2698 CONECT 2700 2698 CONECT 2701 2695 2702 CONECT 2702 2701 2703 2705 CONECT 2703 2702 2704 2710 CONECT 2704 2703 CONECT 2705 2702 2706 CONECT 2706 2705 2707 CONECT 2707 2706 2708 CONECT 2708 2707 2709 CONECT 2709 2708 CONECT 2710 2703 CONECT 2712 2721 CONECT 2721 2712 2722 CONECT 2722 2721 2723 2732 CONECT 2723 2722 2724 CONECT 2724 2723 2725 CONECT 2725 2724 2726 CONECT 2726 2725 2727 CONECT 2727 2726 2728 2729 CONECT 2728 2727 CONECT 2729 2727 CONECT 2730 2731 2732 2733 CONECT 2731 2730 CONECT 2732 2722 2730 CONECT 2733 2730 CONECT 2748 2759 CONECT 2754 2755 CONECT 2755 2754 2756 2757 CONECT 2756 2755 CONECT 2757 2755 2758 CONECT 2758 2757 2759 2760 CONECT 2759 2748 2758 CONECT 2760 2758 2761 CONECT 2761 2760 2762 CONECT 2762 2761 CONECT 2772 2780 CONECT 2778 2779 CONECT 2779 2778 2780 2781 CONECT 2780 2772 2779 CONECT 2781 2779 2782 CONECT 2782 2781 2783 2784 CONECT 2783 2782 CONECT 2784 2782 CONECT 2795 2805 CONECT 2805 2795 CONECT 2807 670 2893 CONECT 2808 669 670 CONECT 2809 334 2856 2876 2877 CONECT 2811 868 869 2885 2898 CONECT 2811 2899 2900 CONECT 2814 1123 2902 2903 CONECT 2815 2816 2817 CONECT 2816 2815 CONECT 2817 2815 2818 CONECT 2818 2817 CONECT 2819 2359 2384 2385 CONECT 2820 2272 2273 2963 2978 CONECT 2820 2979 CONECT 2821 2283 2964 2965 2968 CONECT 2822 1580 2917 2931 2980 CONECT 2823 2669 CONECT 2824 1888 CONECT 2825 2075 2103 2958 CONECT 2828 2981 CONECT 2829 2981 CONECT 2830 2831 2832 CONECT 2831 2830 CONECT 2832 2830 2833 CONECT 2833 2832 CONECT 2856 2809 CONECT 2876 2809 CONECT 2877 2809 CONECT 2885 2811 CONECT 2893 2807 CONECT 2898 2811 CONECT 2899 2811 CONECT 2900 2811 CONECT 2902 2814 CONECT 2903 2814 CONECT 2917 2822 CONECT 2931 2822 CONECT 2958 2825 CONECT 2963 2820 CONECT 2964 2821 CONECT 2965 2821 CONECT 2968 2821 CONECT 2978 2820 CONECT 2979 2820 CONECT 2980 2822 CONECT 2981 2828 2829 MASTER 529 0 34 20 0 0 20 6 2777 4 237 30 END
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Related entries of code: 4bpk
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
Check Database
Protein Sequence Similarity
2yj1
RCSB PDB
PDBbind
23aa, >2YJ1_2|Chains... *
4bpi
RCSB PDB
PDBbind
19aa, >4BPI_2|Chain... at 94%
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
4bpk
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
BCL-xL protein
Ligand Name
alpha beta Puma BH3 peptide 5
EC.Number
E.C.-.-.-.-
Resolution
1.76(Å)
Affinity (Kd/Ki/IC50)
IC50=25nM
Release Year
2014
Protein/NA Sequence
Check fasta file
Primary Reference
(2013) Chembiochem Vol. 14: pp. 1564-1572
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
Q9BXH1
Q07817
Entrez Gene ID
NCBI Entrez Gene ID:
27113
598
ASD
Information of known allosteric effects of PDB entries
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