Browse entries in the PDBbind-CN Database
HEADER TRANSPORT PROTEIN 07-MAR-09 3GJ5 TITLE CRYSTAL STRUCTURE OF HUMAN RANGDP-NUP153ZNF4 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: GTP-BINDING NUCLEAR PROTEIN RAN; COMPND 3 CHAIN: A, C; COMPND 4 SYNONYM: GTPASE RAN, RAS-RELATED NUCLEAR PROTEIN, RAS-LIKE COMPND 5 PROTEIN TC4, ANDROGEN RECEPTOR-ASSOCIATED PROTEIN 24; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: NUCLEAR PORE COMPLEX PROTEIN NUP153; COMPND 10 CHAIN: B, D; COMPND 11 FRAGMENT: NUP153 - ZINC FINGER MODULE 4: UNP RESIDUES 848- COMPND 12 876; COMPND 13 SYNONYM: NUCLEOPORIN NUP153, 153 KDA NUCLEOPORIN; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: RAN, ARA24, OK/SW-CL.81; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_VARIANT: BL21(DE3)-RIL; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 13 ORGANISM_COMMON: RAT; SOURCE 14 ORGANISM_TAXID: 10116; SOURCE 15 GENE: NUP153; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 18 EXPRESSION_SYSTEM_VARIANT: BL21(DE3)-RIL; SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PGEX-6P1 KEYWDS G PROTEIN, GDP, RAN, NUP153, NUCLEAR PORE, ZINC FINGER, KEYWDS 2 ACETYLATION, CYTOPLASM, GTP-BINDING, HOST-VIRUS KEYWDS 3 INTERACTION, ISOPEPTIDE BOND, NUCLEOTIDE-BINDING, NUCLEUS, KEYWDS 4 PHOSPHOPROTEIN, POLYMORPHISM, PROTEIN TRANSPORT, TRANSPORT, KEYWDS 5 UBL CONJUGATION, DNA-BINDING, METAL-BINDING, MRNA KEYWDS 6 TRANSPORT, NUCLEAR PORE COMPLEX, TRANSLOCATION, ZINC, ZINC- KEYWDS 7 FINGER, TRANSPORT PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR J.R.PARTRIDGE,T.U.SCHWARTZ REVDAT 1 04-AUG-09 3GJ5 0 JRNL AUTH J.R.PARTRIDGE,T.U.SCHWARTZ JRNL TITL CRYSTALLOGRAPHIC AND BIOCHEMICAL ANALYSIS OF THE JRNL TITL 2 RAN-BINDING ZINC FINGER DOMAIN. JRNL REF J.MOL.BIOL. V. 391 375 2009 JRNL REFN ISSN 0022-2836 JRNL PMID 19505478 JRNL DOI 10.1016/J.JMB.2009.06.011 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.79 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.79 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.66 REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7 REMARK 3 NUMBER OF REFLECTIONS : 53848 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.200 REMARK 3 R VALUE (WORKING SET) : 0.199 REMARK 3 FREE R VALUE : 0.233 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060 REMARK 3 FREE R VALUE TEST SET COUNT : 2726 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 45.6724 - 4.7751 0.94 2669 149 0.1860 0.2044 REMARK 3 2 4.7751 - 3.7908 0.95 2643 152 0.1704 0.1806 REMARK 3 3 3.7908 - 3.3117 0.97 2686 139 0.1913 0.2087 REMARK 3 4 3.3117 - 3.0090 0.98 2665 159 0.1989 0.2377 REMARK 3 5 3.0090 - 2.7934 0.98 2721 140 0.2147 0.2710 REMARK 3 6 2.7934 - 2.6287 0.99 2718 156 0.2178 0.2517 REMARK 3 7 2.6287 - 2.4971 0.99 2703 153 0.2006 0.2284 REMARK 3 8 2.4971 - 2.3884 0.99 2707 137 0.1879 0.2390 REMARK 3 9 2.3884 - 2.2964 0.99 2732 146 0.1953 0.2404 REMARK 3 10 2.2964 - 2.2172 0.99 2731 139 0.1872 0.2431 REMARK 3 11 2.2172 - 2.1479 0.99 2709 134 0.1872 0.2569 REMARK 3 12 2.1479 - 2.0865 0.99 2726 148 0.1786 0.2444 REMARK 3 13 2.0865 - 2.0315 0.99 2703 146 0.1949 0.2109 REMARK 3 14 2.0315 - 1.9820 0.99 2728 132 0.1929 0.2428 REMARK 3 15 1.9820 - 1.9369 0.99 2710 152 0.2089 0.2591 REMARK 3 16 1.9369 - 1.8957 0.99 2738 128 0.2119 0.2823 REMARK 3 17 1.8957 - 1.8578 0.99 2656 144 0.2194 0.2580 REMARK 3 18 1.8578 - 1.8227 0.98 2712 147 0.2283 0.2935 REMARK 3 19 1.8227 - 1.7900 0.90 2465 125 0.2436 0.2771 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 : 0.33 REMARK 3 B_SOL : 63.38 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.550 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.530 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 23.15 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 : 0.007 3734 REMARK 3 ANGLE : 1.073 5068 REMARK 3 CHIRALITY : 0.069 562 REMARK 3 PLANARITY : 0.005 636 REMARK 3 DIHEDRAL : 14.711 1356 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN D REMARK 3 ORIGIN FOR THE GROUP (A): 50.5799 -4.6085 -3.0582 REMARK 3 T TENSOR REMARK 3 T11: 0.2370 T22: 0.2125 REMARK 3 T33: 0.2201 T12: -0.0011 REMARK 3 T13: -0.0042 T23: -0.0152 REMARK 3 L TENSOR REMARK 3 L11: 1.0703 L22: 0.6261 REMARK 3 L33: 0.8058 L12: -0.3242 REMARK 3 L13: 0.3602 L23: 0.1690 REMARK 3 S TENSOR REMARK 3 S11: -0.0690 S12: -0.1000 S13: 0.0772 REMARK 3 S21: 0.0733 S22: -0.0116 S23: -0.0554 REMARK 3 S31: -0.0279 S32: -0.0481 S33: 0.0696 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 3GJ5 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAR-09. REMARK 100 THE RCSB ID CODE IS RCSB051925. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-AUG-08 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 24-ID-C REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53898 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.790 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1 REMARK 200 DATA REDUNDANCY : 2.700 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.07000 REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1 REMARK 200 DATA REDUNDANCY IN SHELL : 2.70 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.38000 REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600 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 3GJ3 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.86 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 BIS-TRIS PH 6.5, 18-20% PEG REMARK 280 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 30.67150 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 -4 REMARK 465 PRO A -3 REMARK 465 HIS A -2 REMARK 465 MET A -1 REMARK 465 ALA A 0 REMARK 465 SER A 1 REMARK 465 ALA A 2 REMARK 465 ALA A 3 REMARK 465 GLN A 4 REMARK 465 GLY A 5 REMARK 465 GLU A 6 REMARK 465 PRO A 7 REMARK 465 LEU A 209 REMARK 465 PRO A 210 REMARK 465 ASP A 211 REMARK 465 GLU A 212 REMARK 465 ASP A 213 REMARK 465 ASP A 214 REMARK 465 ASP A 215 REMARK 465 LEU A 216 REMARK 465 GLY B 843 REMARK 465 PRO B 844 REMARK 465 LEU B 845 REMARK 465 GLY B 846 REMARK 465 SER B 847 REMARK 465 PRO B 874 REMARK 465 GLY B 875 REMARK 465 THR B 876 REMARK 465 GLY C -4 REMARK 465 PRO C -3 REMARK 465 HIS C -2 REMARK 465 MET C -1 REMARK 465 ALA C 0 REMARK 465 SER C 1 REMARK 465 ALA C 2 REMARK 465 ALA C 3 REMARK 465 GLN C 4 REMARK 465 GLY C 5 REMARK 465 GLU C 6 REMARK 465 PRO C 7 REMARK 465 LEU C 209 REMARK 465 PRO C 210 REMARK 465 ASP C 211 REMARK 465 GLU C 212 REMARK 465 ASP C 213 REMARK 465 ASP C 214 REMARK 465 ASP C 215 REMARK 465 LEU C 216 REMARK 465 GLY D 843 REMARK 465 PRO D 844 REMARK 465 LEU D 845 REMARK 465 GLY D 846 REMARK 465 SER D 847 REMARK 465 PRO D 874 REMARK 465 GLY D 875 REMARK 465 THR D 876 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 GLU A 113 -122.76 60.94 REMARK 500 LEU B 856 2.68 80.16 REMARK 500 GLU C 113 -135.34 65.71 REMARK 500 ASN C 114 32.61 -89.78 REMARK 500 LYS C 123 30.77 77.28 REMARK 500 ASN C 143 27.74 82.94 REMARK 500 REMARK 500 REMARK: NULL 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 MG A 301 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 THR A 24 OG1 REMARK 620 2 GDP A 302 O1B 90.9 REMARK 620 3 HOH A 509 O 88.2 175.1 REMARK 620 4 HOH A 507 O 94.0 86.4 88.8 REMARK 620 5 HOH A 508 O 172.9 92.9 88.5 92.2 REMARK 620 6 HOH A 506 O 86.7 94.9 89.8 178.5 87.0 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN B 300 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS B 852 SG REMARK 620 2 CYS B 855 SG 114.2 REMARK 620 3 CYS B 866 SG 109.5 103.1 REMARK 620 4 CYS B 869 SG 101.3 116.8 112.1 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG C 301 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 THR C 24 OG1 REMARK 620 2 GDP C 302 O1B 90.4 REMARK 620 3 HOH C 512 O 86.0 96.3 REMARK 620 4 HOH C 511 O 175.5 90.4 89.5 REMARK 620 5 HOH C 510 O 86.5 174.6 87.8 93.1 REMARK 620 6 HOH C 513 O 91.6 86.2 176.6 92.8 89.5 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN D 300 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS D 852 SG REMARK 620 2 CYS D 855 SG 114.1 REMARK 620 3 CYS D 866 SG 109.8 102.5 REMARK 620 4 CYS D 869 SG 101.9 116.8 111.8 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 301 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 302 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 300 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 301 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP C 302 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 300 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3CH5 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE RANGDP-NUP153ZNF2 COMPLEX REMARK 900 RELATED ID: 2GQE RELATED DB: PDB REMARK 900 MOLECULAR CHARACTERIZATION OF THE RAN BINDING ZINC FINGER REMARK 900 DOMAIN REMARK 900 RELATED ID: 1BYU RELATED DB: PDB REMARK 900 CANINE GDP-RAN REMARK 900 RELATED ID: 3GJ0 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN NUCLEOPORIN REMARK 900 RELATED ID: 3GJ3 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN NUCLEOPORIN IN COMPLEX WITH REMARK 900 NUP153 - ZINC FINGER MODULE 2 REMARK 900 RELATED ID: 3GJ4 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN NUCLEOPORIN F35S MUTANT IN REMARK 900 COMPLEX WITH NUP153 - ZINC FINGER MODULE 3 REMARK 900 RELATED ID: 3GJ6 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN NUCLEOPORIN F35S MUTANT IN REMARK 900 COMPLEX WITH NUP153 - ZINC FINGER MODULE 1 REMARK 900 RELATED ID: 3GJ7 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN NUCLEOPORIN F35S MUTANT IN REMARK 900 COMPLEX WITH NUP153 - ZINC FINGER MODULE 12 REMARK 900 RELATED ID: 3GJ8 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN NUCLEOPORIN F35S MUTANT IN REMARK 900 COMPLEX WITH NUP153 - ZINC FINGER MODULE 34 DBREF 3GJ5 A 2 216 UNP P62826 RAN_HUMAN 2 216 DBREF 3GJ5 B 848 876 UNP P49791 NU153_RAT 848 876 DBREF 3GJ5 C 2 216 UNP P62826 RAN_HUMAN 2 216 DBREF 3GJ5 D 848 876 UNP P49791 NU153_RAT 848 876 SEQADV 3GJ5 GLY A -4 UNP P62826 EXPRESSION TAG SEQADV 3GJ5 PRO A -3 UNP P62826 EXPRESSION TAG SEQADV 3GJ5 HIS A -2 UNP P62826 EXPRESSION TAG SEQADV 3GJ5 MET A -1 UNP P62826 EXPRESSION TAG SEQADV 3GJ5 ALA A 0 UNP P62826 EXPRESSION TAG SEQADV 3GJ5 SER A 1 UNP P62826 EXPRESSION TAG SEQADV 3GJ5 SER A 35 UNP P62826 PHE 35 ENGINEERED SEQADV 3GJ5 GLY B 843 UNP P49791 EXPRESSION TAG SEQADV 3GJ5 PRO B 844 UNP P49791 EXPRESSION TAG SEQADV 3GJ5 LEU B 845 UNP P49791 EXPRESSION TAG SEQADV 3GJ5 GLY B 846 UNP P49791 EXPRESSION TAG SEQADV 3GJ5 SER B 847 UNP P49791 EXPRESSION TAG SEQADV 3GJ5 GLY C -4 UNP P62826 EXPRESSION TAG SEQADV 3GJ5 PRO C -3 UNP P62826 EXPRESSION TAG SEQADV 3GJ5 HIS C -2 UNP P62826 EXPRESSION TAG SEQADV 3GJ5 MET C -1 UNP P62826 EXPRESSION TAG SEQADV 3GJ5 ALA C 0 UNP P62826 EXPRESSION TAG SEQADV 3GJ5 SER C 1 UNP P62826 EXPRESSION TAG SEQADV 3GJ5 SER C 35 UNP P62826 PHE 35 ENGINEERED SEQADV 3GJ5 GLY D 843 UNP P49791 EXPRESSION TAG SEQADV 3GJ5 PRO D 844 UNP P49791 EXPRESSION TAG SEQADV 3GJ5 LEU D 845 UNP P49791 EXPRESSION TAG SEQADV 3GJ5 GLY D 846 UNP P49791 EXPRESSION TAG SEQADV 3GJ5 SER D 847 UNP P49791 EXPRESSION TAG SEQRES 1 A 221 GLY PRO HIS MET ALA SER ALA ALA GLN GLY GLU PRO GLN SEQRES 2 A 221 VAL GLN PHE LYS LEU VAL LEU VAL GLY ASP GLY GLY THR SEQRES 3 A 221 GLY LYS THR THR PHE VAL LYS ARG HIS LEU THR GLY GLU SEQRES 4 A 221 SER GLU LYS LYS TYR VAL ALA THR LEU GLY VAL GLU VAL SEQRES 5 A 221 HIS PRO LEU VAL PHE HIS THR ASN ARG GLY PRO ILE LYS SEQRES 6 A 221 PHE ASN VAL TRP ASP THR ALA GLY GLN GLU LYS PHE GLY SEQRES 7 A 221 GLY LEU ARG ASP GLY TYR TYR ILE GLN ALA GLN CYS ALA SEQRES 8 A 221 ILE ILE MET PHE ASP VAL THR SER ARG VAL THR TYR LYS SEQRES 9 A 221 ASN VAL PRO ASN TRP HIS ARG ASP LEU VAL ARG VAL CYS SEQRES 10 A 221 GLU ASN ILE PRO ILE VAL LEU CYS GLY ASN LYS VAL ASP SEQRES 11 A 221 ILE LYS ASP ARG LYS VAL LYS ALA LYS SER ILE VAL PHE SEQRES 12 A 221 HIS ARG LYS LYS ASN LEU GLN TYR TYR ASP ILE SER ALA SEQRES 13 A 221 LYS SER ASN TYR ASN PHE GLU LYS PRO PHE LEU TRP LEU SEQRES 14 A 221 ALA ARG LYS LEU ILE GLY ASP PRO ASN LEU GLU PHE VAL SEQRES 15 A 221 ALA MET PRO ALA LEU ALA PRO PRO GLU VAL VAL MET ASP SEQRES 16 A 221 PRO ALA LEU ALA ALA GLN TYR GLU HIS ASP LEU GLU VAL SEQRES 17 A 221 ALA GLN THR THR ALA LEU PRO ASP GLU ASP ASP ASP LEU SEQRES 1 B 34 GLY PRO LEU GLY SER GLY SER TRP ASP CYS GLU VAL CYS SEQRES 2 B 34 LEU VAL GLN ASN LYS ALA ASP SER THR LYS CYS ILE ALA SEQRES 3 B 34 CYS GLU SER ALA LYS PRO GLY THR SEQRES 1 C 221 GLY PRO HIS MET ALA SER ALA ALA GLN GLY GLU PRO GLN SEQRES 2 C 221 VAL GLN PHE LYS LEU VAL LEU VAL GLY ASP GLY GLY THR SEQRES 3 C 221 GLY LYS THR THR PHE VAL LYS ARG HIS LEU THR GLY GLU SEQRES 4 C 221 SER GLU LYS LYS TYR VAL ALA THR LEU GLY VAL GLU VAL SEQRES 5 C 221 HIS PRO LEU VAL PHE HIS THR ASN ARG GLY PRO ILE LYS SEQRES 6 C 221 PHE ASN VAL TRP ASP THR ALA GLY GLN GLU LYS PHE GLY SEQRES 7 C 221 GLY LEU ARG ASP GLY TYR TYR ILE GLN ALA GLN CYS ALA SEQRES 8 C 221 ILE ILE MET PHE ASP VAL THR SER ARG VAL THR TYR LYS SEQRES 9 C 221 ASN VAL PRO ASN TRP HIS ARG ASP LEU VAL ARG VAL CYS SEQRES 10 C 221 GLU ASN ILE PRO ILE VAL LEU CYS GLY ASN LYS VAL ASP SEQRES 11 C 221 ILE LYS ASP ARG LYS VAL LYS ALA LYS SER ILE VAL PHE SEQRES 12 C 221 HIS ARG LYS LYS ASN LEU GLN TYR TYR ASP ILE SER ALA SEQRES 13 C 221 LYS SER ASN TYR ASN PHE GLU LYS PRO PHE LEU TRP LEU SEQRES 14 C 221 ALA ARG LYS LEU ILE GLY ASP PRO ASN LEU GLU PHE VAL SEQRES 15 C 221 ALA MET PRO ALA LEU ALA PRO PRO GLU VAL VAL MET ASP SEQRES 16 C 221 PRO ALA LEU ALA ALA GLN TYR GLU HIS ASP LEU GLU VAL SEQRES 17 C 221 ALA GLN THR THR ALA LEU PRO ASP GLU ASP ASP ASP LEU SEQRES 1 D 34 GLY PRO LEU GLY SER GLY SER TRP ASP CYS GLU VAL CYS SEQRES 2 D 34 LEU VAL GLN ASN LYS ALA ASP SER THR LYS CYS ILE ALA SEQRES 3 D 34 CYS GLU SER ALA LYS PRO GLY THR HET MG A 301 1 HET GDP A 302 28 HET ZN B 300 1 HET MG C 301 1 HET GDP C 302 28 HET ZN D 300 1 HETNAM MG MAGNESIUM ION HETNAM GDP GUANOSINE-5'-DIPHOSPHATE HETNAM ZN ZINC ION FORMUL 5 MG 2(MG 2+) FORMUL 6 GDP 2(C10 H15 N5 O11 P2) FORMUL 7 ZN 2(ZN 2+) FORMUL 11 HOH *458(H2 O) HELIX 1 1 GLY A 22 LYS A 28 1 7 HELIX 2 2 HIS A 30 GLU A 36 1 7 HELIX 3 3 GLY A 68 GLY A 73 5 6 HELIX 4 4 ARG A 76 ILE A 81 1 6 HELIX 5 5 SER A 94 ASN A 100 1 7 HELIX 6 6 ASN A 100 GLU A 113 1 14 HELIX 7 7 LYS A 132 ILE A 136 5 5 HELIX 8 8 VAL A 137 ASN A 143 1 7 HELIX 9 9 GLU A 158 GLY A 170 1 13 HELIX 10 10 ASP A 190 THR A 207 1 18 HELIX 11 11 GLY C 22 LYS C 28 1 7 HELIX 12 12 HIS C 30 GLU C 36 1 7 HELIX 13 13 GLY C 68 GLY C 73 5 6 HELIX 14 14 ARG C 76 ILE C 81 1 6 HELIX 15 15 SER C 94 ASN C 100 1 7 HELIX 16 16 ASN C 100 GLU C 113 1 14 HELIX 17 17 LYS C 132 ILE C 136 5 5 HELIX 18 18 VAL C 137 ASN C 143 1 7 HELIX 19 19 PHE C 157 GLY C 170 1 14 HELIX 20 20 ASP C 190 THR C 207 1 18 SHEET 1 A 7 LYS A 38 VAL A 40 0 SHEET 2 A 7 VAL A 45 THR A 54 -1 O VAL A 45 N VAL A 40 SHEET 3 A 7 GLY A 57 THR A 66 -1 O PHE A 61 N LEU A 50 SHEET 4 A 7 VAL A 9 VAL A 16 1 N PHE A 11 O ASN A 62 SHEET 5 A 7 CYS A 85 ASP A 91 1 O MET A 89 N VAL A 16 SHEET 6 A 7 ILE A 117 ASN A 122 1 O ASN A 122 N PHE A 90 SHEET 7 A 7 GLN A 145 ASP A 148 1 O GLN A 145 N LEU A 119 SHEET 1 B 2 TRP B 850 ASP B 851 0 SHEET 2 B 2 GLN B 858 ASN B 859 -1 O ASN B 859 N TRP B 850 SHEET 1 C 7 LYS C 38 VAL C 40 0 SHEET 2 C 7 VAL C 45 THR C 54 -1 O VAL C 45 N VAL C 40 SHEET 3 C 7 GLY C 57 THR C 66 -1 O PHE C 61 N LEU C 50 SHEET 4 C 7 GLN C 10 VAL C 16 1 N PHE C 11 O ASN C 62 SHEET 5 C 7 CYS C 85 ASP C 91 1 O MET C 89 N VAL C 16 SHEET 6 C 7 ILE C 117 ASN C 122 1 O ASN C 122 N PHE C 90 SHEET 7 C 7 GLN C 145 ASP C 148 1 O GLN C 145 N LEU C 119 SHEET 1 D 2 TRP D 850 ASP D 851 0 SHEET 2 D 2 GLN D 858 ASN D 859 -1 O ASN D 859 N TRP D 850 LINK OG1 THR A 24 MG MG A 301 1555 1555 2.13 LINK SG CYS B 852 ZN ZN B 300 1555 1555 2.48 LINK SG CYS B 855 ZN ZN B 300 1555 1555 2.24 LINK SG CYS B 866 ZN ZN B 300 1555 1555 2.39 LINK SG CYS B 869 ZN ZN B 300 1555 1555 2.38 LINK OG1 THR C 24 MG MG C 301 1555 1555 2.16 LINK SG CYS D 852 ZN ZN D 300 1555 1555 2.44 LINK SG CYS D 855 ZN ZN D 300 1555 1555 2.32 LINK SG CYS D 866 ZN ZN D 300 1555 1555 2.41 LINK SG CYS D 869 ZN ZN D 300 1555 1555 2.38 LINK MG MG A 301 O1B GDP A 302 1555 1555 2.15 LINK MG MG C 301 O1B GDP C 302 1555 1555 2.13 LINK MG MG A 301 O HOH A 509 1555 1555 2.27 LINK MG MG A 301 O HOH A 507 1555 1555 2.24 LINK MG MG A 301 O HOH A 508 1555 1555 2.25 LINK MG MG A 301 O HOH A 506 1555 1555 2.21 LINK MG MG C 301 O HOH C 512 1555 1555 2.23 LINK MG MG C 301 O HOH C 511 1555 1555 2.20 LINK MG MG C 301 O HOH C 510 1555 1555 2.27 LINK MG MG C 301 O HOH C 513 1555 1555 2.22 SITE 1 AC1 6 THR A 24 GDP A 302 HOH A 506 HOH A 507 SITE 2 AC1 6 HOH A 508 HOH A 509 SITE 1 AC2 21 GLY A 20 THR A 21 GLY A 22 LYS A 23 SITE 2 AC2 21 THR A 24 THR A 25 ASN A 122 LYS A 123 SITE 3 AC2 21 ASP A 125 ILE A 126 SER A 150 ALA A 151 SITE 4 AC2 21 LYS A 152 HOH A 248 HOH A 266 MG A 301 SITE 5 AC2 21 HOH A 304 HOH A 372 HOH A 462 HOH A 507 SITE 6 AC2 21 HOH A 508 SITE 1 AC3 4 CYS B 852 CYS B 855 CYS B 866 CYS B 869 SITE 1 AC4 6 THR C 24 GDP C 302 HOH C 510 HOH C 511 SITE 2 AC4 6 HOH C 512 HOH C 513 SITE 1 AC5 22 GLY C 20 THR C 21 GLY C 22 LYS C 23 SITE 2 AC5 22 THR C 24 THR C 25 ASN C 122 LYS C 123 SITE 3 AC5 22 ASP C 125 ILE C 126 SER C 150 ALA C 151 SITE 4 AC5 22 LYS C 152 HOH C 233 HOH C 264 HOH C 275 SITE 5 AC5 22 MG C 301 HOH C 344 HOH C 382 HOH C 436 SITE 6 AC5 22 HOH C 511 HOH C 513 SITE 1 AC6 4 CYS D 852 CYS D 855 CYS D 866 CYS D 869 CRYST1 70.443 61.343 74.025 90.00 112.55 90.00 P 1 21 1 4 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 0.014196 0.000000 0.005895 0.00000 SCALE2 0.000000 0.016302 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014627 0.00000 ATOM 1 N GLN A 8 51.236 10.598 17.081 1.00 79.61 N ANISOU 1 N GLN A 8 10218 10069 9959 -92 173 839 N ATOM 2 CA GLN A 8 50.540 9.782 18.070 1.00 76.86 C ANISOU 2 CA GLN A 8 9874 9704 9625 -65 143 717 C ATOM 3 C GLN A 8 51.043 10.099 19.476 1.00 63.38 C ANISOU 3 C GLN A 8 8149 7917 8016 -115 114 689 C ATOM 4 O GLN A 8 52.250 10.174 19.715 1.00 62.37 O ANISOU 4 O GLN A 8 7979 7792 7929 -164 139 729 O ATOM 5 CB GLN A 8 50.715 8.294 17.759 1.00 83.32 C ANISOU 5 CB GLN A 8 10662 10619 10379 -29 187 657 C ATOM 6 CG GLN A 8 49.802 7.374 18.554 1.00 90.11 C ANISOU 6 CG GLN A 8 11530 11467 11239 5 159 541 C ATOM 7 CD GLN A 8 49.820 5.947 18.035 1.00 96.54 C ANISOU 7 CD GLN A 8 12324 12368 11988 46 194 486 C ATOM 8 OE1 GLN A 8 50.441 5.656 17.012 1.00100.49 O ANISOU 8 OE1 GLN A 8 12805 12945 12431 62 238 526 O ATOM 9 NE2 GLN A 8 49.134 5.050 18.736 1.00 94.10 N ANISOU 9 NE2 GLN A 8 12019 12048 11687 66 174 392 N ATOM 10 N VAL A 9 50.112 10.302 20.401 1.00 45.23 N ANISOU 10 N VAL A 9 5878 5555 5751 -99 59 618 N ATOM 11 CA VAL A 9 50.466 10.630 21.776 1.00 36.30 C ANISOU 11 CA VAL A 9 4736 4352 4703 -135 23 581 C ATOM 12 C VAL A 9 50.540 9.342 22.593 1.00 35.52 C ANISOU 12 C VAL A 9 4612 4293 4592 -122 39 495 C ATOM 13 O VAL A 9 49.550 8.617 22.696 1.00 33.99 O ANISOU 13 O VAL A 9 4434 4123 4357 -79 34 427 O ATOM 14 CB VAL A 9 49.423 11.581 22.387 1.00 34.23 C ANISOU 14 CB VAL A 9 4518 4006 4483 -119 -45 548 C ATOM 15 CG1 VAL A 9 49.723 11.856 23.837 1.00 38.84 C ANISOU 15 CG1 VAL A 9 5091 4526 5142 -146 -85 496 C ATOM 16 CG2 VAL A 9 49.391 12.891 21.604 1.00 42.99 C ANISOU 16 CG2 VAL A 9 5658 5062 5613 -132 -69 639 C ATOM 17 N GLN A 10 51.714 9.054 23.157 1.00 32.06 N ANISOU 17 N GLN A 10 4132 3858 4191 -160 57 501 N ATOM 18 CA GLN A 10 51.875 7.845 23.961 1.00 31.99 C ANISOU 18 CA GLN A 10 4102 3880 4172 -147 68 428 C ATOM 19 C GLN A 10 52.790 8.111 25.155 1.00 33.33 C ANISOU 19 C GLN A 10 4244 4005 4413 -188 45 417 C ATOM 20 O GLN A 10 53.628 9.030 25.132 1.00 35.49 O ANISOU 20 O GLN A 10 4498 4243 4742 -233 36 474 O ATOM 21 CB GLN A 10 52.392 6.690 23.106 1.00 35.73 C ANISOU 21 CB GLN A 10 4547 4443 4586 -128 126 434 C ATOM 22 CG GLN A 10 53.688 6.998 22.380 1.00 42.28 C ANISOU 22 CG GLN A 10 5335 5308 5423 -162 166 515 C ATOM 23 CD GLN A 10 54.075 5.909 21.406 1.00 50.57 C ANISOU 23 CD GLN A 10 6358 6455 6401 -129 221 515 C ATOM 24 OE1 GLN A 10 53.827 4.728 21.647 1.00 46.69 O ANISOU 24 OE1 GLN A 10 5865 5993 5881 -94 226 445 O ATOM 25 NE2 GLN A 10 54.697 6.300 20.299 1.00 52.99 N ANISOU 25 NE2 GLN A 10 6643 6813 6679 -140 262 595 N ATOM 26 N PHE A 11 52.598 7.309 26.195 1.00 32.56 N ANISOU 26 N PHE A 11 4147 3911 4315 -171 33 344 N ATOM 27 CA PHE A 11 53.275 7.491 27.462 1.00 28.48 C ANISOU 27 CA PHE A 11 3611 3355 3854 -197 2 317 C ATOM 28 C PHE A 11 53.658 6.128 28.013 1.00 30.51 C ANISOU 28 C PHE A 11 3848 3657 4086 -179 24 271 C ATOM 29 O PHE A 11 52.812 5.228 28.068 1.00 29.55 O ANISOU 29 O PHE A 11 3748 3561 3917 -144 34 227 O ATOM 30 CB PHE A 11 52.322 8.122 28.463 1.00 29.04 C ANISOU 30 CB PHE A 11 3718 3368 3948 -183 -53 265 C ATOM 31 CG PHE A 11 51.877 9.500 28.075 1.00 26.04 C ANISOU 31 CG PHE A 11 3364 2928 3602 -193 -88 299 C ATOM 32 CD1 PHE A 11 52.737 10.579 28.215 1.00 34.83 C ANISOU 32 CD1 PHE A 11 4462 3983 4788 -239 -117 343 C ATOM 33 CD2 PHE A 11 50.612 9.709 27.577 1.00 32.72 C ANISOU 33 CD2 PHE A 11 4248 3773 4413 -157 -97 287 C ATOM 34 CE1 PHE A 11 52.347 11.843 27.858 1.00 33.22 C ANISOU 34 CE1 PHE A 11 4287 3714 4623 -248 -155 378 C ATOM 35 CE2 PHE A 11 50.205 10.994 27.201 1.00 32.01 C ANISOU 35 CE2 PHE A 11 4186 3622 4355 -160 -135 321 C ATOM 36 CZ PHE A 11 51.072 12.058 27.359 1.00 36.44 C ANISOU 36 CZ PHE A 11 4737 4117 4990 -206 -165 368 C ATOM 37 N LYS A 12 54.911 5.992 28.436 1.00 27.31 N ANISOU 37 N LYS A 12 3402 3259 3717 -205 26 282 N ATOM 38 CA LYS A 12 55.320 4.782 29.158 1.00 28.22 C ANISOU 38 CA LYS A 12 3503 3405 3816 -185 34 237 C ATOM 39 C LYS A 12 54.766 4.854 30.577 1.00 30.72 C ANISOU 39 C LYS A 12 3846 3681 4145 -175 -12 179 C ATOM 40 O LYS A 12 55.004 5.823 31.304 1.00 33.22 O ANISOU 40 O LYS A 12 4161 3950 4511 -196 -55 174 O ATOM 41 CB LYS A 12 56.837 4.628 29.192 1.00 28.25 C ANISOU 41 CB LYS A 12 3449 3432 3853 -209 46 262 C ATOM 42 CG LYS A 12 57.281 3.464 30.080 1.00 28.79 C ANISOU 42 CG LYS A 12 3508 3521 3911 -184 41 213 C ATOM 43 CD LYS A 12 58.759 3.177 29.979 1.00 29.48 C ANISOU 43 CD LYS A 12 3533 3644 4024 -198 56 232 C ATOM 44 CE LYS A 12 59.181 2.285 31.142 1.00 31.44 C ANISOU 44 CE LYS A 12 3778 3894 4275 -173 31 182 C ATOM 45 NZ LYS A 12 60.518 1.665 30.926 1.00 33.86 N ANISOU 45 NZ LYS A 12 4024 4248 4592 -168 50 190 N ATOM 46 N LEU A 13 54.004 3.835 30.956 1.00 27.29 N ANISOU 46 N LEU A 13 3437 3266 3666 -142 -4 136 N ATOM 47 CA LEU A 13 53.395 3.776 32.264 1.00 27.32 C ANISOU 47 CA LEU A 13 3466 3248 3667 -128 -37 86 C ATOM 48 C LEU A 13 53.919 2.528 32.947 1.00 26.63 C ANISOU 48 C LEU A 13 3370 3186 3562 -113 -28 65 C ATOM 49 O LEU A 13 53.726 1.419 32.453 1.00 27.32 O ANISOU 49 O LEU A 13 3461 3304 3615 -95 4 63 O ATOM 50 CB LEU A 13 51.868 3.717 32.129 1.00 31.32 C ANISOU 50 CB LEU A 13 4009 3755 4137 -106 -34 60 C ATOM 51 CG LEU A 13 51.033 3.717 33.422 1.00 31.88 C ANISOU 51 CG LEU A 13 4104 3815 4194 -89 -61 10 C ATOM 52 CD1 LEU A 13 49.595 4.143 33.113 1.00 32.31 C ANISOU 52 CD1 LEU A 13 4182 3866 4228 -73 -63 -10 C ATOM 53 CD2 LEU A 13 51.062 2.374 34.204 1.00 30.02 C ANISOU 53 CD2 LEU A 13 3872 3607 3927 -75 -45 -12 C ATOM 54 N VAL A 14 54.574 2.687 34.087 1.00 28.70 N ANISOU 54 N VAL A 14 3623 3434 3847 -116 -62 46 N ATOM 55 CA VAL A 14 55.010 1.494 34.821 1.00 29.55 C ANISOU 55 CA VAL A 14 3730 3564 3934 -96 -60 28 C ATOM 56 C VAL A 14 54.006 1.076 35.898 1.00 26.74 C ANISOU 56 C VAL A 14 3414 3206 3541 -75 -72 -7 C ATOM 57 O VAL A 14 53.452 1.900 36.609 1.00 28.91 O ANISOU 57 O VAL A 14 3703 3463 3817 -74 -101 -30 O ATOM 58 CB VAL A 14 56.429 1.645 35.394 1.00 33.43 C ANISOU 58 CB VAL A 14 4184 4054 4463 -105 -87 30 C ATOM 59 CG1 VAL A 14 57.425 1.624 34.262 1.00 30.31 C ANISOU 59 CG1 VAL A 14 3742 3680 4093 -122 -58 68 C ATOM 60 CG2 VAL A 14 56.559 2.923 36.248 1.00 40.11 C ANISOU 60 CG2 VAL A 14 5028 4864 5348 -121 -139 11 C ATOM 61 N LEU A 15 53.761 -0.228 35.993 1.00 28.09 N ANISOU 61 N LEU A 15 3599 3396 3678 -57 -48 -10 N ATOM 62 CA LEU A 15 52.733 -0.734 36.875 1.00 26.44 C ANISOU 62 CA LEU A 15 3424 3191 3431 -44 -48 -31 C ATOM 63 C LEU A 15 53.465 -1.560 37.914 1.00 30.73 C ANISOU 63 C LEU A 15 3972 3740 3962 -27 -63 -32 C ATOM 64 O LEU A 15 54.016 -2.600 37.583 1.00 33.53 O ANISOU 64 O LEU A 15 4322 4099 4317 -18 -49 -18 O ATOM 65 CB LEU A 15 51.753 -1.599 36.056 1.00 27.52 C ANISOU 65 CB LEU A 15 3576 3337 3545 -42 -9 -27 C ATOM 66 CG LEU A 15 50.714 -2.458 36.787 1.00 30.25 C ANISOU 66 CG LEU A 15 3950 3690 3855 -36 3 -38 C ATOM 67 CD1 LEU A 15 49.879 -1.586 37.709 1.00 34.33 C ANISOU 67 CD1 LEU A 15 4477 4212 4353 -34 -13 -61 C ATOM 68 CD2 LEU A 15 49.814 -3.205 35.765 1.00 30.37 C ANISOU 68 CD2 LEU A 15 3970 3707 3862 -40 35 -39 C ATOM 69 N VAL A 16 53.488 -1.092 39.159 1.00 27.04 N ANISOU 69 N VAL A 16 3515 3275 3484 -18 -97 -52 N ATOM 70 CA VAL A 16 54.271 -1.761 40.198 1.00 31.65 C ANISOU 70 CA VAL A 16 4105 3868 4053 3 -119 -52 C ATOM 71 C VAL A 16 53.460 -2.017 41.456 1.00 34.22 C ANISOU 71 C VAL A 16 4466 4211 4326 20 -125 -63 C ATOM 72 O VAL A 16 52.350 -1.512 41.614 1.00 31.54 O ANISOU 72 O VAL A 16 4139 3880 3966 16 -116 -79 O ATOM 73 CB VAL A 16 55.514 -0.944 40.572 1.00 40.52 C ANISOU 73 CB VAL A 16 5196 4985 5214 3 -164 -65 C ATOM 74 CG1 VAL A 16 56.391 -0.725 39.337 1.00 41.38 C ANISOU 74 CG1 VAL A 16 5262 5086 5373 -18 -152 -45 C ATOM 75 CG2 VAL A 16 55.092 0.395 41.174 1.00 33.50 C ANISOU 75 CG2 VAL A 16 4310 4087 4331 0 -200 -97 C ATOM 76 N GLY A 17 54.030 -2.805 42.361 1.00 28.75 N ANISOU 76 N GLY A 17 3787 3529 3609 42 -141 -54 N ATOM 77 CA GLY A 17 53.308 -3.281 43.523 1.00 30.29 C ANISOU 77 CA GLY A 17 4017 3747 3744 59 -137 -50 C ATOM 78 C GLY A 17 53.728 -4.712 43.827 1.00 30.27 C ANISOU 78 C GLY A 17 4037 3741 3724 73 -130 -14 C ATOM 79 O GLY A 17 54.273 -5.403 42.969 1.00 31.88 O ANISOU 79 O GLY A 17 4231 3921 3962 69 -120 2 O ATOM 80 N ASP A 18 53.477 -5.146 45.056 1.00 28.99 N ANISOU 80 N ASP A 18 3906 3602 3506 93 -138 -1 N ATOM 81 CA ASP A 18 53.830 -6.489 45.489 1.00 33.66 C ANISOU 81 CA ASP A 18 4528 4184 4078 109 -136 41 C ATOM 82 C ASP A 18 53.292 -7.572 44.569 1.00 35.00 C ANISOU 82 C ASP A 18 4708 4320 4270 85 -95 72 C ATOM 83 O ASP A 18 52.223 -7.416 43.985 1.00 30.28 O ANISOU 83 O ASP A 18 4106 3721 3677 55 -59 68 O ATOM 84 CB ASP A 18 53.252 -6.736 46.872 1.00 36.04 C ANISOU 84 CB ASP A 18 4865 4522 4305 127 -136 61 C ATOM 85 CG ASP A 18 54.120 -6.189 47.968 1.00 40.36 C ANISOU 85 CG ASP A 18 5413 5100 4821 168 -190 37 C ATOM 86 OD1 ASP A 18 55.176 -5.591 47.656 1.00 37.53 O ANISOU 86 OD1 ASP A 18 5023 4729 4509 178 -230 4 O ATOM 87 OD2 ASP A 18 53.736 -6.368 49.142 1.00 38.57 O ANISOU 87 OD2 ASP A 18 5217 4913 4523 190 -193 53 O ATOM 88 N GLY A 19 54.011 -8.692 44.479 1.00 32.99 N ANISOU 88 N GLY A 19 4469 4036 4031 101 -106 99 N ATOM 89 CA GLY A 19 53.501 -9.847 43.764 1.00 30.84 C ANISOU 89 CA GLY A 19 4214 3725 3781 83 -76 125 C ATOM 90 C GLY A 19 52.151 -10.251 44.325 1.00 35.55 C ANISOU 90 C GLY A 19 4840 4328 4339 55 -41 157 C ATOM 91 O GLY A 19 51.951 -10.238 45.531 1.00 32.76 O ANISOU 91 O GLY A 19 4511 4004 3932 66 -46 181 O ATOM 92 N GLY A 20 51.213 -10.580 43.443 1.00 30.46 N ANISOU 92 N GLY A 20 4190 3664 3721 21 -6 157 N ATOM 93 CA GLY A 20 49.920 -11.085 43.862 1.00 31.75 C ANISOU 93 CA GLY A 20 4372 3830 3860 -13 30 189 C ATOM 94 C GLY A 20 48.843 -10.042 44.099 1.00 33.40 C ANISOU 94 C GLY A 20 4560 4092 4037 -32 56 166 C ATOM 95 O GLY A 20 47.744 -10.360 44.555 1.00 39.22 O ANISOU 95 O GLY A 20 5304 4848 4748 -59 90 191 O ATOM 96 N THR A 21 49.141 -8.794 43.779 1.00 33.35 N ANISOU 96 N THR A 21 4526 4110 4036 -17 40 118 N ATOM 97 CA THR A 21 48.195 -7.719 44.054 1.00 27.25 C ANISOU 97 CA THR A 21 3735 3385 3234 -24 55 89 C ATOM 98 C THR A 21 47.157 -7.563 42.936 1.00 34.90 C ANISOU 98 C THR A 21 4680 4347 4235 -54 85 67 C ATOM 99 O THR A 21 46.127 -6.911 43.134 1.00 33.93 O ANISOU 99 O THR A 21 4541 4261 4088 -62 103 47 O ATOM 100 CB THR A 21 48.930 -6.379 44.301 1.00 29.34 C ANISOU 100 CB THR A 21 3984 3671 3495 6 17 46 C ATOM 101 OG1 THR A 21 49.854 -6.118 43.237 1.00 30.73 O ANISOU 101 OG1 THR A 21 4139 3810 3725 8 -3 29 O ATOM 102 CG2 THR A 21 49.705 -6.446 45.620 1.00 31.43 C ANISOU 102 CG2 THR A 21 4270 3958 3715 40 -14 59 C ATOM 103 N GLY A 22 47.433 -8.184 41.785 1.00 33.29 N ANISOU 103 N GLY A 22 4472 4098 4080 -65 86 68 N ATOM 104 CA GLY A 22 46.525 -8.168 40.637 1.00 29.15 C ANISOU 104 CA GLY A 22 3926 3565 3584 -88 108 46 C ATOM 105 C GLY A 22 46.971 -7.305 39.480 1.00 27.87 C ANISOU 105 C GLY A 22 3741 3397 3451 -75 93 11 C ATOM 106 O GLY A 22 46.146 -6.884 38.645 1.00 29.73 O ANISOU 106 O GLY A 22 3958 3641 3698 -86 105 -14 O ATOM 107 N LYS A 23 48.271 -7.024 39.388 1.00 27.04 N ANISOU 107 N LYS A 23 3634 3281 3358 -53 67 11 N ATOM 108 CA LYS A 23 48.753 -6.148 38.315 1.00 31.15 C ANISOU 108 CA LYS A 23 4130 3800 3904 -45 57 -12 C ATOM 109 C LYS A 23 48.496 -6.711 36.925 1.00 30.76 C ANISOU 109 C LYS A 23 4072 3736 3880 -51 73 -20 C ATOM 110 O LYS A 23 47.994 -6.023 36.044 1.00 30.44 O ANISOU 110 O LYS A 23 4015 3705 3845 -55 79 -38 O ATOM 111 CB LYS A 23 50.235 -5.810 38.481 1.00 29.74 C ANISOU 111 CB LYS A 23 3943 3618 3740 -26 28 -7 C ATOM 112 CG LYS A 23 50.547 -5.227 39.837 1.00 26.68 C ANISOU 112 CG LYS A 23 3564 3246 3328 -14 3 -8 C ATOM 113 CD LYS A 23 52.026 -4.804 39.932 1.00 29.18 C ANISOU 113 CD LYS A 23 3862 3558 3667 2 -30 -11 C ATOM 114 CE LYS A 23 52.971 -6.013 39.847 1.00 27.88 C ANISOU 114 CE LYS A 23 3702 3378 3513 18 -35 9 C ATOM 115 NZ LYS A 23 52.711 -7.051 40.897 1.00 33.74 N ANISOU 115 NZ LYS A 23 4481 4116 4223 28 -36 33 N ATOM 116 N THR A 24 48.837 -7.974 36.732 1.00 28.99 N ANISOU 116 N THR A 24 3860 3486 3670 -48 75 -8 N ATOM 117 CA THR A 24 48.681 -8.594 35.431 1.00 30.55 C ANISOU 117 CA THR A 24 4049 3669 3889 -46 84 -24 C ATOM 118 C THR A 24 47.210 -8.725 35.083 1.00 28.91 C ANISOU 118 C THR A 24 3839 3464 3680 -69 102 -40 C ATOM 119 O THR A 24 46.806 -8.453 33.950 1.00 30.04 O ANISOU 119 O THR A 24 3967 3618 3830 -66 107 -65 O ATOM 120 CB THR A 24 49.385 -9.940 35.428 1.00 34.14 C ANISOU 120 CB THR A 24 4519 4089 4362 -31 74 -14 C ATOM 121 OG1 THR A 24 50.777 -9.684 35.589 1.00 26.74 O ANISOU 121 OG1 THR A 24 3573 3160 3428 -4 56 -7 O ATOM 122 CG2 THR A 24 49.171 -10.673 34.123 1.00 31.85 C ANISOU 122 CG2 THR A 24 4223 3784 4094 -23 78 -41 C ATOM 123 N THR A 25 46.412 -9.110 36.070 1.00 29.11 N ANISOU 123 N THR A 25 3878 3487 3695 -93 112 -24 N ATOM 124 CA THR A 25 44.985 -9.266 35.854 1.00 28.78 C ANISOU 124 CA THR A 25 3826 3453 3657 -120 131 -39 C ATOM 125 C THR A 25 44.424 -7.916 35.447 1.00 31.48 C ANISOU 125 C THR A 25 4145 3832 3982 -113 132 -67 C ATOM 126 O THR A 25 43.597 -7.834 34.530 1.00 30.12 O ANISOU 126 O THR A 25 3957 3668 3820 -118 137 -95 O ATOM 127 CB THR A 25 44.282 -9.776 37.111 1.00 31.79 C ANISOU 127 CB THR A 25 4219 3837 4023 -148 148 -9 C ATOM 128 OG1 THR A 25 44.815 -11.061 37.447 1.00 31.84 O ANISOU 128 OG1 THR A 25 4252 3798 4048 -154 141 24 O ATOM 129 CG2 THR A 25 42.784 -9.899 36.893 1.00 32.43 C ANISOU 129 CG2 THR A 25 4278 3934 4111 -181 170 -26 C ATOM 130 N PHE A 26 44.898 -6.857 36.105 1.00 27.66 N ANISOU 130 N PHE A 26 3662 3370 3478 -99 122 -62 N ATOM 131 CA PHE A 26 44.428 -5.508 35.799 1.00 23.70 C ANISOU 131 CA PHE A 26 3145 2894 2967 -89 116 -87 C ATOM 132 C PHE A 26 44.788 -5.080 34.396 1.00 27.17 C ANISOU 132 C PHE A 26 3574 3327 3423 -75 108 -99 C ATOM 133 O PHE A 26 43.914 -4.693 33.612 1.00 30.28 O ANISOU 133 O PHE A 26 3956 3734 3816 -73 110 -122 O ATOM 134 CB PHE A 26 45.012 -4.500 36.806 1.00 23.03 C ANISOU 134 CB PHE A 26 3064 2821 2864 -76 98 -82 C ATOM 135 CG PHE A 26 44.540 -3.091 36.599 1.00 25.62 C ANISOU 135 CG PHE A 26 3380 3164 3189 -63 84 -109 C ATOM 136 CD1 PHE A 26 43.249 -2.730 36.932 1.00 28.06 C ANISOU 136 CD1 PHE A 26 3679 3503 3480 -64 92 -135 C ATOM 137 CD2 PHE A 26 45.390 -2.128 36.094 1.00 30.44 C ANISOU 137 CD2 PHE A 26 3988 3760 3818 -51 60 -108 C ATOM 138 CE1 PHE A 26 42.813 -1.432 36.765 1.00 28.36 C ANISOU 138 CE1 PHE A 26 3708 3550 3518 -45 72 -163 C ATOM 139 CE2 PHE A 26 44.946 -0.811 35.915 1.00 30.22 C ANISOU 139 CE2 PHE A 26 3955 3735 3793 -39 41 -129 C ATOM 140 CZ PHE A 26 43.664 -0.480 36.267 1.00 28.45 C ANISOU 140 CZ PHE A 26 3725 3536 3551 -32 44 -159 C ATOM 141 N VAL A 27 46.066 -5.139 34.042 1.00 28.90 N ANISOU 141 N VAL A 27 3795 3533 3652 -63 99 -82 N ATOM 142 CA VAL A 27 46.420 -4.691 32.696 1.00 26.34 C ANISOU 142 CA VAL A 27 3459 3214 3335 -49 97 -87 C ATOM 143 C VAL A 27 45.727 -5.497 31.601 1.00 28.83 C ANISOU 143 C VAL A 27 3770 3532 3652 -45 107 -108 C ATOM 144 O VAL A 27 45.366 -4.949 30.566 1.00 35.09 O ANISOU 144 O VAL A 27 4554 4341 4437 -33 106 -120 O ATOM 145 CB VAL A 27 47.951 -4.641 32.470 1.00 29.32 C ANISOU 145 CB VAL A 27 3830 3587 3723 -37 91 -65 C ATOM 146 CG1 VAL A 27 48.516 -6.028 32.338 1.00 31.09 C ANISOU 146 CG1 VAL A 27 4059 3799 3955 -28 96 -64 C ATOM 147 CG2 VAL A 27 48.295 -3.807 31.242 1.00 28.16 C ANISOU 147 CG2 VAL A 27 3667 3456 3576 -27 93 -58 C ATOM 148 N LYS A 28 45.522 -6.796 31.817 1.00 29.48 N ANISOU 148 N LYS A 28 3860 3595 3745 -54 113 -114 N ATOM 149 CA LYS A 28 44.935 -7.625 30.769 1.00 27.47 C ANISOU 149 CA LYS A 28 3601 3337 3499 -50 114 -143 C ATOM 150 C LYS A 28 43.444 -7.391 30.469 1.00 29.11 C ANISOU 150 C LYS A 28 3797 3561 3705 -62 116 -172 C ATOM 151 O LYS A 28 42.904 -8.004 29.536 1.00 33.03 O ANISOU 151 O LYS A 28 4285 4056 4209 -56 112 -204 O ATOM 152 CB LYS A 28 45.130 -9.103 31.096 1.00 29.60 C ANISOU 152 CB LYS A 28 3884 3569 3792 -58 112 -142 C ATOM 153 CG LYS A 28 46.527 -9.633 30.805 1.00 32.10 C ANISOU 153 CG LYS A 28 4206 3874 4116 -30 104 -134 C ATOM 154 CD LYS A 28 46.607 -11.114 31.213 1.00 44.69 C ANISOU 154 CD LYS A 28 5820 5420 5739 -36 95 -133 C ATOM 155 CE LYS A 28 48.048 -11.612 31.182 1.00 57.96 C ANISOU 155 CE LYS A 28 7506 7089 7426 -3 83 -125 C ATOM 156 NZ LYS A 28 48.842 -10.922 30.119 1.00 61.42 N ANISOU 156 NZ LYS A 28 7921 7571 7846 30 87 -138 N ATOM 157 N ARG A 29 42.773 -6.573 31.273 1.00 27.50 N ANISOU 157 N ARG A 29 3588 3372 3490 -75 120 -168 N ATOM 158 CA ARG A 29 41.360 -6.268 31.044 1.00 28.73 C ANISOU 158 CA ARG A 29 3725 3550 3643 -82 121 -199 C ATOM 159 C ARG A 29 41.184 -5.621 29.678 1.00 26.26 C ANISOU 159 C ARG A 29 3403 3255 3318 -53 107 -221 C ATOM 160 O ARG A 29 40.168 -5.819 29.001 1.00 32.18 O ANISOU 160 O ARG A 29 4137 4019 4071 -50 101 -257 O ATOM 161 CB ARG A 29 40.790 -5.334 32.128 1.00 30.43 C ANISOU 161 CB ARG A 29 3933 3786 3842 -89 125 -196 C ATOM 162 CG ARG A 29 40.907 -5.838 33.580 1.00 33.60 C ANISOU 162 CG ARG A 29 4343 4183 4240 -113 140 -170 C ATOM 163 CD ARG A 29 40.526 -7.313 33.708 1.00 32.45 C ANISOU 163 CD ARG A 29 4196 4015 4117 -145 155 -163 C ATOM 164 NE ARG A 29 39.107 -7.547 33.440 1.00 31.95 N ANISOU 164 NE ARG A 29 4103 3971 4065 -166 164 -193 N ATOM 165 CZ ARG A 29 38.522 -8.746 33.514 1.00 34.68 C ANISOU 165 CZ ARG A 29 4440 4297 4440 -202 176 -191 C ATOM 166 NH1 ARG A 29 39.235 -9.822 33.831 1.00 34.34 N ANISOU 166 NH1 ARG A 29 4423 4209 4416 -218 177 -159 N ATOM 167 NH2 ARG A 29 37.224 -8.876 33.267 1.00 32.17 N ANISOU 167 NH2 ARG A 29 4086 4000 4136 -224 182 -221 N ATOM 168 N HIS A 30 42.198 -4.868 29.265 1.00 27.59 N ANISOU 168 N HIS A 30 3582 3426 3474 -31 102 -198 N ATOM 169 CA HIS A 30 42.155 -4.121 28.014 1.00 29.80 C ANISOU 169 CA HIS A 30 3859 3727 3736 -2 91 -204 C ATOM 170 C HIS A 30 42.485 -5.063 26.864 1.00 26.21 C ANISOU 170 C HIS A 30 3403 3279 3275 16 93 -219 C ATOM 171 O HIS A 30 43.621 -5.500 26.706 1.00 27.68 O ANISOU 171 O HIS A 30 3595 3460 3463 23 100 -201 O ATOM 172 CB HIS A 30 43.163 -2.955 28.092 1.00 29.18 C ANISOU 172 CB HIS A 30 3790 3647 3652 6 88 -163 C ATOM 173 CG HIS A 30 42.999 -1.931 27.016 1.00 27.96 C ANISOU 173 CG HIS A 30 3637 3509 3478 30 77 -155 C ATOM 174 ND1 HIS A 30 43.294 -2.182 25.696 1.00 28.03 N ANISOU 174 ND1 HIS A 30 3645 3542 3465 54 81 -152 N ATOM 175 CD2 HIS A 30 42.614 -0.633 27.080 1.00 29.81 C ANISOU 175 CD2 HIS A 30 3876 3739 3710 37 59 -145 C ATOM 176 CE1 HIS A 30 43.061 -1.091 24.981 1.00 36.57 C ANISOU 176 CE1 HIS A 30 4733 4636 4528 72 69 -134 C ATOM 177 NE2 HIS A 30 42.656 -0.135 25.799 1.00 28.88 N ANISOU 177 NE2 HIS A 30 3764 3640 3571 62 54 -130 N ATOM 178 N LEU A 31 41.474 -5.373 26.048 1.00 26.96 N ANISOU 178 N LEU A 31 3488 3390 3365 28 82 -261 N ATOM 179 CA LEU A 31 41.588 -6.483 25.112 1.00 29.96 C ANISOU 179 CA LEU A 31 3865 3774 3745 46 77 -293 C ATOM 180 C LEU A 31 42.608 -6.236 24.010 1.00 27.97 C ANISOU 180 C LEU A 31 3619 3551 3459 85 80 -277 C ATOM 181 O LEU A 31 43.377 -7.128 23.665 1.00 28.36 O ANISOU 181 O LEU A 31 3669 3598 3510 99 84 -287 O ATOM 182 CB LEU A 31 40.219 -6.839 24.525 1.00 32.02 C ANISOU 182 CB LEU A 31 4109 4046 4010 50 58 -348 C ATOM 183 CG LEU A 31 39.209 -7.453 25.488 1.00 31.87 C ANISOU 183 CG LEU A 31 4075 4004 4032 7 59 -367 C ATOM 184 CD1 LEU A 31 37.838 -7.561 24.842 1.00 36.04 C ANISOU 184 CD1 LEU A 31 4577 4552 4565 11 38 -422 C ATOM 185 CD2 LEU A 31 39.690 -8.839 25.935 1.00 37.42 C ANISOU 185 CD2 LEU A 31 4786 4662 4770 -18 64 -367 C ATOM 186 N THR A 32 42.614 -5.030 23.439 1.00 24.95 N ANISOU 186 N THR A 32 3238 3197 3044 104 79 -253 N ATOM 187 CA THR A 32 43.593 -4.734 22.401 1.00 28.49 C ANISOU 187 CA THR A 32 3688 3681 3455 136 90 -226 C ATOM 188 C THR A 32 44.995 -4.621 23.002 1.00 29.88 C ANISOU 188 C THR A 32 3864 3845 3644 120 110 -179 C ATOM 189 O THR A 32 45.979 -5.043 22.393 1.00 34.30 O ANISOU 189 O THR A 32 4416 4431 4187 142 125 -171 O ATOM 190 CB THR A 32 43.210 -3.447 21.652 1.00 34.71 C ANISOU 190 CB THR A 32 4483 4498 4208 157 82 -200 C ATOM 191 OG1 THR A 32 41.892 -3.613 21.119 1.00 33.21 O ANISOU 191 OG1 THR A 32 4290 4323 4007 176 58 -252 O ATOM 192 CG2 THR A 32 44.185 -3.177 20.520 1.00 35.62 C ANISOU 192 CG2 THR A 32 4597 4659 4276 188 100 -165 C ATOM 193 N GLY A 33 45.076 -4.068 24.208 1.00 29.01 N ANISOU 193 N GLY A 33 3758 3700 3564 86 110 -153 N ATOM 194 CA GLY A 33 46.331 -4.020 24.937 1.00 25.96 C ANISOU 194 CA GLY A 33 3368 3299 3197 70 122 -117 C ATOM 195 C GLY A 33 46.919 -5.420 25.090 1.00 34.81 C ANISOU 195 C GLY A 33 4485 4411 4329 77 127 -140 C ATOM 196 O GLY A 33 48.130 -5.613 25.046 1.00 34.82 O ANISOU 196 O GLY A 33 4476 4423 4333 85 138 -120 O ATOM 197 N GLU A 34 46.059 -6.410 25.271 1.00 29.84 N ANISOU 197 N GLU A 34 3862 3761 3714 73 116 -182 N ATOM 198 CA GLU A 34 46.546 -7.772 25.429 1.00 30.08 C ANISOU 198 CA GLU A 34 3894 3769 3764 80 113 -204 C ATOM 199 C GLU A 34 46.895 -8.361 24.055 1.00 37.11 C ANISOU 199 C GLU A 34 4776 4695 4629 126 113 -237 C ATOM 200 O GLU A 34 47.934 -9.010 23.895 1.00 33.19 O ANISOU 200 O GLU A 34 4274 4204 4134 149 117 -240 O ATOM 201 CB GLU A 34 45.510 -8.634 26.152 1.00 30.97 C ANISOU 201 CB GLU A 34 4017 3840 3909 53 101 -231 C ATOM 202 CG GLU A 34 45.803 -10.152 26.109 1.00 33.79 C ANISOU 202 CG GLU A 34 4382 4163 4294 63 89 -260 C ATOM 203 CD GLU A 34 47.055 -10.538 26.875 1.00 43.97 C ANISOU 203 CD GLU A 34 5679 5430 5597 66 92 -231 C ATOM 204 OE1 GLU A 34 47.492 -9.750 27.736 1.00 34.63 O ANISOU 204 OE1 GLU A 34 4497 4251 4411 48 102 -189 O ATOM 205 OE2 GLU A 34 47.600 -11.637 26.628 1.00 46.27 O ANISOU 205 OE2 GLU A 34 5975 5701 5906 90 79 -253 O ATOM 206 N SER A 35 46.046 -8.127 23.054 1.00 32.56 N ANISOU 206 N SER A 35 4197 4148 4025 145 106 -264 N ATOM 207 CA SER A 35 46.312 -8.700 21.728 1.00 36.23 C ANISOU 207 CA SER A 35 4654 4655 4456 196 102 -303 C ATOM 208 C SER A 35 47.554 -8.111 21.049 1.00 41.74 C ANISOU 208 C SER A 35 5337 5410 5112 225 128 -264 C ATOM 209 O SER A 35 48.191 -8.773 20.231 1.00 40.36 O ANISOU 209 O SER A 35 5151 5272 4911 269 132 -292 O ATOM 210 CB SER A 35 45.090 -8.598 20.798 1.00 31.22 C ANISOU 210 CB SER A 35 4020 4046 3797 215 83 -346 C ATOM 211 OG SER A 35 44.791 -7.256 20.471 1.00 34.83 O ANISOU 211 OG SER A 35 4478 4536 4220 215 92 -307 O ATOM 212 N GLU A 36 47.909 -6.880 21.406 1.00 36.12 N ANISOU 212 N GLU A 36 4623 4706 4395 199 146 -202 N ATOM 213 CA GLU A 36 49.021 -6.184 20.758 1.00 33.33 C ANISOU 213 CA GLU A 36 4250 4406 4007 215 174 -154 C ATOM 214 C GLU A 36 50.214 -6.001 21.709 1.00 36.05 C ANISOU 214 C GLU A 36 4580 4732 4386 188 188 -113 C ATOM 215 O GLU A 36 51.125 -5.220 21.440 1.00 37.29 O ANISOU 215 O GLU A 36 4716 4923 4530 183 211 -61 O ATOM 216 CB GLU A 36 48.539 -4.845 20.164 1.00 36.34 C ANISOU 216 CB GLU A 36 4638 4814 4355 211 180 -111 C ATOM 217 CG GLU A 36 47.450 -5.092 19.098 1.00 35.19 C ANISOU 217 CG GLU A 36 4504 4701 4167 250 163 -156 C ATOM 218 CD GLU A 36 46.848 -3.834 18.467 1.00 47.28 C ANISOU 218 CD GLU A 36 6047 6255 5662 254 160 -117 C ATOM 219 OE1 GLU A 36 47.182 -2.704 18.888 1.00 50.92 O ANISOU 219 OE1 GLU A 36 6511 6699 6139 222 169 -52 O ATOM 220 OE2 GLU A 36 46.019 -3.998 17.539 1.00 53.56 O ANISOU 220 OE2 GLU A 36 6850 7085 6417 293 143 -154 O ATOM 221 N LYS A 37 50.219 -6.760 22.797 1.00 37.23 N ANISOU 221 N LYS A 37 4739 4828 4580 170 171 -134 N ATOM 222 CA LYS A 37 51.306 -6.665 23.765 1.00 36.78 C ANISOU 222 CA LYS A 37 4669 4752 4555 150 176 -103 C ATOM 223 C LYS A 37 52.632 -7.112 23.151 1.00 39.44 C ANISOU 223 C LYS A 37 4973 5137 4876 185 195 -102 C ATOM 224 O LYS A 37 52.667 -7.908 22.200 1.00 35.82 O ANISOU 224 O LYS A 37 4509 4714 4389 231 198 -143 O ATOM 225 CB LYS A 37 50.994 -7.447 25.050 1.00 35.70 C ANISOU 225 CB LYS A 37 4553 4551 4460 130 154 -123 C ATOM 226 CG LYS A 37 51.136 -8.954 24.936 1.00 36.94 C ANISOU 226 CG LYS A 37 4717 4691 4628 161 140 -170 C ATOM 227 CD LYS A 37 50.762 -9.645 26.242 1.00 37.03 C ANISOU 227 CD LYS A 37 4753 4636 4679 134 120 -173 C ATOM 228 CE LYS A 37 50.693 -11.157 26.057 1.00 40.55 C ANISOU 228 CE LYS A 37 5212 5049 5145 160 100 -219 C ATOM 229 NZ LYS A 37 50.206 -11.824 27.294 1.00 40.34 N ANISOU 229 NZ LYS A 37 5215 4957 5157 129 83 -211 N ATOM 230 N LYS A 38 53.720 -6.574 23.684 1.00 33.61 N ANISOU 230 N LYS A 38 4209 4405 4157 166 206 -61 N ATOM 231 CA LYS A 38 55.053 -6.860 23.171 1.00 33.93 C ANISOU 231 CA LYS A 38 4206 4499 4184 195 227 -56 C ATOM 232 C LYS A 38 55.928 -7.365 24.298 1.00 38.81 C ANISOU 232 C LYS A 38 4814 5085 4847 190 211 -60 C ATOM 233 O LYS A 38 56.002 -6.736 25.346 1.00 35.41 O ANISOU 233 O LYS A 38 4389 4615 4449 150 198 -31 O ATOM 234 CB LYS A 38 55.655 -5.588 22.569 1.00 41.15 C ANISOU 234 CB LYS A 38 5087 5466 5080 175 259 7 C ATOM 235 CG LYS A 38 54.825 -5.028 21.416 1.00 49.38 C ANISOU 235 CG LYS A 38 6144 6545 6073 185 274 20 C ATOM 236 CD LYS A 38 55.577 -3.965 20.641 1.00 66.28 C ANISOU 236 CD LYS A 38 8249 8746 8188 172 312 88 C ATOM 237 CE LYS A 38 54.787 -3.550 19.411 1.00 79.03 C ANISOU 237 CE LYS A 38 9882 10405 9742 194 325 101 C ATOM 238 NZ LYS A 38 55.401 -2.391 18.710 1.00 86.83 N ANISOU 238 NZ LYS A 38 10843 11443 10706 172 362 185 N ATOM 239 N TYR A 39 56.587 -8.499 24.085 1.00 36.29 N ANISOU 239 N TYR A 39 4481 4782 4526 237 206 -100 N ATOM 240 CA TYR A 39 57.467 -9.058 25.107 1.00 36.34 C ANISOU 240 CA TYR A 39 4478 4760 4572 242 186 -105 C ATOM 241 C TYR A 39 58.870 -8.492 24.949 1.00 34.47 C ANISOU 241 C TYR A 39 4179 4582 4337 244 209 -75 C ATOM 242 O TYR A 39 59.404 -8.416 23.842 1.00 41.02 O ANISOU 242 O TYR A 39 4967 5486 5131 272 241 -74 O ATOM 243 CB TYR A 39 57.494 -10.588 25.045 1.00 39.38 C ANISOU 243 CB TYR A 39 4880 5120 4963 295 161 -165 C ATOM 244 CG TYR A 39 58.373 -11.222 26.113 1.00 44.60 C ANISOU 244 CG TYR A 39 5537 5746 5662 307 134 -169 C ATOM 245 CD1 TYR A 39 58.069 -11.086 27.465 1.00 40.79 C ANISOU 245 CD1 TYR A 39 5087 5200 5210 269 109 -144 C ATOM 246 CD2 TYR A 39 59.503 -11.954 25.768 1.00 45.67 C ANISOU 246 CD2 TYR A 39 5636 5919 5798 364 131 -199 C ATOM 247 CE1 TYR A 39 58.875 -11.657 28.449 1.00 41.86 C ANISOU 247 CE1 TYR A 39 5224 5308 5375 285 80 -145 C ATOM 248 CE2 TYR A 39 60.313 -12.528 26.742 1.00 44.07 C ANISOU 248 CE2 TYR A 39 5430 5684 5630 381 100 -204 C ATOM 249 CZ TYR A 39 59.995 -12.377 28.076 1.00 45.64 C ANISOU 249 CZ TYR A 39 5667 5818 5858 342 73 -175 C ATOM 250 OH TYR A 39 60.798 -12.956 29.036 1.00 52.93 O ANISOU 250 OH TYR A 39 6591 6713 6809 365 39 -178 O ATOM 251 N VAL A 40 59.447 -8.072 26.067 1.00 35.75 N ANISOU 251 N VAL A 40 4330 4715 4538 213 192 -50 N ATOM 252 CA VAL A 40 60.776 -7.496 26.082 1.00 35.85 C ANISOU 252 CA VAL A 40 4278 4776 4566 205 207 -22 C ATOM 253 C VAL A 40 61.657 -8.484 26.835 1.00 38.48 C ANISOU 253 C VAL A 40 4598 5096 4925 243 177 -55 C ATOM 254 O VAL A 40 61.690 -8.497 28.072 1.00 37.00 O ANISOU 254 O VAL A 40 4433 4854 4770 226 142 -51 O ATOM 255 CB VAL A 40 60.770 -6.139 26.788 1.00 37.34 C ANISOU 255 CB VAL A 40 4462 4939 4785 141 201 28 C ATOM 256 CG1 VAL A 40 62.151 -5.489 26.722 1.00 40.32 C ANISOU 256 CG1 VAL A 40 4765 5367 5188 124 217 60 C ATOM 257 CG2 VAL A 40 59.717 -5.239 26.156 1.00 34.38 C ANISOU 257 CG2 VAL A 40 4115 4560 4388 109 220 57 C ATOM 258 N ALA A 41 62.349 -9.323 26.073 1.00 37.31 N ANISOU 258 N ALA A 41 4416 5002 4760 301 190 -90 N ATOM 259 CA ALA A 41 63.034 -10.488 26.634 1.00 37.83 C ANISOU 259 CA ALA A 41 4479 5049 4847 354 155 -133 C ATOM 260 C ALA A 41 64.122 -10.125 27.636 1.00 43.19 C ANISOU 260 C ALA A 41 5117 5728 5566 340 134 -115 C ATOM 261 O ALA A 41 64.312 -10.822 28.636 1.00 45.16 O ANISOU 261 O ALA A 41 5393 5926 5839 361 90 -133 O ATOM 262 CB ALA A 41 63.603 -11.346 25.515 1.00 39.34 C ANISOU 262 CB ALA A 41 4633 5305 5008 425 172 -180 C ATOM 263 N THR A 42 64.840 -9.038 27.371 1.00 46.16 N ANISOU 263 N THR A 42 5428 6161 5948 303 164 -77 N ATOM 264 CA THR A 42 65.959 -8.646 28.226 1.00 45.41 C ANISOU 264 CA THR A 42 5282 6075 5896 289 143 -65 C ATOM 265 C THR A 42 65.537 -8.327 29.659 1.00 48.88 C ANISOU 265 C THR A 42 5772 6434 6366 254 95 -53 C ATOM 266 O THR A 42 66.243 -8.669 30.613 1.00 46.07 O ANISOU 266 O THR A 42 5404 6062 6037 273 54 -69 O ATOM 267 CB THR A 42 66.735 -7.446 27.636 1.00 53.80 C ANISOU 267 CB THR A 42 6263 7208 6969 243 185 -20 C ATOM 268 OG1 THR A 42 65.821 -6.384 27.337 1.00 55.93 O ANISOU 268 OG1 THR A 42 6565 7456 7231 183 207 27 O ATOM 269 CG2 THR A 42 67.465 -7.857 26.362 1.00 52.82 C ANISOU 269 CG2 THR A 42 6072 7185 6812 289 233 -33 C ATOM 270 N LEU A 43 64.392 -7.669 29.812 1.00 36.20 N ANISOU 270 N LEU A 43 4219 4783 4751 207 98 -28 N ATOM 271 CA LEU A 43 63.905 -7.289 31.135 1.00 36.35 C ANISOU 271 CA LEU A 43 4284 4736 4789 176 57 -19 C ATOM 272 C LEU A 43 62.787 -8.196 31.638 1.00 37.26 C ANISOU 272 C LEU A 43 4482 4792 4885 195 37 -37 C ATOM 273 O LEU A 43 62.335 -8.071 32.785 1.00 38.75 O ANISOU 273 O LEU A 43 4713 4931 5078 178 5 -31 O ATOM 274 CB LEU A 43 63.429 -5.834 31.122 1.00 37.66 C ANISOU 274 CB LEU A 43 4450 4893 4967 111 69 19 C ATOM 275 CG LEU A 43 64.450 -4.823 30.610 1.00 44.29 C ANISOU 275 CG LEU A 43 5209 5782 5835 77 91 50 C ATOM 276 CD1 LEU A 43 63.777 -3.482 30.322 1.00 37.00 C ANISOU 276 CD1 LEU A 43 4298 4840 4920 17 105 91 C ATOM 277 CD2 LEU A 43 65.569 -4.669 31.616 1.00 44.86 C ANISOU 277 CD2 LEU A 43 5237 5855 5952 75 51 39 C ATOM 278 N GLY A 44 62.336 -9.105 30.781 1.00 39.05 N ANISOU 278 N GLY A 44 4728 5022 5087 229 55 -60 N ATOM 279 CA GLY A 44 61.234 -9.979 31.135 1.00 37.87 C ANISOU 279 CA GLY A 44 4651 4812 4926 239 38 -74 C ATOM 280 C GLY A 44 60.006 -9.158 31.474 1.00 41.38 C ANISOU 280 C GLY A 44 5136 5226 5361 187 45 -50 C ATOM 281 O GLY A 44 59.448 -9.248 32.572 1.00 44.53 O ANISOU 281 O GLY A 44 5578 5579 5762 171 20 -42 O ATOM 282 N VAL A 45 59.585 -8.349 30.511 1.00 33.13 N ANISOU 282 N VAL A 45 4075 4212 4302 163 78 -38 N ATOM 283 CA VAL A 45 58.461 -7.451 30.694 1.00 33.01 C ANISOU 283 CA VAL A 45 4091 4174 4279 118 83 -19 C ATOM 284 C VAL A 45 57.548 -7.619 29.487 1.00 31.23 C ANISOU 284 C VAL A 45 3878 3962 4025 125 111 -30 C ATOM 285 O VAL A 45 58.025 -7.952 28.398 1.00 33.34 O ANISOU 285 O VAL A 45 4116 4274 4277 155 132 -42 O ATOM 286 CB VAL A 45 58.940 -5.989 30.751 1.00 32.47 C ANISOU 286 CB VAL A 45 3986 4125 4227 80 89 14 C ATOM 287 CG1 VAL A 45 57.765 -4.999 30.551 1.00 33.94 C ANISOU 287 CG1 VAL A 45 4199 4294 4402 43 97 30 C ATOM 288 CG2 VAL A 45 59.662 -5.718 32.062 1.00 35.31 C ANISOU 288 CG2 VAL A 45 4336 4465 4615 71 52 17 C ATOM 289 N GLU A 46 56.248 -7.416 29.688 1.00 29.01 N ANISOU 289 N GLU A 46 3639 3648 3735 101 108 -31 N ATOM 290 CA GLU A 46 55.305 -7.327 28.572 1.00 26.76 C ANISOU 290 CA GLU A 46 3364 3380 3424 104 129 -41 C ATOM 291 C GLU A 46 54.772 -5.914 28.557 1.00 30.58 C ANISOU 291 C GLU A 46 3848 3866 3904 66 135 -11 C ATOM 292 O GLU A 46 54.270 -5.435 29.572 1.00 31.52 O ANISOU 292 O GLU A 46 3989 3952 4037 40 117 -5 O ATOM 293 CB GLU A 46 54.118 -8.277 28.764 1.00 33.79 C ANISOU 293 CB GLU A 46 4298 4230 4312 107 117 -71 C ATOM 294 CG GLU A 46 54.464 -9.751 28.615 1.00 40.33 C ANISOU 294 CG GLU A 46 5133 5042 5149 146 105 -105 C ATOM 295 CD GLU A 46 53.236 -10.645 28.650 1.00 53.56 C ANISOU 295 CD GLU A 46 6847 6673 6830 142 93 -132 C ATOM 296 OE1 GLU A 46 52.150 -10.149 29.014 1.00 65.09 O ANISOU 296 OE1 GLU A 46 8325 8117 8288 106 96 -122 O ATOM 297 OE2 GLU A 46 53.358 -11.840 28.309 1.00 55.67 O ANISOU 297 OE2 GLU A 46 7123 6920 7109 174 79 -165 O ATOM 298 N VAL A 47 54.857 -5.260 27.404 1.00 29.85 N ANISOU 298 N VAL A 47 3734 3816 3793 68 159 6 N ATOM 299 CA VAL A 47 54.370 -3.894 27.286 1.00 30.00 C ANISOU 299 CA VAL A 47 3756 3830 3811 36 161 38 C ATOM 300 C VAL A 47 53.014 -3.935 26.579 1.00 26.06 C ANISOU 300 C VAL A 47 3287 3332 3283 45 165 19 C ATOM 301 O VAL A 47 52.917 -4.398 25.443 1.00 31.22 O ANISOU 301 O VAL A 47 3934 4023 3904 74 182 6 O ATOM 302 CB VAL A 47 55.380 -3.017 26.525 1.00 29.03 C ANISOU 302 CB VAL A 47 3591 3749 3689 25 184 83 C ATOM 303 CG1 VAL A 47 54.841 -1.599 26.319 1.00 32.59 C ANISOU 303 CG1 VAL A 47 4052 4185 4146 -7 181 121 C ATOM 304 CG2 VAL A 47 56.717 -2.974 27.276 1.00 31.95 C ANISOU 304 CG2 VAL A 47 3924 4120 4097 14 176 95 C ATOM 305 N HIS A 48 51.967 -3.486 27.272 1.00 29.41 N ANISOU 305 N HIS A 48 3739 3718 3715 25 146 12 N ATOM 306 CA HIS A 48 50.617 -3.510 26.723 1.00 28.35 C ANISOU 306 CA HIS A 48 3628 3584 3559 33 145 -11 C ATOM 307 C HIS A 48 50.250 -2.117 26.204 1.00 30.37 C ANISOU 307 C HIS A 48 3886 3847 3807 22 143 21 C ATOM 308 O HIS A 48 50.172 -1.174 26.979 1.00 29.13 O ANISOU 308 O HIS A 48 3734 3659 3673 -2 126 37 O ATOM 309 CB HIS A 48 49.594 -3.909 27.801 1.00 27.75 C ANISOU 309 CB HIS A 48 3577 3471 3496 19 127 -40 C ATOM 310 CG HIS A 48 49.687 -5.338 28.251 1.00 24.03 C ANISOU 310 CG HIS A 48 3113 2983 3034 27 125 -66 C ATOM 311 ND1 HIS A 48 50.759 -5.836 28.962 1.00 37.67 N ANISOU 311 ND1 HIS A 48 4835 4699 4779 29 121 -55 N ATOM 312 CD2 HIS A 48 48.793 -6.351 28.161 1.00 25.18 C ANISOU 312 CD2 HIS A 48 3273 3115 3179 32 122 -100 C ATOM 313 CE1 HIS A 48 50.541 -7.109 29.253 1.00 33.25 C ANISOU 313 CE1 HIS A 48 4290 4117 4226 38 115 -79 C ATOM 314 NE2 HIS A 48 49.358 -7.449 28.767 1.00 37.20 N ANISOU 314 NE2 HIS A 48 4802 4613 4719 36 116 -105 N ATOM 315 N PRO A 49 50.016 -1.987 24.895 1.00 26.97 N ANISOU 315 N PRO A 49 3452 3454 3340 44 158 28 N ATOM 316 CA PRO A 49 49.658 -0.642 24.421 1.00 31.28 C ANISOU 316 CA PRO A 49 4006 3999 3880 35 152 65 C ATOM 317 C PRO A 49 48.165 -0.406 24.594 1.00 32.63 C ANISOU 317 C PRO A 49 4203 4149 4046 41 129 32 C ATOM 318 O PRO A 49 47.374 -0.964 23.840 1.00 39.86 O ANISOU 318 O PRO A 49 5125 5090 4931 67 130 0 O ATOM 319 CB PRO A 49 49.989 -0.675 22.926 1.00 34.04 C ANISOU 319 CB PRO A 49 4343 4407 4183 62 178 88 C ATOM 320 CG PRO A 49 50.160 -2.130 22.553 1.00 36.55 C ANISOU 320 CG PRO A 49 4651 4756 4478 95 191 41 C ATOM 321 CD PRO A 49 50.250 -2.955 23.811 1.00 24.79 C ANISOU 321 CD PRO A 49 3166 3225 3030 80 177 7 C ATOM 322 N LEU A 50 47.796 0.410 25.566 1.00 27.85 N ANISOU 322 N LEU A 50 3608 3502 3470 19 106 35 N ATOM 323 CA LEU A 50 46.402 0.634 25.905 1.00 24.07 C ANISOU 323 CA LEU A 50 3147 3009 2990 26 84 -2 C ATOM 324 C LEU A 50 45.959 1.969 25.338 1.00 28.99 C ANISOU 324 C LEU A 50 3783 3623 3609 34 66 24 C ATOM 325 O LEU A 50 46.343 3.008 25.853 1.00 30.89 O ANISOU 325 O LEU A 50 4028 3829 3879 16 48 53 O ATOM 326 CB LEU A 50 46.230 0.686 27.418 1.00 26.58 C ANISOU 326 CB LEU A 50 3468 3294 3338 6 69 -23 C ATOM 327 CG LEU A 50 46.055 -0.667 28.117 1.00 39.34 C ANISOU 327 CG LEU A 50 5082 4913 4954 1 80 -57 C ATOM 328 CD1 LEU A 50 47.200 -1.597 27.787 1.00 37.13 C ANISOU 328 CD1 LEU A 50 4791 4645 4673 3 100 -44 C ATOM 329 CD2 LEU A 50 45.892 -0.497 29.626 1.00 38.35 C ANISOU 329 CD2 LEU A 50 4961 4764 4846 -15 67 -70 C ATOM 330 N VAL A 51 45.175 1.936 24.273 1.00 26.70 N ANISOU 330 N VAL A 51 3500 3361 3283 63 64 15 N ATOM 331 CA VAL A 51 44.639 3.155 23.703 1.00 27.73 C ANISOU 331 CA VAL A 51 3648 3481 3407 78 41 40 C ATOM 332 C VAL A 51 43.328 3.516 24.382 1.00 27.71 C ANISOU 332 C VAL A 51 3654 3458 3417 88 9 -9 C ATOM 333 O VAL A 51 42.469 2.669 24.588 1.00 27.77 O ANISOU 333 O VAL A 51 3652 3484 3415 97 11 -64 O ATOM 334 CB VAL A 51 44.416 3.024 22.196 1.00 33.85 C ANISOU 334 CB VAL A 51 4428 4304 4129 112 50 55 C ATOM 335 CG1 VAL A 51 43.885 4.339 21.647 1.00 37.07 C ANISOU 335 CG1 VAL A 51 4860 4696 4530 129 22 90 C ATOM 336 CG2 VAL A 51 45.722 2.648 21.518 1.00 37.81 C ANISOU 336 CG2 VAL A 51 4915 4841 4611 106 87 100 C ATOM 337 N PHE A 52 43.198 4.788 24.734 1.00 25.49 N ANISOU 337 N PHE A 52 3388 3136 3161 87 -21 10 N ATOM 338 CA PHE A 52 41.942 5.366 25.194 1.00 31.29 C ANISOU 338 CA PHE A 52 4130 3855 3903 109 -56 -35 C ATOM 339 C PHE A 52 41.542 6.518 24.277 1.00 31.04 C ANISOU 339 C PHE A 52 4122 3808 3863 138 -87 -3 C ATOM 340 O PHE A 52 42.375 7.332 23.921 1.00 31.78 O ANISOU 340 O PHE A 52 4231 3873 3972 125 -92 61 O ATOM 341 CB PHE A 52 42.129 5.911 26.603 1.00 28.55 C ANISOU 341 CB PHE A 52 3782 3467 3598 91 -75 -50 C ATOM 342 CG PHE A 52 42.378 4.842 27.615 1.00 30.92 C ANISOU 342 CG PHE A 52 4064 3783 3901 68 -50 -80 C ATOM 343 CD1 PHE A 52 43.639 4.305 27.770 1.00 31.60 C ANISOU 343 CD1 PHE A 52 4143 3867 3996 40 -25 -48 C ATOM 344 CD2 PHE A 52 41.344 4.372 28.410 1.00 32.47 C ANISOU 344 CD2 PHE A 52 4248 3998 4090 76 -50 -138 C ATOM 345 CE1 PHE A 52 43.858 3.302 28.704 1.00 29.73 C ANISOU 345 CE1 PHE A 52 3895 3641 3761 24 -7 -72 C ATOM 346 CE2 PHE A 52 41.560 3.379 29.353 1.00 32.01 C ANISOU 346 CE2 PHE A 52 4177 3952 4032 53 -26 -155 C ATOM 347 CZ PHE A 52 42.807 2.839 29.493 1.00 29.74 C ANISOU 347 CZ PHE A 52 3890 3658 3753 29 -7 -121 C ATOM 348 N HIS A 53 40.272 6.587 23.902 1.00 28.32 N ANISOU 348 N HIS A 53 3779 3483 3497 177 -110 -45 N ATOM 349 CA HIS A 53 39.824 7.673 23.032 1.00 25.25 C ANISOU 349 CA HIS A 53 3417 3079 3098 212 -146 -16 C ATOM 350 C HIS A 53 39.287 8.833 23.863 1.00 30.06 C ANISOU 350 C HIS A 53 4039 3634 3748 226 -194 -37 C ATOM 351 O HIS A 53 38.316 8.686 24.601 1.00 29.93 O ANISOU 351 O HIS A 53 4005 3629 3737 244 -209 -108 O ATOM 352 CB HIS A 53 38.800 7.139 22.028 1.00 30.29 C ANISOU 352 CB HIS A 53 4050 3772 3686 255 -151 -51 C ATOM 353 CG HIS A 53 39.413 6.259 20.987 1.00 30.80 C ANISOU 353 CG HIS A 53 4111 3886 3707 254 -114 -23 C ATOM 354 ND1 HIS A 53 39.297 4.888 21.006 1.00 37.98 N ANISOU 354 ND1 HIS A 53 4993 4836 4601 246 -86 -73 N ATOM 355 CD2 HIS A 53 40.186 6.559 19.915 1.00 32.20 C ANISOU 355 CD2 HIS A 53 4306 4077 3851 260 -100 48 C ATOM 356 CE1 HIS A 53 39.951 4.381 19.975 1.00 29.02 C ANISOU 356 CE1 HIS A 53 3861 3741 3425 255 -61 -42 C ATOM 357 NE2 HIS A 53 40.508 5.371 19.304 1.00 38.14 N ANISOU 357 NE2 HIS A 53 5041 4886 4564 263 -65 33 N ATOM 358 N THR A 54 39.950 9.985 23.763 1.00 31.80 N ANISOU 358 N THR A 54 4288 3796 4000 217 -219 23 N ATOM 359 CA THR A 54 39.567 11.151 24.545 1.00 28.81 C ANISOU 359 CA THR A 54 3925 3354 3667 232 -273 2 C ATOM 360 C THR A 54 38.880 12.171 23.666 1.00 30.74 C ANISOU 360 C THR A 54 4203 3571 3906 279 -321 25 C ATOM 361 O THR A 54 38.840 12.028 22.440 1.00 33.29 O ANISOU 361 O THR A 54 4538 3924 4186 294 -310 70 O ATOM 362 CB THR A 54 40.784 11.828 25.205 1.00 26.89 C ANISOU 362 CB THR A 54 3691 3046 3482 187 -282 46 C ATOM 363 OG1 THR A 54 41.428 12.710 24.270 1.00 30.85 O ANISOU 363 OG1 THR A 54 4222 3503 3998 176 -295 137 O ATOM 364 CG2 THR A 54 41.759 10.784 25.661 1.00 29.29 C ANISOU 364 CG2 THR A 54 3966 3381 3781 141 -229 52 C ATOM 365 N ASN A 55 38.333 13.207 24.287 1.00 31.79 N ANISOU 365 N ASN A 55 4351 3648 4080 307 -379 -8 N ATOM 366 CA ASN A 55 37.656 14.235 23.505 1.00 36.26 C ANISOU 366 CA ASN A 55 4953 4179 4646 358 -434 13 C ATOM 367 C ASN A 55 38.648 14.964 22.613 1.00 44.88 C ANISOU 367 C ASN A 55 6083 5218 5751 331 -437 128 C ATOM 368 O ASN A 55 38.262 15.601 21.628 1.00 51.00 O ANISOU 368 O ASN A 55 6892 5977 6508 367 -468 174 O ATOM 369 CB ASN A 55 36.864 15.203 24.389 1.00 32.98 C ANISOU 369 CB ASN A 55 4545 3711 4274 401 -501 -54 C ATOM 370 CG ASN A 55 37.746 15.970 25.360 1.00 37.60 C ANISOU 370 CG ASN A 55 5142 4214 4928 366 -526 -42 C ATOM 371 OD1 ASN A 55 38.588 15.394 26.033 1.00 32.44 O ANISOU 371 OD1 ASN A 55 4467 3573 4286 315 -486 -41 O ATOM 372 ND2 ASN A 55 37.561 17.285 25.415 1.00 42.01 N ANISOU 372 ND2 ASN A 55 5738 4686 5537 396 -598 -35 N ATOM 373 N ARG A 56 39.931 14.837 22.940 1.00 34.09 N ANISOU 373 N ARG A 56 4708 3831 4415 266 -403 178 N ATOM 374 CA ARG A 56 40.976 15.448 22.128 1.00 45.13 C ANISOU 374 CA ARG A 56 6131 5188 5828 228 -395 294 C ATOM 375 C ARG A 56 41.794 14.455 21.309 1.00 42.49 C ANISOU 375 C ARG A 56 5776 4930 5440 196 -320 350 C ATOM 376 O ARG A 56 42.889 14.774 20.851 1.00 55.88 O ANISOU 376 O ARG A 56 7475 6607 7150 150 -296 443 O ATOM 377 CB ARG A 56 41.888 16.305 22.999 1.00 45.39 C ANISOU 377 CB ARG A 56 6170 5129 5949 180 -423 319 C ATOM 378 CG ARG A 56 41.224 17.614 23.391 1.00 48.64 C ANISOU 378 CG ARG A 56 6617 5445 6417 217 -508 295 C ATOM 379 CD ARG A 56 42.085 18.424 24.326 1.00 46.03 C ANISOU 379 CD ARG A 56 6290 5021 6179 171 -545 302 C ATOM 380 NE ARG A 56 43.410 18.669 23.773 1.00 46.53 N ANISOU 380 NE ARG A 56 6353 5054 6273 100 -515 416 N ATOM 381 CZ ARG A 56 44.418 19.159 24.485 1.00 47.72 C ANISOU 381 CZ ARG A 56 6493 5136 6503 43 -533 433 C ATOM 382 NH1 ARG A 56 45.604 19.358 23.929 1.00 45.78 N ANISOU 382 NH1 ARG A 56 6239 4871 6286 -25 -501 540 N ATOM 383 NH2 ARG A 56 44.227 19.445 25.763 1.00 42.12 N ANISOU 383 NH2 ARG A 56 5777 4384 5843 56 -582 340 N ATOM 384 N GLY A 57 41.262 13.252 21.127 1.00 39.83 N ANISOU 384 N GLY A 57 5413 4680 5042 220 -285 291 N ATOM 385 CA GLY A 57 41.926 12.254 20.313 1.00 35.76 C ANISOU 385 CA GLY A 57 4878 4240 4471 202 -221 328 C ATOM 386 C GLY A 57 42.441 11.084 21.139 1.00 30.70 C ANISOU 386 C GLY A 57 4195 3636 3836 169 -177 276 C ATOM 387 O GLY A 57 42.235 11.041 22.354 1.00 30.93 O ANISOU 387 O GLY A 57 4210 3635 3905 159 -194 214 O ATOM 388 N PRO A 58 43.124 10.136 20.482 1.00 34.11 N ANISOU 388 N PRO A 58 4606 4133 4222 156 -122 301 N ATOM 389 CA PRO A 58 43.654 8.941 21.153 1.00 30.32 C ANISOU 389 CA PRO A 58 4088 3686 3744 130 -83 256 C ATOM 390 C PRO A 58 44.859 9.266 22.033 1.00 29.41 C ANISOU 390 C PRO A 58 3960 3526 3691 74 -75 288 C ATOM 391 O PRO A 58 45.702 10.095 21.673 1.00 35.06 O ANISOU 391 O PRO A 58 4681 4209 4430 45 -73 368 O ATOM 392 CB PRO A 58 44.123 8.052 19.988 1.00 41.86 C ANISOU 392 CB PRO A 58 5537 5226 5140 141 -34 284 C ATOM 393 CG PRO A 58 43.587 8.675 18.750 1.00 40.03 C ANISOU 393 CG PRO A 58 5335 5013 4860 181 -50 328 C ATOM 394 CD PRO A 58 43.391 10.124 19.036 1.00 43.00 C ANISOU 394 CD PRO A 58 5743 5309 5286 174 -97 370 C ATOM 395 N ILE A 59 44.927 8.598 23.178 1.00 29.53 N ANISOU 395 N ILE A 59 3953 3537 3728 59 -70 227 N ATOM 396 CA ILE A 59 46.108 8.611 24.025 1.00 30.03 C ANISOU 396 CA ILE A 59 3996 3574 3840 13 -60 244 C ATOM 397 C ILE A 59 46.442 7.152 24.249 1.00 32.62 C ANISOU 397 C ILE A 59 4296 3957 4140 10 -18 206 C ATOM 398 O ILE A 59 45.564 6.352 24.564 1.00 30.69 O ANISOU 398 O ILE A 59 4050 3737 3873 33 -18 142 O ATOM 399 CB ILE A 59 45.826 9.244 25.396 1.00 36.50 C ANISOU 399 CB ILE A 59 4823 4333 4714 6 -106 198 C ATOM 400 CG1 ILE A 59 45.452 10.719 25.248 1.00 49.63 C ANISOU 400 CG1 ILE A 59 6516 5928 6414 14 -158 225 C ATOM 401 CG2 ILE A 59 47.042 9.129 26.309 1.00 40.49 C ANISOU 401 CG2 ILE A 59 5304 4819 5264 -37 -99 205 C ATOM 402 CD1 ILE A 59 45.263 11.425 26.593 1.00 44.63 C ANISOU 402 CD1 ILE A 59 5889 5233 5836 13 -210 173 C ATOM 403 N LYS A 60 47.712 6.814 24.095 1.00 29.78 N ANISOU 403 N LYS A 60 3911 3615 3787 -19 15 247 N ATOM 404 CA LYS A 60 48.142 5.444 24.271 1.00 24.11 C ANISOU 404 CA LYS A 60 3169 2944 3047 -17 49 214 C ATOM 405 C LYS A 60 49.044 5.332 25.494 1.00 31.15 C ANISOU 405 C LYS A 60 4040 3807 3987 -50 44 205 C ATOM 406 O LYS A 60 50.069 5.996 25.561 1.00 34.42 O ANISOU 406 O LYS A 60 4439 4201 4438 -82 43 253 O ATOM 407 CB LYS A 60 48.899 4.968 23.032 1.00 26.94 C ANISOU 407 CB LYS A 60 3509 3363 3364 -11 93 259 C ATOM 408 CG LYS A 60 49.093 3.446 23.017 1.00 40.58 C ANISOU 408 CG LYS A 60 5217 5139 5062 7 122 211 C ATOM 409 CD LYS A 60 49.397 2.904 21.630 1.00 45.15 C ANISOU 409 CD LYS A 60 5784 5789 5582 36 158 232 C ATOM 410 CE LYS A 60 50.863 3.092 21.286 1.00 57.87 C ANISOU 410 CE LYS A 60 7361 7429 7199 13 192 293 C ATOM 411 NZ LYS A 60 51.130 2.760 19.861 1.00 66.43 N ANISOU 411 NZ LYS A 60 8434 8592 8215 46 229 320 N ATOM 412 N PHE A 61 48.658 4.493 26.454 1.00 27.92 N ANISOU 412 N PHE A 61 3632 3400 3577 -42 40 145 N ATOM 413 CA PHE A 61 49.526 4.197 27.593 1.00 25.29 C ANISOU 413 CA PHE A 61 3281 3051 3277 -64 35 133 C ATOM 414 C PHE A 61 50.208 2.860 27.366 1.00 28.83 C ANISOU 414 C PHE A 61 3708 3543 3703 -58 71 126 C ATOM 415 O PHE A 61 49.549 1.820 27.299 1.00 29.00 O ANISOU 415 O PHE A 61 3738 3587 3695 -36 82 88 O ATOM 416 CB PHE A 61 48.724 4.130 28.890 1.00 26.98 C ANISOU 416 CB PHE A 61 3510 3241 3499 -57 7 76 C ATOM 417 CG PHE A 61 48.188 5.459 29.349 1.00 26.06 C ANISOU 417 CG PHE A 61 3412 3079 3412 -57 -36 70 C ATOM 418 CD1 PHE A 61 48.994 6.346 30.063 1.00 24.87 C ANISOU 418 CD1 PHE A 61 3255 2885 3311 -81 -67 82 C ATOM 419 CD2 PHE A 61 46.867 5.788 29.121 1.00 30.52 C ANISOU 419 CD2 PHE A 61 3996 3642 3957 -31 -50 42 C ATOM 420 CE1 PHE A 61 48.483 7.560 30.502 1.00 32.15 C ANISOU 420 CE1 PHE A 61 4195 3757 4263 -75 -114 67 C ATOM 421 CE2 PHE A 61 46.347 7.007 29.551 1.00 30.59 C ANISOU 421 CE2 PHE A 61 4022 3608 3993 -22 -95 28 C ATOM 422 CZ PHE A 61 47.165 7.887 30.251 1.00 32.04 C ANISOU 422 CZ PHE A 61 4203 3742 4227 -44 -128 40 C ATOM 423 N ASN A 62 51.524 2.887 27.227 1.00 28.86 N ANISOU 423 N ASN A 62 3682 3558 3726 -77 86 163 N ATOM 424 CA ASN A 62 52.280 1.662 27.082 1.00 30.66 C ANISOU 424 CA ASN A 62 3886 3825 3937 -65 114 152 C ATOM 425 C ASN A 62 52.602 1.143 28.480 1.00 28.96 C ANISOU 425 C ASN A 62 3670 3586 3747 -71 94 119 C ATOM 426 O ASN A 62 53.508 1.643 29.151 1.00 28.05 O ANISOU 426 O ASN A 62 3534 3453 3670 -93 77 133 O ATOM 427 CB ASN A 62 53.533 1.908 26.249 1.00 30.65 C ANISOU 427 CB ASN A 62 3846 3859 3940 -77 142 205 C ATOM 428 CG ASN A 62 53.210 2.457 24.870 1.00 34.33 C ANISOU 428 CG ASN A 62 4317 4355 4372 -70 163 247 C ATOM 429 OD1 ASN A 62 52.267 2.001 24.213 1.00 33.56 O ANISOU 429 OD1 ASN A 62 4242 4279 4229 -37 170 223 O ATOM 430 ND2 ASN A 62 53.992 3.438 24.421 1.00 33.53 N ANISOU 430 ND2 ASN A 62 4193 4255 4293 -101 174 313 N ATOM 431 N VAL A 63 51.817 0.164 28.923 1.00 30.47 N ANISOU 431 N VAL A 63 3882 3777 3917 -51 92 76 N ATOM 432 CA VAL A 63 51.882 -0.300 30.299 1.00 27.22 C ANISOU 432 CA VAL A 63 3480 3345 3519 -54 73 49 C ATOM 433 C VAL A 63 52.887 -1.444 30.450 1.00 25.72 C ANISOU 433 C VAL A 63 3272 3171 3330 -42 84 45 C ATOM 434 O VAL A 63 52.792 -2.464 29.794 1.00 28.74 O ANISOU 434 O VAL A 63 3655 3574 3691 -21 104 33 O ATOM 435 CB VAL A 63 50.491 -0.727 30.821 1.00 22.77 C ANISOU 435 CB VAL A 63 2947 2771 2935 -45 67 12 C ATOM 436 CG1 VAL A 63 50.584 -1.294 32.275 1.00 25.59 C ANISOU 436 CG1 VAL A 63 3314 3114 3295 -46 53 -6 C ATOM 437 CG2 VAL A 63 49.546 0.431 30.782 1.00 28.05 C ANISOU 437 CG2 VAL A 63 3628 3425 3604 -49 51 8 C ATOM 438 N TRP A 64 53.856 -1.252 31.336 1.00 28.68 N ANISOU 438 N TRP A 64 3630 3536 3731 -52 65 51 N ATOM 439 CA TRP A 64 54.916 -2.226 31.541 1.00 29.61 C ANISOU 439 CA TRP A 64 3728 3668 3854 -36 68 48 C ATOM 440 C TRP A 64 54.490 -3.136 32.690 1.00 28.40 C ANISOU 440 C TRP A 64 3606 3494 3690 -23 51 22 C ATOM 441 O TRP A 64 54.320 -2.681 33.819 1.00 32.41 O ANISOU 441 O TRP A 64 4128 3983 4203 -32 26 16 O ATOM 442 CB TRP A 64 56.237 -1.500 31.841 1.00 30.38 C ANISOU 442 CB TRP A 64 3784 3769 3988 -53 54 68 C ATOM 443 CG TRP A 64 56.883 -0.875 30.609 1.00 28.32 C ANISOU 443 CG TRP A 64 3483 3538 3737 -67 80 105 C ATOM 444 CD1 TRP A 64 56.286 -0.060 29.674 1.00 24.53 C ANISOU 444 CD1 TRP A 64 3010 3062 3249 -82 97 131 C ATOM 445 CD2 TRP A 64 58.248 -1.017 30.196 1.00 33.93 C ANISOU 445 CD2 TRP A 64 4139 4286 4466 -67 95 124 C ATOM 446 NE1 TRP A 64 57.199 0.283 28.693 1.00 30.12 N ANISOU 446 NE1 TRP A 64 3674 3807 3963 -93 125 172 N ATOM 447 CE2 TRP A 64 58.410 -0.283 28.998 1.00 33.02 C ANISOU 447 CE2 TRP A 64 3999 4199 4348 -86 127 166 C ATOM 448 CE3 TRP A 64 59.352 -1.697 30.723 1.00 31.88 C ANISOU 448 CE3 TRP A 64 3848 4043 4223 -51 85 109 C ATOM 449 CZ2 TRP A 64 59.630 -0.213 28.320 1.00 34.60 C ANISOU 449 CZ2 TRP A 64 4138 4448 4559 -93 154 196 C ATOM 450 CZ3 TRP A 64 60.560 -1.630 30.047 1.00 32.67 C ANISOU 450 CZ3 TRP A 64 3884 4190 4338 -54 108 131 C ATOM 451 CH2 TRP A 64 60.689 -0.901 28.859 1.00 32.05 C ANISOU 451 CH2 TRP A 64 3777 4145 4255 -77 146 175 C ATOM 452 N ASP A 65 54.241 -4.402 32.382 1.00 31.86 N ANISOU 452 N ASP A 65 4058 3936 4111 -1 65 8 N ATOM 453 CA ASP A 65 53.843 -5.388 33.390 1.00 25.97 C ANISOU 453 CA ASP A 65 3344 3167 3357 8 53 -5 C ATOM 454 C ASP A 65 54.978 -6.382 33.550 1.00 30.71 C ANISOU 454 C ASP A 65 3933 3769 3968 34 44 -6 C ATOM 455 O ASP A 65 55.543 -6.841 32.563 1.00 31.66 O ANISOU 455 O ASP A 65 4030 3908 4091 54 58 -12 O ATOM 456 CB ASP A 65 52.570 -6.121 32.955 1.00 27.76 C ANISOU 456 CB ASP A 65 3597 3383 3567 8 69 -20 C ATOM 457 CG ASP A 65 52.054 -7.056 34.022 1.00 30.38 C ANISOU 457 CG ASP A 65 3962 3688 3893 6 60 -22 C ATOM 458 OD1 ASP A 65 52.007 -6.635 35.205 1.00 31.55 O ANISOU 458 OD1 ASP A 65 4122 3833 4034 -3 45 -13 O ATOM 459 OD2 ASP A 65 51.721 -8.222 33.701 1.00 34.73 O ANISOU 459 OD2 ASP A 65 4528 4222 4447 15 65 -31 O ATOM 460 N THR A 66 55.325 -6.698 34.795 1.00 30.52 N ANISOU 460 N THR A 66 3924 3728 3945 41 18 -3 N ATOM 461 CA THR A 66 56.396 -7.638 35.064 1.00 30.44 C ANISOU 461 CA THR A 66 3907 3715 3946 72 2 -4 C ATOM 462 C THR A 66 55.998 -9.058 34.734 1.00 33.27 C ANISOU 462 C THR A 66 4293 4049 4300 93 7 -14 C ATOM 463 O THR A 66 54.841 -9.341 34.417 1.00 31.90 O ANISOU 463 O THR A 66 4144 3859 4116 78 23 -19 O ATOM 464 CB THR A 66 56.728 -7.666 36.549 1.00 28.23 C ANISOU 464 CB THR A 66 3645 3422 3661 78 -32 3 C ATOM 465 OG1 THR A 66 55.644 -8.285 37.258 1.00 33.91 O ANISOU 465 OG1 THR A 66 4413 4115 4356 71 -30 12 O ATOM 466 CG2 THR A 66 56.953 -6.263 37.084 1.00 31.36 C ANISOU 466 CG2 THR A 66 4021 3832 4062 56 -48 4 C ATOM 467 N ALA A 67 56.982 -9.944 34.841 1.00 29.68 N ANISOU 467 N ALA A 67 3831 3589 3858 130 -11 -20 N ATOM 468 CA ALA A 67 56.781 -11.380 34.736 1.00 32.67 C ANISOU 468 CA ALA A 67 4241 3930 4242 156 -20 -29 C ATOM 469 C ALA A 67 57.019 -12.043 36.101 1.00 36.26 C ANISOU 469 C ALA A 67 4732 4349 4695 168 -52 -8 C ATOM 470 O ALA A 67 57.516 -13.173 36.178 1.00 36.25 O ANISOU 470 O ALA A 67 4747 4319 4709 204 -75 -12 O ATOM 471 CB ALA A 67 57.709 -11.961 33.694 1.00 38.42 C ANISOU 471 CB ALA A 67 4936 4678 4984 199 -19 -57 C ATOM 472 N GLY A 68 56.691 -11.321 37.172 1.00 33.94 N ANISOU 472 N GLY A 68 4452 4061 4381 143 -58 14 N ATOM 473 CA GLY A 68 56.686 -11.900 38.508 1.00 31.81 C ANISOU 473 CA GLY A 68 4225 3766 4097 153 -84 41 C ATOM 474 C GLY A 68 57.933 -11.647 39.331 1.00 33.26 C ANISOU 474 C GLY A 68 4392 3968 4278 184 -121 42 C ATOM 475 O GLY A 68 57.964 -11.982 40.516 1.00 35.69 O ANISOU 475 O GLY A 68 4735 4264 4563 196 -146 66 O ATOM 476 N GLN A 69 58.954 -11.059 38.711 1.00 35.28 N ANISOU 476 N GLN A 69 4592 4257 4555 197 -126 19 N ATOM 477 CA GLN A 69 60.242 -10.840 39.369 1.00 32.67 C ANISOU 477 CA GLN A 69 4233 3948 4233 227 -165 12 C ATOM 478 C GLN A 69 60.134 -9.959 40.596 1.00 34.01 C ANISOU 478 C GLN A 69 4413 4131 4378 213 -188 20 C ATOM 479 O GLN A 69 61.023 -9.986 41.454 1.00 38.75 O ANISOU 479 O GLN A 69 5006 4742 4976 243 -230 17 O ATOM 480 CB GLN A 69 61.260 -10.229 38.393 1.00 36.83 C ANISOU 480 CB GLN A 69 4686 4516 4791 231 -156 -12 C ATOM 481 CG GLN A 69 61.383 -10.960 37.055 1.00 37.29 C ANISOU 481 CG GLN A 69 4726 4578 4865 250 -129 -28 C ATOM 482 CD GLN A 69 60.466 -10.380 35.975 1.00 40.12 C ANISOU 482 CD GLN A 69 5078 4947 5217 212 -83 -29 C ATOM 483 OE1 GLN A 69 59.376 -9.901 36.266 1.00 40.32 O ANISOU 483 OE1 GLN A 69 5136 4956 5226 175 -71 -15 O ATOM 484 NE2 GLN A 69 60.918 -10.424 34.729 1.00 41.87 N ANISOU 484 NE2 GLN A 69 5257 5203 5449 225 -58 -46 N ATOM 485 N GLU A 70 59.053 -9.182 40.713 1.00 31.08 N ANISOU 485 N GLU A 70 4058 3763 3988 173 -165 25 N ATOM 486 CA GLU A 70 58.901 -8.329 41.912 1.00 27.93 C ANISOU 486 CA GLU A 70 3670 3381 3562 167 -190 24 C ATOM 487 C GLU A 70 58.830 -9.145 43.208 1.00 37.94 C ANISOU 487 C GLU A 70 4989 4640 4788 196 -216 48 C ATOM 488 O GLU A 70 59.038 -8.621 44.311 1.00 36.83 O ANISOU 488 O GLU A 70 4854 4521 4617 210 -249 42 O ATOM 489 CB GLU A 70 57.667 -7.419 41.800 1.00 31.00 C ANISOU 489 CB GLU A 70 4069 3775 3936 127 -161 21 C ATOM 490 CG GLU A 70 56.318 -8.134 41.935 1.00 29.17 C ANISOU 490 CG GLU A 70 3884 3526 3671 112 -128 44 C ATOM 491 CD GLU A 70 55.770 -8.651 40.592 1.00 32.81 C ANISOU 491 CD GLU A 70 4341 3968 4157 94 -90 44 C ATOM 492 OE1 GLU A 70 56.522 -8.711 39.585 1.00 32.64 O ANISOU 492 OE1 GLU A 70 4286 3948 4170 103 -88 31 O ATOM 493 OE2 GLU A 70 54.573 -8.996 40.549 1.00 31.44 O ANISOU 493 OE2 GLU A 70 4194 3783 3967 73 -63 56 O ATOM 494 N LYS A 71 58.531 -10.434 43.079 1.00 37.54 N ANISOU 494 N LYS A 71 4976 4557 4732 208 -205 75 N ATOM 495 CA LYS A 71 58.447 -11.298 44.249 1.00 39.74 C ANISOU 495 CA LYS A 71 5307 4820 4970 234 -227 111 C ATOM 496 C LYS A 71 59.816 -11.509 44.896 1.00 38.87 C ANISOU 496 C LYS A 71 5187 4721 4862 287 -283 103 C ATOM 497 O LYS A 71 59.903 -11.878 46.058 1.00 42.06 O ANISOU 497 O LYS A 71 5630 5128 5222 314 -313 129 O ATOM 498 CB LYS A 71 57.803 -12.640 43.888 1.00 41.61 C ANISOU 498 CB LYS A 71 5587 5007 5215 228 -206 145 C ATOM 499 CG LYS A 71 56.338 -12.515 43.492 1.00 50.09 C ANISOU 499 CG LYS A 71 6675 6074 6282 177 -155 156 C ATOM 500 CD LYS A 71 55.682 -13.870 43.284 1.00 65.56 C ANISOU 500 CD LYS A 71 8677 7977 8255 166 -141 191 C ATOM 501 CE LYS A 71 56.164 -14.525 42.006 1.00 63.58 C ANISOU 501 CE LYS A 71 8407 7691 8060 181 -144 163 C ATOM 502 NZ LYS A 71 55.788 -13.719 40.820 1.00 52.59 N ANISOU 502 NZ LYS A 71 6970 6323 6687 155 -112 122 N ATOM 503 N PHE A 72 60.886 -11.233 44.157 1.00 34.58 N ANISOU 503 N PHE A 72 4586 4189 4364 301 -298 68 N ATOM 504 CA PHE A 72 62.218 -11.590 44.623 1.00 36.26 C ANISOU 504 CA PHE A 72 4779 4410 4586 355 -352 56 C ATOM 505 C PHE A 72 63.095 -10.383 44.943 1.00 39.74 C ANISOU 505 C PHE A 72 5162 4896 5041 356 -385 18 C ATOM 506 O PHE A 72 64.262 -10.516 45.283 1.00 39.97 O ANISOU 506 O PHE A 72 5161 4941 5085 398 -432 -1 O ATOM 507 CB PHE A 72 62.864 -12.532 43.606 1.00 36.38 C ANISOU 507 CB PHE A 72 4773 4403 4645 383 -350 46 C ATOM 508 CG PHE A 72 61.966 -13.678 43.222 1.00 35.08 C ANISOU 508 CG PHE A 72 4666 4186 4479 377 -323 76 C ATOM 509 CD1 PHE A 72 61.772 -14.738 44.094 1.00 39.15 C ANISOU 509 CD1 PHE A 72 5247 4660 4969 405 -349 118 C ATOM 510 CD2 PHE A 72 61.287 -13.675 42.011 1.00 41.08 C ANISOU 510 CD2 PHE A 72 5412 4933 5262 343 -275 65 C ATOM 511 CE1 PHE A 72 60.928 -15.786 43.755 1.00 40.54 C ANISOU 511 CE1 PHE A 72 5473 4777 5154 392 -328 148 C ATOM 512 CE2 PHE A 72 60.441 -14.717 41.662 1.00 37.03 C ANISOU 512 CE2 PHE A 72 4947 4368 4755 335 -257 86 C ATOM 513 CZ PHE A 72 60.256 -15.771 42.540 1.00 36.25 C ANISOU 513 CZ PHE A 72 4912 4222 4641 356 -283 128 C ATOM 514 N GLY A 73 62.510 -9.198 44.858 1.00 41.03 N ANISOU 514 N GLY A 73 5309 5076 5204 311 -365 4 N ATOM 515 CA GLY A 73 63.237 -7.983 45.159 1.00 40.78 C ANISOU 515 CA GLY A 73 5224 5076 5195 304 -399 -34 C ATOM 516 C GLY A 73 62.845 -6.871 44.216 1.00 42.69 C ANISOU 516 C GLY A 73 5426 5320 5473 248 -362 -47 C ATOM 517 O GLY A 73 61.884 -7.005 43.453 1.00 36.93 O ANISOU 517 O GLY A 73 4718 4574 4739 220 -312 -29 O ATOM 518 N GLY A 74 63.599 -5.777 44.259 1.00 36.69 N ANISOU 518 N GLY A 74 4611 4578 4754 233 -392 -78 N ATOM 519 CA GLY A 74 63.298 -4.612 43.446 1.00 39.44 C ANISOU 519 CA GLY A 74 4923 4922 5140 180 -366 -86 C ATOM 520 C GLY A 74 63.523 -4.837 41.962 1.00 42.05 C ANISOU 520 C GLY A 74 5215 5254 5509 159 -316 -70 C ATOM 521 O GLY A 74 64.322 -5.678 41.545 1.00 38.26 O ANISOU 521 O GLY A 74 4708 4786 5042 187 -313 -68 O ATOM 522 N LEU A 75 62.812 -4.067 41.153 1.00 39.74 N ANISOU 522 N LEU A 75 4917 4952 5229 114 -278 -60 N ATOM 523 CA LEU A 75 62.946 -4.169 39.713 1.00 34.65 C ANISOU 523 CA LEU A 75 4239 4317 4611 95 -229 -43 C ATOM 524 C LEU A 75 64.204 -3.446 39.222 1.00 41.23 C ANISOU 524 C LEU A 75 4988 5174 5502 74 -238 -47 C ATOM 525 O LEU A 75 64.709 -2.526 39.881 1.00 40.54 O ANISOU 525 O LEU A 75 4873 5083 5447 57 -280 -64 O ATOM 526 CB LEU A 75 61.685 -3.624 39.051 1.00 33.45 C ANISOU 526 CB LEU A 75 4116 4148 4445 60 -189 -29 C ATOM 527 CG LEU A 75 60.424 -4.368 39.505 1.00 39.80 C ANISOU 527 CG LEU A 75 4991 4934 5196 75 -176 -24 C ATOM 528 CD1 LEU A 75 59.177 -3.762 38.889 1.00 35.42 C ANISOU 528 CD1 LEU A 75 4458 4368 4632 43 -142 -17 C ATOM 529 CD2 LEU A 75 60.526 -5.852 39.156 1.00 36.94 C ANISOU 529 CD2 LEU A 75 4646 4570 4818 108 -159 -15 C ATOM 530 N ARG A 76 64.716 -3.876 38.072 1.00 34.16 N ANISOU 530 N ARG A 76 4051 4307 4621 77 -198 -35 N ATOM 531 CA ARG A 76 65.948 -3.310 37.527 1.00 36.23 C ANISOU 531 CA ARG A 76 4225 4603 4936 56 -196 -32 C ATOM 532 C ARG A 76 65.714 -1.917 36.958 1.00 42.07 C ANISOU 532 C ARG A 76 4940 5333 5711 -8 -178 -8 C ATOM 533 O ARG A 76 64.590 -1.575 36.593 1.00 39.34 O ANISOU 533 O ARG A 76 4641 4962 5342 -28 -153 8 O ATOM 534 CB ARG A 76 66.536 -4.230 36.458 1.00 35.47 C ANISOU 534 CB ARG A 76 4091 4552 4835 86 -155 -27 C ATOM 535 CG ARG A 76 66.942 -5.604 36.996 1.00 41.58 C ANISOU 535 CG ARG A 76 4884 5330 5586 154 -182 -53 C ATOM 536 CD ARG A 76 67.349 -6.533 35.872 1.00 52.84 C ANISOU 536 CD ARG A 76 6280 6795 7004 190 -142 -57 C ATOM 537 NE ARG A 76 68.440 -5.981 35.073 1.00 61.21 N ANISOU 537 NE ARG A 76 7241 7914 8100 172 -118 -52 N ATOM 538 CZ ARG A 76 68.698 -6.336 33.817 1.00 66.87 C ANISOU 538 CZ ARG A 76 7919 8682 8807 186 -66 -48 C ATOM 539 NH1 ARG A 76 67.938 -7.241 33.210 1.00 64.17 N ANISOU 539 NH1 ARG A 76 7629 8330 8422 221 -41 -55 N ATOM 540 NH2 ARG A 76 69.714 -5.785 33.164 1.00 66.02 N ANISOU 540 NH2 ARG A 76 7717 8638 8731 165 -40 -37 N ATOM 541 N ASP A 77 66.778 -1.120 36.885 1.00 39.42 N ANISOU 541 N ASP A 77 4528 5014 5435 -41 -193 -5 N ATOM 542 CA ASP A 77 66.678 0.256 36.392 1.00 38.07 C ANISOU 542 CA ASP A 77 4331 4823 5310 -107 -184 24 C ATOM 543 C ASP A 77 65.973 0.340 35.036 1.00 40.41 C ANISOU 543 C ASP A 77 4642 5131 5582 -127 -116 68 C ATOM 544 O ASP A 77 65.183 1.256 34.795 1.00 38.08 O ANISOU 544 O ASP A 77 4377 4799 5294 -163 -112 89 O ATOM 545 CB ASP A 77 68.065 0.893 36.292 1.00 44.19 C ANISOU 545 CB ASP A 77 5007 5623 6158 -144 -199 30 C ATOM 546 CG ASP A 77 68.616 1.310 37.645 1.00 52.29 C ANISOU 546 CG ASP A 77 6019 6623 7224 -142 -279 -14 C ATOM 547 OD1 ASP A 77 67.954 1.040 38.670 1.00 47.82 O ANISOU 547 OD1 ASP A 77 5522 6029 6618 -106 -319 -48 O ATOM 548 OD2 ASP A 77 69.709 1.912 37.683 1.00 60.92 O ANISOU 548 OD2 ASP A 77 7030 7729 8387 -177 -302 -16 O ATOM 549 N GLY A 78 66.266 -0.612 34.151 1.00 36.73 N ANISOU 549 N GLY A 78 4155 4716 5085 -96 -69 77 N ATOM 550 CA GLY A 78 65.714 -0.593 32.809 1.00 39.06 C ANISOU 550 CA GLY A 78 4457 5034 5349 -105 -7 113 C ATOM 551 C GLY A 78 64.198 -0.670 32.783 1.00 40.07 C ANISOU 551 C GLY A 78 4673 5122 5432 -97 -1 111 C ATOM 552 O GLY A 78 63.543 -0.218 31.831 1.00 38.23 O ANISOU 552 O GLY A 78 4453 4890 5181 -117 36 143 O ATOM 553 N TYR A 79 63.629 -1.254 33.828 1.00 37.30 N ANISOU 553 N TYR A 79 4378 4737 5058 -66 -37 75 N ATOM 554 CA TYR A 79 62.179 -1.345 33.917 1.00 33.94 C ANISOU 554 CA TYR A 79 4027 4277 4592 -61 -32 70 C ATOM 555 C TYR A 79 61.580 0.058 34.077 1.00 31.23 C ANISOU 555 C TYR A 79 3699 3894 4273 -105 -49 84 C ATOM 556 O TYR A 79 60.567 0.405 33.455 1.00 31.92 O ANISOU 556 O TYR A 79 3819 3968 4339 -116 -26 99 O ATOM 557 CB TYR A 79 61.754 -2.255 35.077 1.00 34.68 C ANISOU 557 CB TYR A 79 4172 4349 4656 -22 -64 36 C ATOM 558 CG TYR A 79 60.269 -2.239 35.275 1.00 36.73 C ANISOU 558 CG TYR A 79 4499 4578 4880 -24 -59 31 C ATOM 559 CD1 TYR A 79 59.441 -3.094 34.540 1.00 36.73 C ANISOU 559 CD1 TYR A 79 4530 4583 4843 -7 -23 33 C ATOM 560 CD2 TYR A 79 59.678 -1.340 36.161 1.00 34.13 C ANISOU 560 CD2 TYR A 79 4196 4217 4556 -42 -91 21 C ATOM 561 CE1 TYR A 79 58.067 -3.052 34.690 1.00 34.41 C ANISOU 561 CE1 TYR A 79 4288 4266 4522 -12 -17 27 C ATOM 562 CE2 TYR A 79 58.305 -1.300 36.321 1.00 38.20 C ANISOU 562 CE2 TYR A 79 4764 4713 5037 -42 -83 14 C ATOM 563 CZ TYR A 79 57.507 -2.147 35.578 1.00 40.28 C ANISOU 563 CZ TYR A 79 5053 4985 5268 -30 -45 20 C ATOM 564 OH TYR A 79 56.145 -2.097 35.720 1.00 40.18 O ANISOU 564 OH TYR A 79 5083 4958 5227 -32 -37 11 O ATOM 565 N TYR A 80 62.231 0.865 34.902 1.00 32.87 N ANISOU 565 N TYR A 80 3880 4081 4529 -128 -94 75 N ATOM 566 CA TYR A 80 61.718 2.174 35.288 1.00 36.08 C ANISOU 566 CA TYR A 80 4304 4438 4966 -163 -126 75 C ATOM 567 C TYR A 80 62.045 3.269 34.286 1.00 34.19 C ANISOU 567 C TYR A 80 4025 4191 4774 -215 -107 123 C ATOM 568 O TYR A 80 61.361 4.294 34.232 1.00 40.13 O ANISOU 568 O TYR A 80 4804 4899 5545 -241 -123 133 O ATOM 569 CB TYR A 80 62.288 2.557 36.657 1.00 36.63 C ANISOU 569 CB TYR A 80 4362 4486 5068 -162 -192 36 C ATOM 570 CG TYR A 80 61.694 1.785 37.813 1.00 36.21 C ANISOU 570 CG TYR A 80 4363 4431 4962 -114 -218 -5 C ATOM 571 CD1 TYR A 80 60.366 1.960 38.178 1.00 36.10 C ANISOU 571 CD1 TYR A 80 4411 4395 4909 -104 -220 -20 C ATOM 572 CD2 TYR A 80 62.466 0.893 38.555 1.00 37.54 C ANISOU 572 CD2 TYR A 80 4519 4624 5119 -79 -240 -27 C ATOM 573 CE1 TYR A 80 59.817 1.276 39.244 1.00 32.42 C ANISOU 573 CE1 TYR A 80 3990 3935 4391 -65 -237 -49 C ATOM 574 CE2 TYR A 80 61.919 0.196 39.620 1.00 36.45 C ANISOU 574 CE2 TYR A 80 4434 4486 4928 -37 -261 -53 C ATOM 575 CZ TYR A 80 60.596 0.398 39.960 1.00 31.95 C ANISOU 575 CZ TYR A 80 3923 3898 4318 -33 -257 -61 C ATOM 576 OH TYR A 80 60.052 -0.294 41.009 1.00 35.49 O ANISOU 576 OH TYR A 80 4419 4353 4711 4 -271 -79 O ATOM 577 N ILE A 81 63.090 3.056 33.494 1.00 35.13 N ANISOU 577 N ILE A 81 4080 4355 4911 -229 -73 155 N ATOM 578 CA ILE A 81 63.690 4.141 32.725 1.00 36.91 C ANISOU 578 CA ILE A 81 4254 4576 5192 -287 -59 208 C ATOM 579 C ILE A 81 62.745 4.716 31.673 1.00 40.40 C ANISOU 579 C ILE A 81 4733 5005 5613 -305 -24 255 C ATOM 580 O ILE A 81 62.102 3.978 30.916 1.00 37.85 O ANISOU 580 O ILE A 81 4439 4717 5226 -271 20 261 O ATOM 581 CB ILE A 81 65.028 3.725 32.080 1.00 45.19 C ANISOU 581 CB ILE A 81 5219 5693 6259 -296 -22 234 C ATOM 582 CG1 ILE A 81 65.774 4.951 31.559 1.00 54.56 C ANISOU 582 CG1 ILE A 81 6343 6869 7519 -368 -16 292 C ATOM 583 CG2 ILE A 81 64.803 2.758 30.968 1.00 50.27 C ANISOU 583 CG2 ILE A 81 5866 6399 6834 -259 44 251 C ATOM 584 CD1 ILE A 81 66.134 5.943 32.641 1.00 60.98 C ANISOU 584 CD1 ILE A 81 7142 7615 8413 -408 -89 269 C ATOM 585 N GLN A 82 62.664 6.045 31.649 1.00 37.60 N ANISOU 585 N GLN A 82 4377 4595 5315 -355 -50 285 N ATOM 586 CA GLN A 82 61.797 6.759 30.717 1.00 33.98 C ANISOU 586 CA GLN A 82 3955 4113 4843 -372 -27 333 C ATOM 587 C GLN A 82 60.317 6.608 31.047 1.00 31.35 C ANISOU 587 C GLN A 82 3702 3749 4459 -331 -45 293 C ATOM 588 O GLN A 82 59.462 6.986 30.240 1.00 38.10 O ANISOU 588 O GLN A 82 4592 4595 5289 -329 -26 324 O ATOM 589 CB GLN A 82 62.059 6.336 29.269 1.00 40.07 C ANISOU 589 CB GLN A 82 4698 4955 5570 -371 47 392 C ATOM 590 CG GLN A 82 63.493 6.536 28.823 1.00 56.32 C ANISOU 590 CG GLN A 82 6668 7056 7674 -414 75 440 C ATOM 591 CD GLN A 82 63.900 7.990 28.834 1.00 67.71 C ANISOU 591 CD GLN A 82 8086 8437 9205 -489 47 494 C ATOM 592 OE1 GLN A 82 64.830 8.383 29.539 1.00 72.99 O ANISOU 592 OE1 GLN A 82 8702 9083 9948 -525 11 482 O ATOM 593 NE2 GLN A 82 63.196 8.804 28.058 1.00 72.28 N ANISOU 593 NE2 GLN A 82 8702 8983 9778 -510 59 551 N ATOM 594 N ALA A 83 59.996 6.080 32.224 1.00 32.45 N ANISOU 594 N ALA A 83 3869 3878 4584 -296 -81 226 N ATOM 595 CA ALA A 83 58.596 6.066 32.639 1.00 32.96 C ANISOU 595 CA ALA A 83 4001 3916 4608 -264 -99 188 C ATOM 596 C ALA A 83 58.122 7.504 32.684 1.00 38.33 C ANISOU 596 C ALA A 83 4701 4528 5336 -291 -139 200 C ATOM 597 O ALA A 83 58.864 8.397 33.100 1.00 33.46 O ANISOU 597 O ALA A 83 4056 3868 4790 -328 -180 205 O ATOM 598 CB ALA A 83 58.424 5.422 33.986 1.00 32.07 C ANISOU 598 CB ALA A 83 3908 3803 4474 -229 -132 124 C ATOM 599 N GLN A 84 56.889 7.726 32.251 1.00 32.40 N ANISOU 599 N GLN A 84 3998 3762 4549 -272 -132 200 N ATOM 600 CA GLN A 84 56.328 9.065 32.266 1.00 33.45 C ANISOU 600 CA GLN A 84 4157 3827 4725 -288 -175 207 C ATOM 601 C GLN A 84 55.186 9.138 33.258 1.00 31.65 C ANISOU 601 C GLN A 84 3976 3577 4471 -247 -215 136 C ATOM 602 O GLN A 84 54.726 10.214 33.615 1.00 34.00 O ANISOU 602 O GLN A 84 4296 3815 4806 -248 -266 117 O ATOM 603 CB GLN A 84 55.904 9.468 30.861 1.00 35.61 C ANISOU 603 CB GLN A 84 4444 4102 4984 -299 -140 273 C ATOM 604 CG GLN A 84 57.095 9.505 29.910 1.00 36.74 C ANISOU 604 CG GLN A 84 4534 4274 5150 -343 -98 349 C ATOM 605 CD GLN A 84 56.688 9.449 28.469 1.00 42.28 C ANISOU 605 CD GLN A 84 5247 5012 5804 -338 -46 411 C ATOM 606 OE1 GLN A 84 56.309 8.395 27.968 1.00 36.60 O ANISOU 606 OE1 GLN A 84 4536 4357 5014 -300 -3 397 O ATOM 607 NE2 GLN A 84 56.768 10.589 27.781 1.00 42.77 N ANISOU 607 NE2 GLN A 84 5313 5031 5906 -375 -54 480 N ATOM 608 N CYS A 85 54.769 7.974 33.746 1.00 28.93 N ANISOU 608 N CYS A 85 3644 3283 4065 -210 -193 96 N ATOM 609 CA CYS A 85 53.721 7.914 34.750 1.00 28.57 C ANISOU 609 CA CYS A 85 3635 3233 3987 -171 -221 31 C ATOM 610 C CYS A 85 53.709 6.506 35.322 1.00 32.40 C ANISOU 610 C CYS A 85 4121 3774 4417 -145 -192 6 C ATOM 611 O CYS A 85 54.429 5.635 34.839 1.00 27.94 O ANISOU 611 O CYS A 85 3532 3243 3841 -153 -155 34 O ATOM 612 CB CYS A 85 52.347 8.274 34.155 1.00 31.77 C ANISOU 612 CB CYS A 85 4076 3630 4364 -150 -214 28 C ATOM 613 SG CYS A 85 51.766 7.173 32.821 1.00 31.73 S ANISOU 613 SG CYS A 85 4076 3682 4297 -138 -143 63 S ATOM 614 N ALA A 86 52.901 6.285 36.350 1.00 26.81 N ANISOU 614 N ALA A 86 3439 3076 3673 -113 -209 -47 N ATOM 615 CA ALA A 86 52.915 4.992 37.035 1.00 29.01 C ANISOU 615 CA ALA A 86 3722 3399 3901 -92 -187 -64 C ATOM 616 C ALA A 86 51.634 4.763 37.803 1.00 29.89 C ANISOU 616 C ALA A 86 3865 3529 3962 -60 -188 -106 C ATOM 617 O ALA A 86 50.964 5.711 38.206 1.00 28.94 O ANISOU 617 O ALA A 86 3758 3390 3848 -47 -221 -139 O ATOM 618 CB ALA A 86 54.127 4.907 38.013 1.00 30.80 C ANISOU 618 CB ALA A 86 3927 3625 4150 -93 -221 -78 C ATOM 619 N ILE A 87 51.325 3.489 38.021 1.00 27.65 N ANISOU 619 N ILE A 87 3591 3285 3631 -48 -152 -104 N ATOM 620 CA ILE A 87 50.285 3.066 38.932 1.00 25.37 C ANISOU 620 CA ILE A 87 3324 3024 3290 -24 -145 -135 C ATOM 621 C ILE A 87 50.969 2.171 39.947 1.00 28.48 C ANISOU 621 C ILE A 87 3721 3440 3659 -13 -149 -135 C ATOM 622 O ILE A 87 51.742 1.299 39.574 1.00 30.53 O ANISOU 622 O ILE A 87 3972 3703 3925 -22 -130 -105 O ATOM 623 CB ILE A 87 49.192 2.246 38.193 1.00 25.81 C ANISOU 623 CB ILE A 87 3389 3102 3314 -25 -97 -124 C ATOM 624 CG1 ILE A 87 48.367 3.180 37.317 1.00 26.34 C ANISOU 624 CG1 ILE A 87 3457 3153 3397 -25 -101 -131 C ATOM 625 CG2 ILE A 87 48.280 1.560 39.202 1.00 26.54 C ANISOU 625 CG2 ILE A 87 3497 3231 3355 -9 -81 -144 C ATOM 626 CD1 ILE A 87 47.541 2.405 36.222 1.00 29.15 C ANISOU 626 CD1 ILE A 87 3814 3527 3734 -30 -57 -116 C ATOM 627 N ILE A 88 50.727 2.431 41.228 1.00 26.73 N ANISOU 627 N ILE A 88 3512 3238 3408 11 -176 -170 N ATOM 628 CA ILE A 88 51.212 1.569 42.289 1.00 28.55 C ANISOU 628 CA ILE A 88 3753 3496 3601 28 -180 -167 C ATOM 629 C ILE A 88 50.017 0.834 42.857 1.00 33.79 C ANISOU 629 C ILE A 88 4439 4200 4201 40 -145 -167 C ATOM 630 O ILE A 88 49.058 1.451 43.317 1.00 30.15 O ANISOU 630 O ILE A 88 3983 3760 3713 56 -149 -200 O ATOM 631 CB ILE A 88 51.880 2.365 43.400 1.00 26.99 C ANISOU 631 CB ILE A 88 3551 3298 3406 50 -239 -205 C ATOM 632 CG1 ILE A 88 53.156 3.028 42.890 1.00 30.65 C ANISOU 632 CG1 ILE A 88 3985 3720 3941 29 -275 -201 C ATOM 633 CG2 ILE A 88 52.222 1.446 44.557 1.00 31.37 C ANISOU 633 CG2 ILE A 88 4123 3890 3907 76 -243 -201 C ATOM 634 CD1 ILE A 88 53.946 3.747 44.026 1.00 30.55 C ANISOU 634 CD1 ILE A 88 3963 3703 3940 50 -343 -246 C ATOM 635 N MET A 89 50.065 -0.493 42.803 1.00 28.55 N ANISOU 635 N MET A 89 3786 3546 3516 33 -110 -129 N ATOM 636 CA MET A 89 48.918 -1.283 43.186 1.00 27.63 C ANISOU 636 CA MET A 89 3686 3462 3351 32 -70 -117 C ATOM 637 C MET A 89 49.163 -1.984 44.520 1.00 33.29 C ANISOU 637 C MET A 89 4425 4211 4014 52 -75 -102 C ATOM 638 O MET A 89 50.279 -2.416 44.818 1.00 29.96 O ANISOU 638 O MET A 89 4009 3776 3599 62 -97 -86 O ATOM 639 CB MET A 89 48.601 -2.313 42.090 1.00 29.91 C ANISOU 639 CB MET A 89 3974 3732 3659 5 -28 -84 C ATOM 640 CG MET A 89 47.239 -2.933 42.246 1.00 31.18 C ANISOU 640 CG MET A 89 4142 3919 3787 -7 13 -76 C ATOM 641 SD MET A 89 46.651 -3.787 40.776 1.00 42.26 S ANISOU 641 SD MET A 89 5537 5295 5224 -38 50 -60 S ATOM 642 CE MET A 89 46.697 -2.488 39.555 1.00 29.55 C ANISOU 642 CE MET A 89 3905 3669 3653 -34 32 -89 C ATOM 643 N PHE A 90 48.128 -2.077 45.339 1.00 35.61 N ANISOU 643 N PHE A 90 4729 4551 4251 61 -53 -107 N ATOM 644 CA PHE A 90 48.171 -2.991 46.475 1.00 34.29 C ANISOU 644 CA PHE A 90 4587 4418 4024 74 -42 -74 C ATOM 645 C PHE A 90 46.867 -3.769 46.511 1.00 34.10 C ANISOU 645 C PHE A 90 4567 4421 3969 49 15 -44 C ATOM 646 O PHE A 90 45.960 -3.507 45.730 1.00 31.82 O ANISOU 646 O PHE A 90 4258 4130 3703 29 40 -60 O ATOM 647 CB PHE A 90 48.481 -2.276 47.819 1.00 25.11 C ANISOU 647 CB PHE A 90 3432 3301 2808 118 -82 -108 C ATOM 648 CG PHE A 90 47.394 -1.364 48.288 1.00 28.00 C ANISOU 648 CG PHE A 90 3786 3717 3134 137 -77 -156 C ATOM 649 CD1 PHE A 90 47.297 -0.071 47.794 1.00 28.45 C ANISOU 649 CD1 PHE A 90 3823 3753 3233 145 -109 -214 C ATOM 650 CD2 PHE A 90 46.454 -1.803 49.210 1.00 34.91 C ANISOU 650 CD2 PHE A 90 4671 4661 3932 147 -39 -141 C ATOM 651 CE1 PHE A 90 46.283 0.784 48.227 1.00 26.19 C ANISOU 651 CE1 PHE A 90 3526 3512 2913 171 -110 -266 C ATOM 652 CE2 PHE A 90 45.432 -0.967 49.644 1.00 29.93 C ANISOU 652 CE2 PHE A 90 4023 4087 3261 170 -32 -191 C ATOM 653 CZ PHE A 90 45.347 0.337 49.143 1.00 34.02 C ANISOU 653 CZ PHE A 90 4522 4581 3824 186 -71 -258 C ATOM 654 N ASP A 91 46.795 -4.751 47.399 1.00 33.50 N ANISOU 654 N ASP A 91 4515 4371 3843 50 36 3 N ATOM 655 CA ASP A 91 45.643 -5.632 47.513 1.00 33.42 C ANISOU 655 CA ASP A 91 4507 4383 3809 17 92 45 C ATOM 656 C ASP A 91 44.947 -5.298 48.835 1.00 31.77 C ANISOU 656 C ASP A 91 4299 4259 3513 41 108 40 C ATOM 657 O ASP A 91 45.553 -5.364 49.888 1.00 36.92 O ANISOU 657 O ASP A 91 4975 4940 4111 75 87 53 O ATOM 658 CB ASP A 91 46.150 -7.077 47.488 1.00 32.00 C ANISOU 658 CB ASP A 91 4357 4159 3642 -3 102 113 C ATOM 659 CG ASP A 91 45.086 -8.103 47.848 1.00 36.89 C ANISOU 659 CG ASP A 91 4985 4797 4236 -41 156 170 C ATOM 660 OD1 ASP A 91 43.952 -7.729 48.208 1.00 42.91 O ANISOU 660 OD1 ASP A 91 5724 5619 4961 -51 192 159 O ATOM 661 OD2 ASP A 91 45.403 -9.307 47.769 1.00 44.48 O ANISOU 661 OD2 ASP A 91 5972 5710 5217 -61 162 227 O ATOM 662 N VAL A 92 43.688 -4.889 48.762 1.00 34.74 N ANISOU 662 N VAL A 92 4647 4680 3873 30 143 16 N ATOM 663 CA VAL A 92 42.963 -4.444 49.945 1.00 36.80 C ANISOU 663 CA VAL A 92 4899 5034 4048 59 161 -1 C ATOM 664 C VAL A 92 42.648 -5.601 50.897 1.00 38.82 C ANISOU 664 C VAL A 92 5175 5333 4240 42 207 79 C ATOM 665 O VAL A 92 42.101 -5.394 51.976 1.00 42.81 O ANISOU 665 O VAL A 92 5677 5929 4661 67 230 79 O ATOM 666 CB VAL A 92 41.676 -3.682 49.567 1.00 39.04 C ANISOU 666 CB VAL A 92 5138 5359 4334 56 186 -53 C ATOM 667 CG1 VAL A 92 42.004 -2.589 48.570 1.00 28.86 C ANISOU 667 CG1 VAL A 92 3836 4016 3112 71 138 -119 C ATOM 668 CG2 VAL A 92 40.624 -4.636 48.992 1.00 36.79 C ANISOU 668 CG2 VAL A 92 4832 5071 4074 -3 247 -8 C ATOM 669 N THR A 93 43.014 -6.813 50.494 1.00 41.14 N ANISOU 669 N THR A 93 5493 5564 4573 2 220 147 N ATOM 670 CA THR A 93 42.867 -7.972 51.371 1.00 39.99 C ANISOU 670 CA THR A 93 5377 5441 4377 -17 256 235 C ATOM 671 C THR A 93 44.194 -8.342 52.053 1.00 41.84 C ANISOU 671 C THR A 93 5660 5653 4584 21 210 267 C ATOM 672 O THR A 93 44.219 -9.183 52.951 1.00 46.50 O ANISOU 672 O THR A 93 6283 6269 5118 19 230 341 O ATOM 673 CB THR A 93 42.279 -9.219 50.637 1.00 35.78 C ANISOU 673 CB THR A 93 4841 4849 3904 -88 298 298 C ATOM 674 OG1 THR A 93 43.230 -9.740 49.701 1.00 43.91 O ANISOU 674 OG1 THR A 93 5893 5778 5013 -97 260 303 O ATOM 675 CG2 THR A 93 40.992 -8.876 49.911 1.00 40.29 C ANISOU 675 CG2 THR A 93 5359 5442 4508 -125 337 261 C ATOM 676 N SER A 94 45.291 -7.711 51.639 1.00 37.33 N ANISOU 676 N SER A 94 5092 5040 4053 55 149 214 N ATOM 677 CA SER A 94 46.603 -8.012 52.230 1.00 38.79 C ANISOU 677 CA SER A 94 5314 5205 4218 95 99 234 C ATOM 678 C SER A 94 47.311 -6.773 52.768 1.00 44.90 C ANISOU 678 C SER A 94 6081 6017 4962 155 41 159 C ATOM 679 O SER A 94 47.923 -6.013 52.016 1.00 36.86 O ANISOU 679 O SER A 94 5041 4955 4009 161 1 100 O ATOM 680 CB SER A 94 47.504 -8.727 51.224 1.00 45.19 C ANISOU 680 CB SER A 94 6136 5916 5116 76 74 253 C ATOM 681 OG SER A 94 48.737 -9.094 51.824 1.00 45.00 O ANISOU 681 OG SER A 94 6145 5877 5074 117 26 274 O ATOM 682 N ARG A 95 47.246 -6.585 54.078 1.00 42.68 N ANISOU 682 N ARG A 95 5817 5817 4584 198 36 163 N ATOM 683 CA ARG A 95 47.775 -5.379 54.693 1.00 35.93 C ANISOU 683 CA ARG A 95 4953 5004 3695 259 -22 81 C ATOM 684 C ARG A 95 49.246 -5.157 54.385 1.00 39.55 C ANISOU 684 C ARG A 95 5415 5400 4213 281 -95 52 C ATOM 685 O ARG A 95 49.693 -4.016 54.261 1.00 39.42 O ANISOU 685 O ARG A 95 5375 5378 4226 306 -146 -27 O ATOM 686 CB ARG A 95 47.533 -5.400 56.203 1.00 47.28 C ANISOU 686 CB ARG A 95 6413 6545 5006 309 -18 96 C ATOM 687 CG ARG A 95 46.052 -5.365 56.553 1.00 53.41 C ANISOU 687 CG ARG A 95 7171 7404 5720 293 54 109 C ATOM 688 CD ARG A 95 45.805 -5.411 58.049 1.00 59.69 C ANISOU 688 CD ARG A 95 7987 8316 6378 345 66 128 C ATOM 689 NE ARG A 95 44.374 -5.398 58.342 1.00 63.17 N ANISOU 689 NE ARG A 95 8400 8843 6759 327 142 142 N ATOM 690 CZ ARG A 95 43.837 -5.796 59.489 1.00 65.06 C ANISOU 690 CZ ARG A 95 8653 9190 6879 348 187 194 C ATOM 691 NH1 ARG A 95 44.612 -6.244 60.470 1.00 71.24 N ANISOU 691 NH1 ARG A 95 9482 10003 7582 392 159 239 N ATOM 692 NH2 ARG A 95 42.523 -5.747 59.655 1.00 62.72 N ANISOU 692 NH2 ARG A 95 8319 8975 6537 327 260 203 N ATOM 693 N VAL A 96 50.001 -6.243 54.261 1.00 39.98 N ANISOU 693 N VAL A 96 5498 5406 4289 272 -102 115 N ATOM 694 CA VAL A 96 51.426 -6.128 53.974 1.00 36.17 C ANISOU 694 CA VAL A 96 5011 4870 3861 294 -167 89 C ATOM 695 C VAL A 96 51.682 -5.492 52.607 1.00 37.45 C ANISOU 695 C VAL A 96 5133 4967 4130 260 -177 42 C ATOM 696 O VAL A 96 52.700 -4.835 52.405 1.00 36.88 O ANISOU 696 O VAL A 96 5039 4871 4103 279 -233 -6 O ATOM 697 CB VAL A 96 52.150 -7.487 54.072 1.00 40.03 C ANISOU 697 CB VAL A 96 5538 5319 4354 296 -173 165 C ATOM 698 CG1 VAL A 96 51.766 -8.392 52.907 1.00 43.61 C ANISOU 698 CG1 VAL A 96 5990 5702 4880 238 -127 212 C ATOM 699 CG2 VAL A 96 53.655 -7.280 54.121 1.00 45.23 C ANISOU 699 CG2 VAL A 96 6189 5951 5046 336 -248 130 C ATOM 700 N THR A 97 50.772 -5.696 51.657 1.00 37.09 N ANISOU 700 N THR A 97 5073 4895 4124 211 -123 58 N ATOM 701 CA THR A 97 50.948 -5.087 50.341 1.00 37.41 C ANISOU 701 CA THR A 97 5078 4881 4254 182 -128 19 C ATOM 702 C THR A 97 50.816 -3.566 50.443 1.00 37.86 C ANISOU 702 C THR A 97 5108 4961 4317 200 -160 -58 C ATOM 703 O THR A 97 51.482 -2.828 49.721 1.00 33.07 O ANISOU 703 O THR A 97 4475 4313 3779 193 -194 -96 O ATOM 704 CB THR A 97 49.978 -5.652 49.256 1.00 32.77 C ANISOU 704 CB THR A 97 4483 4263 3706 130 -69 49 C ATOM 705 OG1 THR A 97 48.622 -5.311 49.573 1.00 37.53 O ANISOU 705 OG1 THR A 97 5080 4917 4265 120 -28 40 O ATOM 706 CG2 THR A 97 50.108 -7.172 49.129 1.00 36.93 C ANISOU 706 CG2 THR A 97 5039 4753 4239 111 -45 121 C ATOM 707 N TYR A 98 49.972 -3.095 51.350 1.00 30.94 N ANISOU 707 N TYR A 98 4236 4150 3368 224 -151 -81 N ATOM 708 CA TYR A 98 49.861 -1.649 51.557 1.00 31.58 C ANISOU 708 CA TYR A 98 4296 4251 3454 251 -192 -163 C ATOM 709 C TYR A 98 51.082 -1.100 52.314 1.00 38.51 C ANISOU 709 C TYR A 98 5174 5130 4326 295 -269 -206 C ATOM 710 O TYR A 98 51.573 -0.008 52.016 1.00 35.57 O ANISOU 710 O TYR A 98 4777 4726 4011 300 -320 -266 O ATOM 711 CB TYR A 98 48.561 -1.293 52.280 1.00 31.01 C ANISOU 711 CB TYR A 98 4223 4254 3304 271 -160 -186 C ATOM 712 CG TYR A 98 48.450 0.187 52.556 1.00 37.21 C ANISOU 712 CG TYR A 98 4989 5055 4093 308 -211 -278 C ATOM 713 CD1 TYR A 98 48.023 1.072 51.567 1.00 39.61 C ANISOU 713 CD1 TYR A 98 5267 5315 4468 287 -215 -318 C ATOM 714 CD2 TYR A 98 48.817 0.705 53.790 1.00 41.55 C ANISOU 714 CD2 TYR A 98 5549 5659 4579 368 -261 -327 C ATOM 715 CE1 TYR A 98 47.938 2.433 51.815 1.00 36.47 C ANISOU 715 CE1 TYR A 98 4856 4918 4082 323 -269 -402 C ATOM 716 CE2 TYR A 98 48.736 2.064 54.048 1.00 51.16 C ANISOU 716 CE2 TYR A 98 6750 6882 5807 406 -317 -420 C ATOM 717 CZ TYR A 98 48.298 2.922 53.059 1.00 46.32 C ANISOU 717 CZ TYR A 98 6112 6216 5271 382 -321 -456 C ATOM 718 OH TYR A 98 48.225 4.268 53.323 1.00 42.91 O ANISOU 718 OH TYR A 98 5668 5778 4856 421 -383 -548 O ATOM 719 N LYS A 99 51.576 -1.876 53.279 1.00 34.66 N ANISOU 719 N LYS A 99 4715 4679 3775 326 -280 -172 N ATOM 720 CA LYS A 99 52.767 -1.510 54.040 1.00 39.18 C ANISOU 720 CA LYS A 99 5289 5259 4339 372 -356 -211 C ATOM 721 C LYS A 99 53.977 -1.306 53.120 1.00 41.55 C ANISOU 721 C LYS A 99 5559 5483 4744 348 -396 -222 C ATOM 722 O LYS A 99 54.842 -0.463 53.386 1.00 38.70 O ANISOU 722 O LYS A 99 5176 5112 4416 370 -465 -282 O ATOM 723 CB LYS A 99 53.072 -2.588 55.093 1.00 43.57 C ANISOU 723 CB LYS A 99 5886 5863 4808 408 -355 -155 C ATOM 724 CG LYS A 99 54.145 -2.206 56.102 1.00 58.12 C ANISOU 724 CG LYS A 99 7732 7734 6616 469 -437 -202 C ATOM 725 CD LYS A 99 53.670 -1.088 57.034 1.00 64.70 C ANISOU 725 CD LYS A 99 8561 8635 7387 518 -471 -283 C ATOM 726 CE LYS A 99 54.776 -0.611 57.983 1.00 58.28 C ANISOU 726 CE LYS A 99 7747 7846 6549 581 -565 -344 C ATOM 727 NZ LYS A 99 55.340 -1.719 58.819 1.00 55.85 N ANISOU 727 NZ LYS A 99 7478 7578 6165 619 -574 -284 N ATOM 728 N ASN A 100 54.030 -2.087 52.045 1.00 35.33 N ANISOU 728 N ASN A 100 4768 4646 4011 303 -352 -167 N ATOM 729 CA ASN A 100 55.099 -2.007 51.039 1.00 38.36 C ANISOU 729 CA ASN A 100 5119 4968 4490 277 -375 -170 C ATOM 730 C ASN A 100 54.960 -0.896 49.981 1.00 33.60 C ANISOU 730 C ASN A 100 4478 4322 3968 240 -376 -207 C ATOM 731 O ASN A 100 55.877 -0.670 49.183 1.00 33.38 O ANISOU 731 O ASN A 100 4416 4250 4016 218 -395 -210 O ATOM 732 CB ASN A 100 55.261 -3.356 50.326 1.00 40.71 C ANISOU 732 CB ASN A 100 5428 5234 4807 254 -331 -100 C ATOM 733 CG ASN A 100 56.011 -4.371 51.165 1.00 45.31 C ANISOU 733 CG ASN A 100 6039 5832 5345 292 -356 -65 C ATOM 734 OD1 ASN A 100 55.812 -5.577 51.034 1.00 43.03 O ANISOU 734 OD1 ASN A 100 5779 5529 5041 285 -321 -4 O ATOM 735 ND2 ASN A 100 56.886 -3.881 52.030 1.00 34.81 N ANISOU 735 ND2 ASN A 100 4701 4526 3999 335 -422 -105 N ATOM 736 N VAL A 101 53.828 -0.204 49.972 1.00 34.85 N ANISOU 736 N VAL A 101 4639 4495 4107 235 -356 -233 N ATOM 737 CA VAL A 101 53.614 0.872 48.997 1.00 33.75 C ANISOU 737 CA VAL A 101 4470 4312 4039 204 -361 -264 C ATOM 738 C VAL A 101 54.694 1.959 49.093 1.00 38.34 C ANISOU 738 C VAL A 101 5022 4862 4684 209 -435 -316 C ATOM 739 O VAL A 101 55.232 2.402 48.076 1.00 36.39 O ANISOU 739 O VAL A 101 4744 4564 4519 172 -440 -309 O ATOM 740 CB VAL A 101 52.196 1.455 49.126 1.00 30.33 C ANISOU 740 CB VAL A 101 4047 3905 3570 211 -337 -292 C ATOM 741 CG1 VAL A 101 52.127 2.873 48.577 1.00 38.21 C ANISOU 741 CG1 VAL A 101 5022 4861 4634 201 -373 -344 C ATOM 742 CG2 VAL A 101 51.185 0.542 48.441 1.00 33.61 C ANISOU 742 CG2 VAL A 101 4473 4327 3968 181 -260 -239 C ATOM 743 N PRO A 102 55.039 2.379 50.319 1.00 37.12 N ANISOU 743 N PRO A 102 4874 4740 4491 255 -493 -366 N ATOM 744 CA PRO A 102 56.096 3.394 50.407 1.00 39.75 C ANISOU 744 CA PRO A 102 5173 5036 4894 255 -570 -418 C ATOM 745 C PRO A 102 57.405 2.909 49.788 1.00 36.43 C ANISOU 745 C PRO A 102 4720 4584 4539 227 -577 -383 C ATOM 746 O PRO A 102 58.139 3.721 49.225 1.00 38.74 O ANISOU 746 O PRO A 102 4971 4829 4919 195 -612 -401 O ATOM 747 CB PRO A 102 56.251 3.608 51.920 1.00 44.55 C ANISOU 747 CB PRO A 102 5797 5697 5432 318 -629 -475 C ATOM 748 CG PRO A 102 54.911 3.272 52.476 1.00 45.72 C ANISOU 748 CG PRO A 102 5984 5906 5482 346 -581 -468 C ATOM 749 CD PRO A 102 54.418 2.115 51.627 1.00 40.35 C ANISOU 749 CD PRO A 102 5316 5220 4795 307 -495 -383 C ATOM 750 N ASN A 103 57.697 1.612 49.889 1.00 34.78 N ANISOU 750 N ASN A 103 4526 4400 4289 238 -546 -332 N ATOM 751 CA ASN A 103 58.896 1.065 49.251 1.00 34.20 C ANISOU 751 CA ASN A 103 4419 4303 4273 219 -549 -302 C ATOM 752 C ASN A 103 58.862 1.182 47.721 1.00 39.88 C ANISOU 752 C ASN A 103 5109 4978 5065 162 -501 -267 C ATOM 753 O ASN A 103 59.834 1.623 47.097 1.00 39.08 O ANISOU 753 O ASN A 103 4959 4849 5040 134 -521 -270 O ATOM 754 CB ASN A 103 59.129 -0.395 49.662 1.00 42.63 C ANISOU 754 CB ASN A 103 5515 5400 5282 249 -528 -255 C ATOM 755 CG ASN A 103 59.546 -0.538 51.112 1.00 47.93 C ANISOU 755 CG ASN A 103 6207 6115 5888 308 -586 -284 C ATOM 756 OD1 ASN A 103 59.292 -1.569 51.740 1.00 53.85 O ANISOU 756 OD1 ASN A 103 7000 6898 6562 340 -568 -245 O ATOM 757 ND2 ASN A 103 60.190 0.495 51.654 1.00 43.44 N ANISOU 757 ND2 ASN A 103 5610 5548 5349 323 -659 -350 N ATOM 758 N TRP A 104 57.752 0.759 47.119 1.00 37.12 N ANISOU 758 N TRP A 104 4787 4628 4688 147 -437 -233 N ATOM 759 CA TRP A 104 57.559 0.918 45.678 1.00 36.12 C ANISOU 759 CA TRP A 104 4640 4468 4616 101 -392 -203 C ATOM 760 C TRP A 104 57.687 2.378 45.248 1.00 34.15 C ANISOU 760 C TRP A 104 4359 4181 4434 71 -423 -233 C ATOM 761 O TRP A 104 58.357 2.690 44.260 1.00 34.74 O ANISOU 761 O TRP A 104 4395 4228 4576 35 -416 -213 O ATOM 762 CB TRP A 104 56.210 0.335 45.247 1.00 38.26 C ANISOU 762 CB TRP A 104 4947 4748 4844 94 -329 -175 C ATOM 763 CG TRP A 104 56.238 -1.143 45.363 1.00 32.92 C ANISOU 763 CG TRP A 104 4294 4089 4126 108 -297 -134 C ATOM 764 CD1 TRP A 104 55.597 -1.914 46.296 1.00 32.71 C ANISOU 764 CD1 TRP A 104 4309 4093 4027 134 -284 -121 C ATOM 765 CD2 TRP A 104 57.031 -2.030 44.581 1.00 36.66 C ANISOU 765 CD2 TRP A 104 4750 4548 4630 101 -278 -101 C ATOM 766 NE1 TRP A 104 55.906 -3.244 46.097 1.00 34.80 N ANISOU 766 NE1 TRP A 104 4587 4351 4282 139 -261 -77 N ATOM 767 CE2 TRP A 104 56.792 -3.338 45.055 1.00 34.93 C ANISOU 767 CE2 TRP A 104 4569 4342 4362 123 -260 -70 C ATOM 768 CE3 TRP A 104 57.895 -1.853 43.494 1.00 37.18 C ANISOU 768 CE3 TRP A 104 4772 4596 4760 79 -274 -94 C ATOM 769 CZ2 TRP A 104 57.397 -4.454 44.490 1.00 43.29 C ANISOU 769 CZ2 TRP A 104 5624 5387 5438 129 -245 -41 C ATOM 770 CZ3 TRP A 104 58.499 -2.959 42.941 1.00 43.11 C ANISOU 770 CZ3 TRP A 104 5515 5347 5520 87 -254 -67 C ATOM 771 CH2 TRP A 104 58.247 -4.244 43.437 1.00 47.63 C ANISOU 771 CH2 TRP A 104 6127 5923 6046 114 -243 -45 C ATOM 772 N HIS A 105 57.060 3.273 45.999 1.00 34.90 N ANISOU 772 N HIS A 105 4472 4277 4512 89 -459 -281 N ATOM 773 CA HIS A 105 57.132 4.692 45.676 1.00 37.76 C ANISOU 773 CA HIS A 105 4812 4592 4944 65 -499 -313 C ATOM 774 C HIS A 105 58.574 5.192 45.696 1.00 36.18 C ANISOU 774 C HIS A 105 4562 4365 4820 45 -553 -325 C ATOM 775 O HIS A 105 58.998 5.926 44.812 1.00 35.95 O ANISOU 775 O HIS A 105 4499 4291 4870 -1 -556 -309 O ATOM 776 CB HIS A 105 56.280 5.517 46.634 1.00 38.58 C ANISOU 776 CB HIS A 105 4942 4703 5012 100 -539 -375 C ATOM 777 CG HIS A 105 56.213 6.965 46.271 1.00 38.47 C ANISOU 777 CG HIS A 105 4913 4630 5073 79 -584 -409 C ATOM 778 ND1 HIS A 105 57.106 7.897 46.756 1.00 42.27 N ANISOU 778 ND1 HIS A 105 5368 5075 5618 76 -662 -456 N ATOM 779 CD2 HIS A 105 55.374 7.639 45.448 1.00 37.62 C ANISOU 779 CD2 HIS A 105 4814 4486 4993 59 -565 -400 C ATOM 780 CE1 HIS A 105 56.809 9.084 46.259 1.00 41.76 C ANISOU 780 CE1 HIS A 105 5299 4949 5620 52 -690 -472 C ATOM 781 NE2 HIS A 105 55.763 8.954 45.461 1.00 39.48 N ANISOU 781 NE2 HIS A 105 5033 4660 5307 44 -632 -437 N ATOM 782 N ARG A 106 59.319 4.809 46.728 1.00 38.25 N ANISOU 782 N ARG A 106 4819 4657 5058 79 -596 -353 N ATOM 783 CA ARG A 106 60.731 5.159 46.815 1.00 37.80 C ANISOU 783 CA ARG A 106 4707 4582 5072 63 -649 -369 C ATOM 784 C ARG A 106 61.528 4.665 45.605 1.00 38.72 C ANISOU 784 C ARG A 106 4779 4692 5241 20 -603 -310 C ATOM 785 O ARG A 106 62.245 5.441 44.978 1.00 44.37 O ANISOU 785 O ARG A 106 5444 5372 6044 -27 -619 -303 O ATOM 786 CB ARG A 106 61.329 4.608 48.115 1.00 40.87 C ANISOU 786 CB ARG A 106 5103 5016 5410 118 -699 -406 C ATOM 787 CG ARG A 106 62.836 4.760 48.235 1.00 49.18 C ANISOU 787 CG ARG A 106 6093 6061 6531 107 -754 -424 C ATOM 788 CD ARG A 106 63.351 4.019 49.467 1.00 55.55 C ANISOU 788 CD ARG A 106 6913 6919 7273 170 -799 -453 C ATOM 789 NE ARG A 106 62.773 2.681 49.572 1.00 65.96 N ANISOU 789 NE ARG A 106 8283 8279 8500 204 -740 -404 N ATOM 790 CZ ARG A 106 63.333 1.584 49.074 1.00 72.87 C ANISOU 790 CZ ARG A 106 9146 9166 9374 205 -704 -356 C ATOM 791 NH1 ARG A 106 64.493 1.664 48.439 1.00 81.89 N ANISOU 791 NH1 ARG A 106 10223 10296 10596 177 -716 -351 N ATOM 792 NH2 ARG A 106 62.736 0.407 49.213 1.00 68.85 N ANISOU 792 NH2 ARG A 106 8689 8683 8788 233 -657 -313 N ATOM 793 N ASP A 107 61.407 3.374 45.289 1.00 40.11 N ANISOU 793 N ASP A 107 4973 4902 5366 36 -547 -267 N ATOM 794 CA ASP A 107 62.151 2.767 44.184 1.00 44.11 C ANISOU 794 CA ASP A 107 5438 5413 5909 9 -502 -219 C ATOM 795 C ASP A 107 61.798 3.455 42.878 1.00 46.07 C ANISOU 795 C ASP A 107 5669 5630 6205 -43 -460 -184 C ATOM 796 O ASP A 107 62.651 3.659 42.010 1.00 41.95 O ANISOU 796 O ASP A 107 5093 5103 5744 -81 -446 -156 O ATOM 797 CB ASP A 107 61.842 1.267 44.066 1.00 43.25 C ANISOU 797 CB ASP A 107 5363 5337 5732 42 -452 -186 C ATOM 798 CG ASP A 107 62.406 0.457 45.221 1.00 52.59 C ANISOU 798 CG ASP A 107 6559 6551 6872 94 -492 -205 C ATOM 799 OD1 ASP A 107 63.273 0.981 45.953 1.00 48.44 O ANISOU 799 OD1 ASP A 107 6002 6029 6375 105 -556 -244 O ATOM 800 OD2 ASP A 107 61.979 -0.706 45.394 1.00 59.38 O ANISOU 800 OD2 ASP A 107 7461 7428 7672 125 -462 -179 O ATOM 801 N LEU A 108 60.526 3.810 42.752 1.00 39.92 N ANISOU 801 N LEU A 108 4937 4835 5396 -44 -440 -184 N ATOM 802 CA LEU A 108 60.022 4.485 41.566 1.00 39.66 C ANISOU 802 CA LEU A 108 4899 4771 5398 -86 -405 -152 C ATOM 803 C LEU A 108 60.622 5.880 41.406 1.00 42.23 C ANISOU 803 C LEU A 108 5186 5049 5812 -128 -451 -160 C ATOM 804 O LEU A 108 61.199 6.211 40.368 1.00 48.35 O ANISOU 804 O LEU A 108 5918 5810 6642 -174 -427 -115 O ATOM 805 CB LEU A 108 58.499 4.574 41.643 1.00 40.33 C ANISOU 805 CB LEU A 108 5041 4852 5429 -68 -385 -161 C ATOM 806 CG LEU A 108 57.817 5.300 40.494 1.00 44.77 C ANISOU 806 CG LEU A 108 5608 5383 6019 -100 -356 -132 C ATOM 807 CD1 LEU A 108 58.328 4.746 39.185 1.00 40.40 C ANISOU 807 CD1 LEU A 108 5025 4844 5480 -127 -300 -75 C ATOM 808 CD2 LEU A 108 56.312 5.121 40.615 1.00 52.20 C ANISOU 808 CD2 LEU A 108 6600 6335 6898 -74 -332 -146 C ATOM 809 N VAL A 109 60.485 6.695 42.444 1.00 45.13 N ANISOU 809 N VAL A 109 5565 5390 6192 -114 -519 -217 N ATOM 810 CA VAL A 109 60.912 8.088 42.386 1.00 44.61 C ANISOU 810 CA VAL A 109 5470 5263 6217 -154 -574 -232 C ATOM 811 C VAL A 109 62.438 8.210 42.354 1.00 45.04 C ANISOU 811 C VAL A 109 5452 5315 6346 -188 -603 -226 C ATOM 812 O VAL A 109 62.979 9.213 41.887 1.00 41.08 O ANISOU 812 O VAL A 109 4911 4763 5936 -243 -627 -210 O ATOM 813 CB VAL A 109 60.330 8.887 43.565 1.00 55.30 C ANISOU 813 CB VAL A 109 6859 6592 7563 -118 -647 -309 C ATOM 814 CG1 VAL A 109 61.109 10.174 43.792 1.00 63.82 C ANISOU 814 CG1 VAL A 109 7898 7605 8746 -154 -726 -341 C ATOM 815 CG2 VAL A 109 58.860 9.169 43.316 1.00 49.76 C ANISOU 815 CG2 VAL A 109 6211 5879 6817 -100 -622 -311 C ATOM 816 N ARG A 110 63.128 7.183 42.842 1.00 38.85 N ANISOU 816 N ARG A 110 4651 4584 5527 -157 -600 -235 N ATOM 817 CA ARG A 110 64.578 7.154 42.746 1.00 45.50 C ANISOU 817 CA ARG A 110 5417 5437 6434 -185 -621 -229 C ATOM 818 C ARG A 110 65.026 7.237 41.290 1.00 47.30 C ANISOU 818 C ARG A 110 5596 5663 6711 -243 -558 -155 C ATOM 819 O ARG A 110 66.002 7.914 40.969 1.00 48.60 O ANISOU 819 O ARG A 110 5692 5808 6964 -296 -577 -141 O ATOM 820 CB ARG A 110 65.145 5.889 43.389 1.00 49.27 C ANISOU 820 CB ARG A 110 5889 5976 6855 -132 -622 -246 C ATOM 821 CG ARG A 110 66.621 5.680 43.089 1.00 51.88 C ANISOU 821 CG ARG A 110 6134 6331 7248 -156 -628 -234 C ATOM 822 CD ARG A 110 67.091 4.288 43.489 1.00 62.63 C ANISOU 822 CD ARG A 110 7497 7752 8549 -97 -619 -240 C ATOM 823 NE ARG A 110 68.337 3.938 42.813 1.00 73.58 N ANISOU 823 NE ARG A 110 8799 9172 9986 -119 -599 -215 N ATOM 824 CZ ARG A 110 68.414 3.158 41.739 1.00 75.57 C ANISOU 824 CZ ARG A 110 9037 9458 10220 -121 -524 -165 C ATOM 825 NH1 ARG A 110 67.316 2.629 41.218 1.00 69.69 N ANISOU 825 NH1 ARG A 110 8358 8712 9410 -106 -466 -135 N ATOM 826 NH2 ARG A 110 69.594 2.898 41.188 1.00 82.99 N ANISOU 826 NH2 ARG A 110 9892 10435 11204 -135 -509 -151 N ATOM 827 N VAL A 111 64.302 6.553 40.409 1.00 45.35 N ANISOU 827 N VAL A 111 5382 5442 6407 -234 -482 -109 N ATOM 828 CA VAL A 111 64.666 6.507 38.997 1.00 43.33 C ANISOU 828 CA VAL A 111 5085 5201 6177 -278 -416 -39 C ATOM 829 C VAL A 111 63.927 7.557 38.154 1.00 46.41 C ANISOU 829 C VAL A 111 5497 5540 6598 -322 -399 2 C ATOM 830 O VAL A 111 64.477 8.075 37.183 1.00 47.87 O ANISOU 830 O VAL A 111 5634 5719 6837 -376 -370 58 O ATOM 831 CB VAL A 111 64.407 5.101 38.395 1.00 53.01 C ANISOU 831 CB VAL A 111 6330 6488 7326 -239 -346 -14 C ATOM 832 CG1 VAL A 111 64.831 5.059 36.937 1.00 55.59 C ANISOU 832 CG1 VAL A 111 6610 6842 7671 -275 -279 51 C ATOM 833 CG2 VAL A 111 65.137 4.020 39.203 1.00 44.71 C ANISOU 833 CG2 VAL A 111 5262 5479 6245 -190 -366 -50 C ATOM 834 N CYS A 112 62.691 7.875 38.531 1.00 37.81 N ANISOU 834 N CYS A 112 4476 4418 5471 -296 -416 -25 N ATOM 835 CA CYS A 112 61.807 8.649 37.662 1.00 36.78 C ANISOU 835 CA CYS A 112 4377 4246 5350 -322 -394 14 C ATOM 836 C CYS A 112 61.506 10.086 38.098 1.00 51.30 C ANISOU 836 C CYS A 112 6232 6004 7256 -345 -463 -12 C ATOM 837 O CYS A 112 61.059 10.894 37.282 1.00 51.27 O ANISOU 837 O CYS A 112 6241 5955 7283 -377 -453 31 O ATOM 838 CB CYS A 112 60.498 7.887 37.435 1.00 33.65 C ANISOU 838 CB CYS A 112 4045 3879 4862 -276 -349 11 C ATOM 839 SG CYS A 112 60.760 6.348 36.580 1.00 43.61 S ANISOU 839 SG CYS A 112 5291 5218 6061 -256 -268 49 S ATOM 840 N GLU A 113 61.736 10.403 39.371 1.00 60.40 N ANISOU 840 N GLU A 113 7385 7136 8429 -324 -537 -83 N ATOM 841 CA GLU A 113 61.491 11.758 39.876 1.00 68.35 C ANISOU 841 CA GLU A 113 8407 8061 9503 -339 -615 -123 C ATOM 842 C GLU A 113 60.035 12.205 39.755 1.00 77.94 C ANISOU 842 C GLU A 113 9689 9244 10679 -309 -614 -136 C ATOM 843 O GLU A 113 59.114 11.557 40.245 1.00 86.64 O ANISOU 843 O GLU A 113 10836 10389 11694 -251 -598 -172 O ATOM 844 CB GLU A 113 62.329 12.781 39.101 1.00 75.79 C ANISOU 844 CB GLU A 113 9297 8942 10559 -418 -628 -67 C ATOM 845 CG GLU A 113 63.782 12.882 39.465 1.00 84.35 C ANISOU 845 CG GLU A 113 10303 10027 11719 -458 -664 -75 C ATOM 846 CD GLU A 113 64.457 14.018 38.717 1.00 96.52 C ANISOU 846 CD GLU A 113 11797 11498 13379 -545 -678 -15 C ATOM 847 OE1 GLU A 113 63.820 14.588 37.804 1.00 99.37 O ANISOU 847 OE1 GLU A 113 12189 11818 13751 -571 -649 46 O ATOM 848 OE2 GLU A 113 65.617 14.344 39.042 1.00100.86 O ANISOU 848 OE2 GLU A 113 12277 12033 14013 -588 -719 -26 O ATOM 849 N ASN A 114 59.876 13.324 39.053 1.00 77.47 N ANISOU 849 N ASN A 114 9634 9112 10691 -352 -631 -99 N ATOM 850 CA ASN A 114 58.645 14.108 38.925 1.00 76.06 C ANISOU 850 CA ASN A 114 9511 8880 10507 -329 -654 -115 C ATOM 851 C ASN A 114 57.293 13.412 38.727 1.00 62.61 C ANISOU 851 C ASN A 114 7862 7229 8700 -274 -602 -122 C ATOM 852 O ASN A 114 56.255 13.941 39.131 1.00 54.71 O ANISOU 852 O ASN A 114 6904 6201 7681 -234 -638 -172 O ATOM 853 CB ASN A 114 58.830 15.103 37.769 1.00 86.21 C ANISOU 853 CB ASN A 114 10788 10094 11875 -393 -651 -35 C ATOM 854 CG ASN A 114 59.025 14.410 36.419 1.00 94.92 C ANISOU 854 CG ASN A 114 11872 11251 12943 -423 -555 63 C ATOM 855 OD1 ASN A 114 59.728 13.402 36.314 1.00 98.32 O ANISOU 855 OD1 ASN A 114 12264 11755 13339 -426 -506 80 O ATOM 856 ND2 ASN A 114 58.404 14.959 35.381 1.00 96.49 N ANISOU 856 ND2 ASN A 114 12098 11415 13147 -438 -533 124 N ATOM 857 N ILE A 115 57.300 12.237 38.112 1.00 48.34 N ANISOU 857 N ILE A 115 6046 5494 6826 -270 -523 -77 N ATOM 858 CA ILE A 115 56.119 11.757 37.396 1.00 36.70 C ANISOU 858 CA ILE A 115 4612 4053 5281 -243 -467 -55 C ATOM 859 C ILE A 115 54.814 11.608 38.189 1.00 33.78 C ANISOU 859 C ILE A 115 4289 3701 4845 -181 -482 -124 C ATOM 860 O ILE A 115 54.825 11.322 39.379 1.00 38.76 O ANISOU 860 O ILE A 115 4924 4356 5447 -147 -511 -187 O ATOM 861 CB ILE A 115 56.431 10.428 36.688 1.00 36.30 C ANISOU 861 CB ILE A 115 4542 4076 5174 -246 -387 -8 C ATOM 862 CG1 ILE A 115 56.676 9.329 37.720 1.00 33.34 C ANISOU 862 CG1 ILE A 115 4163 3758 4747 -211 -384 -54 C ATOM 863 CG2 ILE A 115 57.639 10.595 35.764 1.00 38.28 C ANISOU 863 CG2 ILE A 115 4741 4323 5481 -304 -362 64 C ATOM 864 CD1 ILE A 115 56.783 7.963 37.084 1.00 30.01 C ANISOU 864 CD1 ILE A 115 3733 3402 4268 -203 -312 -19 C ATOM 865 N PRO A 116 53.675 11.756 37.496 1.00 33.93 N ANISOU 865 N PRO A 116 4340 3717 4833 -164 -457 -110 N ATOM 866 CA PRO A 116 52.332 11.536 38.048 1.00 29.72 C ANISOU 866 CA PRO A 116 3844 3215 4234 -108 -457 -168 C ATOM 867 C PRO A 116 52.130 10.064 38.404 1.00 36.24 C ANISOU 867 C PRO A 116 4669 4124 4977 -85 -402 -175 C ATOM 868 O PRO A 116 52.500 9.186 37.617 1.00 33.36 O ANISOU 868 O PRO A 116 4289 3791 4594 -106 -346 -122 O ATOM 869 CB PRO A 116 51.402 11.898 36.875 1.00 28.15 C ANISOU 869 CB PRO A 116 3667 2999 4030 -106 -434 -130 C ATOM 870 CG PRO A 116 52.227 12.656 35.930 1.00 42.28 C ANISOU 870 CG PRO A 116 5442 4730 5892 -158 -442 -61 C ATOM 871 CD PRO A 116 53.635 12.220 36.101 1.00 39.49 C ANISOU 871 CD PRO A 116 5046 4391 5569 -198 -431 -36 C ATOM 872 N ILE A 117 51.524 9.801 39.557 1.00 32.82 N ANISOU 872 N ILE A 117 4251 3725 4494 -42 -417 -238 N ATOM 873 CA ILE A 117 51.381 8.438 40.046 1.00 28.15 C ANISOU 873 CA ILE A 117 3662 3205 3830 -24 -371 -240 C ATOM 874 C ILE A 117 50.008 8.252 40.665 1.00 32.52 C ANISOU 874 C ILE A 117 4240 3800 4318 20 -361 -286 C ATOM 875 O ILE A 117 49.552 9.099 41.426 1.00 33.69 O ANISOU 875 O ILE A 117 4397 3936 4466 52 -409 -345 O ATOM 876 CB ILE A 117 52.448 8.126 41.096 1.00 36.06 C ANISOU 876 CB ILE A 117 4647 4219 4833 -20 -400 -260 C ATOM 877 CG1 ILE A 117 53.850 8.293 40.508 1.00 31.71 C ANISOU 877 CG1 ILE A 117 4062 3636 4352 -66 -409 -217 C ATOM 878 CG2 ILE A 117 52.272 6.722 41.633 1.00 36.50 C ANISOU 878 CG2 ILE A 117 4712 4342 4814 0 -356 -255 C ATOM 879 CD1 ILE A 117 54.938 8.223 41.547 1.00 35.77 C ANISOU 879 CD1 ILE A 117 4555 4156 4881 -60 -454 -247 C ATOM 880 N VAL A 118 49.324 7.164 40.311 1.00 28.04 N ANISOU 880 N VAL A 118 3678 3280 3697 22 -300 -263 N ATOM 881 CA VAL A 118 48.056 6.854 40.940 1.00 24.86 C ANISOU 881 CA VAL A 118 3289 2927 3232 57 -282 -301 C ATOM 882 C VAL A 118 48.248 5.645 41.846 1.00 32.29 C ANISOU 882 C VAL A 118 4231 3922 4115 64 -254 -296 C ATOM 883 O VAL A 118 48.951 4.698 41.489 1.00 31.40 O ANISOU 883 O VAL A 118 4114 3813 4004 41 -224 -251 O ATOM 884 CB VAL A 118 46.973 6.478 39.915 1.00 34.15 C ANISOU 884 CB VAL A 118 4467 4118 4390 52 -236 -281 C ATOM 885 CG1 VAL A 118 45.687 6.136 40.646 1.00 38.53 C ANISOU 885 CG1 VAL A 118 5026 4731 4884 83 -215 -320 C ATOM 886 CG2 VAL A 118 46.741 7.630 38.921 1.00 34.36 C ANISOU 886 CG2 VAL A 118 4497 4092 4468 48 -263 -276 C ATOM 887 N LEU A 119 47.630 5.683 43.015 1.00 32.89 N ANISOU 887 N LEU A 119 4316 4042 4138 100 -264 -341 N ATOM 888 CA LEU A 119 47.672 4.548 43.934 1.00 30.29 C ANISOU 888 CA LEU A 119 3994 3769 3745 109 -234 -329 C ATOM 889 C LEU A 119 46.354 3.798 43.821 1.00 29.46 C ANISOU 889 C LEU A 119 3890 3712 3591 109 -176 -318 C ATOM 890 O LEU A 119 45.276 4.398 43.886 1.00 33.60 O ANISOU 890 O LEU A 119 4410 4258 4100 130 -177 -357 O ATOM 891 CB LEU A 119 47.928 5.027 45.368 1.00 32.26 C ANISOU 891 CB LEU A 119 4250 4048 3960 151 -281 -381 C ATOM 892 CG LEU A 119 47.872 4.024 46.523 1.00 35.00 C ANISOU 892 CG LEU A 119 4610 4463 4227 171 -257 -370 C ATOM 893 CD1 LEU A 119 48.823 2.874 46.267 1.00 36.68 C ANISOU 893 CD1 LEU A 119 4826 4661 4448 143 -235 -309 C ATOM 894 CD2 LEU A 119 48.203 4.735 47.836 1.00 32.64 C ANISOU 894 CD2 LEU A 119 4317 4191 3896 220 -316 -432 C ATOM 895 N CYS A 120 46.432 2.486 43.614 1.00 30.80 N ANISOU 895 N CYS A 120 4064 3897 3742 85 -129 -268 N ATOM 896 CA CYS A 120 45.224 1.688 43.409 1.00 26.51 C ANISOU 896 CA CYS A 120 3517 3390 3164 73 -74 -253 C ATOM 897 C CYS A 120 45.130 0.561 44.422 1.00 29.21 C ANISOU 897 C CYS A 120 3870 3779 3448 73 -43 -225 C ATOM 898 O CYS A 120 46.053 -0.226 44.551 1.00 34.37 O ANISOU 898 O CYS A 120 4538 4416 4105 63 -42 -187 O ATOM 899 CB CYS A 120 45.187 1.099 41.993 1.00 29.13 C ANISOU 899 CB CYS A 120 3843 3688 3538 39 -45 -216 C ATOM 900 SG CYS A 120 44.884 2.329 40.696 1.00 33.96 S ANISOU 900 SG CYS A 120 4444 4259 4202 39 -68 -238 S ATOM 901 N GLY A 121 44.016 0.508 45.146 1.00 27.84 N ANISOU 901 N GLY A 121 3692 3667 3221 87 -17 -242 N ATOM 902 CA GLY A 121 43.740 -0.603 46.038 1.00 28.76 C ANISOU 902 CA GLY A 121 3817 3831 3277 80 23 -203 C ATOM 903 C GLY A 121 42.875 -1.581 45.267 1.00 30.65 C ANISOU 903 C GLY A 121 4046 4068 3533 37 77 -166 C ATOM 904 O GLY A 121 41.712 -1.292 44.983 1.00 34.66 O ANISOU 904 O GLY A 121 4528 4604 4036 34 99 -191 O ATOM 905 N ASN A 122 43.449 -2.732 44.921 1.00 28.70 N ANISOU 905 N ASN A 122 3815 3782 3306 7 93 -112 N ATOM 906 CA ASN A 122 42.750 -3.723 44.105 1.00 29.23 C ANISOU 906 CA ASN A 122 3873 3832 3401 -35 134 -81 C ATOM 907 C ASN A 122 42.025 -4.797 44.921 1.00 28.06 C ANISOU 907 C ASN A 122 3727 3723 3210 -60 180 -36 C ATOM 908 O ASN A 122 42.270 -4.959 46.131 1.00 30.00 O ANISOU 908 O ASN A 122 3992 4008 3400 -43 183 -14 O ATOM 909 CB ASN A 122 43.720 -4.345 43.093 1.00 29.48 C ANISOU 909 CB ASN A 122 3918 3796 3488 -51 121 -56 C ATOM 910 CG ASN A 122 43.018 -5.224 42.068 1.00 30.70 C ANISOU 910 CG ASN A 122 4061 3925 3678 -88 151 -42 C ATOM 911 OD1 ASN A 122 41.928 -4.906 41.602 1.00 34.58 O ANISOU 911 OD1 ASN A 122 4527 4437 4175 -98 168 -68 O ATOM 912 ND2 ASN A 122 43.643 -6.348 41.726 1.00 30.99 N ANISOU 912 ND2 ASN A 122 4116 3917 3741 -104 153 -4 N ATOM 913 N LYS A 123 41.100 -5.478 44.254 1.00 29.09 N ANISOU 913 N LYS A 123 3839 3846 3368 -99 216 -22 N ATOM 914 CA LYS A 123 40.339 -6.604 44.820 1.00 31.12 C ANISOU 914 CA LYS A 123 4093 4127 3604 -139 264 29 C ATOM 915 C LYS A 123 39.202 -6.177 45.740 1.00 34.91 C ANISOU 915 C LYS A 123 4543 4698 4023 -134 299 16 C ATOM 916 O LYS A 123 38.812 -6.920 46.632 1.00 35.13 O ANISOU 916 O LYS A 123 4573 4764 4009 -156 338 68 O ATOM 917 CB LYS A 123 41.259 -7.611 45.531 1.00 38.56 C ANISOU 917 CB LYS A 123 5079 5042 4531 -144 261 95 C ATOM 918 CG LYS A 123 42.401 -8.138 44.649 1.00 33.18 C ANISOU 918 CG LYS A 123 4423 4276 3908 -144 227 105 C ATOM 919 CD LYS A 123 43.048 -9.386 45.249 1.00 35.94 C ANISOU 919 CD LYS A 123 4812 4591 4251 -154 228 174 C ATOM 920 CE LYS A 123 44.356 -9.731 44.543 1.00 32.22 C ANISOU 920 CE LYS A 123 4364 4051 3828 -136 187 172 C ATOM 921 NZ LYS A 123 45.006 -10.941 45.171 1.00 34.21 N ANISOU 921 NZ LYS A 123 4658 4266 4075 -138 180 237 N ATOM 922 N VAL A 124 38.641 -4.992 45.505 1.00 34.91 N ANISOU 922 N VAL A 124 4512 4734 4018 -104 287 -51 N ATOM 923 CA VAL A 124 37.577 -4.496 46.390 1.00 36.47 C ANISOU 923 CA VAL A 124 4676 5028 4154 -87 317 -75 C ATOM 924 C VAL A 124 36.253 -5.246 46.201 1.00 37.94 C ANISOU 924 C VAL A 124 4818 5248 4350 -139 374 -54 C ATOM 925 O VAL A 124 35.257 -4.961 46.881 1.00 34.99 O ANISOU 925 O VAL A 124 4405 4964 3927 -132 410 -70 O ATOM 926 CB VAL A 124 37.343 -2.958 46.260 1.00 37.27 C ANISOU 926 CB VAL A 124 4757 5156 4248 -31 280 -161 C ATOM 927 CG1 VAL A 124 38.593 -2.163 46.683 1.00 37.90 C ANISOU 927 CG1 VAL A 124 4875 5211 4316 17 223 -184 C ATOM 928 CG2 VAL A 124 36.911 -2.592 44.856 1.00 36.71 C ANISOU 928 CG2 VAL A 124 4664 5040 4245 -41 264 -198 C ATOM 929 N ASP A 125 36.243 -6.209 45.279 1.00 39.05 N ANISOU 929 N ASP A 125 4960 5320 4555 -190 381 -22 N ATOM 930 CA ASP A 125 35.073 -7.069 45.103 1.00 36.69 C ANISOU 930 CA ASP A 125 4620 5042 4279 -249 431 4 C ATOM 931 C ASP A 125 34.976 -8.096 46.229 1.00 40.11 C ANISOU 931 C ASP A 125 5065 5505 4671 -287 478 88 C ATOM 932 O ASP A 125 33.917 -8.675 46.454 1.00 40.93 O ANISOU 932 O ASP A 125 5126 5650 4775 -336 529 116 O ATOM 933 CB ASP A 125 35.117 -7.792 43.755 1.00 37.01 C ANISOU 933 CB ASP A 125 4662 4995 4405 -288 415 5 C ATOM 934 CG ASP A 125 36.379 -8.623 43.577 1.00 39.87 C ANISOU 934 CG ASP A 125 5082 5271 4795 -296 390 54 C ATOM 935 OD1 ASP A 125 37.442 -8.039 43.255 1.00 37.16 O ANISOU 935 OD1 ASP A 125 4771 4894 4455 -253 347 31 O ATOM 936 OD2 ASP A 125 36.305 -9.861 43.751 1.00 41.39 O ANISOU 936 OD2 ASP A 125 5286 5429 5010 -346 413 115 O ATOM 937 N ILE A 126 36.085 -8.313 46.931 1.00 36.61 N ANISOU 937 N ILE A 126 4676 5040 4193 -265 460 130 N ATOM 938 CA ILE A 126 36.130 -9.294 48.019 1.00 37.34 C ANISOU 938 CA ILE A 126 4793 5155 4241 -295 499 220 C ATOM 939 C ILE A 126 35.488 -8.722 49.277 1.00 49.88 C ANISOU 939 C ILE A 126 6354 6867 5730 -268 538 218 C ATOM 940 O ILE A 126 35.890 -7.665 49.766 1.00 51.09 O ANISOU 940 O ILE A 126 6516 7068 5829 -201 509 165 O ATOM 941 CB ILE A 126 37.580 -9.749 48.309 1.00 39.55 C ANISOU 941 CB ILE A 126 5141 5368 4516 -273 459 263 C ATOM 942 CG1 ILE A 126 38.154 -10.483 47.092 1.00 44.92 C ANISOU 942 CG1 ILE A 126 5843 5933 5292 -300 427 268 C ATOM 943 CG2 ILE A 126 37.638 -10.638 49.562 1.00 40.18 C ANISOU 943 CG2 ILE A 126 5252 5480 4536 -292 495 358 C ATOM 944 CD1 ILE A 126 39.625 -10.839 47.223 1.00 50.72 C ANISOU 944 CD1 ILE A 126 6638 6604 6031 -270 382 295 C ATOM 945 N LYS A 127 34.483 -9.421 49.795 1.00 55.58 N ANISOU 945 N LYS A 127 7041 7645 6430 -321 604 275 N ATOM 946 CA LYS A 127 33.718 -8.909 50.924 1.00 62.78 C ANISOU 946 CA LYS A 127 7916 8693 7245 -297 651 271 C ATOM 947 C LYS A 127 34.585 -8.611 52.142 1.00 54.87 C ANISOU 947 C LYS A 127 6964 7739 6144 -236 636 292 C ATOM 948 O LYS A 127 34.513 -7.519 52.700 1.00 52.31 O ANISOU 948 O LYS A 127 6625 7498 5751 -168 624 225 O ATOM 949 CB LYS A 127 32.567 -9.852 51.283 1.00 79.59 C ANISOU 949 CB LYS A 127 9999 10873 9371 -375 730 346 C ATOM 950 CG LYS A 127 31.416 -9.802 50.287 1.00 95.00 C ANISOU 950 CG LYS A 127 11876 12823 11398 -420 748 297 C ATOM 951 CD LYS A 127 30.230 -10.631 50.753 1.00107.31 C ANISOU 951 CD LYS A 127 13375 14447 12950 -499 830 367 C ATOM 952 CE LYS A 127 29.054 -10.493 49.797 1.00112.93 C ANISOU 952 CE LYS A 127 14003 15169 13735 -536 843 306 C ATOM 953 NZ LYS A 127 27.889 -11.321 50.217 1.00115.96 N ANISOU 953 NZ LYS A 127 14319 15615 14124 -622 923 375 N ATOM 954 N ASP A 128 35.412 -9.569 52.547 1.00 53.48 N ANISOU 954 N ASP A 128 6848 7509 5962 -256 631 380 N ATOM 955 CA ASP A 128 36.227 -9.387 53.745 1.00 55.14 C ANISOU 955 CA ASP A 128 7107 7769 6075 -197 615 405 C ATOM 956 C ASP A 128 37.433 -8.496 53.476 1.00 54.88 C ANISOU 956 C ASP A 128 7110 7687 6054 -126 532 328 C ATOM 957 O ASP A 128 38.565 -8.970 53.352 1.00 49.78 O ANISOU 957 O ASP A 128 6518 6958 5436 -120 489 360 O ATOM 958 CB ASP A 128 36.678 -10.728 54.323 1.00 62.15 C ANISOU 958 CB ASP A 128 8048 8618 6947 -237 635 530 C ATOM 959 CG ASP A 128 37.362 -10.577 55.667 1.00 70.76 C ANISOU 959 CG ASP A 128 9185 9780 7921 -175 625 562 C ATOM 960 OD1 ASP A 128 37.258 -9.483 56.268 1.00 69.23 O ANISOU 960 OD1 ASP A 128 8972 9686 7648 -106 616 489 O ATOM 961 OD2 ASP A 128 38.002 -11.550 56.120 1.00 75.22 O ANISOU 961 OD2 ASP A 128 9806 10301 8472 -189 621 656 O ATOM 962 N ARG A 129 37.176 -7.197 53.400 1.00 47.87 N ANISOU 962 N ARG A 129 6189 6850 5148 -72 509 227 N ATOM 963 CA ARG A 129 38.208 -6.220 53.096 1.00 44.54 C ANISOU 963 CA ARG A 129 5792 6382 4749 -12 431 149 C ATOM 964 C ARG A 129 39.023 -5.880 54.345 1.00 42.03 C ANISOU 964 C ARG A 129 5513 6119 4337 55 400 147 C ATOM 965 O ARG A 129 38.470 -5.671 55.425 1.00 46.31 O ANISOU 965 O ARG A 129 6042 6777 4778 86 433 149 O ATOM 966 CB ARG A 129 37.563 -4.965 52.517 1.00 39.81 C ANISOU 966 CB ARG A 129 5145 5807 4174 18 414 45 C ATOM 967 CG ARG A 129 38.537 -3.873 52.184 1.00 40.07 C ANISOU 967 CG ARG A 129 5199 5789 4238 73 334 -33 C ATOM 968 CD ARG A 129 37.850 -2.771 51.398 1.00 40.82 C ANISOU 968 CD ARG A 129 5251 5883 4377 91 316 -123 C ATOM 969 NE ARG A 129 38.763 -1.669 51.141 1.00 42.48 N ANISOU 969 NE ARG A 129 5480 6041 4617 141 239 -191 N ATOM 970 CZ ARG A 129 38.538 -0.706 50.257 1.00 36.30 C ANISOU 970 CZ ARG A 129 4677 5220 3893 155 205 -259 C ATOM 971 NH1 ARG A 129 37.424 -0.713 49.540 1.00 34.86 N ANISOU 971 NH1 ARG A 129 4455 5051 3741 130 238 -273 N ATOM 972 NH2 ARG A 129 39.430 0.260 50.095 1.00 37.25 N ANISOU 972 NH2 ARG A 129 4818 5289 4046 193 135 -311 N ATOM 973 N LYS A 130 40.342 -5.838 54.201 1.00 42.83 N ANISOU 973 N LYS A 130 5659 6146 4469 79 336 142 N ATOM 974 CA LYS A 130 41.207 -5.598 55.351 1.00 45.79 C ANISOU 974 CA LYS A 130 6071 6566 4761 143 298 139 C ATOM 975 C LYS A 130 41.737 -4.162 55.410 1.00 47.24 C ANISOU 975 C LYS A 130 6247 6756 4945 212 226 27 C ATOM 976 O LYS A 130 41.800 -3.553 56.485 1.00 47.65 O ANISOU 976 O LYS A 130 6304 6895 4907 276 207 -14 O ATOM 977 CB LYS A 130 42.361 -6.597 55.369 1.00 44.42 C ANISOU 977 CB LYS A 130 5952 6314 4610 130 271 213 C ATOM 978 CG LYS A 130 41.927 -8.037 55.570 1.00 54.75 C ANISOU 978 CG LYS A 130 7279 7615 5907 71 332 331 C ATOM 979 CD LYS A 130 41.013 -8.171 56.781 1.00 55.80 C ANISOU 979 CD LYS A 130 7403 7877 5923 79 394 374 C ATOM 980 CE LYS A 130 41.057 -9.575 57.355 1.00 62.81 C ANISOU 980 CE LYS A 130 8332 8755 6777 40 433 506 C ATOM 981 NZ LYS A 130 40.880 -10.606 56.301 1.00 64.39 N ANISOU 981 NZ LYS A 130 8534 8843 7089 -42 452 563 N ATOM 982 N VAL A 131 42.124 -3.629 54.256 1.00 38.29 N ANISOU 982 N VAL A 131 5103 5532 3913 199 186 -23 N ATOM 983 CA VAL A 131 42.633 -2.268 54.182 1.00 37.37 C ANISOU 983 CA VAL A 131 4978 5404 3818 252 115 -123 C ATOM 984 C VAL A 131 41.512 -1.345 53.718 1.00 42.20 C ANISOU 984 C VAL A 131 5544 6044 4447 258 129 -193 C ATOM 985 O VAL A 131 41.218 -1.271 52.520 1.00 37.99 O ANISOU 985 O VAL A 131 4992 5445 3997 218 135 -199 O ATOM 986 CB VAL A 131 43.840 -2.155 53.228 1.00 37.15 C ANISOU 986 CB VAL A 131 4965 5260 3889 237 59 -130 C ATOM 987 CG1 VAL A 131 44.411 -0.739 53.267 1.00 34.71 C ANISOU 987 CG1 VAL A 131 4648 4936 3604 287 -17 -226 C ATOM 988 CG2 VAL A 131 44.916 -3.182 53.616 1.00 35.57 C ANISOU 988 CG2 VAL A 131 4806 5031 3678 232 46 -60 C ATOM 989 N LYS A 132 40.876 -0.664 54.674 1.00 40.48 N ANISOU 989 N LYS A 132 5308 5928 4143 313 133 -247 N ATOM 990 CA LYS A 132 39.714 0.169 54.366 1.00 47.50 C ANISOU 990 CA LYS A 132 6152 6859 5039 329 148 -316 C ATOM 991 C LYS A 132 40.086 1.636 54.164 1.00 45.50 C ANISOU 991 C LYS A 132 5895 6569 4825 384 66 -424 C ATOM 992 O LYS A 132 41.217 2.042 54.430 1.00 44.07 O ANISOU 992 O LYS A 132 5743 6344 4657 413 -1 -449 O ATOM 993 CB LYS A 132 38.649 0.027 55.456 1.00 56.98 C ANISOU 993 CB LYS A 132 7325 8201 6125 356 208 -314 C ATOM 994 CG LYS A 132 38.124 -1.390 55.604 1.00 58.00 C ANISOU 994 CG LYS A 132 7451 8363 6223 290 294 -201 C ATOM 995 CD LYS A 132 37.190 -1.516 56.787 1.00 59.05 C ANISOU 995 CD LYS A 132 7557 8647 6233 318 356 -190 C ATOM 996 CE LYS A 132 36.725 -2.953 56.958 1.00 66.42 C ANISOU 996 CE LYS A 132 8489 9604 7143 243 441 -65 C ATOM 997 NZ LYS A 132 35.993 -3.149 58.241 1.00 66.59 N ANISOU 997 NZ LYS A 132 8490 9780 7031 270 505 -36 N ATOM 998 N ALA A 133 39.119 2.427 53.708 1.00 42.63 N ANISOU 998 N ALA A 133 5493 6221 4484 400 68 -488 N ATOM 999 CA ALA A 133 39.363 3.822 53.350 1.00 42.43 C ANISOU 999 CA ALA A 133 5466 6143 4514 446 -11 -585 C ATOM 1000 C ALA A 133 40.094 4.631 54.428 1.00 47.68 C ANISOU 1000 C ALA A 133 6152 6834 5131 520 -82 -655 C ATOM 1001 O ALA A 133 40.992 5.416 54.120 1.00 47.57 O ANISOU 1001 O ALA A 133 6155 6733 5184 534 -160 -698 O ATOM 1002 CB ALA A 133 38.051 4.509 52.953 1.00 46.13 C ANISOU 1002 CB ALA A 133 5890 6648 4990 467 4 -646 C ATOM 1003 N LYS A 134 39.718 4.436 55.687 1.00 48.17 N ANISOU 1003 N LYS A 134 6209 7016 5076 567 -56 -666 N ATOM 1004 CA LYS A 134 40.294 5.227 56.768 1.00 48.44 C ANISOU 1004 CA LYS A 134 6260 7091 5053 649 -126 -746 C ATOM 1005 C LYS A 134 41.789 4.967 56.976 1.00 51.96 C ANISOU 1005 C LYS A 134 6748 7470 5522 640 -180 -716 C ATOM 1006 O LYS A 134 42.487 5.781 57.578 1.00 53.11 O ANISOU 1006 O LYS A 134 6908 7610 5662 699 -261 -793 O ATOM 1007 CB LYS A 134 39.521 5.017 58.072 1.00 52.63 C ANISOU 1007 CB LYS A 134 6776 7783 5440 706 -78 -760 C ATOM 1008 CG LYS A 134 39.432 3.572 58.518 1.00 62.13 C ANISOU 1008 CG LYS A 134 7990 9048 6569 659 7 -638 C ATOM 1009 CD LYS A 134 38.669 3.459 59.824 1.00 71.13 C ANISOU 1009 CD LYS A 134 9112 10356 7559 718 56 -650 C ATOM 1010 CE LYS A 134 38.666 2.034 60.344 1.00 72.59 C ANISOU 1010 CE LYS A 134 9315 10598 7670 670 136 -518 C ATOM 1011 NZ LYS A 134 38.074 1.960 61.709 1.00 76.70 N ANISOU 1011 NZ LYS A 134 9823 11290 8031 733 180 -524 N ATOM 1012 N SER A 135 42.280 3.843 56.463 1.00 42.17 N ANISOU 1012 N SER A 135 5526 6180 4315 570 -140 -611 N ATOM 1013 CA SER A 135 43.675 3.464 56.662 1.00 46.79 C ANISOU 1013 CA SER A 135 6147 6712 4920 563 -186 -578 C ATOM 1014 C SER A 135 44.552 3.815 55.470 1.00 48.65 C ANISOU 1014 C SER A 135 6384 6811 5289 518 -234 -579 C ATOM 1015 O SER A 135 45.776 3.742 55.553 1.00 46.42 O ANISOU 1015 O SER A 135 6120 6478 5038 516 -285 -570 O ATOM 1016 CB SER A 135 43.786 1.967 56.945 1.00 52.62 C ANISOU 1016 CB SER A 135 6907 7481 5605 522 -119 -462 C ATOM 1017 OG SER A 135 43.198 1.644 58.187 1.00 58.82 O ANISOU 1017 OG SER A 135 7695 8396 6258 566 -81 -451 O ATOM 1018 N ILE A 136 43.923 4.180 54.356 1.00 44.17 N ANISOU 1018 N ILE A 136 5794 6191 4797 483 -217 -586 N ATOM 1019 CA ILE A 136 44.653 4.496 53.134 1.00 38.31 C ANISOU 1019 CA ILE A 136 5052 5328 4175 437 -252 -577 C ATOM 1020 C ILE A 136 45.019 5.975 53.106 1.00 42.92 C ANISOU 1020 C ILE A 136 5630 5862 4814 476 -340 -673 C ATOM 1021 O ILE A 136 44.187 6.829 52.794 1.00 40.81 O ANISOU 1021 O ILE A 136 5347 5592 4568 496 -350 -729 O ATOM 1022 CB ILE A 136 43.827 4.145 51.894 1.00 38.48 C ANISOU 1022 CB ILE A 136 5056 5317 4248 382 -194 -535 C ATOM 1023 CG1 ILE A 136 43.435 2.667 51.937 1.00 39.10 C ANISOU 1023 CG1 ILE A 136 5139 5436 4281 340 -112 -443 C ATOM 1024 CG2 ILE A 136 44.608 4.490 50.630 1.00 42.75 C ANISOU 1024 CG2 ILE A 136 5598 5744 4903 340 -227 -521 C ATOM 1025 CD1 ILE A 136 42.518 2.240 50.797 1.00 36.38 C ANISOU 1025 CD1 ILE A 136 4774 5068 3981 288 -55 -408 C ATOM 1026 N VAL A 137 46.278 6.258 53.423 1.00 48.08 N ANISOU 1026 N VAL A 137 6296 6473 5499 486 -407 -690 N ATOM 1027 CA VAL A 137 46.730 7.609 53.711 1.00 51.32 C ANISOU 1027 CA VAL A 137 6703 6843 5954 528 -501 -786 C ATOM 1028 C VAL A 137 47.925 8.027 52.864 1.00 52.19 C ANISOU 1028 C VAL A 137 6810 6837 6184 482 -554 -773 C ATOM 1029 O VAL A 137 48.163 9.221 52.656 1.00 52.84 O ANISOU 1029 O VAL A 137 6884 6853 6339 493 -625 -837 O ATOM 1030 CB VAL A 137 47.121 7.726 55.200 1.00 54.43 C ANISOU 1030 CB VAL A 137 7109 7313 6259 599 -548 -843 C ATOM 1031 CG1 VAL A 137 48.075 8.884 55.420 1.00 66.49 C ANISOU 1031 CG1 VAL A 137 8634 8773 7857 625 -658 -928 C ATOM 1032 CG2 VAL A 137 45.871 7.863 56.058 1.00 55.32 C ANISOU 1032 CG2 VAL A 137 7217 7541 6262 661 -517 -892 C ATOM 1033 N PHE A 138 48.666 7.041 52.367 1.00 43.87 N ANISOU 1033 N PHE A 138 5759 5758 5153 430 -519 -689 N ATOM 1034 CA PHE A 138 49.930 7.309 51.695 1.00 42.77 C ANISOU 1034 CA PHE A 138 5609 5528 5115 388 -564 -673 C ATOM 1035 C PHE A 138 49.815 8.346 50.580 1.00 43.96 C ANISOU 1035 C PHE A 138 5744 5588 5369 356 -588 -688 C ATOM 1036 O PHE A 138 50.697 9.193 50.425 1.00 42.19 O ANISOU 1036 O PHE A 138 5508 5294 5227 345 -657 -718 O ATOM 1037 CB PHE A 138 50.557 6.016 51.160 1.00 43.72 C ANISOU 1037 CB PHE A 138 5730 5640 5241 340 -510 -579 C ATOM 1038 CG PHE A 138 51.892 6.224 50.509 1.00 44.74 C ANISOU 1038 CG PHE A 138 5840 5692 5467 301 -550 -561 C ATOM 1039 CD1 PHE A 138 53.037 6.354 51.276 1.00 52.20 C ANISOU 1039 CD1 PHE A 138 6778 6636 6418 322 -614 -591 C ATOM 1040 CD2 PHE A 138 51.999 6.314 49.131 1.00 41.79 C ANISOU 1040 CD2 PHE A 138 5450 5253 5174 244 -523 -516 C ATOM 1041 CE1 PHE A 138 54.265 6.557 50.682 1.00 50.55 C ANISOU 1041 CE1 PHE A 138 6541 6364 6302 283 -649 -576 C ATOM 1042 CE2 PHE A 138 53.227 6.516 48.530 1.00 39.51 C ANISOU 1042 CE2 PHE A 138 5137 4905 4971 207 -553 -497 C ATOM 1043 CZ PHE A 138 54.359 6.635 49.306 1.00 41.92 C ANISOU 1043 CZ PHE A 138 5429 5210 5287 223 -614 -526 C ATOM 1044 N HIS A 139 48.742 8.273 49.794 1.00 39.11 N ANISOU 1044 N HIS A 139 5130 4975 4755 339 -534 -663 N ATOM 1045 CA HIS A 139 48.575 9.207 48.691 1.00 40.00 C ANISOU 1045 CA HIS A 139 5235 5005 4959 312 -555 -668 C ATOM 1046 C HIS A 139 48.489 10.632 49.213 1.00 44.83 C ANISOU 1046 C HIS A 139 5848 5583 5603 357 -642 -762 C ATOM 1047 O HIS A 139 49.113 11.537 48.667 1.00 48.49 O ANISOU 1047 O HIS A 139 6305 5955 6163 332 -697 -772 O ATOM 1048 CB HIS A 139 47.339 8.862 47.852 1.00 40.73 C ANISOU 1048 CB HIS A 139 5327 5115 5032 298 -486 -635 C ATOM 1049 CG HIS A 139 46.069 8.818 48.640 1.00 41.12 C ANISOU 1049 CG HIS A 139 5379 5251 4995 350 -463 -682 C ATOM 1050 ND1 HIS A 139 45.034 9.704 48.430 1.00 45.20 N ANISOU 1050 ND1 HIS A 139 5890 5764 5520 382 -479 -736 N ATOM 1051 CD2 HIS A 139 45.667 7.999 49.641 1.00 39.94 C ANISOU 1051 CD2 HIS A 139 5232 5197 4746 378 -423 -680 C ATOM 1052 CE1 HIS A 139 44.049 9.431 49.267 1.00 39.26 C ANISOU 1052 CE1 HIS A 139 5132 5108 4677 427 -448 -771 C ATOM 1053 NE2 HIS A 139 44.407 8.399 50.011 1.00 48.92 N ANISOU 1053 NE2 HIS A 139 6361 6394 5833 423 -411 -734 N ATOM 1054 N ARG A 140 47.726 10.822 50.282 1.00 49.78 N ANISOU 1054 N ARG A 140 6481 6283 6150 424 -654 -832 N ATOM 1055 CA ARG A 140 47.559 12.151 50.864 1.00 59.86 C ANISOU 1055 CA ARG A 140 7760 7534 7450 480 -741 -936 C ATOM 1056 C ARG A 140 48.892 12.702 51.362 1.00 65.96 C ANISOU 1056 C ARG A 140 8530 8252 8281 479 -828 -974 C ATOM 1057 O ARG A 140 49.174 13.893 51.213 1.00 60.45 O ANISOU 1057 O ARG A 140 7830 7468 7669 483 -910 -1029 O ATOM 1058 CB ARG A 140 46.519 12.123 51.986 1.00 60.48 C ANISOU 1058 CB ARG A 140 7842 7723 7414 559 -730 -1006 C ATOM 1059 CG ARG A 140 45.104 11.868 51.488 1.00 62.35 C ANISOU 1059 CG ARG A 140 8072 8008 7612 564 -659 -989 C ATOM 1060 CD ARG A 140 44.094 11.927 52.616 1.00 65.73 C ANISOU 1060 CD ARG A 140 8494 8553 7929 643 -647 -1062 C ATOM 1061 NE ARG A 140 44.089 13.228 53.279 1.00 63.97 N ANISOU 1061 NE ARG A 140 8273 8310 7721 716 -745 -1181 N ATOM 1062 CZ ARG A 140 43.332 13.522 54.330 1.00 66.34 C ANISOU 1062 CZ ARG A 140 8566 8710 7929 800 -755 -1268 C ATOM 1063 NH1 ARG A 140 42.518 12.608 54.836 1.00 65.66 N ANISOU 1063 NH1 ARG A 140 8468 8752 7728 816 -668 -1239 N ATOM 1064 NH2 ARG A 140 43.386 14.730 54.875 1.00 68.34 N ANISOU 1064 NH2 ARG A 140 8824 8935 8207 870 -853 -1384 N ATOM 1065 N LYS A 141 49.709 11.820 51.936 1.00 67.10 N ANISOU 1065 N LYS A 141 8672 8442 8381 472 -815 -943 N ATOM 1066 CA LYS A 141 51.038 12.182 52.420 1.00 67.25 C ANISOU 1066 CA LYS A 141 8682 8420 8451 470 -894 -975 C ATOM 1067 C LYS A 141 51.951 12.625 51.281 1.00 66.35 C ANISOU 1067 C LYS A 141 8548 8190 8472 393 -917 -928 C ATOM 1068 O LYS A 141 52.884 13.398 51.492 1.00 69.36 O ANISOU 1068 O LYS A 141 8914 8507 8932 385 -1001 -972 O ATOM 1069 CB LYS A 141 51.688 11.005 53.162 1.00 64.58 C ANISOU 1069 CB LYS A 141 8347 8158 8034 478 -867 -939 C ATOM 1070 CG LYS A 141 51.194 10.784 54.587 1.00 66.41 C ANISOU 1070 CG LYS A 141 8595 8501 8136 562 -876 -1000 C ATOM 1071 CD LYS A 141 51.728 9.471 55.153 1.00 72.52 C ANISOU 1071 CD LYS A 141 9379 9347 8828 564 -835 -938 C ATOM 1072 CE LYS A 141 51.412 9.321 56.641 1.00 75.43 C ANISOU 1072 CE LYS A 141 9766 9829 9066 650 -853 -996 C ATOM 1073 NZ LYS A 141 51.881 8.012 57.197 1.00 71.89 N ANISOU 1073 NZ LYS A 141 9334 9448 8534 654 -812 -925 N ATOM 1074 N LYS A 142 51.684 12.141 50.072 1.00 57.99 N ANISOU 1074 N LYS A 142 7486 7107 7439 336 -843 -840 N ATOM 1075 CA LYS A 142 52.604 12.381 48.966 1.00 41.67 C ANISOU 1075 CA LYS A 142 5398 4951 5483 262 -848 -779 C ATOM 1076 C LYS A 142 51.977 13.019 47.722 1.00 54.98 C ANISOU 1076 C LYS A 142 7089 6568 7234 227 -830 -745 C ATOM 1077 O LYS A 142 52.575 13.011 46.644 1.00 54.12 O ANISOU 1077 O LYS A 142 6963 6404 7196 163 -809 -674 O ATOM 1078 CB LYS A 142 53.327 11.084 48.611 1.00 50.10 C ANISOU 1078 CB LYS A 142 6452 6053 6529 222 -784 -695 C ATOM 1079 CG LYS A 142 53.971 10.422 49.811 1.00 59.63 C ANISOU 1079 CG LYS A 142 7659 7326 7672 260 -805 -722 C ATOM 1080 CD LYS A 142 55.223 9.677 49.412 1.00 69.11 C ANISOU 1080 CD LYS A 142 8833 8516 8909 215 -789 -660 C ATOM 1081 CE LYS A 142 56.366 10.630 49.114 1.00 73.42 C ANISOU 1081 CE LYS A 142 9341 8981 9575 175 -861 -678 C ATOM 1082 NZ LYS A 142 57.159 10.948 50.330 1.00 74.99 N ANISOU 1082 NZ LYS A 142 9528 9193 9772 213 -947 -754 N ATOM 1083 N ASN A 143 50.781 13.574 47.878 1.00 59.70 N ANISOU 1083 N ASN A 143 7706 7175 7802 274 -839 -796 N ATOM 1084 CA ASN A 143 50.121 14.292 46.792 1.00 72.19 C ANISOU 1084 CA ASN A 143 9296 8690 9441 254 -835 -774 C ATOM 1085 C ASN A 143 49.770 13.388 45.600 1.00 67.97 C ANISOU 1085 C ASN A 143 8761 8176 8889 209 -740 -676 C ATOM 1086 O ASN A 143 49.809 13.823 44.450 1.00 78.24 O ANISOU 1086 O ASN A 143 10061 9410 10256 167 -734 -625 O ATOM 1087 CB ASN A 143 51.000 15.464 46.338 1.00 82.79 C ANISOU 1087 CB ASN A 143 10630 9913 10913 213 -912 -775 C ATOM 1088 CG ASN A 143 50.239 16.779 46.260 1.00 85.59 C ANISOU 1088 CG ASN A 143 11005 10198 11318 248 -980 -836 C ATOM 1089 OD1 ASN A 143 49.031 16.830 46.492 1.00 85.50 O ANISOU 1089 OD1 ASN A 143 11011 10233 11243 306 -966 -881 O ATOM 1090 ND2 ASN A 143 50.951 17.854 45.937 1.00 88.41 N ANISOU 1090 ND2 ASN A 143 11358 10441 11793 212 -1054 -838 N ATOM 1091 N LEU A 144 49.436 12.129 45.884 1.00 60.32 N ANISOU 1091 N LEU A 144 7793 7298 7829 218 -669 -650 N ATOM 1092 CA LEU A 144 49.049 11.161 44.851 1.00 52.85 C ANISOU 1092 CA LEU A 144 6845 6376 6860 182 -582 -570 C ATOM 1093 C LEU A 144 47.538 11.016 44.814 1.00 50.15 C ANISOU 1093 C LEU A 144 6514 6086 6456 218 -544 -592 C ATOM 1094 O LEU A 144 46.860 11.289 45.801 1.00 50.63 O ANISOU 1094 O LEU A 144 6579 6192 6464 274 -565 -662 O ATOM 1095 CB LEU A 144 49.644 9.786 45.158 1.00 50.23 C ANISOU 1095 CB LEU A 144 6506 6103 6476 166 -531 -525 C ATOM 1096 CG LEU A 144 51.067 9.416 44.728 1.00 59.15 C ANISOU 1096 CG LEU A 144 7616 7200 7659 117 -531 -472 C ATOM 1097 CD1 LEU A 144 52.002 10.607 44.772 1.00 59.01 C ANISOU 1097 CD1 LEU A 144 7583 7106 7732 101 -610 -498 C ATOM 1098 CD2 LEU A 144 51.599 8.276 45.590 1.00 62.40 C ANISOU 1098 CD2 LEU A 144 8026 7673 8008 131 -512 -463 C ATOM 1099 N GLN A 145 47.005 10.548 43.691 1.00 43.33 N ANISOU 1099 N GLN A 145 5649 5221 5593 190 -487 -535 N ATOM 1100 CA GLN A 145 45.577 10.278 43.611 1.00 34.20 C ANISOU 1100 CA GLN A 145 4495 4120 4380 219 -446 -553 C ATOM 1101 C GLN A 145 45.348 8.813 43.978 1.00 33.48 C ANISOU 1101 C GLN A 145 4398 4110 4213 209 -374 -520 C ATOM 1102 O GLN A 145 46.167 7.977 43.661 1.00 36.15 O ANISOU 1102 O GLN A 145 4734 4442 4558 171 -345 -462 O ATOM 1103 CB GLN A 145 45.063 10.570 42.204 1.00 36.75 C ANISOU 1103 CB GLN A 145 4819 4400 4744 197 -430 -515 C ATOM 1104 CG GLN A 145 43.642 10.113 41.953 1.00 37.39 C ANISOU 1104 CG GLN A 145 4894 4541 4771 219 -382 -526 C ATOM 1105 CD GLN A 145 42.620 10.965 42.668 1.00 49.07 C ANISOU 1105 CD GLN A 145 6373 6045 6228 282 -419 -610 C ATOM 1106 OE1 GLN A 145 42.770 12.186 42.760 1.00 53.22 O ANISOU 1106 OE1 GLN A 145 6910 6509 6803 308 -490 -654 O ATOM 1107 NE2 GLN A 145 41.569 10.327 43.178 1.00 46.76 N ANISOU 1107 NE2 GLN A 145 6064 5840 5863 307 -373 -636 N ATOM 1108 N TYR A 146 44.268 8.521 44.691 1.00 35.98 N ANISOU 1108 N TYR A 146 4711 4503 4459 246 -347 -557 N ATOM 1109 CA TYR A 146 43.960 7.142 45.041 1.00 39.99 C ANISOU 1109 CA TYR A 146 5214 5082 4899 232 -278 -518 C ATOM 1110 C TYR A 146 42.623 6.692 44.417 1.00 37.81 C ANISOU 1110 C TYR A 146 4923 4844 4600 226 -223 -507 C ATOM 1111 O TYR A 146 41.683 7.488 44.361 1.00 32.02 O ANISOU 1111 O TYR A 146 4180 4121 3865 260 -240 -559 O ATOM 1112 CB TYR A 146 43.930 6.956 46.567 1.00 36.96 C ANISOU 1112 CB TYR A 146 4832 4770 4439 273 -284 -556 C ATOM 1113 CG TYR A 146 43.431 5.596 46.898 1.00 31.71 C ANISOU 1113 CG TYR A 146 4165 4177 3708 256 -211 -508 C ATOM 1114 CD1 TYR A 146 44.272 4.497 46.801 1.00 31.52 C ANISOU 1114 CD1 TYR A 146 4151 4140 3684 218 -184 -441 C ATOM 1115 CD2 TYR A 146 42.096 5.385 47.224 1.00 34.45 C ANISOU 1115 CD2 TYR A 146 4493 4598 3996 275 -167 -528 C ATOM 1116 CE1 TYR A 146 43.804 3.220 47.037 1.00 32.98 C ANISOU 1116 CE1 TYR A 146 4336 4376 3817 197 -120 -391 C ATOM 1117 CE2 TYR A 146 41.622 4.115 47.467 1.00 32.53 C ANISOU 1117 CE2 TYR A 146 4245 4413 3702 248 -98 -475 C ATOM 1118 CZ TYR A 146 42.485 3.033 47.371 1.00 32.76 C ANISOU 1118 CZ TYR A 146 4292 4418 3737 208 -76 -405 C ATOM 1119 OH TYR A 146 42.029 1.758 47.590 1.00 30.68 O ANISOU 1119 OH TYR A 146 4028 4198 3433 179 -13 -348 O ATOM 1120 N TYR A 147 42.555 5.441 43.937 1.00 32.83 N ANISOU 1120 N TYR A 147 4289 4230 3957 184 -163 -446 N ATOM 1121 CA TYR A 147 41.283 4.778 43.565 1.00 27.05 C ANISOU 1121 CA TYR A 147 3537 3544 3195 174 -106 -438 C ATOM 1122 C TYR A 147 41.194 3.354 44.106 1.00 34.21 C ANISOU 1122 C TYR A 147 4443 4502 4054 147 -48 -391 C ATOM 1123 O TYR A 147 42.168 2.615 44.056 1.00 31.78 O ANISOU 1123 O TYR A 147 4151 4167 3757 120 -42 -343 O ATOM 1124 CB TYR A 147 41.055 4.706 42.028 1.00 27.97 C ANISOU 1124 CB TYR A 147 3650 3615 3364 145 -95 -410 C ATOM 1125 CG TYR A 147 40.889 6.067 41.390 1.00 29.37 C ANISOU 1125 CG TYR A 147 3829 3744 3585 171 -147 -446 C ATOM 1126 CD1 TYR A 147 39.724 6.795 41.557 1.00 31.88 C ANISOU 1126 CD1 TYR A 147 4132 4093 3889 212 -161 -504 C ATOM 1127 CD2 TYR A 147 41.921 6.635 40.655 1.00 34.52 C ANISOU 1127 CD2 TYR A 147 4499 4321 4297 154 -183 -420 C ATOM 1128 CE1 TYR A 147 39.586 8.065 40.995 1.00 35.38 C ANISOU 1128 CE1 TYR A 147 4584 4483 4377 241 -216 -536 C ATOM 1129 CE2 TYR A 147 41.788 7.885 40.078 1.00 34.67 C ANISOU 1129 CE2 TYR A 147 4524 4288 4360 174 -232 -443 C ATOM 1130 CZ TYR A 147 40.624 8.595 40.252 1.00 37.95 C ANISOU 1130 CZ TYR A 147 4932 4726 4763 219 -251 -501 C ATOM 1131 OH TYR A 147 40.512 9.847 39.691 1.00 37.50 O ANISOU 1131 OH TYR A 147 4887 4607 4754 242 -307 -521 O ATOM 1132 N ASP A 148 40.015 2.981 44.601 1.00 32.71 N ANISOU 1132 N ASP A 148 4231 4385 3814 154 -7 -404 N ATOM 1133 CA ASP A 148 39.659 1.588 44.770 1.00 30.12 C ANISOU 1133 CA ASP A 148 3896 4093 3456 114 55 -350 C ATOM 1134 C ASP A 148 39.465 1.016 43.363 1.00 30.07 C ANISOU 1134 C ASP A 148 3883 4039 3505 72 75 -319 C ATOM 1135 O ASP A 148 38.886 1.682 42.493 1.00 31.53 O ANISOU 1135 O ASP A 148 4052 4207 3721 82 60 -351 O ATOM 1136 CB ASP A 148 38.305 1.461 45.475 1.00 36.68 C ANISOU 1136 CB ASP A 148 4694 5015 4229 127 97 -373 C ATOM 1137 CG ASP A 148 38.397 1.503 46.990 1.00 39.08 C ANISOU 1137 CG ASP A 148 5003 5392 4455 161 102 -383 C ATOM 1138 OD1 ASP A 148 39.514 1.492 47.547 1.00 37.60 O ANISOU 1138 OD1 ASP A 148 4848 5181 4257 172 73 -368 O ATOM 1139 OD2 ASP A 148 37.322 1.524 47.628 1.00 41.04 O ANISOU 1139 OD2 ASP A 148 5219 5726 4648 177 137 -406 O ATOM 1140 N ILE A 149 39.938 -0.205 43.134 1.00 33.48 N ANISOU 1140 N ILE A 149 4327 4446 3946 31 103 -260 N ATOM 1141 CA ILE A 149 39.639 -0.893 41.871 1.00 28.05 C ANISOU 1141 CA ILE A 149 3631 3724 3303 -5 124 -238 C ATOM 1142 C ILE A 149 39.328 -2.357 42.131 1.00 28.67 C ANISOU 1142 C ILE A 149 3707 3816 3370 -47 171 -189 C ATOM 1143 O ILE A 149 39.538 -2.867 43.225 1.00 28.23 O ANISOU 1143 O ILE A 149 3665 3789 3274 -50 188 -159 O ATOM 1144 CB ILE A 149 40.793 -0.793 40.847 1.00 36.07 C ANISOU 1144 CB ILE A 149 4668 4668 4369 -11 94 -220 C ATOM 1145 CG1 ILE A 149 42.070 -1.414 41.411 1.00 39.88 C ANISOU 1145 CG1 ILE A 149 5177 5128 4847 -18 88 -180 C ATOM 1146 CG2 ILE A 149 41.018 0.664 40.419 1.00 35.39 C ANISOU 1146 CG2 ILE A 149 4582 4558 4306 21 48 -259 C ATOM 1147 CD1 ILE A 149 43.219 -1.514 40.412 1.00 39.74 C ANISOU 1147 CD1 ILE A 149 5172 5052 4877 -26 68 -159 C ATOM 1148 N SER A 150 38.766 -3.013 41.128 1.00 31.98 N ANISOU 1148 N SER A 150 4110 4214 3825 -79 190 -181 N ATOM 1149 CA SER A 150 38.649 -4.466 41.127 1.00 30.25 C ANISOU 1149 CA SER A 150 3895 3982 3618 -125 225 -133 C ATOM 1150 C SER A 150 38.907 -4.904 39.701 1.00 29.95 C ANISOU 1150 C SER A 150 3860 3885 3634 -139 212 -134 C ATOM 1151 O SER A 150 38.054 -4.767 38.827 1.00 31.62 O ANISOU 1151 O SER A 150 4044 4102 3868 -145 214 -165 O ATOM 1152 CB SER A 150 37.273 -4.923 41.639 1.00 27.44 C ANISOU 1152 CB SER A 150 3502 3684 3240 -152 270 -131 C ATOM 1153 OG SER A 150 36.979 -6.244 41.190 1.00 34.46 O ANISOU 1153 OG SER A 150 4387 4540 4166 -204 294 -94 O ATOM 1154 N ALA A 151 40.119 -5.383 39.453 1.00 28.54 N ANISOU 1154 N ALA A 151 3713 3657 3475 -139 196 -105 N ATOM 1155 CA ALA A 151 40.494 -5.838 38.134 1.00 34.48 C ANISOU 1155 CA ALA A 151 4469 4361 4270 -145 184 -107 C ATOM 1156 C ALA A 151 39.489 -6.871 37.599 1.00 38.60 C ANISOU 1156 C ALA A 151 4971 4877 4820 -182 207 -109 C ATOM 1157 O ALA A 151 39.065 -6.792 36.445 1.00 35.76 O ANISOU 1157 O ALA A 151 4595 4509 4485 -179 198 -141 O ATOM 1158 CB ALA A 151 41.920 -6.411 38.151 1.00 31.49 C ANISOU 1158 CB ALA A 151 4123 3940 3904 -139 169 -74 C ATOM 1159 N LYS A 152 39.095 -7.822 38.445 1.00 32.58 N ANISOU 1159 N LYS A 152 4209 4118 4051 -216 234 -74 N ATOM 1160 CA LYS A 152 38.224 -8.923 38.021 1.00 38.95 C ANISOU 1160 CA LYS A 152 4997 4906 4895 -261 253 -69 C ATOM 1161 C LYS A 152 36.820 -8.509 37.585 1.00 34.36 C ANISOU 1161 C LYS A 152 4366 4368 4320 -272 265 -113 C ATOM 1162 O LYS A 152 36.172 -9.235 36.828 1.00 36.92 O ANISOU 1162 O LYS A 152 4669 4671 4687 -301 266 -129 O ATOM 1163 CB LYS A 152 38.119 -9.970 39.133 1.00 42.05 C ANISOU 1163 CB LYS A 152 5402 5292 5281 -300 281 -10 C ATOM 1164 CG LYS A 152 39.341 -10.850 39.264 1.00 50.66 C ANISOU 1164 CG LYS A 152 6540 6321 6387 -297 263 33 C ATOM 1165 CD LYS A 152 39.386 -11.897 38.168 1.00 61.07 C ANISOU 1165 CD LYS A 152 7863 7573 7769 -315 247 22 C ATOM 1166 CE LYS A 152 40.328 -13.030 38.541 1.00 66.50 C ANISOU 1166 CE LYS A 152 8595 8197 8476 -320 234 72 C ATOM 1167 NZ LYS A 152 39.887 -13.718 39.789 1.00 73.96 N ANISOU 1167 NZ LYS A 152 9551 9144 9406 -361 264 138 N ATOM 1168 N SER A 153 36.349 -7.356 38.067 1.00 33.88 N ANISOU 1168 N SER A 153 4285 4367 4221 -246 269 -139 N ATOM 1169 CA SER A 153 35.022 -6.844 37.705 1.00 36.09 C ANISOU 1169 CA SER A 153 4515 4695 4504 -246 276 -187 C ATOM 1170 C SER A 153 35.063 -5.579 36.814 1.00 38.64 C ANISOU 1170 C SER A 153 4835 5024 4824 -195 240 -239 C ATOM 1171 O SER A 153 34.019 -5.031 36.440 1.00 33.39 O ANISOU 1171 O SER A 153 4131 4397 4160 -183 236 -284 O ATOM 1172 CB SER A 153 34.212 -6.558 38.971 1.00 38.87 C ANISOU 1172 CB SER A 153 4836 5121 4813 -254 312 -181 C ATOM 1173 OG SER A 153 34.780 -5.481 39.703 1.00 41.37 O ANISOU 1173 OG SER A 153 5174 5464 5081 -206 298 -190 O ATOM 1174 N ASN A 154 36.266 -5.123 36.475 1.00 33.43 N ANISOU 1174 N ASN A 154 4214 4325 4161 -165 211 -229 N ATOM 1175 CA ASN A 154 36.429 -3.884 35.715 1.00 33.26 C ANISOU 1175 CA ASN A 154 4198 4303 4138 -121 177 -263 C ATOM 1176 C ASN A 154 36.070 -2.636 36.522 1.00 31.50 C ANISOU 1176 C ASN A 154 3965 4121 3883 -87 169 -289 C ATOM 1177 O ASN A 154 35.997 -1.518 35.977 1.00 30.41 O ANISOU 1177 O ASN A 154 3827 3980 3745 -50 137 -319 O ATOM 1178 CB ASN A 154 35.615 -3.941 34.423 1.00 32.91 C ANISOU 1178 CB ASN A 154 4128 4259 4118 -117 165 -300 C ATOM 1179 CG ASN A 154 36.108 -5.003 33.486 1.00 37.03 C ANISOU 1179 CG ASN A 154 4664 4738 4669 -135 162 -286 C ATOM 1180 OD1 ASN A 154 37.277 -5.388 33.528 1.00 30.84 O ANISOU 1180 OD1 ASN A 154 3913 3916 3888 -137 160 -253 O ATOM 1181 ND2 ASN A 154 35.227 -5.477 32.613 1.00 35.26 N ANISOU 1181 ND2 ASN A 154 4411 4518 4467 -144 157 -320 N ATOM 1182 N TYR A 155 35.854 -2.820 37.822 1.00 28.79 N ANISOU 1182 N TYR A 155 3614 3816 3508 -98 194 -276 N ATOM 1183 CA TYR A 155 35.427 -1.689 38.645 1.00 31.29 C ANISOU 1183 CA TYR A 155 3918 4181 3790 -59 185 -312 C ATOM 1184 C TYR A 155 36.485 -0.585 38.678 1.00 33.73 C ANISOU 1184 C TYR A 155 4262 4455 4098 -20 141 -318 C ATOM 1185 O TYR A 155 37.636 -0.802 39.086 1.00 31.12 O ANISOU 1185 O TYR A 155 3964 4094 3765 -26 135 -284 O ATOM 1186 CB TYR A 155 35.044 -2.135 40.061 1.00 35.31 C ANISOU 1186 CB TYR A 155 4412 4748 4255 -74 225 -295 C ATOM 1187 CG TYR A 155 34.722 -0.993 41.013 1.00 30.07 C ANISOU 1187 CG TYR A 155 3738 4142 3547 -25 213 -338 C ATOM 1188 CD1 TYR A 155 33.595 -0.204 40.832 1.00 37.27 C ANISOU 1188 CD1 TYR A 155 4608 5100 4454 6 206 -397 C ATOM 1189 CD2 TYR A 155 35.546 -0.715 42.097 1.00 33.87 C ANISOU 1189 CD2 TYR A 155 4248 4631 3989 -4 204 -325 C ATOM 1190 CE1 TYR A 155 33.303 0.846 41.702 1.00 41.42 C ANISOU 1190 CE1 TYR A 155 5123 5676 4937 59 191 -446 C ATOM 1191 CE2 TYR A 155 35.263 0.317 42.961 1.00 35.65 C ANISOU 1191 CE2 TYR A 155 4463 4908 4172 47 187 -374 C ATOM 1192 CZ TYR A 155 34.141 1.095 42.766 1.00 40.16 C ANISOU 1192 CZ TYR A 155 4994 5523 4740 79 181 -435 C ATOM 1193 OH TYR A 155 33.870 2.128 43.648 1.00 41.85 O ANISOU 1193 OH TYR A 155 5199 5789 4913 137 160 -492 O ATOM 1194 N ASN A 156 36.071 0.600 38.239 1.00 31.65 N ANISOU 1194 N ASN A 156 3991 4193 3841 20 108 -363 N ATOM 1195 CA ASN A 156 36.931 1.778 38.233 1.00 30.42 C ANISOU 1195 CA ASN A 156 3864 3998 3694 54 61 -373 C ATOM 1196 C ASN A 156 38.139 1.635 37.309 1.00 28.14 C ANISOU 1196 C ASN A 156 3607 3644 3440 38 45 -331 C ATOM 1197 O ASN A 156 39.128 2.348 37.459 1.00 31.84 O ANISOU 1197 O ASN A 156 4100 4078 3922 50 14 -322 O ATOM 1198 CB ASN A 156 37.366 2.151 39.655 1.00 29.48 C ANISOU 1198 CB ASN A 156 3756 3902 3542 73 54 -381 C ATOM 1199 CG ASN A 156 36.381 3.080 40.336 1.00 35.85 C ANISOU 1199 CG ASN A 156 4538 4762 4320 118 40 -444 C ATOM 1200 OD1 ASN A 156 35.412 3.533 39.722 1.00 34.48 O ANISOU 1200 OD1 ASN A 156 4341 4602 4158 138 32 -480 O ATOM 1201 ND2 ASN A 156 36.633 3.387 41.606 1.00 33.22 N ANISOU 1201 ND2 ASN A 156 4210 4462 3948 142 34 -461 N ATOM 1202 N PHE A 157 38.045 0.731 36.333 1.00 29.79 N ANISOU 1202 N PHE A 157 3812 3842 3666 11 66 -309 N ATOM 1203 CA PHE A 157 39.190 0.456 35.461 1.00 28.25 C ANISOU 1203 CA PHE A 157 3640 3598 3494 -1 58 -271 C ATOM 1204 C PHE A 157 39.787 1.723 34.834 1.00 30.12 C ANISOU 1204 C PHE A 157 3894 3800 3751 24 19 -269 C ATOM 1205 O PHE A 157 41.008 1.909 34.811 1.00 30.37 O ANISOU 1205 O PHE A 157 3943 3798 3797 17 7 -239 O ATOM 1206 CB PHE A 157 38.831 -0.556 34.344 1.00 28.46 C ANISOU 1206 CB PHE A 157 3657 3623 3534 -20 78 -264 C ATOM 1207 CG PHE A 157 39.976 -0.820 33.410 1.00 29.68 C ANISOU 1207 CG PHE A 157 3831 3740 3705 -24 72 -231 C ATOM 1208 CD1 PHE A 157 40.979 -1.713 33.773 1.00 29.73 C ANISOU 1208 CD1 PHE A 157 3851 3728 3716 -44 86 -199 C ATOM 1209 CD2 PHE A 157 40.077 -0.151 32.194 1.00 28.43 C ANISOU 1209 CD2 PHE A 157 3678 3570 3554 -4 53 -231 C ATOM 1210 CE1 PHE A 157 42.056 -1.923 32.954 1.00 27.37 C ANISOU 1210 CE1 PHE A 157 3564 3406 3430 -42 82 -174 C ATOM 1211 CE2 PHE A 157 41.163 -0.349 31.369 1.00 27.93 C ANISOU 1211 CE2 PHE A 157 3628 3486 3500 -6 53 -198 C ATOM 1212 CZ PHE A 157 42.156 -1.258 31.752 1.00 28.77 C ANISOU 1212 CZ PHE A 157 3741 3579 3611 -25 69 -173 C ATOM 1213 N GLU A 158 38.924 2.588 34.307 1.00 31.26 N ANISOU 1213 N GLU A 158 4030 3949 3898 51 -3 -300 N ATOM 1214 CA GLU A 158 39.390 3.734 33.547 1.00 27.86 C ANISOU 1214 CA GLU A 158 3618 3477 3489 71 -41 -288 C ATOM 1215 C GLU A 158 39.944 4.851 34.431 1.00 31.09 C ANISOU 1215 C GLU A 158 4042 3860 3912 86 -78 -297 C ATOM 1216 O GLU A 158 40.677 5.703 33.944 1.00 31.02 O ANISOU 1216 O GLU A 158 4051 3804 3932 89 -108 -273 O ATOM 1217 CB GLU A 158 38.255 4.299 32.663 1.00 29.14 C ANISOU 1217 CB GLU A 158 3771 3650 3649 101 -59 -317 C ATOM 1218 CG GLU A 158 37.343 5.287 33.394 1.00 35.57 C ANISOU 1218 CG GLU A 158 4576 4479 4461 139 -89 -370 C ATOM 1219 CD GLU A 158 36.393 4.648 34.398 1.00 36.42 C ANISOU 1219 CD GLU A 158 4650 4648 4541 137 -60 -411 C ATOM 1220 OE1 GLU A 158 36.478 3.425 34.660 1.00 39.33 O ANISOU 1220 OE1 GLU A 158 5006 5040 4897 100 -17 -392 O ATOM 1221 OE2 GLU A 158 35.552 5.397 34.946 1.00 38.82 O ANISOU 1221 OE2 GLU A 158 4938 4977 4835 174 -80 -461 O ATOM 1222 N LYS A 159 39.591 4.845 35.717 1.00 30.01 N ANISOU 1222 N LYS A 159 3895 3752 3754 96 -76 -332 N ATOM 1223 CA LYS A 159 39.852 5.997 36.592 1.00 28.19 C ANISOU 1223 CA LYS A 159 3676 3503 3533 124 -120 -362 C ATOM 1224 C LYS A 159 41.319 6.416 36.640 1.00 29.38 C ANISOU 1224 C LYS A 159 3847 3598 3718 106 -146 -327 C ATOM 1225 O LYS A 159 41.636 7.594 36.491 1.00 29.92 O ANISOU 1225 O LYS A 159 3929 3617 3822 121 -194 -333 O ATOM 1226 CB LYS A 159 39.341 5.742 38.017 1.00 33.06 C ANISOU 1226 CB LYS A 159 4277 4175 4108 139 -108 -403 C ATOM 1227 CG LYS A 159 37.834 5.561 38.138 1.00 37.75 C ANISOU 1227 CG LYS A 159 4840 4831 4672 160 -86 -446 C ATOM 1228 CD LYS A 159 37.088 6.865 38.011 1.00 45.15 C ANISOU 1228 CD LYS A 159 5774 5760 5621 211 -133 -500 C ATOM 1229 CE LYS A 159 35.627 6.712 38.420 1.00 50.25 C ANISOU 1229 CE LYS A 159 6378 6483 6230 238 -111 -553 C ATOM 1230 NZ LYS A 159 34.942 5.623 37.656 1.00 54.63 N ANISOU 1230 NZ LYS A 159 6908 7070 6781 204 -64 -532 N ATOM 1231 N PRO A 160 42.221 5.462 36.901 1.00 28.36 N ANISOU 1231 N PRO A 160 3719 3474 3582 76 -118 -292 N ATOM 1232 CA PRO A 160 43.644 5.838 36.993 1.00 29.01 C ANISOU 1232 CA PRO A 160 3811 3511 3699 59 -143 -262 C ATOM 1233 C PRO A 160 44.161 6.420 35.677 1.00 29.79 C ANISOU 1233 C PRO A 160 3917 3563 3840 44 -155 -221 C ATOM 1234 O PRO A 160 44.908 7.386 35.659 1.00 27.49 O ANISOU 1234 O PRO A 160 3631 3223 3590 39 -194 -210 O ATOM 1235 CB PRO A 160 44.333 4.504 37.290 1.00 36.13 C ANISOU 1235 CB PRO A 160 4710 4437 4582 33 -105 -231 C ATOM 1236 CG PRO A 160 43.268 3.683 37.987 1.00 37.41 C ANISOU 1236 CG PRO A 160 4865 4654 4696 42 -72 -256 C ATOM 1237 CD PRO A 160 41.971 4.075 37.336 1.00 26.97 C ANISOU 1237 CD PRO A 160 3533 3346 3369 58 -70 -282 C ATOM 1238 N PHE A 161 43.743 5.834 34.563 1.00 26.47 N ANISOU 1238 N PHE A 161 3493 3159 3407 37 -122 -197 N ATOM 1239 CA PHE A 161 44.181 6.330 33.267 1.00 25.24 C ANISOU 1239 CA PHE A 161 3343 2970 3276 27 -128 -152 C ATOM 1240 C PHE A 161 43.659 7.722 32.995 1.00 27.16 C ANISOU 1240 C PHE A 161 3600 3175 3545 50 -174 -164 C ATOM 1241 O PHE A 161 44.364 8.545 32.426 1.00 28.40 O ANISOU 1241 O PHE A 161 3767 3284 3739 37 -196 -124 O ATOM 1242 CB PHE A 161 43.743 5.350 32.161 1.00 24.24 C ANISOU 1242 CB PHE A 161 3210 2878 3121 25 -87 -135 C ATOM 1243 CG PHE A 161 44.265 3.959 32.398 1.00 25.86 C ANISOU 1243 CG PHE A 161 3405 3112 3309 5 -48 -126 C ATOM 1244 CD1 PHE A 161 45.584 3.650 32.114 1.00 24.65 C ANISOU 1244 CD1 PHE A 161 3247 2948 3171 -16 -36 -85 C ATOM 1245 CD2 PHE A 161 43.465 2.993 32.975 1.00 26.23 C ANISOU 1245 CD2 PHE A 161 3445 3193 3329 7 -25 -157 C ATOM 1246 CE1 PHE A 161 46.084 2.368 32.354 1.00 29.44 C ANISOU 1246 CE1 PHE A 161 3846 3575 3765 -27 -7 -79 C ATOM 1247 CE2 PHE A 161 43.958 1.705 33.222 1.00 30.39 C ANISOU 1247 CE2 PHE A 161 3967 3733 3846 -11 4 -144 C ATOM 1248 CZ PHE A 161 45.268 1.403 32.915 1.00 30.86 C ANISOU 1248 CZ PHE A 161 4027 3779 3920 -24 10 -108 C ATOM 1249 N LEU A 162 42.415 7.981 33.374 1.00 25.17 N ANISOU 1249 N LEU A 162 3348 2942 3274 85 -188 -218 N ATOM 1250 CA LEU A 162 41.841 9.283 33.071 1.00 31.03 C ANISOU 1250 CA LEU A 162 4106 3644 4041 116 -238 -234 C ATOM 1251 C LEU A 162 42.538 10.342 33.927 1.00 30.91 C ANISOU 1251 C LEU A 162 4102 3573 4071 117 -290 -247 C ATOM 1252 O LEU A 162 42.860 11.421 33.435 1.00 27.47 O ANISOU 1252 O LEU A 162 3684 3072 3680 116 -332 -222 O ATOM 1253 CB LEU A 162 40.332 9.288 33.304 1.00 31.50 C ANISOU 1253 CB LEU A 162 4154 3745 4068 159 -242 -296 C ATOM 1254 CG LEU A 162 39.653 10.643 33.128 1.00 39.24 C ANISOU 1254 CG LEU A 162 5151 4685 5074 203 -301 -326 C ATOM 1255 CD1 LEU A 162 39.807 11.143 31.685 1.00 31.52 C ANISOU 1255 CD1 LEU A 162 4196 3666 4116 201 -314 -267 C ATOM 1256 CD2 LEU A 162 38.182 10.527 33.528 1.00 41.22 C ANISOU 1256 CD2 LEU A 162 5379 4992 5290 248 -301 -397 C ATOM 1257 N TRP A 163 42.786 10.029 35.196 1.00 28.15 N ANISOU 1257 N TRP A 163 3742 3245 3708 118 -290 -286 N ATOM 1258 CA TRP A 163 43.485 10.993 36.061 1.00 31.69 C ANISOU 1258 CA TRP A 163 4198 3642 4199 122 -346 -309 C ATOM 1259 C TRP A 163 44.881 11.275 35.494 1.00 30.50 C ANISOU 1259 C TRP A 163 4051 3435 4102 74 -354 -242 C ATOM 1260 O TRP A 163 45.273 12.432 35.356 1.00 30.25 O ANISOU 1260 O TRP A 163 4031 3331 4129 70 -407 -234 O ATOM 1261 CB TRP A 163 43.556 10.512 37.516 1.00 32.70 C ANISOU 1261 CB TRP A 163 4315 3816 4293 135 -343 -360 C ATOM 1262 CG TRP A 163 44.105 11.556 38.467 1.00 31.47 C ANISOU 1262 CG TRP A 163 4168 3614 4176 152 -411 -403 C ATOM 1263 CD1 TRP A 163 43.399 12.515 39.122 1.00 35.21 C ANISOU 1263 CD1 TRP A 163 4649 4076 4654 203 -465 -476 C ATOM 1264 CD2 TRP A 163 45.473 11.734 38.853 1.00 29.36 C ANISOU 1264 CD2 TRP A 163 3898 3307 3951 121 -437 -385 C ATOM 1265 NE1 TRP A 163 44.238 13.289 39.890 1.00 38.45 N ANISOU 1265 NE1 TRP A 163 5065 4435 5108 206 -526 -506 N ATOM 1266 CE2 TRP A 163 45.519 12.826 39.745 1.00 36.07 C ANISOU 1266 CE2 TRP A 163 4755 4117 4831 153 -510 -450 C ATOM 1267 CE3 TRP A 163 46.661 11.078 38.533 1.00 30.79 C ANISOU 1267 CE3 TRP A 163 4066 3484 4147 72 -408 -325 C ATOM 1268 CZ2 TRP A 163 46.700 13.269 40.319 1.00 36.27 C ANISOU 1268 CZ2 TRP A 163 4777 4097 4906 134 -557 -456 C ATOM 1269 CZ3 TRP A 163 47.837 11.519 39.102 1.00 43.42 C ANISOU 1269 CZ3 TRP A 163 5659 5045 5795 53 -451 -328 C ATOM 1270 CH2 TRP A 163 47.851 12.600 39.989 1.00 38.47 C ANISOU 1270 CH2 TRP A 163 5040 4376 5201 81 -525 -393 C ATOM 1271 N LEU A 164 45.614 10.222 35.137 1.00 29.19 N ANISOU 1271 N LEU A 164 3871 3301 3920 39 -303 -195 N ATOM 1272 CA LEU A 164 46.937 10.395 34.530 1.00 26.50 C ANISOU 1272 CA LEU A 164 3521 2922 3624 -7 -301 -130 C ATOM 1273 C LEU A 164 46.921 11.189 33.228 1.00 32.64 C ANISOU 1273 C LEU A 164 4312 3656 4434 -19 -309 -74 C ATOM 1274 O LEU A 164 47.820 11.968 32.961 1.00 29.86 O ANISOU 1274 O LEU A 164 3957 3248 4139 -51 -334 -31 O ATOM 1275 CB LEU A 164 47.619 9.050 34.285 1.00 28.34 C ANISOU 1275 CB LEU A 164 3735 3207 3827 -32 -242 -96 C ATOM 1276 CG LEU A 164 48.110 8.290 35.514 1.00 27.33 C ANISOU 1276 CG LEU A 164 3596 3110 3680 -31 -238 -127 C ATOM 1277 CD1 LEU A 164 48.570 6.911 35.092 1.00 28.98 C ANISOU 1277 CD1 LEU A 164 3790 3363 3857 -47 -181 -94 C ATOM 1278 CD2 LEU A 164 49.243 9.027 36.238 1.00 28.01 C ANISOU 1278 CD2 LEU A 164 3671 3151 3820 -48 -286 -133 C ATOM 1279 N ALA A 165 45.923 10.950 32.392 1.00 27.50 N ANISOU 1279 N ALA A 165 3672 3033 3744 5 -286 -69 N ATOM 1280 CA ALA A 165 45.845 11.646 31.123 1.00 29.02 C ANISOU 1280 CA ALA A 165 3880 3192 3954 0 -293 -11 C ATOM 1281 C ALA A 165 45.666 13.140 31.362 1.00 27.97 C ANISOU 1281 C ALA A 165 3772 2977 3880 12 -364 -21 C ATOM 1282 O ALA A 165 46.313 13.969 30.722 1.00 30.20 O ANISOU 1282 O ALA A 165 4063 3199 4211 -17 -384 43 O ATOM 1283 CB ALA A 165 44.701 11.091 30.294 1.00 28.66 C ANISOU 1283 CB ALA A 165 3842 3197 3852 33 -264 -18 C ATOM 1284 N ARG A 166 44.760 13.481 32.271 1.00 30.81 N ANISOU 1284 N ARG A 166 4139 3333 4234 56 -403 -101 N ATOM 1285 CA ARG A 166 44.509 14.878 32.593 1.00 28.08 C ANISOU 1285 CA ARG A 166 3818 2907 3946 79 -480 -127 C ATOM 1286 C ARG A 166 45.782 15.540 33.086 1.00 31.48 C ANISOU 1286 C ARG A 166 4244 3268 4450 36 -517 -107 C ATOM 1287 O ARG A 166 46.058 16.693 32.759 1.00 32.83 O ANISOU 1287 O ARG A 166 4434 3350 4689 23 -570 -76 O ATOM 1288 CB ARG A 166 43.415 14.987 33.652 1.00 33.78 C ANISOU 1288 CB ARG A 166 4539 3654 4640 139 -509 -230 C ATOM 1289 CG ARG A 166 42.039 14.623 33.099 1.00 32.01 C ANISOU 1289 CG ARG A 166 4316 3485 4360 184 -487 -253 C ATOM 1290 CD ARG A 166 40.955 14.593 34.164 1.00 34.62 C ANISOU 1290 CD ARG A 166 4635 3863 4657 241 -503 -353 C ATOM 1291 NE ARG A 166 39.628 14.512 33.554 1.00 36.81 N ANISOU 1291 NE ARG A 166 4910 4179 4898 285 -496 -377 N ATOM 1292 CZ ARG A 166 38.498 14.331 34.227 1.00 49.54 C ANISOU 1292 CZ ARG A 166 6500 5852 6471 334 -495 -457 C ATOM 1293 NH1 ARG A 166 38.519 14.205 35.546 1.00 53.07 N ANISOU 1293 NH1 ARG A 166 6931 6332 6902 347 -498 -518 N ATOM 1294 NH2 ARG A 166 37.341 14.279 33.579 1.00 52.72 N ANISOU 1294 NH2 ARG A 166 6894 6289 6847 371 -492 -476 N ATOM 1295 N LYS A 167 46.558 14.809 33.874 1.00 30.11 N ANISOU 1295 N LYS A 167 4044 3131 4267 12 -494 -123 N ATOM 1296 CA LYS A 167 47.782 15.366 34.452 1.00 31.63 C ANISOU 1296 CA LYS A 167 4223 3265 4530 -27 -534 -116 C ATOM 1297 C LYS A 167 48.867 15.560 33.397 1.00 32.90 C ANISOU 1297 C LYS A 167 4372 3391 4737 -91 -512 -14 C ATOM 1298 O LYS A 167 49.551 16.590 33.368 1.00 32.93 O ANISOU 1298 O LYS A 167 4378 3310 4824 -126 -562 14 O ATOM 1299 CB LYS A 167 48.330 14.471 35.567 1.00 34.31 C ANISOU 1299 CB LYS A 167 4537 3662 4839 -29 -516 -160 C ATOM 1300 CG LYS A 167 47.462 14.363 36.817 1.00 41.97 C ANISOU 1300 CG LYS A 167 5514 4669 5764 30 -540 -259 C ATOM 1301 CD LYS A 167 47.505 15.639 37.659 1.00 46.45 C ANISOU 1301 CD LYS A 167 6094 5164 6392 54 -631 -324 C ATOM 1302 CE LYS A 167 48.917 15.980 38.099 1.00 49.10 C ANISOU 1302 CE LYS A 167 6411 5450 6797 8 -668 -312 C ATOM 1303 NZ LYS A 167 48.933 17.243 38.900 1.00 52.63 N ANISOU 1303 NZ LYS A 167 6871 5818 7309 33 -766 -383 N ATOM 1304 N LEU A 168 49.038 14.555 32.545 1.00 28.32 N ANISOU 1304 N LEU A 168 3777 2878 4105 -108 -437 41 N ATOM 1305 CA LEU A 168 50.102 14.577 31.551 1.00 31.66 C ANISOU 1305 CA LEU A 168 4180 3293 4556 -165 -403 137 C ATOM 1306 C LEU A 168 49.817 15.602 30.457 1.00 35.67 C ANISOU 1306 C LEU A 168 4716 3741 5095 -175 -422 206 C ATOM 1307 O LEU A 168 50.709 16.316 30.003 1.00 35.68 O ANISOU 1307 O LEU A 168 4707 3687 5161 -227 -433 278 O ATOM 1308 CB LEU A 168 50.255 13.186 30.926 1.00 25.84 C ANISOU 1308 CB LEU A 168 3422 2651 3746 -167 -321 165 C ATOM 1309 CG LEU A 168 50.743 12.053 31.833 1.00 29.98 C ANISOU 1309 CG LEU A 168 3918 3233 4241 -165 -296 119 C ATOM 1310 CD1 LEU A 168 50.425 10.716 31.172 1.00 30.46 C ANISOU 1310 CD1 LEU A 168 3972 3376 4224 -149 -227 130 C ATOM 1311 CD2 LEU A 168 52.231 12.196 32.093 1.00 34.71 C ANISOU 1311 CD2 LEU A 168 4478 3812 4898 -216 -301 150 C ATOM 1312 N ILE A 169 48.564 15.647 30.021 1.00 35.56 N ANISOU 1312 N ILE A 169 4736 3741 5035 -124 -424 187 N ATOM 1313 CA ILE A 169 48.155 16.526 28.938 1.00 35.53 C ANISOU 1313 CA ILE A 169 4765 3688 5046 -120 -443 252 C ATOM 1314 C ILE A 169 47.972 17.961 29.427 1.00 37.29 C ANISOU 1314 C ILE A 169 5017 3796 5354 -114 -532 233 C ATOM 1315 O ILE A 169 48.068 18.909 28.649 1.00 36.33 O ANISOU 1315 O ILE A 169 4922 3604 5278 -132 -559 306 O ATOM 1316 CB ILE A 169 46.834 16.023 28.285 1.00 27.92 C ANISOU 1316 CB ILE A 169 3824 2785 4002 -60 -419 231 C ATOM 1317 CG1 ILE A 169 47.026 14.622 27.690 1.00 37.79 C ANISOU 1317 CG1 ILE A 169 5047 4138 5175 -66 -337 250 C ATOM 1318 CG2 ILE A 169 46.341 16.985 27.241 1.00 33.80 C ANISOU 1318 CG2 ILE A 169 4607 3476 4758 -46 -448 292 C ATOM 1319 CD1 ILE A 169 48.118 14.532 26.669 1.00 42.45 C ANISOU 1319 CD1 ILE A 169 5620 4743 5767 -116 -290 352 C ATOM 1320 N GLY A 170 47.717 18.116 30.722 1.00 33.61 N ANISOU 1320 N GLY A 170 4550 3312 4908 -85 -581 134 N ATOM 1321 CA GLY A 170 47.507 19.436 31.291 1.00 31.58 C ANISOU 1321 CA GLY A 170 4321 2948 4732 -69 -675 95 C ATOM 1322 C GLY A 170 46.125 19.956 30.933 1.00 38.60 C ANISOU 1322 C GLY A 170 5251 3819 5597 0 -710 65 C ATOM 1323 O GLY A 170 45.969 21.134 30.630 1.00 37.41 O ANISOU 1323 O GLY A 170 5135 3568 5511 6 -776 89 O ATOM 1324 N ASP A 171 45.123 19.077 30.956 1.00 37.18 N ANISOU 1324 N ASP A 171 5065 3733 5328 52 -670 13 N ATOM 1325 CA ASP A 171 43.754 19.490 30.627 1.00 33.87 C ANISOU 1325 CA ASP A 171 4676 3311 4881 123 -702 -25 C ATOM 1326 C ASP A 171 42.784 18.850 31.609 1.00 35.47 C ANISOU 1326 C ASP A 171 4860 3594 5025 182 -695 -140 C ATOM 1327 O ASP A 171 42.462 17.665 31.491 1.00 33.07 O ANISOU 1327 O ASP A 171 4530 3388 4646 184 -626 -148 O ATOM 1328 CB ASP A 171 43.407 19.073 29.191 1.00 35.05 C ANISOU 1328 CB ASP A 171 4837 3505 4977 123 -651 55 C ATOM 1329 CG ASP A 171 42.031 19.544 28.756 1.00 41.49 C ANISOU 1329 CG ASP A 171 5683 4315 5768 197 -690 22 C ATOM 1330 OD1 ASP A 171 41.263 20.041 29.606 1.00 40.14 O ANISOU 1330 OD1 ASP A 171 5517 4122 5612 253 -747 -73 O ATOM 1331 OD2 ASP A 171 41.726 19.433 27.547 1.00 42.01 O ANISOU 1331 OD2 ASP A 171 5764 4401 5795 204 -666 87 O ATOM 1332 N PRO A 172 42.299 19.630 32.576 1.00 35.29 N ANISOU 1332 N PRO A 172 4847 3528 5034 231 -766 -229 N ATOM 1333 CA PRO A 172 41.448 19.076 33.638 1.00 35.36 C ANISOU 1333 CA PRO A 172 4831 3620 4984 285 -757 -338 C ATOM 1334 C PRO A 172 40.070 18.655 33.128 1.00 39.12 C ANISOU 1334 C PRO A 172 5302 4168 5393 340 -730 -366 C ATOM 1335 O PRO A 172 39.330 17.981 33.843 1.00 40.86 O ANISOU 1335 O PRO A 172 5494 4476 5555 374 -702 -440 O ATOM 1336 CB PRO A 172 41.283 20.258 34.611 1.00 45.10 C ANISOU 1336 CB PRO A 172 6081 4778 6276 331 -852 -423 C ATOM 1337 CG PRO A 172 42.316 21.265 34.211 1.00 50.41 C ANISOU 1337 CG PRO A 172 6781 5324 7048 282 -906 -355 C ATOM 1338 CD PRO A 172 42.556 21.072 32.761 1.00 43.21 C ANISOU 1338 CD PRO A 172 5882 4403 6132 237 -861 -234 C ATOM 1339 N ASN A 173 39.731 19.066 31.913 1.00 36.88 N ANISOU 1339 N ASN A 173 5045 3849 5118 348 -741 -306 N ATOM 1340 CA ASN A 173 38.419 18.765 31.348 1.00 41.37 C ANISOU 1340 CA ASN A 173 5608 4480 5630 403 -728 -335 C ATOM 1341 C ASN A 173 38.459 17.653 30.311 1.00 34.91 C ANISOU 1341 C ASN A 173 4776 3735 4754 369 -650 -268 C ATOM 1342 O ASN A 173 37.470 17.388 29.628 1.00 36.61 O ANISOU 1342 O ASN A 173 4987 3997 4926 408 -640 -280 O ATOM 1343 CB ASN A 173 37.793 20.034 30.784 1.00 44.60 C ANISOU 1343 CB ASN A 173 6059 4807 6082 457 -808 -334 C ATOM 1344 CG ASN A 173 37.726 21.132 31.816 1.00 48.00 C ANISOU 1344 CG ASN A 173 6504 5161 6574 498 -894 -412 C ATOM 1345 OD1 ASN A 173 37.314 20.895 32.955 1.00 46.17 O ANISOU 1345 OD1 ASN A 173 6242 4983 6317 533 -895 -511 O ATOM 1346 ND2 ASN A 173 38.163 22.332 31.442 1.00 47.22 N ANISOU 1346 ND2 ASN A 173 6450 4935 6555 494 -967 -367 N ATOM 1347 N LEU A 174 39.607 16.990 30.213 1.00 36.99 N ANISOU 1347 N LEU A 174 5030 4009 5018 301 -598 -206 N ATOM 1348 CA LEU A 174 39.746 15.848 29.310 1.00 33.25 C ANISOU 1348 CA LEU A 174 4539 3606 4487 271 -523 -153 C ATOM 1349 C LEU A 174 38.777 14.756 29.731 1.00 35.08 C ANISOU 1349 C LEU A 174 4734 3937 4656 297 -482 -225 C ATOM 1350 O LEU A 174 38.592 14.499 30.919 1.00 32.93 O ANISOU 1350 O LEU A 174 4440 3693 4379 305 -480 -293 O ATOM 1351 CB LEU A 174 41.189 15.329 29.326 1.00 38.06 C ANISOU 1351 CB LEU A 174 5138 4213 5112 199 -479 -88 C ATOM 1352 CG LEU A 174 41.707 14.528 28.124 1.00 40.29 C ANISOU 1352 CG LEU A 174 5414 4538 5355 164 -417 -7 C ATOM 1353 CD1 LEU A 174 41.407 15.225 26.812 1.00 48.84 C ANISOU 1353 CD1 LEU A 174 6530 5591 6435 183 -437 57 C ATOM 1354 CD2 LEU A 174 43.210 14.299 28.264 1.00 38.15 C ANISOU 1354 CD2 LEU A 174 5130 4252 5114 99 -388 51 C ATOM 1355 N GLU A 175 38.129 14.127 28.749 1.00 30.56 N ANISOU 1355 N GLU A 175 4156 3419 4038 311 -451 -211 N ATOM 1356 CA GLU A 175 37.209 13.037 29.033 1.00 34.43 C ANISOU 1356 CA GLU A 175 4607 3999 4476 326 -411 -273 C ATOM 1357 C GLU A 175 37.516 11.894 28.082 1.00 31.17 C ANISOU 1357 C GLU A 175 4184 3636 4024 294 -352 -225 C ATOM 1358 O GLU A 175 38.061 12.117 27.005 1.00 32.82 O ANISOU 1358 O GLU A 175 4416 3821 4232 282 -350 -154 O ATOM 1359 CB GLU A 175 35.755 13.478 28.802 1.00 33.15 C ANISOU 1359 CB GLU A 175 4439 3858 4299 394 -449 -334 C ATOM 1360 CG GLU A 175 35.319 14.700 29.596 1.00 43.98 C ANISOU 1360 CG GLU A 175 5822 5180 5708 443 -517 -391 C ATOM 1361 CD GLU A 175 35.102 14.408 31.071 1.00 53.91 C ANISOU 1361 CD GLU A 175 7046 6479 6958 448 -505 -468 C ATOM 1362 OE1 GLU A 175 35.224 13.233 31.476 1.00 56.49 O ANISOU 1362 OE1 GLU A 175 7341 6871 7251 411 -442 -472 O ATOM 1363 OE2 GLU A 175 34.807 15.357 31.831 1.00 57.86 O ANISOU 1363 OE2 GLU A 175 7553 6946 7485 492 -560 -525 O ATOM 1364 N PHE A 176 37.176 10.674 28.485 1.00 28.15 N ANISOU 1364 N PHE A 176 3766 3322 3609 279 -304 -263 N ATOM 1365 CA PHE A 176 37.194 9.554 27.552 1.00 28.78 C ANISOU 1365 CA PHE A 176 3832 3450 3651 262 -259 -239 C ATOM 1366 C PHE A 176 35.847 9.539 26.838 1.00 33.37 C ANISOU 1366 C PHE A 176 4402 4070 4206 310 -277 -280 C ATOM 1367 O PHE A 176 34.797 9.592 27.478 1.00 34.91 O ANISOU 1367 O PHE A 176 4571 4293 4399 338 -290 -349 O ATOM 1368 CB PHE A 176 37.436 8.217 28.274 1.00 31.18 C ANISOU 1368 CB PHE A 176 4107 3800 3942 223 -205 -258 C ATOM 1369 CG PHE A 176 38.818 8.072 28.872 1.00 30.90 C ANISOU 1369 CG PHE A 176 4080 3734 3927 179 -187 -217 C ATOM 1370 CD1 PHE A 176 39.896 8.800 28.388 1.00 33.44 C ANISOU 1370 CD1 PHE A 176 4427 4005 4274 163 -201 -153 C ATOM 1371 CD2 PHE A 176 39.039 7.183 29.918 1.00 27.21 C ANISOU 1371 CD2 PHE A 176 3592 3292 3454 153 -155 -240 C ATOM 1372 CE1 PHE A 176 41.181 8.667 28.961 1.00 33.61 C ANISOU 1372 CE1 PHE A 176 4447 4003 4319 122 -187 -120 C ATOM 1373 CE2 PHE A 176 40.328 7.029 30.485 1.00 29.84 C ANISOU 1373 CE2 PHE A 176 3931 3602 3805 118 -143 -206 C ATOM 1374 CZ PHE A 176 41.396 7.771 30.002 1.00 25.60 C ANISOU 1374 CZ PHE A 176 3414 3016 3297 103 -160 -150 C ATOM 1375 N VAL A 177 35.871 9.482 25.512 1.00 30.45 N ANISOU 1375 N VAL A 177 4049 3709 3813 322 -278 -240 N ATOM 1376 CA VAL A 177 34.624 9.500 24.745 1.00 35.07 C ANISOU 1376 CA VAL A 177 4623 4331 4371 373 -303 -280 C ATOM 1377 C VAL A 177 33.856 8.182 24.935 1.00 37.07 C ANISOU 1377 C VAL A 177 4828 4654 4604 362 -268 -341 C ATOM 1378 O VAL A 177 32.624 8.162 24.950 1.00 35.17 O ANISOU 1378 O VAL A 177 4557 4450 4356 397 -287 -405 O ATOM 1379 CB VAL A 177 34.880 9.775 23.255 1.00 42.87 C ANISOU 1379 CB VAL A 177 5644 5315 5329 393 -315 -218 C ATOM 1380 CG1 VAL A 177 35.326 11.222 23.055 1.00 42.10 C ANISOU 1380 CG1 VAL A 177 5594 5143 5259 409 -360 -159 C ATOM 1381 CG2 VAL A 177 35.923 8.833 22.727 1.00 49.20 C ANISOU 1381 CG2 VAL A 177 6446 6140 6109 351 -262 -168 C ATOM 1382 N ALA A 178 34.597 7.087 25.099 1.00 31.40 N ANISOU 1382 N ALA A 178 4098 3951 3880 313 -218 -323 N ATOM 1383 CA ALA A 178 33.986 5.792 25.353 1.00 30.68 C ANISOU 1383 CA ALA A 178 3964 3911 3780 292 -185 -373 C ATOM 1384 C ALA A 178 34.957 4.918 26.135 1.00 28.64 C ANISOU 1384 C ALA A 178 3703 3645 3534 237 -139 -349 C ATOM 1385 O ALA A 178 36.161 5.140 26.097 1.00 32.70 O ANISOU 1385 O ALA A 178 4245 4125 4054 217 -130 -293 O ATOM 1386 CB ALA A 178 33.622 5.122 24.045 1.00 30.27 C ANISOU 1386 CB ALA A 178 3906 3895 3699 309 -186 -380 C ATOM 1387 N MET A 179 34.438 3.914 26.828 1.00 33.65 N ANISOU 1387 N MET A 179 4301 4311 4172 210 -111 -389 N ATOM 1388 CA MET A 179 35.313 2.935 27.472 1.00 30.85 C ANISOU 1388 CA MET A 179 3946 3950 3826 162 -70 -365 C ATOM 1389 C MET A 179 35.975 2.046 26.424 1.00 30.84 C ANISOU 1389 C MET A 179 3955 3950 3814 150 -53 -339 C ATOM 1390 O MET A 179 35.358 1.715 25.406 1.00 34.66 O ANISOU 1390 O MET A 179 4429 4459 4282 171 -64 -363 O ATOM 1391 CB MET A 179 34.521 2.086 28.470 1.00 29.03 C ANISOU 1391 CB MET A 179 3676 3751 3603 135 -44 -407 C ATOM 1392 CG MET A 179 33.939 2.880 29.626 1.00 37.87 C ANISOU 1392 CG MET A 179 4781 4882 4724 149 -53 -436 C ATOM 1393 SD MET A 179 35.207 3.253 30.876 1.00 46.29 S ANISOU 1393 SD MET A 179 5877 5914 5797 130 -44 -398 S ATOM 1394 CE MET A 179 35.581 1.622 31.494 1.00 35.81 C ANISOU 1394 CE MET A 179 4537 4600 4468 74 8 -379 C ATOM 1395 N PRO A 180 37.224 1.622 26.679 1.00 33.19 N ANISOU 1395 N PRO A 180 4269 4225 4117 121 -29 -296 N ATOM 1396 CA PRO A 180 37.868 0.652 25.792 1.00 32.71 C ANISOU 1396 CA PRO A 180 4212 4171 4044 114 -11 -280 C ATOM 1397 C PRO A 180 37.136 -0.658 25.907 1.00 27.65 C ANISOU 1397 C PRO A 180 3544 3549 3412 96 3 -325 C ATOM 1398 O PRO A 180 36.394 -0.854 26.855 1.00 30.58 O ANISOU 1398 O PRO A 180 3893 3925 3799 77 9 -352 O ATOM 1399 CB PRO A 180 39.268 0.491 26.390 1.00 38.30 C ANISOU 1399 CB PRO A 180 4935 4852 4764 87 10 -234 C ATOM 1400 CG PRO A 180 39.420 1.620 27.372 1.00 38.15 C ANISOU 1400 CG PRO A 180 4925 4807 4761 84 -4 -220 C ATOM 1401 CD PRO A 180 38.056 1.929 27.856 1.00 38.28 C ANISOU 1401 CD PRO A 180 4924 4841 4778 98 -20 -270 C ATOM 1402 N ALA A 181 37.319 -1.533 24.931 1.00 31.26 N ANISOU 1402 N ALA A 181 4001 4018 3860 102 6 -335 N ATOM 1403 CA ALA A 181 36.704 -2.843 24.994 1.00 32.05 C ANISOU 1403 CA ALA A 181 4077 4123 3980 81 13 -378 C ATOM 1404 C ALA A 181 37.460 -3.650 26.035 1.00 31.36 C ANISOU 1404 C ALA A 181 3994 4005 3916 39 41 -353 C ATOM 1405 O ALA A 181 38.674 -3.816 25.923 1.00 28.02 O ANISOU 1405 O ALA A 181 3593 3567 3488 40 51 -318 O ATOM 1406 CB ALA A 181 36.773 -3.504 23.648 1.00 28.36 C ANISOU 1406 CB ALA A 181 3609 3671 3494 107 1 -401 C ATOM 1407 N LEU A 182 36.739 -4.125 27.048 1.00 29.74 N ANISOU 1407 N LEU A 182 3768 3797 3735 5 53 -369 N ATOM 1408 CA LEU A 182 37.343 -4.848 28.180 1.00 26.91 C ANISOU 1408 CA LEU A 182 3417 3412 3395 -33 78 -340 C ATOM 1409 C LEU A 182 36.838 -6.274 28.235 1.00 32.14 C ANISOU 1409 C LEU A 182 4063 4059 4089 -67 85 -361 C ATOM 1410 O LEU A 182 35.715 -6.551 27.829 1.00 28.61 O ANISOU 1410 O LEU A 182 3585 3629 3655 -73 76 -404 O ATOM 1411 CB LEU A 182 36.963 -4.189 29.506 1.00 27.07 C ANISOU 1411 CB LEU A 182 3430 3443 3412 -48 89 -329 C ATOM 1412 CG LEU A 182 37.398 -2.736 29.700 1.00 29.41 C ANISOU 1412 CG LEU A 182 3743 3743 3688 -19 75 -312 C ATOM 1413 CD1 LEU A 182 36.962 -2.255 31.069 1.00 35.33 C ANISOU 1413 CD1 LEU A 182 4483 4509 4433 -28 84 -315 C ATOM 1414 CD2 LEU A 182 38.910 -2.637 29.525 1.00 30.79 C ANISOU 1414 CD2 LEU A 182 3949 3890 3860 -14 76 -269 C ATOM 1415 N ALA A 183 37.653 -7.168 28.782 1.00 30.48 N ANISOU 1415 N ALA A 183 3871 3815 3895 -90 99 -332 N ATOM 1416 CA ALA A 183 37.192 -8.517 29.079 1.00 32.86 C ANISOU 1416 CA ALA A 183 4160 4088 4235 -131 106 -341 C ATOM 1417 C ALA A 183 35.992 -8.401 30.009 1.00 37.41 C ANISOU 1417 C ALA A 183 4704 4688 4820 -167 124 -345 C ATOM 1418 O ALA A 183 36.011 -7.613 30.952 1.00 35.00 O ANISOU 1418 O ALA A 183 4401 4406 4491 -167 140 -321 O ATOM 1419 CB ALA A 183 38.293 -9.310 29.755 1.00 37.32 C ANISOU 1419 CB ALA A 183 4756 4611 4813 -146 117 -298 C ATOM 1420 N PRO A 184 34.942 -9.190 29.751 1.00 37.48 N ANISOU 1420 N PRO A 184 4680 4695 4866 -198 121 -378 N ATOM 1421 CA PRO A 184 33.718 -9.163 30.559 1.00 37.04 C ANISOU 1421 CA PRO A 184 4581 4671 4821 -236 143 -383 C ATOM 1422 C PRO A 184 34.029 -9.449 32.016 1.00 32.37 C ANISOU 1422 C PRO A 184 4002 4073 4224 -273 179 -325 C ATOM 1423 O PRO A 184 34.930 -10.239 32.291 1.00 36.66 O ANISOU 1423 O PRO A 184 4581 4568 4780 -286 182 -287 O ATOM 1424 CB PRO A 184 32.888 -10.320 29.986 1.00 40.28 C ANISOU 1424 CB PRO A 184 4959 5059 5288 -274 131 -419 C ATOM 1425 CG PRO A 184 33.434 -10.573 28.646 1.00 40.70 C ANISOU 1425 CG PRO A 184 5033 5087 5344 -234 93 -455 C ATOM 1426 CD PRO A 184 34.860 -10.141 28.628 1.00 40.17 C ANISOU 1426 CD PRO A 184 5017 5006 5239 -195 94 -418 C ATOM 1427 N PRO A 185 33.305 -8.810 32.942 1.00 34.97 N ANISOU 1427 N PRO A 185 4304 4456 4530 -282 205 -319 N ATOM 1428 CA PRO A 185 33.569 -9.045 34.369 1.00 34.80 C ANISOU 1428 CA PRO A 185 4294 4440 4489 -311 240 -263 C ATOM 1429 C PRO A 185 33.488 -10.521 34.731 1.00 37.71 C ANISOU 1429 C PRO A 185 4665 4764 4901 -372 258 -224 C ATOM 1430 O PRO A 185 32.548 -11.209 34.324 1.00 39.21 O ANISOU 1430 O PRO A 185 4815 4946 5136 -412 259 -246 O ATOM 1431 CB PRO A 185 32.449 -8.267 35.060 1.00 37.62 C ANISOU 1431 CB PRO A 185 4602 4873 4818 -312 264 -282 C ATOM 1432 CG PRO A 185 32.143 -7.152 34.114 1.00 44.72 C ANISOU 1432 CG PRO A 185 5488 5796 5706 -258 231 -340 C ATOM 1433 CD PRO A 185 32.325 -7.730 32.729 1.00 35.33 C ANISOU 1433 CD PRO A 185 4309 4562 4555 -254 198 -366 C ATOM 1434 N GLU A 186 34.478 -11.008 35.469 1.00 38.18 N ANISOU 1434 N GLU A 186 4769 4786 4950 -379 266 -167 N ATOM 1435 CA GLU A 186 34.475 -12.402 35.913 1.00 41.02 C ANISOU 1435 CA GLU A 186 5140 5094 5351 -435 280 -119 C ATOM 1436 C GLU A 186 33.779 -12.542 37.255 1.00 44.46 C ANISOU 1436 C GLU A 186 5554 5575 5765 -480 328 -68 C ATOM 1437 O GLU A 186 33.298 -13.620 37.615 1.00 49.97 O ANISOU 1437 O GLU A 186 6241 6244 6503 -542 348 -28 O ATOM 1438 CB GLU A 186 35.901 -12.937 35.991 1.00 46.23 C ANISOU 1438 CB GLU A 186 5861 5690 6013 -415 260 -82 C ATOM 1439 CG GLU A 186 36.609 -12.915 34.652 1.00 55.37 C ANISOU 1439 CG GLU A 186 7037 6812 7191 -372 218 -130 C ATOM 1440 CD GLU A 186 38.070 -13.290 34.756 1.00 70.73 C ANISOU 1440 CD GLU A 186 9034 8709 9131 -342 200 -99 C ATOM 1441 OE1 GLU A 186 38.409 -14.162 35.587 1.00 75.61 O ANISOU 1441 OE1 GLU A 186 9679 9288 9762 -369 208 -46 O ATOM 1442 OE2 GLU A 186 38.876 -12.711 33.997 1.00 74.12 O ANISOU 1442 OE2 GLU A 186 9476 9144 9544 -292 178 -127 O ATOM 1443 N VAL A 187 33.748 -11.448 38.003 1.00 37.26 N ANISOU 1443 N VAL A 187 4635 4734 4788 -448 347 -68 N ATOM 1444 CA VAL A 187 33.004 -11.395 39.252 1.00 45.73 C ANISOU 1444 CA VAL A 187 5678 5873 5823 -479 396 -31 C ATOM 1445 C VAL A 187 32.152 -10.144 39.237 1.00 47.60 C ANISOU 1445 C VAL A 187 5866 6197 6024 -445 403 -90 C ATOM 1446 O VAL A 187 32.481 -9.174 38.554 1.00 42.15 O ANISOU 1446 O VAL A 187 5185 5508 5322 -389 368 -142 O ATOM 1447 CB VAL A 187 33.934 -11.363 40.491 1.00 45.20 C ANISOU 1447 CB VAL A 187 5661 5815 5699 -462 410 32 C ATOM 1448 CG1 VAL A 187 34.682 -12.675 40.630 1.00 55.50 C ANISOU 1448 CG1 VAL A 187 7014 7035 7039 -496 403 96 C ATOM 1449 CG2 VAL A 187 34.901 -10.196 40.405 1.00 44.56 C ANISOU 1449 CG2 VAL A 187 5612 5744 5575 -390 377 -2 C ATOM 1450 N VAL A 188 31.053 -10.170 39.980 1.00 49.14 N ANISOU 1450 N VAL A 188 6007 6464 6202 -478 448 -80 N ATOM 1451 CA VAL A 188 30.175 -9.012 40.080 1.00 54.69 C ANISOU 1451 CA VAL A 188 6657 7256 6868 -441 456 -140 C ATOM 1452 C VAL A 188 30.628 -8.079 41.200 1.00 50.48 C ANISOU 1452 C VAL A 188 6145 6781 6252 -390 467 -132 C ATOM 1453 O VAL A 188 30.869 -8.518 42.324 1.00 58.68 O ANISOU 1453 O VAL A 188 7201 7843 7251 -410 502 -70 O ATOM 1454 CB VAL A 188 28.719 -9.432 40.360 1.00 62.20 C ANISOU 1454 CB VAL A 188 7526 8271 7835 -496 502 -142 C ATOM 1455 CG1 VAL A 188 27.855 -8.207 40.601 1.00 61.99 C ANISOU 1455 CG1 VAL A 188 7444 8347 7763 -448 510 -206 C ATOM 1456 CG2 VAL A 188 28.171 -10.267 39.211 1.00 62.66 C ANISOU 1456 CG2 VAL A 188 7554 8273 7980 -544 483 -166 C ATOM 1457 N MET A 189 30.755 -6.793 40.888 1.00 48.37 N ANISOU 1457 N MET A 189 5881 6536 5961 -323 432 -194 N ATOM 1458 CA MET A 189 31.007 -5.786 41.917 1.00 43.28 C ANISOU 1458 CA MET A 189 5247 5953 5245 -269 434 -206 C ATOM 1459 C MET A 189 29.674 -5.209 42.381 1.00 46.38 C ANISOU 1459 C MET A 189 5568 6450 5606 -256 464 -251 C ATOM 1460 O MET A 189 29.064 -4.404 41.681 1.00 50.23 O ANISOU 1460 O MET A 189 6022 6955 6109 -220 437 -320 O ATOM 1461 CB MET A 189 31.900 -4.668 41.382 1.00 39.43 C ANISOU 1461 CB MET A 189 4802 5424 4756 -203 375 -248 C ATOM 1462 CG MET A 189 32.160 -3.554 42.391 1.00 42.48 C ANISOU 1462 CG MET A 189 5200 5864 5078 -144 365 -273 C ATOM 1463 SD MET A 189 33.161 -4.156 43.757 1.00 43.68 S ANISOU 1463 SD MET A 189 5400 6021 5177 -155 387 -201 S ATOM 1464 CE MET A 189 33.134 -2.752 44.881 1.00 46.57 C ANISOU 1464 CE MET A 189 5761 6467 5465 -77 371 -257 C ATOM 1465 N ASP A 190 29.230 -5.628 43.561 1.00 52.27 N ANISOU 1465 N ASP A 190 6288 7270 6304 -282 521 -210 N ATOM 1466 CA ASP A 190 27.946 -5.202 44.108 1.00 54.54 C ANISOU 1466 CA ASP A 190 6496 7672 6554 -273 560 -248 C ATOM 1467 C ASP A 190 27.828 -3.682 44.124 1.00 55.54 C ANISOU 1467 C ASP A 190 6616 7842 6645 -182 520 -335 C ATOM 1468 O ASP A 190 28.602 -3.006 44.797 1.00 55.78 O ANISOU 1468 O ASP A 190 6692 7879 6625 -129 498 -342 O ATOM 1469 CB ASP A 190 27.774 -5.763 45.522 1.00 70.27 C ANISOU 1469 CB ASP A 190 8477 9742 8479 -302 627 -181 C ATOM 1470 CG ASP A 190 26.536 -5.230 46.219 1.00 83.75 C ANISOU 1470 CG ASP A 190 10101 11588 10133 -282 673 -222 C ATOM 1471 OD1 ASP A 190 25.663 -4.651 45.538 1.00 88.25 O ANISOU 1471 OD1 ASP A 190 10612 12186 10732 -260 657 -297 O ATOM 1472 OD2 ASP A 190 26.434 -5.395 47.453 1.00 89.41 O ANISOU 1472 OD2 ASP A 190 10809 12390 10773 -284 724 -179 O ATOM 1473 N PRO A 191 26.846 -3.140 43.386 1.00 55.05 N ANISOU 1473 N PRO A 191 6496 7808 6611 -162 504 -406 N ATOM 1474 CA PRO A 191 26.679 -1.687 43.250 1.00 53.47 C ANISOU 1474 CA PRO A 191 6291 7634 6390 -73 456 -493 C ATOM 1475 C PRO A 191 26.540 -0.984 44.601 1.00 57.80 C ANISOU 1475 C PRO A 191 6826 8281 6854 -18 476 -517 C ATOM 1476 O PRO A 191 27.068 0.114 44.775 1.00 57.45 O ANISOU 1476 O PRO A 191 6819 8224 6787 55 425 -565 O ATOM 1477 CB PRO A 191 25.384 -1.556 42.444 1.00 57.05 C ANISOU 1477 CB PRO A 191 6668 8126 6884 -74 454 -552 C ATOM 1478 CG PRO A 191 25.262 -2.850 41.708 1.00 60.80 C ANISOU 1478 CG PRO A 191 7132 8547 7423 -160 474 -501 C ATOM 1479 CD PRO A 191 25.839 -3.891 42.617 1.00 58.43 C ANISOU 1479 CD PRO A 191 6861 8240 7100 -221 525 -410 C ATOM 1480 N ALA A 192 25.835 -1.610 45.539 1.00 60.61 N ANISOU 1480 N ALA A 192 7129 8736 7164 -54 548 -485 N ATOM 1481 CA ALA A 192 25.687 -1.058 46.882 1.00 63.44 C ANISOU 1481 CA ALA A 192 7471 9203 7428 -1 575 -504 C ATOM 1482 C ALA A 192 27.038 -0.968 47.583 1.00 61.39 C ANISOU 1482 C ALA A 192 7299 8901 7127 22 552 -466 C ATOM 1483 O ALA A 192 27.370 0.052 48.190 1.00 61.41 O ANISOU 1483 O ALA A 192 7322 8934 7078 101 516 -521 O ATOM 1484 CB ALA A 192 24.722 -1.902 47.701 1.00 64.50 C ANISOU 1484 CB ALA A 192 7532 9453 7521 -56 666 -458 C ATOM 1485 N LEU A 193 27.809 -2.047 47.502 1.00 62.24 N ANISOU 1485 N LEU A 193 7454 8935 7259 -45 567 -375 N ATOM 1486 CA LEU A 193 29.131 -2.090 48.107 1.00 60.83 C ANISOU 1486 CA LEU A 193 7354 8711 7046 -28 543 -334 C ATOM 1487 C LEU A 193 29.994 -0.983 47.524 1.00 52.99 C ANISOU 1487 C LEU A 193 6411 7638 6084 35 459 -396 C ATOM 1488 O LEU A 193 30.663 -0.252 48.253 1.00 54.69 O ANISOU 1488 O LEU A 193 6662 7866 6251 94 425 -423 O ATOM 1489 CB LEU A 193 29.783 -3.454 47.870 1.00 60.89 C ANISOU 1489 CB LEU A 193 7404 8638 7094 -109 564 -233 C ATOM 1490 CG LEU A 193 31.121 -3.683 48.570 1.00 62.04 C ANISOU 1490 CG LEU A 193 7625 8743 7202 -96 545 -181 C ATOM 1491 CD1 LEU A 193 30.944 -3.596 50.071 1.00 64.15 C ANISOU 1491 CD1 LEU A 193 7885 9127 7362 -66 585 -163 C ATOM 1492 CD2 LEU A 193 31.732 -5.020 48.174 1.00 62.68 C ANISOU 1492 CD2 LEU A 193 7746 8733 7335 -169 556 -90 C ATOM 1493 N ALA A 194 29.964 -0.855 46.202 1.00 48.09 N ANISOU 1493 N ALA A 194 5792 6935 5543 21 423 -418 N ATOM 1494 CA ALA A 194 30.727 0.181 45.517 1.00 48.75 C ANISOU 1494 CA ALA A 194 5920 6940 5664 72 346 -466 C ATOM 1495 C ALA A 194 30.325 1.575 46.006 1.00 50.96 C ANISOU 1495 C ALA A 194 6181 7275 5905 158 310 -556 C ATOM 1496 O ALA A 194 31.176 2.439 46.222 1.00 47.08 O ANISOU 1496 O ALA A 194 5735 6743 5409 207 254 -586 O ATOM 1497 CB ALA A 194 30.542 0.065 44.007 1.00 45.00 C ANISOU 1497 CB ALA A 194 5440 6388 5269 46 322 -473 C ATOM 1498 N ALA A 195 29.024 1.782 46.191 1.00 49.24 N ANISOU 1498 N ALA A 195 5894 7152 5664 176 341 -603 N ATOM 1499 CA ALA A 195 28.511 3.061 46.676 1.00 47.98 C ANISOU 1499 CA ALA A 195 5709 7054 5466 264 307 -698 C ATOM 1500 C ALA A 195 29.062 3.379 48.065 1.00 51.26 C ANISOU 1500 C ALA A 195 6149 7526 5800 310 307 -707 C ATOM 1501 O ALA A 195 29.489 4.502 48.341 1.00 53.33 O ANISOU 1501 O ALA A 195 6439 7769 6053 382 243 -773 O ATOM 1502 CB ALA A 195 26.990 3.039 46.705 1.00 49.25 C ANISOU 1502 CB ALA A 195 5781 7322 5611 271 351 -741 C ATOM 1503 N GLN A 196 29.042 2.375 48.932 1.00 45.90 N ANISOU 1503 N GLN A 196 5461 6915 5064 266 376 -639 N ATOM 1504 CA GLN A 196 29.552 2.512 50.288 1.00 50.06 C ANISOU 1504 CA GLN A 196 6011 7507 5501 307 382 -637 C ATOM 1505 C GLN A 196 31.043 2.853 50.303 1.00 49.61 C ANISOU 1505 C GLN A 196 6037 7348 5466 324 314 -628 C ATOM 1506 O GLN A 196 31.480 3.742 51.035 1.00 49.45 O ANISOU 1506 O GLN A 196 6038 7348 5403 396 267 -688 O ATOM 1507 CB GLN A 196 29.299 1.224 51.078 1.00 56.86 C ANISOU 1507 CB GLN A 196 6854 8446 6303 245 472 -544 C ATOM 1508 CG GLN A 196 29.672 1.312 52.551 1.00 68.35 C ANISOU 1508 CG GLN A 196 8328 9995 7648 292 487 -539 C ATOM 1509 CD GLN A 196 28.747 2.231 53.329 1.00 83.77 C ANISOU 1509 CD GLN A 196 10223 12083 9522 376 495 -633 C ATOM 1510 OE1 GLN A 196 27.546 2.293 53.061 1.00 89.46 O ANISOU 1510 OE1 GLN A 196 10869 12873 10248 372 534 -665 O ATOM 1511 NE2 GLN A 196 29.302 2.947 54.301 1.00 87.39 N ANISOU 1511 NE2 GLN A 196 10713 12584 9906 456 456 -684 N ATOM 1512 N TYR A 197 31.825 2.143 49.497 1.00 46.89 N ANISOU 1512 N TYR A 197 5732 6896 5187 260 308 -558 N ATOM 1513 CA TYR A 197 33.262 2.384 49.463 1.00 49.27 C ANISOU 1513 CA TYR A 197 6103 7105 5514 270 248 -544 C ATOM 1514 C TYR A 197 33.578 3.787 48.962 1.00 44.73 C ANISOU 1514 C TYR A 197 5543 6466 4985 329 164 -628 C ATOM 1515 O TYR A 197 34.519 4.421 49.427 1.00 43.20 O ANISOU 1515 O TYR A 197 5390 6240 4785 368 109 -654 O ATOM 1516 CB TYR A 197 33.983 1.343 48.601 1.00 44.45 C ANISOU 1516 CB TYR A 197 5525 6396 4967 194 259 -459 C ATOM 1517 CG TYR A 197 34.105 -0.022 49.245 1.00 43.33 C ANISOU 1517 CG TYR A 197 5392 6288 4785 140 321 -367 C ATOM 1518 CD1 TYR A 197 34.122 -0.162 50.625 1.00 44.00 C ANISOU 1518 CD1 TYR A 197 5479 6464 4774 167 348 -353 C ATOM 1519 CD2 TYR A 197 34.227 -1.170 48.466 1.00 46.09 C ANISOU 1519 CD2 TYR A 197 5749 6573 5190 66 349 -295 C ATOM 1520 CE1 TYR A 197 34.236 -1.411 51.215 1.00 44.77 C ANISOU 1520 CE1 TYR A 197 5589 6587 4834 117 404 -259 C ATOM 1521 CE2 TYR A 197 34.348 -2.423 49.045 1.00 45.15 C ANISOU 1521 CE2 TYR A 197 5642 6470 5042 16 400 -207 C ATOM 1522 CZ TYR A 197 34.352 -2.536 50.417 1.00 51.25 C ANISOU 1522 CZ TYR A 197 6420 7331 5721 40 428 -185 C ATOM 1523 OH TYR A 197 34.473 -3.780 50.994 1.00 47.27 O ANISOU 1523 OH TYR A 197 5934 6840 5188 -10 477 -88 O ATOM 1524 N GLU A 198 32.788 4.267 48.008 1.00 39.73 N ANISOU 1524 N GLU A 198 4880 5813 4403 335 152 -668 N ATOM 1525 CA GLU A 198 33.006 5.591 47.443 1.00 41.37 C ANISOU 1525 CA GLU A 198 5105 5952 4661 388 72 -739 C ATOM 1526 C GLU A 198 32.715 6.644 48.510 1.00 48.77 C ANISOU 1526 C GLU A 198 6030 6958 5541 476 36 -830 C ATOM 1527 O GLU A 198 33.481 7.587 48.691 1.00 47.07 O ANISOU 1527 O GLU A 198 5853 6686 5347 520 -37 -875 O ATOM 1528 CB GLU A 198 32.144 5.792 46.189 1.00 43.15 C ANISOU 1528 CB GLU A 198 5301 6149 4946 378 68 -757 C ATOM 1529 CG GLU A 198 32.676 5.045 44.965 1.00 42.34 C ANISOU 1529 CG GLU A 198 5222 5955 4910 308 76 -683 C ATOM 1530 CD GLU A 198 31.590 4.665 43.959 1.00 54.61 C ANISOU 1530 CD GLU A 198 6732 7522 6496 282 104 -684 C ATOM 1531 OE1 GLU A 198 30.433 5.117 44.109 1.00 60.51 O ANISOU 1531 OE1 GLU A 198 7429 8340 7223 322 110 -745 O ATOM 1532 OE2 GLU A 198 31.903 3.906 43.011 1.00 46.88 O ANISOU 1532 OE2 GLU A 198 5766 6484 5561 226 117 -628 O ATOM 1533 N HIS A 199 31.620 6.457 49.236 1.00 48.89 N ANISOU 1533 N HIS A 199 5992 7099 5486 500 89 -859 N ATOM 1534 CA HIS A 199 31.295 7.333 50.353 1.00 47.13 C ANISOU 1534 CA HIS A 199 5752 6962 5192 590 64 -949 C ATOM 1535 C HIS A 199 32.386 7.281 51.420 1.00 49.18 C ANISOU 1535 C HIS A 199 6058 7229 5399 608 44 -937 C ATOM 1536 O HIS A 199 32.854 8.318 51.885 1.00 51.03 O ANISOU 1536 O HIS A 199 6316 7443 5630 677 -30 -1013 O ATOM 1537 CB HIS A 199 29.947 6.952 50.962 1.00 53.17 C ANISOU 1537 CB HIS A 199 6443 7879 5881 604 140 -968 C ATOM 1538 CG HIS A 199 29.575 7.776 52.155 1.00 65.81 C ANISOU 1538 CG HIS A 199 8021 9588 7395 702 122 -1063 C ATOM 1539 ND1 HIS A 199 29.113 9.071 52.050 1.00 67.53 N ANISOU 1539 ND1 HIS A 199 8224 9801 7631 791 53 -1178 N ATOM 1540 CD2 HIS A 199 29.606 7.493 53.480 1.00 66.56 C ANISOU 1540 CD2 HIS A 199 8109 9801 7382 731 160 -1062 C ATOM 1541 CE1 HIS A 199 28.871 9.548 53.258 1.00 69.42 C ANISOU 1541 CE1 HIS A 199 8445 10153 7779 873 49 -1252 C ATOM 1542 NE2 HIS A 199 29.162 8.611 54.143 1.00 68.80 N ANISOU 1542 NE2 HIS A 199 8370 10154 7617 839 115 -1182 N ATOM 1543 N ASP A 200 32.797 6.072 51.796 1.00 47.09 N ANISOU 1543 N ASP A 200 5806 6989 5097 547 104 -842 N ATOM 1544 CA ASP A 200 33.829 5.899 52.819 1.00 47.92 C ANISOU 1544 CA ASP A 200 5955 7108 5146 563 88 -823 C ATOM 1545 C ASP A 200 35.108 6.652 52.474 1.00 48.99 C ANISOU 1545 C ASP A 200 6144 7117 5351 578 -6 -849 C ATOM 1546 O ASP A 200 35.752 7.224 53.353 1.00 51.09 O ANISOU 1546 O ASP A 200 6435 7397 5580 634 -58 -899 O ATOM 1547 CB ASP A 200 34.134 4.418 53.051 1.00 51.48 C ANISOU 1547 CB ASP A 200 6418 7578 5566 488 161 -705 C ATOM 1548 CG ASP A 200 32.989 3.688 53.721 1.00 58.12 C ANISOU 1548 CG ASP A 200 7206 8556 6321 475 254 -673 C ATOM 1549 OD1 ASP A 200 32.064 4.369 54.209 1.00 59.96 O ANISOU 1549 OD1 ASP A 200 7393 8890 6501 537 261 -752 O ATOM 1550 OD2 ASP A 200 33.008 2.439 53.755 1.00 60.30 O ANISOU 1550 OD2 ASP A 200 7486 8840 6586 403 319 -571 O ATOM 1551 N LEU A 201 35.477 6.653 51.196 1.00 42.23 N ANISOU 1551 N LEU A 201 5305 6144 4598 527 -27 -816 N ATOM 1552 CA LEU A 201 36.644 7.410 50.749 1.00 39.01 C ANISOU 1552 CA LEU A 201 4941 5615 4266 533 -111 -834 C ATOM 1553 C LEU A 201 36.409 8.921 50.866 1.00 45.22 C ANISOU 1553 C LEU A 201 5724 6382 5075 611 -192 -946 C ATOM 1554 O LEU A 201 37.312 9.670 51.245 1.00 45.79 O ANISOU 1554 O LEU A 201 5827 6401 5169 644 -267 -988 O ATOM 1555 CB LEU A 201 37.016 7.040 49.315 1.00 39.58 C ANISOU 1555 CB LEU A 201 5027 5580 4433 462 -107 -768 C ATOM 1556 CG LEU A 201 37.650 5.657 49.145 1.00 38.76 C ANISOU 1556 CG LEU A 201 4939 5461 4328 389 -54 -665 C ATOM 1557 CD1 LEU A 201 37.734 5.281 47.680 1.00 43.20 C ANISOU 1557 CD1 LEU A 201 5504 5938 4971 330 -42 -613 C ATOM 1558 CD2 LEU A 201 39.026 5.645 49.796 1.00 44.28 C ANISOU 1558 CD2 LEU A 201 5678 6127 5020 396 -95 -651 C ATOM 1559 N GLU A 202 35.201 9.367 50.535 1.00 48.44 N ANISOU 1559 N GLU A 202 6095 6828 5484 643 -182 -996 N ATOM 1560 CA GLU A 202 34.851 10.776 50.709 1.00 52.53 C ANISOU 1560 CA GLU A 202 6608 7332 6019 727 -260 -1108 C ATOM 1561 C GLU A 202 34.972 11.201 52.172 1.00 48.19 C ANISOU 1561 C GLU A 202 6059 6869 5384 805 -288 -1186 C ATOM 1562 O GLU A 202 35.596 12.214 52.489 1.00 52.20 O ANISOU 1562 O GLU A 202 6594 7318 5922 856 -378 -1257 O ATOM 1563 CB GLU A 202 33.433 11.050 50.207 1.00 51.08 C ANISOU 1563 CB GLU A 202 6376 7196 5836 754 -237 -1151 C ATOM 1564 CG GLU A 202 33.302 10.986 48.706 1.00 58.55 C ANISOU 1564 CG GLU A 202 7327 8047 6873 701 -238 -1102 C ATOM 1565 CD GLU A 202 31.856 10.974 48.254 1.00 67.27 C ANISOU 1565 CD GLU A 202 8376 9217 7967 720 -202 -1132 C ATOM 1566 OE1 GLU A 202 30.958 10.974 49.126 1.00 69.09 O ANISOU 1566 OE1 GLU A 202 8559 9573 8121 770 -169 -1188 O ATOM 1567 OE2 GLU A 202 31.620 10.959 47.028 1.00 67.66 O ANISOU 1567 OE2 GLU A 202 8425 9199 8083 687 -206 -1102 O ATOM 1568 N VAL A 203 34.357 10.427 53.059 1.00 49.45 N ANISOU 1568 N VAL A 203 6186 7168 5435 814 -211 -1171 N ATOM 1569 CA VAL A 203 34.440 10.701 54.484 1.00 49.66 C ANISOU 1569 CA VAL A 203 6211 7297 5361 891 -226 -1237 C ATOM 1570 C VAL A 203 35.894 10.738 54.926 1.00 48.33 C ANISOU 1570 C VAL A 203 6097 7063 5205 884 -284 -1222 C ATOM 1571 O VAL A 203 36.307 11.630 55.663 1.00 47.59 O ANISOU 1571 O VAL A 203 6018 6969 5094 958 -362 -1314 O ATOM 1572 CB VAL A 203 33.695 9.636 55.306 1.00 54.69 C ANISOU 1572 CB VAL A 203 6808 8094 5876 881 -120 -1189 C ATOM 1573 CG1 VAL A 203 33.926 9.853 56.802 1.00 54.68 C ANISOU 1573 CG1 VAL A 203 6814 8205 5759 961 -135 -1246 C ATOM 1574 CG2 VAL A 203 32.211 9.655 54.976 1.00 53.05 C ANISOU 1574 CG2 VAL A 203 6534 7968 5654 893 -64 -1215 C ATOM 1575 N ALA A 204 36.670 9.759 54.478 1.00 48.71 N ANISOU 1575 N ALA A 204 6169 7054 5284 798 -249 -1111 N ATOM 1576 CA ALA A 204 38.076 9.677 54.853 1.00 48.98 C ANISOU 1576 CA ALA A 204 6249 7030 5332 787 -299 -1090 C ATOM 1577 C ALA A 204 38.844 10.892 54.340 1.00 45.73 C ANISOU 1577 C ALA A 204 5861 6484 5028 804 -407 -1153 C ATOM 1578 O ALA A 204 39.739 11.405 55.014 1.00 46.89 O ANISOU 1578 O ALA A 204 6032 6608 5175 841 -480 -1203 O ATOM 1579 CB ALA A 204 38.692 8.388 54.327 1.00 48.66 C ANISOU 1579 CB ALA A 204 6225 6949 5314 693 -240 -961 C ATOM 1580 N GLN A 205 38.484 11.362 53.150 1.00 45.49 N ANISOU 1580 N GLN A 205 5826 6368 5092 777 -420 -1151 N ATOM 1581 CA GLN A 205 39.192 12.486 52.547 1.00 51.62 C ANISOU 1581 CA GLN A 205 6625 7006 5980 781 -518 -1193 C ATOM 1582 C GLN A 205 38.977 13.777 53.333 1.00 52.56 C ANISOU 1582 C GLN A 205 6745 7136 6089 880 -607 -1327 C ATOM 1583 O GLN A 205 39.898 14.577 53.487 1.00 53.41 O ANISOU 1583 O GLN A 205 6878 7156 6259 894 -698 -1372 O ATOM 1584 CB GLN A 205 38.771 12.684 51.089 1.00 59.81 C ANISOU 1584 CB GLN A 205 7658 7957 7108 735 -509 -1153 C ATOM 1585 CG GLN A 205 39.383 13.916 50.434 1.00 68.35 C ANISOU 1585 CG GLN A 205 8766 8898 8306 739 -607 -1189 C ATOM 1586 CD GLN A 205 40.894 13.834 50.331 1.00 78.98 C ANISOU 1586 CD GLN A 205 10140 10157 9712 686 -644 -1141 C ATOM 1587 OE1 GLN A 205 41.613 14.644 50.919 1.00 84.75 O ANISOU 1587 OE1 GLN A 205 10885 10842 10473 719 -728 -1204 O ATOM 1588 NE2 GLN A 205 41.385 12.849 49.587 1.00 78.11 N ANISOU 1588 NE2 GLN A 205 10033 10025 9621 606 -583 -1034 N ATOM 1589 N THR A 206 37.758 13.971 53.826 1.00 51.72 N ANISOU 1589 N THR A 206 6607 7137 5908 947 -582 -1393 N ATOM 1590 CA THR A 206 37.426 15.175 54.578 1.00 59.13 C ANISOU 1590 CA THR A 206 7542 8096 6830 1053 -665 -1532 C ATOM 1591 C THR A 206 37.906 15.074 56.024 1.00 54.71 C ANISOU 1591 C THR A 206 6988 7630 6170 1111 -684 -1585 C ATOM 1592 O THR A 206 37.911 16.062 56.752 1.00 56.15 O ANISOU 1592 O THR A 206 7174 7822 6340 1201 -769 -1706 O ATOM 1593 CB THR A 206 35.911 15.447 54.574 1.00 63.59 C ANISOU 1593 CB THR A 206 8062 8752 7347 1114 -632 -1593 C ATOM 1594 OG1 THR A 206 35.253 14.526 55.451 1.00 71.36 O ANISOU 1594 OG1 THR A 206 9010 9908 8196 1130 -537 -1576 O ATOM 1595 CG2 THR A 206 35.348 15.298 53.175 1.00 56.26 C ANISOU 1595 CG2 THR A 206 7123 7757 6498 1054 -597 -1529 C ATOM 1596 N THR A 207 38.311 13.875 56.427 1.00 53.66 N ANISOU 1596 N THR A 207 6858 7565 5965 1063 -611 -1494 N ATOM 1597 CA THR A 207 38.740 13.621 57.799 1.00 55.57 C ANISOU 1597 CA THR A 207 7108 7911 6096 1117 -618 -1527 C ATOM 1598 C THR A 207 40.229 13.909 57.989 1.00 59.77 C ANISOU 1598 C THR A 207 7678 8343 6688 1103 -706 -1534 C ATOM 1599 O THR A 207 41.017 13.804 57.047 1.00 58.27 O ANISOU 1599 O THR A 207 7507 8025 6608 1023 -722 -1466 O ATOM 1600 CB THR A 207 38.446 12.150 58.216 1.00 56.80 C ANISOU 1600 CB THR A 207 7251 8190 6140 1075 -497 -1418 C ATOM 1601 OG1 THR A 207 37.031 11.928 58.244 1.00 56.55 O ANISOU 1601 OG1 THR A 207 7174 8272 6042 1095 -417 -1424 O ATOM 1602 CG2 THR A 207 39.018 11.844 59.591 1.00 59.82 C ANISOU 1602 CG2 THR A 207 7651 8673 6407 1127 -508 -1437 C ATOM 1603 N ALA A 208 40.597 14.301 59.206 1.00 62.24 N ANISOU 1603 N ALA A 208 8000 8721 6927 1185 -766 -1624 N ATOM 1604 CA ALA A 208 41.995 14.310 59.636 1.00 69.08 C ANISOU 1604 CA ALA A 208 8897 9531 7820 1176 -836 -1625 C ATOM 1605 C ALA A 208 42.939 14.971 58.641 1.00 69.71 C ANISOU 1605 C ALA A 208 8993 9426 8068 1114 -915 -1617 C ATOM 1606 O ALA A 208 44.046 14.478 58.417 1.00 63.41 O ANISOU 1606 O ALA A 208 8210 8567 7316 1051 -922 -1546 O ATOM 1607 CB ALA A 208 42.458 12.888 59.921 1.00 67.02 C ANISOU 1607 CB ALA A 208 8645 9335 7482 1122 -752 -1503 C TER 1608 ALA A 208 ATOM 1609 N GLY B 848 67.265 11.321 13.375 1.00105.98 N ANISOU 1609 N GLY B 848 13370 12749 14149 139 3093 573 N ATOM 1610 CA GLY B 848 66.819 11.894 14.631 1.00102.72 C ANISOU 1610 CA GLY B 848 12924 12383 13724 64 3052 576 C ATOM 1611 C GLY B 848 66.504 10.840 15.676 1.00 94.16 C ANISOU 1611 C GLY B 848 11696 11416 12663 83 2808 606 C ATOM 1612 O GLY B 848 67.093 9.758 15.678 1.00 87.45 O ANISOU 1612 O GLY B 848 10709 10647 11873 120 2692 594 O ATOM 1613 N SER B 849 65.573 11.159 16.570 1.00 92.21 N ANISOU 1613 N SER B 849 11495 11164 12378 59 2750 647 N ATOM 1614 CA SER B 849 65.171 10.228 17.617 1.00 88.93 C ANISOU 1614 CA SER B 849 10976 10842 11970 61 2519 663 C ATOM 1615 C SER B 849 64.443 9.031 17.016 1.00 80.43 C ANISOU 1615 C SER B 849 9924 9786 10848 232 2358 745 C ATOM 1616 O SER B 849 63.894 9.112 15.917 1.00 75.65 O ANISOU 1616 O SER B 849 9449 9113 10182 327 2419 822 O ATOM 1617 CB SER B 849 64.277 10.924 18.644 1.00 92.83 C ANISOU 1617 CB SER B 849 11553 11285 12434 -17 2538 681 C ATOM 1618 OG SER B 849 62.975 11.128 18.127 1.00 95.96 O ANISOU 1618 OG SER B 849 12086 11591 12783 125 2566 800 O ATOM 1619 N TRP B 850 64.438 7.917 17.738 1.00 73.38 N ANISOU 1619 N TRP B 850 8924 8992 9966 248 2154 735 N ATOM 1620 CA TRP B 850 63.832 6.697 17.223 1.00 67.94 C ANISOU 1620 CA TRP B 850 8279 8330 9204 382 2018 798 C ATOM 1621 C TRP B 850 63.111 5.917 18.316 1.00 64.24 C ANISOU 1621 C TRP B 850 7776 7935 8697 390 1801 801 C ATOM 1622 O TRP B 850 63.614 5.777 19.431 1.00 64.49 O ANISOU 1622 O TRP B 850 7684 8029 8792 297 1712 737 O ATOM 1623 CB TRP B 850 64.890 5.819 16.554 1.00 66.23 C ANISOU 1623 CB TRP B 850 7990 8135 9038 428 2049 774 C ATOM 1624 CG TRP B 850 66.026 5.464 17.456 1.00 68.31 C ANISOU 1624 CG TRP B 850 8033 8492 9430 367 1991 714 C ATOM 1625 CD1 TRP B 850 67.115 6.231 17.744 1.00 70.29 C ANISOU 1625 CD1 TRP B 850 8150 8770 9786 247 2091 661 C ATOM 1626 CD2 TRP B 850 66.185 4.246 18.195 1.00 70.29 C ANISOU 1626 CD2 TRP B 850 8165 8835 9706 409 1811 723 C ATOM 1627 NE1 TRP B 850 67.945 5.567 18.614 1.00 74.21 N ANISOU 1627 NE1 TRP B 850 8427 9388 10383 205 1967 659 N ATOM 1628 CE2 TRP B 850 67.398 4.348 18.906 1.00 71.31 C ANISOU 1628 CE2 TRP B 850 8066 9054 9977 315 1798 698 C ATOM 1629 CE3 TRP B 850 65.421 3.082 18.322 1.00 70.32 C ANISOU 1629 CE3 TRP B 850 8239 8863 9616 508 1663 755 C ATOM 1630 CZ2 TRP B 850 67.863 3.328 19.733 1.00 69.52 C ANISOU 1630 CZ2 TRP B 850 7664 8933 9818 333 1633 726 C ATOM 1631 CZ3 TRP B 850 65.885 2.071 19.146 1.00 70.72 C ANISOU 1631 CZ3 TRP B 850 8144 9002 9723 531 1520 754 C ATOM 1632 CH2 TRP B 850 67.095 2.201 19.840 1.00 69.90 C ANISOU 1632 CH2 TRP B 850 7800 8981 9780 452 1502 749 C ATOM 1633 N ASP B 851 61.925 5.418 17.985 1.00 60.10 N ANISOU 1633 N ASP B 851 7367 7409 8057 478 1711 881 N ATOM 1634 CA ASP B 851 61.137 4.629 18.917 1.00 61.97 C ANISOU 1634 CA ASP B 851 7599 7709 8236 489 1511 875 C ATOM 1635 C ASP B 851 61.578 3.183 18.851 1.00 55.48 C ANISOU 1635 C ASP B 851 6742 6962 7375 548 1393 848 C ATOM 1636 O ASP B 851 61.689 2.612 17.770 1.00 56.06 O ANISOU 1636 O ASP B 851 6895 7023 7380 614 1452 892 O ATOM 1637 CB ASP B 851 59.646 4.734 18.592 1.00 67.39 C ANISOU 1637 CB ASP B 851 8414 8380 8810 550 1471 988 C ATOM 1638 CG ASP B 851 59.110 6.139 18.772 1.00 75.28 C ANISOU 1638 CG ASP B 851 9445 9285 9872 520 1612 1043 C ATOM 1639 OD1 ASP B 851 59.790 6.956 19.429 1.00 75.65 O ANISOU 1639 OD1 ASP B 851 9443 9279 10021 419 1722 961 O ATOM 1640 OD2 ASP B 851 58.009 6.428 18.258 1.00 80.03 O ANISOU 1640 OD2 ASP B 851 10123 9868 10416 587 1626 1183 O ATOM 1641 N CYS B 852 61.837 2.593 20.011 1.00 47.95 N ANISOU 1641 N CYS B 852 5688 6072 6459 509 1245 780 N ATOM 1642 CA CYS B 852 62.232 1.197 20.069 1.00 39.53 C ANISOU 1642 CA CYS B 852 4588 5067 5363 581 1145 765 C ATOM 1643 C CYS B 852 61.074 0.309 19.642 1.00 45.24 C ANISOU 1643 C CYS B 852 5490 5808 5892 656 1063 807 C ATOM 1644 O CYS B 852 59.955 0.443 20.126 1.00 51.31 O ANISOU 1644 O CYS B 852 6329 6592 6576 633 956 813 O ATOM 1645 CB CYS B 852 62.687 0.831 21.490 1.00 39.87 C ANISOU 1645 CB CYS B 852 4487 5179 5483 508 982 701 C ATOM 1646 SG CYS B 852 63.236 -0.889 21.698 1.00 44.34 S ANISOU 1646 SG CYS B 852 4995 5814 6037 618 870 704 S ATOM 1647 N GLU B 853 61.351 -0.609 18.732 1.00 43.14 N ANISOU 1647 N GLU B 853 5307 5535 5549 728 1131 839 N ATOM 1648 CA GLU B 853 60.323 -1.495 18.235 1.00 49.41 C ANISOU 1648 CA GLU B 853 6300 6356 6116 756 1073 883 C ATOM 1649 C GLU B 853 60.204 -2.718 19.133 1.00 47.38 C ANISOU 1649 C GLU B 853 6050 6163 5791 790 921 820 C ATOM 1650 O GLU B 853 59.335 -3.557 18.923 1.00 54.20 O ANISOU 1650 O GLU B 853 7087 7066 6442 795 856 835 O ATOM 1651 CB GLU B 853 60.646 -1.922 16.804 1.00 65.68 C ANISOU 1651 CB GLU B 853 8509 8356 8090 771 1254 945 C ATOM 1652 CG GLU B 853 61.947 -2.699 16.686 1.00 78.82 C ANISOU 1652 CG GLU B 853 10108 9972 9869 835 1381 911 C ATOM 1653 CD GLU B 853 62.364 -2.932 15.248 1.00 86.56 C ANISOU 1653 CD GLU B 853 11251 10841 10795 824 1619 962 C ATOM 1654 OE1 GLU B 853 61.599 -2.555 14.333 1.00 87.97 O ANISOU 1654 OE1 GLU B 853 11612 11000 10814 745 1653 1028 O ATOM 1655 OE2 GLU B 853 63.461 -3.493 15.036 1.00 87.12 O ANISOU 1655 OE2 GLU B 853 11270 10841 10991 885 1778 950 O ATOM 1656 N VAL B 854 61.075 -2.818 20.135 1.00 40.52 N ANISOU 1656 N VAL B 854 4998 5311 5087 795 858 758 N ATOM 1657 CA VAL B 854 60.949 -3.879 21.128 1.00 40.78 C ANISOU 1657 CA VAL B 854 5028 5400 5066 819 692 699 C ATOM 1658 C VAL B 854 60.115 -3.447 22.341 1.00 39.06 C ANISOU 1658 C VAL B 854 4794 5216 4832 726 498 632 C ATOM 1659 O VAL B 854 59.197 -4.166 22.744 1.00 40.43 O ANISOU 1659 O VAL B 854 5097 5423 4841 728 368 590 O ATOM 1660 CB VAL B 854 62.327 -4.422 21.586 1.00 47.09 C ANISOU 1660 CB VAL B 854 5637 6211 6045 872 709 702 C ATOM 1661 CG1 VAL B 854 62.158 -5.553 22.597 1.00 46.09 C ANISOU 1661 CG1 VAL B 854 5524 6137 5850 902 532 655 C ATOM 1662 CG2 VAL B 854 63.125 -4.905 20.387 1.00 53.31 C ANISOU 1662 CG2 VAL B 854 6456 6932 6867 972 945 771 C ATOM 1663 N CYS B 855 60.424 -2.285 22.921 1.00 36.69 N ANISOU 1663 N CYS B 855 4360 4892 4687 627 501 615 N ATOM 1664 CA CYS B 855 59.737 -1.854 24.145 1.00 33.98 C ANISOU 1664 CA CYS B 855 4024 4542 4347 508 361 546 C ATOM 1665 C CYS B 855 59.002 -0.514 24.024 1.00 38.07 C ANISOU 1665 C CYS B 855 4585 4988 4893 441 459 575 C ATOM 1666 O CYS B 855 58.316 -0.105 24.955 1.00 38.23 O ANISOU 1666 O CYS B 855 4643 4966 4918 343 395 526 O ATOM 1667 CB CYS B 855 60.705 -1.809 25.339 1.00 33.16 C ANISOU 1667 CB CYS B 855 3756 4464 4380 390 259 495 C ATOM 1668 SG CYS B 855 61.767 -0.339 25.346 1.00 39.54 S ANISOU 1668 SG CYS B 855 4400 5246 5377 251 409 525 S ATOM 1669 N LEU B 856 59.164 0.155 22.886 1.00 41.98 N ANISOU 1669 N LEU B 856 5086 5451 5414 493 634 658 N ATOM 1670 CA LEU B 856 58.418 1.381 22.562 1.00 41.32 C ANISOU 1670 CA LEU B 856 5055 5294 5352 470 757 723 C ATOM 1671 C LEU B 856 58.951 2.659 23.203 1.00 45.02 C ANISOU 1671 C LEU B 856 5451 5683 5971 339 872 689 C ATOM 1672 O LEU B 856 58.361 3.722 23.037 1.00 39.19 O ANISOU 1672 O LEU B 856 4767 4859 5265 323 1010 745 O ATOM 1673 CB LEU B 856 56.930 1.225 22.898 1.00 42.33 C ANISOU 1673 CB LEU B 856 5289 5420 5373 484 664 749 C ATOM 1674 CG LEU B 856 56.206 0.034 22.267 1.00 48.31 C ANISOU 1674 CG LEU B 856 6153 6272 5931 571 554 792 C ATOM 1675 CD1 LEU B 856 54.754 -0.018 22.737 1.00 46.58 C ANISOU 1675 CD1 LEU B 856 6007 6065 5624 562 458 819 C ATOM 1676 CD2 LEU B 856 56.289 0.094 20.745 1.00 53.41 C ANISOU 1676 CD2 LEU B 856 6852 6936 6504 636 672 917 C ATOM 1677 N VAL B 857 60.054 2.564 23.939 1.00 43.69 N ANISOU 1677 N VAL B 857 5166 5547 5888 232 827 614 N ATOM 1678 CA VAL B 857 60.642 3.746 24.568 1.00 41.23 C ANISOU 1678 CA VAL B 857 4808 5178 5680 51 941 580 C ATOM 1679 C VAL B 857 61.268 4.675 23.523 1.00 45.18 C ANISOU 1679 C VAL B 857 5286 5644 6238 79 1163 630 C ATOM 1680 O VAL B 857 61.892 4.215 22.564 1.00 42.82 O ANISOU 1680 O VAL B 857 4931 5393 5947 190 1191 662 O ATOM 1681 CB VAL B 857 61.694 3.351 25.644 1.00 38.97 C ANISOU 1681 CB VAL B 857 4386 4972 5450 -111 803 515 C ATOM 1682 CG1 VAL B 857 62.558 4.540 26.029 1.00 40.82 C ANISOU 1682 CG1 VAL B 857 4565 5183 5762 -327 941 500 C ATOM 1683 CG2 VAL B 857 61.000 2.780 26.868 1.00 37.87 C ANISOU 1683 CG2 VAL B 857 4313 4824 5254 -204 612 448 C ATOM 1684 N GLN B 858 61.093 5.981 23.703 1.00 45.79 N ANISOU 1684 N GLN B 858 5431 5617 6351 -29 1345 633 N ATOM 1685 CA GLN B 858 61.710 6.955 22.804 1.00 52.61 C ANISOU 1685 CA GLN B 858 6295 6437 7257 -25 1568 662 C ATOM 1686 C GLN B 858 63.191 7.149 23.129 1.00 57.07 C ANISOU 1686 C GLN B 858 6720 7076 7889 -183 1590 600 C ATOM 1687 O GLN B 858 63.556 7.390 24.281 1.00 60.01 O ANISOU 1687 O GLN B 858 7058 7470 8272 -399 1543 546 O ATOM 1688 CB GLN B 858 60.978 8.295 22.879 1.00 64.80 C ANISOU 1688 CB GLN B 858 7982 7831 8808 -76 1789 697 C ATOM 1689 CG GLN B 858 61.497 9.338 21.895 1.00 81.62 C ANISOU 1689 CG GLN B 858 10150 9901 10962 -59 2034 727 C ATOM 1690 CD GLN B 858 60.808 10.681 22.047 1.00 90.28 C ANISOU 1690 CD GLN B 858 11400 10832 12071 -104 2288 773 C ATOM 1691 OE1 GLN B 858 59.944 10.856 22.906 1.00 92.52 O ANISOU 1691 OE1 GLN B 858 11760 11032 12363 -151 2301 787 O ATOM 1692 NE2 GLN B 858 61.190 11.639 21.211 1.00 96.15 N ANISOU 1692 NE2 GLN B 858 12203 11507 12822 -87 2515 797 N ATOM 1693 N ASN B 859 64.037 7.049 22.108 1.00 60.34 N ANISOU 1693 N ASN B 859 7056 7530 8341 -97 1665 617 N ATOM 1694 CA ASN B 859 65.481 7.193 22.284 1.00 63.60 C ANISOU 1694 CA ASN B 859 7300 8033 8834 -227 1692 583 C ATOM 1695 C ASN B 859 66.090 8.358 21.502 1.00 74.67 C ANISOU 1695 C ASN B 859 8740 9376 10255 -279 1947 566 C ATOM 1696 O ASN B 859 65.513 8.823 20.522 1.00 76.16 O ANISOU 1696 O ASN B 859 9072 9458 10408 -157 2092 594 O ATOM 1697 CB ASN B 859 66.181 5.888 21.912 1.00 56.39 C ANISOU 1697 CB ASN B 859 6222 7222 7982 -90 1564 615 C ATOM 1698 CG ASN B 859 65.945 4.799 22.934 1.00 50.40 C ANISOU 1698 CG ASN B 859 5392 6545 7211 -95 1313 619 C ATOM 1699 OD1 ASN B 859 66.591 4.772 23.979 1.00 52.26 O ANISOU 1699 OD1 ASN B 859 5491 6875 7492 -271 1199 612 O ATOM 1700 ND2 ASN B 859 65.012 3.898 22.640 1.00 49.71 N ANISOU 1700 ND2 ASN B 859 5409 6430 7048 75 1221 637 N ATOM 1701 N LYS B 860 67.258 8.821 21.942 1.00 79.73 N ANISOU 1701 N LYS B 860 9253 10099 10941 -476 1992 529 N ATOM 1702 CA LYS B 860 67.958 9.912 21.267 1.00 87.55 C ANISOU 1702 CA LYS B 860 10280 11049 11935 -554 2237 492 C ATOM 1703 C LYS B 860 68.549 9.442 19.943 1.00 93.77 C ANISOU 1703 C LYS B 860 11000 11836 12794 -366 2302 508 C ATOM 1704 O LYS B 860 68.639 8.242 19.683 1.00 90.06 O ANISOU 1704 O LYS B 860 10426 11413 12380 -211 2167 553 O ATOM 1705 CB LYS B 860 69.085 10.463 22.144 1.00 88.31 C ANISOU 1705 CB LYS B 860 10248 11267 12038 -855 2252 455 C ATOM 1706 CG LYS B 860 68.676 10.846 23.555 1.00 88.91 C ANISOU 1706 CG LYS B 860 10404 11346 12033 -1115 2188 436 C ATOM 1707 CD LYS B 860 69.896 11.260 24.368 1.00 93.36 C ANISOU 1707 CD LYS B 860 10826 12067 12579 -1457 2171 426 C ATOM 1708 CE LYS B 860 69.596 11.307 25.859 1.00 96.26 C ANISOU 1708 CE LYS B 860 11251 12460 12864 -1750 2043 423 C ATOM 1709 NZ LYS B 860 68.636 12.389 26.213 1.00 97.93 N ANISOU 1709 NZ LYS B 860 11789 12464 12957 -1880 2274 362 N ATOM 1710 N ALA B 861 68.957 10.395 19.112 1.00102.10 N ANISOU 1710 N ALA B 861 12140 12816 13837 -394 2535 466 N ATOM 1711 CA ALA B 861 69.612 10.074 17.851 1.00108.31 C ANISOU 1711 CA ALA B 861 12889 13572 14691 -262 2636 462 C ATOM 1712 C ALA B 861 70.958 9.414 18.119 1.00114.98 C ANISOU 1712 C ALA B 861 13451 14565 15671 -311 2569 471 C ATOM 1713 O ALA B 861 71.329 8.448 17.454 1.00116.11 O ANISOU 1713 O ALA B 861 13507 14702 15909 -151 2555 510 O ATOM 1714 CB ALA B 861 69.789 11.326 17.011 1.00109.59 C ANISOU 1714 CB ALA B 861 13218 13619 14804 -313 2901 400 C ATOM 1715 N ASP B 862 71.682 9.941 19.103 1.00119.51 N ANISOU 1715 N ASP B 862 13887 15270 16253 -548 2541 453 N ATOM 1716 CA ASP B 862 72.977 9.392 19.490 1.00124.34 C ANISOU 1716 CA ASP B 862 14181 16059 17002 -622 2455 504 C ATOM 1717 C ASP B 862 72.871 7.928 19.894 1.00115.56 C ANISOU 1717 C ASP B 862 12903 15020 15985 -464 2225 605 C ATOM 1718 O ASP B 862 73.741 7.120 19.567 1.00118.70 O ANISOU 1718 O ASP B 862 13081 15479 16542 -354 2219 677 O ATOM 1719 CB ASP B 862 73.582 10.198 20.639 1.00135.95 C ANISOU 1719 CB ASP B 862 15556 17682 18415 -961 2419 494 C ATOM 1720 CG ASP B 862 74.259 11.466 20.167 1.00145.76 C ANISOU 1720 CG ASP B 862 16874 18910 19600 -1136 2672 406 C ATOM 1721 OD1 ASP B 862 74.093 11.823 18.982 1.00147.89 O ANISOU 1721 OD1 ASP B 862 17306 19022 19865 -985 2874 340 O ATOM 1722 OD2 ASP B 862 74.960 12.104 20.980 1.00150.15 O ANISOU 1722 OD2 ASP B 862 17341 19613 20097 -1447 2670 403 O ATOM 1723 N SER B 863 71.803 7.596 20.612 1.00101.50 N ANISOU 1723 N SER B 863 11235 13218 14111 -450 2058 613 N ATOM 1724 CA SER B 863 71.589 6.235 21.091 1.00 87.62 C ANISOU 1724 CA SER B 863 9362 11522 12407 -316 1837 692 C ATOM 1725 C SER B 863 71.688 5.208 19.970 1.00 80.25 C ANISOU 1725 C SER B 863 8424 10509 11559 -38 1912 733 C ATOM 1726 O SER B 863 70.982 5.297 18.963 1.00 73.43 O ANISOU 1726 O SER B 863 7789 9493 10617 87 2040 693 O ATOM 1727 CB SER B 863 70.231 6.115 21.789 1.00 82.15 C ANISOU 1727 CB SER B 863 8863 10774 11577 -322 1694 664 C ATOM 1728 OG SER B 863 70.254 6.728 23.066 1.00 80.29 O ANISOU 1728 OG SER B 863 8608 10615 11285 -600 1596 645 O ATOM 1729 N THR B 864 72.576 4.236 20.153 1.00 79.89 N ANISOU 1729 N THR B 864 8124 10562 11671 40 1846 831 N ATOM 1730 CA THR B 864 72.704 3.127 19.220 1.00 78.28 C ANISOU 1730 CA THR B 864 7931 10262 11551 291 1946 882 C ATOM 1731 C THR B 864 71.820 1.974 19.683 1.00 76.96 C ANISOU 1731 C THR B 864 7849 10089 11305 418 1767 916 C ATOM 1732 O THR B 864 71.317 1.196 18.871 1.00 77.42 O ANISOU 1732 O THR B 864 8082 10023 11310 591 1853 918 O ATOM 1733 CB THR B 864 74.163 2.640 19.114 1.00 83.02 C ANISOU 1733 CB THR B 864 8206 10945 12394 342 2025 994 C ATOM 1734 OG1 THR B 864 74.528 1.938 20.310 1.00 83.87 O ANISOU 1734 OG1 THR B 864 8055 11228 12585 316 1790 1116 O ATOM 1735 CG2 THR B 864 75.103 3.818 18.914 1.00 83.21 C ANISOU 1735 CG2 THR B 864 8106 11026 12483 165 2161 959 C ATOM 1736 N LYS B 865 71.635 1.877 20.997 1.00 72.01 N ANISOU 1736 N LYS B 865 7120 9592 10649 300 1523 937 N ATOM 1737 CA LYS B 865 70.762 0.865 21.586 1.00 66.06 C ANISOU 1737 CA LYS B 865 6458 8840 9801 389 1333 947 C ATOM 1738 C LYS B 865 69.771 1.514 22.550 1.00 61.32 C ANISOU 1738 C LYS B 865 5997 8258 9044 209 1166 865 C ATOM 1739 O LYS B 865 69.992 2.629 23.018 1.00 63.48 O ANISOU 1739 O LYS B 865 6240 8572 9308 -9 1177 830 O ATOM 1740 CB LYS B 865 71.582 -0.204 22.309 1.00 68.73 C ANISOU 1740 CB LYS B 865 6524 9302 10288 450 1196 1077 C ATOM 1741 CG LYS B 865 72.451 0.331 23.435 1.00 72.78 C ANISOU 1741 CG LYS B 865 6754 10005 10896 216 1036 1146 C ATOM 1742 CD LYS B 865 73.169 -0.798 24.157 1.00 80.25 C ANISOU 1742 CD LYS B 865 7421 11080 11989 291 874 1313 C ATOM 1743 CE LYS B 865 74.217 -0.267 25.129 1.00 90.20 C ANISOU 1743 CE LYS B 865 8356 12559 13357 33 721 1431 C ATOM 1744 NZ LYS B 865 73.621 0.476 26.274 1.00 92.16 N ANISOU 1744 NZ LYS B 865 8720 12870 13428 -287 516 1345 N ATOM 1745 N CYS B 866 68.679 0.812 22.843 1.00 54.30 N ANISOU 1745 N CYS B 866 5278 7328 8026 288 1037 834 N ATOM 1746 CA CYS B 866 67.634 1.352 23.708 1.00 48.47 C ANISOU 1746 CA CYS B 866 4691 6573 7152 138 909 756 C ATOM 1747 C CYS B 866 68.123 1.567 25.137 1.00 52.92 C ANISOU 1747 C CYS B 866 5099 7255 7755 -102 723 768 C ATOM 1748 O CYS B 866 68.713 0.670 25.744 1.00 56.59 O ANISOU 1748 O CYS B 866 5382 7825 8292 -87 563 842 O ATOM 1749 CB CYS B 866 66.401 0.438 23.709 1.00 41.95 C ANISOU 1749 CB CYS B 866 4064 5693 6183 274 805 725 C ATOM 1750 SG CYS B 866 65.017 1.117 24.637 1.00 45.27 S ANISOU 1750 SG CYS B 866 4681 6057 6462 117 697 635 S ATOM 1751 N ILE B 867 67.863 2.755 25.673 1.00 50.97 N ANISOU 1751 N ILE B 867 4937 6979 7449 -339 758 706 N ATOM 1752 CA ILE B 867 68.272 3.096 27.035 1.00 56.24 C ANISOU 1752 CA ILE B 867 5515 7743 8113 -645 604 712 C ATOM 1753 C ILE B 867 67.577 2.198 28.057 1.00 53.51 C ANISOU 1753 C ILE B 867 5229 7403 7697 -667 359 690 C ATOM 1754 O ILE B 867 68.081 1.972 29.164 1.00 49.23 O ANISOU 1754 O ILE B 867 4565 6970 7170 -877 166 731 O ATOM 1755 CB ILE B 867 67.967 4.574 27.354 1.00 61.14 C ANISOU 1755 CB ILE B 867 6300 8280 8649 -907 755 635 C ATOM 1756 CG1 ILE B 867 68.436 4.930 28.767 1.00 67.49 C ANISOU 1756 CG1 ILE B 867 7049 9177 9417 -1290 614 644 C ATOM 1757 CG2 ILE B 867 66.480 4.859 27.187 1.00 55.32 C ANISOU 1757 CG2 ILE B 867 5850 7362 7808 -816 837 554 C ATOM 1758 CD1 ILE B 867 69.908 4.687 29.002 1.00 70.71 C ANISOU 1758 CD1 ILE B 867 7136 9801 9931 -1411 508 768 C ATOM 1759 N ALA B 868 66.417 1.679 27.672 1.00 41.56 N ANISOU 1759 N ALA B 868 3911 5781 6098 -466 361 631 N ATOM 1760 CA ALA B 868 65.634 0.830 28.555 1.00 46.83 C ANISOU 1760 CA ALA B 868 4676 6438 6680 -474 149 584 C ATOM 1761 C ALA B 868 66.051 -0.629 28.449 1.00 45.47 C ANISOU 1761 C ALA B 868 4375 6352 6548 -267 14 653 C ATOM 1762 O ALA B 868 66.576 -1.197 29.406 1.00 38.81 O ANISOU 1762 O ALA B 868 3397 5607 5741 -371 -186 701 O ATOM 1763 CB ALA B 868 64.151 0.975 28.259 1.00 47.87 C ANISOU 1763 CB ALA B 868 5073 6427 6688 -379 215 497 C ATOM 1764 N CYS B 869 65.831 -1.214 27.272 1.00 41.36 N ANISOU 1764 N CYS B 869 3911 5788 6015 9 141 672 N ATOM 1765 CA CYS B 869 65.891 -2.665 27.094 1.00 42.29 C ANISOU 1765 CA CYS B 869 4014 5934 6121 224 70 715 C ATOM 1766 C CYS B 869 67.140 -3.167 26.371 1.00 50.08 C ANISOU 1766 C CYS B 869 4783 6971 7273 385 193 847 C ATOM 1767 O CYS B 869 67.292 -4.375 26.167 1.00 48.67 O ANISOU 1767 O CYS B 869 4598 6793 7102 576 192 901 O ATOM 1768 CB CYS B 869 64.658 -3.153 26.332 1.00 41.37 C ANISOU 1768 CB CYS B 869 4165 5722 5831 392 138 647 C ATOM 1769 SG CYS B 869 64.716 -2.826 24.558 1.00 43.85 S ANISOU 1769 SG CYS B 869 4556 5957 6146 555 431 691 S ATOM 1770 N GLU B 870 68.013 -2.246 25.971 1.00 51.59 N ANISOU 1770 N GLU B 870 4817 7191 7595 308 327 897 N ATOM 1771 CA GLU B 870 69.294 -2.602 25.357 1.00 58.71 C ANISOU 1771 CA GLU B 870 5477 8140 8691 436 458 1030 C ATOM 1772 C GLU B 870 69.156 -3.102 23.920 1.00 59.08 C ANISOU 1772 C GLU B 870 5667 8056 8725 680 711 1032 C ATOM 1773 O GLU B 870 70.145 -3.477 23.291 1.00 61.90 O ANISOU 1773 O GLU B 870 5865 8406 9248 810 874 1136 O ATOM 1774 CB GLU B 870 70.028 -3.653 26.203 1.00 59.75 C ANISOU 1774 CB GLU B 870 5375 8388 8939 481 285 1165 C ATOM 1775 CG GLU B 870 70.150 -3.304 27.679 1.00 72.68 C ANISOU 1775 CG GLU B 870 6895 10158 10563 201 5 1179 C ATOM 1776 CD GLU B 870 71.141 -2.186 27.939 1.00 88.66 C ANISOU 1776 CD GLU B 870 8687 12302 12699 -46 14 1248 C ATOM 1777 OE1 GLU B 870 71.646 -1.594 26.960 1.00 94.35 O ANISOU 1777 OE1 GLU B 870 9355 12992 13502 11 243 1258 O ATOM 1778 OE2 GLU B 870 71.421 -1.902 29.124 1.00 94.55 O ANISOU 1778 OE2 GLU B 870 9321 13172 13432 -324 -204 1291 O ATOM 1779 N SER B 871 67.931 -3.118 23.406 1.00 55.92 N ANISOU 1779 N SER B 871 5568 7551 8126 725 750 930 N ATOM 1780 CA SER B 871 67.699 -3.568 22.042 1.00 61.62 C ANISOU 1780 CA SER B 871 6476 8152 8787 893 979 934 C ATOM 1781 C SER B 871 68.394 -2.632 21.060 1.00 64.74 C ANISOU 1781 C SER B 871 6813 8492 9295 870 1207 949 C ATOM 1782 O SER B 871 68.481 -1.429 21.299 1.00 58.02 O ANISOU 1782 O SER B 871 5901 7673 8470 714 1189 909 O ATOM 1783 CB SER B 871 66.202 -3.649 21.743 1.00 61.35 C ANISOU 1783 CB SER B 871 6756 8054 8499 892 941 847 C ATOM 1784 OG SER B 871 65.973 -3.924 20.374 1.00 71.27 O ANISOU 1784 OG SER B 871 8210 9202 9667 987 1159 863 O ATOM 1785 N ALA B 872 68.902 -3.188 19.964 1.00 71.64 N ANISOU 1785 N ALA B 872 7727 9267 10227 1011 1443 1000 N ATOM 1786 CA ALA B 872 69.586 -2.389 18.951 1.00 74.79 C ANISOU 1786 CA ALA B 872 8097 9590 10731 991 1679 1003 C ATOM 1787 C ALA B 872 68.595 -1.550 18.146 1.00 73.60 C ANISOU 1787 C ALA B 872 8219 9349 10395 918 1745 920 C ATOM 1788 O ALA B 872 67.444 -1.946 17.959 1.00 73.17 O ANISOU 1788 O ALA B 872 8405 9260 10135 936 1683 895 O ATOM 1789 CB ALA B 872 70.403 -3.283 18.030 1.00 76.46 C ANISOU 1789 CB ALA B 872 8298 9686 11066 1151 1942 1082 C ATOM 1790 N LYS B 873 69.052 -0.394 17.673 1.00 75.37 N ANISOU 1790 N LYS B 873 8400 9545 10692 830 1869 890 N ATOM 1791 CA LYS B 873 68.210 0.520 16.906 1.00 81.34 C ANISOU 1791 CA LYS B 873 9390 10217 11300 765 1942 838 C ATOM 1792 C LYS B 873 67.435 -0.191 15.797 1.00 83.63 C ANISOU 1792 C LYS B 873 9970 10390 11417 836 2040 860 C ATOM 1793 O LYS B 873 68.020 -0.679 14.830 1.00 85.38 O ANISOU 1793 O LYS B 873 10261 10500 11681 889 2253 883 O ATOM 1794 CB LYS B 873 69.059 1.648 16.317 1.00 83.41 C ANISOU 1794 CB LYS B 873 9582 10432 11676 688 2128 807 C ATOM 1795 CG LYS B 873 68.328 2.523 15.317 1.00 85.41 C ANISOU 1795 CG LYS B 873 10084 10573 11793 643 2244 776 C ATOM 1796 CD LYS B 873 69.293 3.462 14.612 1.00 89.72 C ANISOU 1796 CD LYS B 873 10587 11052 12451 581 2461 732 C ATOM 1797 CE LYS B 873 69.733 4.600 15.517 1.00 92.51 C ANISOU 1797 CE LYS B 873 10772 11507 12873 446 2416 685 C ATOM 1798 NZ LYS B 873 68.740 5.707 15.531 1.00 91.63 N ANISOU 1798 NZ LYS B 873 10839 11354 12621 372 2410 656 N TER 1799 LYS B 873 ATOM 1800 N GLN C 8 48.238 -12.191 11.904 1.00 69.16 N ANISOU 1800 N GLN C 8 8451 8737 9088 707 61 333 N ATOM 1801 CA GLN C 8 47.045 -11.385 12.148 1.00 70.11 C ANISOU 1801 CA GLN C 8 8610 8843 9187 589 37 296 C ATOM 1802 C GLN C 8 45.955 -11.705 11.129 1.00 62.35 C ANISOU 1802 C GLN C 8 7732 7782 8177 583 68 240 C ATOM 1803 O GLN C 8 46.206 -11.739 9.923 1.00 63.45 O ANISOU 1803 O GLN C 8 7881 7915 8311 633 123 219 O ATOM 1804 CB GLN C 8 47.389 -9.894 12.114 1.00 78.92 C ANISOU 1804 CB GLN C 8 9633 10044 10310 520 40 300 C ATOM 1805 CG GLN C 8 46.238 -8.981 12.508 1.00 86.66 C ANISOU 1805 CG GLN C 8 10645 11011 11269 408 14 266 C ATOM 1806 CD GLN C 8 46.690 -7.560 12.792 1.00 93.12 C ANISOU 1806 CD GLN C 8 11381 11906 12093 338 5 279 C ATOM 1807 OE1 GLN C 8 47.872 -7.236 12.674 1.00 97.43 O ANISOU 1807 OE1 GLN C 8 11840 12521 12657 361 14 316 O ATOM 1808 NE2 GLN C 8 45.747 -6.705 13.173 1.00 91.46 N ANISOU 1808 NE2 GLN C 8 11200 11684 11866 250 -14 250 N ATOM 1809 N VAL C 9 44.747 -11.959 11.619 1.00 45.68 N ANISOU 1809 N VAL C 9 5699 5616 6042 519 34 218 N ATOM 1810 CA VAL C 9 43.621 -12.265 10.744 1.00 34.85 C ANISOU 1810 CA VAL C 9 4425 4177 4641 497 53 170 C ATOM 1811 C VAL C 9 42.936 -10.970 10.316 1.00 33.72 C ANISOU 1811 C VAL C 9 4255 4069 4490 417 62 141 C ATOM 1812 O VAL C 9 42.388 -10.242 11.153 1.00 34.84 O ANISOU 1812 O VAL C 9 4370 4237 4631 341 29 142 O ATOM 1813 CB VAL C 9 42.598 -13.175 11.443 1.00 35.60 C ANISOU 1813 CB VAL C 9 4613 4203 4711 459 10 166 C ATOM 1814 CG1 VAL C 9 41.406 -13.420 10.557 1.00 40.49 C ANISOU 1814 CG1 VAL C 9 5324 4765 5297 421 23 123 C ATOM 1815 CG2 VAL C 9 43.248 -14.509 11.829 1.00 40.77 C ANISOU 1815 CG2 VAL C 9 5312 4808 5371 541 -1 196 C ATOM 1816 N GLN C 10 42.985 -10.681 9.018 1.00 34.07 N ANISOU 1816 N GLN C 10 4308 4112 4527 439 108 117 N ATOM 1817 CA GLN C 10 42.340 -9.485 8.481 1.00 30.34 C ANISOU 1817 CA GLN C 10 3817 3665 4046 372 116 92 C ATOM 1818 C GLN C 10 41.696 -9.766 7.118 1.00 34.50 C ANISOU 1818 C GLN C 10 4420 4146 4544 378 148 57 C ATOM 1819 O GLN C 10 42.134 -10.646 6.363 1.00 35.37 O ANISOU 1819 O GLN C 10 4577 4220 4642 447 181 50 O ATOM 1820 CB GLN C 10 43.325 -8.318 8.398 1.00 33.67 C ANISOU 1820 CB GLN C 10 4138 4165 4491 368 134 111 C ATOM 1821 CG GLN C 10 44.483 -8.544 7.444 1.00 41.25 C ANISOU 1821 CG GLN C 10 5066 5150 5457 447 185 122 C ATOM 1822 CD GLN C 10 45.543 -7.455 7.531 1.00 53.82 C ANISOU 1822 CD GLN C 10 6549 6829 7070 433 195 151 C ATOM 1823 OE1 GLN C 10 45.236 -6.275 7.736 1.00 46.44 O ANISOU 1823 OE1 GLN C 10 5586 5925 6137 357 178 148 O ATOM 1824 NE2 GLN C 10 46.801 -7.846 7.359 1.00 60.39 N ANISOU 1824 NE2 GLN C 10 7321 7705 7918 508 224 182 N ATOM 1825 N PHE C 11 40.646 -9.008 6.832 1.00 32.57 N ANISOU 1825 N PHE C 11 4187 3902 4285 308 137 35 N ATOM 1826 CA PHE C 11 39.854 -9.169 5.630 1.00 27.54 C ANISOU 1826 CA PHE C 11 3620 3227 3617 294 154 6 C ATOM 1827 C PHE C 11 39.545 -7.789 5.063 1.00 27.96 C ANISOU 1827 C PHE C 11 3630 3321 3672 248 162 -1 C ATOM 1828 O PHE C 11 39.149 -6.898 5.822 1.00 28.49 O ANISOU 1828 O PHE C 11 3651 3418 3755 198 136 5 O ATOM 1829 CB PHE C 11 38.519 -9.786 6.005 1.00 28.58 C ANISOU 1829 CB PHE C 11 3821 3312 3725 241 115 -5 C ATOM 1830 CG PHE C 11 38.639 -11.143 6.629 1.00 28.29 C ANISOU 1830 CG PHE C 11 3843 3224 3680 272 98 4 C ATOM 1831 CD1 PHE C 11 38.898 -12.255 5.841 1.00 35.68 C ANISOU 1831 CD1 PHE C 11 4865 4100 4592 325 121 -9 C ATOM 1832 CD2 PHE C 11 38.487 -11.303 7.988 1.00 33.46 C ANISOU 1832 CD2 PHE C 11 4477 3888 4349 247 59 24 C ATOM 1833 CE1 PHE C 11 39.013 -13.506 6.395 1.00 36.35 C ANISOU 1833 CE1 PHE C 11 5016 4127 4669 357 104 1 C ATOM 1834 CE2 PHE C 11 38.605 -12.569 8.565 1.00 35.14 C ANISOU 1834 CE2 PHE C 11 4750 4048 4552 273 40 37 C ATOM 1835 CZ PHE C 11 38.859 -13.670 7.761 1.00 38.36 C ANISOU 1835 CZ PHE C 11 5246 4390 4939 329 61 26 C ATOM 1836 N LYS C 12 39.679 -7.636 3.743 1.00 28.17 N ANISOU 1836 N LYS C 12 3681 3344 3679 263 197 -16 N ATOM 1837 CA LYS C 12 39.228 -6.414 3.067 1.00 27.60 C ANISOU 1837 CA LYS C 12 3586 3298 3602 216 200 -21 C ATOM 1838 C LYS C 12 37.711 -6.466 2.935 1.00 30.17 C ANISOU 1838 C LYS C 12 3964 3593 3905 159 166 -36 C ATOM 1839 O LYS C 12 37.154 -7.436 2.405 1.00 31.20 O ANISOU 1839 O LYS C 12 4172 3678 4004 159 163 -50 O ATOM 1840 CB LYS C 12 39.865 -6.251 1.681 1.00 29.59 C ANISOU 1840 CB LYS C 12 3850 3560 3834 245 248 -29 C ATOM 1841 CG LYS C 12 39.268 -5.061 0.885 1.00 28.75 C ANISOU 1841 CG LYS C 12 3737 3470 3715 192 245 -32 C ATOM 1842 CD LYS C 12 39.972 -4.837 -0.434 1.00 29.30 C ANISOU 1842 CD LYS C 12 3816 3557 3762 214 294 -35 C ATOM 1843 CE LYS C 12 39.140 -3.935 -1.351 1.00 30.83 C ANISOU 1843 CE LYS C 12 4032 3750 3933 160 282 -39 C ATOM 1844 NZ LYS C 12 39.961 -3.312 -2.425 1.00 31.78 N ANISOU 1844 NZ LYS C 12 4137 3902 4035 166 326 -33 N ATOM 1845 N LEU C 13 37.044 -5.437 3.445 1.00 28.05 N ANISOU 1845 N LEU C 13 3654 3350 3653 112 141 -30 N ATOM 1846 CA LEU C 13 35.598 -5.391 3.408 1.00 27.46 C ANISOU 1846 CA LEU C 13 3609 3262 3563 62 109 -37 C ATOM 1847 C LEU C 13 35.230 -4.151 2.629 1.00 28.53 C ANISOU 1847 C LEU C 13 3723 3419 3699 38 112 -35 C ATOM 1848 O LEU C 13 35.632 -3.051 2.987 1.00 28.60 O ANISOU 1848 O LEU C 13 3679 3456 3733 35 116 -27 O ATOM 1849 CB LEU C 13 35.026 -5.319 4.827 1.00 29.43 C ANISOU 1849 CB LEU C 13 3829 3523 3831 35 78 -30 C ATOM 1850 CG LEU C 13 33.493 -5.320 4.951 1.00 30.65 C ANISOU 1850 CG LEU C 13 3999 3676 3971 -15 47 -32 C ATOM 1851 CD1 LEU C 13 33.104 -5.747 6.364 1.00 32.11 C ANISOU 1851 CD1 LEU C 13 4172 3866 4163 -35 25 -26 C ATOM 1852 CD2 LEU C 13 32.848 -3.965 4.597 1.00 29.58 C ANISOU 1852 CD2 LEU C 13 3825 3568 3845 -36 44 -29 C ATOM 1853 N VAL C 14 34.465 -4.308 1.558 1.00 26.71 N ANISOU 1853 N VAL C 14 3539 3172 3437 17 106 -41 N ATOM 1854 CA VAL C 14 34.019 -3.115 0.836 1.00 26.92 C ANISOU 1854 CA VAL C 14 3547 3217 3463 -6 102 -33 C ATOM 1855 C VAL C 14 32.613 -2.693 1.253 1.00 27.68 C ANISOU 1855 C VAL C 14 3628 3324 3566 -43 64 -26 C ATOM 1856 O VAL C 14 31.719 -3.516 1.415 1.00 28.31 O ANISOU 1856 O VAL C 14 3734 3394 3628 -67 39 -26 O ATOM 1857 CB VAL C 14 34.131 -3.275 -0.702 1.00 31.61 C ANISOU 1857 CB VAL C 14 4193 3798 4019 -7 119 -38 C ATOM 1858 CG1 VAL C 14 35.592 -3.292 -1.101 1.00 30.02 C ANISOU 1858 CG1 VAL C 14 3985 3605 3818 35 166 -41 C ATOM 1859 CG2 VAL C 14 33.398 -4.540 -1.195 1.00 36.13 C ANISOU 1859 CG2 VAL C 14 4842 4336 4549 -25 103 -49 C ATOM 1860 N LEU C 15 32.427 -1.390 1.435 1.00 28.68 N ANISOU 1860 N LEU C 15 3710 3470 3716 -47 60 -16 N ATOM 1861 CA LEU C 15 31.165 -0.891 1.919 1.00 26.29 C ANISOU 1861 CA LEU C 15 3382 3183 3425 -67 32 -8 C ATOM 1862 C LEU C 15 30.596 -0.059 0.791 1.00 27.88 C ANISOU 1862 C LEU C 15 3589 3388 3617 -77 21 7 C ATOM 1863 O LEU C 15 31.172 0.962 0.427 1.00 31.77 O ANISOU 1863 O LEU C 15 4071 3879 4120 -66 35 12 O ATOM 1864 CB LEU C 15 31.413 -0.047 3.176 1.00 28.95 C ANISOU 1864 CB LEU C 15 3673 3532 3797 -56 38 -11 C ATOM 1865 CG LEU C 15 30.292 0.777 3.804 1.00 28.62 C ANISOU 1865 CG LEU C 15 3598 3505 3770 -61 24 -5 C ATOM 1866 CD1 LEU C 15 29.136 -0.115 4.223 1.00 34.70 C ANISOU 1866 CD1 LEU C 15 4364 4292 4528 -82 3 -2 C ATOM 1867 CD2 LEU C 15 30.872 1.534 5.020 1.00 31.90 C ANISOU 1867 CD2 LEU C 15 3987 3922 4210 -51 37 -15 C ATOM 1868 N VAL C 16 29.488 -0.512 0.214 1.00 26.17 N ANISOU 1868 N VAL C 16 3390 3177 3376 -104 -7 17 N ATOM 1869 CA VAL C 16 28.938 0.167 -0.957 1.00 29.78 C ANISOU 1869 CA VAL C 16 3856 3640 3819 -116 -24 37 C ATOM 1870 C VAL C 16 27.456 0.438 -0.781 1.00 33.59 C ANISOU 1870 C VAL C 16 4304 4151 4307 -131 -60 59 C ATOM 1871 O VAL C 16 26.837 -0.056 0.153 1.00 31.99 O ANISOU 1871 O VAL C 16 4076 3966 4113 -140 -69 58 O ATOM 1872 CB VAL C 16 29.144 -0.662 -2.231 1.00 35.28 C ANISOU 1872 CB VAL C 16 4618 4320 4467 -138 -24 34 C ATOM 1873 CG1 VAL C 16 30.637 -0.788 -2.557 1.00 37.27 C ANISOU 1873 CG1 VAL C 16 4895 4552 4712 -112 20 16 C ATOM 1874 CG2 VAL C 16 28.500 -2.047 -2.067 1.00 32.84 C ANISOU 1874 CG2 VAL C 16 4344 4006 4129 -170 -46 28 C ATOM 1875 N GLY C 17 26.890 1.224 -1.694 1.00 27.59 N ANISOU 1875 N GLY C 17 3540 3401 3543 -135 -81 85 N ATOM 1876 CA GLY C 17 25.522 1.681 -1.570 1.00 30.84 C ANISOU 1876 CA GLY C 17 3905 3847 3966 -137 -113 113 C ATOM 1877 C GLY C 17 25.436 3.107 -2.087 1.00 30.85 C ANISOU 1877 C GLY C 17 3891 3843 3987 -107 -118 135 C ATOM 1878 O GLY C 17 26.459 3.775 -2.243 1.00 29.59 O ANISOU 1878 O GLY C 17 3754 3653 3837 -89 -92 124 O ATOM 1879 N ASP C 18 24.219 3.570 -2.364 1.00 28.99 N ANISOU 1879 N ASP C 18 3618 3638 3757 -103 -152 170 N ATOM 1880 CA ASP C 18 24.020 4.916 -2.895 1.00 32.63 C ANISOU 1880 CA ASP C 18 4071 4090 4238 -70 -162 198 C ATOM 1881 C ASP C 18 24.623 5.989 -2.002 1.00 35.44 C ANISOU 1881 C ASP C 18 4418 4414 4634 -20 -127 178 C ATOM 1882 O ASP C 18 24.721 5.811 -0.786 1.00 31.15 O ANISOU 1882 O ASP C 18 3851 3874 4111 -5 -103 152 O ATOM 1883 CB ASP C 18 22.535 5.207 -3.033 1.00 36.30 C ANISOU 1883 CB ASP C 18 4480 4601 4711 -59 -201 241 C ATOM 1884 CG ASP C 18 21.944 4.616 -4.282 1.00 38.78 C ANISOU 1884 CG ASP C 18 4812 4942 4982 -112 -249 275 C ATOM 1885 OD1 ASP C 18 22.690 3.950 -5.035 1.00 35.29 O ANISOU 1885 OD1 ASP C 18 4435 4476 4498 -155 -246 258 O ATOM 1886 OD2 ASP C 18 20.732 4.830 -4.506 1.00 40.14 O ANISOU 1886 OD2 ASP C 18 4931 5160 5158 -109 -288 318 O ATOM 1887 N GLY C 19 25.004 7.117 -2.600 1.00 32.75 N ANISOU 1887 N GLY C 19 4103 4040 4300 -1 -128 193 N ATOM 1888 CA GLY C 19 25.418 8.256 -1.810 1.00 29.98 C ANISOU 1888 CA GLY C 19 3754 3655 3984 41 -102 180 C ATOM 1889 C GLY C 19 24.305 8.660 -0.862 1.00 35.80 C ANISOU 1889 C GLY C 19 4439 4411 4753 90 -102 185 C ATOM 1890 O GLY C 19 23.124 8.622 -1.218 1.00 31.18 O ANISOU 1890 O GLY C 19 3814 3862 4169 104 -132 218 O ATOM 1891 N GLY C 20 24.678 9.026 0.358 1.00 28.86 N ANISOU 1891 N GLY C 20 3558 3512 3895 114 -69 152 N ATOM 1892 CA GLY C 20 23.719 9.523 1.321 1.00 29.58 C ANISOU 1892 CA GLY C 20 3607 3617 4013 167 -57 151 C ATOM 1893 C GLY C 20 23.046 8.477 2.181 1.00 32.47 C ANISOU 1893 C GLY C 20 3920 4040 4376 156 -50 140 C ATOM 1894 O GLY C 20 22.188 8.791 3.008 1.00 35.59 O ANISOU 1894 O GLY C 20 4273 4459 4790 200 -35 139 O ATOM 1895 N THR C 21 23.449 7.230 2.009 1.00 31.38 N ANISOU 1895 N THR C 21 3789 3922 4214 100 -58 131 N ATOM 1896 CA THR C 21 22.828 6.136 2.749 1.00 28.46 C ANISOU 1896 CA THR C 21 3376 3602 3834 77 -57 125 C ATOM 1897 C THR C 21 23.383 5.975 4.163 1.00 32.90 C ANISOU 1897 C THR C 21 3943 4155 4403 79 -21 85 C ATOM 1898 O THR C 21 22.740 5.354 5.009 1.00 32.70 O ANISOU 1898 O THR C 21 3880 4172 4374 70 -14 81 O ATOM 1899 CB THR C 21 22.934 4.811 1.961 1.00 28.09 C ANISOU 1899 CB THR C 21 3348 3573 3752 14 -85 134 C ATOM 1900 OG1 THR C 21 24.302 4.558 1.623 1.00 31.78 O ANISOU 1900 OG1 THR C 21 3874 3996 4206 -7 -72 111 O ATOM 1901 CG2 THR C 21 22.114 4.926 0.672 1.00 29.59 C ANISOU 1901 CG2 THR C 21 3527 3787 3930 4 -126 178 C ATOM 1902 N GLY C 22 24.555 6.567 4.409 1.00 30.78 N ANISOU 1902 N GLY C 22 3719 3835 4140 85 -1 61 N ATOM 1903 CA GLY C 22 25.160 6.593 5.740 1.00 28.02 C ANISOU 1903 CA GLY C 22 3379 3474 3795 84 29 26 C ATOM 1904 C GLY C 22 26.382 5.719 5.888 1.00 27.08 C ANISOU 1904 C GLY C 22 3287 3342 3660 41 30 9 C ATOM 1905 O GLY C 22 26.744 5.323 7.012 1.00 30.68 O ANISOU 1905 O GLY C 22 3741 3803 4113 29 45 -12 O ATOM 1906 N LYS C 23 27.051 5.417 4.774 1.00 25.07 N ANISOU 1906 N LYS C 23 3059 3074 3395 21 17 20 N ATOM 1907 CA LYS C 23 28.202 4.514 4.828 1.00 28.56 C ANISOU 1907 CA LYS C 23 3521 3508 3823 -8 23 7 C ATOM 1908 C LYS C 23 29.310 5.095 5.676 1.00 27.91 C ANISOU 1908 C LYS C 23 3451 3404 3750 -8 42 -12 C ATOM 1909 O LYS C 23 29.895 4.413 6.510 1.00 30.06 O ANISOU 1909 O LYS C 23 3720 3684 4018 -23 49 -25 O ATOM 1910 CB LYS C 23 28.732 4.189 3.433 1.00 29.05 C ANISOU 1910 CB LYS C 23 3610 3559 3867 -23 14 20 C ATOM 1911 CG LYS C 23 27.650 3.643 2.518 1.00 27.17 C ANISOU 1911 CG LYS C 23 3369 3341 3612 -34 -12 41 C ATOM 1912 CD LYS C 23 28.232 3.227 1.176 1.00 29.46 C ANISOU 1912 CD LYS C 23 3700 3619 3876 -53 -17 48 C ATOM 1913 CE LYS C 23 28.694 4.436 0.371 1.00 28.26 C ANISOU 1913 CE LYS C 23 3563 3446 3729 -42 -13 61 C ATOM 1914 NZ LYS C 23 27.615 5.467 0.179 1.00 33.30 N ANISOU 1914 NZ LYS C 23 4183 4088 4383 -21 -34 85 N ATOM 1915 N THR C 24 29.605 6.369 5.460 1.00 26.21 N ANISOU 1915 N THR C 24 3253 3161 3546 4 48 -10 N ATOM 1916 CA THR C 24 30.695 7.010 6.187 1.00 29.50 C ANISOU 1916 CA THR C 24 3686 3556 3965 -9 61 -25 C ATOM 1917 C THR C 24 30.347 7.144 7.658 1.00 29.05 C ANISOU 1917 C THR C 24 3623 3503 3912 -4 72 -46 C ATOM 1918 O THR C 24 31.193 6.900 8.523 1.00 30.58 O ANISOU 1918 O THR C 24 3819 3701 4100 -28 76 -58 O ATOM 1919 CB THR C 24 31.035 8.367 5.556 1.00 30.30 C ANISOU 1919 CB THR C 24 3820 3621 4072 -6 61 -15 C ATOM 1920 OG1 THR C 24 31.534 8.125 4.245 1.00 27.64 O ANISOU 1920 OG1 THR C 24 3490 3288 3726 -20 55 5 O ATOM 1921 CG2 THR C 24 32.123 9.086 6.349 1.00 30.21 C ANISOU 1921 CG2 THR C 24 3830 3588 4059 -32 70 -28 C ATOM 1922 N THR C 25 29.099 7.504 7.936 1.00 27.26 N ANISOU 1922 N THR C 25 3384 3281 3692 28 76 -49 N ATOM 1923 CA THR C 25 28.644 7.655 9.314 1.00 29.57 C ANISOU 1923 CA THR C 25 3672 3581 3981 37 94 -71 C ATOM 1924 C THR C 25 28.758 6.306 10.003 1.00 30.80 C ANISOU 1924 C THR C 25 3805 3774 4124 8 90 -76 C ATOM 1925 O THR C 25 29.215 6.218 11.146 1.00 28.14 O ANISOU 1925 O THR C 25 3477 3439 3777 -11 98 -93 O ATOM 1926 CB THR C 25 27.195 8.161 9.384 1.00 31.03 C ANISOU 1926 CB THR C 25 3837 3777 4177 85 104 -68 C ATOM 1927 OG1 THR C 25 27.114 9.456 8.775 1.00 30.94 O ANISOU 1927 OG1 THR C 25 3856 3722 4179 119 106 -62 O ATOM 1928 CG2 THR C 25 26.711 8.249 10.819 1.00 29.14 C ANISOU 1928 CG2 THR C 25 3591 3552 3929 96 131 -94 C ATOM 1929 N PHE C 26 28.384 5.246 9.290 1.00 28.56 N ANISOU 1929 N PHE C 26 3499 3515 3836 0 74 -58 N ATOM 1930 CA PHE C 26 28.465 3.899 9.843 1.00 25.43 C ANISOU 1930 CA PHE C 26 3091 3145 3425 -29 67 -59 C ATOM 1931 C PHE C 26 29.894 3.471 10.173 1.00 27.00 C ANISOU 1931 C PHE C 26 3309 3331 3620 -51 64 -64 C ATOM 1932 O PHE C 26 30.194 3.105 11.319 1.00 28.46 O ANISOU 1932 O PHE C 26 3494 3525 3795 -69 66 -73 O ATOM 1933 CB PHE C 26 27.812 2.899 8.870 1.00 24.34 C ANISOU 1933 CB PHE C 26 2943 3027 3279 -38 48 -39 C ATOM 1934 CG PHE C 26 27.812 1.477 9.359 1.00 27.20 C ANISOU 1934 CG PHE C 26 3306 3405 3622 -69 37 -37 C ATOM 1935 CD1 PHE C 26 26.948 1.078 10.364 1.00 27.84 C ANISOU 1935 CD1 PHE C 26 3367 3519 3694 -84 40 -39 C ATOM 1936 CD2 PHE C 26 28.642 0.537 8.787 1.00 26.71 C ANISOU 1936 CD2 PHE C 26 3272 3326 3551 -82 26 -32 C ATOM 1937 CE1 PHE C 26 26.924 -0.225 10.800 1.00 28.37 C ANISOU 1937 CE1 PHE C 26 3443 3596 3740 -118 26 -34 C ATOM 1938 CE2 PHE C 26 28.635 -0.786 9.245 1.00 30.10 C ANISOU 1938 CE2 PHE C 26 3714 3759 3962 -108 14 -30 C ATOM 1939 CZ PHE C 26 27.770 -1.157 10.236 1.00 28.00 C ANISOU 1939 CZ PHE C 26 3431 3522 3685 -129 11 -29 C ATOM 1940 N VAL C 27 30.790 3.518 9.196 1.00 28.34 N ANISOU 1940 N VAL C 27 3491 3484 3793 -51 60 -54 N ATOM 1941 CA VAL C 27 32.151 3.059 9.466 1.00 27.78 C ANISOU 1941 CA VAL C 27 3423 3411 3719 -66 58 -53 C ATOM 1942 C VAL C 27 32.824 3.875 10.574 1.00 28.96 C ANISOU 1942 C VAL C 27 3576 3556 3870 -83 63 -63 C ATOM 1943 O VAL C 27 33.637 3.355 11.338 1.00 31.86 O ANISOU 1943 O VAL C 27 3939 3936 4232 -100 56 -61 O ATOM 1944 CB VAL C 27 33.024 3.020 8.181 1.00 27.91 C ANISOU 1944 CB VAL C 27 3447 3419 3738 -61 61 -39 C ATOM 1945 CG1 VAL C 27 33.417 4.417 7.754 1.00 30.19 C ANISOU 1945 CG1 VAL C 27 3745 3692 4035 -63 67 -37 C ATOM 1946 CG2 VAL C 27 34.275 2.170 8.390 1.00 27.51 C ANISOU 1946 CG2 VAL C 27 3388 3378 3685 -64 61 -33 C ATOM 1947 N LYS C 28 32.479 5.151 10.686 1.00 28.44 N ANISOU 1947 N LYS C 28 3526 3471 3808 -78 71 -74 N ATOM 1948 CA LYS C 28 33.168 5.996 11.646 1.00 25.41 C ANISOU 1948 CA LYS C 28 3161 3076 3419 -102 74 -85 C ATOM 1949 C LYS C 28 32.787 5.760 13.115 1.00 28.77 C ANISOU 1949 C LYS C 28 3590 3514 3828 -115 77 -103 C ATOM 1950 O LYS C 28 33.412 6.337 14.010 1.00 34.51 O ANISOU 1950 O LYS C 28 4338 4232 4542 -144 75 -113 O ATOM 1951 CB LYS C 28 32.953 7.473 11.295 1.00 29.00 C ANISOU 1951 CB LYS C 28 3648 3493 3878 -93 82 -92 C ATOM 1952 CG LYS C 28 33.841 7.984 10.177 1.00 32.92 C ANISOU 1952 CG LYS C 28 4153 3976 4381 -105 76 -73 C ATOM 1953 CD LYS C 28 33.523 9.459 9.883 1.00 43.55 C ANISOU 1953 CD LYS C 28 5543 5275 5729 -97 81 -79 C ATOM 1954 CE LYS C 28 34.392 9.981 8.750 1.00 51.27 C ANISOU 1954 CE LYS C 28 6531 6240 6708 -118 75 -56 C ATOM 1955 NZ LYS C 28 34.202 11.438 8.533 1.00 53.35 N ANISOU 1955 NZ LYS C 28 6850 6450 6970 -118 75 -58 N ATOM 1956 N ARG C 29 31.746 4.962 13.361 1.00 27.76 N ANISOU 1956 N ARG C 29 3444 3407 3696 -100 81 -105 N ATOM 1957 CA ARG C 29 31.325 4.649 14.720 1.00 28.30 C ANISOU 1957 CA ARG C 29 3515 3494 3745 -116 87 -120 C ATOM 1958 C ARG C 29 32.468 3.996 15.487 1.00 25.48 C ANISOU 1958 C ARG C 29 3159 3148 3375 -153 67 -111 C ATOM 1959 O ARG C 29 32.613 4.183 16.694 1.00 30.23 O ANISOU 1959 O ARG C 29 3777 3755 3954 -180 67 -124 O ATOM 1960 CB ARG C 29 30.117 3.693 14.739 1.00 28.93 C ANISOU 1960 CB ARG C 29 3569 3603 3820 -106 90 -115 C ATOM 1961 CG ARG C 29 28.865 4.196 13.995 1.00 31.45 C ANISOU 1961 CG ARG C 29 3871 3926 4151 -68 104 -114 C ATOM 1962 CD ARG C 29 28.614 5.687 14.270 1.00 30.28 C ANISOU 1962 CD ARG C 29 3745 3752 4007 -40 129 -135 C ATOM 1963 NE ARG C 29 28.193 5.944 15.652 1.00 30.26 N ANISOU 1963 NE ARG C 29 3754 3761 3983 -45 153 -159 N ATOM 1964 CZ ARG C 29 27.869 7.153 16.119 1.00 32.21 C ANISOU 1964 CZ ARG C 29 4031 3982 4225 -17 181 -184 C ATOM 1965 NH1 ARG C 29 27.920 8.216 15.326 1.00 32.60 N ANISOU 1965 NH1 ARG C 29 4102 3990 4294 16 184 -184 N ATOM 1966 NH2 ARG C 29 27.484 7.302 17.378 1.00 32.80 N ANISOU 1966 NH2 ARG C 29 4120 4070 4273 -22 208 -209 N ATOM 1967 N HIS C 30 33.279 3.229 14.772 1.00 26.25 N ANISOU 1967 N HIS C 30 3240 3250 3483 -152 50 -89 N ATOM 1968 CA HIS C 30 34.377 2.492 15.382 1.00 28.53 C ANISOU 1968 CA HIS C 30 3520 3554 3766 -176 29 -72 C ATOM 1969 C HIS C 30 35.573 3.427 15.587 1.00 25.60 C ANISOU 1969 C HIS C 30 3153 3180 3394 -202 21 -68 C ATOM 1970 O HIS C 30 36.248 3.818 14.635 1.00 28.32 O ANISOU 1970 O HIS C 30 3487 3520 3754 -195 23 -56 O ATOM 1971 CB HIS C 30 34.727 1.306 14.466 1.00 27.69 C ANISOU 1971 CB HIS C 30 3397 3451 3671 -152 20 -50 C ATOM 1972 CG HIS C 30 35.641 0.300 15.083 1.00 27.25 C ANISOU 1972 CG HIS C 30 3332 3410 3611 -160 -1 -29 C ATOM 1973 ND1 HIS C 30 36.956 0.574 15.376 1.00 26.31 N ANISOU 1973 ND1 HIS C 30 3194 3305 3496 -173 -13 -12 N ATOM 1974 CD2 HIS C 30 35.446 -1.005 15.396 1.00 29.55 C ANISOU 1974 CD2 HIS C 30 3630 3703 3895 -155 -14 -17 C ATOM 1975 CE1 HIS C 30 37.526 -0.509 15.888 1.00 34.12 C ANISOU 1975 CE1 HIS C 30 4174 4308 4483 -169 -34 11 C ATOM 1976 NE2 HIS C 30 36.634 -1.484 15.900 1.00 29.95 N ANISOU 1976 NE2 HIS C 30 3667 3766 3948 -156 -34 7 N ATOM 1977 N LEU C 31 35.834 3.773 16.847 1.00 26.30 N ANISOU 1977 N LEU C 31 3257 3275 3459 -240 12 -75 N ATOM 1978 CA LEU C 31 36.718 4.895 17.154 1.00 30.08 C ANISOU 1978 CA LEU C 31 3753 3746 3928 -279 3 -76 C ATOM 1979 C LEU C 31 38.153 4.646 16.749 1.00 29.37 C ANISOU 1979 C LEU C 31 3626 3682 3850 -295 -19 -41 C ATOM 1980 O LEU C 31 38.819 5.550 16.250 1.00 30.13 O ANISOU 1980 O LEU C 31 3724 3772 3950 -315 -20 -34 O ATOM 1981 CB LEU C 31 36.642 5.261 18.635 1.00 29.63 C ANISOU 1981 CB LEU C 31 3732 3691 3837 -323 -4 -94 C ATOM 1982 CG LEU C 31 35.292 5.750 19.138 1.00 31.61 C ANISOU 1982 CG LEU C 31 4020 3919 4070 -307 28 -132 C ATOM 1983 CD1 LEU C 31 35.334 6.023 20.628 1.00 31.50 C ANISOU 1983 CD1 LEU C 31 4047 3910 4013 -354 23 -150 C ATOM 1984 CD2 LEU C 31 34.894 7.019 18.391 1.00 38.15 C ANISOU 1984 CD2 LEU C 31 4879 4707 4910 -284 51 -152 C ATOM 1985 N THR C 32 38.654 3.438 16.998 1.00 27.54 N ANISOU 1985 N THR C 32 3360 3480 3623 -285 -37 -16 N ATOM 1986 CA THR C 32 40.014 3.121 16.582 1.00 26.01 C ANISOU 1986 CA THR C 32 3120 3319 3443 -286 -53 22 C ATOM 1987 C THR C 32 40.112 2.974 15.062 1.00 27.40 C ANISOU 1987 C THR C 32 3277 3490 3646 -241 -29 28 C ATOM 1988 O THR C 32 41.121 3.348 14.444 1.00 34.25 O ANISOU 1988 O THR C 32 4112 4380 4522 -248 -28 51 O ATOM 1989 CB THR C 32 40.503 1.834 17.248 1.00 35.19 C ANISOU 1989 CB THR C 32 4255 4510 4605 -275 -77 50 C ATOM 1990 OG1 THR C 32 40.426 1.995 18.668 1.00 33.72 O ANISOU 1990 OG1 THR C 32 4091 4331 4389 -325 -101 46 O ATOM 1991 CG2 THR C 32 41.946 1.541 16.834 1.00 37.37 C ANISOU 1991 CG2 THR C 32 4473 4827 4899 -266 -90 93 C ATOM 1992 N GLY C 33 39.067 2.431 14.458 1.00 27.61 N ANISOU 1992 N GLY C 33 3321 3492 3679 -200 -11 11 N ATOM 1993 CA GLY C 33 39.024 2.354 13.013 1.00 26.00 C ANISOU 1993 CA GLY C 33 3111 3279 3491 -164 11 13 C ATOM 1994 C GLY C 33 39.177 3.754 12.438 1.00 35.28 C ANISOU 1994 C GLY C 33 4296 4442 4666 -187 21 7 C ATOM 1995 O GLY C 33 39.773 3.953 11.382 1.00 33.81 O ANISOU 1995 O GLY C 33 4093 4265 4488 -178 33 22 O ATOM 1996 N GLU C 34 38.645 4.743 13.140 1.00 27.08 N ANISOU 1996 N GLU C 34 3291 3382 3616 -218 17 -13 N ATOM 1997 CA GLU C 34 38.719 6.104 12.618 1.00 30.51 C ANISOU 1997 CA GLU C 34 3751 3793 4048 -240 24 -19 C ATOM 1998 C GLU C 34 40.085 6.722 12.915 1.00 34.71 C ANISOU 1998 C GLU C 34 4268 4350 4572 -295 7 4 C ATOM 1999 O GLU C 34 40.659 7.405 12.065 1.00 32.65 O ANISOU 1999 O GLU C 34 4003 4089 4313 -312 12 19 O ATOM 2000 CB GLU C 34 37.570 6.970 13.153 1.00 34.77 C ANISOU 2000 CB GLU C 34 4342 4290 4577 -241 32 -51 C ATOM 2001 CG GLU C 34 37.768 8.491 12.965 1.00 35.56 C ANISOU 2001 CG GLU C 34 4486 4354 4670 -271 33 -58 C ATOM 2002 CD GLU C 34 37.558 8.957 11.530 1.00 43.25 C ANISOU 2002 CD GLU C 34 5466 5308 5658 -247 45 -48 C ATOM 2003 OE1 GLU C 34 36.921 8.229 10.744 1.00 35.81 O ANISOU 2003 OE1 GLU C 34 4504 4373 4731 -202 55 -46 O ATOM 2004 OE2 GLU C 34 38.020 10.065 11.189 1.00 42.02 O ANISOU 2004 OE2 GLU C 34 5342 5127 5496 -280 42 -42 O ATOM 2005 N SER C 35 40.631 6.468 14.101 1.00 32.01 N ANISOU 2005 N SER C 35 3914 4032 4215 -329 -16 12 N ATOM 2006 CA SER C 35 41.917 7.092 14.435 1.00 36.23 C ANISOU 2006 CA SER C 35 4431 4598 4738 -393 -39 39 C ATOM 2007 C SER C 35 43.083 6.487 13.652 1.00 44.46 C ANISOU 2007 C SER C 35 5399 5696 5797 -380 -38 81 C ATOM 2008 O SER C 35 44.118 7.131 13.474 1.00 40.63 O ANISOU 2008 O SER C 35 4889 5242 5305 -430 -49 109 O ATOM 2009 CB SER C 35 42.196 7.067 15.947 1.00 33.42 C ANISOU 2009 CB SER C 35 4085 4256 4356 -442 -69 40 C ATOM 2010 OG SER C 35 42.224 5.748 16.457 1.00 38.01 O ANISOU 2010 OG SER C 35 4629 4868 4944 -410 -79 53 O ATOM 2011 N GLU C 36 42.906 5.258 13.174 1.00 38.44 N ANISOU 2011 N GLU C 36 4606 4945 5054 -314 -23 86 N ATOM 2012 CA GLU C 36 43.972 4.549 12.466 1.00 33.71 C ANISOU 2012 CA GLU C 36 3939 4397 4470 -284 -13 123 C ATOM 2013 C GLU C 36 43.668 4.380 10.971 1.00 33.47 C ANISOU 2013 C GLU C 36 3913 4352 4451 -235 24 115 C ATOM 2014 O GLU C 36 44.341 3.622 10.271 1.00 33.88 O ANISOU 2014 O GLU C 36 3921 4438 4514 -193 44 136 O ATOM 2015 CB GLU C 36 44.247 3.189 13.137 1.00 34.38 C ANISOU 2015 CB GLU C 36 3990 4508 4564 -244 -27 140 C ATOM 2016 CG GLU C 36 44.563 3.344 14.629 1.00 34.90 C ANISOU 2016 CG GLU C 36 4054 4593 4613 -299 -68 152 C ATOM 2017 CD GLU C 36 44.980 2.045 15.335 1.00 48.59 C ANISOU 2017 CD GLU C 36 5752 6356 6354 -264 -89 179 C ATOM 2018 OE1 GLU C 36 44.708 0.944 14.809 1.00 53.62 O ANISOU 2018 OE1 GLU C 36 6387 6979 7007 -193 -70 177 O ATOM 2019 OE2 GLU C 36 45.568 2.143 16.438 1.00 58.11 O ANISOU 2019 OE2 GLU C 36 6939 7595 7546 -311 -128 203 O ATOM 2020 N LYS C 37 42.674 5.111 10.475 1.00 34.96 N ANISOU 2020 N LYS C 37 4157 4491 4635 -240 35 86 N ATOM 2021 CA LYS C 37 42.309 4.987 9.072 1.00 34.12 C ANISOU 2021 CA LYS C 37 4061 4369 4534 -202 65 80 C ATOM 2022 C LYS C 37 43.455 5.412 8.157 1.00 37.62 C ANISOU 2022 C LYS C 37 4465 4853 4974 -220 81 110 C ATOM 2023 O LYS C 37 44.311 6.233 8.527 1.00 34.26 O ANISOU 2023 O LYS C 37 4018 4457 4542 -278 67 132 O ATOM 2024 CB LYS C 37 41.030 5.776 8.753 1.00 33.63 C ANISOU 2024 CB LYS C 37 4060 4251 4468 -205 67 52 C ATOM 2025 CG LYS C 37 41.226 7.273 8.648 1.00 35.60 C ANISOU 2025 CG LYS C 37 4337 4481 4706 -258 60 55 C ATOM 2026 CD LYS C 37 39.891 7.980 8.465 1.00 38.10 C ANISOU 2026 CD LYS C 37 4715 4740 5024 -245 62 28 C ATOM 2027 CE LYS C 37 40.062 9.486 8.505 1.00 39.15 C ANISOU 2027 CE LYS C 37 4891 4839 5145 -294 53 29 C ATOM 2028 NZ LYS C 37 38.738 10.164 8.582 1.00 43.13 N ANISOU 2028 NZ LYS C 37 5453 5284 5651 -270 54 2 N ATOM 2029 N LYS C 38 43.474 4.838 6.961 1.00 32.27 N ANISOU 2029 N LYS C 38 3781 4182 4298 -174 112 112 N ATOM 2030 CA LYS C 38 44.534 5.098 5.993 1.00 33.90 C ANISOU 2030 CA LYS C 38 3948 4434 4498 -183 138 140 C ATOM 2031 C LYS C 38 43.918 5.658 4.729 1.00 37.12 C ANISOU 2031 C LYS C 38 4402 4809 4893 -185 158 129 C ATOM 2032 O LYS C 38 42.968 5.089 4.220 1.00 35.63 O ANISOU 2032 O LYS C 38 4252 4583 4703 -143 166 105 O ATOM 2033 CB LYS C 38 45.271 3.797 5.686 1.00 38.48 C ANISOU 2033 CB LYS C 38 4477 5058 5085 -120 165 155 C ATOM 2034 CG LYS C 38 45.820 3.123 6.937 1.00 47.55 C ANISOU 2034 CG LYS C 38 5581 6237 6249 -109 141 171 C ATOM 2035 CD LYS C 38 46.660 1.905 6.615 1.00 59.18 C ANISOU 2035 CD LYS C 38 7003 7753 7732 -37 169 192 C ATOM 2036 CE LYS C 38 48.094 2.293 6.298 1.00 69.07 C ANISOU 2036 CE LYS C 38 8170 9088 8984 -54 187 236 C ATOM 2037 NZ LYS C 38 49.011 1.123 6.412 1.00 77.06 N ANISOU 2037 NZ LYS C 38 9117 10151 10012 21 206 263 N ATOM 2038 N TYR C 39 44.439 6.778 4.231 1.00 38.81 N ANISOU 2038 N TYR C 39 4615 5035 5094 -239 160 148 N ATOM 2039 CA TYR C 39 43.902 7.363 3.000 1.00 36.76 C ANISOU 2039 CA TYR C 39 4403 4745 4820 -245 174 143 C ATOM 2040 C TYR C 39 44.635 6.822 1.779 1.00 32.99 C ANISOU 2040 C TYR C 39 3893 4313 4327 -220 218 160 C ATOM 2041 O TYR C 39 45.866 6.746 1.754 1.00 39.18 O ANISOU 2041 O TYR C 39 4613 5164 5109 -233 236 189 O ATOM 2042 CB TYR C 39 43.950 8.898 3.024 1.00 39.98 C ANISOU 2042 CB TYR C 39 4846 5129 5217 -318 153 155 C ATOM 2043 CG TYR C 39 43.419 9.535 1.747 1.00 42.51 C ANISOU 2043 CG TYR C 39 5216 5414 5520 -324 163 157 C ATOM 2044 CD1 TYR C 39 42.073 9.436 1.399 1.00 42.22 C ANISOU 2044 CD1 TYR C 39 5234 5321 5487 -285 156 133 C ATOM 2045 CD2 TYR C 39 44.267 10.228 0.888 1.00 43.15 C ANISOU 2045 CD2 TYR C 39 5289 5527 5579 -374 178 188 C ATOM 2046 CE1 TYR C 39 41.587 10.012 0.229 1.00 42.42 C ANISOU 2046 CE1 TYR C 39 5304 5318 5495 -291 159 140 C ATOM 2047 CE2 TYR C 39 43.789 10.803 -0.285 1.00 42.20 C ANISOU 2047 CE2 TYR C 39 5220 5375 5439 -383 184 194 C ATOM 2048 CZ TYR C 39 42.453 10.690 -0.608 1.00 42.52 C ANISOU 2048 CZ TYR C 39 5315 5357 5485 -340 173 170 C ATOM 2049 OH TYR C 39 41.984 11.269 -1.765 1.00 49.18 O ANISOU 2049 OH TYR C 39 6207 6171 6307 -351 172 182 O ATOM 2050 N VAL C 40 43.865 6.422 0.774 1.00 32.68 N ANISOU 2050 N VAL C 40 3898 4244 4276 -184 235 142 N ATOM 2051 CA VAL C 40 44.424 5.840 -0.433 1.00 34.96 C ANISOU 2051 CA VAL C 40 4173 4568 4543 -155 281 150 C ATOM 2052 C VAL C 40 44.179 6.837 -1.560 1.00 38.13 C ANISOU 2052 C VAL C 40 4617 4953 4917 -199 286 160 C ATOM 2053 O VAL C 40 43.100 6.867 -2.167 1.00 37.98 O ANISOU 2053 O VAL C 40 4659 4884 4887 -188 275 144 O ATOM 2054 CB VAL C 40 43.753 4.499 -0.766 1.00 34.92 C ANISOU 2054 CB VAL C 40 4198 4536 4534 -86 296 121 C ATOM 2055 CG1 VAL C 40 44.438 3.840 -1.960 1.00 42.68 C ANISOU 2055 CG1 VAL C 40 5173 5555 5489 -51 351 125 C ATOM 2056 CG2 VAL C 40 43.804 3.573 0.442 1.00 34.87 C ANISOU 2056 CG2 VAL C 40 4164 4531 4554 -48 282 112 C ATOM 2057 N ALA C 41 45.185 7.666 -1.816 1.00 38.26 N ANISOU 2057 N ALA C 41 4601 5015 4921 -253 297 192 N ATOM 2058 CA ALA C 41 45.014 8.832 -2.678 1.00 40.04 C ANISOU 2058 CA ALA C 41 4871 5219 5121 -310 291 209 C ATOM 2059 C ALA C 41 44.596 8.483 -4.103 1.00 43.64 C ANISOU 2059 C ALA C 41 5370 5667 5545 -287 320 203 C ATOM 2060 O ALA C 41 43.778 9.186 -4.701 1.00 42.24 O ANISOU 2060 O ALA C 41 5256 5440 5354 -310 297 204 O ATOM 2061 CB ALA C 41 46.286 9.685 -2.676 1.00 39.73 C ANISOU 2061 CB ALA C 41 4786 5240 5071 -382 299 250 C ATOM 2062 N THR C 42 45.148 7.400 -4.644 1.00 44.08 N ANISOU 2062 N THR C 42 5395 5768 5586 -238 369 197 N ATOM 2063 CA THR C 42 44.879 7.024 -6.030 1.00 42.08 C ANISOU 2063 CA THR C 42 5187 5511 5292 -221 402 189 C ATOM 2064 C THR C 42 43.407 6.711 -6.277 1.00 46.33 C ANISOU 2064 C THR C 42 5801 5977 5827 -198 369 161 C ATOM 2065 O THR C 42 42.849 7.077 -7.320 1.00 44.06 O ANISOU 2065 O THR C 42 5569 5665 5505 -220 365 166 O ATOM 2066 CB THR C 42 45.742 5.825 -6.477 1.00 50.18 C ANISOU 2066 CB THR C 42 6175 6592 6301 -162 466 181 C ATOM 2067 OG1 THR C 42 45.618 4.757 -5.527 1.00 46.89 O ANISOU 2067 OG1 THR C 42 5736 6163 5916 -99 460 158 O ATOM 2068 CG2 THR C 42 47.204 6.236 -6.592 1.00 48.72 C ANISOU 2068 CG2 THR C 42 5909 6495 6107 -191 507 218 C ATOM 2069 N LEU C 43 42.777 6.038 -5.320 1.00 34.62 N ANISOU 2069 N LEU C 43 4315 4462 4375 -159 344 137 N ATOM 2070 CA LEU C 43 41.380 5.642 -5.463 1.00 35.44 C ANISOU 2070 CA LEU C 43 4479 4510 4478 -139 312 115 C ATOM 2071 C LEU C 43 40.431 6.561 -4.707 1.00 35.12 C ANISOU 2071 C LEU C 43 4453 4425 4467 -163 258 118 C ATOM 2072 O LEU C 43 39.208 6.455 -4.845 1.00 39.78 O ANISOU 2072 O LEU C 43 5083 4976 5057 -153 227 108 O ATOM 2073 CB LEU C 43 41.179 4.198 -4.987 1.00 34.80 C ANISOU 2073 CB LEU C 43 4396 4422 4406 -82 322 86 C ATOM 2074 CG LEU C 43 41.921 3.110 -5.756 1.00 40.82 C ANISOU 2074 CG LEU C 43 5162 5211 5136 -40 378 75 C ATOM 2075 CD1 LEU C 43 41.783 1.783 -5.025 1.00 34.68 C ANISOU 2075 CD1 LEU C 43 4385 4416 4375 16 379 51 C ATOM 2076 CD2 LEU C 43 41.388 3.003 -7.173 1.00 43.27 C ANISOU 2076 CD2 LEU C 43 5543 5503 5394 -53 389 69 C ATOM 2077 N GLY C 44 40.989 7.449 -3.894 1.00 37.72 N ANISOU 2077 N GLY C 44 4750 4763 4819 -194 246 133 N ATOM 2078 CA GLY C 44 40.175 8.334 -3.083 1.00 41.64 C ANISOU 2078 CA GLY C 44 5267 5214 5342 -209 202 131 C ATOM 2079 C GLY C 44 39.330 7.535 -2.113 1.00 42.05 C ANISOU 2079 C GLY C 44 5312 5246 5419 -168 183 105 C ATOM 2080 O GLY C 44 38.101 7.630 -2.096 1.00 42.37 O ANISOU 2080 O GLY C 44 5384 5250 5466 -154 156 96 O ATOM 2081 N VAL C 45 40.009 6.740 -1.298 1.00 35.77 N ANISOU 2081 N VAL C 45 4474 4480 4637 -150 198 95 N ATOM 2082 CA VAL C 45 39.362 5.822 -0.385 1.00 30.83 C ANISOU 2082 CA VAL C 45 3842 3842 4031 -114 184 73 C ATOM 2083 C VAL C 45 40.016 5.981 0.981 1.00 28.14 C ANISOU 2083 C VAL C 45 3461 3519 3714 -126 175 74 C ATOM 2084 O VAL C 45 41.217 6.245 1.060 1.00 33.87 O ANISOU 2084 O VAL C 45 4148 4282 4437 -148 190 92 O ATOM 2085 CB VAL C 45 39.555 4.358 -0.859 1.00 30.63 C ANISOU 2085 CB VAL C 45 3815 3832 3989 -73 210 61 C ATOM 2086 CG1 VAL C 45 39.231 3.359 0.264 1.00 34.85 C ANISOU 2086 CG1 VAL C 45 4339 4360 4544 -44 197 44 C ATOM 2087 CG2 VAL C 45 38.702 4.079 -2.096 1.00 34.09 C ANISOU 2087 CG2 VAL C 45 4307 4248 4399 -68 210 55 C ATOM 2088 N GLU C 46 39.225 5.841 2.043 1.00 26.34 N ANISOU 2088 N GLU C 46 3238 3267 3502 -116 151 57 N ATOM 2089 CA GLU C 46 39.779 5.729 3.398 1.00 27.92 C ANISOU 2089 CA GLU C 46 3405 3484 3719 -126 141 56 C ATOM 2090 C GLU C 46 39.553 4.309 3.864 1.00 27.77 C ANISOU 2090 C GLU C 46 3375 3472 3705 -85 143 43 C ATOM 2091 O GLU C 46 38.420 3.828 3.869 1.00 29.04 O ANISOU 2091 O GLU C 46 3564 3606 3865 -67 132 27 O ATOM 2092 CB GLU C 46 39.085 6.694 4.364 1.00 34.43 C ANISOU 2092 CB GLU C 46 4253 4275 4553 -149 115 45 C ATOM 2093 CG GLU C 46 39.474 8.147 4.138 1.00 38.17 C ANISOU 2093 CG GLU C 46 4748 4735 5021 -195 110 58 C ATOM 2094 CD GLU C 46 38.796 9.097 5.105 1.00 50.47 C ANISOU 2094 CD GLU C 46 6342 6249 6584 -210 89 42 C ATOM 2095 OE1 GLU C 46 37.818 8.687 5.758 1.00 63.68 O ANISOU 2095 OE1 GLU C 46 8022 7906 8266 -180 83 21 O ATOM 2096 OE2 GLU C 46 39.244 10.256 5.213 1.00 61.20 O ANISOU 2096 OE2 GLU C 46 7727 7589 7936 -255 81 51 O ATOM 2097 N VAL C 47 40.627 3.635 4.257 1.00 28.85 N ANISOU 2097 N VAL C 47 3470 3645 3846 -73 153 55 N ATOM 2098 CA VAL C 47 40.510 2.262 4.753 1.00 30.76 C ANISOU 2098 CA VAL C 47 3709 3886 4093 -33 152 46 C ATOM 2099 C VAL C 47 40.544 2.301 6.278 1.00 28.80 C ANISOU 2099 C VAL C 47 3441 3643 3857 -51 125 47 C ATOM 2100 O VAL C 47 41.530 2.753 6.866 1.00 31.27 O ANISOU 2100 O VAL C 47 3715 3989 4176 -76 118 66 O ATOM 2101 CB VAL C 47 41.644 1.375 4.203 1.00 30.24 C ANISOU 2101 CB VAL C 47 3613 3854 4023 8 184 61 C ATOM 2102 CG1 VAL C 47 41.580 -0.042 4.789 1.00 31.43 C ANISOU 2102 CG1 VAL C 47 3769 3994 4179 53 179 55 C ATOM 2103 CG2 VAL C 47 41.567 1.316 2.676 1.00 32.32 C ANISOU 2103 CG2 VAL C 47 3905 4110 4265 23 215 56 C ATOM 2104 N HIS C 48 39.455 1.864 6.912 1.00 27.99 N ANISOU 2104 N HIS C 48 3368 3512 3756 -46 107 28 N ATOM 2105 CA HIS C 48 39.350 1.879 8.365 1.00 29.07 C ANISOU 2105 CA HIS C 48 3495 3652 3897 -66 83 26 C ATOM 2106 C HIS C 48 39.617 0.490 8.917 1.00 30.02 C ANISOU 2106 C HIS C 48 3607 3780 4019 -37 76 33 C ATOM 2107 O HIS C 48 38.883 -0.444 8.630 1.00 28.20 O ANISOU 2107 O HIS C 48 3407 3525 3782 -12 78 22 O ATOM 2108 CB HIS C 48 37.952 2.296 8.825 1.00 26.78 C ANISOU 2108 CB HIS C 48 3239 3332 3603 -80 71 3 C ATOM 2109 CG HIS C 48 37.599 3.712 8.497 1.00 24.23 C ANISOU 2109 CG HIS C 48 2933 2993 3281 -103 73 -4 C ATOM 2110 ND1 HIS C 48 37.534 4.186 7.202 1.00 37.01 N ANISOU 2110 ND1 HIS C 48 4563 4601 4898 -96 86 2 N ATOM 2111 CD2 HIS C 48 37.242 4.742 9.296 1.00 24.05 C ANISOU 2111 CD2 HIS C 48 2926 2955 3256 -129 65 -15 C ATOM 2112 CE1 HIS C 48 37.169 5.458 7.221 1.00 33.84 C ANISOU 2112 CE1 HIS C 48 4183 4178 4497 -116 82 -3 C ATOM 2113 NE2 HIS C 48 36.992 5.822 8.479 1.00 39.14 N ANISOU 2113 NE2 HIS C 48 4860 4844 5169 -133 71 -15 N ATOM 2114 N PRO C 49 40.657 0.358 9.731 1.00 26.47 N ANISOU 2114 N PRO C 49 3119 3362 3576 -43 65 54 N ATOM 2115 CA PRO C 49 40.915 -0.985 10.255 1.00 28.43 C ANISOU 2115 CA PRO C 49 3363 3612 3826 -8 56 65 C ATOM 2116 C PRO C 49 40.107 -1.216 11.531 1.00 29.99 C ANISOU 2116 C PRO C 49 3583 3794 4015 -35 27 55 C ATOM 2117 O PRO C 49 40.427 -0.653 12.576 1.00 38.66 O ANISOU 2117 O PRO C 49 4665 4913 5112 -73 6 63 O ATOM 2118 CB PRO C 49 42.412 -0.965 10.574 1.00 31.82 C ANISOU 2118 CB PRO C 49 3731 4092 4267 -2 52 100 C ATOM 2119 CG PRO C 49 42.812 0.495 10.644 1.00 35.89 C ANISOU 2119 CG PRO C 49 4224 4633 4781 -60 48 105 C ATOM 2120 CD PRO C 49 41.701 1.334 10.066 1.00 22.20 C ANISOU 2120 CD PRO C 49 2538 2859 3039 -80 58 74 C ATOM 2121 N LEU C 50 39.070 -2.029 11.438 1.00 27.27 N ANISOU 2121 N LEU C 50 3281 3418 3663 -22 26 40 N ATOM 2122 CA LEU C 50 38.166 -2.265 12.549 1.00 24.44 C ANISOU 2122 CA LEU C 50 2944 3049 3291 -50 4 30 C ATOM 2123 C LEU C 50 38.477 -3.606 13.173 1.00 32.64 C ANISOU 2123 C LEU C 50 3993 4082 4326 -31 -14 49 C ATOM 2124 O LEU C 50 38.192 -4.644 12.582 1.00 31.01 O ANISOU 2124 O LEU C 50 3819 3847 4115 -1 -9 48 O ATOM 2125 CB LEU C 50 36.720 -2.323 12.053 1.00 26.24 C ANISOU 2125 CB LEU C 50 3208 3253 3510 -57 11 7 C ATOM 2126 CG LEU C 50 36.016 -0.972 11.876 1.00 38.21 C ANISOU 2126 CG LEU C 50 4721 4771 5027 -79 22 -11 C ATOM 2127 CD1 LEU C 50 36.776 -0.094 10.920 1.00 35.51 C ANISOU 2127 CD1 LEU C 50 4363 4432 4696 -70 37 -7 C ATOM 2128 CD2 LEU C 50 34.588 -1.167 11.420 1.00 36.46 C ANISOU 2128 CD2 LEU C 50 4522 4535 4796 -81 24 -25 C ATOM 2129 N VAL C 51 39.057 -3.581 14.360 1.00 27.51 N ANISOU 2129 N VAL C 51 3323 3456 3675 -52 -38 67 N ATOM 2130 CA VAL C 51 39.323 -4.804 15.103 1.00 30.00 C ANISOU 2130 CA VAL C 51 3651 3764 3985 -37 -63 90 C ATOM 2131 C VAL C 51 38.118 -5.156 15.966 1.00 31.54 C ANISOU 2131 C VAL C 51 3886 3943 4155 -77 -78 77 C ATOM 2132 O VAL C 51 37.524 -4.287 16.616 1.00 27.24 O ANISOU 2132 O VAL C 51 3339 3414 3598 -122 -78 59 O ATOM 2133 CB VAL C 51 40.557 -4.648 16.000 1.00 31.70 C ANISOU 2133 CB VAL C 51 3820 4019 4207 -44 -88 123 C ATOM 2134 CG1 VAL C 51 40.820 -5.946 16.759 1.00 38.24 C ANISOU 2134 CG1 VAL C 51 4664 4836 5029 -23 -117 153 C ATOM 2135 CG2 VAL C 51 41.758 -4.254 15.159 1.00 38.69 C ANISOU 2135 CG2 VAL C 51 4653 4934 5114 -10 -70 141 C ATOM 2136 N PHE C 52 37.759 -6.434 15.942 1.00 27.69 N ANISOU 2136 N PHE C 52 3439 3424 3658 -60 -89 85 N ATOM 2137 CA PHE C 52 36.772 -7.003 16.848 1.00 31.74 C ANISOU 2137 CA PHE C 52 3989 3926 4144 -102 -108 83 C ATOM 2138 C PHE C 52 37.438 -8.128 17.615 1.00 29.79 C ANISOU 2138 C PHE C 52 3760 3667 3891 -88 -140 118 C ATOM 2139 O PHE C 52 38.181 -8.905 17.034 1.00 32.57 O ANISOU 2139 O PHE C 52 4122 3995 4259 -32 -140 135 O ATOM 2140 CB PHE C 52 35.596 -7.564 16.050 1.00 29.83 C ANISOU 2140 CB PHE C 52 3791 3654 3890 -107 -97 66 C ATOM 2141 CG PHE C 52 34.780 -6.499 15.383 1.00 28.44 C ANISOU 2141 CG PHE C 52 3596 3493 3717 -121 -72 38 C ATOM 2142 CD1 PHE C 52 35.180 -5.961 14.176 1.00 29.26 C ANISOU 2142 CD1 PHE C 52 3685 3593 3841 -87 -50 28 C ATOM 2143 CD2 PHE C 52 33.620 -6.025 15.981 1.00 32.92 C ANISOU 2143 CD2 PHE C 52 4160 4082 4268 -166 -69 23 C ATOM 2144 CE1 PHE C 52 34.432 -4.958 13.581 1.00 29.13 C ANISOU 2144 CE1 PHE C 52 3654 3586 3827 -99 -31 8 C ATOM 2145 CE2 PHE C 52 32.856 -5.032 15.377 1.00 31.34 C ANISOU 2145 CE2 PHE C 52 3939 3894 4073 -170 -47 2 C ATOM 2146 CZ PHE C 52 33.271 -4.491 14.190 1.00 30.01 C ANISOU 2146 CZ PHE C 52 3761 3717 3926 -137 -31 -4 C ATOM 2147 N HIS C 53 37.177 -8.211 18.912 1.00 26.85 N ANISOU 2147 N HIS C 53 3395 3310 3496 -136 -166 129 N ATOM 2148 CA HIS C 53 37.764 -9.284 19.715 1.00 25.62 C ANISOU 2148 CA HIS C 53 3261 3142 3332 -127 -203 167 C ATOM 2149 C HIS C 53 36.790 -10.446 19.833 1.00 32.32 C ANISOU 2149 C HIS C 53 4179 3948 4154 -147 -216 170 C ATOM 2150 O HIS C 53 35.718 -10.305 20.420 1.00 31.52 O ANISOU 2150 O HIS C 53 4093 3859 4023 -209 -216 156 O ATOM 2151 CB HIS C 53 38.190 -8.741 21.082 1.00 34.18 C ANISOU 2151 CB HIS C 53 4318 4268 4400 -173 -230 184 C ATOM 2152 CG HIS C 53 39.428 -7.904 21.013 1.00 31.12 C ANISOU 2152 CG HIS C 53 3869 3919 4036 -154 -232 198 C ATOM 2153 ND1 HIS C 53 39.414 -6.534 21.153 1.00 38.31 N ANISOU 2153 ND1 HIS C 53 4749 4863 4943 -193 -217 174 N ATOM 2154 CD2 HIS C 53 40.714 -8.245 20.762 1.00 33.71 C ANISOU 2154 CD2 HIS C 53 4160 4257 4391 -101 -245 234 C ATOM 2155 CE1 HIS C 53 40.645 -6.070 21.020 1.00 29.68 C ANISOU 2155 CE1 HIS C 53 3605 3802 3872 -176 -226 197 C ATOM 2156 NE2 HIS C 53 41.452 -7.087 20.777 1.00 39.26 N ANISOU 2156 NE2 HIS C 53 4805 5008 5104 -118 -242 235 N ATOM 2157 N THR C 54 37.168 -11.588 19.253 1.00 32.90 N ANISOU 2157 N THR C 54 4294 3971 4235 -96 -224 187 N ATOM 2158 CA THR C 54 36.309 -12.771 19.220 1.00 29.08 C ANISOU 2158 CA THR C 54 3890 3435 3724 -117 -239 191 C ATOM 2159 C THR C 54 36.797 -13.793 20.230 1.00 33.73 C ANISOU 2159 C THR C 54 4518 3999 4299 -115 -282 234 C ATOM 2160 O THR C 54 37.902 -13.671 20.759 1.00 33.83 O ANISOU 2160 O THR C 54 4491 4033 4329 -81 -299 263 O ATOM 2161 CB THR C 54 36.306 -13.451 17.829 1.00 26.54 C ANISOU 2161 CB THR C 54 3617 3056 3411 -64 -219 178 C ATOM 2162 OG1 THR C 54 37.432 -14.343 17.695 1.00 30.43 O ANISOU 2162 OG1 THR C 54 4135 3507 3920 14 -230 206 O ATOM 2163 CG2 THR C 54 36.334 -12.424 16.729 1.00 30.72 C ANISOU 2163 CG2 THR C 54 4098 3611 3962 -42 -179 146 C ATOM 2164 N ASN C 55 35.981 -14.806 20.487 1.00 32.49 N ANISOU 2164 N ASN C 55 4438 3799 4108 -155 -303 243 N ATOM 2165 CA ASN C 55 36.379 -15.846 21.437 1.00 34.31 C ANISOU 2165 CA ASN C 55 4718 3996 4321 -157 -349 288 C ATOM 2166 C ASN C 55 37.609 -16.590 20.948 1.00 42.13 C ANISOU 2166 C ASN C 55 5727 4938 5343 -54 -356 315 C ATOM 2167 O ASN C 55 38.294 -17.259 21.725 1.00 46.30 O ANISOU 2167 O ASN C 55 6274 5448 5871 -29 -395 360 O ATOM 2168 CB ASN C 55 35.226 -16.802 21.754 1.00 34.56 C ANISOU 2168 CB ASN C 55 4836 3988 4307 -229 -371 295 C ATOM 2169 CG ASN C 55 34.731 -17.552 20.532 1.00 39.14 C ANISOU 2169 CG ASN C 55 5490 4501 4882 -211 -358 277 C ATOM 2170 OD1 ASN C 55 34.372 -16.952 19.523 1.00 33.29 O ANISOU 2170 OD1 ASN C 55 4721 3773 4153 -203 -322 240 O ATOM 2171 ND2 ASN C 55 34.705 -18.874 20.624 1.00 45.59 N ANISOU 2171 ND2 ASN C 55 6406 5239 5675 -210 -389 303 N ATOM 2172 N ARG C 56 37.906 -16.442 19.662 1.00 34.17 N ANISOU 2172 N ARG C 56 4711 3912 4362 11 -318 289 N ATOM 2173 CA ARG C 56 39.073 -17.082 19.072 1.00 46.22 C ANISOU 2173 CA ARG C 56 6248 5396 5918 120 -311 308 C ATOM 2174 C ARG C 56 40.147 -16.093 18.655 1.00 46.30 C ANISOU 2174 C ARG C 56 6153 5469 5969 179 -282 306 C ATOM 2175 O ARG C 56 40.971 -16.392 17.792 1.00 53.67 O ANISOU 2175 O ARG C 56 7082 6381 6928 272 -255 308 O ATOM 2176 CB ARG C 56 38.662 -17.925 17.872 1.00 41.20 C ANISOU 2176 CB ARG C 56 5706 4679 5271 155 -288 283 C ATOM 2177 CG ARG C 56 38.039 -19.249 18.273 1.00 44.22 C ANISOU 2177 CG ARG C 56 6208 4978 5614 122 -326 301 C ATOM 2178 CD ARG C 56 37.590 -20.044 17.066 1.00 39.80 C ANISOU 2178 CD ARG C 56 5752 4334 5035 143 -305 272 C ATOM 2179 NE ARG C 56 38.683 -20.313 16.140 1.00 43.92 N ANISOU 2179 NE ARG C 56 6280 4821 5587 267 -270 267 N ATOM 2180 CZ ARG C 56 38.508 -20.846 14.936 1.00 48.50 C ANISOU 2180 CZ ARG C 56 6943 5333 6151 302 -240 235 C ATOM 2181 NH1 ARG C 56 39.542 -21.058 14.136 1.00 46.71 N ANISOU 2181 NH1 ARG C 56 6716 5081 5950 420 -200 230 N ATOM 2182 NH2 ARG C 56 37.288 -21.170 14.539 1.00 41.37 N ANISOU 2182 NH2 ARG C 56 6124 4391 5205 215 -249 210 N ATOM 2183 N GLY C 57 40.129 -14.911 19.257 1.00 41.03 N ANISOU 2183 N GLY C 57 5406 4879 5305 123 -285 302 N ATOM 2184 CA GLY C 57 41.148 -13.925 18.970 1.00 36.67 C ANISOU 2184 CA GLY C 57 4757 4390 4788 160 -264 306 C ATOM 2185 C GLY C 57 40.617 -12.749 18.170 1.00 33.56 C ANISOU 2185 C GLY C 57 4327 4027 4397 127 -223 259 C ATOM 2186 O GLY C 57 39.461 -12.736 17.757 1.00 32.95 O ANISOU 2186 O GLY C 57 4296 3924 4298 85 -209 224 O ATOM 2187 N PRO C 58 41.476 -11.752 17.947 1.00 33.07 N ANISOU 2187 N PRO C 58 4182 4024 4361 144 -206 262 N ATOM 2188 CA PRO C 58 41.138 -10.548 17.185 1.00 30.93 C ANISOU 2188 CA PRO C 58 3876 3783 4095 117 -170 223 C ATOM 2189 C PRO C 58 40.917 -10.869 15.713 1.00 31.43 C ANISOU 2189 C PRO C 58 3973 3805 4164 167 -128 196 C ATOM 2190 O PRO C 58 41.623 -11.712 15.154 1.00 35.17 O ANISOU 2190 O PRO C 58 4463 4250 4650 245 -115 211 O ATOM 2191 CB PRO C 58 42.402 -9.681 17.311 1.00 36.15 C ANISOU 2191 CB PRO C 58 4445 4510 4781 132 -169 248 C ATOM 2192 CG PRO C 58 43.237 -10.309 18.366 1.00 39.54 C ANISOU 2192 CG PRO C 58 4855 4956 5214 149 -213 300 C ATOM 2193 CD PRO C 58 42.869 -11.748 18.420 1.00 40.63 C ANISOU 2193 CD PRO C 58 5071 5025 5341 189 -226 310 C ATOM 2194 N ILE C 59 39.944 -10.204 15.094 1.00 29.00 N ANISOU 2194 N ILE C 59 3679 3495 3845 125 -106 157 N ATOM 2195 CA ILE C 59 39.833 -10.226 13.642 1.00 28.07 C ANISOU 2195 CA ILE C 59 3583 3353 3731 162 -67 132 C ATOM 2196 C ILE C 59 39.697 -8.785 13.208 1.00 31.78 C ANISOU 2196 C ILE C 59 4000 3868 4209 128 -45 111 C ATOM 2197 O ILE C 59 39.008 -7.993 13.848 1.00 31.71 O ANISOU 2197 O ILE C 59 3976 3881 4192 67 -58 100 O ATOM 2198 CB ILE C 59 38.638 -11.048 13.139 1.00 38.42 C ANISOU 2198 CB ILE C 59 4981 4603 5012 142 -68 109 C ATOM 2199 CG1 ILE C 59 37.329 -10.477 13.679 1.00 36.40 C ANISOU 2199 CG1 ILE C 59 4727 4364 4737 57 -84 93 C ATOM 2200 CG2 ILE C 59 38.793 -12.510 13.548 1.00 45.10 C ANISOU 2200 CG2 ILE C 59 5897 5393 5847 173 -91 130 C ATOM 2201 CD1 ILE C 59 36.098 -11.112 13.067 1.00 51.75 C ANISOU 2201 CD1 ILE C 59 6743 6267 6653 25 -86 74 C ATOM 2202 N LYS C 60 40.389 -8.451 12.136 1.00 30.43 N ANISOU 2202 N LYS C 60 3803 3709 4052 172 -11 107 N ATOM 2203 CA LYS C 60 40.414 -7.093 11.662 1.00 25.31 C ANISOU 2203 CA LYS C 60 3108 3099 3411 143 8 94 C ATOM 2204 C LYS C 60 39.693 -6.994 10.318 1.00 27.20 C ANISOU 2204 C LYS C 60 3388 3310 3638 146 37 64 C ATOM 2205 O LYS C 60 40.068 -7.662 9.363 1.00 33.61 O ANISOU 2205 O LYS C 60 4227 4098 4445 198 62 61 O ATOM 2206 CB LYS C 60 41.856 -6.607 11.523 1.00 29.62 C ANISOU 2206 CB LYS C 60 3580 3694 3979 176 23 120 C ATOM 2207 CG LYS C 60 41.941 -5.086 11.349 1.00 41.79 C ANISOU 2207 CG LYS C 60 5077 5277 5526 127 31 112 C ATOM 2208 CD LYS C 60 43.293 -4.531 11.780 1.00 47.44 C ANISOU 2208 CD LYS C 60 5714 6055 6258 126 25 148 C ATOM 2209 CE LYS C 60 44.314 -4.690 10.672 1.00 57.89 C ANISOU 2209 CE LYS C 60 6999 7404 7593 185 64 162 C ATOM 2210 NZ LYS C 60 45.690 -4.454 11.187 1.00 65.44 N ANISOU 2210 NZ LYS C 60 7869 8428 8565 191 54 208 N ATOM 2211 N PHE C 61 38.658 -6.156 10.257 1.00 27.65 N ANISOU 2211 N PHE C 61 3450 3370 3687 93 32 44 N ATOM 2212 CA PHE C 61 38.041 -5.829 8.973 1.00 27.38 C ANISOU 2212 CA PHE C 61 3441 3321 3642 90 54 23 C ATOM 2213 C PHE C 61 38.566 -4.500 8.471 1.00 30.07 C ANISOU 2213 C PHE C 61 3732 3696 3995 83 73 23 C ATOM 2214 O PHE C 61 38.361 -3.466 9.103 1.00 28.94 O ANISOU 2214 O PHE C 61 3560 3576 3861 44 62 22 O ATOM 2215 CB PHE C 61 36.520 -5.748 9.092 1.00 24.89 C ANISOU 2215 CB PHE C 61 3158 2990 3310 42 36 6 C ATOM 2216 CG PHE C 61 35.865 -7.058 9.366 1.00 26.13 C ANISOU 2216 CG PHE C 61 3372 3111 3445 34 16 7 C ATOM 2217 CD1 PHE C 61 35.589 -7.954 8.330 1.00 27.80 C ANISOU 2217 CD1 PHE C 61 3647 3280 3634 49 24 -2 C ATOM 2218 CD2 PHE C 61 35.483 -7.379 10.658 1.00 33.44 C ANISOU 2218 CD2 PHE C 61 4298 4042 4368 4 -11 16 C ATOM 2219 CE1 PHE C 61 34.961 -9.163 8.603 1.00 34.96 C ANISOU 2219 CE1 PHE C 61 4619 4148 4516 32 1 -1 C ATOM 2220 CE2 PHE C 61 34.859 -8.582 10.936 1.00 31.76 C ANISOU 2220 CE2 PHE C 61 4142 3795 4131 -13 -32 20 C ATOM 2221 CZ PHE C 61 34.594 -9.472 9.901 1.00 34.97 C ANISOU 2221 CZ PHE C 61 4615 4156 4516 0 -27 12 C ATOM 2222 N ASN C 62 39.254 -4.533 7.337 1.00 28.53 N ANISOU 2222 N ASN C 62 3536 3505 3799 119 105 24 N ATOM 2223 CA ASN C 62 39.762 -3.326 6.727 1.00 28.20 C ANISOU 2223 CA ASN C 62 3456 3496 3765 106 124 27 C ATOM 2224 C ASN C 62 38.678 -2.791 5.803 1.00 27.61 C ANISOU 2224 C ASN C 62 3417 3400 3675 80 127 8 C ATOM 2225 O ASN C 62 38.525 -3.271 4.672 1.00 27.24 O ANISOU 2225 O ASN C 62 3409 3333 3608 99 146 -1 O ATOM 2226 CB ASN C 62 41.048 -3.630 5.969 1.00 28.68 C ANISOU 2226 CB ASN C 62 3490 3578 3827 156 160 41 C ATOM 2227 CG ASN C 62 42.156 -4.128 6.890 1.00 32.90 C ANISOU 2227 CG ASN C 62 3976 4143 4381 187 154 69 C ATOM 2228 OD1 ASN C 62 42.324 -3.623 8.006 1.00 33.54 O ANISOU 2228 OD1 ASN C 62 4020 4249 4475 152 124 83 O ATOM 2229 ND2 ASN C 62 42.917 -5.111 6.428 1.00 34.64 N ANISOU 2229 ND2 ASN C 62 4199 4362 4602 255 181 78 N ATOM 2230 N VAL C 63 37.919 -1.823 6.317 1.00 31.02 N ANISOU 2230 N VAL C 63 3839 3834 4112 38 107 3 N ATOM 2231 CA VAL C 63 36.719 -1.331 5.648 1.00 27.02 C ANISOU 2231 CA VAL C 63 3361 3312 3595 16 101 -9 C ATOM 2232 C VAL C 63 37.029 -0.181 4.676 1.00 25.89 C ANISOU 2232 C VAL C 63 3208 3178 3452 7 117 -4 C ATOM 2233 O VAL C 63 37.566 0.843 5.053 1.00 26.80 O ANISOU 2233 O VAL C 63 3294 3310 3580 -10 118 4 O ATOM 2234 CB VAL C 63 35.627 -0.916 6.669 1.00 23.52 C ANISOU 2234 CB VAL C 63 2914 2867 3157 -14 76 -16 C ATOM 2235 CG1 VAL C 63 34.374 -0.350 5.941 1.00 25.34 C ANISOU 2235 CG1 VAL C 63 3160 3087 3379 -28 70 -22 C ATOM 2236 CG2 VAL C 63 35.221 -2.089 7.505 1.00 27.61 C ANISOU 2236 CG2 VAL C 63 3447 3375 3667 -14 60 -18 C ATOM 2237 N TRP C 64 36.665 -0.371 3.414 1.00 29.22 N ANISOU 2237 N TRP C 64 3664 3586 3853 13 128 -8 N ATOM 2238 CA TRP C 64 36.976 0.604 2.385 1.00 30.39 C ANISOU 2238 CA TRP C 64 3811 3742 3995 3 143 0 C ATOM 2239 C TRP C 64 35.782 1.537 2.237 1.00 28.78 C ANISOU 2239 C TRP C 64 3619 3525 3793 -22 120 0 C ATOM 2240 O TRP C 64 34.701 1.115 1.835 1.00 31.30 O ANISOU 2240 O TRP C 64 3965 3830 4099 -26 104 -4 O ATOM 2241 CB TRP C 64 37.287 -0.106 1.067 1.00 28.45 C ANISOU 2241 CB TRP C 64 3599 3490 3719 23 169 -3 C ATOM 2242 CG TRP C 64 38.667 -0.736 1.027 1.00 29.25 C ANISOU 2242 CG TRP C 64 3680 3613 3822 60 204 1 C ATOM 2243 CD1 TRP C 64 39.233 -1.540 1.974 1.00 26.89 C ANISOU 2243 CD1 TRP C 64 3360 3320 3539 88 204 3 C ATOM 2244 CD2 TRP C 64 39.637 -0.610 -0.021 1.00 32.59 C ANISOU 2244 CD2 TRP C 64 4097 4058 4227 75 245 8 C ATOM 2245 NE1 TRP C 64 40.511 -1.905 1.588 1.00 29.12 N ANISOU 2245 NE1 TRP C 64 3617 3628 3819 128 243 13 N ATOM 2246 CE2 TRP C 64 40.777 -1.350 0.363 1.00 32.06 C ANISOU 2246 CE2 TRP C 64 3997 4014 4170 120 271 15 C ATOM 2247 CE3 TRP C 64 39.654 0.060 -1.250 1.00 31.03 C ANISOU 2247 CE3 TRP C 64 3919 3867 4006 56 262 13 C ATOM 2248 CZ2 TRP C 64 41.918 -1.438 -0.432 1.00 33.98 C ANISOU 2248 CZ2 TRP C 64 4219 4292 4401 150 320 24 C ATOM 2249 CZ3 TRP C 64 40.788 -0.029 -2.043 1.00 30.07 C ANISOU 2249 CZ3 TRP C 64 3782 3776 3866 78 310 20 C ATOM 2250 CH2 TRP C 64 41.905 -0.765 -1.628 1.00 31.61 C ANISOU 2250 CH2 TRP C 64 3937 4000 4073 126 341 25 C ATOM 2251 N ASP C 65 35.959 2.794 2.620 1.00 33.29 N ANISOU 2251 N ASP C 65 4169 4099 4380 -39 115 7 N ATOM 2252 CA ASP C 65 34.883 3.771 2.511 1.00 28.49 C ANISOU 2252 CA ASP C 65 3574 3475 3778 -50 96 9 C ATOM 2253 C ASP C 65 35.226 4.756 1.399 1.00 33.77 C ANISOU 2253 C ASP C 65 4257 4137 4436 -63 103 24 C ATOM 2254 O ASP C 65 36.363 5.202 1.286 1.00 29.53 O ANISOU 2254 O ASP C 65 3710 3613 3899 -76 120 33 O ATOM 2255 CB ASP C 65 34.707 4.515 3.834 1.00 26.53 C ANISOU 2255 CB ASP C 65 3310 3222 3550 -57 87 2 C ATOM 2256 CG ASP C 65 33.507 5.442 3.824 1.00 28.47 C ANISOU 2256 CG ASP C 65 3567 3447 3803 -53 72 2 C ATOM 2257 OD1 ASP C 65 32.419 5.010 3.368 1.00 31.23 O ANISOU 2257 OD1 ASP C 65 3921 3799 4147 -42 60 5 O ATOM 2258 OD2 ASP C 65 33.654 6.613 4.237 1.00 33.31 O ANISOU 2258 OD2 ASP C 65 4188 4043 4426 -60 72 2 O ATOM 2259 N THR C 66 34.247 5.084 0.563 1.00 30.31 N ANISOU 2259 N THR C 66 3844 3685 3989 -63 88 32 N ATOM 2260 CA THR C 66 34.472 6.026 -0.525 1.00 30.35 C ANISOU 2260 CA THR C 66 3870 3680 3981 -78 90 51 C ATOM 2261 C THR C 66 34.617 7.446 -0.018 1.00 29.72 C ANISOU 2261 C THR C 66 3792 3581 3920 -90 83 59 C ATOM 2262 O THR C 66 34.363 7.727 1.156 1.00 33.19 O ANISOU 2262 O THR C 66 4219 4010 4380 -83 76 47 O ATOM 2263 CB THR C 66 33.275 6.054 -1.476 1.00 29.77 C ANISOU 2263 CB THR C 66 3822 3597 3893 -76 66 64 C ATOM 2264 OG1 THR C 66 32.185 6.732 -0.829 1.00 33.34 O ANISOU 2264 OG1 THR C 66 4264 4035 4368 -61 42 67 O ATOM 2265 CG2 THR C 66 32.853 4.637 -1.835 1.00 32.59 C ANISOU 2265 CG2 THR C 66 4189 3967 4228 -72 64 54 C ATOM 2266 N ALA C 67 35.027 8.328 -0.925 1.00 29.16 N ANISOU 2266 N ALA C 67 3745 3500 3836 -111 84 79 N ATOM 2267 CA ALA C 67 34.989 9.774 -0.694 1.00 32.66 C ANISOU 2267 CA ALA C 67 4212 3908 4290 -125 72 91 C ATOM 2268 C ALA C 67 33.884 10.416 -1.539 1.00 37.86 C ANISOU 2268 C ALA C 67 4902 4537 4945 -110 47 110 C ATOM 2269 O ALA C 67 34.031 11.539 -2.044 1.00 38.16 O ANISOU 2269 O ALA C 67 4975 4545 4977 -127 38 132 O ATOM 2270 CB ALA C 67 36.330 10.392 -1.012 1.00 35.94 C ANISOU 2270 CB ALA C 67 4632 4331 4691 -169 87 106 C ATOM 2271 N GLY C 68 32.784 9.688 -1.715 1.00 32.67 N ANISOU 2271 N GLY C 68 4233 3891 4288 -82 33 108 N ATOM 2272 CA GLY C 68 31.589 10.271 -2.304 1.00 34.34 C ANISOU 2272 CA GLY C 68 4461 4084 4504 -62 4 131 C ATOM 2273 C GLY C 68 31.419 10.037 -3.788 1.00 33.26 C ANISOU 2273 C GLY C 68 4347 3958 4334 -80 -10 157 C ATOM 2274 O GLY C 68 30.409 10.437 -4.360 1.00 36.69 O ANISOU 2274 O GLY C 68 4790 4383 4767 -65 -41 182 O ATOM 2275 N GLN C 69 32.402 9.395 -4.415 1.00 32.62 N ANISOU 2275 N GLN C 69 4275 3898 4223 -110 14 151 N ATOM 2276 CA GLN C 69 32.405 9.228 -5.867 1.00 32.02 C ANISOU 2276 CA GLN C 69 4231 3831 4105 -134 8 172 C ATOM 2277 C GLN C 69 31.256 8.360 -6.354 1.00 31.82 C ANISOU 2277 C GLN C 69 4206 3820 4063 -127 -19 177 C ATOM 2278 O GLN C 69 30.891 8.423 -7.527 1.00 40.22 O ANISOU 2278 O GLN C 69 5302 4886 5093 -148 -39 202 O ATOM 2279 CB GLN C 69 33.741 8.650 -6.356 1.00 35.37 C ANISOU 2279 CB GLN C 69 4662 4279 4499 -160 50 161 C ATOM 2280 CG GLN C 69 34.985 9.394 -5.848 1.00 39.86 C ANISOU 2280 CG GLN C 69 5217 4847 5080 -178 76 161 C ATOM 2281 CD GLN C 69 35.528 8.793 -4.553 1.00 40.91 C ANISOU 2281 CD GLN C 69 5307 4996 5241 -160 96 133 C ATOM 2282 OE1 GLN C 69 34.779 8.212 -3.783 1.00 38.31 O ANISOU 2282 OE1 GLN C 69 4960 4663 4932 -133 83 115 O ATOM 2283 NE2 GLN C 69 36.831 8.927 -4.324 1.00 43.46 N ANISOU 2283 NE2 GLN C 69 5609 5342 5562 -181 126 133 N ATOM 2284 N GLU C 70 30.659 7.569 -5.460 1.00 29.53 N ANISOU 2284 N GLU C 70 3884 3543 3792 -107 -24 157 N ATOM 2285 CA GLU C 70 29.512 6.728 -5.867 1.00 26.96 C ANISOU 2285 CA GLU C 70 3557 3237 3448 -112 -55 165 C ATOM 2286 C GLU C 70 28.334 7.569 -6.374 1.00 32.43 C ANISOU 2286 C GLU C 70 4246 3928 4147 -104 -101 206 C ATOM 2287 O GLU C 70 27.419 7.059 -7.036 1.00 33.73 O ANISOU 2287 O GLU C 70 4413 4114 4287 -121 -135 226 O ATOM 2288 CB GLU C 70 29.054 5.820 -4.717 1.00 32.43 C ANISOU 2288 CB GLU C 70 4214 3945 4162 -98 -53 141 C ATOM 2289 CG GLU C 70 28.357 6.532 -3.552 1.00 27.76 C ANISOU 2289 CG GLU C 70 3578 3353 3618 -63 -62 143 C ATOM 2290 CD GLU C 70 29.344 7.042 -2.476 1.00 31.76 C ANISOU 2290 CD GLU C 70 4075 3840 4151 -48 -29 118 C ATOM 2291 OE1 GLU C 70 30.568 7.125 -2.746 1.00 32.39 O ANISOU 2291 OE1 GLU C 70 4177 3911 4220 -64 -4 110 O ATOM 2292 OE2 GLU C 70 28.889 7.368 -1.358 1.00 31.91 O ANISOU 2292 OE2 GLU C 70 4066 3857 4201 -22 -27 109 O ATOM 2293 N LYS C 71 28.352 8.861 -6.057 1.00 35.83 N ANISOU 2293 N LYS C 71 4672 4332 4609 -78 -103 220 N ATOM 2294 CA LYS C 71 27.296 9.763 -6.515 1.00 41.04 C ANISOU 2294 CA LYS C 71 5329 4984 5279 -56 -145 262 C ATOM 2295 C LYS C 71 27.316 9.941 -8.030 1.00 45.42 C ANISOU 2295 C LYS C 71 5928 5538 5789 -92 -170 298 C ATOM 2296 O LYS C 71 26.314 10.322 -8.627 1.00 40.16 O ANISOU 2296 O LYS C 71 5258 4880 5120 -84 -215 339 O ATOM 2297 CB LYS C 71 27.423 11.129 -5.842 1.00 44.81 C ANISOU 2297 CB LYS C 71 5811 5420 5797 -17 -138 266 C ATOM 2298 CG LYS C 71 27.402 11.071 -4.330 1.00 48.96 C ANISOU 2298 CG LYS C 71 6301 5942 6359 16 -112 231 C ATOM 2299 CD LYS C 71 27.975 12.340 -3.714 1.00 59.95 C ANISOU 2299 CD LYS C 71 7723 7281 7775 35 -95 224 C ATOM 2300 CE LYS C 71 28.096 12.180 -2.214 1.00 57.95 C ANISOU 2300 CE LYS C 71 7443 7028 7548 56 -67 184 C ATOM 2301 NZ LYS C 71 26.797 11.693 -1.678 1.00 54.60 N ANISOU 2301 NZ LYS C 71 6965 6637 7141 97 -77 185 N ATOM 2302 N PHE C 72 28.449 9.647 -8.656 1.00 40.03 N ANISOU 2302 N PHE C 72 5286 4852 5070 -132 -141 283 N ATOM 2303 CA PHE C 72 28.635 10.006 -10.054 1.00 37.20 C ANISOU 2303 CA PHE C 72 4979 4490 4666 -169 -158 316 C ATOM 2304 C PHE C 72 28.766 8.810 -10.991 1.00 43.40 C ANISOU 2304 C PHE C 72 5796 5303 5391 -214 -153 306 C ATOM 2305 O PHE C 72 28.950 8.964 -12.189 1.00 41.72 O ANISOU 2305 O PHE C 72 5631 5091 5129 -251 -162 328 O ATOM 2306 CB PHE C 72 29.822 10.963 -10.177 1.00 34.30 C ANISOU 2306 CB PHE C 72 4643 4092 4297 -183 -128 317 C ATOM 2307 CG PHE C 72 29.771 12.090 -9.187 1.00 34.74 C ANISOU 2307 CG PHE C 72 4684 4111 4405 -145 -130 320 C ATOM 2308 CD1 PHE C 72 28.895 13.148 -9.369 1.00 38.64 C ANISOU 2308 CD1 PHE C 72 5189 4573 4918 -116 -172 360 C ATOM 2309 CD2 PHE C 72 30.572 12.074 -8.052 1.00 38.10 C ANISOU 2309 CD2 PHE C 72 5088 4529 4858 -136 -92 283 C ATOM 2310 CE1 PHE C 72 28.833 14.173 -8.448 1.00 39.87 C ANISOU 2310 CE1 PHE C 72 5346 4685 5118 -76 -170 358 C ATOM 2311 CE2 PHE C 72 30.514 13.099 -7.128 1.00 37.89 C ANISOU 2311 CE2 PHE C 72 5062 4463 4872 -107 -94 282 C ATOM 2312 CZ PHE C 72 29.643 14.150 -7.327 1.00 43.45 C ANISOU 2312 CZ PHE C 72 5787 5128 5593 -76 -130 317 C ATOM 2313 N GLY C 73 28.647 7.613 -10.438 1.00 41.64 N ANISOU 2313 N GLY C 73 5553 5099 5168 -211 -139 272 N ATOM 2314 CA GLY C 73 28.679 6.414 -11.245 1.00 42.61 C ANISOU 2314 CA GLY C 73 5719 5240 5233 -250 -136 258 C ATOM 2315 C GLY C 73 29.288 5.276 -10.473 1.00 41.62 C ANISOU 2315 C GLY C 73 5586 5117 5113 -239 -93 209 C ATOM 2316 O GLY C 73 29.518 5.394 -9.266 1.00 35.16 O ANISOU 2316 O GLY C 73 4720 4294 4344 -204 -75 191 O ATOM 2317 N GLY C 74 29.557 4.177 -11.173 1.00 35.13 N ANISOU 2317 N GLY C 74 4816 4297 4235 -267 -77 188 N ATOM 2318 CA GLY C 74 30.141 3.006 -10.545 1.00 39.24 C ANISOU 2318 CA GLY C 74 5341 4813 4755 -252 -37 144 C ATOM 2319 C GLY C 74 31.547 3.255 -10.026 1.00 40.78 C ANISOU 2319 C GLY C 74 5515 5005 4976 -219 23 121 C ATOM 2320 O GLY C 74 32.244 4.172 -10.467 1.00 39.10 O ANISOU 2320 O GLY C 74 5302 4794 4761 -223 42 136 O ATOM 2321 N LEU C 75 31.966 2.421 -9.081 1.00 36.71 N ANISOU 2321 N LEU C 75 4979 4485 4482 -191 49 90 N ATOM 2322 CA LEU C 75 33.301 2.517 -8.516 1.00 34.83 C ANISOU 2322 CA LEU C 75 4712 4252 4268 -160 102 73 C ATOM 2323 C LEU C 75 34.299 1.787 -9.414 1.00 38.71 C ANISOU 2323 C LEU C 75 5251 4747 4709 -157 155 53 C ATOM 2324 O LEU C 75 33.934 0.851 -10.131 1.00 37.03 O ANISOU 2324 O LEU C 75 5101 4521 4447 -170 153 39 O ATOM 2325 CB LEU C 75 33.301 1.957 -7.089 1.00 34.38 C ANISOU 2325 CB LEU C 75 4613 4193 4256 -130 103 53 C ATOM 2326 CG LEU C 75 32.371 2.720 -6.137 1.00 40.70 C ANISOU 2326 CG LEU C 75 5365 4993 5104 -128 62 69 C ATOM 2327 CD1 LEU C 75 32.279 2.060 -4.756 1.00 33.75 C ANISOU 2327 CD1 LEU C 75 4452 4114 4258 -107 63 49 C ATOM 2328 CD2 LEU C 75 32.827 4.181 -6.017 1.00 35.99 C ANISOU 2328 CD2 LEU C 75 4741 4398 4534 -126 66 88 C ATOM 2329 N ARG C 76 35.553 2.230 -9.383 1.00 34.78 N ANISOU 2329 N ARG C 76 4725 4270 4221 -141 202 53 N ATOM 2330 CA ARG C 76 36.598 1.649 -10.215 1.00 33.42 C ANISOU 2330 CA ARG C 76 4585 4111 4003 -128 263 37 C ATOM 2331 C ARG C 76 36.983 0.243 -9.733 1.00 39.36 C ANISOU 2331 C ARG C 76 5350 4852 4755 -82 294 2 C ATOM 2332 O ARG C 76 36.766 -0.100 -8.570 1.00 36.46 O ANISOU 2332 O ARG C 76 4947 4474 4431 -61 275 -4 O ATOM 2333 CB ARG C 76 37.818 2.575 -10.247 1.00 34.00 C ANISOU 2333 CB ARG C 76 4608 4220 4089 -128 302 54 C ATOM 2334 CG ARG C 76 37.528 3.952 -10.866 1.00 41.79 C ANISOU 2334 CG ARG C 76 5601 5209 5067 -177 274 90 C ATOM 2335 CD ARG C 76 38.652 4.935 -10.585 1.00 50.31 C ANISOU 2335 CD ARG C 76 6627 6320 6169 -188 301 111 C ATOM 2336 NE ARG C 76 39.941 4.436 -11.052 1.00 56.01 N ANISOU 2336 NE ARG C 76 7336 7084 6860 -172 372 101 N ATOM 2337 CZ ARG C 76 41.118 4.888 -10.625 1.00 62.59 C ANISOU 2337 CZ ARG C 76 8106 7961 7715 -172 406 115 C ATOM 2338 NH1 ARG C 76 41.173 5.849 -9.712 1.00 57.92 N ANISOU 2338 NH1 ARG C 76 7470 7367 7170 -194 373 135 N ATOM 2339 NH2 ARG C 76 42.242 4.377 -11.108 1.00 61.47 N ANISOU 2339 NH2 ARG C 76 7945 7866 7544 -150 474 110 N ATOM 2340 N ASP C 77 37.540 -0.565 -10.635 1.00 41.77 N ANISOU 2340 N ASP C 77 5711 5153 5005 -66 343 -19 N ATOM 2341 CA ASP C 77 37.922 -1.940 -10.316 1.00 38.34 C ANISOU 2341 CA ASP C 77 5306 4697 4563 -15 377 -52 C ATOM 2342 C ASP C 77 38.804 -2.021 -9.070 1.00 37.86 C ANISOU 2342 C ASP C 77 5165 4658 4564 37 398 -51 C ATOM 2343 O ASP C 77 38.640 -2.915 -8.242 1.00 38.23 O ANISOU 2343 O ASP C 77 5216 4678 4631 68 388 -66 O ATOM 2344 CB ASP C 77 38.668 -2.585 -11.490 1.00 43.20 C ANISOU 2344 CB ASP C 77 5988 5313 5113 8 444 -75 C ATOM 2345 CG ASP C 77 37.736 -3.066 -12.602 1.00 51.73 C ANISOU 2345 CG ASP C 77 7180 6357 6120 -37 422 -89 C ATOM 2346 OD1 ASP C 77 36.541 -2.708 -12.596 1.00 42.06 O ANISOU 2346 OD1 ASP C 77 5966 5118 4896 -93 352 -71 O ATOM 2347 OD2 ASP C 77 38.207 -3.812 -13.488 1.00 60.72 O ANISOU 2347 OD2 ASP C 77 8394 7481 7196 -17 476 -116 O ATOM 2348 N GLY C 78 39.751 -1.097 -8.950 1.00 35.11 N ANISOU 2348 N GLY C 78 4744 4357 4240 40 425 -29 N ATOM 2349 CA GLY C 78 40.685 -1.111 -7.836 1.00 37.71 C ANISOU 2349 CA GLY C 78 4991 4716 4621 80 443 -21 C ATOM 2350 C GLY C 78 40.010 -1.015 -6.479 1.00 39.68 C ANISOU 2350 C GLY C 78 5207 4947 4923 72 386 -17 C ATOM 2351 O GLY C 78 40.528 -1.509 -5.467 1.00 35.51 O ANISOU 2351 O GLY C 78 4637 4426 4430 110 391 -19 O ATOM 2352 N TYR C 79 38.850 -0.371 -6.443 1.00 32.98 N ANISOU 2352 N TYR C 79 4374 4077 4079 24 332 -9 N ATOM 2353 CA TYR C 79 38.109 -0.285 -5.190 1.00 30.97 C ANISOU 2353 CA TYR C 79 4092 3808 3869 17 283 -7 C ATOM 2354 C TYR C 79 37.682 -1.685 -4.748 1.00 30.21 C ANISOU 2354 C TYR C 79 4034 3678 3766 44 275 -30 C ATOM 2355 O TYR C 79 37.790 -2.056 -3.571 1.00 30.92 O ANISOU 2355 O TYR C 79 4091 3766 3891 63 264 -32 O ATOM 2356 CB TYR C 79 36.889 0.631 -5.334 1.00 33.34 C ANISOU 2356 CB TYR C 79 4402 4095 4172 -30 233 7 C ATOM 2357 CG TYR C 79 36.046 0.636 -4.094 1.00 34.38 C ANISOU 2357 CG TYR C 79 4506 4213 4342 -32 191 6 C ATOM 2358 CD1 TYR C 79 36.317 1.521 -3.040 1.00 32.77 C ANISOU 2358 CD1 TYR C 79 4246 4023 4181 -34 181 16 C ATOM 2359 CD2 TYR C 79 35.005 -0.273 -3.945 1.00 34.93 C ANISOU 2359 CD2 TYR C 79 4611 4261 4400 -38 162 -5 C ATOM 2360 CE1 TYR C 79 35.559 1.491 -1.873 1.00 32.08 C ANISOU 2360 CE1 TYR C 79 4138 3928 4125 -34 150 12 C ATOM 2361 CE2 TYR C 79 34.244 -0.301 -2.792 1.00 39.63 C ANISOU 2361 CE2 TYR C 79 5178 4853 5027 -42 129 -5 C ATOM 2362 CZ TYR C 79 34.529 0.568 -1.761 1.00 41.29 C ANISOU 2362 CZ TYR C 79 5332 5077 5279 -36 126 2 C ATOM 2363 OH TYR C 79 33.768 0.508 -0.622 1.00 37.88 O ANISOU 2363 OH TYR C 79 4877 4645 4872 -40 100 0 O ATOM 2364 N TYR C 80 37.209 -2.472 -5.705 1.00 34.09 N ANISOU 2364 N TYR C 80 4603 4141 4208 38 280 -46 N ATOM 2365 CA TYR C 80 36.638 -3.781 -5.411 1.00 33.31 C ANISOU 2365 CA TYR C 80 4562 4001 4095 48 264 -66 C ATOM 2366 C TYR C 80 37.674 -4.885 -5.258 1.00 37.49 C ANISOU 2366 C TYR C 80 5111 4515 4619 112 312 -85 C ATOM 2367 O TYR C 80 37.441 -5.878 -4.559 1.00 40.09 O ANISOU 2367 O TYR C 80 5467 4811 4954 130 298 -95 O ATOM 2368 CB TYR C 80 35.660 -4.168 -6.519 1.00 31.65 C ANISOU 2368 CB TYR C 80 4437 3761 3826 5 243 -74 C ATOM 2369 CG TYR C 80 34.371 -3.393 -6.497 1.00 35.79 C ANISOU 2369 CG TYR C 80 4944 4295 4358 -53 183 -53 C ATOM 2370 CD1 TYR C 80 33.436 -3.585 -5.484 1.00 37.81 C ANISOU 2370 CD1 TYR C 80 5176 4547 4642 -71 137 -46 C ATOM 2371 CD2 TYR C 80 34.075 -2.475 -7.500 1.00 34.69 C ANISOU 2371 CD2 TYR C 80 4812 4173 4197 -87 173 -35 C ATOM 2372 CE1 TYR C 80 32.242 -2.880 -5.466 1.00 36.54 C ANISOU 2372 CE1 TYR C 80 4990 4403 4490 -114 87 -23 C ATOM 2373 CE2 TYR C 80 32.891 -1.768 -7.485 1.00 37.86 C ANISOU 2373 CE2 TYR C 80 5192 4584 4607 -129 117 -10 C ATOM 2374 CZ TYR C 80 31.977 -1.976 -6.472 1.00 34.23 C ANISOU 2374 CZ TYR C 80 4703 4125 4179 -138 77 -5 C ATOM 2375 OH TYR C 80 30.806 -1.261 -6.476 1.00 35.79 O ANISOU 2375 OH TYR C 80 4870 4339 4387 -170 27 23 O ATOM 2376 N ILE C 81 38.817 -4.716 -5.914 1.00 34.77 N ANISOU 2376 N ILE C 81 4752 4197 4261 149 371 -86 N ATOM 2377 CA ILE C 81 39.761 -5.816 -6.075 1.00 36.65 C ANISOU 2377 CA ILE C 81 5021 4420 4483 221 426 -104 C ATOM 2378 C ILE C 81 40.239 -6.389 -4.742 1.00 39.48 C ANISOU 2378 C ILE C 81 5334 4776 4891 270 419 -98 C ATOM 2379 O ILE C 81 40.569 -5.648 -3.812 1.00 37.44 O ANISOU 2379 O ILE C 81 4985 4559 4681 263 402 -74 O ATOM 2380 CB ILE C 81 40.964 -5.440 -6.969 1.00 44.20 C ANISOU 2380 CB ILE C 81 5952 5422 5421 256 496 -101 C ATOM 2381 CG1 ILE C 81 41.596 -6.705 -7.557 1.00 52.78 C ANISOU 2381 CG1 ILE C 81 7110 6478 6468 329 558 -130 C ATOM 2382 CG2 ILE C 81 41.991 -4.674 -6.195 1.00 46.65 C ANISOU 2382 CG2 ILE C 81 6144 5797 5784 275 510 -72 C ATOM 2383 CD1 ILE C 81 40.639 -7.525 -8.404 1.00 55.63 C ANISOU 2383 CD1 ILE C 81 7606 6769 6764 302 545 -163 C ATOM 2384 N GLN C 82 40.254 -7.718 -4.667 1.00 39.52 N ANISOU 2384 N GLN C 82 5411 4728 4877 315 431 -119 N ATOM 2385 CA GLN C 82 40.697 -8.432 -3.474 1.00 36.60 C ANISOU 2385 CA GLN C 82 5013 4346 4546 366 423 -111 C ATOM 2386 C GLN C 82 39.766 -8.261 -2.276 1.00 32.27 C ANISOU 2386 C GLN C 82 4441 3790 4030 313 354 -98 C ATOM 2387 O GLN C 82 40.131 -8.631 -1.159 1.00 34.11 O ANISOU 2387 O GLN C 82 4637 4024 4299 343 341 -85 O ATOM 2388 CB GLN C 82 42.123 -8.031 -3.086 1.00 40.50 C ANISOU 2388 CB GLN C 82 5403 4905 5079 426 465 -87 C ATOM 2389 CG GLN C 82 43.141 -8.237 -4.190 1.00 55.94 C ANISOU 2389 CG GLN C 82 7368 6881 7004 488 543 -97 C ATOM 2390 CD GLN C 82 43.389 -9.699 -4.484 1.00 70.39 C ANISOU 2390 CD GLN C 82 9291 8647 8805 569 581 -123 C ATOM 2391 OE1 GLN C 82 43.284 -10.139 -5.628 1.00 77.63 O ANISOU 2391 OE1 GLN C 82 10300 9529 9666 581 621 -154 O ATOM 2392 NE2 GLN C 82 43.713 -10.464 -3.449 1.00 76.72 N ANISOU 2392 NE2 GLN C 82 10080 9429 9642 623 566 -112 N ATOM 2393 N ALA C 83 38.571 -7.712 -2.484 1.00 33.54 N ANISOU 2393 N ALA C 83 4620 3946 4178 237 311 -99 N ATOM 2394 CA ALA C 83 37.589 -7.701 -1.397 1.00 30.63 C ANISOU 2394 CA ALA C 83 4237 3570 3833 190 252 -90 C ATOM 2395 C ALA C 83 37.312 -9.142 -1.008 1.00 35.31 C ANISOU 2395 C ALA C 83 4908 4101 4406 207 239 -102 C ATOM 2396 O ALA C 83 37.262 -10.025 -1.880 1.00 31.70 O ANISOU 2396 O ALA C 83 4547 3594 3902 221 258 -124 O ATOM 2397 CB ALA C 83 36.312 -7.025 -1.818 1.00 32.44 C ANISOU 2397 CB ALA C 83 4477 3804 4045 116 213 -88 C ATOM 2398 N GLN C 84 37.129 -9.379 0.289 1.00 31.12 N ANISOU 2398 N GLN C 84 4347 3571 3908 202 206 -89 N ATOM 2399 CA GLN C 84 36.872 -10.726 0.779 1.00 33.86 C ANISOU 2399 CA GLN C 84 4770 3857 4238 212 187 -95 C ATOM 2400 C GLN C 84 35.467 -10.803 1.348 1.00 28.98 C ANISOU 2400 C GLN C 84 4169 3232 3611 130 130 -89 C ATOM 2401 O GLN C 84 34.934 -11.889 1.593 1.00 33.20 O ANISOU 2401 O GLN C 84 4781 3714 4118 110 105 -93 O ATOM 2402 CB GLN C 84 37.936 -11.130 1.798 1.00 36.46 C ANISOU 2402 CB GLN C 84 5058 4191 4605 279 199 -79 C ATOM 2403 CG GLN C 84 39.328 -11.214 1.173 1.00 37.82 C ANISOU 2403 CG GLN C 84 5213 4376 4783 367 260 -81 C ATOM 2404 CD GLN C 84 40.436 -11.105 2.185 1.00 42.13 C ANISOU 2404 CD GLN C 84 5670 4962 5377 422 267 -52 C ATOM 2405 OE1 GLN C 84 40.638 -10.048 2.776 1.00 36.07 O ANISOU 2405 OE1 GLN C 84 4806 4257 4642 393 253 -33 O ATOM 2406 NE2 GLN C 84 41.169 -12.203 2.394 1.00 42.27 N ANISOU 2406 NE2 GLN C 84 5723 4942 5396 502 286 -48 N ATOM 2407 N CYS C 85 34.853 -9.634 1.504 1.00 29.82 N ANISOU 2407 N CYS C 85 4204 3391 3736 82 110 -78 N ATOM 2408 CA CYS C 85 33.488 -9.537 2.005 1.00 29.91 C ANISOU 2408 CA CYS C 85 4210 3412 3742 9 62 -69 C ATOM 2409 C CYS C 85 32.975 -8.126 1.748 1.00 31.84 C ANISOU 2409 C CYS C 85 4384 3711 4004 -21 56 -61 C ATOM 2410 O CYS C 85 33.736 -7.263 1.329 1.00 27.56 O ANISOU 2410 O CYS C 85 3800 3192 3478 10 85 -61 O ATOM 2411 CB CYS C 85 33.414 -9.871 3.501 1.00 30.10 C ANISOU 2411 CB CYS C 85 4205 3441 3790 4 38 -56 C ATOM 2412 SG CYS C 85 34.419 -8.814 4.602 1.00 31.33 S ANISOU 2412 SG CYS C 85 4251 3650 4003 43 54 -42 S ATOM 2413 N ALA C 86 31.690 -7.900 2.004 1.00 28.45 N ANISOU 2413 N ALA C 86 3941 3301 3568 -80 18 -51 N ATOM 2414 CA ALA C 86 31.074 -6.610 1.701 1.00 29.87 C ANISOU 2414 CA ALA C 86 4061 3524 3762 -101 9 -40 C ATOM 2415 C ALA C 86 29.815 -6.373 2.516 1.00 29.10 C ANISOU 2415 C ALA C 86 3923 3460 3674 -147 -26 -25 C ATOM 2416 O ALA C 86 29.153 -7.305 2.967 1.00 28.45 O ANISOU 2416 O ALA C 86 3871 3367 3571 -184 -51 -21 O ATOM 2417 CB ALA C 86 30.739 -6.522 0.191 1.00 30.33 C ANISOU 2417 CB ALA C 86 4166 3574 3783 -121 8 -42 C ATOM 2418 N ILE C 87 29.472 -5.102 2.665 1.00 26.67 N ANISOU 2418 N ILE C 87 3548 3191 3394 -144 -26 -16 N ATOM 2419 CA ILE C 87 28.199 -4.688 3.199 1.00 26.55 C ANISOU 2419 CA ILE C 87 3487 3215 3386 -178 -51 -1 C ATOM 2420 C ILE C 87 27.642 -3.767 2.131 1.00 26.58 C ANISOU 2420 C ILE C 87 3474 3238 3388 -183 -60 12 C ATOM 2421 O ILE C 87 28.351 -2.902 1.626 1.00 29.61 O ANISOU 2421 O ILE C 87 3849 3615 3786 -151 -40 9 O ATOM 2422 CB ILE C 87 28.381 -3.877 4.508 1.00 26.37 C ANISOU 2422 CB ILE C 87 3400 3216 3402 -155 -37 -3 C ATOM 2423 CG1 ILE C 87 28.882 -4.795 5.613 1.00 25.18 C ANISOU 2423 CG1 ILE C 87 3266 3052 3251 -155 -35 -10 C ATOM 2424 CG2 ILE C 87 27.066 -3.244 4.909 1.00 27.37 C ANISOU 2424 CG2 ILE C 87 3475 3388 3537 -174 -53 12 C ATOM 2425 CD1 ILE C 87 29.420 -4.018 6.867 1.00 29.75 C ANISOU 2425 CD1 ILE C 87 3795 3647 3861 -132 -19 -16 C ATOM 2426 N ILE C 88 26.400 -4.016 1.735 1.00 26.43 N ANISOU 2426 N ILE C 88 3454 3243 3346 -227 -94 32 N ATOM 2427 CA ILE C 88 25.688 -3.145 0.822 1.00 26.81 C ANISOU 2427 CA ILE C 88 3477 3317 3392 -234 -112 53 C ATOM 2428 C ILE C 88 24.655 -2.423 1.654 1.00 30.94 C ANISOU 2428 C ILE C 88 3921 3890 3944 -230 -122 72 C ATOM 2429 O ILE C 88 23.847 -3.050 2.331 1.00 30.57 O ANISOU 2429 O ILE C 88 3855 3873 3889 -264 -139 81 O ATOM 2430 CB ILE C 88 24.994 -3.958 -0.260 1.00 24.19 C ANISOU 2430 CB ILE C 88 3197 2983 3010 -291 -148 68 C ATOM 2431 CG1 ILE C 88 26.030 -4.691 -1.108 1.00 29.13 C ANISOU 2431 CG1 ILE C 88 3913 3554 3602 -287 -129 44 C ATOM 2432 CG2 ILE C 88 24.167 -3.049 -1.160 1.00 32.35 C ANISOU 2432 CG2 ILE C 88 4197 4052 4042 -300 -174 99 C ATOM 2433 CD1 ILE C 88 25.395 -5.394 -2.344 1.00 29.76 C ANISOU 2433 CD1 ILE C 88 4061 3625 3621 -348 -164 54 C ATOM 2434 N MET C 89 24.696 -1.096 1.630 1.00 28.27 N ANISOU 2434 N MET C 89 3541 3562 3639 -188 -109 77 N ATOM 2435 CA MET C 89 23.845 -0.321 2.509 1.00 26.96 C ANISOU 2435 CA MET C 89 3304 3436 3503 -166 -107 89 C ATOM 2436 C MET C 89 22.779 0.402 1.692 1.00 29.23 C ANISOU 2436 C MET C 89 3554 3759 3793 -163 -134 125 C ATOM 2437 O MET C 89 23.034 0.841 0.573 1.00 31.83 O ANISOU 2437 O MET C 89 3911 4069 4114 -158 -145 135 O ATOM 2438 CB MET C 89 24.696 0.703 3.283 1.00 28.33 C ANISOU 2438 CB MET C 89 3465 3587 3712 -114 -70 67 C ATOM 2439 CG MET C 89 23.950 1.387 4.395 1.00 32.28 C ANISOU 2439 CG MET C 89 3907 4120 4238 -88 -57 68 C ATOM 2440 SD MET C 89 25.038 2.218 5.580 1.00 40.67 S ANISOU 2440 SD MET C 89 4977 5149 5327 -50 -17 34 S ATOM 2441 CE MET C 89 26.028 0.858 6.170 1.00 30.05 C ANISOU 2441 CE MET C 89 3667 3787 3963 -85 -13 14 C ATOM 2442 N PHE C 90 21.578 0.513 2.241 1.00 30.64 N ANISOU 2442 N PHE C 90 3668 3993 3980 -165 -145 147 N ATOM 2443 CA PHE C 90 20.601 1.442 1.677 1.00 30.38 C ANISOU 2443 CA PHE C 90 3582 3998 3962 -139 -165 184 C ATOM 2444 C PHE C 90 19.992 2.219 2.832 1.00 34.70 C ANISOU 2444 C PHE C 90 4061 4580 4546 -87 -138 184 C ATOM 2445 O PHE C 90 20.334 1.974 3.984 1.00 33.48 O ANISOU 2445 O PHE C 90 3905 4419 4396 -83 -107 155 O ATOM 2446 CB PHE C 90 19.534 0.734 0.809 1.00 25.38 C ANISOU 2446 CB PHE C 90 2935 3415 3295 -200 -217 226 C ATOM 2447 CG PHE C 90 18.665 -0.200 1.572 1.00 29.52 C ANISOU 2447 CG PHE C 90 3419 3996 3803 -248 -229 238 C ATOM 2448 CD1 PHE C 90 19.093 -1.501 1.840 1.00 25.08 C ANISOU 2448 CD1 PHE C 90 2914 3409 3206 -308 -232 217 C ATOM 2449 CD2 PHE C 90 17.425 0.210 2.037 1.00 31.04 C ANISOU 2449 CD2 PHE C 90 3515 4265 4013 -233 -235 273 C ATOM 2450 CE1 PHE C 90 18.287 -2.382 2.560 1.00 26.79 C ANISOU 2450 CE1 PHE C 90 3100 3676 3404 -363 -246 231 C ATOM 2451 CE2 PHE C 90 16.621 -0.660 2.764 1.00 28.80 C ANISOU 2451 CE2 PHE C 90 3189 4042 3710 -286 -243 287 C ATOM 2452 CZ PHE C 90 17.062 -1.960 3.024 1.00 30.61 C ANISOU 2452 CZ PHE C 90 3484 4244 3903 -357 -251 266 C ATOM 2453 N ASP C 91 19.121 3.176 2.517 1.00 32.36 N ANISOU 2453 N ASP C 91 3710 4315 4270 -42 -147 216 N ATOM 2454 CA ASP C 91 18.536 4.079 3.503 1.00 31.53 C ANISOU 2454 CA ASP C 91 3545 4236 4200 25 -113 215 C ATOM 2455 C ASP C 91 17.048 3.734 3.557 1.00 33.30 C ANISOU 2455 C ASP C 91 3680 4554 4420 11 -136 260 C ATOM 2456 O ASP C 91 16.370 3.786 2.543 1.00 36.57 O ANISOU 2456 O ASP C 91 4067 5002 4827 -2 -179 306 O ATOM 2457 CB ASP C 91 18.755 5.513 3.010 1.00 32.64 C ANISOU 2457 CB ASP C 91 3699 4333 4371 97 -106 221 C ATOM 2458 CG ASP C 91 18.077 6.574 3.877 1.00 39.17 C ANISOU 2458 CG ASP C 91 4474 5176 5232 180 -71 221 C ATOM 2459 OD1 ASP C 91 17.267 6.246 4.769 1.00 39.82 O ANISOU 2459 OD1 ASP C 91 4494 5320 5315 186 -52 223 O ATOM 2460 OD2 ASP C 91 18.366 7.769 3.643 1.00 42.78 O ANISOU 2460 OD2 ASP C 91 4960 5582 5713 241 -60 219 O ATOM 2461 N VAL C 92 16.549 3.335 4.720 1.00 34.66 N ANISOU 2461 N VAL C 92 3805 4774 4590 5 -109 251 N ATOM 2462 CA VAL C 92 15.161 2.882 4.806 1.00 34.89 C ANISOU 2462 CA VAL C 92 3742 4905 4609 -21 -130 298 C ATOM 2463 C VAL C 92 14.181 4.043 4.645 1.00 37.63 C ANISOU 2463 C VAL C 92 4006 5301 4992 64 -123 335 C ATOM 2464 O VAL C 92 12.971 3.841 4.629 1.00 37.73 O ANISOU 2464 O VAL C 92 3925 5409 5001 55 -140 383 O ATOM 2465 CB VAL C 92 14.884 2.099 6.112 1.00 35.34 C ANISOU 2465 CB VAL C 92 3771 5008 4650 -58 -101 281 C ATOM 2466 CG1 VAL C 92 15.878 0.962 6.244 1.00 34.94 C ANISOU 2466 CG1 VAL C 92 3808 4902 4568 -133 -111 248 C ATOM 2467 CG2 VAL C 92 14.950 3.022 7.336 1.00 34.84 C ANISOU 2467 CG2 VAL C 92 3685 4937 4614 25 -35 247 C ATOM 2468 N THR C 93 14.713 5.256 4.520 1.00 35.29 N ANISOU 2468 N THR C 93 3744 4937 4727 147 -100 317 N ATOM 2469 CA THR C 93 13.867 6.428 4.283 1.00 34.93 C ANISOU 2469 CA THR C 93 3636 4920 4717 242 -95 353 C ATOM 2470 C THR C 93 13.904 6.871 2.815 1.00 42.93 C ANISOU 2470 C THR C 93 4672 5907 5733 245 -149 393 C ATOM 2471 O THR C 93 13.255 7.853 2.441 1.00 43.12 O ANISOU 2471 O THR C 93 4652 5945 5787 323 -155 431 O ATOM 2472 CB THR C 93 14.251 7.631 5.175 1.00 38.45 C ANISOU 2472 CB THR C 93 4108 5306 5195 342 -31 310 C ATOM 2473 OG1 THR C 93 15.496 8.184 4.732 1.00 45.52 O ANISOU 2473 OG1 THR C 93 5108 6095 6095 347 -33 279 O ATOM 2474 CG2 THR C 93 14.358 7.225 6.637 1.00 44.11 C ANISOU 2474 CG2 THR C 93 4818 6039 5901 333 23 265 C ATOM 2475 N SER C 94 14.664 6.153 1.989 1.00 40.37 N ANISOU 2475 N SER C 94 4420 5542 5376 163 -186 386 N ATOM 2476 CA SER C 94 14.771 6.487 0.564 1.00 38.14 C ANISOU 2476 CA SER C 94 4170 5235 5086 152 -237 422 C ATOM 2477 C SER C 94 14.618 5.254 -0.316 1.00 41.39 C ANISOU 2477 C SER C 94 4596 5680 5448 43 -293 446 C ATOM 2478 O SER C 94 15.566 4.496 -0.513 1.00 40.28 O ANISOU 2478 O SER C 94 4538 5489 5277 -19 -293 410 O ATOM 2479 CB SER C 94 16.097 7.180 0.252 1.00 44.17 C ANISOU 2479 CB SER C 94 5035 5891 5857 176 -218 383 C ATOM 2480 OG SER C 94 16.176 7.506 -1.130 1.00 42.79 O ANISOU 2480 OG SER C 94 4894 5697 5669 161 -266 420 O ATOM 2481 N ARG C 95 13.422 5.065 -0.857 1.00 39.76 N ANISOU 2481 N ARG C 95 4313 5561 5233 20 -342 510 N ATOM 2482 CA ARG C 95 13.130 3.861 -1.621 1.00 35.76 C ANISOU 2482 CA ARG C 95 3821 5093 4672 -95 -400 536 C ATOM 2483 C ARG C 95 14.082 3.666 -2.792 1.00 39.56 C ANISOU 2483 C ARG C 95 4415 5499 5119 -142 -427 521 C ATOM 2484 O ARG C 95 14.436 2.537 -3.125 1.00 39.38 O ANISOU 2484 O ARG C 95 4454 5461 5047 -233 -446 504 O ATOM 2485 CB ARG C 95 11.675 3.875 -2.096 1.00 44.97 C ANISOU 2485 CB ARG C 95 4880 6371 5836 -110 -456 617 C ATOM 2486 CG ARG C 95 10.703 3.671 -0.951 1.00 52.50 C ANISOU 2486 CG ARG C 95 5721 7418 6808 -94 -430 632 C ATOM 2487 CD ARG C 95 9.298 4.107 -1.295 1.00 56.77 C ANISOU 2487 CD ARG C 95 6131 8073 7365 -66 -470 716 C ATOM 2488 NE ARG C 95 8.381 3.812 -0.200 1.00 60.90 N ANISOU 2488 NE ARG C 95 6543 8698 7900 -59 -440 731 N ATOM 2489 CZ ARG C 95 7.253 4.473 0.028 1.00 62.63 C ANISOU 2489 CZ ARG C 95 6628 9015 8153 16 -435 788 C ATOM 2490 NH1 ARG C 95 6.902 5.481 -0.759 1.00 65.53 N ANISOU 2490 NH1 ARG C 95 6962 9386 8551 95 -464 836 N ATOM 2491 NH2 ARG C 95 6.481 4.130 1.050 1.00 60.22 N ANISOU 2491 NH2 ARG C 95 6222 8806 7852 16 -401 799 N ATOM 2492 N VAL C 96 14.505 4.757 -3.421 1.00 41.25 N ANISOU 2492 N VAL C 96 4658 5662 5353 -81 -426 528 N ATOM 2493 CA VAL C 96 15.404 4.613 -4.557 1.00 38.70 C ANISOU 2493 CA VAL C 96 4438 5274 4992 -127 -447 516 C ATOM 2494 C VAL C 96 16.734 3.965 -4.151 1.00 38.67 C ANISOU 2494 C VAL C 96 4524 5198 4973 -154 -400 444 C ATOM 2495 O VAL C 96 17.365 3.278 -4.949 1.00 34.71 O ANISOU 2495 O VAL C 96 4103 4662 4425 -217 -414 429 O ATOM 2496 CB VAL C 96 15.663 5.938 -5.280 1.00 39.77 C ANISOU 2496 CB VAL C 96 4594 5366 5151 -62 -453 538 C ATOM 2497 CG1 VAL C 96 16.522 6.864 -4.423 1.00 39.44 C ANISOU 2497 CG1 VAL C 96 4576 5254 5154 22 -389 491 C ATOM 2498 CG2 VAL C 96 16.333 5.672 -6.616 1.00 41.23 C ANISOU 2498 CG2 VAL C 96 4872 5509 5283 -126 -485 540 C ATOM 2499 N THR C 97 17.166 4.173 -2.913 1.00 35.97 N ANISOU 2499 N THR C 97 4167 4833 4665 -104 -344 402 N ATOM 2500 CA THR C 97 18.421 3.547 -2.493 1.00 35.56 C ANISOU 2500 CA THR C 97 4191 4721 4601 -127 -304 341 C ATOM 2501 C THR C 97 18.285 2.024 -2.428 1.00 38.13 C ANISOU 2501 C THR C 97 4540 5068 4882 -212 -321 332 C ATOM 2502 O THR C 97 19.247 1.298 -2.684 1.00 34.62 O ANISOU 2502 O THR C 97 4175 4571 4407 -247 -309 296 O ATOM 2503 CB THR C 97 18.992 4.129 -1.164 1.00 33.83 C ANISOU 2503 CB THR C 97 3959 4471 4425 -62 -245 299 C ATOM 2504 OG1 THR C 97 18.137 3.801 -0.057 1.00 36.81 O ANISOU 2504 OG1 THR C 97 4264 4906 4816 -56 -233 302 O ATOM 2505 CG2 THR C 97 19.161 5.659 -1.267 1.00 33.37 C ANISOU 2505 CG2 THR C 97 3896 4377 4404 18 -230 307 C ATOM 2506 N TYR C 98 17.091 1.543 -2.098 1.00 32.09 N ANISOU 2506 N TYR C 98 3706 4378 4110 -245 -349 366 N ATOM 2507 CA TYR C 98 16.847 0.104 -2.090 1.00 35.17 C ANISOU 2507 CA TYR C 98 4125 4786 4451 -337 -375 364 C ATOM 2508 C TYR C 98 16.713 -0.435 -3.516 1.00 38.57 C ANISOU 2508 C TYR C 98 4616 5212 4826 -412 -429 389 C ATOM 2509 O TYR C 98 17.160 -1.544 -3.815 1.00 33.49 O ANISOU 2509 O TYR C 98 4057 4532 4134 -479 -437 364 O ATOM 2510 CB TYR C 98 15.604 -0.250 -1.268 1.00 31.62 C ANISOU 2510 CB TYR C 98 3581 4427 4008 -361 -388 396 C ATOM 2511 CG TYR C 98 15.298 -1.723 -1.300 1.00 38.03 C ANISOU 2511 CG TYR C 98 4430 5255 4764 -470 -421 400 C ATOM 2512 CD1 TYR C 98 16.015 -2.623 -0.510 1.00 36.29 C ANISOU 2512 CD1 TYR C 98 4270 4988 4531 -493 -391 353 C ATOM 2513 CD2 TYR C 98 14.317 -2.224 -2.142 1.00 42.20 C ANISOU 2513 CD2 TYR C 98 4942 5842 5249 -552 -487 453 C ATOM 2514 CE1 TYR C 98 15.744 -3.977 -0.552 1.00 37.04 C ANISOU 2514 CE1 TYR C 98 4414 5087 4573 -593 -423 358 C ATOM 2515 CE2 TYR C 98 14.042 -3.572 -2.190 1.00 46.33 C ANISOU 2515 CE2 TYR C 98 5515 6374 5716 -661 -520 456 C ATOM 2516 CZ TYR C 98 14.756 -4.444 -1.395 1.00 40.63 C ANISOU 2516 CZ TYR C 98 4858 5595 4982 -679 -487 407 C ATOM 2517 OH TYR C 98 14.485 -5.786 -1.449 1.00 40.10 O ANISOU 2517 OH TYR C 98 4854 5525 4857 -787 -523 411 O ATOM 2518 N LYS C 99 16.105 0.361 -4.394 1.00 36.64 N ANISOU 2518 N LYS C 99 4335 5001 4585 -398 -467 437 N ATOM 2519 CA LYS C 99 15.962 -0.019 -5.793 1.00 34.95 C ANISOU 2519 CA LYS C 99 4181 4784 4313 -470 -522 464 C ATOM 2520 C LYS C 99 17.316 -0.217 -6.464 1.00 38.74 C ANISOU 2520 C LYS C 99 4782 5175 4765 -474 -494 415 C ATOM 2521 O LYS C 99 17.444 -1.021 -7.393 1.00 35.09 O ANISOU 2521 O LYS C 99 4402 4692 4238 -549 -523 413 O ATOM 2522 CB LYS C 99 15.173 1.050 -6.562 1.00 43.87 C ANISOU 2522 CB LYS C 99 5247 5962 5459 -440 -565 528 C ATOM 2523 CG LYS C 99 13.678 1.029 -6.321 1.00 54.38 C ANISOU 2523 CG LYS C 99 6462 7402 6799 -459 -612 593 C ATOM 2524 CD LYS C 99 12.968 1.923 -7.323 1.00 62.33 C ANISOU 2524 CD LYS C 99 7422 8451 7810 -440 -667 663 C ATOM 2525 CE LYS C 99 11.460 1.878 -7.136 1.00 78.93 C ANISOU 2525 CE LYS C 99 9396 10675 9921 -459 -717 736 C ATOM 2526 NZ LYS C 99 11.059 2.301 -5.765 1.00 83.98 N ANISOU 2526 NZ LYS C 99 9932 11354 10623 -376 -664 729 N ATOM 2527 N ASN C 100 18.317 0.530 -6.001 1.00 38.94 N ANISOU 2527 N ASN C 100 4817 5147 4833 -395 -437 377 N ATOM 2528 CA ASN C 100 19.685 0.439 -6.529 1.00 37.27 C ANISOU 2528 CA ASN C 100 4702 4859 4600 -389 -401 333 C ATOM 2529 C ASN C 100 20.554 -0.675 -5.927 1.00 33.39 C ANISOU 2529 C ASN C 100 4272 4324 4093 -406 -361 278 C ATOM 2530 O ASN C 100 21.663 -0.933 -6.401 1.00 32.48 O ANISOU 2530 O ASN C 100 4234 4152 3954 -403 -330 243 O ATOM 2531 CB ASN C 100 20.404 1.787 -6.391 1.00 33.76 C ANISOU 2531 CB ASN C 100 4241 4382 4204 -307 -363 324 C ATOM 2532 CG ASN C 100 19.888 2.812 -7.374 1.00 39.30 C ANISOU 2532 CG ASN C 100 4926 5101 4906 -294 -402 375 C ATOM 2533 OD1 ASN C 100 19.960 4.017 -7.142 1.00 44.12 O ANISOU 2533 OD1 ASN C 100 5501 5700 5561 -227 -388 387 O ATOM 2534 ND2 ASN C 100 19.350 2.329 -8.481 1.00 36.13 N ANISOU 2534 ND2 ASN C 100 4556 4723 4449 -362 -454 408 N ATOM 2535 N VAL C 101 20.051 -1.336 -4.895 1.00 32.47 N ANISOU 2535 N VAL C 101 4116 4233 3986 -422 -361 273 N ATOM 2536 CA VAL C 101 20.797 -2.431 -4.275 1.00 31.10 C ANISOU 2536 CA VAL C 101 4002 4017 3798 -437 -330 228 C ATOM 2537 C VAL C 101 21.206 -3.512 -5.292 1.00 37.41 C ANISOU 2537 C VAL C 101 4916 4772 4529 -499 -343 211 C ATOM 2538 O VAL C 101 22.349 -3.952 -5.316 1.00 37.22 O ANISOU 2538 O VAL C 101 4960 4687 4494 -476 -302 168 O ATOM 2539 CB VAL C 101 20.027 -3.021 -3.074 1.00 28.68 C ANISOU 2539 CB VAL C 101 3641 3752 3505 -460 -338 235 C ATOM 2540 CG1 VAL C 101 20.509 -4.435 -2.762 1.00 37.16 C ANISOU 2540 CG1 VAL C 101 4797 4781 4541 -506 -331 202 C ATOM 2541 CG2 VAL C 101 20.157 -2.091 -1.847 1.00 30.26 C ANISOU 2541 CG2 VAL C 101 3760 3967 3770 -384 -298 225 C ATOM 2542 N PRO C 102 20.278 -3.928 -6.162 1.00 36.11 N ANISOU 2542 N PRO C 102 4772 4637 4313 -575 -401 245 N ATOM 2543 CA PRO C 102 20.679 -4.934 -7.157 1.00 39.84 C ANISOU 2543 CA PRO C 102 5368 5058 4711 -634 -410 224 C ATOM 2544 C PRO C 102 21.843 -4.473 -8.054 1.00 37.89 C ANISOU 2544 C PRO C 102 5184 4760 4451 -591 -370 196 C ATOM 2545 O PRO C 102 22.671 -5.308 -8.434 1.00 39.14 O ANISOU 2545 O PRO C 102 5444 4858 4567 -599 -341 156 O ATOM 2546 CB PRO C 102 19.404 -5.132 -7.988 1.00 44.95 C ANISOU 2546 CB PRO C 102 6012 5759 5308 -725 -486 276 C ATOM 2547 CG PRO C 102 18.292 -4.750 -7.069 1.00 47.37 C ANISOU 2547 CG PRO C 102 6192 6145 5660 -723 -513 318 C ATOM 2548 CD PRO C 102 18.839 -3.624 -6.222 1.00 42.21 C ANISOU 2548 CD PRO C 102 5460 5490 5087 -615 -459 304 C ATOM 2549 N ASN C 103 21.897 -3.188 -8.398 1.00 36.00 N ANISOU 2549 N ASN C 103 4890 4543 4245 -547 -367 219 N ATOM 2550 CA ASN C 103 23.004 -2.661 -9.206 1.00 34.17 C ANISOU 2550 CA ASN C 103 4710 4271 4002 -511 -328 198 C ATOM 2551 C ASN C 103 24.338 -2.739 -8.457 1.00 40.47 C ANISOU 2551 C ASN C 103 5517 5025 4835 -444 -256 149 C ATOM 2552 O ASN C 103 25.368 -3.107 -9.029 1.00 37.88 O ANISOU 2552 O ASN C 103 5264 4655 4475 -433 -215 117 O ATOM 2553 CB ASN C 103 22.754 -1.210 -9.631 1.00 41.31 C ANISOU 2553 CB ASN C 103 5553 5204 4937 -480 -343 238 C ATOM 2554 CG ASN C 103 21.548 -1.056 -10.527 1.00 51.10 C ANISOU 2554 CG ASN C 103 6784 6490 6141 -540 -416 293 C ATOM 2555 OD1 ASN C 103 20.843 -0.048 -10.455 1.00 55.29 O ANISOU 2555 OD1 ASN C 103 7235 7063 6710 -514 -446 338 O ATOM 2556 ND2 ASN C 103 21.303 -2.051 -11.379 1.00 47.35 N ANISOU 2556 ND2 ASN C 103 6395 6008 5589 -620 -447 291 N ATOM 2557 N TRP C 104 24.323 -2.371 -7.181 1.00 35.86 N ANISOU 2557 N TRP C 104 4855 4456 4314 -399 -240 147 N ATOM 2558 CA TRP C 104 25.517 -2.495 -6.354 1.00 32.97 C ANISOU 2558 CA TRP C 104 4490 4056 3981 -344 -182 107 C ATOM 2559 C TRP C 104 25.976 -3.952 -6.261 1.00 35.44 C ANISOU 2559 C TRP C 104 4882 4328 4255 -363 -166 72 C ATOM 2560 O TRP C 104 27.162 -4.260 -6.414 1.00 37.29 O ANISOU 2560 O TRP C 104 5163 4524 4482 -327 -117 40 O ATOM 2561 CB TRP C 104 25.281 -1.901 -4.961 1.00 38.34 C ANISOU 2561 CB TRP C 104 5079 4761 4727 -304 -175 112 C ATOM 2562 CG TRP C 104 25.202 -0.426 -5.030 1.00 32.41 C ANISOU 2562 CG TRP C 104 4271 4029 4015 -266 -175 134 C ATOM 2563 CD1 TRP C 104 24.105 0.359 -4.802 1.00 32.38 C ANISOU 2563 CD1 TRP C 104 4200 4066 4039 -260 -207 170 C ATOM 2564 CD2 TRP C 104 26.252 0.454 -5.428 1.00 37.89 C ANISOU 2564 CD2 TRP C 104 4976 4699 4721 -230 -141 126 C ATOM 2565 NE1 TRP C 104 24.426 1.683 -4.997 1.00 33.57 N ANISOU 2565 NE1 TRP C 104 4328 4208 4219 -217 -196 181 N ATOM 2566 CE2 TRP C 104 25.736 1.765 -5.391 1.00 34.60 C ANISOU 2566 CE2 TRP C 104 4507 4300 4338 -206 -157 156 C ATOM 2567 CE3 TRP C 104 27.591 0.263 -5.795 1.00 44.26 C ANISOU 2567 CE3 TRP C 104 5830 5474 5513 -216 -96 98 C ATOM 2568 CZ2 TRP C 104 26.512 2.879 -5.713 1.00 41.93 C ANISOU 2568 CZ2 TRP C 104 5439 5209 5283 -177 -135 158 C ATOM 2569 CZ3 TRP C 104 28.357 1.369 -6.114 1.00 46.72 C ANISOU 2569 CZ3 TRP C 104 6133 5779 5841 -190 -73 103 C ATOM 2570 CH2 TRP C 104 27.814 2.662 -6.071 1.00 42.09 C ANISOU 2570 CH2 TRP C 104 5503 5203 5284 -176 -95 133 C ATOM 2571 N HIS C 105 25.031 -4.853 -6.030 1.00 35.71 N ANISOU 2571 N HIS C 105 4934 4370 4264 -419 -206 82 N ATOM 2572 CA HIS C 105 25.360 -6.265 -5.943 1.00 32.42 C ANISOU 2572 CA HIS C 105 4607 3905 3806 -441 -197 52 C ATOM 2573 C HIS C 105 25.982 -6.753 -7.247 1.00 34.62 C ANISOU 2573 C HIS C 105 4995 4137 4021 -453 -179 29 C ATOM 2574 O HIS C 105 26.971 -7.473 -7.243 1.00 34.58 O ANISOU 2574 O HIS C 105 5057 4081 4002 -418 -134 -7 O ATOM 2575 CB HIS C 105 24.118 -7.087 -5.601 1.00 33.09 C ANISOU 2575 CB HIS C 105 4698 4009 3864 -519 -252 74 C ATOM 2576 CG HIS C 105 24.390 -8.549 -5.453 1.00 41.50 C ANISOU 2576 CG HIS C 105 5867 5016 4887 -547 -248 45 C ATOM 2577 ND1 HIS C 105 24.332 -9.427 -6.515 1.00 45.56 N ANISOU 2577 ND1 HIS C 105 6501 5484 5323 -602 -264 33 N ATOM 2578 CD2 HIS C 105 24.736 -9.286 -4.372 1.00 42.90 C ANISOU 2578 CD2 HIS C 105 6055 5164 5083 -528 -231 27 C ATOM 2579 CE1 HIS C 105 24.625 -10.643 -6.089 1.00 47.99 C ANISOU 2579 CE1 HIS C 105 6894 5734 5607 -611 -255 7 C ATOM 2580 NE2 HIS C 105 24.877 -10.584 -4.795 1.00 44.71 N ANISOU 2580 NE2 HIS C 105 6410 5328 5250 -566 -237 6 N ATOM 2581 N ARG C 106 25.399 -6.352 -8.371 1.00 38.68 N ANISOU 2581 N ARG C 106 5528 4672 4495 -500 -212 53 N ATOM 2582 CA ARG C 106 25.940 -6.722 -9.674 1.00 38.43 C ANISOU 2582 CA ARG C 106 5605 4603 4396 -516 -194 32 C ATOM 2583 C ARG C 106 27.372 -6.218 -9.874 1.00 37.16 C ANISOU 2583 C ARG C 106 5444 4421 4254 -437 -120 4 C ATOM 2584 O ARG C 106 28.242 -6.975 -10.310 1.00 39.97 O ANISOU 2584 O ARG C 106 5887 4729 4571 -415 -74 -34 O ATOM 2585 CB ARG C 106 25.039 -6.190 -10.790 1.00 38.82 C ANISOU 2585 CB ARG C 106 5660 4688 4402 -582 -248 71 C ATOM 2586 CG ARG C 106 25.619 -6.350 -12.183 1.00 51.20 C ANISOU 2586 CG ARG C 106 7335 6224 5897 -599 -226 52 C ATOM 2587 CD ARG C 106 24.652 -5.825 -13.233 1.00 64.00 C ANISOU 2587 CD ARG C 106 8959 7884 7473 -672 -291 97 C ATOM 2588 NE ARG C 106 24.058 -4.550 -12.838 1.00 69.93 N ANISOU 2588 NE ARG C 106 9583 8697 8291 -650 -322 147 N ATOM 2589 CZ ARG C 106 24.644 -3.369 -13.007 1.00 72.08 C ANISOU 2589 CZ ARG C 106 9806 8980 8602 -595 -293 156 C ATOM 2590 NH1 ARG C 106 25.846 -3.300 -13.560 1.00 79.12 N ANISOU 2590 NH1 ARG C 106 10754 9836 9470 -561 -232 123 N ATOM 2591 NH2 ARG C 106 24.031 -2.258 -12.622 1.00 68.07 N ANISOU 2591 NH2 ARG C 106 9195 8518 8152 -573 -325 200 N ATOM 2592 N ASP C 107 27.606 -4.941 -9.572 1.00 40.09 N ANISOU 2592 N ASP C 107 5719 4829 4683 -395 -110 24 N ATOM 2593 CA ASP C 107 28.918 -4.325 -9.770 1.00 46.76 C ANISOU 2593 CA ASP C 107 6553 5668 5548 -333 -46 7 C ATOM 2594 C ASP C 107 29.934 -5.033 -8.891 1.00 44.57 C ANISOU 2594 C ASP C 107 6277 5361 5296 -275 6 -28 C ATOM 2595 O ASP C 107 31.086 -5.236 -9.282 1.00 40.74 O ANISOU 2595 O ASP C 107 5827 4857 4797 -232 64 -54 O ATOM 2596 CB ASP C 107 28.896 -2.830 -9.412 1.00 47.28 C ANISOU 2596 CB ASP C 107 6518 5773 5673 -308 -53 37 C ATOM 2597 CG ASP C 107 28.126 -1.986 -10.420 1.00 55.35 C ANISOU 2597 CG ASP C 107 7539 6820 6670 -350 -96 76 C ATOM 2598 OD1 ASP C 107 27.797 -2.492 -11.513 1.00 49.23 O ANISOU 2598 OD1 ASP C 107 6842 6036 5826 -401 -116 78 O ATOM 2599 OD2 ASP C 107 27.852 -0.804 -10.115 1.00 61.71 O ANISOU 2599 OD2 ASP C 107 8272 7652 7523 -332 -113 106 O ATOM 2600 N LEU C 108 29.479 -5.406 -7.698 1.00 38.38 N ANISOU 2600 N LEU C 108 5453 4579 4551 -273 -17 -26 N ATOM 2601 CA LEU C 108 30.304 -6.071 -6.698 1.00 38.79 C ANISOU 2601 CA LEU C 108 5500 4606 4633 -221 20 -50 C ATOM 2602 C LEU C 108 30.734 -7.467 -7.133 1.00 40.28 C ANISOU 2602 C LEU C 108 5800 4737 4767 -215 44 -83 C ATOM 2603 O LEU C 108 31.922 -7.797 -7.116 1.00 44.55 O ANISOU 2603 O LEU C 108 6359 5255 5312 -152 101 -107 O ATOM 2604 CB LEU C 108 29.537 -6.154 -5.375 1.00 40.18 C ANISOU 2604 CB LEU C 108 5616 4800 4852 -234 -17 -36 C ATOM 2605 CG LEU C 108 30.251 -6.863 -4.231 1.00 44.97 C ANISOU 2605 CG LEU C 108 6217 5383 5489 -189 9 -55 C ATOM 2606 CD1 LEU C 108 31.652 -6.299 -4.059 1.00 41.24 C ANISOU 2606 CD1 LEU C 108 5702 4917 5051 -119 64 -65 C ATOM 2607 CD2 LEU C 108 29.438 -6.707 -2.953 1.00 55.34 C ANISOU 2607 CD2 LEU C 108 7462 6725 6842 -209 -26 -37 C ATOM 2608 N VAL C 109 29.767 -8.290 -7.524 1.00 41.57 N ANISOU 2608 N VAL C 109 6041 4876 4878 -281 0 -83 N ATOM 2609 CA VAL C 109 30.064 -9.685 -7.829 1.00 39.46 C ANISOU 2609 CA VAL C 109 5897 4541 4556 -281 18 -116 C ATOM 2610 C VAL C 109 30.678 -9.833 -9.220 1.00 40.95 C ANISOU 2610 C VAL C 109 6176 4702 4681 -271 59 -140 C ATOM 2611 O VAL C 109 31.221 -10.879 -9.544 1.00 43.51 O ANISOU 2611 O VAL C 109 6606 4965 4961 -245 95 -175 O ATOM 2612 CB VAL C 109 28.821 -10.578 -7.716 1.00 45.47 C ANISOU 2612 CB VAL C 109 6720 5281 5276 -368 -47 -106 C ATOM 2613 CG1 VAL C 109 28.242 -10.497 -6.312 1.00 42.97 C ANISOU 2613 CG1 VAL C 109 6315 4995 5016 -377 -80 -83 C ATOM 2614 CG2 VAL C 109 27.794 -10.180 -8.753 1.00 46.29 C ANISOU 2614 CG2 VAL C 109 6842 5415 5330 -453 -97 -82 C ATOM 2615 N ARG C 110 30.593 -8.785 -10.036 1.00 40.35 N ANISOU 2615 N ARG C 110 6065 4669 4597 -289 57 -122 N ATOM 2616 CA ARG C 110 31.294 -8.783 -11.308 1.00 47.53 C ANISOU 2616 CA ARG C 110 7048 5563 5448 -275 106 -144 C ATOM 2617 C ARG C 110 32.798 -8.844 -11.070 1.00 48.53 C ANISOU 2617 C ARG C 110 7155 5682 5604 -175 190 -170 C ATOM 2618 O ARG C 110 33.532 -9.485 -11.821 1.00 48.93 O ANISOU 2618 O ARG C 110 7294 5696 5602 -141 246 -203 O ATOM 2619 CB ARG C 110 30.948 -7.546 -12.135 1.00 47.88 C ANISOU 2619 CB ARG C 110 7049 5659 5484 -315 84 -113 C ATOM 2620 CG ARG C 110 31.829 -7.407 -13.368 1.00 48.68 C ANISOU 2620 CG ARG C 110 7212 5754 5529 -296 144 -133 C ATOM 2621 CD ARG C 110 31.729 -6.030 -14.006 1.00 60.49 C ANISOU 2621 CD ARG C 110 8649 7304 7031 -321 130 -97 C ATOM 2622 NE ARG C 110 32.914 -5.752 -14.812 1.00 70.01 N ANISOU 2622 NE ARG C 110 9878 8517 8208 -281 206 -115 N ATOM 2623 CZ ARG C 110 33.935 -5.001 -14.409 1.00 74.05 C ANISOU 2623 CZ ARG C 110 10302 9062 8772 -222 256 -109 C ATOM 2624 NH1 ARG C 110 33.914 -4.427 -13.212 1.00 67.15 N ANISOU 2624 NH1 ARG C 110 9321 8211 7983 -196 236 -89 N ATOM 2625 NH2 ARG C 110 34.974 -4.811 -15.213 1.00 81.72 N ANISOU 2625 NH2 ARG C 110 11295 10047 9709 -194 326 -123 N ATOM 2626 N VAL C 111 33.251 -8.185 -10.010 1.00 43.78 N ANISOU 2626 N VAL C 111 6435 5117 5082 -129 199 -153 N ATOM 2627 CA VAL C 111 34.674 -8.129 -9.692 1.00 43.62 C ANISOU 2627 CA VAL C 111 6372 5106 5095 -39 270 -167 C ATOM 2628 C VAL C 111 35.093 -9.174 -8.654 1.00 46.67 C ANISOU 2628 C VAL C 111 6770 5454 5511 17 284 -183 C ATOM 2629 O VAL C 111 36.221 -9.666 -8.684 1.00 49.15 O ANISOU 2629 O VAL C 111 7098 5753 5825 95 347 -203 O ATOM 2630 CB VAL C 111 35.072 -6.716 -9.175 1.00 46.34 C ANISOU 2630 CB VAL C 111 6585 5517 5507 -26 272 -136 C ATOM 2631 CG1 VAL C 111 36.577 -6.627 -8.937 1.00 49.84 C ANISOU 2631 CG1 VAL C 111 6977 5981 5979 55 344 -143 C ATOM 2632 CG2 VAL C 111 34.624 -5.635 -10.158 1.00 43.38 C ANISOU 2632 CG2 VAL C 111 6202 5174 5107 -80 253 -114 C ATOM 2633 N CYS C 112 34.186 -9.516 -7.742 1.00 37.61 N ANISOU 2633 N CYS C 112 5614 4292 4385 -22 225 -172 N ATOM 2634 CA CYS C 112 34.559 -10.288 -6.562 1.00 36.50 C ANISOU 2634 CA CYS C 112 5463 4125 4282 26 229 -176 C ATOM 2635 C CYS C 112 33.943 -11.671 -6.526 1.00 51.42 C ANISOU 2635 C CYS C 112 7472 5940 6124 -2 203 -195 C ATOM 2636 O CYS C 112 34.357 -12.521 -5.732 1.00 49.30 O ANISOU 2636 O CYS C 112 7226 5632 5873 45 212 -202 O ATOM 2637 CB CYS C 112 34.195 -9.523 -5.283 1.00 34.02 C ANISOU 2637 CB CYS C 112 5031 3857 4037 11 190 -146 C ATOM 2638 SG CYS C 112 35.066 -7.975 -5.154 1.00 43.44 S ANISOU 2638 SG CYS C 112 6097 5124 5285 45 221 -127 S ATOM 2639 N GLU C 113 32.954 -11.896 -7.384 1.00 58.85 N ANISOU 2639 N GLU C 113 8496 6862 7004 -82 165 -198 N ATOM 2640 CA GLU C 113 32.216 -13.157 -7.386 1.00 64.36 C ANISOU 2640 CA GLU C 113 9315 7491 7649 -134 129 -211 C ATOM 2641 C GLU C 113 31.409 -13.354 -6.101 1.00 65.85 C ANISOU 2641 C GLU C 113 9454 7690 7876 -176 70 -185 C ATOM 2642 O GLU C 113 30.765 -12.418 -5.608 1.00 66.99 O ANISOU 2642 O GLU C 113 9489 7902 8062 -213 34 -154 O ATOM 2643 CB GLU C 113 33.159 -14.336 -7.591 1.00 74.53 C ANISOU 2643 CB GLU C 113 10717 8697 8905 -58 184 -249 C ATOM 2644 CG GLU C 113 33.798 -14.421 -8.964 1.00 83.77 C ANISOU 2644 CG GLU C 113 11971 9844 10014 -27 244 -282 C ATOM 2645 CD GLU C 113 34.816 -15.541 -9.041 1.00 94.69 C ANISOU 2645 CD GLU C 113 13454 11150 11375 71 310 -319 C ATOM 2646 OE1 GLU C 113 35.203 -16.056 -7.971 1.00 98.67 O ANISOU 2646 OE1 GLU C 113 13934 11631 11927 127 311 -313 O ATOM 2647 OE2 GLU C 113 35.224 -15.907 -10.164 1.00 97.67 O ANISOU 2647 OE2 GLU C 113 13935 11489 11686 94 361 -353 O ATOM 2648 N ASN C 114 31.486 -14.568 -5.558 1.00 56.60 N ANISOU 2648 N ASN C 114 8366 6450 6690 -165 65 -198 N ATOM 2649 CA ASN C 114 30.582 -15.030 -4.512 1.00 63.33 C ANISOU 2649 CA ASN C 114 9210 7300 7555 -227 6 -176 C ATOM 2650 C ASN C 114 31.006 -14.765 -3.064 1.00 54.74 C ANISOU 2650 C ASN C 114 8015 6242 6542 -176 10 -157 C ATOM 2651 O ASN C 114 30.682 -15.549 -2.165 1.00 54.30 O ANISOU 2651 O ASN C 114 7989 6155 6488 -199 -20 -148 O ATOM 2652 CB ASN C 114 30.345 -16.542 -4.687 1.00 73.15 C ANISOU 2652 CB ASN C 114 10618 8443 8731 -259 -11 -196 C ATOM 2653 CG ASN C 114 29.322 -17.095 -3.715 1.00 81.28 C ANISOU 2653 CG ASN C 114 11652 9470 9760 -343 -77 -169 C ATOM 2654 OD1 ASN C 114 28.306 -16.462 -3.422 1.00 86.77 O ANISOU 2654 OD1 ASN C 114 12260 10238 10469 -420 -125 -137 O ATOM 2655 ND2 ASN C 114 29.594 -18.286 -3.203 1.00 77.64 N ANISOU 2655 ND2 ASN C 114 11292 8925 9281 -326 -78 -180 N ATOM 2656 N ILE C 115 31.704 -13.662 -2.813 1.00 45.92 N ANISOU 2656 N ILE C 115 6778 5186 5483 -117 43 -149 N ATOM 2657 CA ILE C 115 32.117 -13.350 -1.447 1.00 36.84 C ANISOU 2657 CA ILE C 115 5530 4068 4399 -77 43 -132 C ATOM 2658 C ILE C 115 30.901 -13.167 -0.532 1.00 34.32 C ANISOU 2658 C ILE C 115 5160 3787 4094 -157 -15 -105 C ATOM 2659 O ILE C 115 29.811 -12.856 -1.005 1.00 39.96 O ANISOU 2659 O ILE C 115 5871 4529 4783 -233 -51 -93 O ATOM 2660 CB ILE C 115 32.989 -12.069 -1.395 1.00 32.69 C ANISOU 2660 CB ILE C 115 4888 3607 3927 -18 82 -126 C ATOM 2661 CG1 ILE C 115 32.228 -10.871 -1.959 1.00 35.27 C ANISOU 2661 CG1 ILE C 115 5154 3992 4255 -72 63 -112 C ATOM 2662 CG2 ILE C 115 34.288 -12.276 -2.169 1.00 34.13 C ANISOU 2662 CG2 ILE C 115 5103 3764 4099 66 147 -147 C ATOM 2663 CD1 ILE C 115 32.979 -9.575 -1.854 1.00 32.15 C ANISOU 2663 CD1 ILE C 115 4654 3653 3908 -29 93 -104 C ATOM 2664 N PRO C 116 31.082 -13.350 0.788 1.00 32.48 N ANISOU 2664 N PRO C 116 4883 3560 3898 -140 -24 -92 N ATOM 2665 CA PRO C 116 30.000 -13.108 1.751 1.00 29.55 C ANISOU 2665 CA PRO C 116 4453 3235 3541 -209 -70 -67 C ATOM 2666 C PRO C 116 29.603 -11.636 1.808 1.00 37.93 C ANISOU 2666 C PRO C 116 5395 4377 4639 -219 -70 -53 C ATOM 2667 O PRO C 116 30.471 -10.759 1.861 1.00 34.74 O ANISOU 2667 O PRO C 116 4926 3998 4274 -159 -36 -57 O ATOM 2668 CB PRO C 116 30.613 -13.534 3.099 1.00 28.58 C ANISOU 2668 CB PRO C 116 4309 3098 3450 -170 -66 -59 C ATOM 2669 CG PRO C 116 31.788 -14.342 2.759 1.00 41.51 C ANISOU 2669 CG PRO C 116 6022 4668 5080 -93 -32 -76 C ATOM 2670 CD PRO C 116 32.283 -13.909 1.433 1.00 36.91 C ANISOU 2670 CD PRO C 116 5455 4084 4484 -57 7 -97 C ATOM 2671 N ILE C 117 28.298 -11.380 1.823 1.00 31.17 N ANISOU 2671 N ILE C 117 4512 3563 3770 -294 -109 -34 N ATOM 2672 CA ILE C 117 27.772 -10.019 1.729 1.00 26.75 C ANISOU 2672 CA ILE C 117 3852 3073 3240 -300 -112 -20 C ATOM 2673 C ILE C 117 26.600 -9.856 2.694 1.00 32.58 C ANISOU 2673 C ILE C 117 4526 3864 3987 -354 -145 4 C ATOM 2674 O ILE C 117 25.742 -10.734 2.787 1.00 32.14 O ANISOU 2674 O ILE C 117 4514 3804 3895 -423 -181 17 O ATOM 2675 CB ILE C 117 27.295 -9.735 0.307 1.00 35.66 C ANISOU 2675 CB ILE C 117 5010 4207 4334 -331 -124 -18 C ATOM 2676 CG1 ILE C 117 28.440 -9.920 -0.692 1.00 33.29 C ANISOU 2676 CG1 ILE C 117 4776 3857 4015 -279 -84 -44 C ATOM 2677 CG2 ILE C 117 26.720 -8.337 0.201 1.00 35.78 C ANISOU 2677 CG2 ILE C 117 4927 4288 4380 -331 -130 2 C ATOM 2678 CD1 ILE C 117 28.018 -9.725 -2.111 1.00 37.78 C ANISOU 2678 CD1 ILE C 117 5389 4427 4541 -315 -96 -43 C ATOM 2679 N VAL C 118 26.582 -8.756 3.443 1.00 27.82 N ANISOU 2679 N VAL C 118 3828 3313 3432 -325 -131 11 N ATOM 2680 CA VAL C 118 25.452 -8.451 4.302 1.00 24.99 C ANISOU 2680 CA VAL C 118 3400 3013 3082 -366 -152 32 C ATOM 2681 C VAL C 118 24.745 -7.228 3.715 1.00 31.61 C ANISOU 2681 C VAL C 118 4169 3905 3937 -363 -155 47 C ATOM 2682 O VAL C 118 25.396 -6.308 3.214 1.00 30.84 O ANISOU 2682 O VAL C 118 4053 3800 3863 -312 -132 37 O ATOM 2683 CB VAL C 118 25.877 -8.098 5.729 1.00 34.72 C ANISOU 2683 CB VAL C 118 4580 4262 4350 -334 -131 27 C ATOM 2684 CG1 VAL C 118 24.652 -7.750 6.541 1.00 36.25 C ANISOU 2684 CG1 VAL C 118 4703 4522 4548 -374 -144 47 C ATOM 2685 CG2 VAL C 118 26.621 -9.274 6.380 1.00 36.49 C ANISOU 2685 CG2 VAL C 118 4869 4434 4561 -332 -131 19 C ATOM 2686 N LEU C 119 23.421 -7.240 3.757 1.00 31.98 N ANISOU 2686 N LEU C 119 4177 4005 3970 -417 -186 74 N ATOM 2687 CA LEU C 119 22.624 -6.118 3.284 1.00 29.26 C ANISOU 2687 CA LEU C 119 3760 3716 3643 -409 -194 96 C ATOM 2688 C LEU C 119 22.122 -5.379 4.513 1.00 28.07 C ANISOU 2688 C LEU C 119 3518 3619 3527 -385 -177 103 C ATOM 2689 O LEU C 119 21.557 -5.984 5.429 1.00 32.46 O ANISOU 2689 O LEU C 119 4058 4204 4073 -424 -184 112 O ATOM 2690 CB LEU C 119 21.453 -6.626 2.427 1.00 32.33 C ANISOU 2690 CB LEU C 119 4158 4137 3989 -484 -243 128 C ATOM 2691 CG LEU C 119 20.443 -5.595 1.915 1.00 33.40 C ANISOU 2691 CG LEU C 119 4211 4341 4139 -481 -261 162 C ATOM 2692 CD1 LEU C 119 21.147 -4.557 1.063 1.00 33.49 C ANISOU 2692 CD1 LEU C 119 4227 4324 4172 -419 -243 152 C ATOM 2693 CD2 LEU C 119 19.332 -6.293 1.124 1.00 34.73 C ANISOU 2693 CD2 LEU C 119 4393 4545 4258 -571 -317 199 C ATOM 2694 N CYS C 120 22.345 -4.067 4.557 1.00 29.70 N ANISOU 2694 N CYS C 120 3674 3837 3774 -323 -151 97 N ATOM 2695 CA CYS C 120 21.976 -3.285 5.740 1.00 25.00 C ANISOU 2695 CA CYS C 120 3007 3283 3210 -291 -126 96 C ATOM 2696 C CYS C 120 21.060 -2.145 5.364 1.00 25.09 C ANISOU 2696 C CYS C 120 2949 3343 3243 -261 -128 119 C ATOM 2697 O CYS C 120 21.405 -1.343 4.513 1.00 30.49 O ANISOU 2697 O CYS C 120 3641 4003 3941 -225 -127 120 O ATOM 2698 CB CYS C 120 23.215 -2.696 6.424 1.00 28.10 C ANISOU 2698 CB CYS C 120 3413 3634 3631 -236 -88 63 C ATOM 2699 SG CYS C 120 24.253 -3.976 7.227 1.00 32.80 S ANISOU 2699 SG CYS C 120 4071 4184 4209 -258 -84 43 S ATOM 2700 N GLY C 121 19.902 -2.086 6.013 1.00 26.07 N ANISOU 2700 N GLY C 121 3003 3535 3369 -274 -130 141 N ATOM 2701 CA GLY C 121 19.000 -0.956 5.870 1.00 29.72 C ANISOU 2701 CA GLY C 121 3388 4047 3856 -228 -125 164 C ATOM 2702 C GLY C 121 19.291 0.019 6.994 1.00 32.85 C ANISOU 2702 C GLY C 121 3758 4438 4286 -161 -75 137 C ATOM 2703 O GLY C 121 19.018 -0.261 8.167 1.00 34.75 O ANISOU 2703 O GLY C 121 3974 4709 4521 -171 -53 128 O ATOM 2704 N ASN C 122 19.867 1.160 6.630 1.00 29.46 N ANISOU 2704 N ASN C 122 3343 3966 3884 -100 -59 124 N ATOM 2705 CA ASN C 122 20.297 2.148 7.610 1.00 28.63 C ANISOU 2705 CA ASN C 122 3235 3838 3805 -41 -14 94 C ATOM 2706 C ASN C 122 19.244 3.217 7.887 1.00 29.18 C ANISOU 2706 C ASN C 122 3238 3950 3898 21 7 109 C ATOM 2707 O ASN C 122 18.289 3.381 7.115 1.00 30.69 O ANISOU 2707 O ASN C 122 3380 4185 4094 29 -17 148 O ATOM 2708 CB ASN C 122 21.625 2.782 7.176 1.00 27.90 C ANISOU 2708 CB ASN C 122 3206 3670 3726 -16 -6 69 C ATOM 2709 CG ASN C 122 22.238 3.657 8.266 1.00 30.05 C ANISOU 2709 CG ASN C 122 3492 3911 4014 24 34 35 C ATOM 2710 OD1 ASN C 122 22.137 3.345 9.445 1.00 30.73 O ANISOU 2710 OD1 ASN C 122 3567 4016 4091 14 55 18 O ATOM 2711 ND2 ASN C 122 22.851 4.771 7.872 1.00 31.59 N ANISOU 2711 ND2 ASN C 122 3717 4056 4228 63 43 26 N ATOM 2712 N LYS C 123 19.424 3.912 9.009 1.00 30.07 N ANISOU 2712 N LYS C 123 3351 4051 4023 64 52 78 N ATOM 2713 CA LYS C 123 18.566 5.034 9.440 1.00 29.45 C ANISOU 2713 CA LYS C 123 3223 3999 3967 140 86 81 C ATOM 2714 C LYS C 123 17.225 4.602 10.040 1.00 33.31 C ANISOU 2714 C LYS C 123 3625 4584 4446 136 99 105 C ATOM 2715 O LYS C 123 16.235 5.328 9.934 1.00 33.41 O ANISOU 2715 O LYS C 123 3575 4641 4479 198 113 129 O ATOM 2716 CB LYS C 123 18.340 6.045 8.301 1.00 30.83 C ANISOU 2716 CB LYS C 123 3395 4151 4168 196 68 107 C ATOM 2717 CG LYS C 123 19.637 6.504 7.624 1.00 32.07 C ANISOU 2717 CG LYS C 123 3635 4220 4331 193 56 89 C ATOM 2718 CD LYS C 123 19.416 7.754 6.789 1.00 36.39 C ANISOU 2718 CD LYS C 123 4188 4734 4903 258 49 109 C ATOM 2719 CE LYS C 123 20.643 8.106 5.947 1.00 29.59 C ANISOU 2719 CE LYS C 123 3404 3798 4041 239 31 101 C ATOM 2720 NZ LYS C 123 20.367 9.359 5.120 1.00 30.55 N ANISOU 2720 NZ LYS C 123 3537 3886 4186 299 20 126 N ATOM 2721 N VAL C 124 17.188 3.437 10.683 1.00 34.19 N ANISOU 2721 N VAL C 124 3732 4732 4528 65 95 102 N ATOM 2722 CA VAL C 124 15.922 2.939 11.244 1.00 34.69 C ANISOU 2722 CA VAL C 124 3709 4895 4576 45 106 130 C ATOM 2723 C VAL C 124 15.502 3.694 12.501 1.00 37.01 C ANISOU 2723 C VAL C 124 3971 5217 4875 108 171 105 C ATOM 2724 O VAL C 124 14.449 3.414 13.092 1.00 35.11 O ANISOU 2724 O VAL C 124 3653 5068 4621 101 194 126 O ATOM 2725 CB VAL C 124 15.953 1.420 11.540 1.00 35.54 C ANISOU 2725 CB VAL C 124 3829 5030 4644 -59 78 139 C ATOM 2726 CG1 VAL C 124 16.161 0.616 10.255 1.00 35.44 C ANISOU 2726 CG1 VAL C 124 3848 4997 4619 -120 16 166 C ATOM 2727 CG2 VAL C 124 17.015 1.092 12.588 1.00 36.52 C ANISOU 2727 CG2 VAL C 124 4023 5100 4751 -81 101 94 C ATOM 2728 N ASP C 125 16.325 4.655 12.914 1.00 33.57 N ANISOU 2728 N ASP C 125 3597 4704 4452 164 204 61 N ATOM 2729 CA ASP C 125 15.951 5.515 14.031 1.00 36.80 C ANISOU 2729 CA ASP C 125 3994 5127 4863 231 270 32 C ATOM 2730 C ASP C 125 14.896 6.534 13.627 1.00 38.17 C ANISOU 2730 C ASP C 125 4100 5336 5067 329 293 57 C ATOM 2731 O ASP C 125 14.214 7.092 14.478 1.00 40.20 O ANISOU 2731 O ASP C 125 4320 5632 5322 391 352 44 O ATOM 2732 CB ASP C 125 17.165 6.254 14.600 1.00 36.35 C ANISOU 2732 CB ASP C 125 4035 4972 4805 253 294 -22 C ATOM 2733 CG ASP C 125 17.897 7.061 13.549 1.00 36.34 C ANISOU 2733 CG ASP C 125 4088 4887 4833 286 267 -23 C ATOM 2734 OD1 ASP C 125 17.685 8.293 13.483 1.00 37.64 O ANISOU 2734 OD1 ASP C 125 4265 5018 5019 369 295 -32 O ATOM 2735 OD2 ASP C 125 18.678 6.460 12.782 1.00 35.21 O ANISOU 2735 OD2 ASP C 125 3978 4712 4689 230 220 -13 O ATOM 2736 N ILE C 126 14.775 6.790 12.329 1.00 35.97 N ANISOU 2736 N ILE C 126 3809 5044 4814 346 248 93 N ATOM 2737 CA ILE C 126 13.835 7.805 11.852 1.00 38.83 C ANISOU 2737 CA ILE C 126 4111 5433 5209 446 261 124 C ATOM 2738 C ILE C 126 12.410 7.253 11.874 1.00 45.89 C ANISOU 2738 C ILE C 126 4877 6460 6100 441 261 176 C ATOM 2739 O ILE C 126 12.133 6.213 11.285 1.00 46.79 O ANISOU 2739 O ILE C 126 4953 6627 6197 354 208 216 O ATOM 2740 CB ILE C 126 14.225 8.318 10.448 1.00 42.81 C ANISOU 2740 CB ILE C 126 4651 5875 5739 464 209 149 C ATOM 2741 CG1 ILE C 126 15.557 9.076 10.513 1.00 43.12 C ANISOU 2741 CG1 ILE C 126 4809 5791 5783 479 219 99 C ATOM 2742 CG2 ILE C 126 13.121 9.219 9.865 1.00 41.37 C ANISOU 2742 CG2 ILE C 126 4394 5733 5591 563 211 195 C ATOM 2743 CD1 ILE C 126 16.186 9.333 9.155 1.00 45.52 C ANISOU 2743 CD1 ILE C 126 5162 6034 6101 465 166 120 C ATOM 2744 N LYS C 127 11.510 7.941 12.570 1.00 49.65 N ANISOU 2744 N LYS C 127 5287 6990 6586 531 322 177 N ATOM 2745 CA LYS C 127 10.153 7.429 12.745 1.00 59.62 C ANISOU 2745 CA LYS C 127 6415 8394 7843 525 330 228 C ATOM 2746 C LYS C 127 9.452 7.126 11.424 1.00 52.99 C ANISOU 2746 C LYS C 127 5498 7616 7019 501 259 304 C ATOM 2747 O LYS C 127 8.842 6.067 11.268 1.00 51.65 O ANISOU 2747 O LYS C 127 5257 7541 6825 411 224 347 O ATOM 2748 CB LYS C 127 9.303 8.380 13.594 1.00 73.18 C ANISOU 2748 CB LYS C 127 8071 10158 9574 648 414 219 C ATOM 2749 CG LYS C 127 9.443 8.168 15.098 1.00 85.55 C ANISOU 2749 CG LYS C 127 9662 11739 11104 634 486 165 C ATOM 2750 CD LYS C 127 8.408 8.977 15.873 1.00 91.55 C ANISOU 2750 CD LYS C 127 10345 12569 11873 755 573 163 C ATOM 2751 CE LYS C 127 8.410 8.616 17.354 1.00 93.19 C ANISOU 2751 CE LYS C 127 10564 12811 12032 725 644 116 C ATOM 2752 NZ LYS C 127 7.399 9.395 18.129 1.00 93.39 N ANISOU 2752 NZ LYS C 127 10516 12908 12061 848 739 110 N ATOM 2753 N ASP C 128 9.539 8.052 10.474 1.00 50.44 N ANISOU 2753 N ASP C 128 5194 7238 6732 576 235 321 N ATOM 2754 CA ASP C 128 8.821 7.896 9.212 1.00 55.06 C ANISOU 2754 CA ASP C 128 5705 7884 7331 561 166 397 C ATOM 2755 C ASP C 128 9.568 6.981 8.252 1.00 52.72 C ANISOU 2755 C ASP C 128 5478 7544 7010 439 89 404 C ATOM 2756 O ASP C 128 10.148 7.432 7.262 1.00 48.77 O ANISOU 2756 O ASP C 128 5042 6966 6523 451 49 408 O ATOM 2757 CB ASP C 128 8.553 9.254 8.558 1.00 62.28 C ANISOU 2757 CB ASP C 128 6613 8760 8292 691 168 420 C ATOM 2758 CG ASP C 128 7.590 9.154 7.390 1.00 71.60 C ANISOU 2758 CG ASP C 128 7692 10027 9485 688 101 508 C ATOM 2759 OD1 ASP C 128 7.111 8.035 7.104 1.00 70.82 O ANISOU 2759 OD1 ASP C 128 7530 10021 9358 579 54 550 O ATOM 2760 OD2 ASP C 128 7.311 10.195 6.757 1.00 77.01 O ANISOU 2760 OD2 ASP C 128 8367 10686 10208 790 91 539 O ATOM 2761 N ARG C 129 9.544 5.688 8.555 1.00 49.49 N ANISOU 2761 N ARG C 129 5059 7184 6561 322 70 406 N ATOM 2762 CA ARG C 129 10.242 4.695 7.753 1.00 45.54 C ANISOU 2762 CA ARG C 129 4633 6641 6031 206 4 407 C ATOM 2763 C ARG C 129 9.471 4.380 6.469 1.00 43.65 C ANISOU 2763 C ARG C 129 4334 6465 5785 162 -71 481 C ATOM 2764 O ARG C 129 8.257 4.205 6.494 1.00 45.03 O ANISOU 2764 O ARG C 129 4389 6760 5958 156 -81 538 O ATOM 2765 CB ARG C 129 10.445 3.422 8.567 1.00 41.65 C ANISOU 2765 CB ARG C 129 4159 6171 5494 101 10 385 C ATOM 2766 CG ARG C 129 11.267 2.386 7.864 1.00 37.32 C ANISOU 2766 CG ARG C 129 3704 5563 4915 -6 -48 377 C ATOM 2767 CD ARG C 129 11.578 1.217 8.785 1.00 37.03 C ANISOU 2767 CD ARG C 129 3703 5530 4839 -96 -37 351 C ATOM 2768 NE ARG C 129 12.214 0.141 8.037 1.00 35.97 N ANISOU 2768 NE ARG C 129 3652 5343 4671 -195 -94 350 N ATOM 2769 CZ ARG C 129 12.918 -0.841 8.586 1.00 34.91 C ANISOU 2769 CZ ARG C 129 3593 5166 4506 -263 -94 319 C ATOM 2770 NH1 ARG C 129 13.099 -0.879 9.898 1.00 33.05 N ANISOU 2770 NH1 ARG C 129 3356 4935 4267 -251 -44 287 N ATOM 2771 NH2 ARG C 129 13.456 -1.767 7.813 1.00 35.80 N ANISOU 2771 NH2 ARG C 129 3786 5228 4590 -339 -143 319 N ATOM 2772 N LYS C 130 10.183 4.306 5.350 1.00 39.71 N ANISOU 2772 N LYS C 130 3917 5891 5279 127 -123 481 N ATOM 2773 CA LYS C 130 9.542 4.079 4.061 1.00 48.09 C ANISOU 2773 CA LYS C 130 4939 7002 6329 81 -198 549 C ATOM 2774 C LYS C 130 9.761 2.665 3.526 1.00 49.84 C ANISOU 2774 C LYS C 130 5213 7226 6496 -64 -256 556 C ATOM 2775 O LYS C 130 8.846 2.062 2.965 1.00 48.37 O ANISOU 2775 O LYS C 130 4965 7130 6285 -137 -312 616 O ATOM 2776 CB LYS C 130 10.009 5.113 3.036 1.00 49.94 C ANISOU 2776 CB LYS C 130 5226 7160 6591 149 -219 555 C ATOM 2777 CG LYS C 130 9.594 6.534 3.367 1.00 56.38 C ANISOU 2777 CG LYS C 130 5989 7976 7459 294 -176 563 C ATOM 2778 CD LYS C 130 8.119 6.601 3.747 1.00 57.59 C ANISOU 2778 CD LYS C 130 5988 8267 7625 332 -168 623 C ATOM 2779 CE LYS C 130 7.535 7.977 3.475 1.00 65.17 C ANISOU 2779 CE LYS C 130 6892 9233 8636 474 -156 659 C ATOM 2780 NZ LYS C 130 8.404 9.063 4.001 1.00 69.21 N ANISOU 2780 NZ LYS C 130 7497 9623 9177 577 -94 594 N ATOM 2781 N VAL C 131 10.973 2.141 3.688 1.00 38.64 N ANISOU 2781 N VAL C 131 3913 5709 5058 -105 -244 495 N ATOM 2782 CA VAL C 131 11.256 0.784 3.248 1.00 36.12 C ANISOU 2782 CA VAL C 131 3661 5378 4686 -232 -290 494 C ATOM 2783 C VAL C 131 11.159 -0.155 4.441 1.00 43.85 C ANISOU 2783 C VAL C 131 4631 6387 5642 -289 -263 474 C ATOM 2784 O VAL C 131 12.086 -0.233 5.259 1.00 37.14 O ANISOU 2784 O VAL C 131 3846 5469 4797 -270 -218 416 O ATOM 2785 CB VAL C 131 12.644 0.653 2.600 1.00 40.23 C ANISOU 2785 CB VAL C 131 4315 5775 5195 -244 -297 447 C ATOM 2786 CG1 VAL C 131 12.859 -0.769 2.112 1.00 38.41 C ANISOU 2786 CG1 VAL C 131 4159 5528 4906 -366 -342 447 C ATOM 2787 CG2 VAL C 131 12.795 1.641 1.441 1.00 41.07 C ANISOU 2787 CG2 VAL C 131 4436 5848 5320 -190 -320 468 C ATOM 2788 N LYS C 132 10.029 -0.851 4.541 1.00 37.85 N ANISOU 2788 N LYS C 132 3791 5735 4854 -364 -294 525 N ATOM 2789 CA LYS C 132 9.759 -1.697 5.704 1.00 45.79 C ANISOU 2789 CA LYS C 132 4777 6787 5836 -423 -269 516 C ATOM 2790 C LYS C 132 10.130 -3.160 5.459 1.00 41.54 C ANISOU 2790 C LYS C 132 4335 6209 5239 -556 -315 510 C ATOM 2791 O LYS C 132 10.395 -3.565 4.323 1.00 43.27 O ANISOU 2791 O LYS C 132 4623 6384 5432 -609 -369 519 O ATOM 2792 CB LYS C 132 8.291 -1.583 6.122 1.00 54.38 C ANISOU 2792 CB LYS C 132 5712 8023 6926 -428 -266 578 C ATOM 2793 CG LYS C 132 7.889 -0.203 6.626 1.00 56.93 C ANISOU 2793 CG LYS C 132 5942 8386 7305 -284 -204 578 C ATOM 2794 CD LYS C 132 6.424 -0.179 7.037 1.00 62.89 C ANISOU 2794 CD LYS C 132 6537 9300 8060 -287 -197 643 C ATOM 2795 CE LYS C 132 6.013 1.180 7.586 1.00 68.67 C ANISOU 2795 CE LYS C 132 7180 10065 8845 -131 -127 640 C ATOM 2796 NZ LYS C 132 6.003 2.227 6.528 1.00 75.15 N ANISOU 2796 NZ LYS C 132 7993 10853 9707 -40 -153 663 N ATOM 2797 N ALA C 133 10.123 -3.947 6.532 1.00 39.14 N ANISOU 2797 N ALA C 133 4040 5920 4911 -610 -293 494 N ATOM 2798 CA ALA C 133 10.537 -5.348 6.475 1.00 41.46 C ANISOU 2798 CA ALA C 133 4439 6164 5151 -727 -330 483 C ATOM 2799 C ALA C 133 9.880 -6.125 5.332 1.00 41.31 C ANISOU 2799 C ALA C 133 4434 6178 5085 -840 -410 535 C ATOM 2800 O ALA C 133 10.532 -6.928 4.667 1.00 42.51 O ANISOU 2800 O ALA C 133 4709 6244 5200 -901 -446 516 O ATOM 2801 CB ALA C 133 10.265 -6.037 7.802 1.00 42.53 C ANISOU 2801 CB ALA C 133 4555 6342 5264 -778 -302 480 C ATOM 2802 N LYS C 134 8.593 -5.889 5.109 1.00 43.43 N ANISOU 2802 N LYS C 134 4578 6573 5351 -866 -437 601 N ATOM 2803 CA LYS C 134 7.865 -6.646 4.095 1.00 51.08 C ANISOU 2803 CA LYS C 134 5551 7588 6267 -989 -520 658 C ATOM 2804 C LYS C 134 8.383 -6.382 2.682 1.00 51.13 C ANISOU 2804 C LYS C 134 5637 7520 6269 -977 -561 652 C ATOM 2805 O LYS C 134 8.242 -7.222 1.790 1.00 48.68 O ANISOU 2805 O LYS C 134 5399 7194 5902 -1088 -628 673 O ATOM 2806 CB LYS C 134 6.358 -6.378 4.180 1.00 57.60 C ANISOU 2806 CB LYS C 134 6208 8583 7096 -1016 -540 739 C ATOM 2807 CG LYS C 134 5.956 -4.921 4.022 1.00 64.59 C ANISOU 2807 CG LYS C 134 6972 9525 8046 -877 -510 760 C ATOM 2808 CD LYS C 134 4.462 -4.746 4.265 1.00 73.02 C ANISOU 2808 CD LYS C 134 7860 10769 9116 -898 -522 842 C ATOM 2809 CE LYS C 134 4.063 -5.285 5.635 1.00 77.55 C ANISOU 2809 CE LYS C 134 8380 11412 9674 -938 -475 839 C ATOM 2810 NZ LYS C 134 2.586 -5.300 5.837 1.00 80.56 N ANISOU 2810 NZ LYS C 134 8584 11978 10046 -980 -490 925 N ATOM 2811 N SER C 135 8.996 -5.222 2.484 1.00 41.25 N ANISOU 2811 N SER C 135 4381 6220 5073 -846 -522 623 N ATOM 2812 CA SER C 135 9.484 -4.835 1.165 1.00 43.57 C ANISOU 2812 CA SER C 135 4741 6449 5364 -827 -556 620 C ATOM 2813 C SER C 135 10.926 -5.260 0.914 1.00 42.11 C ANISOU 2813 C SER C 135 4716 6120 5164 -821 -537 549 C ATOM 2814 O SER C 135 11.404 -5.214 -0.215 1.00 42.17 O ANISOU 2814 O SER C 135 4801 6069 5153 -829 -566 543 O ATOM 2815 CB SER C 135 9.361 -3.323 0.982 1.00 52.98 C ANISOU 2815 CB SER C 135 5847 7663 6619 -694 -528 632 C ATOM 2816 OG SER C 135 8.004 -2.937 0.870 1.00 50.92 O ANISOU 2816 OG SER C 135 5443 7537 6369 -697 -558 708 O ATOM 2817 N ILE C 136 11.624 -5.661 1.972 1.00 39.98 N ANISOU 2817 N ILE C 136 4490 5798 4902 -805 -488 500 N ATOM 2818 CA ILE C 136 13.045 -5.980 1.862 1.00 36.58 C ANISOU 2818 CA ILE C 136 4193 5239 4466 -781 -463 435 C ATOM 2819 C ILE C 136 13.251 -7.454 1.509 1.00 43.90 C ANISOU 2819 C ILE C 136 5240 6114 5326 -896 -503 427 C ATOM 2820 O ILE C 136 13.202 -8.323 2.379 1.00 41.10 O ANISOU 2820 O ILE C 136 4908 5757 4950 -948 -498 420 O ATOM 2821 CB ILE C 136 13.772 -5.645 3.168 1.00 37.66 C ANISOU 2821 CB ILE C 136 4322 5342 4645 -702 -394 388 C ATOM 2822 CG1 ILE C 136 13.667 -4.142 3.450 1.00 36.25 C ANISOU 2822 CG1 ILE C 136 4051 5195 4529 -585 -352 388 C ATOM 2823 CG2 ILE C 136 15.227 -6.097 3.102 1.00 44.23 C ANISOU 2823 CG2 ILE C 136 5282 6052 5469 -684 -372 330 C ATOM 2824 CD1 ILE C 136 14.167 -3.748 4.841 1.00 36.26 C ANISOU 2824 CD1 ILE C 136 4033 5180 4564 -518 -286 348 C ATOM 2825 N VAL C 137 13.492 -7.720 0.228 1.00 46.24 N ANISOU 2825 N VAL C 137 5621 6364 5585 -934 -543 428 N ATOM 2826 CA VAL C 137 13.433 -9.076 -0.302 1.00 48.73 C ANISOU 2826 CA VAL C 137 6052 6639 5826 -1054 -591 430 C ATOM 2827 C VAL C 137 14.701 -9.487 -1.040 1.00 46.60 C ANISOU 2827 C VAL C 137 5933 6242 5532 -1034 -577 375 C ATOM 2828 O VAL C 137 14.948 -10.672 -1.261 1.00 48.54 O ANISOU 2828 O VAL C 137 6299 6423 5719 -1109 -598 359 O ATOM 2829 CB VAL C 137 12.225 -9.219 -1.255 1.00 54.40 C ANISOU 2829 CB VAL C 137 6733 7439 6498 -1154 -667 495 C ATOM 2830 CG1 VAL C 137 12.280 -10.533 -2.013 1.00 67.17 C ANISOU 2830 CG1 VAL C 137 8497 8995 8030 -1279 -719 490 C ATOM 2831 CG2 VAL C 137 10.926 -9.100 -0.469 1.00 49.68 C ANISOU 2831 CG2 VAL C 137 5988 6974 5913 -1193 -683 554 C ATOM 2832 N PHE C 138 15.516 -8.507 -1.409 1.00 42.55 N ANISOU 2832 N PHE C 138 5414 5692 5060 -930 -538 348 N ATOM 2833 CA PHE C 138 16.670 -8.787 -2.247 1.00 44.42 C ANISOU 2833 CA PHE C 138 5778 5826 5273 -908 -521 303 C ATOM 2834 C PHE C 138 17.609 -9.835 -1.655 1.00 43.38 C ANISOU 2834 C PHE C 138 5752 5604 5125 -907 -490 255 C ATOM 2835 O PHE C 138 18.191 -10.636 -2.389 1.00 43.29 O ANISOU 2835 O PHE C 138 5871 5514 5064 -935 -496 228 O ATOM 2836 CB PHE C 138 17.450 -7.509 -2.574 1.00 43.04 C ANISOU 2836 CB PHE C 138 5570 5632 5149 -797 -478 284 C ATOM 2837 CG PHE C 138 18.607 -7.746 -3.498 1.00 42.37 C ANISOU 2837 CG PHE C 138 5606 5457 5038 -776 -457 242 C ATOM 2838 CD1 PHE C 138 18.397 -7.923 -4.854 1.00 48.45 C ANISOU 2838 CD1 PHE C 138 6441 6216 5750 -831 -496 256 C ATOM 2839 CD2 PHE C 138 19.900 -7.831 -3.007 1.00 43.47 C ANISOU 2839 CD2 PHE C 138 5789 5524 5201 -703 -398 192 C ATOM 2840 CE1 PHE C 138 19.455 -8.160 -5.706 1.00 47.37 C ANISOU 2840 CE1 PHE C 138 6416 5999 5582 -810 -469 215 C ATOM 2841 CE2 PHE C 138 20.963 -8.068 -3.856 1.00 36.90 C ANISOU 2841 CE2 PHE C 138 5059 4619 4344 -679 -373 156 C ATOM 2842 CZ PHE C 138 20.741 -8.228 -5.204 1.00 41.05 C ANISOU 2842 CZ PHE C 138 5652 5133 4811 -730 -404 165 C ATOM 2843 N HIS C 139 17.774 -9.817 -0.335 1.00 39.36 N ANISOU 2843 N HIS C 139 5192 5105 4656 -870 -457 244 N ATOM 2844 CA HIS C 139 18.706 -10.735 0.312 1.00 36.53 C ANISOU 2844 CA HIS C 139 4926 4664 4290 -857 -429 204 C ATOM 2845 C HIS C 139 18.254 -12.180 0.188 1.00 45.47 C ANISOU 2845 C HIS C 139 6161 5764 5352 -969 -475 213 C ATOM 2846 O HIS C 139 19.075 -13.087 0.074 1.00 49.76 O ANISOU 2846 O HIS C 139 6829 6212 5867 -967 -464 178 O ATOM 2847 CB HIS C 139 18.900 -10.379 1.789 1.00 39.55 C ANISOU 2847 CB HIS C 139 5230 5073 4726 -803 -391 197 C ATOM 2848 CG HIS C 139 17.624 -10.316 2.570 1.00 38.89 C ANISOU 2848 CG HIS C 139 5045 5086 4644 -859 -413 239 C ATOM 2849 ND1 HIS C 139 17.340 -11.184 3.604 1.00 46.31 N ANISOU 2849 ND1 HIS C 139 5998 6033 5565 -914 -419 246 N ATOM 2850 CD2 HIS C 139 16.560 -9.483 2.473 1.00 36.05 C ANISOU 2850 CD2 HIS C 139 4569 4827 4302 -865 -428 280 C ATOM 2851 CE1 HIS C 139 16.155 -10.890 4.108 1.00 40.69 C ANISOU 2851 CE1 HIS C 139 5177 5426 4857 -955 -434 288 C ATOM 2852 NE2 HIS C 139 15.661 -9.860 3.440 1.00 44.72 N ANISOU 2852 NE2 HIS C 139 5605 5995 5392 -922 -438 309 N ATOM 2853 N ARG C 140 16.943 -12.382 0.224 1.00 49.50 N ANISOU 2853 N ARG C 140 6618 6354 5834 -1066 -526 262 N ATOM 2854 CA ARG C 140 16.376 -13.720 0.118 1.00 54.67 C ANISOU 2854 CA ARG C 140 7368 6987 6416 -1193 -577 278 C ATOM 2855 C ARG C 140 16.600 -14.289 -1.279 1.00 60.77 C ANISOU 2855 C ARG C 140 8277 7689 7124 -1241 -608 264 C ATOM 2856 O ARG C 140 16.717 -15.502 -1.459 1.00 64.58 O ANISOU 2856 O ARG C 140 8899 8094 7544 -1313 -632 251 O ATOM 2857 CB ARG C 140 14.888 -13.690 0.470 1.00 51.23 C ANISOU 2857 CB ARG C 140 6824 6673 5967 -1289 -625 342 C ATOM 2858 CG ARG C 140 14.626 -13.237 1.900 1.00 57.12 C ANISOU 2858 CG ARG C 140 7447 7490 6767 -1248 -590 353 C ATOM 2859 CD ARG C 140 13.153 -13.290 2.246 1.00 67.42 C ANISOU 2859 CD ARG C 140 8642 8922 8053 -1345 -631 418 C ATOM 2860 NE ARG C 140 12.621 -14.647 2.156 1.00 69.65 N ANISOU 2860 NE ARG C 140 9018 9188 8257 -1492 -689 441 N ATOM 2861 CZ ARG C 140 11.340 -14.954 2.326 1.00 73.29 C ANISOU 2861 CZ ARG C 140 9406 9756 8684 -1609 -737 503 C ATOM 2862 NH1 ARG C 140 10.461 -13.999 2.595 1.00 72.34 N ANISOU 2862 NH1 ARG C 140 9111 9771 8604 -1582 -730 546 N ATOM 2863 NH2 ARG C 140 10.937 -16.214 2.225 1.00 72.11 N ANISOU 2863 NH2 ARG C 140 9361 9580 8459 -1751 -792 522 N ATOM 2864 N LYS C 141 16.688 -13.399 -2.263 1.00 59.89 N ANISOU 2864 N LYS C 141 8135 7598 7024 -1200 -605 266 N ATOM 2865 CA LYS C 141 16.881 -13.809 -3.649 1.00 65.19 C ANISOU 2865 CA LYS C 141 8930 8209 7628 -1244 -631 252 C ATOM 2866 C LYS C 141 18.340 -14.169 -3.975 1.00 65.11 C ANISOU 2866 C LYS C 141 9048 8076 7613 -1162 -575 187 C ATOM 2867 O LYS C 141 18.602 -14.782 -5.009 1.00 69.50 O ANISOU 2867 O LYS C 141 9739 8564 8103 -1201 -587 166 O ATOM 2868 CB LYS C 141 16.407 -12.702 -4.603 1.00 64.22 C ANISOU 2868 CB LYS C 141 8725 8159 7516 -1234 -652 284 C ATOM 2869 CG LYS C 141 14.930 -12.339 -4.480 1.00 69.17 C ANISOU 2869 CG LYS C 141 9223 8914 8144 -1312 -712 356 C ATOM 2870 CD LYS C 141 14.610 -11.078 -5.283 1.00 79.11 C ANISOU 2870 CD LYS C 141 10388 10239 9430 -1268 -724 388 C ATOM 2871 CE LYS C 141 13.113 -10.794 -5.342 1.00 84.86 C ANISOU 2871 CE LYS C 141 10992 11098 10152 -1347 -790 467 C ATOM 2872 NZ LYS C 141 12.808 -9.530 -6.076 1.00 87.02 N ANISOU 2872 NZ LYS C 141 11172 11434 10458 -1292 -803 502 N ATOM 2873 N LYS C 142 19.279 -13.810 -3.101 1.00 55.11 N ANISOU 2873 N LYS C 142 7741 6785 6412 -1051 -513 157 N ATOM 2874 CA LYS C 142 20.674 -13.815 -3.497 1.00 50.65 C ANISOU 2874 CA LYS C 142 7257 6132 5856 -955 -455 104 C ATOM 2875 C LYS C 142 21.702 -14.469 -2.555 1.00 57.64 C ANISOU 2875 C LYS C 142 8192 6943 6765 -888 -409 68 C ATOM 2876 O LYS C 142 22.911 -14.421 -2.848 1.00 59.49 O ANISOU 2876 O LYS C 142 8475 7115 7012 -798 -356 28 O ATOM 2877 CB LYS C 142 21.114 -12.378 -3.809 1.00 49.23 C ANISOU 2877 CB LYS C 142 6975 5997 5734 -864 -418 103 C ATOM 2878 CG LYS C 142 20.713 -11.891 -5.198 1.00 52.20 C ANISOU 2878 CG LYS C 142 7366 6397 6071 -901 -447 119 C ATOM 2879 CD LYS C 142 21.611 -12.520 -6.252 1.00 53.55 C ANISOU 2879 CD LYS C 142 7687 6475 6184 -891 -421 76 C ATOM 2880 CE LYS C 142 21.327 -11.992 -7.647 1.00 52.13 C ANISOU 2880 CE LYS C 142 7529 6316 5961 -925 -445 89 C ATOM 2881 NZ LYS C 142 22.261 -12.570 -8.665 1.00 55.33 N ANISOU 2881 NZ LYS C 142 8084 6634 6306 -908 -409 42 N ATOM 2882 N ASN C 143 21.257 -15.073 -1.450 1.00 58.69 N ANISOU 2882 N ASN C 143 8312 7084 6902 -930 -429 84 N ATOM 2883 CA ASN C 143 22.183 -15.685 -0.475 1.00 71.03 C ANISOU 2883 CA ASN C 143 9918 8581 8489 -868 -393 58 C ATOM 2884 C ASN C 143 22.768 -14.677 0.516 1.00 68.43 C ANISOU 2884 C ASN C 143 9460 8299 8243 -770 -347 55 C ATOM 2885 O ASN C 143 23.888 -14.835 1.007 1.00 74.15 O ANISOU 2885 O ASN C 143 10207 8971 8997 -686 -306 29 O ATOM 2886 CB ASN C 143 23.314 -16.451 -1.187 1.00 82.78 C ANISOU 2886 CB ASN C 143 11553 9954 9944 -815 -360 13 C ATOM 2887 CG ASN C 143 24.237 -17.167 -0.214 1.00 92.30 C ANISOU 2887 CG ASN C 143 12806 11090 11172 -750 -329 -7 C ATOM 2888 OD1 ASN C 143 23.785 -17.646 0.825 1.00 94.46 O ANISOU 2888 OD1 ASN C 143 13068 11373 11450 -794 -355 15 O ATOM 2889 ND2 ASN C 143 25.529 -17.248 -0.544 1.00 95.74 N ANISOU 2889 ND2 ASN C 143 13293 11461 11622 -644 -275 -44 N ATOM 2890 N LEU C 144 22.029 -13.611 0.780 1.00 58.95 N ANISOU 2890 N LEU C 144 8125 7195 7079 -777 -356 84 N ATOM 2891 CA LEU C 144 22.557 -12.569 1.652 1.00 47.97 C ANISOU 2891 CA LEU C 144 6623 5843 5760 -688 -313 78 C ATOM 2892 C LEU C 144 21.852 -12.510 3.005 1.00 50.67 C ANISOU 2892 C LEU C 144 6882 6247 6124 -718 -323 103 C ATOM 2893 O LEU C 144 20.671 -12.822 3.125 1.00 50.42 O ANISOU 2893 O LEU C 144 6827 6268 6063 -807 -364 136 O ATOM 2894 CB LEU C 144 22.469 -11.198 0.967 1.00 46.14 C ANISOU 2894 CB LEU C 144 6305 5665 5560 -646 -300 84 C ATOM 2895 CG LEU C 144 22.707 -11.119 -0.542 1.00 52.14 C ANISOU 2895 CG LEU C 144 7132 6395 6286 -648 -304 74 C ATOM 2896 CD1 LEU C 144 22.707 -9.657 -1.008 1.00 53.01 C ANISOU 2896 CD1 LEU C 144 7150 6556 6435 -598 -289 84 C ATOM 2897 CD2 LEU C 144 24.005 -11.811 -0.922 1.00 50.54 C ANISOU 2897 CD2 LEU C 144 7040 6098 6065 -597 -267 33 C ATOM 2898 N GLN C 145 22.584 -12.105 4.034 1.00 39.77 N ANISOU 2898 N GLN C 145 5454 4866 4792 -647 -286 89 N ATOM 2899 CA GLN C 145 21.963 -11.868 5.323 1.00 31.16 C ANISOU 2899 CA GLN C 145 4279 3840 3722 -667 -286 108 C ATOM 2900 C GLN C 145 21.538 -10.401 5.354 1.00 30.25 C ANISOU 2900 C GLN C 145 4040 3803 3651 -625 -267 117 C ATOM 2901 O GLN C 145 22.191 -9.571 4.749 1.00 33.40 O ANISOU 2901 O GLN C 145 4427 4187 4078 -559 -243 100 O ATOM 2902 CB GLN C 145 22.960 -12.161 6.439 1.00 36.97 C ANISOU 2902 CB GLN C 145 5033 4533 4481 -617 -259 90 C ATOM 2903 CG GLN C 145 22.567 -11.609 7.781 1.00 35.77 C ANISOU 2903 CG GLN C 145 4788 4448 4356 -616 -245 102 C ATOM 2904 CD GLN C 145 21.450 -12.391 8.427 1.00 45.85 C ANISOU 2904 CD GLN C 145 6063 5764 5594 -712 -278 132 C ATOM 2905 OE1 GLN C 145 21.370 -13.611 8.284 1.00 50.46 O ANISOU 2905 OE1 GLN C 145 6742 6298 6134 -774 -309 140 O ATOM 2906 NE2 GLN C 145 20.581 -11.694 9.152 1.00 46.64 N ANISOU 2906 NE2 GLN C 145 6058 5954 5709 -727 -268 151 N ATOM 2907 N TYR C 146 20.428 -10.098 6.015 1.00 36.08 N ANISOU 2907 N TYR C 146 4693 4624 4393 -664 -278 146 N ATOM 2908 CA TYR C 146 19.982 -8.713 6.114 1.00 35.75 C ANISOU 2908 CA TYR C 146 4538 4651 4393 -614 -256 155 C ATOM 2909 C TYR C 146 19.912 -8.272 7.581 1.00 31.07 C ANISOU 2909 C TYR C 146 3877 4099 3828 -587 -223 150 C ATOM 2910 O TYR C 146 19.516 -9.074 8.435 1.00 30.18 O ANISOU 2910 O TYR C 146 3773 4004 3691 -644 -233 162 O ATOM 2911 CB TYR C 146 18.605 -8.532 5.464 1.00 33.37 C ANISOU 2911 CB TYR C 146 4178 4428 4073 -671 -292 196 C ATOM 2912 CG TYR C 146 18.086 -7.165 5.761 1.00 29.66 C ANISOU 2912 CG TYR C 146 3591 4029 3648 -610 -267 208 C ATOM 2913 CD1 TYR C 146 18.527 -6.069 5.034 1.00 32.02 C ANISOU 2913 CD1 TYR C 146 3875 4311 3981 -537 -251 197 C ATOM 2914 CD2 TYR C 146 17.211 -6.953 6.816 1.00 35.55 C ANISOU 2914 CD2 TYR C 146 4250 4855 4404 -621 -253 227 C ATOM 2915 CE1 TYR C 146 18.092 -4.792 5.339 1.00 31.61 C ANISOU 2915 CE1 TYR C 146 3729 4310 3971 -473 -226 206 C ATOM 2916 CE2 TYR C 146 16.770 -5.689 7.125 1.00 34.47 C ANISOU 2916 CE2 TYR C 146 4014 4775 4308 -552 -223 234 C ATOM 2917 CZ TYR C 146 17.219 -4.610 6.384 1.00 30.79 C ANISOU 2917 CZ TYR C 146 3542 4280 3875 -477 -210 222 C ATOM 2918 OH TYR C 146 16.798 -3.347 6.711 1.00 32.25 O ANISOU 2918 OH TYR C 146 3643 4510 4101 -403 -179 227 O ATOM 2919 N TYR C 147 20.292 -7.016 7.870 1.00 32.01 N ANISOU 2919 N TYR C 147 3938 4230 3993 -506 -185 133 N ATOM 2920 CA TYR C 147 20.055 -6.380 9.183 1.00 28.08 C ANISOU 2920 CA TYR C 147 3372 3780 3518 -478 -151 129 C ATOM 2921 C TYR C 147 19.550 -4.948 9.030 1.00 32.42 C ANISOU 2921 C TYR C 147 3837 4377 4104 -417 -127 133 C ATOM 2922 O TYR C 147 20.046 -4.223 8.182 1.00 29.33 O ANISOU 2922 O TYR C 147 3456 3953 3734 -369 -123 123 O ATOM 2923 CB TYR C 147 21.337 -6.315 10.051 1.00 29.02 C ANISOU 2923 CB TYR C 147 3529 3844 3655 -434 -122 95 C ATOM 2924 CG TYR C 147 21.826 -7.681 10.487 1.00 28.48 C ANISOU 2924 CG TYR C 147 3537 3729 3554 -482 -141 94 C ATOM 2925 CD1 TYR C 147 21.154 -8.399 11.459 1.00 32.74 C ANISOU 2925 CD1 TYR C 147 4069 4305 4065 -544 -150 111 C ATOM 2926 CD2 TYR C 147 22.931 -8.265 9.882 1.00 33.60 C ANISOU 2926 CD2 TYR C 147 4267 4300 4200 -464 -149 78 C ATOM 2927 CE1 TYR C 147 21.580 -9.665 11.832 1.00 35.60 C ANISOU 2927 CE1 TYR C 147 4511 4619 4398 -588 -173 114 C ATOM 2928 CE2 TYR C 147 23.379 -9.515 10.263 1.00 30.92 C ANISOU 2928 CE2 TYR C 147 4004 3911 3833 -496 -167 79 C ATOM 2929 CZ TYR C 147 22.695 -10.212 11.230 1.00 37.27 C ANISOU 2929 CZ TYR C 147 4807 4744 4610 -560 -182 98 C ATOM 2930 OH TYR C 147 23.130 -11.462 11.594 1.00 38.02 O ANISOU 2930 OH TYR C 147 4986 4783 4676 -592 -203 103 O ATOM 2931 N ASP C 148 18.583 -4.553 9.861 1.00 31.34 N ANISOU 2931 N ASP C 148 3621 4316 3971 -417 -108 147 N ATOM 2932 CA ASP C 148 18.284 -3.141 10.080 1.00 30.60 C ANISOU 2932 CA ASP C 148 3458 4254 3915 -340 -71 141 C ATOM 2933 C ASP C 148 19.474 -2.582 10.862 1.00 27.30 C ANISOU 2933 C ASP C 148 3079 3777 3518 -287 -34 98 C ATOM 2934 O ASP C 148 19.989 -3.245 11.781 1.00 28.96 O ANISOU 2934 O ASP C 148 3324 3969 3710 -315 -28 83 O ATOM 2935 CB ASP C 148 17.057 -2.978 10.988 1.00 30.01 C ANISOU 2935 CB ASP C 148 3294 4273 3834 -348 -49 162 C ATOM 2936 CG ASP C 148 15.731 -3.107 10.252 1.00 35.19 C ANISOU 2936 CG ASP C 148 3879 5012 4481 -382 -80 212 C ATOM 2937 OD1 ASP C 148 15.720 -3.118 9.008 1.00 36.65 O ANISOU 2937 OD1 ASP C 148 4081 5178 4666 -390 -118 230 O ATOM 2938 OD2 ASP C 148 14.685 -3.169 10.941 1.00 37.39 O ANISOU 2938 OD2 ASP C 148 4078 5380 4749 -401 -65 237 O ATOM 2939 N ILE C 149 19.924 -1.376 10.518 1.00 31.35 N ANISOU 2939 N ILE C 149 3587 4260 4063 -216 -14 81 N ATOM 2940 CA ILE C 149 20.905 -0.699 11.383 1.00 27.01 C ANISOU 2940 CA ILE C 149 3066 3668 3530 -174 21 44 C ATOM 2941 C ILE C 149 20.522 0.763 11.558 1.00 27.76 C ANISOU 2941 C ILE C 149 3120 3774 3652 -102 56 35 C ATOM 2942 O ILE C 149 19.684 1.285 10.827 1.00 28.29 O ANISOU 2942 O ILE C 149 3143 3872 3734 -75 49 59 O ATOM 2943 CB ILE C 149 22.344 -0.786 10.836 1.00 30.47 C ANISOU 2943 CB ILE C 149 3573 4029 3975 -167 10 26 C ATOM 2944 CG1 ILE C 149 22.424 -0.175 9.439 1.00 32.25 C ANISOU 2944 CG1 ILE C 149 3803 4233 4217 -138 -4 36 C ATOM 2945 CG2 ILE C 149 22.840 -2.237 10.816 1.00 35.32 C ANISOU 2945 CG2 ILE C 149 4237 4621 4562 -223 -17 30 C ATOM 2946 CD1 ILE C 149 23.832 -0.143 8.852 1.00 39.10 C ANISOU 2946 CD1 ILE C 149 4729 5035 5091 -128 -7 20 C ATOM 2947 N SER C 150 21.114 1.407 12.551 1.00 28.06 N ANISOU 2947 N SER C 150 3179 3787 3696 -74 90 2 N ATOM 2948 CA SER C 150 21.094 2.869 12.650 1.00 27.13 C ANISOU 2948 CA SER C 150 3056 3649 3603 -3 123 -15 C ATOM 2949 C SER C 150 22.490 3.300 13.057 1.00 27.17 C ANISOU 2949 C SER C 150 3127 3587 3611 1 131 -48 C ATOM 2950 O SER C 150 22.885 3.168 14.213 1.00 29.94 O ANISOU 2950 O SER C 150 3496 3934 3944 -17 150 -71 O ATOM 2951 CB SER C 150 20.058 3.349 13.665 1.00 29.56 C ANISOU 2951 CB SER C 150 3313 4011 3905 29 166 -21 C ATOM 2952 OG SER C 150 20.331 4.688 14.079 1.00 34.11 O ANISOU 2952 OG SER C 150 3916 4547 4497 94 203 -51 O ATOM 2953 N ALA C 151 23.252 3.779 12.086 1.00 28.94 N ANISOU 2953 N ALA C 151 3383 3760 3853 16 115 -47 N ATOM 2954 CA ALA C 151 24.607 4.244 12.330 1.00 33.92 C ANISOU 2954 CA ALA C 151 4068 4334 4486 14 119 -71 C ATOM 2955 C ALA C 151 24.673 5.278 13.465 1.00 36.24 C ANISOU 2955 C ALA C 151 4381 4612 4778 41 155 -101 C ATOM 2956 O ALA C 151 25.573 5.232 14.304 1.00 33.54 O ANISOU 2956 O ALA C 151 4073 4249 4420 14 159 -122 O ATOM 2957 CB ALA C 151 25.217 4.822 11.033 1.00 31.01 C ANISOU 2957 CB ALA C 151 3722 3922 4136 31 102 -60 C ATOM 2958 N LYS C 152 23.711 6.198 13.495 1.00 31.65 N ANISOU 2958 N LYS C 152 3779 4040 4207 95 181 -104 N ATOM 2959 CA LYS C 152 23.732 7.301 14.459 1.00 34.80 C ANISOU 2959 CA LYS C 152 4211 4411 4600 129 220 -137 C ATOM 2960 C LYS C 152 23.458 6.877 15.895 1.00 34.31 C ANISOU 2960 C LYS C 152 4144 4386 4508 108 249 -159 C ATOM 2961 O LYS C 152 23.831 7.592 16.819 1.00 34.10 O ANISOU 2961 O LYS C 152 4165 4327 4464 114 276 -192 O ATOM 2962 CB LYS C 152 22.744 8.396 14.052 1.00 42.78 C ANISOU 2962 CB LYS C 152 5204 5417 5633 207 244 -132 C ATOM 2963 CG LYS C 152 23.213 9.265 12.901 1.00 53.68 C ANISOU 2963 CG LYS C 152 6620 6739 7038 233 223 -120 C ATOM 2964 CD LYS C 152 24.263 10.267 13.355 1.00 64.83 C ANISOU 2964 CD LYS C 152 8115 8075 8442 229 234 -152 C ATOM 2965 CE LYS C 152 24.426 11.387 12.337 1.00 65.63 C ANISOU 2965 CE LYS C 152 8254 8117 8566 267 222 -140 C ATOM 2966 NZ LYS C 152 23.165 12.167 12.172 1.00 69.13 N ANISOU 2966 NZ LYS C 152 8674 8563 9028 354 246 -131 N ATOM 2967 N SER C 153 22.814 5.719 16.075 1.00 31.36 N ANISOU 2967 N SER C 153 3720 4075 4122 75 241 -139 N ATOM 2968 CA SER C 153 22.519 5.192 17.404 1.00 31.32 C ANISOU 2968 CA SER C 153 3707 4110 4081 45 265 -154 C ATOM 2969 C SER C 153 23.353 3.942 17.770 1.00 32.58 C ANISOU 2969 C SER C 153 3887 4272 4219 -31 231 -146 C ATOM 2970 O SER C 153 23.253 3.422 18.876 1.00 31.60 O ANISOU 2970 O SER C 153 3766 4177 4062 -67 243 -154 O ATOM 2971 CB SER C 153 21.013 4.909 17.555 1.00 35.58 C ANISOU 2971 CB SER C 153 4172 4730 4615 64 291 -135 C ATOM 2972 OG SER C 153 20.563 3.922 16.641 1.00 40.92 O ANISOU 2972 OG SER C 153 4802 5445 5300 32 251 -94 O ATOM 2973 N ASN C 154 24.191 3.483 16.847 1.00 34.17 N ANISOU 2973 N ASN C 154 4104 4440 4437 -50 190 -129 N ATOM 2974 CA ASN C 154 24.952 2.250 17.049 1.00 32.34 C ANISOU 2974 CA ASN C 154 3891 4207 4190 -107 157 -117 C ATOM 2975 C ASN C 154 24.070 1.009 17.012 1.00 27.87 C ANISOU 2975 C ASN C 154 3291 3691 3609 -144 142 -91 C ATOM 2976 O ASN C 154 24.526 -0.096 17.319 1.00 31.25 O ANISOU 2976 O ASN C 154 3739 4117 4019 -190 117 -80 O ATOM 2977 CB ASN C 154 25.743 2.307 18.357 1.00 32.77 C ANISOU 2977 CB ASN C 154 3983 4248 4218 -136 164 -138 C ATOM 2978 CG ASN C 154 26.794 3.383 18.340 1.00 36.10 C ANISOU 2978 CG ASN C 154 4447 4619 4651 -121 166 -159 C ATOM 2979 OD1 ASN C 154 27.289 3.769 17.274 1.00 31.99 O ANISOU 2979 OD1 ASN C 154 3930 4066 4157 -100 152 -151 O ATOM 2980 ND2 ASN C 154 27.152 3.874 19.516 1.00 35.89 N ANISOU 2980 ND2 ASN C 154 4455 4585 4598 -138 182 -183 N ATOM 2981 N TYR C 155 22.815 1.181 16.601 1.00 25.86 N ANISOU 2981 N TYR C 155 2986 3482 3360 -123 155 -77 N ATOM 2982 CA TYR C 155 21.889 0.050 16.611 1.00 32.55 C ANISOU 2982 CA TYR C 155 3798 4385 4186 -170 140 -48 C ATOM 2983 C TYR C 155 22.350 -1.060 15.654 1.00 29.38 C ANISOU 2983 C TYR C 155 3423 3956 3784 -209 91 -26 C ATOM 2984 O TYR C 155 22.506 -0.831 14.441 1.00 29.88 O ANISOU 2984 O TYR C 155 3489 3994 3869 -187 74 -17 O ATOM 2985 CB TYR C 155 20.458 0.511 16.283 1.00 30.61 C ANISOU 2985 CB TYR C 155 3479 4203 3948 -140 161 -31 C ATOM 2986 CG TYR C 155 19.459 -0.624 16.151 1.00 30.32 C ANISOU 2986 CG TYR C 155 3400 4232 3888 -200 139 6 C ATOM 2987 CD1 TYR C 155 19.161 -1.453 17.229 1.00 37.45 C ANISOU 2987 CD1 TYR C 155 4300 5176 4754 -257 146 11 C ATOM 2988 CD2 TYR C 155 18.808 -0.860 14.948 1.00 33.15 C ANISOU 2988 CD2 TYR C 155 3725 4614 4258 -206 108 39 C ATOM 2989 CE1 TYR C 155 18.248 -2.503 17.097 1.00 38.64 C ANISOU 2989 CE1 TYR C 155 4417 5386 4879 -324 122 48 C ATOM 2990 CE2 TYR C 155 17.905 -1.895 14.810 1.00 36.25 C ANISOU 2990 CE2 TYR C 155 4083 5067 4625 -273 82 76 C ATOM 2991 CZ TYR C 155 17.626 -2.713 15.882 1.00 34.06 C ANISOU 2991 CZ TYR C 155 3804 4827 4310 -333 90 81 C ATOM 2992 OH TYR C 155 16.711 -3.735 15.713 1.00 36.51 O ANISOU 2992 OH TYR C 155 4084 5198 4590 -411 61 121 O ATOM 2993 N ASN C 156 22.553 -2.252 16.216 1.00 30.37 N ANISOU 2993 N ASN C 156 3574 4083 3881 -267 71 -16 N ATOM 2994 CA ASN C 156 22.958 -3.434 15.464 1.00 30.79 C ANISOU 2994 CA ASN C 156 3668 4105 3927 -304 29 3 C ATOM 2995 C ASN C 156 24.312 -3.268 14.792 1.00 28.92 C ANISOU 2995 C ASN C 156 3476 3800 3713 -272 17 -9 C ATOM 2996 O ASN C 156 24.602 -3.949 13.812 1.00 30.59 O ANISOU 2996 O ASN C 156 3718 3981 3925 -280 -9 2 O ATOM 2997 CB ASN C 156 21.905 -3.814 14.417 1.00 30.59 C ANISOU 2997 CB ASN C 156 3614 4111 3898 -326 8 31 C ATOM 2998 CG ASN C 156 20.804 -4.685 14.985 1.00 33.64 C ANISOU 2998 CG ASN C 156 3975 4559 4249 -392 -1 57 C ATOM 2999 OD1 ASN C 156 20.855 -5.105 16.142 1.00 35.16 O ANISOU 2999 OD1 ASN C 156 4177 4765 4418 -424 9 54 O ATOM 3000 ND2 ASN C 156 19.807 -4.985 14.159 1.00 35.17 N ANISOU 3000 ND2 ASN C 156 4135 4793 4434 -422 -22 86 N ATOM 3001 N PHE C 157 25.146 -2.378 15.325 1.00 27.61 N ANISOU 3001 N PHE C 157 3316 3612 3561 -238 37 -32 N ATOM 3002 CA PHE C 157 26.437 -2.098 14.689 1.00 26.68 C ANISOU 3002 CA PHE C 157 3229 3443 3466 -209 29 -40 C ATOM 3003 C PHE C 157 27.243 -3.380 14.426 1.00 26.31 C ANISOU 3003 C PHE C 157 3225 3363 3410 -229 1 -27 C ATOM 3004 O PHE C 157 27.802 -3.579 13.335 1.00 30.19 O ANISOU 3004 O PHE C 157 3736 3822 3912 -210 -9 -23 O ATOM 3005 CB PHE C 157 27.277 -1.094 15.525 1.00 30.12 C ANISOU 3005 CB PHE C 157 3670 3864 3908 -190 49 -62 C ATOM 3006 CG PHE C 157 28.624 -0.814 14.921 1.00 29.50 C ANISOU 3006 CG PHE C 157 3613 3746 3850 -169 40 -64 C ATOM 3007 CD1 PHE C 157 28.753 0.081 13.867 1.00 28.19 C ANISOU 3007 CD1 PHE C 157 3442 3562 3706 -138 48 -68 C ATOM 3008 CD2 PHE C 157 29.754 -1.481 15.372 1.00 28.62 C ANISOU 3008 CD2 PHE C 157 3523 3618 3733 -183 23 -57 C ATOM 3009 CE1 PHE C 157 29.975 0.282 13.271 1.00 25.72 C ANISOU 3009 CE1 PHE C 157 3143 3221 3408 -125 42 -65 C ATOM 3010 CE2 PHE C 157 30.972 -1.282 14.772 1.00 27.07 C ANISOU 3010 CE2 PHE C 157 3334 3396 3555 -163 17 -53 C ATOM 3011 CZ PHE C 157 31.085 -0.384 13.732 1.00 32.08 C ANISOU 3011 CZ PHE C 157 3962 4018 4209 -137 29 -59 C ATOM 3012 N GLU C 158 27.316 -4.243 15.437 1.00 26.69 N ANISOU 3012 N GLU C 158 3291 3416 3434 -264 -11 -19 N ATOM 3013 CA GLU C 158 28.201 -5.386 15.370 1.00 26.56 C ANISOU 3013 CA GLU C 158 3319 3360 3410 -271 -37 -7 C ATOM 3014 C GLU C 158 27.629 -6.501 14.478 1.00 29.82 C ANISOU 3014 C GLU C 158 3766 3757 3808 -294 -59 9 C ATOM 3015 O GLU C 158 28.370 -7.367 14.036 1.00 29.32 O ANISOU 3015 O GLU C 158 3750 3649 3743 -284 -75 16 O ATOM 3016 CB GLU C 158 28.462 -5.931 16.787 1.00 29.31 C ANISOU 3016 CB GLU C 158 3683 3716 3737 -302 -47 1 C ATOM 3017 CG GLU C 158 27.397 -6.916 17.285 1.00 37.74 C ANISOU 3017 CG GLU C 158 4764 4806 4769 -359 -61 18 C ATOM 3018 CD GLU C 158 26.063 -6.271 17.663 1.00 37.77 C ANISOU 3018 CD GLU C 158 4719 4871 4761 -382 -36 12 C ATOM 3019 OE1 GLU C 158 25.863 -5.060 17.434 1.00 38.06 O ANISOU 3019 OE1 GLU C 158 4716 4926 4818 -345 -8 -6 O ATOM 3020 OE2 GLU C 158 25.198 -6.999 18.206 1.00 35.80 O ANISOU 3020 OE2 GLU C 158 4471 4652 4479 -436 -44 29 O ATOM 3021 N LYS C 159 26.322 -6.475 14.216 1.00 29.06 N ANISOU 3021 N LYS C 159 3646 3698 3698 -326 -59 16 N ATOM 3022 CA LYS C 159 25.651 -7.624 13.574 1.00 29.88 C ANISOU 3022 CA LYS C 159 3787 3792 3775 -371 -87 35 C ATOM 3023 C LYS C 159 26.277 -8.039 12.238 1.00 29.95 C ANISOU 3023 C LYS C 159 3845 3747 3789 -347 -99 32 C ATOM 3024 O LYS C 159 26.569 -9.216 12.018 1.00 32.22 O ANISOU 3024 O LYS C 159 4199 3988 4054 -365 -120 39 O ATOM 3025 CB LYS C 159 24.154 -7.349 13.382 1.00 31.62 C ANISOU 3025 CB LYS C 159 3956 4074 3982 -408 -87 48 C ATOM 3026 CG LYS C 159 23.390 -7.085 14.678 1.00 36.41 C ANISOU 3026 CG LYS C 159 4515 4743 4577 -435 -69 52 C ATOM 3027 CD LYS C 159 23.157 -8.365 15.450 1.00 42.69 C ANISOU 3027 CD LYS C 159 5351 5537 5333 -503 -93 72 C ATOM 3028 CE LYS C 159 22.005 -8.230 16.443 1.00 49.25 C ANISOU 3028 CE LYS C 159 6125 6447 6139 -548 -77 84 C ATOM 3029 NZ LYS C 159 22.274 -7.193 17.486 1.00 53.58 N ANISOU 3029 NZ LYS C 159 6636 7021 6700 -508 -36 61 N ATOM 3030 N PRO C 160 26.450 -7.083 11.320 1.00 29.60 N ANISOU 3030 N PRO C 160 3774 3703 3767 -306 -83 21 N ATOM 3031 CA PRO C 160 27.012 -7.468 10.015 1.00 29.27 C ANISOU 3031 CA PRO C 160 3783 3616 3724 -286 -89 17 C ATOM 3032 C PRO C 160 28.412 -8.050 10.163 1.00 29.74 C ANISOU 3032 C PRO C 160 3887 3623 3789 -248 -83 10 C ATOM 3033 O PRO C 160 28.770 -9.008 9.501 1.00 26.47 O ANISOU 3033 O PRO C 160 3538 3161 3357 -245 -93 10 O ATOM 3034 CB PRO C 160 27.083 -6.146 9.262 1.00 33.49 C ANISOU 3034 CB PRO C 160 4273 4166 4284 -248 -69 8 C ATOM 3035 CG PRO C 160 26.032 -5.285 9.913 1.00 37.65 C ANISOU 3035 CG PRO C 160 4735 4752 4821 -260 -62 14 C ATOM 3036 CD PRO C 160 25.952 -5.694 11.337 1.00 29.94 C ANISOU 3036 CD PRO C 160 3751 3791 3835 -283 -61 14 C ATOM 3037 N PHE C 161 29.210 -7.460 11.038 1.00 28.14 N ANISOU 3037 N PHE C 161 3650 3430 3610 -218 -68 5 N ATOM 3038 CA PHE C 161 30.569 -7.947 11.210 1.00 25.24 C ANISOU 3038 CA PHE C 161 3310 3027 3253 -178 -65 5 C ATOM 3039 C PHE C 161 30.590 -9.339 11.794 1.00 26.93 C ANISOU 3039 C PHE C 161 3581 3208 3443 -199 -89 19 C ATOM 3040 O PHE C 161 31.429 -10.158 11.421 1.00 28.56 O ANISOU 3040 O PHE C 161 3838 3367 3648 -164 -90 22 O ATOM 3041 CB PHE C 161 31.372 -6.970 12.074 1.00 25.80 C ANISOU 3041 CB PHE C 161 3329 3123 3350 -155 -51 2 C ATOM 3042 CG PHE C 161 31.386 -5.580 11.502 1.00 24.67 C ANISOU 3042 CG PHE C 161 3143 3003 3229 -137 -29 -10 C ATOM 3043 CD1 PHE C 161 32.237 -5.258 10.463 1.00 24.80 C ANISOU 3043 CD1 PHE C 161 3160 3003 3259 -100 -14 -14 C ATOM 3044 CD2 PHE C 161 30.518 -4.624 11.970 1.00 25.14 C ANISOU 3044 CD2 PHE C 161 3165 3097 3291 -157 -23 -17 C ATOM 3045 CE1 PHE C 161 32.245 -3.978 9.918 1.00 29.48 C ANISOU 3045 CE1 PHE C 161 3721 3611 3867 -90 2 -22 C ATOM 3046 CE2 PHE C 161 30.523 -3.334 11.434 1.00 31.70 C ANISOU 3046 CE2 PHE C 161 3967 3938 4141 -137 -5 -27 C ATOM 3047 CZ PHE C 161 31.384 -3.020 10.401 1.00 27.20 C ANISOU 3047 CZ PHE C 161 3402 3348 3584 -108 5 -28 C ATOM 3048 N LEU C 162 29.681 -9.613 12.721 1.00 24.58 N ANISOU 3048 N LEU C 162 3279 2934 3125 -254 -106 29 N ATOM 3049 CA LEU C 162 29.706 -10.914 13.366 1.00 29.20 C ANISOU 3049 CA LEU C 162 3925 3485 3685 -280 -132 46 C ATOM 3050 C LEU C 162 29.248 -11.976 12.366 1.00 28.08 C ANISOU 3050 C LEU C 162 3861 3295 3514 -303 -149 49 C ATOM 3051 O LEU C 162 29.803 -13.075 12.326 1.00 26.46 O ANISOU 3051 O LEU C 162 3731 3030 3295 -288 -163 56 O ATOM 3052 CB LEU C 162 28.824 -10.906 14.609 1.00 31.79 C ANISOU 3052 CB LEU C 162 4229 3858 3993 -342 -143 58 C ATOM 3053 CG LEU C 162 28.697 -12.225 15.363 1.00 36.59 C ANISOU 3053 CG LEU C 162 4900 4434 4567 -385 -175 81 C ATOM 3054 CD1 LEU C 162 30.068 -12.692 15.870 1.00 31.71 C ANISOU 3054 CD1 LEU C 162 4312 3773 3963 -334 -184 91 C ATOM 3055 CD2 LEU C 162 27.708 -12.040 16.508 1.00 33.27 C ANISOU 3055 CD2 LEU C 162 4444 4074 4123 -452 -178 92 C ATOM 3056 N TRP C 163 28.252 -11.642 11.550 1.00 28.38 N ANISOU 3056 N TRP C 163 3885 3357 3539 -337 -150 44 N ATOM 3057 CA TRP C 163 27.780 -12.597 10.546 1.00 30.02 C ANISOU 3057 CA TRP C 163 4173 3521 3712 -371 -170 46 C ATOM 3058 C TRP C 163 28.904 -12.882 9.547 1.00 29.47 C ANISOU 3058 C TRP C 163 4159 3390 3650 -302 -152 29 C ATOM 3059 O TRP C 163 29.178 -14.040 9.240 1.00 29.55 O ANISOU 3059 O TRP C 163 4264 3331 3633 -301 -165 29 O ATOM 3060 CB TRP C 163 26.514 -12.102 9.826 1.00 28.27 C ANISOU 3060 CB TRP C 163 3917 3348 3476 -423 -178 50 C ATOM 3061 CG TRP C 163 25.913 -13.150 8.907 1.00 31.73 C ANISOU 3061 CG TRP C 163 4444 3746 3867 -480 -208 56 C ATOM 3062 CD1 TRP C 163 24.981 -14.084 9.234 1.00 37.23 C ANISOU 3062 CD1 TRP C 163 5183 4442 4520 -568 -244 78 C ATOM 3063 CD2 TRP C 163 26.215 -13.354 7.519 1.00 27.86 C ANISOU 3063 CD2 TRP C 163 4015 3209 3361 -461 -205 41 C ATOM 3064 NE1 TRP C 163 24.683 -14.868 8.137 1.00 40.43 N ANISOU 3064 NE1 TRP C 163 5678 4799 4883 -608 -268 76 N ATOM 3065 CE2 TRP C 163 25.422 -14.429 7.068 1.00 34.56 C ANISOU 3065 CE2 TRP C 163 4950 4026 4155 -541 -243 52 C ATOM 3066 CE3 TRP C 163 27.071 -12.723 6.613 1.00 30.72 C ANISOU 3066 CE3 TRP C 163 4371 3556 3746 -390 -174 20 C ATOM 3067 CZ2 TRP C 163 25.470 -14.896 5.763 1.00 37.91 C ANISOU 3067 CZ2 TRP C 163 5461 4400 4545 -551 -250 39 C ATOM 3068 CZ3 TRP C 163 27.116 -13.183 5.308 1.00 42.33 C ANISOU 3068 CZ3 TRP C 163 5921 4981 5183 -396 -177 8 C ATOM 3069 CH2 TRP C 163 26.316 -14.257 4.895 1.00 42.74 C ANISOU 3069 CH2 TRP C 163 6064 4997 5178 -475 -215 16 C ATOM 3070 N LEU C 164 29.567 -11.833 9.060 1.00 26.92 N ANISOU 3070 N LEU C 164 3780 3089 3361 -245 -121 15 N ATOM 3071 CA LEU C 164 30.698 -12.015 8.147 1.00 27.30 C ANISOU 3071 CA LEU C 164 3866 3091 3416 -176 -96 1 C ATOM 3072 C LEU C 164 31.842 -12.812 8.785 1.00 31.37 C ANISOU 3072 C LEU C 164 4415 3562 3941 -122 -92 7 C ATOM 3073 O LEU C 164 32.487 -13.620 8.126 1.00 31.28 O ANISOU 3073 O LEU C 164 4476 3492 3917 -77 -81 -1 O ATOM 3074 CB LEU C 164 31.223 -10.679 7.611 1.00 30.35 C ANISOU 3074 CB LEU C 164 4179 3516 3835 -134 -65 -10 C ATOM 3075 CG LEU C 164 30.352 -9.900 6.618 1.00 26.34 C ANISOU 3075 CG LEU C 164 3651 3038 3319 -164 -65 -16 C ATOM 3076 CD1 LEU C 164 30.923 -8.503 6.345 1.00 26.77 C ANISOU 3076 CD1 LEU C 164 3634 3130 3409 -125 -37 -21 C ATOM 3077 CD2 LEU C 164 30.196 -10.658 5.322 1.00 27.54 C ANISOU 3077 CD2 LEU C 164 3888 3144 3432 -174 -68 -25 C ATOM 3078 N ALA C 165 32.127 -12.551 10.053 1.00 27.96 N ANISOU 3078 N ALA C 165 3933 3161 3531 -120 -100 22 N ATOM 3079 CA ALA C 165 33.206 -13.272 10.720 1.00 29.33 C ANISOU 3079 CA ALA C 165 4129 3300 3715 -69 -103 36 C ATOM 3080 C ALA C 165 32.909 -14.767 10.759 1.00 30.61 C ANISOU 3080 C ALA C 165 4401 3388 3841 -87 -129 45 C ATOM 3081 O ALA C 165 33.773 -15.608 10.465 1.00 30.81 O ANISOU 3081 O ALA C 165 4488 3354 3865 -23 -121 46 O ATOM 3082 CB ALA C 165 33.400 -12.741 12.126 1.00 26.29 C ANISOU 3082 CB ALA C 165 3676 2963 3350 -83 -115 53 C ATOM 3083 N ARG C 166 31.693 -15.108 11.162 1.00 32.53 N ANISOU 3083 N ARG C 166 4670 3638 4052 -173 -160 52 N ATOM 3084 CA ARG C 166 31.305 -16.515 11.211 1.00 29.71 C ANISOU 3084 CA ARG C 166 4427 3209 3654 -209 -190 63 C ATOM 3085 C ARG C 166 31.440 -17.174 9.853 1.00 32.02 C ANISOU 3085 C ARG C 166 4815 3431 3921 -184 -179 43 C ATOM 3086 O ARG C 166 31.831 -18.334 9.760 1.00 31.08 O ANISOU 3086 O ARG C 166 4801 3227 3779 -158 -188 46 O ATOM 3087 CB ARG C 166 29.880 -16.661 11.738 1.00 31.91 C ANISOU 3087 CB ARG C 166 4707 3520 3898 -320 -224 77 C ATOM 3088 CG ARG C 166 29.772 -16.278 13.217 1.00 32.63 C ANISOU 3088 CG ARG C 166 4729 3667 4001 -347 -234 98 C ATOM 3089 CD ARG C 166 28.343 -16.201 13.705 1.00 33.94 C ANISOU 3089 CD ARG C 166 4872 3889 4137 -451 -254 110 C ATOM 3090 NE ARG C 166 28.278 -16.225 15.166 1.00 36.47 N ANISOU 3090 NE ARG C 166 5162 4242 4452 -482 -267 132 N ATOM 3091 CZ ARG C 166 27.186 -15.946 15.872 1.00 48.48 C ANISOU 3091 CZ ARG C 166 6637 5832 5953 -561 -272 144 C ATOM 3092 NH1 ARG C 166 26.062 -15.612 15.254 1.00 52.75 N ANISOU 3092 NH1 ARG C 166 7146 6417 6479 -612 -269 140 N ATOM 3093 NH2 ARG C 166 27.216 -15.999 17.198 1.00 49.18 N ANISOU 3093 NH2 ARG C 166 6708 5947 6032 -587 -280 161 N ATOM 3094 N LYS C 167 31.111 -16.437 8.797 1.00 29.36 N ANISOU 3094 N LYS C 167 4449 3124 3584 -190 -159 22 N ATOM 3095 CA LYS C 167 31.138 -16.997 7.449 1.00 29.43 C ANISOU 3095 CA LYS C 167 4552 3071 3559 -178 -147 0 C ATOM 3096 C LYS C 167 32.564 -17.187 6.944 1.00 31.94 C ANISOU 3096 C LYS C 167 4894 3346 3897 -63 -105 -15 C ATOM 3097 O LYS C 167 32.899 -18.213 6.357 1.00 31.45 O ANISOU 3097 O LYS C 167 4946 3199 3804 -30 -97 -27 O ATOM 3098 CB LYS C 167 30.365 -16.108 6.475 1.00 35.61 C ANISOU 3098 CB LYS C 167 5292 3905 4332 -222 -142 -12 C ATOM 3099 CG LYS C 167 28.869 -16.080 6.702 1.00 45.14 C ANISOU 3099 CG LYS C 167 6486 5154 5510 -334 -184 4 C ATOM 3100 CD LYS C 167 28.230 -17.394 6.272 1.00 47.59 C ANISOU 3100 CD LYS C 167 6932 5394 5758 -404 -219 7 C ATOM 3101 CE LYS C 167 28.570 -17.725 4.833 1.00 47.76 C ANISOU 3101 CE LYS C 167 7045 5355 5748 -377 -201 -21 C ATOM 3102 NZ LYS C 167 27.827 -18.941 4.393 1.00 51.69 N ANISOU 3102 NZ LYS C 167 7682 5783 6176 -461 -240 -20 N ATOM 3103 N LEU C 168 33.407 -16.198 7.192 1.00 28.90 N ANISOU 3103 N LEU C 168 4401 3019 3561 -2 -75 -13 N ATOM 3104 CA LEU C 168 34.767 -16.213 6.681 1.00 27.20 C ANISOU 3104 CA LEU C 168 4181 2785 3368 105 -30 -22 C ATOM 3105 C LEU C 168 35.629 -17.229 7.434 1.00 33.84 C ANISOU 3105 C LEU C 168 5066 3572 4219 171 -34 -3 C ATOM 3106 O LEU C 168 36.425 -17.963 6.838 1.00 36.63 O ANISOU 3106 O LEU C 168 5488 3865 4565 253 -5 -13 O ATOM 3107 CB LEU C 168 35.369 -14.802 6.812 1.00 25.46 C ANISOU 3107 CB LEU C 168 3826 2651 3195 133 -4 -18 C ATOM 3108 CG LEU C 168 34.760 -13.723 5.901 1.00 29.02 C ANISOU 3108 CG LEU C 168 4236 3149 3641 91 8 -34 C ATOM 3109 CD1 LEU C 168 35.115 -12.353 6.454 1.00 29.75 C ANISOU 3109 CD1 LEU C 168 4205 3322 3778 95 17 -24 C ATOM 3110 CD2 LEU C 168 35.257 -13.879 4.478 1.00 33.97 C ANISOU 3110 CD2 LEU C 168 4915 3746 4247 138 49 -58 C ATOM 3111 N ILE C 169 35.470 -17.262 8.752 1.00 32.31 N ANISOU 3111 N ILE C 169 4834 3400 4040 140 -70 25 N ATOM 3112 CA ILE C 169 36.241 -18.163 9.605 1.00 34.64 C ANISOU 3112 CA ILE C 169 5164 3652 4347 197 -85 51 C ATOM 3113 C ILE C 169 35.683 -19.578 9.543 1.00 36.77 C ANISOU 3113 C ILE C 169 5583 3820 4569 170 -113 52 C ATOM 3114 O ILE C 169 36.395 -20.553 9.795 1.00 34.69 O ANISOU 3114 O ILE C 169 5388 3486 4305 240 -116 66 O ATOM 3115 CB ILE C 169 36.232 -17.681 11.085 1.00 28.57 C ANISOU 3115 CB ILE C 169 4307 2944 3603 161 -118 84 C ATOM 3116 CG1 ILE C 169 36.808 -16.260 11.196 1.00 37.63 C ANISOU 3116 CG1 ILE C 169 5319 4186 4793 180 -93 83 C ATOM 3117 CG2 ILE C 169 37.009 -18.606 11.964 1.00 32.36 C ANISOU 3117 CG2 ILE C 169 4822 3380 4092 215 -140 117 C ATOM 3118 CD1 ILE C 169 38.193 -16.132 10.653 1.00 44.43 C ANISOU 3118 CD1 ILE C 169 6142 5054 5686 286 -53 86 C ATOM 3119 N GLY C 170 34.407 -19.698 9.191 1.00 33.32 N ANISOU 3119 N GLY C 170 5198 3372 4089 67 -137 39 N ATOM 3120 CA GLY C 170 33.776 -21.006 9.126 1.00 32.33 C ANISOU 3120 CA GLY C 170 5221 3152 3910 19 -170 41 C ATOM 3121 C GLY C 170 33.480 -21.554 10.515 1.00 42.08 C ANISOU 3121 C GLY C 170 6470 4379 5141 -30 -219 78 C ATOM 3122 O GLY C 170 33.684 -22.742 10.779 1.00 39.33 O ANISOU 3122 O GLY C 170 6238 3938 4769 -13 -241 92 O ATOM 3123 N ASP C 171 32.998 -20.686 11.405 1.00 36.56 N ANISOU 3123 N ASP C 171 5658 3773 4461 -91 -235 95 N ATOM 3124 CA ASP C 171 32.691 -21.092 12.782 1.00 34.19 C ANISOU 3124 CA ASP C 171 5360 3479 4152 -146 -278 131 C ATOM 3125 C ASP C 171 31.375 -20.447 13.206 1.00 34.44 C ANISOU 3125 C ASP C 171 5328 3593 4165 -266 -296 135 C ATOM 3126 O ASP C 171 31.330 -19.254 13.525 1.00 34.23 O ANISOU 3126 O ASP C 171 5179 3658 4170 -268 -278 130 O ATOM 3127 CB ASP C 171 33.823 -20.657 13.719 1.00 37.06 C ANISOU 3127 CB ASP C 171 5636 3882 4565 -68 -271 154 C ATOM 3128 CG ASP C 171 33.635 -21.141 15.143 1.00 41.73 C ANISOU 3128 CG ASP C 171 6239 4473 5142 -118 -316 194 C ATOM 3129 OD1 ASP C 171 32.560 -21.695 15.460 1.00 39.25 O ANISOU 3129 OD1 ASP C 171 5988 4142 4783 -220 -349 204 O ATOM 3130 OD2 ASP C 171 34.583 -20.975 15.950 1.00 43.25 O ANISOU 3130 OD2 ASP C 171 6378 4687 5367 -59 -321 219 O ATOM 3131 N PRO C 172 30.296 -21.227 13.212 1.00 34.03 N ANISOU 3131 N PRO C 172 5360 3509 4060 -367 -332 145 N ATOM 3132 CA PRO C 172 28.962 -20.680 13.498 1.00 37.57 C ANISOU 3132 CA PRO C 172 5746 4043 4488 -481 -346 151 C ATOM 3133 C PRO C 172 28.811 -20.256 14.959 1.00 38.18 C ANISOU 3133 C PRO C 172 5741 4191 4576 -514 -356 177 C ATOM 3134 O PRO C 172 27.843 -19.578 15.312 1.00 41.08 O ANISOU 3134 O PRO C 172 6028 4644 4935 -587 -355 180 O ATOM 3135 CB PRO C 172 28.024 -21.870 13.214 1.00 43.00 C ANISOU 3135 CB PRO C 172 6561 4667 5110 -581 -387 163 C ATOM 3136 CG PRO C 172 28.859 -22.883 12.468 1.00 51.60 C ANISOU 3136 CG PRO C 172 7789 5630 6187 -510 -386 150 C ATOM 3137 CD PRO C 172 30.258 -22.677 12.935 1.00 44.39 C ANISOU 3137 CD PRO C 172 6836 4704 5327 -382 -360 152 C ATOM 3138 N ASN C 173 29.761 -20.664 15.791 1.00 35.33 N ANISOU 3138 N ASN C 173 5401 3794 4231 -460 -366 196 N ATOM 3139 CA ASN C 173 29.722 -20.388 17.226 1.00 39.75 C ANISOU 3139 CA ASN C 173 5901 4410 4792 -493 -380 223 C ATOM 3140 C ASN C 173 30.680 -19.280 17.646 1.00 36.63 C ANISOU 3140 C ASN C 173 5396 4074 4449 -415 -352 215 C ATOM 3141 O ASN C 173 30.861 -19.014 18.838 1.00 36.71 O ANISOU 3141 O ASN C 173 5361 4125 4460 -432 -363 236 O ATOM 3142 CB ASN C 173 30.014 -21.661 18.010 1.00 43.39 C ANISOU 3142 CB ASN C 173 6467 4794 5224 -507 -423 260 C ATOM 3143 CG ASN C 173 29.081 -22.784 17.629 1.00 46.81 C ANISOU 3143 CG ASN C 173 7023 5162 5600 -597 -456 270 C ATOM 3144 OD1 ASN C 173 27.872 -22.576 17.521 1.00 45.61 O ANISOU 3144 OD1 ASN C 173 6847 5065 5416 -698 -460 269 O ATOM 3145 ND2 ASN C 173 29.634 -23.973 17.389 1.00 47.69 N ANISOU 3145 ND2 ASN C 173 7268 5156 5695 -558 -479 282 N ATOM 3146 N LEU C 174 31.296 -18.639 16.663 1.00 34.17 N ANISOU 3146 N LEU C 174 5044 3764 4174 -337 -317 187 N ATOM 3147 CA LEU C 174 32.165 -17.502 16.943 1.00 30.56 C ANISOU 3147 CA LEU C 174 4482 3366 3763 -275 -290 180 C ATOM 3148 C LEU C 174 31.346 -16.405 17.615 1.00 35.30 C ANISOU 3148 C LEU C 174 4993 4060 4361 -340 -280 172 C ATOM 3149 O LEU C 174 30.210 -16.137 17.220 1.00 33.18 O ANISOU 3149 O LEU C 174 4711 3822 4073 -400 -273 159 O ATOM 3150 CB LEU C 174 32.777 -16.993 15.639 1.00 38.74 C ANISOU 3150 CB LEU C 174 5495 4394 4831 -197 -253 151 C ATOM 3151 CG LEU C 174 34.048 -16.152 15.680 1.00 41.08 C ANISOU 3151 CG LEU C 174 5709 4724 5174 -114 -228 149 C ATOM 3152 CD1 LEU C 174 35.096 -16.819 16.530 1.00 45.83 C ANISOU 3152 CD1 LEU C 174 6327 5298 5786 -64 -251 184 C ATOM 3153 CD2 LEU C 174 34.561 -15.946 14.251 1.00 37.06 C ANISOU 3153 CD2 LEU C 174 5203 4194 4684 -46 -191 124 C ATOM 3154 N GLU C 175 31.913 -15.782 18.649 1.00 31.45 N ANISOU 3154 N GLU C 175 4444 3618 3889 -329 -280 182 N ATOM 3155 CA GLU C 175 31.239 -14.682 19.331 1.00 32.24 C ANISOU 3155 CA GLU C 175 4465 3800 3984 -380 -264 170 C ATOM 3156 C GLU C 175 32.216 -13.519 19.474 1.00 28.37 C ANISOU 3156 C GLU C 175 3898 3347 3532 -324 -242 158 C ATOM 3157 O GLU C 175 33.425 -13.731 19.453 1.00 33.35 O ANISOU 3157 O GLU C 175 4532 3953 4187 -262 -251 173 O ATOM 3158 CB GLU C 175 30.792 -15.110 20.736 1.00 35.17 C ANISOU 3158 CB GLU C 175 4854 4193 4317 -451 -290 197 C ATOM 3159 CG GLU C 175 29.856 -16.317 20.774 1.00 39.56 C ANISOU 3159 CG GLU C 175 5490 4713 4827 -522 -318 217 C ATOM 3160 CD GLU C 175 28.458 -15.995 20.277 1.00 52.23 C ANISOU 3160 CD GLU C 175 7070 6364 6413 -587 -300 200 C ATOM 3161 OE1 GLU C 175 28.183 -14.809 19.996 1.00 58.40 O ANISOU 3161 OE1 GLU C 175 7770 7204 7216 -570 -264 174 O ATOM 3162 OE2 GLU C 175 27.631 -16.930 20.166 1.00 57.94 O ANISOU 3162 OE2 GLU C 175 7854 7065 7097 -655 -323 218 O ATOM 3163 N PHE C 176 31.692 -12.300 19.608 1.00 26.58 N ANISOU 3163 N PHE C 176 3606 3182 3311 -346 -215 134 N ATOM 3164 CA PHE C 176 32.536 -11.170 20.008 1.00 25.87 C ANISOU 3164 CA PHE C 176 3454 3128 3246 -316 -200 126 C ATOM 3165 C PHE C 176 32.592 -11.151 21.535 1.00 33.67 C ANISOU 3165 C PHE C 176 4440 4147 4207 -362 -220 143 C ATOM 3166 O PHE C 176 31.554 -11.191 22.207 1.00 35.01 O ANISOU 3166 O PHE C 176 4617 4345 4342 -425 -216 140 O ATOM 3167 CB PHE C 176 32.008 -9.834 19.461 1.00 30.94 C ANISOU 3167 CB PHE C 176 4042 3811 3905 -313 -162 91 C ATOM 3168 CG PHE C 176 32.109 -9.687 17.950 1.00 31.07 C ANISOU 3168 CG PHE C 176 4056 3802 3947 -267 -144 76 C ATOM 3169 CD1 PHE C 176 33.056 -10.383 17.210 1.00 37.55 C ANISOU 3169 CD1 PHE C 176 4906 4576 4784 -214 -152 87 C ATOM 3170 CD2 PHE C 176 31.242 -8.836 17.268 1.00 28.96 C ANISOU 3170 CD2 PHE C 176 3758 3560 3685 -275 -119 53 C ATOM 3171 CE1 PHE C 176 33.124 -10.248 15.806 1.00 32.09 C ANISOU 3171 CE1 PHE C 176 4219 3864 4109 -176 -131 71 C ATOM 3172 CE2 PHE C 176 31.326 -8.675 15.868 1.00 30.40 C ANISOU 3172 CE2 PHE C 176 3942 3721 3886 -239 -105 41 C ATOM 3173 CZ PHE C 176 32.263 -9.372 15.139 1.00 25.69 C ANISOU 3173 CZ PHE C 176 3380 3079 3301 -193 -110 49 C ATOM 3174 N VAL C 177 33.807 -11.101 22.077 1.00 28.01 N ANISOU 3174 N VAL C 177 3711 3428 3502 -334 -240 163 N ATOM 3175 CA VAL C 177 34.028 -11.086 23.522 1.00 35.10 C ANISOU 3175 CA VAL C 177 4611 4354 4371 -379 -264 184 C ATOM 3176 C VAL C 177 33.469 -9.791 24.126 1.00 39.33 C ANISOU 3176 C VAL C 177 5108 4946 4890 -421 -235 152 C ATOM 3177 O VAL C 177 32.932 -9.781 25.236 1.00 35.85 O ANISOU 3177 O VAL C 177 4679 4533 4407 -481 -239 154 O ATOM 3178 CB VAL C 177 35.540 -11.193 23.838 1.00 36.17 C ANISOU 3178 CB VAL C 177 4731 4485 4529 -335 -295 216 C ATOM 3179 CG1 VAL C 177 35.815 -10.954 25.317 1.00 38.19 C ANISOU 3179 CG1 VAL C 177 4982 4777 4750 -389 -323 236 C ATOM 3180 CG2 VAL C 177 36.077 -12.559 23.403 1.00 40.54 C ANISOU 3180 CG2 VAL C 177 5330 4978 5094 -284 -323 251 C ATOM 3181 N ALA C 178 33.600 -8.698 23.382 1.00 29.74 N ANISOU 3181 N ALA C 178 3850 3743 3705 -389 -203 122 N ATOM 3182 CA ALA C 178 33.113 -7.412 23.852 1.00 32.00 C ANISOU 3182 CA ALA C 178 4110 4070 3978 -417 -171 88 C ATOM 3183 C ALA C 178 32.841 -6.527 22.648 1.00 26.35 C ANISOU 3183 C ALA C 178 3364 3351 3296 -377 -135 58 C ATOM 3184 O ALA C 178 33.400 -6.738 21.577 1.00 31.57 O ANISOU 3184 O ALA C 178 4018 3985 3991 -330 -138 64 O ATOM 3185 CB ALA C 178 34.141 -6.756 24.761 1.00 31.72 C ANISOU 3185 CB ALA C 178 4063 4054 3934 -431 -189 95 C ATOM 3186 N MET C 179 31.995 -5.521 22.819 1.00 29.57 N ANISOU 3186 N MET C 179 3755 3785 3693 -392 -100 25 N ATOM 3187 CA MET C 179 31.788 -4.562 21.727 1.00 32.30 C ANISOU 3187 CA MET C 179 4074 4126 4071 -353 -69 0 C ATOM 3188 C MET C 179 33.011 -3.651 21.597 1.00 31.99 C ANISOU 3188 C MET C 179 4021 4079 4053 -332 -73 -4 C ATOM 3189 O MET C 179 33.640 -3.309 22.601 1.00 34.47 O ANISOU 3189 O MET C 179 4342 4406 4348 -361 -87 -1 O ATOM 3190 CB MET C 179 30.534 -3.723 21.990 1.00 31.65 C ANISOU 3190 CB MET C 179 3979 4073 3973 -365 -30 -30 C ATOM 3191 CG MET C 179 29.239 -4.540 21.990 1.00 38.18 C ANISOU 3191 CG MET C 179 4805 4922 4780 -390 -24 -22 C ATOM 3192 SD MET C 179 28.710 -4.926 20.301 1.00 48.95 S ANISOU 3192 SD MET C 179 6155 6267 6175 -358 -25 -16 S ATOM 3193 CE MET C 179 28.598 -3.287 19.599 1.00 37.96 C ANISOU 3193 CE MET C 179 4729 4878 4814 -310 11 -46 C ATOM 3194 N PRO C 180 33.347 -3.241 20.364 1.00 31.54 N ANISOU 3194 N PRO C 180 3947 4005 4032 -291 -62 -9 N ATOM 3195 CA PRO C 180 34.421 -2.259 20.168 1.00 32.17 C ANISOU 3195 CA PRO C 180 4010 4083 4129 -280 -63 -12 C ATOM 3196 C PRO C 180 34.004 -0.958 20.795 1.00 27.48 C ANISOU 3196 C PRO C 180 3425 3499 3518 -304 -40 -43 C ATOM 3197 O PRO C 180 32.827 -0.766 21.057 1.00 30.53 O ANISOU 3197 O PRO C 180 3819 3893 3889 -309 -15 -64 O ATOM 3198 CB PRO C 180 34.480 -2.084 18.650 1.00 38.80 C ANISOU 3198 CB PRO C 180 4835 4904 5003 -236 -47 -15 C ATOM 3199 CG PRO C 180 33.674 -3.219 18.078 1.00 40.72 C ANISOU 3199 CG PRO C 180 5091 5135 5245 -223 -49 -9 C ATOM 3200 CD PRO C 180 32.662 -3.577 19.103 1.00 41.54 C ANISOU 3200 CD PRO C 180 5210 5256 5317 -261 -49 -13 C ATOM 3201 N ALA C 181 34.966 -0.088 21.070 1.00 30.17 N ANISOU 3201 N ALA C 181 3765 3840 3858 -320 -48 -44 N ATOM 3202 CA ALA C 181 34.647 1.228 21.596 1.00 32.55 C ANISOU 3202 CA ALA C 181 4091 4136 4140 -341 -26 -77 C ATOM 3203 C ALA C 181 34.019 2.020 20.469 1.00 31.66 C ANISOU 3203 C ALA C 181 3974 4002 4053 -301 6 -98 C ATOM 3204 O ALA C 181 34.635 2.201 19.424 1.00 26.57 O ANISOU 3204 O ALA C 181 3312 3346 3438 -279 1 -86 O ATOM 3205 CB ALA C 181 35.903 1.906 22.099 1.00 29.30 C ANISOU 3205 CB ALA C 181 3687 3728 3718 -380 -51 -68 C ATOM 3206 N LEU C 182 32.791 2.481 20.678 1.00 28.43 N ANISOU 3206 N LEU C 182 3578 3591 3633 -288 39 -126 N ATOM 3207 CA LEU C 182 32.056 3.218 19.639 1.00 27.33 C ANISOU 3207 CA LEU C 182 3432 3434 3519 -244 67 -141 C ATOM 3208 C LEU C 182 31.805 4.669 20.044 1.00 32.00 C ANISOU 3208 C LEU C 182 4060 4001 4096 -241 94 -174 C ATOM 3209 O LEU C 182 31.681 4.978 21.222 1.00 28.65 O ANISOU 3209 O LEU C 182 3667 3581 3637 -268 105 -194 O ATOM 3210 CB LEU C 182 30.705 2.556 19.367 1.00 27.33 C ANISOU 3210 CB LEU C 182 3407 3455 3520 -221 84 -140 C ATOM 3211 CG LEU C 182 30.728 1.079 18.978 1.00 32.74 C ANISOU 3211 CG LEU C 182 4073 4155 4212 -228 58 -111 C ATOM 3212 CD1 LEU C 182 29.315 0.587 18.688 1.00 35.64 C ANISOU 3212 CD1 LEU C 182 4419 4547 4577 -218 73 -109 C ATOM 3213 CD2 LEU C 182 31.645 0.886 17.777 1.00 29.47 C ANISOU 3213 CD2 LEU C 182 3650 3719 3827 -208 39 -92 C ATOM 3214 N ALA C 183 31.705 5.555 19.058 1.00 32.39 N ANISOU 3214 N ALA C 183 4114 4021 4172 -207 106 -180 N ATOM 3215 CA ALA C 183 31.226 6.907 19.323 1.00 30.52 C ANISOU 3215 CA ALA C 183 3920 3752 3925 -189 137 -212 C ATOM 3216 C ALA C 183 29.849 6.786 19.971 1.00 33.95 C ANISOU 3216 C ALA C 183 4347 4210 4343 -161 174 -232 C ATOM 3217 O ALA C 183 29.028 5.969 19.548 1.00 33.49 O ANISOU 3217 O ALA C 183 4241 4186 4299 -139 177 -216 O ATOM 3218 CB ALA C 183 31.142 7.685 18.026 1.00 32.71 C ANISOU 3218 CB ALA C 183 4198 3996 4235 -150 141 -207 C ATOM 3219 N PRO C 184 29.596 7.575 21.026 1.00 34.25 N ANISOU 3219 N PRO C 184 4433 4233 4347 -166 203 -266 N ATOM 3220 CA PRO C 184 28.324 7.479 21.748 1.00 36.51 C ANISOU 3220 CA PRO C 184 4709 4551 4612 -138 247 -286 C ATOM 3221 C PRO C 184 27.164 7.812 20.826 1.00 34.00 C ANISOU 3221 C PRO C 184 4352 4239 4328 -65 274 -282 C ATOM 3222 O PRO C 184 27.321 8.643 19.928 1.00 34.80 O ANISOU 3222 O PRO C 184 4469 4297 4458 -31 271 -281 O ATOM 3223 CB PRO C 184 28.449 8.557 22.836 1.00 44.22 C ANISOU 3223 CB PRO C 184 5763 5493 5547 -149 277 -329 C ATOM 3224 CG PRO C 184 29.899 8.768 23.007 1.00 44.33 C ANISOU 3224 CG PRO C 184 5820 5475 5547 -213 233 -323 C ATOM 3225 CD PRO C 184 30.555 8.480 21.688 1.00 36.93 C ANISOU 3225 CD PRO C 184 4842 4533 4658 -208 195 -286 C ATOM 3226 N PRO C 185 26.012 7.166 21.032 1.00 34.47 N ANISOU 3226 N PRO C 185 4359 4355 4383 -46 298 -275 N ATOM 3227 CA PRO C 185 24.863 7.437 20.156 1.00 32.09 C ANISOU 3227 CA PRO C 185 4008 4072 4114 21 319 -263 C ATOM 3228 C PRO C 185 24.546 8.928 20.092 1.00 38.40 C ANISOU 3228 C PRO C 185 4849 4822 4921 88 357 -292 C ATOM 3229 O PRO C 185 24.561 9.596 21.128 1.00 42.44 O ANISOU 3229 O PRO C 185 5416 5312 5399 92 393 -329 O ATOM 3230 CB PRO C 185 23.722 6.691 20.847 1.00 35.66 C ANISOU 3230 CB PRO C 185 4407 4599 4544 20 348 -259 C ATOM 3231 CG PRO C 185 24.401 5.560 21.567 1.00 41.97 C ANISOU 3231 CG PRO C 185 5216 5419 5313 -60 318 -250 C ATOM 3232 CD PRO C 185 25.742 6.082 21.996 1.00 35.49 C ANISOU 3232 CD PRO C 185 4467 4540 4478 -92 299 -270 C ATOM 3233 N GLU C 186 24.279 9.434 18.891 1.00 38.76 N ANISOU 3233 N GLU C 186 4877 4844 5006 138 347 -273 N ATOM 3234 CA GLU C 186 23.894 10.835 18.699 1.00 37.69 C ANISOU 3234 CA GLU C 186 4782 4655 4882 211 380 -293 C ATOM 3235 C GLU C 186 22.375 10.975 18.739 1.00 46.41 C ANISOU 3235 C GLU C 186 5826 5812 5998 290 425 -288 C ATOM 3236 O GLU C 186 21.830 12.054 19.012 1.00 48.13 O ANISOU 3236 O GLU C 186 6075 5996 6214 364 470 -312 O ATOM 3237 CB GLU C 186 24.390 11.342 17.347 1.00 42.35 C ANISOU 3237 CB GLU C 186 5387 5196 5510 225 343 -269 C ATOM 3238 CG GLU C 186 25.897 11.406 17.182 1.00 52.80 C ANISOU 3238 CG GLU C 186 6765 6471 6825 156 303 -270 C ATOM 3239 CD GLU C 186 26.285 12.036 15.854 1.00 67.49 C ANISOU 3239 CD GLU C 186 8641 8284 8717 172 276 -247 C ATOM 3240 OE1 GLU C 186 25.535 12.909 15.367 1.00 71.53 O ANISOU 3240 OE1 GLU C 186 9162 8768 9247 242 294 -244 O ATOM 3241 OE2 GLU C 186 27.332 11.659 15.295 1.00 73.29 O ANISOU 3241 OE2 GLU C 186 9379 9012 9456 118 238 -229 O ATOM 3242 N VAL C 187 21.697 9.883 18.410 1.00 38.70 N ANISOU 3242 N VAL C 187 4759 4914 5029 275 410 -253 N ATOM 3243 CA VAL C 187 20.251 9.803 18.522 1.00 45.31 C ANISOU 3243 CA VAL C 187 5519 5825 5873 333 449 -239 C ATOM 3244 C VAL C 187 19.905 8.543 19.289 1.00 47.07 C ANISOU 3244 C VAL C 187 5691 6130 6065 270 452 -230 C ATOM 3245 O VAL C 187 20.683 7.581 19.311 1.00 41.86 O ANISOU 3245 O VAL C 187 5043 5469 5391 189 409 -220 O ATOM 3246 CB VAL C 187 19.555 9.765 17.143 1.00 46.33 C ANISOU 3246 CB VAL C 187 5579 5980 6045 373 420 -190 C ATOM 3247 CG1 VAL C 187 19.911 11.002 16.324 1.00 53.74 C ANISOU 3247 CG1 VAL C 187 6572 6834 7013 431 412 -193 C ATOM 3248 CG2 VAL C 187 19.919 8.491 16.393 1.00 44.38 C ANISOU 3248 CG2 VAL C 187 5297 5764 5803 294 360 -154 C ATOM 3249 N VAL C 188 18.742 8.554 19.927 1.00 48.91 N ANISOU 3249 N VAL C 188 5869 6433 6283 309 504 -232 N ATOM 3250 CA VAL C 188 18.270 7.402 20.679 1.00 52.25 C ANISOU 3250 CA VAL C 188 6240 6941 6672 247 511 -219 C ATOM 3251 C VAL C 188 17.480 6.463 19.774 1.00 45.69 C ANISOU 3251 C VAL C 188 5314 6185 5862 225 475 -163 C ATOM 3252 O VAL C 188 16.616 6.901 19.021 1.00 54.92 O ANISOU 3252 O VAL C 188 6420 7384 7062 289 481 -136 O ATOM 3253 CB VAL C 188 17.375 7.833 21.859 1.00 62.50 C ANISOU 3253 CB VAL C 188 7521 8290 7937 292 591 -247 C ATOM 3254 CG1 VAL C 188 16.780 6.613 22.551 1.00 59.65 C ANISOU 3254 CG1 VAL C 188 7097 8028 7539 222 597 -226 C ATOM 3255 CG2 VAL C 188 18.166 8.687 22.844 1.00 63.14 C ANISOU 3255 CG2 VAL C 188 7712 8294 7985 300 626 -307 C ATOM 3256 N MET C 189 17.798 5.172 19.834 1.00 45.46 N ANISOU 3256 N MET C 189 5278 6182 5813 132 432 -142 N ATOM 3257 CA MET C 189 16.994 4.159 19.154 1.00 40.57 C ANISOU 3257 CA MET C 189 4578 5637 5199 92 398 -91 C ATOM 3258 C MET C 189 16.016 3.576 20.170 1.00 43.85 C ANISOU 3258 C MET C 189 4935 6151 5576 61 437 -81 C ATOM 3259 O MET C 189 16.406 2.827 21.060 1.00 47.20 O ANISOU 3259 O MET C 189 5392 6581 5960 -9 435 -92 O ATOM 3260 CB MET C 189 17.877 3.053 18.573 1.00 33.11 C ANISOU 3260 CB MET C 189 3672 4657 4252 9 330 -73 C ATOM 3261 CG MET C 189 17.116 1.978 17.814 1.00 39.13 C ANISOU 3261 CG MET C 189 4372 5481 5012 -43 288 -22 C ATOM 3262 SD MET C 189 16.368 2.653 16.317 1.00 42.30 S ANISOU 3262 SD MET C 189 4714 5900 5460 21 269 13 S ATOM 3263 CE MET C 189 15.340 1.283 15.776 1.00 51.33 C ANISOU 3263 CE MET C 189 5785 7135 6582 -65 224 73 C ATOM 3264 N ASP C 190 14.748 3.944 20.043 1.00 52.90 N ANISOU 3264 N ASP C 190 5989 7378 6732 116 473 -58 N ATOM 3265 CA ASP C 190 13.713 3.473 20.952 1.00 56.44 C ANISOU 3265 CA ASP C 190 6365 7935 7144 92 517 -45 C ATOM 3266 C ASP C 190 13.693 1.949 21.003 1.00 55.78 C ANISOU 3266 C ASP C 190 6271 7896 7029 -32 467 -9 C ATOM 3267 O ASP C 190 13.483 1.297 19.981 1.00 50.79 O ANISOU 3267 O ASP C 190 5607 7278 6412 -73 408 34 O ATOM 3268 CB ASP C 190 12.351 4.003 20.507 1.00 67.46 C ANISOU 3268 CB ASP C 190 7646 9421 8565 168 550 -10 C ATOM 3269 CG ASP C 190 11.210 3.417 21.305 1.00 78.33 C ANISOU 3269 CG ASP C 190 8929 10930 9904 134 592 16 C ATOM 3270 OD1 ASP C 190 11.368 3.250 22.533 1.00 82.26 O ANISOU 3270 OD1 ASP C 190 9461 11439 10355 105 637 -17 O ATOM 3271 OD2 ASP C 190 10.156 3.124 20.702 1.00 83.21 O ANISOU 3271 OD2 ASP C 190 9437 11646 10535 132 578 72 O ATOM 3272 N PRO C 191 13.913 1.377 22.196 1.00 57.33 N ANISOU 3272 N PRO C 191 6500 8108 7175 -94 487 -27 N ATOM 3273 CA PRO C 191 13.984 -0.079 22.381 1.00 54.06 C ANISOU 3273 CA PRO C 191 6096 7721 6725 -214 439 5 C ATOM 3274 C PRO C 191 12.703 -0.790 21.951 1.00 57.72 C ANISOU 3274 C PRO C 191 6454 8297 7181 -260 425 64 C ATOM 3275 O PRO C 191 12.763 -1.931 21.495 1.00 56.16 O ANISOU 3275 O PRO C 191 6269 8100 6969 -352 362 100 O ATOM 3276 CB PRO C 191 14.186 -0.231 23.894 1.00 56.19 C ANISOU 3276 CB PRO C 191 6405 8005 6940 -249 483 -25 C ATOM 3277 CG PRO C 191 14.773 1.066 24.333 1.00 60.11 C ANISOU 3277 CG PRO C 191 6956 8435 7446 -162 531 -82 C ATOM 3278 CD PRO C 191 14.148 2.107 23.453 1.00 61.07 C ANISOU 3278 CD PRO C 191 7019 8567 7619 -56 555 -79 C ATOM 3279 N ALA C 192 11.562 -0.127 22.106 1.00 59.08 N ANISOU 3279 N ALA C 192 6527 8562 7358 -198 483 76 N ATOM 3280 CA ALA C 192 10.289 -0.697 21.680 1.00 61.87 C ANISOU 3280 CA ALA C 192 6764 9038 7706 -240 470 139 C ATOM 3281 C ALA C 192 10.226 -0.783 20.158 1.00 58.08 C ANISOU 3281 C ALA C 192 6264 8536 7268 -237 401 177 C ATOM 3282 O ALA C 192 9.809 -1.801 19.603 1.00 55.72 O ANISOU 3282 O ALA C 192 5936 8281 6953 -332 343 226 O ATOM 3283 CB ALA C 192 9.127 0.125 22.217 1.00 62.02 C ANISOU 3283 CB ALA C 192 6674 9168 7725 -157 555 144 C ATOM 3284 N LEU C 193 10.648 0.288 19.492 1.00 55.12 N ANISOU 3284 N LEU C 193 5911 8090 6942 -135 405 153 N ATOM 3285 CA LEU C 193 10.664 0.336 18.033 1.00 54.24 C ANISOU 3285 CA LEU C 193 5790 7950 6869 -125 342 184 C ATOM 3286 C LEU C 193 11.592 -0.732 17.465 1.00 49.87 C ANISOU 3286 C LEU C 193 5329 7317 6301 -222 267 187 C ATOM 3287 O LEU C 193 11.243 -1.433 16.513 1.00 49.75 O ANISOU 3287 O LEU C 193 5294 7326 6284 -284 206 231 O ATOM 3288 CB LEU C 193 11.088 1.722 17.544 1.00 53.08 C ANISOU 3288 CB LEU C 193 5670 7727 6772 0 364 153 C ATOM 3289 CG LEU C 193 11.077 1.899 16.027 1.00 55.83 C ANISOU 3289 CG LEU C 193 6008 8048 7157 16 302 188 C ATOM 3290 CD1 LEU C 193 9.659 1.752 15.503 1.00 55.45 C ANISOU 3290 CD1 LEU C 193 5826 8127 7114 13 290 255 C ATOM 3291 CD2 LEU C 193 11.672 3.240 15.618 1.00 59.01 C ANISOU 3291 CD2 LEU C 193 6459 8359 7603 128 321 154 C ATOM 3292 N ALA C 194 12.775 -0.857 18.059 1.00 47.13 N ANISOU 3292 N ALA C 194 5086 6878 5943 -235 270 140 N ATOM 3293 CA ALA C 194 13.718 -1.895 17.659 1.00 44.60 C ANISOU 3293 CA ALA C 194 4856 6482 5609 -315 208 140 C ATOM 3294 C ALA C 194 13.077 -3.277 17.784 1.00 47.10 C ANISOU 3294 C ALA C 194 5152 6863 5881 -433 171 184 C ATOM 3295 O ALA C 194 13.194 -4.107 16.884 1.00 43.45 O ANISOU 3295 O ALA C 194 4722 6375 5413 -496 109 210 O ATOM 3296 CB ALA C 194 14.974 -1.820 18.505 1.00 38.08 C ANISOU 3296 CB ALA C 194 4126 5570 4774 -309 223 90 C ATOM 3297 N ALA C 195 12.401 -3.517 18.905 1.00 48.48 N ANISOU 3297 N ALA C 195 5280 7120 6020 -467 211 192 N ATOM 3298 CA ALA C 195 11.711 -4.786 19.130 1.00 52.52 C ANISOU 3298 CA ALA C 195 5771 7702 6484 -588 180 237 C ATOM 3299 C ALA C 195 10.683 -5.061 18.032 1.00 49.77 C ANISOU 3299 C ALA C 195 5343 7427 6141 -624 138 295 C ATOM 3300 O ALA C 195 10.634 -6.156 17.470 1.00 50.54 O ANISOU 3300 O ALA C 195 5477 7513 6212 -724 74 327 O ATOM 3301 CB ALA C 195 11.041 -4.791 20.497 1.00 54.12 C ANISOU 3301 CB ALA C 195 5919 7996 6646 -608 241 238 C ATOM 3302 N GLN C 196 9.864 -4.059 17.737 1.00 45.44 N ANISOU 3302 N GLN C 196 4688 6952 5624 -542 173 309 N ATOM 3303 CA GLN C 196 8.851 -4.174 16.696 1.00 50.65 C ANISOU 3303 CA GLN C 196 5259 7694 6292 -567 132 369 C ATOM 3304 C GLN C 196 9.467 -4.465 15.335 1.00 47.42 C ANISOU 3304 C GLN C 196 4924 7194 5899 -588 58 374 C ATOM 3305 O GLN C 196 8.980 -5.318 14.593 1.00 49.54 O ANISOU 3305 O GLN C 196 5185 7495 6143 -683 -5 421 O ATOM 3306 CB GLN C 196 8.025 -2.893 16.608 1.00 49.61 C ANISOU 3306 CB GLN C 196 5008 7641 6201 -448 185 380 C ATOM 3307 CG GLN C 196 7.074 -2.876 15.427 1.00 61.65 C ANISOU 3307 CG GLN C 196 6438 9244 7741 -461 136 446 C ATOM 3308 CD GLN C 196 6.409 -1.532 15.234 1.00 71.73 C ANISOU 3308 CD GLN C 196 7610 10578 9067 -323 183 456 C ATOM 3309 OE1 GLN C 196 6.620 -0.605 16.014 1.00 75.08 O ANISOU 3309 OE1 GLN C 196 8036 10981 9511 -217 259 411 O ATOM 3310 NE2 GLN C 196 5.597 -1.419 14.189 1.00 79.59 N ANISOU 3310 NE2 GLN C 196 8518 11643 10079 -324 137 518 N ATOM 3311 N TYR C 197 10.527 -3.733 14.999 1.00 43.59 N ANISOU 3311 N TYR C 197 4512 6598 5452 -502 67 326 N ATOM 3312 CA TYR C 197 11.204 -3.929 13.725 1.00 45.17 C ANISOU 3312 CA TYR C 197 4787 6709 5665 -512 7 325 C ATOM 3313 C TYR C 197 11.776 -5.339 13.620 1.00 41.88 C ANISOU 3313 C TYR C 197 4472 6233 5206 -625 -46 326 C ATOM 3314 O TYR C 197 11.712 -5.966 12.566 1.00 41.68 O ANISOU 3314 O TYR C 197 4480 6189 5166 -685 -106 352 O ATOM 3315 CB TYR C 197 12.303 -2.882 13.515 1.00 40.97 C ANISOU 3315 CB TYR C 197 4316 6074 5178 -405 32 273 C ATOM 3316 CG TYR C 197 11.770 -1.525 13.106 1.00 38.31 C ANISOU 3316 CG TYR C 197 3901 5770 4885 -296 61 281 C ATOM 3317 CD1 TYR C 197 10.507 -1.399 12.544 1.00 43.95 C ANISOU 3317 CD1 TYR C 197 4505 6589 5604 -298 44 339 C ATOM 3318 CD2 TYR C 197 12.535 -0.375 13.268 1.00 45.67 C ANISOU 3318 CD2 TYR C 197 4872 6627 5853 -192 101 235 C ATOM 3319 CE1 TYR C 197 10.012 -0.165 12.165 1.00 46.90 C ANISOU 3319 CE1 TYR C 197 4809 6990 6020 -189 68 351 C ATOM 3320 CE2 TYR C 197 12.050 0.870 12.882 1.00 45.59 C ANISOU 3320 CE2 TYR C 197 4803 6636 5882 -89 126 243 C ATOM 3321 CZ TYR C 197 10.786 0.965 12.335 1.00 48.15 C ANISOU 3321 CZ TYR C 197 5018 7063 6214 -83 110 302 C ATOM 3322 OH TYR C 197 10.287 2.191 11.947 1.00 47.19 O ANISOU 3322 OH TYR C 197 4838 6959 6134 28 132 315 O ATOM 3323 N GLU C 198 12.330 -5.833 14.721 1.00 38.06 N ANISOU 3323 N GLU C 198 4044 5719 4700 -653 -23 298 N ATOM 3324 CA GLU C 198 12.919 -7.166 14.741 1.00 41.10 C ANISOU 3324 CA GLU C 198 4533 6038 5045 -748 -70 299 C ATOM 3325 C GLU C 198 11.835 -8.221 14.545 1.00 47.92 C ANISOU 3325 C GLU C 198 5366 6982 5861 -872 -115 356 C ATOM 3326 O GLU C 198 12.047 -9.231 13.876 1.00 46.02 O ANISOU 3326 O GLU C 198 5206 6688 5590 -952 -173 370 O ATOM 3327 CB GLU C 198 13.696 -7.390 16.048 1.00 43.30 C ANISOU 3327 CB GLU C 198 4868 6274 5309 -747 -37 263 C ATOM 3328 CG GLU C 198 15.029 -6.629 16.080 1.00 44.03 C ANISOU 3328 CG GLU C 198 5022 6266 5440 -652 -14 210 C ATOM 3329 CD GLU C 198 15.511 -6.291 17.486 1.00 49.10 C ANISOU 3329 CD GLU C 198 5677 6902 6076 -624 35 177 C ATOM 3330 OE1 GLU C 198 14.923 -6.799 18.464 1.00 51.66 O ANISOU 3330 OE1 GLU C 198 5978 7289 6362 -684 50 193 O ATOM 3331 OE2 GLU C 198 16.482 -5.506 17.607 1.00 40.50 O ANISOU 3331 OE2 GLU C 198 4623 5748 5016 -548 58 136 O ATOM 3332 N HIS C 199 10.666 -7.969 15.120 1.00 50.01 N ANISOU 3332 N HIS C 199 5513 7374 6115 -888 -85 390 N ATOM 3333 CA HIS C 199 9.532 -8.863 14.953 1.00 48.66 C ANISOU 3333 CA HIS C 199 5292 7299 5898 -1012 -127 452 C ATOM 3334 C HIS C 199 9.006 -8.772 13.528 1.00 47.70 C ANISOU 3334 C HIS C 199 5137 7200 5785 -1027 -181 490 C ATOM 3335 O HIS C 199 8.717 -9.790 12.909 1.00 48.52 O ANISOU 3335 O HIS C 199 5287 7302 5847 -1143 -247 524 O ATOM 3336 CB HIS C 199 8.428 -8.517 15.952 1.00 49.70 C ANISOU 3336 CB HIS C 199 5291 7575 6018 -1014 -73 480 C ATOM 3337 CG HIS C 199 7.205 -9.369 15.819 1.00 61.29 C ANISOU 3337 CG HIS C 199 6689 9161 7437 -1147 -113 551 C ATOM 3338 ND1 HIS C 199 7.172 -10.691 16.209 1.00 63.79 N ANISOU 3338 ND1 HIS C 199 7078 9466 7691 -1287 -154 573 N ATOM 3339 CD2 HIS C 199 5.969 -9.085 15.344 1.00 61.78 C ANISOU 3339 CD2 HIS C 199 6614 9358 7501 -1164 -123 610 C ATOM 3340 CE1 HIS C 199 5.969 -11.185 15.976 1.00 66.81 C ANISOU 3340 CE1 HIS C 199 7375 9972 8038 -1394 -187 641 C ATOM 3341 NE2 HIS C 199 5.219 -10.232 15.454 1.00 64.89 N ANISOU 3341 NE2 HIS C 199 6997 9825 7833 -1321 -169 667 N ATOM 3342 N ASP C 200 8.902 -7.551 13.006 1.00 43.96 N ANISOU 3342 N ASP C 200 4595 6745 5364 -914 -156 483 N ATOM 3343 CA ASP C 200 8.455 -7.339 11.627 1.00 40.12 C ANISOU 3343 CA ASP C 200 4077 6277 4889 -918 -208 520 C ATOM 3344 C ASP C 200 9.313 -8.115 10.629 1.00 44.36 C ANISOU 3344 C ASP C 200 4757 6694 5406 -973 -270 503 C ATOM 3345 O ASP C 200 8.805 -8.626 9.626 1.00 44.60 O ANISOU 3345 O ASP C 200 4793 6746 5408 -1054 -334 545 O ATOM 3346 CB ASP C 200 8.466 -5.850 11.266 1.00 47.19 C ANISOU 3346 CB ASP C 200 4904 7180 5848 -772 -169 506 C ATOM 3347 CG ASP C 200 7.406 -5.062 12.012 1.00 54.57 C ANISOU 3347 CG ASP C 200 5687 8247 6802 -712 -112 533 C ATOM 3348 OD1 ASP C 200 6.468 -5.687 12.550 1.00 58.99 O ANISOU 3348 OD1 ASP C 200 6171 8918 7324 -796 -114 577 O ATOM 3349 OD2 ASP C 200 7.518 -3.820 12.067 1.00 58.20 O ANISOU 3349 OD2 ASP C 200 6106 8697 7311 -579 -63 510 O ATOM 3350 N LEU C 201 10.613 -8.197 10.900 1.00 39.85 N ANISOU 3350 N LEU C 201 4299 5998 4845 -929 -250 444 N ATOM 3351 CA LEU C 201 11.513 -8.963 10.043 1.00 38.92 C ANISOU 3351 CA LEU C 201 4320 5762 4707 -969 -297 423 C ATOM 3352 C LEU C 201 11.272 -10.468 10.179 1.00 40.30 C ANISOU 3352 C LEU C 201 4571 5926 4816 -1111 -346 447 C ATOM 3353 O LEU C 201 11.322 -11.199 9.186 1.00 44.89 O ANISOU 3353 O LEU C 201 5234 6460 5364 -1181 -404 459 O ATOM 3354 CB LEU C 201 12.976 -8.625 10.332 1.00 40.60 C ANISOU 3354 CB LEU C 201 4621 5856 4951 -879 -260 359 C ATOM 3355 CG LEU C 201 13.454 -7.299 9.725 1.00 40.41 C ANISOU 3355 CG LEU C 201 4569 5803 4981 -758 -233 334 C ATOM 3356 CD1 LEU C 201 14.741 -6.833 10.363 1.00 36.76 C ANISOU 3356 CD1 LEU C 201 4163 5255 4550 -675 -187 278 C ATOM 3357 CD2 LEU C 201 13.609 -7.427 8.209 1.00 40.50 C ANISOU 3357 CD2 LEU C 201 4632 5771 4985 -776 -283 345 C ATOM 3358 N GLU C 202 11.016 -10.925 11.402 1.00 46.75 N ANISOU 3358 N GLU C 202 5370 6783 5611 -1155 -324 453 N ATOM 3359 CA GLU C 202 10.694 -12.334 11.624 1.00 47.81 C ANISOU 3359 CA GLU C 202 5575 6912 5680 -1297 -372 482 C ATOM 3360 C GLU C 202 9.426 -12.709 10.862 1.00 46.71 C ANISOU 3360 C GLU C 202 5375 6870 5502 -1407 -428 547 C ATOM 3361 O GLU C 202 9.380 -13.726 10.171 1.00 48.35 O ANISOU 3361 O GLU C 202 5682 7031 5660 -1514 -492 564 O ATOM 3362 CB GLU C 202 10.512 -12.629 13.117 1.00 46.09 C ANISOU 3362 CB GLU C 202 5331 6739 5444 -1327 -335 485 C ATOM 3363 CG GLU C 202 11.763 -12.394 13.949 1.00 49.16 C ANISOU 3363 CG GLU C 202 5786 7033 5859 -1239 -289 427 C ATOM 3364 CD GLU C 202 11.498 -12.469 15.444 1.00 59.24 C ANISOU 3364 CD GLU C 202 7021 8370 7118 -1260 -246 431 C ATOM 3365 OE1 GLU C 202 10.316 -12.429 15.850 1.00 65.04 O ANISOU 3365 OE1 GLU C 202 7648 9233 7830 -1316 -236 474 O ATOM 3366 OE2 GLU C 202 12.478 -12.562 16.216 1.00 57.81 O ANISOU 3366 OE2 GLU C 202 6911 8113 6943 -1221 -224 393 O ATOM 3367 N VAL C 203 8.395 -11.883 11.000 1.00 45.14 N ANISOU 3367 N VAL C 203 5016 6810 5326 -1381 -405 585 N ATOM 3368 CA VAL C 203 7.146 -12.110 10.282 1.00 47.91 C ANISOU 3368 CA VAL C 203 5284 7274 5645 -1479 -460 655 C ATOM 3369 C VAL C 203 7.394 -12.137 8.784 1.00 49.35 C ANISOU 3369 C VAL C 203 5535 7392 5824 -1487 -518 656 C ATOM 3370 O VAL C 203 6.940 -13.044 8.082 1.00 44.05 O ANISOU 3370 O VAL C 203 4917 6725 5096 -1619 -590 694 O ATOM 3371 CB VAL C 203 6.098 -11.036 10.616 1.00 43.70 C ANISOU 3371 CB VAL C 203 4556 6900 5150 -1414 -417 694 C ATOM 3372 CG1 VAL C 203 4.879 -11.164 9.696 1.00 45.47 C ANISOU 3372 CG1 VAL C 203 4685 7242 5349 -1502 -481 772 C ATOM 3373 CG2 VAL C 203 5.685 -11.151 12.074 1.00 46.57 C ANISOU 3373 CG2 VAL C 203 4850 7343 5500 -1431 -361 700 C ATOM 3374 N ALA C 204 8.128 -11.145 8.297 1.00 50.32 N ANISOU 3374 N ALA C 204 5663 7452 6002 -1353 -488 615 N ATOM 3375 CA ALA C 204 8.433 -11.051 6.875 1.00 52.82 C ANISOU 3375 CA ALA C 204 6045 7708 6316 -1349 -535 612 C ATOM 3376 C ALA C 204 9.182 -12.288 6.382 1.00 48.70 C ANISOU 3376 C ALA C 204 5706 7057 5740 -1436 -580 586 C ATOM 3377 O ALA C 204 8.972 -12.751 5.263 1.00 52.89 O ANISOU 3377 O ALA C 204 6298 7568 6229 -1512 -642 606 O ATOM 3378 CB ALA C 204 9.243 -9.788 6.591 1.00 43.80 C ANISOU 3378 CB ALA C 204 4891 6510 5242 -1190 -487 567 C ATOM 3379 N GLN C 205 10.060 -12.817 7.226 1.00 51.12 N ANISOU 3379 N GLN C 205 6104 7274 6043 -1420 -548 540 N ATOM 3380 CA GLN C 205 10.889 -13.955 6.852 1.00 57.37 C ANISOU 3380 CA GLN C 205 7077 7932 6791 -1477 -580 510 C ATOM 3381 C GLN C 205 10.069 -15.218 6.566 1.00 60.24 C ANISOU 3381 C GLN C 205 7501 8315 7074 -1651 -652 557 C ATOM 3382 O GLN C 205 10.522 -16.101 5.840 1.00 56.07 O ANISOU 3382 O GLN C 205 7125 7682 6498 -1709 -693 540 O ATOM 3383 CB GLN C 205 11.922 -14.239 7.942 1.00 66.38 C ANISOU 3383 CB GLN C 205 8287 8987 7948 -1421 -533 462 C ATOM 3384 CG GLN C 205 12.898 -15.345 7.590 1.00 79.31 C ANISOU 3384 CG GLN C 205 10109 10477 9549 -1450 -557 428 C ATOM 3385 CD GLN C 205 13.623 -15.080 6.286 1.00 92.20 C ANISOU 3385 CD GLN C 205 11815 12027 11190 -1392 -563 396 C ATOM 3386 OE1 GLN C 205 14.367 -14.106 6.162 1.00 94.65 O ANISOU 3386 OE1 GLN C 205 12090 12315 11557 -1268 -518 361 O ATOM 3387 NE2 GLN C 205 13.411 -15.950 5.305 1.00 96.47 N ANISOU 3387 NE2 GLN C 205 12464 12521 11670 -1487 -620 407 N ATOM 3388 N THR C 206 8.872 -15.300 7.141 1.00 62.38 N ANISOU 3388 N THR C 206 7656 8721 7325 -1735 -666 615 N ATOM 3389 CA THR C 206 8.017 -16.473 6.959 1.00 63.71 C ANISOU 3389 CA THR C 206 7871 8922 7412 -1917 -737 667 C ATOM 3390 C THR C 206 7.165 -16.377 5.697 1.00 73.14 C ANISOU 3390 C THR C 206 9028 10185 8578 -1993 -803 717 C ATOM 3391 O THR C 206 6.726 -17.395 5.159 1.00 79.23 O ANISOU 3391 O THR C 206 9889 10941 9274 -2144 -874 748 O ATOM 3392 CB THR C 206 7.081 -16.698 8.165 1.00 58.83 C ANISOU 3392 CB THR C 206 7143 8431 6779 -1992 -725 716 C ATOM 3393 OG1 THR C 206 6.020 -15.735 8.140 1.00 52.84 O ANISOU 3393 OG1 THR C 206 6185 7840 6051 -1967 -712 766 O ATOM 3394 CG2 THR C 206 7.845 -16.576 9.466 1.00 52.34 C ANISOU 3394 CG2 THR C 206 6333 7563 5989 -1906 -656 671 C ATOM 3395 N THR C 207 6.923 -15.155 5.233 1.00 68.04 N ANISOU 3395 N THR C 207 8253 9611 7987 -1892 -783 727 N ATOM 3396 CA THR C 207 6.116 -14.942 4.034 1.00 66.66 C ANISOU 3396 CA THR C 207 8028 9509 7789 -1953 -847 779 C ATOM 3397 C THR C 207 6.833 -15.505 2.810 1.00 72.41 C ANISOU 3397 C THR C 207 8939 10100 8473 -1988 -892 745 C ATOM 3398 O THR C 207 8.031 -15.287 2.628 1.00 73.51 O ANISOU 3398 O THR C 207 9176 10112 8642 -1880 -851 677 O ATOM 3399 CB THR C 207 5.806 -13.444 3.810 1.00 65.89 C ANISOU 3399 CB THR C 207 7764 9504 7766 -1817 -811 795 C ATOM 3400 OG1 THR C 207 5.424 -12.835 5.051 1.00 67.03 O ANISOU 3400 OG1 THR C 207 7764 9746 7959 -1746 -746 805 O ATOM 3401 CG2 THR C 207 4.682 -13.273 2.795 1.00 62.92 C ANISOU 3401 CG2 THR C 207 7298 9246 7364 -1898 -885 873 C ATOM 3402 N ALA C 208 6.101 -16.235 1.974 1.00 75.29 N ANISOU 3402 N ALA C 208 9350 10493 8763 -2143 -977 793 N ATOM 3403 CA ALA C 208 6.680 -16.828 0.773 1.00 79.52 C ANISOU 3403 CA ALA C 208 10068 10902 9243 -2191 -1022 762 C ATOM 3404 C ALA C 208 7.163 -15.758 -0.204 1.00 83.43 C ANISOU 3404 C ALA C 208 10541 11375 9783 -2068 -1004 739 C ATOM 3405 O ALA C 208 6.536 -14.709 -0.353 1.00 88.10 O ANISOU 3405 O ALA C 208 10968 12084 10421 -2012 -1002 781 O ATOM 3406 CB ALA C 208 5.675 -17.754 0.100 1.00 78.41 C ANISOU 3406 CB ALA C 208 9974 10812 9008 -2395 -1121 825 C TER 3407 ALA C 208 ATOM 3408 N GLY D 848 58.026 -14.438 -1.507 1.00110.00 N ANISOU 3408 N GLY D 848 11851 14088 15854 2893 1563 723 N ATOM 3409 CA GLY D 848 57.332 -13.927 -0.340 1.00105.64 C ANISOU 3409 CA GLY D 848 11469 13481 15190 2779 1273 727 C ATOM 3410 C GLY D 848 56.354 -12.816 -0.673 1.00 99.32 C ANISOU 3410 C GLY D 848 10792 12690 14256 2498 1333 745 C ATOM 3411 O GLY D 848 56.740 -11.769 -1.195 1.00101.18 O ANISOU 3411 O GLY D 848 10802 13023 14619 2338 1415 761 O ATOM 3412 N SER D 849 55.080 -13.049 -0.372 1.00 87.92 N ANISOU 3412 N SER D 849 9714 11139 12553 2438 1295 730 N ATOM 3413 CA SER D 849 54.038 -12.058 -0.617 1.00 78.24 C ANISOU 3413 CA SER D 849 8631 9906 11191 2192 1327 732 C ATOM 3414 C SER D 849 54.208 -10.858 0.306 1.00 68.96 C ANISOU 3414 C SER D 849 7327 8775 10099 2043 1081 759 C ATOM 3415 O SER D 849 54.906 -10.932 1.316 1.00 65.65 O ANISOU 3415 O SER D 849 6791 8351 9801 2132 851 776 O ATOM 3416 CB SER D 849 52.657 -12.679 -0.419 1.00 79.87 C ANISOU 3416 CB SER D 849 9235 9984 11129 2179 1334 696 C ATOM 3417 OG SER D 849 52.506 -13.161 0.904 1.00 84.04 O ANISOU 3417 OG SER D 849 9911 10422 11597 2262 1099 681 O ATOM 3418 N TRP D 850 53.563 -9.749 -0.039 1.00 62.07 N ANISOU 3418 N TRP D 850 6499 7932 9154 1820 1117 764 N ATOM 3419 CA TRP D 850 53.718 -8.526 0.732 1.00 62.63 C ANISOU 3419 CA TRP D 850 6464 8049 9284 1664 903 801 C ATOM 3420 C TRP D 850 52.391 -7.800 0.895 1.00 59.01 C ANISOU 3420 C TRP D 850 6267 7536 8619 1479 862 787 C ATOM 3421 O TRP D 850 51.539 -7.838 0.009 1.00 58.39 O ANISOU 3421 O TRP D 850 6349 7430 8406 1416 1042 746 O ATOM 3422 CB TRP D 850 54.743 -7.605 0.068 1.00 64.38 C ANISOU 3422 CB TRP D 850 6354 8410 9697 1566 985 826 C ATOM 3423 CG TRP D 850 54.446 -7.329 -1.375 1.00 65.91 C ANISOU 3423 CG TRP D 850 6583 8630 9829 1465 1280 795 C ATOM 3424 CD1 TRP D 850 54.656 -8.169 -2.427 1.00 67.63 C ANISOU 3424 CD1 TRP D 850 6802 8831 10063 1577 1542 769 C ATOM 3425 CD2 TRP D 850 53.882 -6.130 -1.925 1.00 66.81 C ANISOU 3425 CD2 TRP D 850 6778 8769 9839 1236 1333 785 C ATOM 3426 NE1 TRP D 850 54.260 -7.571 -3.597 1.00 66.49 N ANISOU 3426 NE1 TRP D 850 6746 8682 9836 1427 1754 744 N ATOM 3427 CE2 TRP D 850 53.782 -6.318 -3.317 1.00 63.62 C ANISOU 3427 CE2 TRP D 850 6432 8344 9395 1219 1624 746 C ATOM 3428 CE3 TRP D 850 53.452 -4.917 -1.375 1.00 66.40 C ANISOU 3428 CE3 TRP D 850 6778 8739 9711 1049 1156 804 C ATOM 3429 CZ2 TRP D 850 53.272 -5.340 -4.168 1.00 57.96 C ANISOU 3429 CZ2 TRP D 850 5836 7620 8566 1024 1729 715 C ATOM 3430 CZ3 TRP D 850 52.945 -3.946 -2.222 1.00 62.04 C ANISOU 3430 CZ3 TRP D 850 6330 8199 9044 861 1265 774 C ATOM 3431 CH2 TRP D 850 52.860 -4.163 -3.603 1.00 53.71 C ANISOU 3431 CH2 TRP D 850 5341 7114 7952 851 1542 725 C ATOM 3432 N ASP D 851 52.223 -7.146 2.038 1.00 56.37 N ANISOU 3432 N ASP D 851 5980 7173 8266 1399 617 819 N ATOM 3433 CA ASP D 851 51.027 -6.361 2.299 1.00 56.44 C ANISOU 3433 CA ASP D 851 6211 7132 8100 1227 564 806 C ATOM 3434 C ASP D 851 51.283 -4.913 1.923 1.00 54.60 C ANISOU 3434 C ASP D 851 5834 7009 7904 1035 547 840 C ATOM 3435 O ASP D 851 52.325 -4.356 2.257 1.00 52.22 O ANISOU 3435 O ASP D 851 5300 6787 7753 1011 432 898 O ATOM 3436 CB ASP D 851 50.625 -6.466 3.771 1.00 62.98 C ANISOU 3436 CB ASP D 851 7228 7839 8861 1242 326 822 C ATOM 3437 CG ASP D 851 50.289 -7.887 4.180 1.00 74.13 C ANISOU 3437 CG ASP D 851 8844 9123 10199 1414 345 773 C ATOM 3438 OD1 ASP D 851 49.994 -8.708 3.285 1.00 73.15 O ANISOU 3438 OD1 ASP D 851 8771 9000 10023 1489 554 723 O ATOM 3439 OD2 ASP D 851 50.320 -8.185 5.393 1.00 79.38 O ANISOU 3439 OD2 ASP D 851 9647 9671 10843 1469 151 783 O ATOM 3440 N CYS D 852 50.339 -4.308 1.212 1.00 44.69 N ANISOU 3440 N CYS D 852 4722 5753 6507 898 654 798 N ATOM 3441 CA CYS D 852 50.469 -2.909 0.846 1.00 40.44 C ANISOU 3441 CA CYS D 852 4109 5301 5955 709 633 818 C ATOM 3442 C CYS D 852 50.367 -2.049 2.095 1.00 42.50 C ANISOU 3442 C CYS D 852 4414 5551 6184 615 372 880 C ATOM 3443 O CYS D 852 49.431 -2.180 2.879 1.00 44.70 O ANISOU 3443 O CYS D 852 4913 5726 6346 615 272 867 O ATOM 3444 CB CYS D 852 49.382 -2.513 -0.160 1.00 41.48 C ANISOU 3444 CB CYS D 852 4435 5404 5924 603 776 742 C ATOM 3445 SG CYS D 852 49.469 -0.797 -0.731 1.00 43.23 S ANISOU 3445 SG CYS D 852 4632 5712 6080 372 758 744 S ATOM 3446 N GLU D 853 51.331 -1.161 2.285 1.00 44.37 N ANISOU 3446 N GLU D 853 4450 5885 6524 528 270 947 N ATOM 3447 CA GLU D 853 51.284 -0.265 3.422 1.00 45.15 C ANISOU 3447 CA GLU D 853 4609 5966 6581 428 18 1022 C ATOM 3448 C GLU D 853 50.441 0.963 3.123 1.00 47.72 C ANISOU 3448 C GLU D 853 5097 6311 6724 238 15 1009 C ATOM 3449 O GLU D 853 50.255 1.816 3.987 1.00 51.11 O ANISOU 3449 O GLU D 853 5619 6721 7080 139 -178 1072 O ATOM 3450 CB GLU D 853 52.695 0.147 3.847 1.00 52.03 C ANISOU 3450 CB GLU D 853 5201 6924 7645 414 -122 1106 C ATOM 3451 CG GLU D 853 53.436 -0.907 4.657 1.00 64.01 C ANISOU 3451 CG GLU D 853 6612 8381 9330 607 -247 1132 C ATOM 3452 CD GLU D 853 54.905 -0.567 4.850 1.00 77.02 C ANISOU 3452 CD GLU D 853 7924 10128 11214 606 -362 1192 C ATOM 3453 OE1 GLU D 853 55.392 0.376 4.186 1.00 77.91 O ANISOU 3453 OE1 GLU D 853 7867 10370 11367 453 -285 1203 O ATOM 3454 OE2 GLU D 853 55.572 -1.247 5.662 1.00 80.84 O ANISOU 3454 OE2 GLU D 853 8320 10551 11843 756 -534 1218 O ATOM 3455 N VAL D 854 49.930 1.060 1.900 1.00 43.25 N ANISOU 3455 N VAL D 854 4588 5769 6076 193 217 925 N ATOM 3456 CA VAL D 854 49.025 2.145 1.572 1.00 41.59 C ANISOU 3456 CA VAL D 854 4565 5558 5679 37 202 888 C ATOM 3457 C VAL D 854 47.571 1.739 1.809 1.00 42.19 C ANISOU 3457 C VAL D 854 4896 5514 5620 76 202 817 C ATOM 3458 O VAL D 854 46.820 2.476 2.443 1.00 41.54 O ANISOU 3458 O VAL D 854 4973 5393 5417 -7 70 824 O ATOM 3459 CB VAL D 854 49.218 2.655 0.121 1.00 39.51 C ANISOU 3459 CB VAL D 854 4274 5359 5380 -57 390 823 C ATOM 3460 CG1 VAL D 854 48.250 3.799 -0.186 1.00 44.21 C ANISOU 3460 CG1 VAL D 854 5096 5936 5763 -205 340 772 C ATOM 3461 CG2 VAL D 854 50.652 3.101 -0.095 1.00 46.62 C ANISOU 3461 CG2 VAL D 854 4914 6378 6423 -119 415 881 C ATOM 3462 N CYS D 855 47.174 0.567 1.316 1.00 38.79 N ANISOU 3462 N CYS D 855 4504 5022 5213 201 355 746 N ATOM 3463 CA CYS D 855 45.766 0.173 1.381 1.00 35.88 C ANISOU 3463 CA CYS D 855 4360 4545 4729 222 381 658 C ATOM 3464 C CYS D 855 45.513 -1.168 2.073 1.00 37.81 C ANISOU 3464 C CYS D 855 4663 4691 5011 367 397 646 C ATOM 3465 O CYS D 855 44.364 -1.559 2.247 1.00 40.48 O ANISOU 3465 O CYS D 855 5180 4935 5267 376 424 570 O ATOM 3466 CB CYS D 855 45.144 0.144 -0.019 1.00 36.04 C ANISOU 3466 CB CYS D 855 4462 4551 4681 199 550 553 C ATOM 3467 SG CYS D 855 45.516 -1.367 -0.957 1.00 38.85 S ANISOU 3467 SG CYS D 855 4762 4875 5123 358 778 521 S ATOM 3468 N LEU D 856 46.584 -1.860 2.449 1.00 40.63 N ANISOU 3468 N LEU D 856 4875 5068 5496 478 379 711 N ATOM 3469 CA LEU D 856 46.493 -3.095 3.247 1.00 40.07 C ANISOU 3469 CA LEU D 856 4888 4892 5445 620 359 705 C ATOM 3470 C LEU D 856 46.119 -4.351 2.457 1.00 45.30 C ANISOU 3470 C LEU D 856 5613 5511 6089 737 556 628 C ATOM 3471 O LEU D 856 45.952 -5.426 3.036 1.00 40.33 O ANISOU 3471 O LEU D 856 5092 4787 5443 850 557 608 O ATOM 3472 CB LEU D 856 45.525 -2.925 4.422 1.00 40.41 C ANISOU 3472 CB LEU D 856 5157 4813 5385 569 234 690 C ATOM 3473 CG LEU D 856 45.765 -1.712 5.318 1.00 48.19 C ANISOU 3473 CG LEU D 856 6144 5809 6358 455 30 777 C ATOM 3474 CD1 LEU D 856 44.763 -1.700 6.460 1.00 49.38 C ANISOU 3474 CD1 LEU D 856 6550 5807 6406 418 -53 755 C ATOM 3475 CD2 LEU D 856 47.197 -1.716 5.843 1.00 55.63 C ANISOU 3475 CD2 LEU D 856 6904 6794 7440 513 -110 884 C ATOM 3476 N VAL D 857 45.979 -4.224 1.145 1.00 39.48 N ANISOU 3476 N VAL D 857 4840 4823 5336 706 718 584 N ATOM 3477 CA VAL D 857 45.704 -5.393 0.314 1.00 41.37 C ANISOU 3477 CA VAL D 857 5150 5015 5555 815 905 528 C ATOM 3478 C VAL D 857 46.930 -6.310 0.207 1.00 49.75 C ANISOU 3478 C VAL D 857 6055 6112 6737 976 968 581 C ATOM 3479 O VAL D 857 48.059 -5.840 0.062 1.00 44.57 O ANISOU 3479 O VAL D 857 5175 5552 6207 973 951 641 O ATOM 3480 CB VAL D 857 45.205 -4.968 -1.077 1.00 40.75 C ANISOU 3480 CB VAL D 857 5120 4945 5420 736 1047 469 C ATOM 3481 CG1 VAL D 857 45.458 -6.055 -2.107 1.00 42.87 C ANISOU 3481 CG1 VAL D 857 5402 5183 5703 854 1250 453 C ATOM 3482 CG2 VAL D 857 43.733 -4.629 -0.997 1.00 35.24 C ANISOU 3482 CG2 VAL D 857 4622 4170 4599 644 1004 379 C ATOM 3483 N GLN D 858 46.712 -7.620 0.302 1.00 47.70 N ANISOU 3483 N GLN D 858 5911 5773 6440 1115 1040 553 N ATOM 3484 CA GLN D 858 47.817 -8.565 0.154 1.00 53.16 C ANISOU 3484 CA GLN D 858 6474 6491 7234 1290 1103 593 C ATOM 3485 C GLN D 858 48.163 -8.793 -1.314 1.00 53.06 C ANISOU 3485 C GLN D 858 6391 6518 7252 1321 1333 588 C ATOM 3486 O GLN D 858 47.288 -9.076 -2.134 1.00 55.36 O ANISOU 3486 O GLN D 858 6859 6746 7429 1292 1467 537 O ATOM 3487 CB GLN D 858 47.508 -9.900 0.832 1.00 67.29 C ANISOU 3487 CB GLN D 858 8450 8171 8944 1436 1087 563 C ATOM 3488 CG GLN D 858 48.627 -10.922 0.674 1.00 83.32 C ANISOU 3488 CG GLN D 858 10367 10223 11068 1640 1140 596 C ATOM 3489 CD GLN D 858 48.375 -12.201 1.446 1.00 92.05 C ANISOU 3489 CD GLN D 858 11694 11210 12069 1786 1095 562 C ATOM 3490 OE1 GLN D 858 47.334 -12.362 2.081 1.00 94.75 O ANISOU 3490 OE1 GLN D 858 12283 11448 12269 1721 1047 510 O ATOM 3491 NE2 GLN D 858 49.332 -13.120 1.395 1.00 97.88 N ANISOU 3491 NE2 GLN D 858 12356 11958 12875 1983 1116 583 N ATOM 3492 N ASN D 859 49.445 -8.664 -1.637 1.00 53.52 N ANISOU 3492 N ASN D 859 6196 6668 7471 1375 1378 638 N ATOM 3493 CA ASN D 859 49.911 -8.854 -3.006 1.00 55.00 C ANISOU 3493 CA ASN D 859 6317 6878 7702 1402 1620 637 C ATOM 3494 C ASN D 859 50.870 -10.028 -3.169 1.00 62.50 C ANISOU 3494 C ASN D 859 7157 7836 8754 1615 1726 663 C ATOM 3495 O ASN D 859 51.545 -10.429 -2.223 1.00 60.78 O ANISOU 3495 O ASN D 859 6818 7644 8633 1734 1581 688 O ATOM 3496 CB ASN D 859 50.545 -7.570 -3.530 1.00 53.36 C ANISOU 3496 CB ASN D 859 5917 6764 7592 1250 1651 653 C ATOM 3497 CG ASN D 859 49.514 -6.512 -3.846 1.00 46.29 C ANISOU 3497 CG ASN D 859 5192 5841 6557 1054 1615 611 C ATOM 3498 OD1 ASN D 859 48.917 -6.518 -4.919 1.00 50.72 O ANISOU 3498 OD1 ASN D 859 5919 6331 7019 1008 1766 564 O ATOM 3499 ND2 ASN D 859 49.290 -5.605 -2.905 1.00 46.06 N ANISOU 3499 ND2 ASN D 859 5139 5850 6512 946 1403 625 N ATOM 3500 N LYS D 860 50.923 -10.570 -4.381 1.00 69.16 N ANISOU 3500 N LYS D 860 8064 8642 9571 1667 1971 656 N ATOM 3501 CA LYS D 860 51.757 -11.732 -4.669 1.00 82.13 C ANISOU 3501 CA LYS D 860 9633 10281 11289 1879 2102 680 C ATOM 3502 C LYS D 860 53.240 -11.377 -4.688 1.00 88.03 C ANISOU 3502 C LYS D 860 10013 11147 12289 1925 2128 710 C ATOM 3503 O LYS D 860 53.620 -10.277 -5.091 1.00 85.38 O ANISOU 3503 O LYS D 860 9516 10877 12045 1768 2171 711 O ATOM 3504 CB LYS D 860 51.340 -12.372 -5.995 1.00 87.13 C ANISOU 3504 CB LYS D 860 10476 10820 11809 1910 2366 672 C ATOM 3505 CG LYS D 860 49.942 -12.972 -5.963 1.00 91.76 C ANISOU 3505 CG LYS D 860 11412 11287 12166 1897 2341 638 C ATOM 3506 CD LYS D 860 49.571 -13.615 -7.290 1.00 98.29 C ANISOU 3506 CD LYS D 860 12460 12003 12881 1930 2583 641 C ATOM 3507 CE LYS D 860 49.306 -12.570 -8.360 1.00100.60 C ANISOU 3507 CE LYS D 860 12796 12261 13168 1749 2690 620 C ATOM 3508 NZ LYS D 860 48.902 -13.193 -9.651 1.00101.91 N ANISOU 3508 NZ LYS D 860 13225 12280 13214 1777 2908 626 N ATOM 3509 N ALA D 861 54.068 -12.320 -4.244 1.00 93.45 N ANISOU 3509 N ALA D 861 10571 11851 13084 2139 2098 725 N ATOM 3510 CA ALA D 861 55.515 -12.133 -4.192 1.00 97.51 C ANISOU 3510 CA ALA D 861 10704 12476 13871 2214 2108 740 C ATOM 3511 C ALA D 861 56.053 -11.593 -5.509 1.00 96.09 C ANISOU 3511 C ALA D 861 10383 12333 13792 2117 2399 738 C ATOM 3512 O ALA D 861 57.097 -10.944 -5.545 1.00 96.01 O ANISOU 3512 O ALA D 861 10043 12428 14009 2072 2418 738 O ATOM 3513 CB ALA D 861 56.200 -13.444 -3.845 1.00101.52 C ANISOU 3513 CB ALA D 861 11155 12967 14450 2493 2090 741 C ATOM 3514 N ASP D 862 55.326 -11.870 -6.586 1.00 97.28 N ANISOU 3514 N ASP D 862 10807 12384 13771 2079 2624 731 N ATOM 3515 CA ASP D 862 55.737 -11.482 -7.928 1.00103.35 C ANISOU 3515 CA ASP D 862 11538 13135 14595 1992 2928 723 C ATOM 3516 C ASP D 862 55.431 -10.021 -8.245 1.00 99.25 C ANISOU 3516 C ASP D 862 11029 12636 14046 1720 2918 698 C ATOM 3517 O ASP D 862 56.286 -9.299 -8.757 1.00101.01 O ANISOU 3517 O ASP D 862 11038 12918 14423 1620 3059 685 O ATOM 3518 CB ASP D 862 55.054 -12.379 -8.960 1.00113.45 C ANISOU 3518 CB ASP D 862 13159 14263 15683 2062 3154 730 C ATOM 3519 CG ASP D 862 55.201 -11.857 -10.372 1.00124.16 C ANISOU 3519 CG ASP D 862 14594 15544 17037 1931 3452 716 C ATOM 3520 OD1 ASP D 862 56.336 -11.858 -10.894 1.00130.78 O ANISOU 3520 OD1 ASP D 862 15200 16422 18069 1973 3664 717 O ATOM 3521 OD2 ASP D 862 54.180 -11.449 -10.963 1.00125.18 O ANISOU 3521 OD2 ASP D 862 15028 15560 16973 1788 3476 696 O ATOM 3522 N SER D 863 54.207 -9.594 -7.944 1.00 91.92 N ANISOU 3522 N SER D 863 10355 11654 12915 1601 2757 684 N ATOM 3523 CA SER D 863 53.739 -8.260 -8.318 1.00 84.44 C ANISOU 3523 CA SER D 863 9492 10702 11891 1356 2738 652 C ATOM 3524 C SER D 863 54.691 -7.145 -7.891 1.00 78.93 C ANISOU 3524 C SER D 863 8474 10144 11370 1230 2658 656 C ATOM 3525 O SER D 863 55.269 -7.182 -6.802 1.00 72.18 O ANISOU 3525 O SER D 863 7377 9392 10655 1299 2461 687 O ATOM 3526 CB SER D 863 52.335 -7.999 -7.762 1.00 82.41 C ANISOU 3526 CB SER D 863 9496 10389 11427 1277 2522 631 C ATOM 3527 OG SER D 863 52.342 -7.964 -6.347 1.00 85.36 O ANISOU 3527 OG SER D 863 9748 10840 11844 1315 2251 655 O ATOM 3528 N THR D 864 54.843 -6.156 -8.765 1.00 77.94 N ANISOU 3528 N THR D 864 8378 10008 11228 1041 2806 622 N ATOM 3529 CA THR D 864 55.729 -5.027 -8.516 1.00 78.50 C ANISOU 3529 CA THR D 864 8177 10206 11445 888 2764 619 C ATOM 3530 C THR D 864 55.000 -3.900 -7.790 1.00 68.72 C ANISOU 3530 C THR D 864 7037 9004 10070 715 2493 619 C ATOM 3531 O THR D 864 55.582 -3.206 -6.956 1.00 67.85 O ANISOU 3531 O THR D 864 6695 9014 10070 645 2317 649 O ATOM 3532 CB THR D 864 56.326 -4.486 -9.829 1.00 85.71 C ANISOU 3532 CB THR D 864 9094 11078 12394 751 3081 570 C ATOM 3533 OG1 THR D 864 56.824 -3.159 -9.619 1.00 90.70 O ANISOU 3533 OG1 THR D 864 9571 11812 13078 539 3012 554 O ATOM 3534 CG2 THR D 864 55.266 -4.452 -10.921 1.00 84.24 C ANISOU 3534 CG2 THR D 864 9342 10706 11959 680 3219 525 C ATOM 3535 N LYS D 865 53.725 -3.719 -8.116 1.00 58.53 N ANISOU 3535 N LYS D 865 6094 7601 8543 651 2455 585 N ATOM 3536 CA LYS D 865 52.904 -2.722 -7.440 1.00 62.01 C ANISOU 3536 CA LYS D 865 6658 8062 8841 509 2203 579 C ATOM 3537 C LYS D 865 51.567 -3.315 -7.014 1.00 58.97 C ANISOU 3537 C LYS D 865 6526 7586 8295 590 2065 568 C ATOM 3538 O LYS D 865 51.167 -4.375 -7.496 1.00 59.40 O ANISOU 3538 O LYS D 865 6719 7543 8308 719 2189 554 O ATOM 3539 CB LYS D 865 52.702 -1.485 -8.317 1.00 68.11 C ANISOU 3539 CB LYS D 865 7596 8799 9484 287 2281 520 C ATOM 3540 CG LYS D 865 52.150 -1.768 -9.702 1.00 75.54 C ANISOU 3540 CG LYS D 865 8839 9569 10293 276 2509 452 C ATOM 3541 CD LYS D 865 52.160 -0.503 -10.548 1.00 86.08 C ANISOU 3541 CD LYS D 865 10341 10857 11509 55 2585 383 C ATOM 3542 CE LYS D 865 51.788 -0.788 -11.995 1.00 93.98 C ANISOU 3542 CE LYS D 865 11661 11655 12393 43 2826 314 C ATOM 3543 NZ LYS D 865 50.376 -1.232 -12.131 1.00 94.71 N ANISOU 3543 NZ LYS D 865 12062 11609 12313 111 2709 280 N ATOM 3544 N CYS D 866 50.885 -2.628 -6.102 1.00 53.22 N ANISOU 3544 N CYS D 866 5860 6884 7477 508 1818 573 N ATOM 3545 CA CYS D 866 49.634 -3.126 -5.538 1.00 49.78 C ANISOU 3545 CA CYS D 866 5633 6370 6913 569 1685 553 C ATOM 3546 C CYS D 866 48.541 -3.283 -6.594 1.00 49.54 C ANISOU 3546 C CYS D 866 5902 6202 6721 543 1796 473 C ATOM 3547 O CYS D 866 48.242 -2.347 -7.341 1.00 53.57 O ANISOU 3547 O CYS D 866 6545 6675 7135 400 1824 420 O ATOM 3548 CB CYS D 866 49.142 -2.210 -4.409 1.00 42.64 C ANISOU 3548 CB CYS D 866 4745 5509 5946 467 1421 570 C ATOM 3549 SG CYS D 866 47.629 -2.798 -3.629 1.00 41.92 S ANISOU 3549 SG CYS D 866 4890 5315 5722 527 1283 531 S ATOM 3550 N ILE D 867 47.937 -4.466 -6.635 1.00 48.01 N ANISOU 3550 N ILE D 867 5831 5921 6489 679 1845 460 N ATOM 3551 CA ILE D 867 46.882 -4.761 -7.597 1.00 53.66 C ANISOU 3551 CA ILE D 867 6830 6492 7067 668 1932 388 C ATOM 3552 C ILE D 867 45.703 -3.815 -7.418 1.00 50.26 C ANISOU 3552 C ILE D 867 6566 6024 6507 535 1758 315 C ATOM 3553 O ILE D 867 44.960 -3.535 -8.362 1.00 50.10 O ANISOU 3553 O ILE D 867 6767 5890 6380 474 1796 238 O ATOM 3554 CB ILE D 867 46.384 -6.215 -7.455 1.00 58.90 C ANISOU 3554 CB ILE D 867 7594 7080 7705 830 1980 392 C ATOM 3555 CG1 ILE D 867 45.407 -6.561 -8.581 1.00 62.47 C ANISOU 3555 CG1 ILE D 867 8334 7371 8030 818 2080 325 C ATOM 3556 CG2 ILE D 867 45.731 -6.427 -6.094 1.00 53.69 C ANISOU 3556 CG2 ILE D 867 6929 6448 7024 855 1781 388 C ATOM 3557 CD1 ILE D 867 46.014 -6.482 -9.964 1.00 64.59 C ANISOU 3557 CD1 ILE D 867 8677 7563 8302 801 2298 328 C ATOM 3558 N ALA D 868 45.538 -3.316 -6.199 1.00 41.89 N ANISOU 3558 N ALA D 868 5412 5047 5459 497 1560 336 N ATOM 3559 CA ALA D 868 44.402 -2.468 -5.887 1.00 43.99 C ANISOU 3559 CA ALA D 868 5821 5282 5612 390 1393 268 C ATOM 3560 C ALA D 868 44.681 -1.014 -6.226 1.00 44.96 C ANISOU 3560 C ALA D 868 5948 5452 5683 232 1335 255 C ATOM 3561 O ALA D 868 44.056 -0.459 -7.125 1.00 37.05 O ANISOU 3561 O ALA D 868 5141 4365 4572 156 1345 169 O ATOM 3562 CB ALA D 868 44.021 -2.599 -4.422 1.00 44.85 C ANISOU 3562 CB ALA D 868 5875 5429 5737 416 1224 296 C ATOM 3563 N CYS D 869 45.633 -0.421 -5.507 1.00 40.02 N ANISOU 3563 N CYS D 869 5125 4952 5130 186 1263 336 N ATOM 3564 CA CYS D 869 45.831 1.027 -5.504 1.00 43.68 C ANISOU 3564 CA CYS D 869 5598 5476 5521 23 1163 334 C ATOM 3565 C CYS D 869 47.046 1.469 -6.316 1.00 46.72 C ANISOU 3565 C CYS D 869 5880 5912 5958 -51 1314 355 C ATOM 3566 O CYS D 869 47.322 2.663 -6.418 1.00 42.91 O ANISOU 3566 O CYS D 869 5420 5479 5404 -200 1256 349 O ATOM 3567 CB CYS D 869 45.971 1.544 -4.068 1.00 39.63 C ANISOU 3567 CB CYS D 869 4968 5058 5033 -8 953 412 C ATOM 3568 SG CYS D 869 47.565 1.157 -3.296 1.00 42.01 S ANISOU 3568 SG CYS D 869 4944 5480 5539 53 954 541 S ATOM 3569 N GLU D 870 47.777 0.499 -6.863 1.00 50.69 N ANISOU 3569 N GLU D 870 6277 6401 6583 52 1516 377 N ATOM 3570 CA GLU D 870 48.899 0.770 -7.762 1.00 57.11 C ANISOU 3570 CA GLU D 870 6998 7237 7463 -12 1717 380 C ATOM 3571 C GLU D 870 50.163 1.260 -7.056 1.00 53.07 C ANISOU 3571 C GLU D 870 6178 6886 7100 -64 1673 461 C ATOM 3572 O GLU D 870 51.142 1.611 -7.711 1.00 53.06 O ANISOU 3572 O GLU D 870 6070 6921 7171 -143 1839 455 O ATOM 3573 CB GLU D 870 48.486 1.768 -8.851 1.00 63.08 C ANISOU 3573 CB GLU D 870 8025 7899 8045 -170 1770 285 C ATOM 3574 CG GLU D 870 47.327 1.294 -9.705 1.00 72.54 C ANISOU 3574 CG GLU D 870 9532 8915 9115 -119 1811 196 C ATOM 3575 CD GLU D 870 46.785 2.384 -10.602 1.00 84.08 C ANISOU 3575 CD GLU D 870 11298 10265 10385 -269 1786 90 C ATOM 3576 OE1 GLU D 870 47.218 3.545 -10.453 1.00 86.64 O ANISOU 3576 OE1 GLU D 870 11604 10666 10650 -418 1722 87 O ATOM 3577 OE2 GLU D 870 45.925 2.079 -11.454 1.00 90.43 O ANISOU 3577 OE2 GLU D 870 12375 10894 11089 -239 1817 6 O ATOM 3578 N SER D 871 50.147 1.285 -5.728 1.00 51.18 N ANISOU 3578 N SER D 871 5807 6728 6911 -27 1452 531 N ATOM 3579 CA SER D 871 51.315 1.729 -4.976 1.00 54.16 C ANISOU 3579 CA SER D 871 5897 7243 7438 -70 1367 612 C ATOM 3580 C SER D 871 52.478 0.758 -5.151 1.00 56.66 C ANISOU 3580 C SER D 871 5938 7603 7989 63 1530 644 C ATOM 3581 O SER D 871 52.281 -0.450 -5.213 1.00 54.60 O ANISOU 3581 O SER D 871 5691 7281 7774 239 1605 640 O ATOM 3582 CB SER D 871 50.980 1.886 -3.491 1.00 53.41 C ANISOU 3582 CB SER D 871 5774 7183 7335 -46 1082 684 C ATOM 3583 OG SER D 871 50.046 2.934 -3.285 1.00 52.97 O ANISOU 3583 OG SER D 871 5942 7104 7079 -179 934 661 O ATOM 3584 N ALA D 872 53.691 1.290 -5.235 1.00 63.87 N ANISOU 3584 N ALA D 872 6599 8620 9048 -22 1585 668 N ATOM 3585 CA ALA D 872 54.871 0.443 -5.365 1.00 67.73 C ANISOU 3585 CA ALA D 872 6784 9162 9791 106 1733 688 C ATOM 3586 C ALA D 872 55.104 -0.353 -4.084 1.00 68.90 C ANISOU 3586 C ALA D 872 6760 9342 10075 285 1519 759 C ATOM 3587 O ALA D 872 54.672 0.054 -3.005 1.00 71.39 O ANISOU 3587 O ALA D 872 7136 9667 10323 256 1252 807 O ATOM 3588 CB ALA D 872 56.089 1.282 -5.700 1.00 70.69 C ANISOU 3588 CB ALA D 872 6910 9642 10306 -47 1834 685 C ATOM 3589 N LYS D 873 55.783 -1.489 -4.208 1.00 68.87 N ANISOU 3589 N LYS D 873 6574 9341 10253 474 1637 761 N ATOM 3590 CA LYS D 873 56.069 -2.348 -3.061 1.00 69.67 C ANISOU 3590 CA LYS D 873 6542 9451 10480 666 1437 811 C ATOM 3591 C LYS D 873 56.797 -1.591 -1.950 1.00 69.01 C ANISOU 3591 C LYS D 873 6235 9459 10527 596 1168 875 C ATOM 3592 O LYS D 873 57.980 -1.274 -2.074 1.00 72.90 O ANISOU 3592 O LYS D 873 6410 10051 11235 559 1210 880 O ATOM 3593 CB LYS D 873 56.898 -3.553 -3.501 1.00 69.90 C ANISOU 3593 CB LYS D 873 6376 9482 10701 871 1621 794 C ATOM 3594 CG LYS D 873 57.289 -4.489 -2.376 1.00 76.51 C ANISOU 3594 CG LYS D 873 7089 10313 11666 1088 1410 830 C ATOM 3595 CD LYS D 873 58.409 -5.417 -2.815 1.00 82.08 C ANISOU 3595 CD LYS D 873 7518 11057 12612 1274 1579 809 C ATOM 3596 CE LYS D 873 58.637 -6.533 -1.813 1.00 89.21 C ANISOU 3596 CE LYS D 873 8383 11918 13593 1523 1377 825 C ATOM 3597 NZ LYS D 873 57.506 -7.498 -1.808 1.00 91.12 N ANISOU 3597 NZ LYS D 873 8990 12033 13599 1637 1402 813 N TER 3598 LYS D 873 HETATM 3599 MG MG A 301 51.961 -10.286 37.253 1.00 31.36 MG ANISOU 3599 MG MG A 301 4183 3727 4004 18 24 28 MG HETATM 3600 PB GDP A 302 50.262 -9.806 40.090 1.00 33.42 P ANISOU 3600 PB GDP A 302 4493 4018 4187 -21 37 76 P HETATM 3601 O1B GDP A 302 50.448 -9.612 38.616 1.00 29.64 O ANISOU 3601 O1B GDP A 302 3987 3532 3744 -19 42 46 O HETATM 3602 O2B GDP A 302 51.281 -10.818 40.588 1.00 31.25 O ANISOU 3602 O2B GDP A 302 4242 3714 3918 5 12 103 O HETATM 3603 O3B GDP A 302 50.384 -8.500 40.812 1.00 29.80 O ANISOU 3603 O3B GDP A 302 4023 3600 3700 -14 25 63 O HETATM 3604 O3A GDP A 302 48.780 -10.382 40.364 1.00 28.91 O ANISOU 3604 O3A GDP A 302 3938 3444 3604 -58 69 95 O HETATM 3605 PA GDP A 302 47.963 -11.344 39.370 1.00 31.88 P ANISOU 3605 PA GDP A 302 4313 3783 4018 -84 87 90 P HETATM 3606 O1A GDP A 302 47.362 -10.583 38.212 1.00 32.22 O ANISOU 3606 O1A GDP A 302 4324 3844 4075 -92 99 47 O HETATM 3607 O2A GDP A 302 48.764 -12.545 38.908 1.00 30.46 O ANISOU 3607 O2A GDP A 302 4151 3548 3875 -67 67 98 O HETATM 3608 O5' GDP A 302 46.790 -11.819 40.339 1.00 30.43 O ANISOU 3608 O5' GDP A 302 4145 3606 3812 -121 114 126 O HETATM 3609 C5' GDP A 302 47.151 -12.648 41.456 1.00 36.50 C ANISOU 3609 C5' GDP A 302 4950 4356 4562 -118 108 180 C HETATM 3610 C4' GDP A 302 45.917 -13.335 42.012 1.00 36.89 C ANISOU 3610 C4' GDP A 302 5009 4404 4605 -165 141 221 C HETATM 3611 O4' GDP A 302 44.968 -12.360 42.453 1.00 34.51 O ANISOU 3611 O4' GDP A 302 4681 4170 4261 -180 170 207 O HETATM 3612 C3' GDP A 302 45.247 -14.141 40.916 1.00 37.62 C ANISOU 3612 C3' GDP A 302 5090 4446 4757 -198 148 205 C HETATM 3613 O3' GDP A 302 44.740 -15.357 41.481 1.00 43.44 O ANISOU 3613 O3' GDP A 302 5854 5140 5511 -236 160 263 O HETATM 3614 C2' GDP A 302 44.087 -13.277 40.474 1.00 36.38 C ANISOU 3614 C2' GDP A 302 4892 4338 4593 -221 176 166 C HETATM 3615 O2' GDP A 302 43.001 -14.069 39.978 1.00 38.39 O ANISOU 3615 O2' GDP A 302 5132 4564 4890 -268 194 166 O HETATM 3616 C1' GDP A 302 43.727 -12.555 41.758 1.00 35.92 C ANISOU 3616 C1' GDP A 302 4832 4346 4470 -222 198 190 C HETATM 3617 N9 GDP A 302 43.112 -11.245 41.441 1.00 34.67 N ANISOU 3617 N9 GDP A 302 4636 4246 4293 -214 208 138 N HETATM 3618 C8 GDP A 302 43.655 -10.259 40.697 1.00 31.92 C ANISOU 3618 C8 GDP A 302 4273 3905 3950 -181 185 90 C HETATM 3619 N7 GDP A 302 42.815 -9.190 40.628 1.00 32.89 N ANISOU 3619 N7 GDP A 302 4366 4078 4053 -180 196 53 N HETATM 3620 C5 GDP A 302 41.714 -9.497 41.343 1.00 33.77 C ANISOU 3620 C5 GDP A 302 4466 4224 4143 -210 231 73 C HETATM 3621 C6 GDP A 302 40.439 -8.834 41.683 1.00 36.73 C ANISOU 3621 C6 GDP A 302 4804 4662 4488 -221 259 50 C HETATM 3622 O6 GDP A 302 40.183 -7.685 41.260 1.00 33.94 O ANISOU 3622 O6 GDP A 302 4429 4337 4130 -196 246 -1 O HETATM 3623 N1 GDP A 302 39.568 -9.498 42.450 1.00 31.89 N ANISOU 3623 N1 GDP A 302 4182 4078 3858 -258 297 88 N HETATM 3624 C2 GDP A 302 39.802 -10.748 42.909 1.00 37.68 C ANISOU 3624 C2 GDP A 302 4943 4773 4600 -288 309 152 C HETATM 3625 N2 GDP A 302 38.851 -11.349 43.668 1.00 39.63 N ANISOU 3625 N2 GDP A 302 5176 5053 4829 -332 353 197 N HETATM 3626 N3 GDP A 302 40.945 -11.425 42.636 1.00 35.39 N ANISOU 3626 N3 GDP A 302 4693 4414 4339 -277 278 174 N HETATM 3627 C4 GDP A 302 41.915 -10.856 41.876 1.00 33.65 C ANISOU 3627 C4 GDP A 302 4480 4170 4136 -237 240 134 C HETATM 3628 ZN ZN B 300 63.617 -0.757 24.147 1.00 41.74 ZN ANISOU 3628 ZN ZN B 300 4461 5585 5813 393 572 627 ZN HETATM 3629 MG MG C 301 30.545 8.690 2.416 1.00 30.77 MG ANISOU 3629 MG MG C 301 3904 3671 4117 -1 33 40 MG HETATM 3630 PB GDP C 302 27.271 8.197 2.714 1.00 32.39 P ANISOU 3630 PB GDP C 302 4040 3926 4339 65 3 60 P HETATM 3631 O1B GDP C 302 28.676 8.055 3.215 1.00 29.03 O ANISOU 3631 O1B GDP C 302 3638 3485 3909 37 23 36 O HETATM 3632 O2B GDP C 302 27.265 9.184 1.551 1.00 33.34 O ANISOU 3632 O2B GDP C 302 4189 4018 4460 75 -13 87 O HETATM 3633 O3B GDP C 302 26.653 6.883 2.326 1.00 29.00 O ANISOU 3633 O3B GDP C 302 3584 3541 3893 43 -14 70 O HETATM 3634 O3A GDP C 302 26.358 8.791 3.903 1.00 28.64 O ANISOU 3634 O3A GDP C 302 3539 3455 3886 109 17 48 O HETATM 3635 PA GDP C 302 26.866 9.761 5.078 1.00 31.88 P ANISOU 3635 PA GDP C 302 3979 3827 4309 126 45 19 P HETATM 3636 O1A GDP C 302 27.646 9.005 6.122 1.00 31.43 O ANISOU 3636 O1A GDP C 302 3919 3782 4240 91 60 -10 O HETATM 3637 O2A GDP C 302 27.642 10.938 4.540 1.00 30.60 O ANISOU 3637 O2A GDP C 302 3870 3607 4148 124 43 24 O HETATM 3638 O5' GDP C 302 25.441 10.213 5.668 1.00 30.10 O ANISOU 3638 O5' GDP C 302 3719 3618 4099 185 55 21 O HETATM 3639 C5' GDP C 302 24.588 11.022 4.840 1.00 35.11 C ANISOU 3639 C5' GDP C 302 4349 4243 4749 233 40 53 C HETATM 3640 C4' GDP C 302 23.579 11.745 5.716 1.00 36.32 C ANISOU 3640 C4' GDP C 302 4482 4397 4919 302 66 45 C HETATM 3641 O4' GDP C 302 22.769 10.784 6.397 1.00 34.26 O ANISOU 3641 O4' GDP C 302 4156 4206 4655 300 76 41 O HETATM 3642 C3' GDP C 302 24.306 12.534 6.784 1.00 39.34 C ANISOU 3642 C3' GDP C 302 4925 4724 5300 308 98 4 C HETATM 3643 O3' GDP C 302 23.612 13.774 6.968 1.00 42.24 O ANISOU 3643 O3' GDP C 302 5314 5050 5684 385 115 4 O HETATM 3644 C2' GDP C 302 24.184 11.678 8.030 1.00 34.24 C ANISOU 3644 C2' GDP C 302 4246 4123 4642 289 123 -26 C HETATM 3645 O2' GDP C 302 24.137 12.455 9.230 1.00 40.47 O ANISOU 3645 O2' GDP C 302 5069 4879 5428 322 161 -62 O HETATM 3646 C1' GDP C 302 22.874 10.957 7.809 1.00 35.65 C ANISOU 3646 C1' GDP C 302 4343 4374 4826 312 116 1 C HETATM 3647 N9 GDP C 302 22.873 9.636 8.485 1.00 35.02 N ANISOU 3647 N9 GDP C 302 4226 4351 4728 261 119 -10 N HETATM 3648 C8 GDP C 302 23.753 8.631 8.309 1.00 31.76 C ANISOU 3648 C8 GDP C 302 3825 3943 4299 195 100 -14 C HETATM 3649 N7 GDP C 302 23.424 7.568 9.095 1.00 31.57 N ANISOU 3649 N7 GDP C 302 3767 3969 4260 166 106 -21 N HETATM 3650 C5 GDP C 302 22.308 7.900 9.778 1.00 28.83 C ANISOU 3650 C5 GDP C 302 3378 3658 3918 209 132 -22 C HETATM 3651 C6 GDP C 302 21.433 7.253 10.777 1.00 33.85 C ANISOU 3651 C6 GDP C 302 3962 4359 4541 204 153 -26 C HETATM 3652 O6 GDP C 302 21.671 6.084 11.182 1.00 32.24 O ANISOU 3652 O6 GDP C 302 3752 4182 4315 144 143 -28 O HETATM 3653 N1 GDP C 302 20.381 7.951 11.230 1.00 33.25 N ANISOU 3653 N1 GDP C 302 3847 4310 4475 266 185 -24 N HETATM 3654 C2 GDP C 302 20.099 9.208 10.830 1.00 39.65 C ANISOU 3654 C2 GDP C 302 4671 5086 5310 340 197 -20 C HETATM 3655 N2 GDP C 302 19.016 9.833 11.356 1.00 40.81 N ANISOU 3655 N2 GDP C 302 4775 5264 5466 413 235 -19 N HETATM 3656 N3 GDP C 302 20.860 9.871 9.923 1.00 36.36 N ANISOU 3656 N3 GDP C 302 4309 4601 4906 345 173 -15 N HETATM 3657 C4 GDP C 302 21.952 9.268 9.374 1.00 33.15 C ANISOU 3657 C4 GDP C 302 3940 4169 4489 278 142 -15 C HETATM 3658 ZN ZN D 300 47.469 -0.914 -2.129 1.00 41.32 ZN ANISOU 3658 ZN ZN D 300 4783 5329 5587 324 937 586 ZN HETATM 3659 O HOH A 217 39.557 -0.528 22.772 1.00 27.75 O ANISOU 3659 O HOH A 217 3607 3585 3351 155 9 -235 O HETATM 3660 O HOH A 218 45.119 -0.458 22.536 1.00 32.09 O ANISOU 3660 O HOH A 218 4165 4131 3898 111 100 -41 O HETATM 3661 O HOH A 219 61.598 11.428 34.761 1.00 59.39 O ANISOU 3661 O HOH A 219 7222 6984 8360 -469 -355 195 O HETATM 3662 O HOH A 220 37.126 9.840 37.126 1.00 51.76 O ANISOU 3662 O HOH A 220 6654 6471 6541 292 -271 -548 O HETATM 3663 O HOH A 221 42.269 -10.071 33.517 1.00 30.20 O ANISOU 3663 O HOH A 221 3959 3630 3886 -157 145 -121 O HETATM 3664 O HOH A 222 32.916 0.670 24.895 1.00 37.23 O ANISOU 3664 O HOH A 222 4680 4853 4611 186 -82 -478 O HETATM 3665 O HOH A 223 51.845 -3.436 46.951 1.00 35.32 O ANISOU 3665 O HOH A 223 4725 4489 4208 118 -150 -58 O HETATM 3666 O HOH A 224 38.767 19.772 23.814 1.00 66.33 O ANISOU 3666 O HOH A 224 8928 7558 8715 370 -690 180 O HETATM 3667 O HOH A 225 50.746 -13.020 29.852 1.00 56.88 O ANISOU 3667 O HOH A 225 7355 6951 7306 97 55 -161 O HETATM 3668 O HOH A 226 29.875 -6.071 38.489 1.00 53.48 O ANISOU 3668 O HOH A 226 6484 7150 6687 -288 365 -309 O HETATM 3669 O HOH A 227 56.256 -9.016 45.899 1.00 35.56 O ANISOU 3669 O HOH A 227 4800 4373 4339 178 -195 101 O HETATM 3670 O HOH A 228 31.298 -4.949 30.419 1.00 40.85 O ANISOU 3670 O HOH A 228 4981 5331 5209 -116 113 -487 O HETATM 3671 O HOH A 229 33.448 6.892 30.939 1.00 60.89 O ANISOU 3671 O HOH A 229 7734 7745 7658 272 -172 -492 O HETATM 3672 O HOH A 230 39.943 9.639 37.199 1.00 36.19 O ANISOU 3672 O HOH A 230 4725 4403 4622 213 -278 -447 O HETATM 3673 O HOH A 231 34.713 -0.450 33.825 1.00 35.56 O ANISOU 3673 O HOH A 231 4452 4637 4423 -2 91 -385 O HETATM 3674 O HOH A 232 39.174 -2.418 37.271 1.00 34.03 O ANISOU 3674 O HOH A 232 4368 4363 4197 -72 137 -216 O HETATM 3675 O HOH A 233 39.230 8.293 45.104 1.00 50.48 O ANISOU 3675 O HOH A 233 6479 6574 6128 349 -232 -675 O HETATM 3676 O HOH A 234 33.168 -6.151 28.276 1.00 36.87 O ANISOU 3676 O HOH A 234 4551 4738 4720 -94 74 -470 O HETATM 3677 O HOH A 235 32.192 3.524 33.911 1.00 61.24 O ANISOU 3677 O HOH A 235 7657 7959 7651 160 -14 -539 O HETATM 3678 O HOH A 236 46.213 -5.292 28.012 1.00 31.65 O ANISOU 3678 O HOH A 236 4104 3939 3983 11 113 -128 O HETATM 3679 O HOH A 237 42.924 -9.845 23.757 1.00 36.95 O ANISOU 3679 O HOH A 237 4756 4621 4660 89 58 -369 O HETATM 3680 O HOH A 238 55.648 12.569 32.664 1.00 38.89 O ANISOU 3680 O HOH A 238 4896 4308 5573 -336 -320 214 O HETATM 3681 O HOH A 239 65.526 -8.412 34.063 1.00 52.87 O ANISOU 3681 O HOH A 239 6382 6777 6929 240 -65 -59 O HETATM 3682 O HOH A 240 38.513 4.673 24.837 1.00 37.53 O ANISOU 3682 O HOH A 240 4894 4716 4651 181 -90 -179 O HETATM 3683 O HOH A 241 61.983 -1.653 42.417 1.00 37.40 O ANISOU 3683 O HOH A 241 4635 4631 4943 70 -336 -100 O HETATM 3684 O HOH A 242 38.319 12.686 18.883 1.00 60.52 O ANISOU 3684 O HOH A 242 8057 7432 7507 383 -330 212 O HETATM 3685 O HOH A 243 50.998 4.826 54.228 1.00 60.05 O ANISOU 3685 O HOH A 243 7842 7890 7085 457 -537 -603 O HETATM 3686 O HOH A 244 34.077 1.990 34.772 1.00 36.35 O ANISOU 3686 O HOH A 244 4546 4768 4496 79 41 -448 O HETATM 3687 O HOH A 245 53.327 15.978 30.385 1.00 37.68 O ANISOU 3687 O HOH A 245 4870 3950 5498 -338 -401 339 O HETATM 3688 O HOH A 246 53.673 -5.163 36.673 1.00 32.87 O ANISOU 3688 O HOH A 246 4264 4012 4213 2 -2 -3 O HETATM 3689 O HOH A 247 33.861 -3.560 27.180 1.00 36.17 O ANISOU 3689 O HOH A 247 4508 4676 4561 11 31 -459 O HETATM 3690 O HOH A 248 51.244 -13.421 41.215 1.00 35.80 O ANISOU 3690 O HOH A 248 4887 4202 4513 6 1 171 O HETATM 3691 O HOH A 249 65.830 6.600 47.727 1.00 61.40 O ANISOU 3691 O HOH A 249 7459 7533 8339 7 -882 -473 O HETATM 3692 O HOH A 250 35.335 10.610 30.737 1.00 36.32 O ANISOU 3692 O HOH A 250 4741 4430 4629 332 -316 -424 O HETATM 3693 O HOH A 251 36.142 -12.373 31.244 1.00 36.68 O ANISOU 3693 O HOH A 251 4631 4452 4853 -296 144 -286 O HETATM 3694 O HOH A 252 35.467 2.906 46.008 1.00 40.21 O ANISOU 3694 O HOH A 252 5050 5617 4613 206 117 -508 O HETATM 3695 O HOH A 253 56.613 4.390 25.278 1.00 38.18 O ANISOU 3695 O HOH A 253 4690 4825 4990 -184 174 384 O HETATM 3696 O HOH A 254 39.866 -12.255 29.679 1.00 53.12 O ANISOU 3696 O HOH A 254 6806 6489 6888 -164 97 -279 O HETATM 3697 O HOH A 255 63.382 -6.126 36.799 1.00 40.80 O ANISOU 3697 O HOH A 255 4974 5140 5390 131 -127 -23 O HETATM 3698 O HOH A 256 51.393 -9.040 31.281 1.00 37.63 O ANISOU 3698 O HOH A 256 4876 4605 4816 42 87 -73 O HETATM 3699 O HOH A 257 44.572 -6.712 17.646 1.00 39.80 O ANISOU 3699 O HOH A 257 5103 5297 4721 318 87 -332 O HETATM 3700 O HOH A 258 36.698 2.529 50.110 1.00 42.46 O ANISOU 3700 O HOH A 258 5379 6084 4669 287 134 -495 O HETATM 3701 O HOH A 259 49.223 18.956 34.599 1.00 42.58 O ANISOU 3701 O HOH A 259 5641 4354 6184 -92 -735 -83 O HETATM 3702 O HOH A 260 30.590 6.162 25.408 1.00 42.65 O ANISOU 3702 O HOH A 260 5393 5522 5293 381 -246 -537 O HETATM 3703 O HOH A 261 40.403 -3.184 23.951 1.00 37.05 O ANISOU 3703 O HOH A 261 4766 4734 4577 97 49 -268 O HETATM 3704 O HOH A 262 47.443 19.223 36.514 1.00 52.39 O ANISOU 3704 O HOH A 262 6910 5631 7365 45 -814 -291 O HETATM 3705 O HOH A 263 31.515 -4.467 37.079 1.00 53.59 O ANISOU 3705 O HOH A 263 6584 7081 6699 -187 272 -351 O HETATM 3706 O HOH A 264 45.085 18.718 34.696 1.00 41.52 O ANISOU 3706 O HOH A 264 5570 4333 5871 117 -739 -249 O HETATM 3707 O HOH A 265 32.702 -3.977 32.392 1.00 38.14 O ANISOU 3707 O HOH A 265 4692 4981 4817 -108 143 -414 O HETATM 3708 O HOH A 266 43.385 -13.348 37.063 1.00 48.02 O ANISOU 3708 O HOH A 266 6310 5769 6168 -220 155 40 O HETATM 3709 O HOH A 267 51.313 -5.857 57.511 1.00 50.85 O ANISOU 3709 O HOH A 267 6935 6943 5442 432 -209 91 O HETATM 3710 O HOH A 268 31.466 -0.307 37.260 1.00 57.50 O ANISOU 3710 O HOH A 268 7095 7629 7124 -4 174 -473 O HETATM 3711 O HOH A 269 39.309 19.243 26.664 1.00 45.04 O ANISOU 3711 O HOH A 269 6165 4867 6083 332 -686 14 O HETATM 3712 O HOH A 270 57.014 6.954 25.829 1.00 44.81 O ANISOU 3712 O HOH A 270 5529 5548 5950 -275 115 465 O HETATM 3713 O HOH A 271 64.950 2.124 41.902 1.00 47.55 O ANISOU 3713 O HOH A 271 5708 5881 6478 -54 -446 -144 O HETATM 3714 O HOH A 272 51.038 -10.385 50.068 1.00 42.32 O ANISOU 3714 O HOH A 272 5817 5368 4892 121 -46 284 O HETATM 3715 O HOH A 273 63.764 7.956 33.531 1.00 51.04 O ANISOU 3715 O HOH A 273 6032 6180 7180 -428 -183 244 O HETATM 3716 O HOH A 274 44.602 0.323 19.611 1.00 45.56 O ANISOU 3716 O HOH A 274 5886 5931 5492 190 99 -7 O HETATM 3717 O HOH A 275 31.560 3.916 27.022 1.00 42.63 O ANISOU 3717 O HOH A 275 5354 5534 5308 258 -139 -520 O HETATM 3718 O HOH A 276 30.959 -12.659 41.549 1.00 53.59 O ANISOU 3718 O HOH A 276 6589 6977 6795 -615 523 90 O HETATM 3719 O HOH A 277 52.024 15.837 34.606 1.00 42.05 O ANISOU 3719 O HOH A 277 5453 4490 6036 -205 -553 12 O HETATM 3720 O HOH A 278 59.134 7.934 48.659 1.00 53.14 O ANISOU 3720 O HOH A 278 6703 6479 7008 120 -791 -541 O HETATM 3721 O HOH A 279 43.410 17.408 36.177 1.00 52.92 O ANISOU 3721 O HOH A 279 6987 5947 7173 214 -694 -402 O HETATM 3722 O HOH A 280 69.263 -2.010 37.925 1.00 44.86 O ANISOU 3722 O HOH A 280 5103 5766 6174 19 -266 -59 O HETATM 3723 O HOH A 281 43.043 -13.014 45.171 1.00 48.18 O ANISOU 3723 O HOH A 281 6428 5996 5883 -244 254 328 O HETATM 3724 O HOH A 282 46.119 -8.575 56.271 1.00 52.58 O ANISOU 3724 O HOH A 282 7137 7196 5646 190 135 349 O HETATM 3725 O HOH A 283 35.816 10.995 18.962 1.00 44.90 O ANISOU 3725 O HOH A 283 6014 5579 5467 467 -346 5 O HETATM 3726 O HOH A 284 30.595 1.408 27.006 1.00 50.80 O ANISOU 3726 O HOH A 284 6311 6629 6359 187 -84 -571 O HETATM 3727 O HOH A 285 39.983 22.381 29.241 1.00 59.90 O ANISOU 3727 O HOH A 285 8100 6457 8204 355 -910 -101 O HETATM 3728 O HOH A 286 46.931 -0.418 20.241 1.00 51.46 O ANISOU 3728 O HOH A 286 6600 6683 6270 153 151 36 O HETATM 3729 O HOH A 287 37.592 4.798 44.392 1.00 38.49 O ANISOU 3729 O HOH A 287 4906 5186 4533 232 -28 -535 O HETATM 3730 O HOH A 288 61.152 8.920 33.877 1.00 50.80 O ANISOU 3730 O HOH A 288 6148 6050 7104 -391 -228 208 O HETATM 3731 O HOH A 289 34.776 -11.770 44.663 1.00 46.97 O ANISOU 3731 O HOH A 289 5957 6157 5733 -466 501 226 O HETATM 3732 O HOH A 290 36.089 -14.358 43.407 1.00 59.36 O ANISOU 3732 O HOH A 290 7611 7487 7454 -530 444 303 O HETATM 3733 O HOH A 291 35.544 14.360 50.386 1.00 60.40 O ANISOU 3733 O HOH A 291 7664 8103 7183 874 -528 -1324 O HETATM 3734 O HOH A 292 37.982 10.337 20.507 1.00 46.86 O ANISOU 3734 O HOH A 292 6236 5785 5782 343 -264 49 O HETATM 3735 O HOH A 293 66.395 -7.171 42.404 1.00 58.86 O ANISOU 3735 O HOH A 293 7279 7424 7661 285 -389 -92 O HETATM 3736 O HOH A 294 28.304 0.732 26.201 1.00 71.22 O ANISOU 3736 O HOH A 294 8803 9295 8961 204 -110 -680 O HETATM 3737 O HOH A 295 57.770 -15.663 34.692 1.00 44.63 O ANISOU 3737 O HOH A 295 5828 5312 5816 279 -98 -66 O HETATM 3738 O HOH A 296 42.521 10.743 46.106 1.00 48.90 O ANISOU 3738 O HOH A 296 6342 6181 6057 382 -444 -745 O HETATM 3739 O HOH A 297 31.605 -2.319 38.616 1.00 53.47 O ANISOU 3739 O HOH A 297 6575 7145 6598 -96 257 -391 O HETATM 3740 O HOH A 298 57.735 -5.740 48.261 1.00 44.62 O ANISOU 3740 O HOH A 298 5891 5623 5440 237 -328 -19 O HETATM 3741 O HOH A 299 33.410 1.197 37.340 1.00 38.72 O ANISOU 3741 O HOH A 299 4804 5167 4741 52 108 -456 O HETATM 3742 O HOH A 300 42.154 24.257 30.583 1.00 64.17 O ANISOU 3742 O HOH A 300 8665 6757 8962 260 -1035 -81 O HETATM 3743 O HOH A 303 35.489 18.215 28.413 1.00 51.68 O ANISOU 3743 O HOH A 303 6919 5908 6809 522 -708 -315 O HETATM 3744 O HOH A 304 47.638 -13.649 36.540 1.00 48.69 O ANISOU 3744 O HOH A 304 6438 5804 6257 -89 77 38 O HETATM 3745 O HOH A 305 32.875 3.611 38.676 1.00 59.42 O ANISOU 3745 O HOH A 305 7418 7838 7322 160 49 -552 O HETATM 3746 O HOH A 306 35.581 7.971 34.491 1.00 56.22 O ANISOU 3746 O HOH A 306 7180 7100 7080 253 -186 -495 O HETATM 3747 O HOH A 307 33.697 7.039 28.531 1.00 47.44 O ANISOU 3747 O HOH A 307 6067 6007 5951 289 -199 -435 O HETATM 3748 O HOH A 308 28.449 -7.488 36.180 1.00 55.77 O ANISOU 3748 O HOH A 308 6699 7385 7104 -356 336 -369 O HETATM 3749 O HOH A 309 42.205 -11.337 26.044 1.00 35.86 O ANISOU 3749 O HOH A 309 4630 4379 4617 -1 58 -351 O HETATM 3750 O HOH A 310 48.125 22.622 29.836 1.00 43.86 O ANISOU 3750 O HOH A 310 5952 4208 6503 -139 -816 269 O HETATM 3751 O HOH A 311 31.546 10.684 25.317 1.00 36.60 O ANISOU 3751 O HOH A 311 4769 4569 4571 500 -399 -446 O HETATM 3752 O HOH A 312 58.461 12.383 43.762 1.00 68.31 O ANISOU 3752 O HOH A 312 8570 8061 9324 -124 -781 -406 O HETATM 3753 O HOH A 313 42.803 -10.315 28.336 1.00 43.06 O ANISOU 3753 O HOH A 313 5558 5281 5522 -47 93 -257 O HETATM 3754 O HOH A 314 37.083 1.135 52.669 1.00 49.01 O ANISOU 3754 O HOH A 314 6236 7074 5313 302 204 -407 O HETATM 3755 O HOH A 315 46.851 5.979 19.570 1.00 47.76 O ANISOU 3755 O HOH A 315 6211 6084 5854 90 86 324 O HETATM 3756 O HOH A 316 43.079 -1.979 16.982 1.00 44.17 O ANISOU 3756 O HOH A 316 5272 5719 5791 -139 -119 170 O HETATM 3757 O HOH A 317 65.605 0.095 39.759 1.00 49.78 O ANISOU 3757 O HOH A 317 5947 6234 6735 -38 -323 -71 O HETATM 3758 O HOH A 318 40.112 -11.203 52.912 1.00 51.47 O ANISOU 3758 O HOH A 318 6831 6981 5743 -178 454 505 O HETATM 3759 O HOH A 319 50.093 -8.097 57.924 1.00 65.72 O ANISOU 3759 O HOH A 319 8880 8843 7249 375 -92 283 O HETATM 3760 O HOH A 320 36.254 6.536 55.922 1.00 49.15 O ANISOU 3760 O HOH A 320 6207 7343 5124 703 -24 -889 O HETATM 3761 O HOH A 321 38.286 -6.416 49.781 1.00 50.96 O ANISOU 3761 O HOH A 321 6580 6973 5808 -95 388 99 O HETATM 3762 O HOH A 323 55.342 10.982 25.295 1.00 52.88 O ANISOU 3762 O HOH A 323 6657 6352 7084 -341 5 586 O HETATM 3763 O HOH A 324 52.928 -13.579 44.799 1.00 68.02 O ANISOU 3763 O HOH A 324 9041 8326 8477 82 -68 262 O HETATM 3764 O HOH A 325 63.456 -8.574 41.138 1.00 42.62 O ANISOU 3764 O HOH A 325 5361 5299 5535 255 -275 -32 O HETATM 3765 O HOH A 326 55.023 13.930 29.503 1.00 58.99 O ANISOU 3765 O HOH A 326 7477 6814 8122 -382 -260 413 O HETATM 3766 O HOH A 327 40.224 12.311 36.840 1.00 51.47 O ANISOU 3766 O HOH A 327 6702 6198 6656 260 -409 -476 O HETATM 3767 O HOH A 328 46.931 -10.535 54.543 1.00 71.45 O ANISOU 3767 O HOH A 328 9560 9380 8208 107 130 444 O HETATM 3768 O HOH A 329 37.094 16.735 50.620 1.00 72.31 O ANISOU 3768 O HOH A 329 9243 9394 8838 943 -750 -1449 O HETATM 3769 O HOH A 330 48.879 -11.391 22.465 1.00 54.98 O ANISOU 3769 O HOH A 330 7025 6975 6891 239 94 -338 O HETATM 3770 O HOH A 331 36.984 7.253 44.638 1.00 46.91 O ANISOU 3770 O HOH A 331 5967 6238 5619 339 -131 -671 O HETATM 3771 O HOH A 332 30.760 -3.727 34.383 1.00 45.54 O ANISOU 3771 O HOH A 332 5541 6032 5730 -134 197 -443 O HETATM 3772 O HOH A 333 46.828 20.384 26.617 1.00 44.79 O ANISOU 3772 O HOH A 333 6081 4591 6348 -90 -603 428 O HETATM 3773 O HOH A 334 38.821 6.497 61.924 1.00 66.32 O ANISOU 3773 O HOH A 334 8493 9896 6809 990 -133 -988 O HETATM 3774 O HOH A 335 29.274 -6.729 30.430 1.00 66.45 O ANISOU 3774 O HOH A 335 8120 8602 8526 -203 135 -538 O HETATM 3775 O HOH A 336 41.144 -10.199 31.158 1.00 47.76 O ANISOU 3775 O HOH A 336 6147 5864 6134 -140 126 -204 O HETATM 3776 O HOH A 337 28.822 7.246 26.687 1.00 57.79 O ANISOU 3776 O HOH A 337 7253 7479 7227 442 -286 -642 O HETATM 3777 O HOH A 338 35.166 8.760 46.595 1.00 53.05 O ANISOU 3777 O HOH A 338 6691 7176 6289 486 -163 -849 O HETATM 3778 O HOH A 339 62.206 -9.140 23.249 1.00 49.52 O ANISOU 3778 O HOH A 339 5913 6697 6205 350 274 -96 O HETATM 3779 O HOH A 340 36.602 13.352 48.018 1.00 60.78 O ANISOU 3779 O HOH A 340 7749 7976 7370 701 -481 -1122 O HETATM 3780 O HOH A 341 36.267 -4.749 49.346 1.00 60.51 O ANISOU 3780 O HOH A 341 7690 8294 7008 -66 411 -30 O HETATM 3781 O HOH A 342 42.574 -11.196 53.900 1.00 51.73 O ANISOU 3781 O HOH A 342 6962 6974 5717 -73 350 520 O HETATM 3782 O HOH A 343 41.230 -2.093 18.769 1.00 44.19 O ANISOU 3782 O HOH A 343 5698 5798 5295 259 33 -229 O HETATM 3783 O HOH A 344 38.855 11.461 40.900 1.00 48.56 O ANISOU 3783 O HOH A 344 6276 6046 6130 356 -380 -669 O HETATM 3784 O HOH A 345 54.627 -13.275 46.823 1.00 64.60 O ANISOU 3784 O HOH A 345 8636 7942 7968 165 -143 283 O HETATM 3785 O HOH A 347 55.207 -10.106 51.230 1.00 48.03 O ANISOU 3785 O HOH A 347 6545 6083 5620 274 -235 228 O HETATM 3786 O HOH A 348 63.411 -8.489 35.255 1.00 46.89 O ANISOU 3786 O HOH A 348 5759 5924 6135 209 -85 -41 O HETATM 3787 O HOH A 349 53.409 -9.011 49.738 1.00 40.25 O ANISOU 3787 O HOH A 349 5510 5097 4687 189 -152 182 O HETATM 3788 O HOH A 350 50.027 -10.594 47.441 1.00 55.30 O ANISOU 3788 O HOH A 350 7411 6928 6673 39 10 250 O HETATM 3789 O HOH A 351 38.118 10.789 43.964 1.00 60.42 O ANISOU 3789 O HOH A 351 7738 7740 7480 429 -343 -782 O HETATM 3790 O HOH A 352 51.947 2.241 53.959 1.00 52.20 O ANISOU 3790 O HOH A 352 6875 6899 6061 407 -457 -435 O HETATM 3791 O HOH A 353 54.310 12.109 41.924 1.00 44.33 O ANISOU 3791 O HOH A 353 5658 5057 6128 -63 -632 -350 O HETATM 3792 O HOH A 354 54.088 -10.228 31.863 1.00 41.73 O ANISOU 3792 O HOH A 354 5375 5118 5361 101 58 -65 O HETATM 3793 O HOH A 355 30.198 -10.889 32.908 1.00 48.20 O ANISOU 3793 O HOH A 355 5839 6152 6324 -422 236 -365 O HETATM 3794 O HOH A 357 44.543 22.514 28.798 1.00 45.30 O ANISOU 3794 O HOH A 357 6220 4475 6518 68 -834 178 O HETATM 3795 O HOH A 358 30.639 -13.074 30.843 1.00 59.56 O ANISOU 3795 O HOH A 358 7304 7447 7881 -448 160 -419 O HETATM 3796 O HOH A 359 39.720 9.609 47.529 1.00 54.51 O ANISOU 3796 O HOH A 359 7000 7141 6570 458 -324 -806 O HETATM 3797 O HOH A 360 60.257 -7.306 34.987 1.00 54.36 O ANISOU 3797 O HOH A 360 6806 6813 7034 120 -36 -10 O HETATM 3798 O HOH A 361 35.139 1.283 54.482 1.00 55.53 O ANISOU 3798 O HOH A 361 6987 8156 5957 367 296 -448 O HETATM 3799 O HOH A 362 44.369 -1.796 57.848 1.00 48.22 O ANISOU 3799 O HOH A 362 6429 6963 4931 434 13 -161 O HETATM 3800 O HOH A 363 46.941 -13.248 45.610 1.00 52.03 O ANISOU 3800 O HOH A 363 7000 6403 6367 -114 129 335 O HETATM 3801 O HOH A 365 51.422 12.182 41.422 1.00 44.23 O ANISOU 3801 O HOH A 365 5712 5079 6012 8 -581 -377 O HETATM 3802 O HOH A 366 68.638 -9.671 30.738 1.00 56.08 O ANISOU 3802 O HOH A 366 6554 7416 7339 364 27 -121 O HETATM 3803 O HOH A 367 28.639 6.950 47.150 1.00 53.43 O ANISOU 3803 O HOH A 367 6434 7722 6146 514 111 -949 O HETATM 3804 O HOH A 368 52.710 11.913 15.017 1.00 55.55 O ANISOU 3804 O HOH A 368 7153 7091 6863 -149 256 1091 O HETATM 3805 O HOH A 369 56.456 -9.762 21.462 1.00 48.93 O ANISOU 3805 O HOH A 369 6062 6495 6035 349 231 -185 O HETATM 3806 O HOH A 370 42.090 17.368 19.477 1.00 52.20 O ANISOU 3806 O HOH A 370 7114 6001 6717 203 -409 577 O HETATM 3807 O HOH A 371 51.169 -9.459 20.598 1.00 51.71 O ANISOU 3807 O HOH A 371 6546 6743 6358 302 168 -258 O HETATM 3808 O HOH A 372 44.371 -17.194 39.709 1.00 59.92 O ANISOU 3808 O HOH A 372 7945 7097 7726 -269 133 232 O HETATM 3809 O HOH A 373 63.563 7.298 46.267 1.00 47.85 O ANISOU 3809 O HOH A 373 5822 5758 6602 -40 -777 -408 O HETATM 3810 O HOH A 374 28.606 -8.830 32.956 1.00 64.33 O ANISOU 3810 O HOH A 374 7800 8335 8309 -362 239 -444 O HETATM 3811 O HOH A 375 32.613 11.840 27.275 1.00 49.01 O ANISOU 3811 O HOH A 375 6365 6053 6202 477 -417 -443 O HETATM 3812 O HOH A 376 58.335 12.067 47.070 1.00 61.67 O ANISOU 3812 O HOH A 376 7764 7315 8353 22 -904 -601 O HETATM 3813 O HOH A 377 40.039 9.125 19.147 1.00 48.50 O ANISOU 3813 O HOH A 377 6436 6065 5927 292 -166 159 O HETATM 3814 O HOH A 378 28.962 -1.282 24.646 1.00 52.96 O ANISOU 3814 O HOH A 378 6503 6960 6660 163 -104 -675 O HETATM 3815 O HOH A 379 39.815 2.411 23.740 1.00 43.12 O ANISOU 3815 O HOH A 379 5587 5473 5323 154 -25 -159 O HETATM 3816 O HOH A 380 47.753 8.297 20.590 1.00 60.44 O ANISOU 3816 O HOH A 380 7831 7557 7578 13 44 427 O HETATM 3817 O HOH A 381 30.178 -2.904 26.048 1.00 49.92 O ANISOU 3817 O HOH A 381 6132 6523 6312 61 -31 -614 O HETATM 3818 O HOH A 382 34.041 14.211 25.927 1.00 51.92 O ANISOU 3818 O HOH A 382 6853 6246 6630 496 -511 -296 O HETATM 3819 O HOH A 383 34.513 17.808 25.131 1.00 67.56 O ANISOU 3819 O HOH A 383 8967 7978 8725 566 -689 -189 O HETATM 3820 O HOH A 384 33.551 14.205 23.236 1.00 54.49 O ANISOU 3820 O HOH A 384 7217 6599 6886 544 -526 -208 O HETATM 3821 O HOH A 385 35.319 14.780 20.995 1.00 59.54 O ANISOU 3821 O HOH A 385 7942 7187 7494 506 -508 10 O HETATM 3822 O HOH A 386 31.439 12.389 23.073 1.00 49.68 O ANISOU 3822 O HOH A 386 6512 6157 6208 588 -494 -358 O HETATM 3823 O HOH A 387 30.123 -2.601 28.810 1.00 55.69 O ANISOU 3823 O HOH A 387 6841 7268 7050 4 35 -572 O HETATM 3824 O HOH A 405 55.505 11.369 43.993 1.00 42.04 O ANISOU 3824 O HOH A 405 5345 4832 5795 -20 -688 -431 O HETATM 3825 O HOH A 406 30.235 3.785 29.694 1.00 68.44 O ANISOU 3825 O HOH A 406 8542 8873 8589 234 -98 -597 O HETATM 3826 O HOH A 409 35.858 10.223 59.808 1.00 62.72 O ANISOU 3826 O HOH A 409 7907 9352 6571 1109 -238 -1338 O HETATM 3827 O HOH A 410 41.004 8.621 60.664 1.00 75.58 O ANISOU 3827 O HOH A 410 9715 10746 8257 1003 -384 -1147 O HETATM 3828 O HOH A 411 27.090 1.636 42.740 1.00 62.41 O ANISOU 3828 O HOH A 411 7473 8735 7507 129 306 -664 O HETATM 3829 O HOH A 413 43.358 -12.427 33.997 1.00 46.77 O ANISOU 3829 O HOH A 413 6102 5633 6035 -169 129 -80 O HETATM 3830 O HOH A 421 56.662 -8.102 52.406 1.00 54.74 O ANISOU 3830 O HOH A 421 7349 7013 6437 349 -342 113 O HETATM 3831 O HOH A 422 44.688 -11.814 22.904 1.00 48.65 O ANISOU 3831 O HOH A 422 6248 6084 6154 151 42 -413 O HETATM 3832 O HOH A 427 48.853 15.563 41.985 1.00 55.81 O ANISOU 3832 O HOH A 427 7247 6411 7546 126 -753 -551 O HETATM 3833 O HOH A 428 46.341 17.062 41.145 1.00 51.45 O ANISOU 3833 O HOH A 428 6743 5807 6997 214 -796 -609 O HETATM 3834 O HOH A 429 70.861 -8.228 31.056 1.00 64.11 O ANISOU 3834 O HOH A 429 7396 8533 8429 316 28 -100 O HETATM 3835 O HOH A 430 68.424 -2.559 33.509 1.00 52.40 O ANISOU 3835 O HOH A 430 6022 6823 7063 -9 -41 45 O HETATM 3836 O HOH A 431 57.402 -2.429 17.138 1.00 51.52 O ANISOU 3836 O HOH A 431 6275 7141 6160 207 450 245 O HETATM 3837 O HOH A 441 47.450 3.712 57.460 1.00 53.45 O ANISOU 3837 O HOH A 441 7048 7427 5831 604 -383 -608 O HETATM 3838 O HOH A 442 44.103 5.385 59.725 1.00 61.71 O ANISOU 3838 O HOH A 442 8050 8794 6603 788 -334 -804 O HETATM 3839 O HOH A 443 39.732 8.102 58.412 1.00 60.68 O ANISOU 3839 O HOH A 443 7787 8753 6518 867 -277 -1042 O HETATM 3840 O HOH A 444 40.194 17.720 56.544 1.00 74.32 O ANISOU 3840 O HOH A 444 9543 9844 8851 1189 -993 -1782 O HETATM 3841 O HOH A 445 32.481 14.368 54.000 1.00 67.77 O ANISOU 3841 O HOH A 445 8455 9543 7751 1129 -425 -1576 O HETATM 3842 O HOH A 446 37.082 10.575 47.687 1.00 54.43 O ANISOU 3842 O HOH A 446 6934 7245 6504 559 -314 -933 O HETATM 3843 O HOH A 447 43.377 12.993 47.379 1.00 60.11 O ANISOU 3843 O HOH A 447 7781 7518 7540 464 -615 -890 O HETATM 3844 O HOH A 448 46.076 13.334 47.605 1.00 60.22 O ANISOU 3844 O HOH A 448 7805 7410 7664 401 -704 -858 O HETATM 3845 O HOH A 449 41.473 7.168 51.911 1.00 53.39 O ANISOU 3845 O HOH A 449 6890 7252 6142 503 -264 -761 O HETATM 3846 O HOH A 450 46.408 -9.115 59.415 1.00 71.04 O ANISOU 3846 O HOH A 450 9556 9729 7709 298 135 451 O HETATM 3847 O HOH A 451 46.719 -5.386 64.039 1.00 82.68 O ANISOU 3847 O HOH A 451 11024 11676 8712 649 -4 164 O HETATM 3848 O HOH A 452 45.378 -3.714 62.158 1.00 67.89 O ANISOU 3848 O HOH A 452 9045 9735 7014 583 22 7 O HETATM 3849 O HOH A 454 44.341 14.758 36.928 1.00 46.79 O ANISOU 3849 O HOH A 454 6156 5335 6286 156 -555 -374 O HETATM 3850 O HOH A 455 41.201 14.735 37.316 1.00 55.37 O ANISOU 3850 O HOH A 455 7239 6534 7267 285 -550 -509 O HETATM 3851 O HOH A 456 67.626 8.479 36.861 1.00 66.64 O ANISOU 3851 O HOH A 456 7805 8138 9376 -473 -385 97 O HETATM 3852 O HOH A 457 71.290 1.962 34.909 1.00 72.46 O ANISOU 3852 O HOH A 457 8317 9316 9899 -244 -160 86 O HETATM 3853 O HOH A 460 45.513 -15.198 37.271 1.00 58.66 O ANISOU 3853 O HOH A 460 7722 7009 7556 -176 104 83 O HETATM 3854 O HOH A 461 40.697 -16.155 36.838 1.00 72.21 O ANISOU 3854 O HOH A 461 9356 8725 9356 -357 178 66 O HETATM 3855 O HOH A 462 38.687 -14.012 44.655 1.00 56.22 O ANISOU 3855 O HOH A 462 7326 7070 6964 -426 391 353 O HETATM 3856 O HOH A 463 42.230 -12.228 48.731 1.00 57.50 O ANISOU 3856 O HOH A 463 7625 7385 6840 -216 320 418 O HETATM 3857 O HOH A 464 49.073 -8.674 55.708 1.00 55.99 O ANISOU 3857 O HOH A 464 7606 7485 6181 252 -13 309 O HETATM 3858 O HOH A 466 64.321 -0.879 42.128 1.00 59.77 O ANISOU 3858 O HOH A 466 7345 7482 7885 48 -386 -119 O HETATM 3859 O HOH A 467 59.798 -7.046 46.516 1.00 67.57 O ANISOU 3859 O HOH A 467 8739 8473 8460 246 -338 -2 O HETATM 3860 O HOH A 468 66.074 -9.058 47.235 1.00 62.36 O ANISOU 3860 O HOH A 468 7931 7849 7914 448 -559 -67 O HETATM 3861 O HOH A 469 59.946 -2.224 46.466 1.00 58.59 O ANISOU 3861 O HOH A 469 7485 7355 7421 173 -410 -142 O HETATM 3862 O HOH A 470 59.211 -3.634 48.828 1.00 57.43 O ANISOU 3862 O HOH A 470 7440 7265 7115 256 -431 -118 O HETATM 3863 O HOH A 471 45.816 -13.646 28.298 1.00 66.05 O ANISOU 3863 O HOH A 471 8518 8077 8499 11 53 -260 O HETATM 3864 O HOH A 473 41.342 -13.226 35.273 1.00 57.01 O ANISOU 3864 O HOH A 473 7386 6924 7350 -255 165 -44 O HETATM 3865 O HOH A 475 29.367 -2.114 40.262 1.00 69.50 O ANISOU 3865 O HOH A 475 8489 9352 8565 -96 328 -440 O HETATM 3866 O HOH A 476 35.177 -5.794 55.311 1.00 75.46 O ANISOU 3866 O HOH A 476 9587 10644 8439 8 595 150 O HETATM 3867 O HOH A 486 34.484 12.191 34.160 1.00 53.97 O ANISOU 3867 O HOH A 486 6948 6684 6874 419 -387 -600 O HETATM 3868 O HOH A 490 58.849 12.153 31.522 1.00 82.72 O ANISOU 3868 O HOH A 490 10300 9922 11207 -457 -241 353 O HETATM 3869 O HOH A 491 58.604 12.975 28.629 1.00 59.90 O ANISOU 3869 O HOH A 491 7418 7047 8292 -507 -146 547 O HETATM 3870 O HOH A 492 57.856 13.737 51.141 1.00 67.55 O ANISOU 3870 O HOH A 492 8556 8107 9002 224 -1161 -926 O HETATM 3871 O HOH A 493 55.045 13.475 46.044 1.00 74.77 O ANISOU 3871 O HOH A 493 9517 8916 9977 63 -867 -619 O HETATM 3872 O HOH A 496 64.758 9.784 45.456 1.00 50.81 O ANISOU 3872 O HOH A 496 6095 6001 7210 -163 -864 -420 O HETATM 3873 O HOH A 497 51.273 14.793 39.772 1.00 57.00 O ANISOU 3873 O HOH A 497 7349 6509 7800 -38 -667 -334 O HETATM 3874 O HOH A 498 41.271 10.313 50.236 1.00 76.51 O ANISOU 3874 O HOH A 498 9815 9980 9275 549 -427 -911 O HETATM 3875 O HOH A 499 40.931 9.727 56.891 1.00 67.29 O ANISOU 3875 O HOH A 499 8646 9333 7587 843 -429 -1119 O HETATM 3876 O HOH A 500 56.249 -4.454 41.266 1.00 52.04 O ANISOU 3876 O HOH A 500 6700 6459 6614 59 -142 -19 O HETATM 3877 O HOH A 501 54.085 -10.672 47.798 1.00 53.90 O ANISOU 3877 O HOH A 501 7234 6708 6536 162 -140 214 O HETATM 3878 O HOH A 502 50.720 -14.420 43.666 1.00 62.81 O ANISOU 3878 O HOH A 502 8383 7620 7863 -6 3 278 O HETATM 3879 O HOH A 504 33.125 10.238 19.455 1.00 57.40 O ANISOU 3879 O HOH A 504 7528 7240 7042 544 -396 -191 O HETATM 3880 O HOH A 505 46.117 -12.899 34.292 1.00 56.91 O ANISOU 3880 O HOH A 505 7426 6882 7316 -103 96 -47 O HETATM 3881 O HOH A 506 52.961 -8.317 37.090 1.00 26.94 O ANISOU 3881 O HOH A 506 3576 3217 3443 24 13 12 O HETATM 3882 O HOH A 507 50.999 -12.305 37.405 1.00 31.39 O ANISOU 3882 O HOH A 507 4235 3665 4027 3 30 49 O HETATM 3883 O HOH A 508 53.408 -10.753 38.912 1.00 28.48 O ANISOU 3883 O HOH A 508 3841 3354 3625 54 -19 60 O HETATM 3884 O HOH A 509 53.455 -11.159 35.785 1.00 28.29 O ANISOU 3884 O HOH A 509 3767 3328 3654 66 11 1 O HETATM 3885 O HOH A 517 33.276 -1.530 31.775 1.00 46.52 O ANISOU 3885 O HOH A 517 5793 6039 5842 -13 85 -431 O HETATM 3886 O HOH A 518 31.411 -0.168 28.821 1.00 51.22 O ANISOU 3886 O HOH A 518 6355 6670 6435 88 -5 -529 O HETATM 3887 O HOH A 519 34.115 -1.340 28.993 1.00 46.59 O ANISOU 3887 O HOH A 519 5847 6003 5854 34 33 -425 O HETATM 3888 O HOH A 524 59.822 -10.366 21.064 1.00 72.62 O ANISOU 3888 O HOH A 524 8930 9637 9027 431 275 -190 O HETATM 3889 O HOH B 12 57.147 1.911 26.352 1.00 33.25 O ANISOU 3889 O HOH B 12 4098 4130 4407 107 524 491 O HETATM 3890 O HOH B 108 59.577 6.706 26.249 1.00 53.26 O ANISOU 3890 O HOH B 108 6580 6372 7286 -345 1325 537 O HETATM 3891 O HOH B 150 58.963 -6.590 21.618 1.00 44.18 O ANISOU 3891 O HOH B 150 5890 5930 4966 872 448 612 O HETATM 3892 O HOH B 158 67.859 7.414 24.212 1.00 62.16 O ANISOU 3892 O HOH B 158 6745 8116 8758 -715 1545 553 O HETATM 3893 O HOH B 176 68.321 -2.794 30.369 1.00 51.16 O ANISOU 3893 O HOH B 176 4520 7421 7499 -342 -487 941 O HETATM 3894 O HOH B 303 60.410 -7.794 19.339 1.00 64.31 O ANISOU 3894 O HOH B 303 8627 8342 7468 1001 923 745 O HETATM 3895 O HOH B 523 59.457 -5.628 17.139 1.00 71.35 O ANISOU 3895 O HOH B 523 9649 9187 8272 820 1091 902 O HETATM 3896 O HOH C 217 36.146 9.766 16.142 1.00 36.64 O ANISOU 3896 O HOH C 217 4746 4429 4747 -299 48 -140 O HETATM 3897 O HOH C 218 37.902 -1.057 20.077 1.00 29.44 O ANISOU 3897 O HOH C 218 3608 3762 3816 -285 -106 33 O HETATM 3898 O HOH C 219 21.815 1.833 -1.754 1.00 35.85 O ANISOU 3898 O HOH C 219 4411 4610 4600 -172 -212 206 O HETATM 3899 O HOH C 220 29.544 8.484 12.800 1.00 28.30 O ANISOU 3899 O HOH C 220 3569 3398 3786 -2 133 -139 O HETATM 3900 O HOH C 221 26.931 11.329 24.348 1.00 59.30 O ANISOU 3900 O HOH C 221 7825 7318 7390 -48 410 -440 O HETATM 3901 O HOH C 222 42.839 -18.098 12.957 1.00 58.11 O ANISOU 3901 O HOH C 222 7771 6782 7526 626 -74 238 O HETATM 3902 O HOH C 223 36.187 3.647 11.749 1.00 31.22 O ANISOU 3902 O HOH C 223 3838 3871 4152 -136 45 -39 O HETATM 3903 O HOH C 224 32.993 -2.303 24.964 1.00 38.11 O ANISOU 3903 O HOH C 224 4842 4910 4730 -446 -68 -33 O HETATM 3904 O HOH C 225 25.141 -11.297 13.306 1.00 35.82 O ANISOU 3904 O HOH C 225 4721 4454 4436 -503 -172 80 O HETATM 3905 O HOH C 226 27.396 3.347 23.979 1.00 37.60 O ANISOU 3905 O HOH C 226 4757 4859 4670 -267 215 -230 O HETATM 3906 O HOH C 227 12.658 3.218 11.158 1.00 65.15 O ANISOU 3906 O HOH C 227 7317 8994 8445 94 119 234 O HETATM 3907 O HOH C 228 24.808 -5.019 21.640 1.00 57.08 O ANISOU 3907 O HOH C 228 7111 7449 7127 -449 41 -16 O HETATM 3908 O HOH C 229 37.316 1.531 18.768 1.00 32.21 O ANISOU 3908 O HOH C 229 3973 4083 4182 -284 -51 -22 O HETATM 3909 O HOH C 230 34.212 -18.371 -11.470 1.00 54.89 O ANISOU 3909 O HOH C 230 8915 5861 6080 3 335 -425 O HETATM 3910 O HOH C 231 38.580 8.236 16.581 1.00 32.71 O ANISOU 3910 O HOH C 231 4153 4028 4245 -377 -9 -75 O HETATM 3911 O HOH C 232 14.554 -6.255 -4.251 1.00 52.75 O ANISOU 3911 O HOH C 232 6612 7075 6356 -896 -614 435 O HETATM 3912 O HOH C 233 26.746 11.822 1.277 1.00 35.66 O ANISOU 3912 O HOH C 233 4534 4231 4785 145 -20 114 O HETATM 3913 O HOH C 234 36.216 -14.271 1.253 1.00 39.81 O ANISOU 3913 O HOH C 234 5791 4418 4915 228 149 -116 O HETATM 3914 O HOH C 235 40.646 -1.160 15.152 1.00 32.65 O ANISOU 3914 O HOH C 235 3899 4175 4331 -124 -50 83 O HETATM 3915 O HOH C 236 27.696 -8.883 -12.054 1.00 50.10 O ANISOU 3915 O HOH C 236 7416 5930 5688 -525 -101 -68 O HETATM 3916 O HOH C 237 19.206 6.307 -8.565 1.00 55.63 O ANISOU 3916 O HOH C 237 6931 7161 7044 -162 -448 482 O HETATM 3917 O HOH C 238 43.398 -9.732 13.619 1.00 50.50 O ANISOU 3917 O HOH C 238 6245 6304 6638 296 -45 209 O HETATM 3918 O HOH C 239 30.026 4.492 23.284 1.00 39.57 O ANISOU 3918 O HOH C 239 5067 5016 4950 -289 153 -227 O HETATM 3919 O HOH C 240 23.974 11.575 -7.083 1.00 60.25 O ANISOU 3919 O HOH C 240 7697 7433 7764 46 -257 380 O HETATM 3920 O HOH C 241 37.237 -17.684 4.232 1.00 35.31 O ANISOU 3920 O HOH C 241 5373 3676 4369 346 93 -71 O HETATM 3921 O HOH C 242 24.877 0.822 13.833 1.00 31.65 O ANISOU 3921 O HOH C 242 3785 4103 4138 -116 83 -57 O HETATM 3922 O HOH C 243 15.394 -4.639 13.261 1.00 36.04 O ANISOU 3922 O HOH C 243 3982 5189 4524 -490 -34 200 O HETATM 3923 O HOH C 244 31.982 10.610 16.543 1.00 52.99 O ANISOU 3923 O HOH C 244 6866 6443 6826 -132 143 -217 O HETATM 3924 O HOH C 245 31.357 1.923 23.220 1.00 34.95 O ANISOU 3924 O HOH C 245 4439 4467 4376 -346 65 -151 O HETATM 3925 O HOH C 246 19.060 -17.387 -1.010 1.00 79.99 O ANISOU 3925 O HOH C 246 11144 9781 9466 -1218 -561 147 O HETATM 3926 O HOH C 248 23.278 4.342 -7.550 1.00 48.29 O ANISOU 3926 O HOH C 248 6184 6091 6072 -206 -278 291 O HETATM 3927 O HOH C 249 34.361 -20.862 18.480 1.00 41.09 O ANISOU 3927 O HOH C 249 6045 4486 5080 -154 -383 281 O HETATM 3928 O HOH C 250 34.807 -15.738 25.004 1.00 53.10 O ANISOU 3928 O HOH C 250 7116 6470 6588 -389 -413 330 O HETATM 3929 O HOH C 251 19.638 13.893 18.738 1.00 58.91 O ANISOU 3929 O HOH C 251 7410 7355 7618 586 565 -317 O HETATM 3930 O HOH C 252 31.359 8.582 14.654 1.00 53.38 O ANISOU 3930 O HOH C 252 6794 6564 6925 -87 124 -164 O HETATM 3931 O HOH C 253 15.832 -11.143 8.742 1.00 56.08 O ANISOU 3931 O HOH C 253 6980 7482 6847 -946 -340 286 O HETATM 3932 O HOH C 254 24.672 -3.592 19.575 1.00 35.50 O ANISOU 3932 O HOH C 254 4334 4693 4463 -355 60 -36 O HETATM 3933 O HOH C 255 24.792 7.435 -5.331 1.00 35.51 O ANISOU 3933 O HOH C 255 4516 4388 4590 -50 -186 256 O HETATM 3934 O HOH C 256 37.174 -13.189 -5.085 1.00 57.11 O ANISOU 3934 O HOH C 256 8171 6607 6923 267 338 -219 O HETATM 3935 O HOH C 257 17.146 -9.014 12.710 1.00 45.61 O ANISOU 3935 O HOH C 257 5511 6198 5621 -737 -173 210 O HETATM 3936 O HOH C 258 25.855 -1.083 19.409 1.00 33.85 O ANISOU 3936 O HOH C 258 4130 4434 4299 -262 101 -88 O HETATM 3937 O HOH C 259 27.393 -13.743 -1.674 1.00 45.61 O ANISOU 3937 O HOH C 259 6681 5244 5403 -424 -153 -67 O HETATM 3938 O HOH C 260 17.735 -6.305 12.038 1.00 36.39 O ANISOU 3938 O HOH C 260 4254 5027 4548 -543 -108 167 O HETATM 3939 O HOH C 261 41.295 -10.726 21.355 1.00 47.64 O ANISOU 3939 O HOH C 261 5984 5964 6154 -30 -300 304 O HETATM 3940 O HOH C 262 35.553 -6.263 20.118 1.00 39.33 O ANISOU 3940 O HOH C 262 4958 4947 5039 -240 -141 78 O HETATM 3941 O HOH C 263 30.289 0.156 -8.819 1.00 40.42 O ANISOU 3941 O HOH C 263 5503 4943 4913 -224 -3 68 O HETATM 3942 O HOH C 264 26.966 11.726 10.088 1.00 46.13 O ANISOU 3942 O HOH C 264 5862 5561 6105 175 148 -103 O HETATM 3943 O HOH C 265 20.168 0.749 19.988 1.00 50.15 O ANISOU 3943 O HOH C 265 5969 6745 6342 -171 259 -87 O HETATM 3944 O HOH C 266 12.305 -4.182 10.260 1.00 39.50 O ANISOU 3944 O HOH C 266 4210 5829 4969 -533 -131 342 O HETATM 3945 O HOH C 267 28.747 -12.189 20.288 1.00 36.54 O ANISOU 3945 O HOH C 267 4850 4531 4505 -496 -200 126 O HETATM 3946 O HOH C 268 44.670 5.017 17.786 1.00 38.34 O ANISOU 3946 O HOH C 268 4567 5028 4974 -483 -153 140 O HETATM 3947 O HOH C 269 19.441 8.439 -6.726 1.00 46.69 O ANISOU 3947 O HOH C 269 5734 5974 6031 9 -377 461 O HETATM 3948 O HOH C 270 41.127 -14.280 22.888 1.00 57.26 O ANISOU 3948 O HOH C 270 7370 7055 7330 7 -400 399 O HETATM 3949 O HOH C 271 21.135 -1.443 20.792 1.00 56.96 O ANISOU 3949 O HOH C 271 6896 7592 7154 -303 196 -62 O HETATM 3950 O HOH C 272 29.068 10.728 16.744 1.00 51.89 O ANISOU 3950 O HOH C 272 6695 6322 6699 -3 212 -244 O HETATM 3951 O HOH C 273 31.836 3.625 1.117 1.00 31.76 O ANISOU 3951 O HOH C 273 4024 3873 4170 -49 49 22 O HETATM 3952 O HOH C 274 37.268 -10.525 -4.267 1.00 50.52 O ANISOU 3952 O HOH C 274 7076 5931 6188 223 312 -164 O HETATM 3953 O HOH C 275 29.424 11.916 6.711 1.00 43.08 O ANISOU 3953 O HOH C 275 5522 5129 5719 81 79 -35 O HETATM 3954 O HOH C 276 32.144 -3.686 -11.354 1.00 45.18 O ANISOU 3954 O HOH C 276 6406 5453 5308 -232 117 -40 O HETATM 3955 O HOH C 277 25.734 -14.032 13.155 1.00 46.17 O ANISOU 3955 O HOH C 277 6230 5627 5686 -555 -230 102 O HETATM 3956 O HOH C 278 35.695 7.312 5.497 1.00 36.47 O ANISOU 3956 O HOH C 278 4576 4451 4829 -106 82 0 O HETATM 3957 O HOH C 279 27.208 -0.162 21.555 1.00 47.64 O ANISOU 3957 O HOH C 279 5934 6162 6006 -289 116 -124 O HETATM 3958 O HOH C 280 32.833 -25.517 14.571 1.00 52.06 O ANISOU 3958 O HOH C 280 8053 5420 6308 -179 -409 224 O HETATM 3959 O HOH C 281 35.553 -24.310 9.115 1.00 45.51 O ANISOU 3959 O HOH C 281 7222 4527 5541 219 -170 55 O HETATM 3960 O HOH C 282 36.140 4.505 -7.634 1.00 40.29 O ANISOU 3960 O HOH C 282 5306 4982 5020 -141 182 88 O HETATM 3961 O HOH C 283 30.741 -13.508 24.272 1.00 50.42 O ANISOU 3961 O HOH C 283 6684 6276 6198 -555 -287 210 O HETATM 3962 O HOH C 284 25.118 -10.281 -11.410 1.00 48.93 O ANISOU 3962 O HOH C 284 7307 5793 5491 -707 -252 -21 O HETATM 3963 O HOH C 285 13.333 4.796 9.359 1.00 47.59 O ANISOU 3963 O HOH C 285 5152 6655 6275 198 83 241 O HETATM 3964 O HOH C 286 23.974 -11.435 15.639 1.00 50.90 O ANISOU 3964 O HOH C 286 6574 6457 6309 -594 -170 106 O HETATM 3965 O HOH C 287 21.340 -18.636 -0.186 1.00 71.79 O ANISOU 3965 O HOH C 287 10289 8540 8447 -1063 -479 68 O HETATM 3966 O HOH C 288 25.938 -12.963 -3.772 1.00 41.46 O ANISOU 3966 O HOH C 288 6172 4776 4805 -541 -206 -46 O HETATM 3967 O HOH C 289 27.428 -13.921 -6.093 1.00 57.60 O ANISOU 3967 O HOH C 289 8455 6688 6741 -490 -136 -116 O HETATM 3968 O HOH C 290 18.565 8.795 -2.286 1.00 45.03 O ANISOU 3968 O HOH C 290 5360 5803 5946 171 -249 376 O HETATM 3969 O HOH C 291 43.384 -1.220 14.522 1.00 49.52 O ANISOU 3969 O HOH C 291 5924 6394 6497 -89 -52 153 O HETATM 3970 O HOH C 292 45.815 -4.388 14.675 1.00 59.21 O ANISOU 3970 O HOH C 292 7054 7677 7766 83 -69 258 O HETATM 3971 O HOH C 293 22.177 -2.809 19.020 1.00 34.29 O ANISOU 3971 O HOH C 293 4073 4643 4312 -334 108 -27 O HETATM 3972 O HOH C 294 26.179 2.323 21.867 1.00 37.17 O ANISOU 3972 O HOH C 294 4607 4835 4680 -216 201 -183 O HETATM 3973 O HOH C 296 32.071 -12.327 25.988 1.00 34.25 O ANISOU 3973 O HOH C 296 4586 4283 4144 -553 -297 216 O HETATM 3974 O HOH C 297 28.810 10.685 19.399 1.00 39.32 O ANISOU 3974 O HOH C 297 5157 4750 5035 -41 255 -302 O HETATM 3975 O HOH C 298 23.433 -9.367 -9.064 1.00 58.51 O ANISOU 3975 O HOH C 298 8255 7133 6841 -721 -328 58 O HETATM 3976 O HOH C 299 27.515 11.866 12.690 1.00 64.06 O ANISOU 3976 O HOH C 299 8182 7821 8336 140 190 -169 O HETATM 3977 O HOH C 303 31.688 -20.534 6.128 1.00 42.60 O ANISOU 3977 O HOH C 303 6621 4454 5112 -138 -161 -27 O HETATM 3978 O HOH C 304 6.506 -7.651 8.362 1.00 48.97 O ANISOU 3978 O HOH C 304 5092 7538 5977 -1062 -385 668 O HETATM 3979 O HOH C 305 27.371 -16.365 9.399 1.00 44.76 O ANISOU 3979 O HOH C 305 6362 5189 5457 -468 -244 60 O HETATM 3980 O HOH C 306 42.989 -8.550 3.008 1.00 41.90 O ANISOU 3980 O HOH C 306 5344 5135 5440 453 305 15 O HETATM 3981 O HOH C 308 24.589 9.123 23.893 1.00 46.67 O ANISOU 3981 O HOH C 308 6012 5892 5829 12 442 -382 O HETATM 3982 O HOH C 309 17.179 11.132 19.724 1.00 61.09 O ANISOU 3982 O HOH C 309 7406 7938 7866 544 609 -256 O HETATM 3983 O HOH C 310 45.004 7.827 10.352 1.00 52.00 O ANISOU 3983 O HOH C 310 6284 6710 6764 -409 9 145 O HETATM 3984 O HOH C 311 40.858 -0.730 -12.709 1.00 57.96 O ANISOU 3984 O HOH C 311 7763 7299 6960 0 549 -33 O HETATM 3985 O HOH C 312 30.586 -5.467 25.269 1.00 41.89 O ANISOU 3985 O HOH C 312 5342 5412 5161 -496 -80 14 O HETATM 3986 O HOH C 313 37.652 -14.570 -1.126 1.00 55.31 O ANISOU 3986 O HOH C 313 7848 6344 6825 345 263 -164 O HETATM 3987 O HOH C 314 36.952 13.212 0.823 1.00 60.56 O ANISOU 3987 O HOH C 314 7816 7364 7830 -231 62 107 O HETATM 3988 O HOH C 315 36.457 -21.591 20.142 1.00 77.68 O ANISOU 3988 O HOH C 315 10669 9094 9751 -34 -435 364 O HETATM 3989 O HOH C 317 14.645 -10.277 13.138 1.00 46.20 O ANISOU 3989 O HOH C 317 5495 6443 5615 -929 -218 299 O HETATM 3990 O HOH C 318 20.812 11.558 3.295 1.00 45.17 O ANISOU 3990 O HOH C 318 5474 5625 6063 368 -13 167 O HETATM 3991 O HOH C 319 35.512 13.971 -1.537 1.00 44.69 O ANISOU 3991 O HOH C 319 5871 5307 5803 -199 36 151 O HETATM 3992 O HOH C 321 32.785 -17.420 3.362 1.00 43.73 O ANISOU 3992 O HOH C 321 6549 4754 5311 -20 -36 -86 O HETATM 3993 O HOH C 322 29.870 -20.445 9.881 1.00 44.62 O ANISOU 3993 O HOH C 322 6730 4840 5383 -342 -273 67 O HETATM 3994 O HOH C 323 37.935 0.480 -13.348 1.00 44.09 O ANISOU 3994 O HOH C 323 6090 5479 5182 -137 385 5 O HETATM 3995 O HOH C 324 16.460 10.294 14.549 1.00 44.38 O ANISOU 3995 O HOH C 324 5106 5868 5890 545 399 -63 O HETATM 3996 O HOH C 325 25.446 -9.591 18.370 1.00 47.46 O ANISOU 3996 O HOH C 325 6057 6068 5908 -516 -111 73 O HETATM 3997 O HOH C 326 39.407 -12.572 25.181 1.00 44.96 O ANISOU 3997 O HOH C 326 5807 5593 5683 -222 -418 360 O HETATM 3998 O HOH C 327 20.158 7.435 -4.462 1.00 40.09 O ANISOU 3998 O HOH C 327 4875 5133 5226 19 -290 367 O HETATM 3999 O HOH C 328 29.611 10.767 11.510 1.00 50.29 O ANISOU 3999 O HOH C 328 6423 6092 6591 39 135 -134 O HETATM 4000 O HOH C 329 29.395 -8.644 28.130 1.00 50.88 O ANISOU 4000 O HOH C 329 6581 6593 6158 -675 -147 99 O HETATM 4001 O HOH C 330 47.654 7.576 -0.330 1.00 43.44 O ANISOU 4001 O HOH C 330 5093 5811 5601 -291 306 248 O HETATM 4002 O HOH C 331 7.810 12.019 2.787 1.00 62.40 O ANISOU 4002 O HOH C 331 6629 8671 8409 857 -103 666 O HETATM 4003 O HOH C 332 11.362 9.676 3.476 1.00 50.46 O ANISOU 4003 O HOH C 332 5422 6960 6790 542 -89 476 O HETATM 4004 O HOH C 333 39.766 11.395 12.738 1.00 55.08 O ANISOU 4004 O HOH C 333 7039 6781 7107 -411 5 -34 O HETATM 4005 O HOH C 334 47.450 6.131 -3.078 1.00 50.34 O ANISOU 4005 O HOH C 334 6009 6696 6421 -184 412 223 O HETATM 4006 O HOH C 335 10.212 -2.576 9.115 1.00 39.92 O ANISOU 4006 O HOH C 335 4043 6055 5069 -443 -141 433 O HETATM 4007 O HOH C 336 27.538 -8.008 -14.627 1.00 57.11 O ANISOU 4007 O HOH C 336 8398 6842 6460 -602 -114 -50 O HETATM 4008 O HOH C 337 34.260 8.801 14.770 1.00 44.96 O ANISOU 4008 O HOH C 337 5748 5493 5844 -190 79 -139 O HETATM 4009 O HOH C 338 39.261 -11.997 22.487 1.00 50.23 O ANISOU 4009 O HOH C 338 6444 6229 6414 -122 -330 294 O HETATM 4010 O HOH C 339 42.303 9.582 11.776 1.00 52.02 O ANISOU 4010 O HOH C 339 6480 6545 6741 -433 -8 51 O HETATM 4011 O HOH C 340 37.623 -22.105 11.889 1.00 44.29 O ANISOU 4011 O HOH C 340 6654 4627 5548 332 -173 144 O HETATM 4012 O HOH C 341 27.483 -19.040 10.364 1.00 58.54 O ANISOU 4012 O HOH C 341 8326 6786 7132 -528 -304 89 O HETATM 4013 O HOH C 342 15.740 -3.706 -5.059 1.00 46.69 O ANISOU 4013 O HOH C 342 5801 6261 5677 -696 -553 418 O HETATM 4014 O HOH C 343 46.893 7.871 5.463 1.00 49.01 O ANISOU 4014 O HOH C 343 5799 6442 6379 -363 130 218 O HETATM 4015 O HOH C 344 27.261 13.471 3.901 1.00 60.63 O ANISOU 4015 O HOH C 344 7755 7311 7971 188 36 48 O HETATM 4016 O HOH C 345 41.263 0.874 -10.633 1.00 47.97 O ANISOU 4016 O HOH C 345 6327 6076 5821 -15 493 17 O HETATM 4017 O HOH C 346 30.079 -8.601 22.912 1.00 48.67 O ANISOU 4017 O HOH C 346 6247 6190 6058 -467 -138 76 O HETATM 4018 O HOH C 347 37.616 -16.499 24.845 1.00 55.68 O ANISOU 4018 O HOH C 347 7424 6748 6985 -218 -463 401 O HETATM 4019 O HOH C 348 17.865 -0.566 -11.488 1.00 66.20 O ANISOU 4019 O HOH C 348 8544 8586 8025 -662 -616 466 O HETATM 4020 O HOH C 349 44.111 -7.623 15.150 1.00 50.67 O ANISOU 4020 O HOH C 349 6139 6445 6667 181 -88 239 O HETATM 4021 O HOH C 350 32.347 6.936 -9.586 1.00 42.27 O ANISOU 4021 O HOH C 350 5637 5178 5246 -207 16 185 O HETATM 4022 O HOH C 351 8.223 7.317 -2.840 1.00 64.70 O ANISOU 4022 O HOH C 351 7028 9085 8470 193 -515 842 O HETATM 4023 O HOH C 352 39.142 -9.652 -6.445 1.00 47.48 O ANISOU 4023 O HOH C 352 6675 5606 5758 302 444 -181 O HETATM 4024 O HOH C 353 42.796 -12.460 4.697 1.00 51.82 O ANISOU 4024 O HOH C 353 6791 6211 6687 584 256 22 O HETATM 4025 O HOH C 354 34.377 -1.759 -10.896 1.00 48.67 O ANISOU 4025 O HOH C 354 6707 5953 5831 -149 209 -24 O HETATM 4026 O HOH C 355 17.631 -9.770 10.215 1.00 50.66 O ANISOU 4026 O HOH C 355 6270 6734 6243 -764 -243 214 O HETATM 4027 O HOH C 356 29.831 -0.182 22.049 1.00 45.79 O ANISOU 4027 O HOH C 356 5753 5872 5774 -319 60 -113 O HETATM 4028 O HOH C 357 31.600 -7.821 26.885 1.00 44.37 O ANISOU 4028 O HOH C 357 5728 5708 5421 -567 -175 96 O HETATM 4029 O HOH C 358 32.356 -23.991 16.647 1.00 53.53 O ANISOU 4029 O HOH C 358 8010 5803 6525 -277 -431 265 O HETATM 4030 O HOH C 359 17.958 -3.889 -11.179 1.00 58.24 O ANISOU 4030 O HOH C 359 7712 7523 6892 -834 -622 390 O HETATM 4031 O HOH C 360 33.982 -14.001 27.061 1.00 48.89 O ANISOU 4031 O HOH C 360 6511 6072 5993 -524 -395 306 O HETATM 4032 O HOH C 361 12.879 7.238 -3.020 1.00 51.57 O ANISOU 4032 O HOH C 361 5800 7032 6762 128 -418 611 O HETATM 4033 O HOH C 362 34.551 -24.174 12.990 1.00 46.86 O ANISOU 4033 O HOH C 362 7257 4813 5734 33 -305 169 O HETATM 4034 O HOH C 363 37.067 -4.062 19.578 1.00 42.97 O ANISOU 4034 O HOH C 363 5349 5441 5535 -223 -121 64 O HETATM 4035 O HOH C 364 26.526 -13.748 1.140 1.00 40.83 O ANISOU 4035 O HOH C 364 5934 4710 4869 -462 -194 -23 O HETATM 4036 O HOH C 365 36.157 8.829 3.053 1.00 45.53 O ANISOU 4036 O HOH C 365 5767 5573 5959 -130 87 37 O HETATM 4037 O HOH C 366 19.423 11.529 6.933 1.00 49.03 O ANISOU 4037 O HOH C 366 5874 6187 6566 463 106 91 O HETATM 4038 O HOH C 367 30.420 11.201 9.071 1.00 53.13 O ANISOU 4038 O HOH C 367 6792 6424 6969 28 102 -85 O HETATM 4039 O HOH C 368 41.332 9.573 -7.114 1.00 53.45 O ANISOU 4039 O HOH C 368 6838 6757 6716 -304 263 200 O HETATM 4040 O HOH C 369 42.628 2.415 19.653 1.00 61.68 O ANISOU 4040 O HOH C 369 7577 7943 7915 -403 -161 107 O HETATM 4041 O HOH C 370 42.596 14.373 -1.880 1.00 51.52 O ANISOU 4041 O HOH C 370 6602 6398 6576 -500 126 234 O HETATM 4042 O HOH C 371 45.005 12.941 -3.053 1.00 61.02 O ANISOU 4042 O HOH C 371 7657 7787 7743 -525 212 274 O HETATM 4043 O HOH C 372 33.309 11.726 2.848 1.00 60.87 O ANISOU 4043 O HOH C 372 7810 7392 7925 -72 50 42 O HETATM 4044 O HOH C 373 7.878 -0.871 2.623 1.00 47.10 O ANISOU 4044 O HOH C 373 4805 7089 6002 -444 -421 677 O HETATM 4045 O HOH C 374 36.210 5.820 -3.832 1.00 47.69 O ANISOU 4045 O HOH C 374 6120 5906 6093 -113 144 81 O HETATM 4046 O HOH C 376 45.851 -1.558 10.544 1.00 62.17 O ANISOU 4046 O HOH C 376 7409 8073 8141 59 65 196 O HETATM 4047 O HOH C 377 45.277 -0.606 17.220 1.00 68.93 O ANISOU 4047 O HOH C 377 8303 8955 8933 -201 -147 228 O HETATM 4048 O HOH C 378 30.918 -12.583 -11.480 1.00 57.90 O ANISOU 4048 O HOH C 378 8709 6676 6615 -315 101 -227 O HETATM 4049 O HOH C 379 11.124 6.952 -1.047 1.00 51.89 O ANISOU 4049 O HOH C 379 5642 7229 6843 187 -367 631 O HETATM 4050 O HOH C 380 45.029 -17.184 14.045 1.00 67.00 O ANISOU 4050 O HOH C 380 8674 8057 8725 712 -85 320 O HETATM 4051 O HOH C 381 23.610 2.014 22.674 1.00 45.94 O ANISOU 4051 O HOH C 381 5642 6058 5754 -204 271 -184 O HETATM 4052 O HOH C 382 18.039 12.451 10.916 1.00 52.50 O ANISOU 4052 O HOH C 382 6281 6670 6997 606 277 -9 O HETATM 4053 O HOH C 383 6.974 -5.131 7.366 1.00 52.60 O ANISOU 4053 O HOH C 383 5482 7954 6551 -796 -337 641 O HETATM 4054 O HOH C 384 7.646 -2.148 10.094 1.00 72.79 O ANISOU 4054 O HOH C 384 7932 10490 9236 -428 -98 525 O HETATM 4055 O HOH C 385 44.103 -12.857 7.517 1.00 56.21 O ANISOU 4055 O HOH C 385 7218 6825 7316 629 183 109 O HETATM 4056 O HOH C 386 18.130 -5.067 19.596 1.00 50.45 O ANISOU 4056 O HOH C 386 5970 6933 6264 -513 105 73 O HETATM 4057 O HOH C 387 18.085 12.584 13.875 1.00 70.32 O ANISOU 4057 O HOH C 387 8584 8932 9202 619 393 -109 O HETATM 4058 O HOH C 388 20.625 -5.192 18.882 1.00 56.00 O ANISOU 4058 O HOH C 388 6805 7466 7005 -468 57 40 O HETATM 4059 O HOH C 389 18.444 -6.979 16.213 1.00 63.12 O ANISOU 4059 O HOH C 389 7664 8433 7885 -585 -33 129 O HETATM 4060 O HOH C 390 13.864 -14.911 11.336 1.00 61.00 O ANISOU 4060 O HOH C 390 7701 8183 7295 -1328 -429 386 O HETATM 4061 O HOH C 391 10.968 -15.710 11.114 1.00 53.94 O ANISOU 4061 O HOH C 391 6670 7519 6307 -1588 -510 511 O HETATM 4062 O HOH C 392 2.541 -12.069 6.848 1.00 69.00 O ANISOU 4062 O HOH C 392 7564 10421 8231 -1790 -700 956 O HETATM 4063 O HOH C 393 5.985 -9.906 4.221 1.00 53.00 O ANISOU 4063 O HOH C 393 5830 7974 6333 -1412 -665 770 O HETATM 4064 O HOH C 394 18.574 -12.374 6.846 1.00 49.77 O ANISOU 4064 O HOH C 394 6481 6404 6026 -883 -358 206 O HETATM 4065 O HOH C 395 21.359 -13.006 12.753 1.00 48.12 O ANISOU 4065 O HOH C 395 6285 6121 5878 -762 -251 156 O HETATM 4066 O HOH C 396 24.099 -14.341 16.574 1.00 66.29 O ANISOU 4066 O HOH C 396 8700 8308 8177 -711 -245 154 O HETATM 4067 O HOH C 397 11.140 -8.792 18.804 1.00 54.22 O ANISOU 4067 O HOH C 397 6099 7935 6569 -958 14 348 O HETATM 4068 O HOH C 400 29.031 -11.206 -12.881 1.00 51.00 O ANISOU 4068 O HOH C 400 7798 5895 5684 -487 -11 -164 O HETATM 4069 O HOH C 401 42.998 -9.839 -8.180 1.00 69.40 O ANISOU 4069 O HOH C 401 9385 8477 8506 538 690 -197 O HETATM 4070 O HOH C 402 41.289 -3.553 -13.606 1.00 66.02 O ANISOU 4070 O HOH C 402 8945 8253 7886 108 649 -117 O HETATM 4071 O HOH C 407 26.200 5.264 25.692 1.00 60.41 O ANISOU 4071 O HOH C 407 7712 7750 7491 -231 323 -311 O HETATM 4072 O HOH C 408 9.052 0.158 -0.260 1.00 49.16 O ANISOU 4072 O HOH C 408 5224 7192 6261 -407 -509 685 O HETATM 4073 O HOH C 414 39.141 6.826 -7.962 1.00 48.70 O ANISOU 4073 O HOH C 414 6306 6113 6086 -199 255 137 O HETATM 4074 O HOH C 415 37.365 4.359 -5.619 1.00 54.29 O ANISOU 4074 O HOH C 415 6993 6777 6860 -105 209 71 O HETATM 4075 O HOH C 416 39.954 -17.644 14.424 1.00 54.76 O ANISOU 4075 O HOH C 416 7413 6357 7035 352 -162 215 O HETATM 4076 O HOH C 417 36.627 -23.652 16.670 1.00 65.70 O ANISOU 4076 O HOH C 417 9422 7324 8217 128 -370 294 O HETATM 4077 O HOH C 418 42.147 -23.177 14.724 1.00 62.09 O ANISOU 4077 O HOH C 418 8736 6908 7948 705 -209 319 O HETATM 4078 O HOH C 425 28.409 -8.078 21.340 1.00 54.91 O ANISOU 4078 O HOH C 425 6995 7002 6866 -455 -95 49 O HETATM 4079 O HOH C 426 10.372 -5.122 -2.544 1.00 51.65 O ANISOU 4079 O HOH C 426 6001 7330 6292 -928 -688 632 O HETATM 4080 O HOH C 433 21.479 2.876 20.754 1.00 51.93 O ANISOU 4080 O HOH C 433 6284 6870 6577 -91 308 -160 O HETATM 4081 O HOH C 434 19.639 4.294 21.698 1.00 52.56 O ANISOU 4081 O HOH C 434 6307 7023 6641 6 418 -190 O HETATM 4082 O HOH C 435 20.655 6.266 24.028 1.00 68.73 O ANISOU 4082 O HOH C 435 8515 8979 8620 40 509 -299 O HETATM 4083 O HOH C 436 24.617 15.853 8.000 1.00 62.42 O ANISOU 4083 O HOH C 436 8023 7462 8233 410 152 -47 O HETATM 4084 O HOH C 437 24.443 14.819 4.128 1.00 70.95 O ANISOU 4084 O HOH C 437 9025 8610 9325 357 42 77 O HETATM 4085 O HOH C 438 30.934 -10.202 26.866 1.00 82.37 O ANISOU 4085 O HOH C 438 10608 10483 10207 -608 -223 153 O HETATM 4086 O HOH C 439 32.492 -15.828 23.707 1.00 50.60 O ANISOU 4086 O HOH C 439 6835 6149 6243 -464 -364 275 O HETATM 4087 O HOH C 472 29.566 -11.295 28.911 1.00 67.21 O ANISOU 4087 O HOH C 472 8746 8615 8177 -751 -237 187 O HETATM 4088 O HOH C 477 10.238 -8.236 -5.752 1.00 79.96 O ANISOU 4088 O HOH C 477 9950 10813 9618 -1321 -885 656 O HETATM 4089 O HOH C 478 18.853 -14.455 -8.248 1.00 68.24 O ANISOU 4089 O HOH C 478 9757 8354 7818 -1253 -615 147 O HETATM 4090 O HOH C 479 15.781 9.622 17.453 1.00 64.07 O ANISOU 4090 O HOH C 479 7573 8464 8308 520 514 -127 O HETATM 4091 O HOH C 481 23.873 11.569 -2.711 1.00 62.39 O ANISOU 4091 O HOH C 481 7868 7697 8140 160 -149 265 O HETATM 4092 O HOH C 484 46.626 2.400 10.637 1.00 51.67 O ANISOU 4092 O HOH C 484 6038 6809 6786 -156 38 212 O HETATM 4093 O HOH C 487 12.119 4.773 -5.832 1.00 57.51 O ANISOU 4093 O HOH C 487 6605 7883 7362 -165 -597 704 O HETATM 4094 O HOH C 488 8.862 4.058 -5.779 1.00 69.13 O ANISOU 4094 O HOH C 488 7798 9645 8825 -236 -710 871 O HETATM 4095 O HOH C 489 41.979 0.248 20.411 1.00 50.05 O ANISOU 4095 O HOH C 489 6107 6466 6442 -346 -177 123 O HETATM 4096 O HOH C 494 13.758 -11.478 6.486 1.00 80.14 O ANISOU 4096 O HOH C 494 9982 10638 9828 -1102 -448 374 O HETATM 4097 O HOH C 503 11.357 9.834 6.176 1.00 56.75 O ANISOU 4097 O HOH C 503 6202 7767 7593 614 51 382 O HETATM 4098 O HOH C 510 32.557 9.489 1.737 1.00 28.71 O ANISOU 4098 O HOH C 510 3680 3388 3840 -50 47 50 O HETATM 4099 O HOH C 511 29.591 9.118 0.484 1.00 27.49 O ANISOU 4099 O HOH C 511 3507 3249 3688 9 2 84 O HETATM 4100 O HOH C 512 31.173 6.692 1.643 1.00 27.56 O ANISOU 4100 O HOH C 512 3485 3305 3680 -30 37 38 O HETATM 4101 O HOH C 513 30.044 10.695 3.231 1.00 29.56 O ANISOU 4101 O HOH C 513 3785 3459 3988 35 36 36 O HETATM 4102 O HOH C 515 40.211 10.223 15.373 1.00 51.39 O ANISOU 4102 O HOH C 515 6547 6371 6607 -458 -26 -45 O HETATM 4103 O HOH C 521 17.338 -2.401 21.495 1.00 60.44 O ANISOU 4103 O HOH C 521 7147 8286 7532 -377 255 6 O HETATM 4104 O HOH C 522 18.395 2.325 23.220 1.00 64.15 O ANISOU 4104 O HOH C 522 7702 8641 8030 -111 435 -156 O HETATM 4105 O HOH C 525 31.610 -0.637 -10.980 1.00 59.70 O ANISOU 4105 O HOH C 525 8079 7363 7242 -244 63 40 O HETATM 4106 O HOH C 526 39.739 12.767 -1.536 1.00 75.32 O ANISOU 4106 O HOH C 526 9634 9346 9637 -331 111 167 O HETATM 4107 O HOH D 11 42.578 -3.516 2.687 1.00 33.38 O ANISOU 4107 O HOH D 11 4583 3819 4281 502 565 415 O HETATM 4108 O HOH D 89 47.594 4.871 3.248 1.00 41.28 O ANISOU 4108 O HOH D 89 4926 5481 5279 -270 -224 979 O HETATM 4109 O HOH D 92 44.047 -8.465 0.197 1.00 51.89 O ANISOU 4109 O HOH D 92 6909 6105 6703 1047 1143 384 O HETATM 4110 O HOH D 134 43.780 1.127 -9.065 1.00 45.02 O ANISOU 4110 O HOH D 134 6496 5233 5377 -44 1392 27 O HETATM 4111 O HOH D 182 49.246 -9.044 -6.172 1.00 58.14 O ANISOU 4111 O HOH D 182 6998 7142 7952 1326 2131 576 O HETATM 4112 O HOH D 306 50.285 6.009 2.862 1.00 53.11 O ANISOU 4112 O HOH D 306 5982 7221 6978 -434 -273 1124 O HETATM 4113 O HOH D 307 43.191 -6.047 3.671 1.00 36.62 O ANISOU 4113 O HOH D 307 4532 4573 4807 345 275 44 O HETATM 4114 O HOH D 403 49.619 -3.287 -13.710 1.00 74.27 O ANISOU 4114 O HOH D 403 9874 8700 9644 343 3015 269 O HETATM 4115 O HOH D 404 51.547 -11.159 -9.863 1.00 72.85 O ANISOU 4115 O HOH D 404 8860 8848 9973 1642 3029 651 O HETATM 4116 O HOH D 483 44.533 -11.785 1.065 1.00 67.85 O ANISOU 4116 O HOH D 483 9199 7958 8621 1420 1246 371 O CONECT 121 3599 CONECT 1646 3628 CONECT 1668 3628 CONECT 1750 3628 CONECT 1769 3628 CONECT 1920 3629 CONECT 3445 3658 CONECT 3467 3658 CONECT 3549 3658 CONECT 3568 3658 CONECT 3599 121 3601 3881 3882 CONECT 3599 3883 3884 CONECT 3600 3601 3602 3603 3604 CONECT 3601 3599 3600 CONECT 3602 3600 CONECT 3603 3600 CONECT 3604 3600 3605 CONECT 3605 3604 3606 3607 3608 CONECT 3606 3605 CONECT 3607 3605 CONECT 3608 3605 3609 CONECT 3609 3608 3610 CONECT 3610 3609 3611 3612 CONECT 3611 3610 3616 CONECT 3612 3610 3613 3614 CONECT 3613 3612 CONECT 3614 3612 3615 3616 CONECT 3615 3614 CONECT 3616 3611 3614 3617 CONECT 3617 3616 3618 3627 CONECT 3618 3617 3619 CONECT 3619 3618 3620 CONECT 3620 3619 3621 3627 CONECT 3621 3620 3622 3623 CONECT 3622 3621 CONECT 3623 3621 3624 CONECT 3624 3623 3625 3626 CONECT 3625 3624 CONECT 3626 3624 3627 CONECT 3627 3617 3620 3626 CONECT 3628 1646 1668 1750 1769 CONECT 3629 1920 3631 4098 4099 CONECT 3629 4100 4101 CONECT 3630 3631 3632 3633 3634 CONECT 3631 3629 3630 CONECT 3632 3630 CONECT 3633 3630 CONECT 3634 3630 3635 CONECT 3635 3634 3636 3637 3638 CONECT 3636 3635 CONECT 3637 3635 CONECT 3638 3635 3639 CONECT 3639 3638 3640 CONECT 3640 3639 3641 3642 CONECT 3641 3640 3646 CONECT 3642 3640 3643 3644 CONECT 3643 3642 CONECT 3644 3642 3645 3646 CONECT 3645 3644 CONECT 3646 3641 3644 3647 CONECT 3647 3646 3648 3657 CONECT 3648 3647 3649 CONECT 3649 3648 3650 CONECT 3650 3649 3651 3657 CONECT 3651 3650 3652 3653 CONECT 3652 3651 CONECT 3653 3651 3654 CONECT 3654 3653 3655 3656 CONECT 3655 3654 CONECT 3656 3654 3657 CONECT 3657 3647 3650 3656 CONECT 3658 3445 3467 3549 3568 CONECT 3881 3599 CONECT 3882 3599 CONECT 3883 3599 CONECT 3884 3599 CONECT 4098 3629 CONECT 4099 3629 CONECT 4100 3629 CONECT 4101 3629 MASTER 397 0 6 20 18 0 18 6 4112 4 80 40 END
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Related entries of code: 3gj5
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
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Protein Sequence Similarity
No similar entries are found!
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
3gj6
RCSB PDB
PDBbind
34-mer
3qbr
RCSB PDB
PDBbind
34-mer
Entry Information
PDB ID
3gj5
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
GTP-binding nuclear protein Ran
Ligand Name
34-mer
EC.Number
E.C.-.-.-.-
Resolution
1.79(Å)
Affinity (Kd/Ki/IC50)
Kd=47uM
Release Year
2009
Protein/NA Sequence
Check fasta file
Primary Reference
(2009) J.Mol.Biol. Vol. 391: pp. 375-389
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):
P49791
P62826
Entrez Gene ID
NCBI Entrez Gene ID:
5901
ASD
Information of known allosteric effects of PDB entries
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