HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 20-JUL-12 4G7G TITLE STEROL 14-ALPHA DEMETHYLASE (CYP51) FROM TRYPANOSOMA BRUCEI IN COMPLEX TITLE 2 WITH THE VNI DERIVATIVE (R)-N-(1-(3,4'-DIFLUOROBIPHENYL-4-YL)-2-(1H- TITLE 3 IMIDAZOL-1-YL)ETHYL)-4-(5-PHENYL-1,3,4-OXADIAZOL-2-YL)BENZAMIDE TITLE 4 [VNI/VNF (VFV)] COMPND MOL_ID: 1; COMPND 2 MOLECULE: STEROL 14-ALPHA-DEMETHYLASE; COMPND 3 CHAIN: A, B, C, D; COMPND 4 FRAGMENT: UNP RESIDUES 29-476; COMPND 5 SYNONYM: CYP51; COMPND 6 EC: 1.14.13.70; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA BRUCEI; SOURCE 3 ORGANISM_TAXID: 5691; SOURCE 4 GENE: CYP51, TB11.02.4080; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: HMS174; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCW KEYWDS CYTOCHROME P450 FOLD, HEME, MONOOXYGENASE, STEROL BIOSYNTHESIS, KEYWDS 2 EUKARYOTIC MEMBRANE BIOGENESIS, CYTOCHROME P450 REDUCTASE, KEYWDS 3 ENDOPLASMIC RETICULUM MEMBRANE, OXIDOREDUCTASE-OXIDOREDUCTASE KEYWDS 4 INHIBITOR COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR T.Y.HARGROVE,Z.WAWRZAK,M.R.WATERMAN,G.I.LEPESHEVA JRNL AUTH T.Y.HARGROVE,Z.WAWRZAK,M.R.WATERMAN,G.I.LEPESHEVA JRNL TITL CYP51 STRUCTURE-BASED VNI SCAFFOLD DEVELOPMENT JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.05 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.6.0117 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.82 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0 REMARK 3 NUMBER OF REFLECTIONS : 114765 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.166 REMARK 3 R VALUE (WORKING SET) : 0.163 REMARK 3 FREE R VALUE : 0.226 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 6065 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.05 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10 REMARK 3 REFLECTION IN BIN (WORKING SET) : 8323 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.90 REMARK 3 BIN R VALUE (WORKING SET) : 0.2050 REMARK 3 BIN FREE R VALUE SET COUNT : 452 REMARK 3 BIN FREE R VALUE : 0.3010 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 14228 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 336 REMARK 3 SOLVENT ATOMS : 504 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 37.85 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.80 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.91000 REMARK 3 B22 (A**2) : -0.60000 REMARK 3 B33 (A**2) : 0.09000 REMARK 3 B12 (A**2) : -0.72000 REMARK 3 B13 (A**2) : 0.32000 REMARK 3 B23 (A**2) : 0.04000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.172 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.137 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.406 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 14940 ; 0.008 ; 0.020 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 20272 ; 1.976 ; 2.004 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1788 ; 5.385 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 652 ;36.073 ;23.252 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2596 ;15.321 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 120 ;20.936 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2184 ; 0.076 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11364 ; 0.006 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): 14940 ; 2.287 ; 3.000 REMARK 3 SPHERICITY; FREE ATOMS (A**2): 159 ;20.980 ; 5.000 REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 14911 ;16.799 ; 5.000 REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT REMARK 3 U VALUES : REFINED INDIVIDUALLY REMARK 4 REMARK 4 4G7G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-AUG-12. REMARK 100 THE RCSB ID CODE IS RCSB073833. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-APR-12 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.3 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 21-ID-F REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872 REMARK 200 MONOCHROMATOR : DIAMOND(111) REMARK 200 OPTICS : BE LENSES/DIAMOND LAUE MONO REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 120831 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050 REMARK 200 RESOLUTION RANGE LOW (A) : 29.817 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.600 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0 REMARK 200 DATA REDUNDANCY : 4.600 REMARK 200 R MERGE (I) : 0.04600 REMARK 200 R SYM (I) : 0.04600 REMARK 200 FOR THE DATA SET : 31.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.09 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0 REMARK 200 DATA REDUNDANCY IN SHELL : 4.50 REMARK 200 R MERGE FOR SHELL (I) : 0.58000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 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: MOLREP REMARK 200 STARTING MODEL: PDB ENTRY 3G1Q REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.63 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: POTASSIUM PHOSPHATE, SODIUM CHLORIDE, REMARK 280 GLYCEROL, PEG3350, N-TETRADECYL-BETA-D-MALTOSIDE, PH 7.3, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 294K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,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 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 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: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A 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: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C 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: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 ILE A 41 -10.06 78.97 REMARK 500 SER A 51 87.59 -151.28 REMARK 500 ALA A 115 -127.72 54.51 REMARK 500 GLN A 293 -71.02 -65.66 REMARK 500 ILE B 41 -56.00 75.41 REMARK 500 ALA B 115 -125.12 59.29 REMARK 500 TRP B 158 56.13 -111.71 REMARK 500 LEU B 448 56.02 -90.69 REMARK 500 ARG B 475 150.91 -47.41 REMARK 500 ILE C 41 -57.08 73.29 REMARK 500 ALA C 115 -122.29 53.63 REMARK 500 LEU C 134 50.83 -105.07 REMARK 500 ALA C 417 176.29 178.66 REMARK 500 PRO C 453 154.58 -49.08 REMARK 500 ILE D 41 -51.79 71.17 REMARK 500 SER D 51 80.60 -154.94 REMARK 500 ALA D 115 -127.99 57.37 REMARK 500 TRP D 158 50.16 -113.50 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 HEM D 501 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 VFV D 502 NAX REMARK 620 2 HEM D 501 NA 81.8 REMARK 620 3 HEM D 501 NB 104.5 83.4 REMARK 620 4 HEM D 501 NC 105.9 167.6 85.3 REMARK 620 5 HEM D 501 ND 74.2 94.1 177.3 97.3 REMARK 620 6 CYS D 422 SG 168.0 90.3 83.5 83.5 97.4 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM A 501 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 VFV A 502 NAX REMARK 620 2 HEM A 501 NA 89.9 REMARK 620 3 HEM A 501 NB 92.4 86.0 REMARK 620 4 HEM A 501 NC 103.3 166.6 91.1 REMARK 620 5 HEM A 501 ND 88.6 85.8 171.8 96.6 REMARK 620 6 CYS A 422 SG 178.8 89.6 86.5 77.1 92.5 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM C 501 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 VFV C 502 NAX REMARK 620 2 HEM C 501 NA 97.5 REMARK 620 3 HEM C 501 NB 94.6 85.3 REMARK 620 4 HEM C 501 NC 101.4 159.7 85.7 REMARK 620 5 HEM C 501 ND 92.9 90.7 171.8 95.9 REMARK 620 6 CYS C 422 SG 174.3 85.8 80.9 74.8 91.7 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 HEM B 501 FE REMARK 620 N RES CSSEQI ATOM REMARK 620 1 VFV B 502 NAX REMARK 620 2 HEM B 501 NA 78.3 REMARK 620 3 HEM B 501 NB 85.3 86.2 REMARK 620 4 HEM B 501 NC 82.5 160.1 87.0 REMARK 620 5 HEM B 501 ND 84.4 89.8 169.5 93.5 REMARK 620 6 CYS B 422 SG 173.4 104.4 89.0 94.2 101.5 REMARK 620 N 1 2 3 4 5 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VFV A 502 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VFV B 502 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VFV C 502 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VFV D 502 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3GW9 RELATED DB: PDB REMARK 900 STEROL 14-ALPHA DEMETHYLASE (CYP51) FROM TRYPANOSOMA BRUCEI REMARK 900 IN COMPLEX WITH VNI REMARK 900 RELATED ID: 4G3J RELATED DB: PDB REMARK 900 STEROL 14-ALPHA DEMETHYLASE (CYP51) FROM TRYPANOSOMA BRUCEI REMARK 900 IN COMPLEX WITH THE VNI DERIVATIVE (S)-N-(1-(2,4- REMARK 900 DICHLOROPHENYL)-2-(1H-1,2,4-TRIAZOL-1-YL)ETHYL)-4-(5-PHENYL REMARK 900 -1,3,4-OXADIAZOL-2-YL)BENZAMIDE [S-VNI-TRIAZOLE (VNT)] DBREF 4G7G A 29 476 UNP Q385E8 Q385E8_TRYB2 29 476 DBREF 4G7G B 29 476 UNP Q385E8 Q385E8_TRYB2 29 476 DBREF 4G7G C 29 476 UNP Q385E8 Q385E8_TRYB2 29 476 DBREF 4G7G D 29 476 UNP Q385E8 Q385E8_TRYB2 29 476 SEQADV 4G7G GLY A 29 UNP Q385E8 PRO 29 ENGINEERED MUTATION SEQADV 4G7G LYS A 30 UNP Q385E8 THR 30 ENGINEERED MUTATION SEQADV 4G7G LEU A 31 UNP Q385E8 ASP 31 ENGINEERED MUTATION SEQADV 4G7G GLY B 29 UNP Q385E8 PRO 29 ENGINEERED MUTATION SEQADV 4G7G LYS B 30 UNP Q385E8 THR 30 ENGINEERED MUTATION SEQADV 4G7G LEU B 31 UNP Q385E8 ASP 31 ENGINEERED MUTATION SEQADV 4G7G GLY C 29 UNP Q385E8 PRO 29 ENGINEERED MUTATION SEQADV 4G7G LYS C 30 UNP Q385E8 THR 30 ENGINEERED MUTATION SEQADV 4G7G LEU C 31 UNP Q385E8 ASP 31 ENGINEERED MUTATION SEQADV 4G7G GLY D 29 UNP Q385E8 PRO 29 ENGINEERED MUTATION SEQADV 4G7G LYS D 30 UNP Q385E8 THR 30 ENGINEERED MUTATION SEQADV 4G7G LEU D 31 UNP Q385E8 ASP 31 ENGINEERED MUTATION SEQRES 1 A 448 GLY LYS LEU PRO PRO VAL TYR PRO VAL THR VAL PRO ILE SEQRES 2 A 448 LEU GLY HIS ILE ILE GLN PHE GLY LYS SER PRO LEU GLY SEQRES 3 A 448 PHE MET GLN GLU CYS LYS ARG GLN LEU LYS SER GLY ILE SEQRES 4 A 448 PHE THR ILE ASN ILE VAL GLY LYS ARG VAL THR ILE VAL SEQRES 5 A 448 GLY ASP PRO HIS GLU HIS SER ARG PHE PHE LEU PRO ARG SEQRES 6 A 448 ASN GLU VAL LEU SER PRO ARG GLU VAL TYR SER PHE MET SEQRES 7 A 448 VAL PRO VAL PHE GLY GLU GLY VAL ALA TYR ALA ALA PRO SEQRES 8 A 448 TYR PRO ARG MET ARG GLU GLN LEU ASN PHE LEU ALA GLU SEQRES 9 A 448 GLU LEU THR ILE ALA LYS PHE GLN ASN PHE VAL PRO ALA SEQRES 10 A 448 ILE GLN HIS GLU VAL ARG LYS PHE MET ALA ALA ASN TRP SEQRES 11 A 448 ASP LYS ASP GLU GLY GLU ILE ASN LEU LEU GLU ASP CYS SEQRES 12 A 448 SER THR MET ILE ILE ASN THR ALA CYS GLN CYS LEU PHE SEQRES 13 A 448 GLY GLU ASP LEU ARG LYS ARG LEU ASP ALA ARG ARG PHE SEQRES 14 A 448 ALA GLN LEU LEU ALA LYS MET GLU SER SER LEU ILE PRO SEQRES 15 A 448 ALA ALA VAL PHE LEU PRO ILE LEU LEU LYS LEU PRO LEU SEQRES 16 A 448 PRO GLN SER ALA ARG CYS HIS GLU ALA ARG THR GLU LEU SEQRES 17 A 448 GLN LYS ILE LEU SER GLU ILE ILE ILE ALA ARG LYS GLU SEQRES 18 A 448 GLU GLU VAL ASN LYS ASP SER SER THR SER ASP LEU LEU SEQRES 19 A 448 SER GLY LEU LEU SER ALA VAL TYR ARG ASP GLY THR PRO SEQRES 20 A 448 MET SER LEU HIS GLU VAL CYS GLY MET ILE VAL ALA ALA SEQRES 21 A 448 MET PHE ALA GLY GLN HIS THR SER SER ILE THR THR THR SEQRES 22 A 448 TRP SER MET LEU HIS LEU MET HIS PRO ALA ASN VAL LYS SEQRES 23 A 448 HIS LEU GLU ALA LEU ARG LYS GLU ILE GLU GLU PHE PRO SEQRES 24 A 448 ALA GLN LEU ASN TYR ASN ASN VAL MET ASP GLU MET PRO SEQRES 25 A 448 PHE ALA GLU ARG CYS ALA ARG GLU SER ILE ARG ARG ASP SEQRES 26 A 448 PRO PRO LEU LEU MET LEU MET ARG LYS VAL MET ALA ASP SEQRES 27 A 448 VAL LYS VAL GLY SER TYR VAL VAL PRO LYS GLY ASP ILE SEQRES 28 A 448 ILE ALA CYS SER PRO LEU LEU SER HIS HIS ASP GLU GLU SEQRES 29 A 448 ALA PHE PRO GLU PRO ARG ARG TRP ASP PRO GLU ARG ASP SEQRES 30 A 448 GLU LYS VAL GLU GLY ALA PHE ILE GLY PHE GLY ALA GLY SEQRES 31 A 448 VAL HIS LYS CYS ILE GLY GLN LYS PHE GLY LEU LEU GLN SEQRES 32 A 448 VAL LYS THR ILE LEU ALA THR ALA PHE ARG SER TYR ASP SEQRES 33 A 448 PHE GLN LEU LEU ARG ASP GLU VAL PRO ASP PRO ASP TYR SEQRES 34 A 448 HIS THR MET VAL VAL GLY PRO THR ALA SER GLN CYS ARG SEQRES 35 A 448 VAL LYS TYR ILE ARG ARG SEQRES 1 B 448 GLY LYS LEU PRO PRO VAL TYR PRO VAL THR VAL PRO ILE SEQRES 2 B 448 LEU GLY HIS ILE ILE GLN PHE GLY LYS SER PRO LEU GLY SEQRES 3 B 448 PHE MET GLN GLU CYS LYS ARG GLN LEU LYS SER GLY ILE SEQRES 4 B 448 PHE THR ILE ASN ILE VAL GLY LYS ARG VAL THR ILE VAL SEQRES 5 B 448 GLY ASP PRO HIS GLU HIS SER ARG PHE PHE LEU PRO ARG SEQRES 6 B 448 ASN GLU VAL LEU SER PRO ARG GLU VAL TYR SER PHE MET SEQRES 7 B 448 VAL PRO VAL PHE GLY GLU GLY VAL ALA TYR ALA ALA PRO SEQRES 8 B 448 TYR PRO ARG MET ARG GLU GLN LEU ASN PHE LEU ALA GLU SEQRES 9 B 448 GLU LEU THR ILE ALA LYS PHE GLN ASN PHE VAL PRO ALA SEQRES 10 B 448 ILE GLN HIS GLU VAL ARG LYS PHE MET ALA ALA ASN TRP SEQRES 11 B 448 ASP LYS ASP GLU GLY GLU ILE ASN LEU LEU GLU ASP CYS SEQRES 12 B 448 SER THR MET ILE ILE ASN THR ALA CYS GLN CYS LEU PHE SEQRES 13 B 448 GLY GLU ASP LEU ARG LYS ARG LEU ASP ALA ARG ARG PHE SEQRES 14 B 448 ALA GLN LEU LEU ALA LYS MET GLU SER SER LEU ILE PRO SEQRES 15 B 448 ALA ALA VAL PHE LEU PRO ILE LEU LEU LYS LEU PRO LEU SEQRES 16 B 448 PRO GLN SER ALA ARG CYS HIS GLU ALA ARG THR GLU LEU SEQRES 17 B 448 GLN LYS ILE LEU SER GLU ILE ILE ILE ALA ARG LYS GLU SEQRES 18 B 448 GLU GLU VAL ASN LYS ASP SER SER THR SER ASP LEU LEU SEQRES 19 B 448 SER GLY LEU LEU SER ALA VAL TYR ARG ASP GLY THR PRO SEQRES 20 B 448 MET SER LEU HIS GLU VAL CYS GLY MET ILE VAL ALA ALA SEQRES 21 B 448 MET PHE ALA GLY GLN HIS THR SER SER ILE THR THR THR SEQRES 22 B 448 TRP SER MET LEU HIS LEU MET HIS PRO ALA ASN VAL LYS SEQRES 23 B 448 HIS LEU GLU ALA LEU ARG LYS GLU ILE GLU GLU PHE PRO SEQRES 24 B 448 ALA GLN LEU ASN TYR ASN ASN VAL MET ASP GLU MET PRO SEQRES 25 B 448 PHE ALA GLU ARG CYS ALA ARG GLU SER ILE ARG ARG ASP SEQRES 26 B 448 PRO PRO LEU LEU MET LEU MET ARG LYS VAL MET ALA ASP SEQRES 27 B 448 VAL LYS VAL GLY SER TYR VAL VAL PRO LYS GLY ASP ILE SEQRES 28 B 448 ILE ALA CYS SER PRO LEU LEU SER HIS HIS ASP GLU GLU SEQRES 29 B 448 ALA PHE PRO GLU PRO ARG ARG TRP ASP PRO GLU ARG ASP SEQRES 30 B 448 GLU LYS VAL GLU GLY ALA PHE ILE GLY PHE GLY ALA GLY SEQRES 31 B 448 VAL HIS LYS CYS ILE GLY GLN LYS PHE GLY LEU LEU GLN SEQRES 32 B 448 VAL LYS THR ILE LEU ALA THR ALA PHE ARG SER TYR ASP SEQRES 33 B 448 PHE GLN LEU LEU ARG ASP GLU VAL PRO ASP PRO ASP TYR SEQRES 34 B 448 HIS THR MET VAL VAL GLY PRO THR ALA SER GLN CYS ARG SEQRES 35 B 448 VAL LYS TYR ILE ARG ARG SEQRES 1 C 448 GLY LYS LEU PRO PRO VAL TYR PRO VAL THR VAL PRO ILE SEQRES 2 C 448 LEU GLY HIS ILE ILE GLN PHE GLY LYS SER PRO LEU GLY SEQRES 3 C 448 PHE MET GLN GLU CYS LYS ARG GLN LEU LYS SER GLY ILE SEQRES 4 C 448 PHE THR ILE ASN ILE VAL GLY LYS ARG VAL THR ILE VAL SEQRES 5 C 448 GLY ASP PRO HIS GLU HIS SER ARG PHE PHE LEU PRO ARG SEQRES 6 C 448 ASN GLU VAL LEU SER PRO ARG GLU VAL TYR SER PHE MET SEQRES 7 C 448 VAL PRO VAL PHE GLY GLU GLY VAL ALA TYR ALA ALA PRO SEQRES 8 C 448 TYR PRO ARG MET ARG GLU GLN LEU ASN PHE LEU ALA GLU SEQRES 9 C 448 GLU LEU THR ILE ALA LYS PHE GLN ASN PHE VAL PRO ALA SEQRES 10 C 448 ILE GLN HIS GLU VAL ARG LYS PHE MET ALA ALA ASN TRP SEQRES 11 C 448 ASP LYS ASP GLU GLY GLU ILE ASN LEU LEU GLU ASP CYS SEQRES 12 C 448 SER THR MET ILE ILE ASN THR ALA CYS GLN CYS LEU PHE SEQRES 13 C 448 GLY GLU ASP LEU ARG LYS ARG LEU ASP ALA ARG ARG PHE SEQRES 14 C 448 ALA GLN LEU LEU ALA LYS MET GLU SER SER LEU ILE PRO SEQRES 15 C 448 ALA ALA VAL PHE LEU PRO ILE LEU LEU LYS LEU PRO LEU SEQRES 16 C 448 PRO GLN SER ALA ARG CYS HIS GLU ALA ARG THR GLU LEU SEQRES 17 C 448 GLN LYS ILE LEU SER GLU ILE ILE ILE ALA ARG LYS GLU SEQRES 18 C 448 GLU GLU VAL ASN LYS ASP SER SER THR SER ASP LEU LEU SEQRES 19 C 448 SER GLY LEU LEU SER ALA VAL TYR ARG ASP GLY THR PRO SEQRES 20 C 448 MET SER LEU HIS GLU VAL CYS GLY MET ILE VAL ALA ALA SEQRES 21 C 448 MET PHE ALA GLY GLN HIS THR SER SER ILE THR THR THR SEQRES 22 C 448 TRP SER MET LEU HIS LEU MET HIS PRO ALA ASN VAL LYS SEQRES 23 C 448 HIS LEU GLU ALA LEU ARG LYS GLU ILE GLU GLU PHE PRO SEQRES 24 C 448 ALA GLN LEU ASN TYR ASN ASN VAL MET ASP GLU MET PRO SEQRES 25 C 448 PHE ALA GLU ARG CYS ALA ARG GLU SER ILE ARG ARG ASP SEQRES 26 C 448 PRO PRO LEU LEU MET LEU MET ARG LYS VAL MET ALA ASP SEQRES 27 C 448 VAL LYS VAL GLY SER TYR VAL VAL PRO LYS GLY ASP ILE SEQRES 28 C 448 ILE ALA CYS SER PRO LEU LEU SER HIS HIS ASP GLU GLU SEQRES 29 C 448 ALA PHE PRO GLU PRO ARG ARG TRP ASP PRO GLU ARG ASP SEQRES 30 C 448 GLU LYS VAL GLU GLY ALA PHE ILE GLY PHE GLY ALA GLY SEQRES 31 C 448 VAL HIS LYS CYS ILE GLY GLN LYS PHE GLY LEU LEU GLN SEQRES 32 C 448 VAL LYS THR ILE LEU ALA THR ALA PHE ARG SER TYR ASP SEQRES 33 C 448 PHE GLN LEU LEU ARG ASP GLU VAL PRO ASP PRO ASP TYR SEQRES 34 C 448 HIS THR MET VAL VAL GLY PRO THR ALA SER GLN CYS ARG SEQRES 35 C 448 VAL LYS TYR ILE ARG ARG SEQRES 1 D 448 GLY LYS LEU PRO PRO VAL TYR PRO VAL THR VAL PRO ILE SEQRES 2 D 448 LEU GLY HIS ILE ILE GLN PHE GLY LYS SER PRO LEU GLY SEQRES 3 D 448 PHE MET GLN GLU CYS LYS ARG GLN LEU LYS SER GLY ILE SEQRES 4 D 448 PHE THR ILE ASN ILE VAL GLY LYS ARG VAL THR ILE VAL SEQRES 5 D 448 GLY ASP PRO HIS GLU HIS SER ARG PHE PHE LEU PRO ARG SEQRES 6 D 448 ASN GLU VAL LEU SER PRO ARG GLU VAL TYR SER PHE MET SEQRES 7 D 448 VAL PRO VAL PHE GLY GLU GLY VAL ALA TYR ALA ALA PRO SEQRES 8 D 448 TYR PRO ARG MET ARG GLU GLN LEU ASN PHE LEU ALA GLU SEQRES 9 D 448 GLU LEU THR ILE ALA LYS PHE GLN ASN PHE VAL PRO ALA SEQRES 10 D 448 ILE GLN HIS GLU VAL ARG LYS PHE MET ALA ALA ASN TRP SEQRES 11 D 448 ASP LYS ASP GLU GLY GLU ILE ASN LEU LEU GLU ASP CYS SEQRES 12 D 448 SER THR MET ILE ILE ASN THR ALA CYS GLN CYS LEU PHE SEQRES 13 D 448 GLY GLU ASP LEU ARG LYS ARG LEU ASP ALA ARG ARG PHE SEQRES 14 D 448 ALA GLN LEU LEU ALA LYS MET GLU SER SER LEU ILE PRO SEQRES 15 D 448 ALA ALA VAL PHE LEU PRO ILE LEU LEU LYS LEU PRO LEU SEQRES 16 D 448 PRO GLN SER ALA ARG CYS HIS GLU ALA ARG THR GLU LEU SEQRES 17 D 448 GLN LYS ILE LEU SER GLU ILE ILE ILE ALA ARG LYS GLU SEQRES 18 D 448 GLU GLU VAL ASN LYS ASP SER SER THR SER ASP LEU LEU SEQRES 19 D 448 SER GLY LEU LEU SER ALA VAL TYR ARG ASP GLY THR PRO SEQRES 20 D 448 MET SER LEU HIS GLU VAL CYS GLY MET ILE VAL ALA ALA SEQRES 21 D 448 MET PHE ALA GLY GLN HIS THR SER SER ILE THR THR THR SEQRES 22 D 448 TRP SER MET LEU HIS LEU MET HIS PRO ALA ASN VAL LYS SEQRES 23 D 448 HIS LEU GLU ALA LEU ARG LYS GLU ILE GLU GLU PHE PRO SEQRES 24 D 448 ALA GLN LEU ASN TYR ASN ASN VAL MET ASP GLU MET PRO SEQRES 25 D 448 PHE ALA GLU ARG CYS ALA ARG GLU SER ILE ARG ARG ASP SEQRES 26 D 448 PRO PRO LEU LEU MET LEU MET ARG LYS VAL MET ALA ASP SEQRES 27 D 448 VAL LYS VAL GLY SER TYR VAL VAL PRO LYS GLY ASP ILE SEQRES 28 D 448 ILE ALA CYS SER PRO LEU LEU SER HIS HIS ASP GLU GLU SEQRES 29 D 448 ALA PHE PRO GLU PRO ARG ARG TRP ASP PRO GLU ARG ASP SEQRES 30 D 448 GLU LYS VAL GLU GLY ALA PHE ILE GLY PHE GLY ALA GLY SEQRES 31 D 448 VAL HIS LYS CYS ILE GLY GLN LYS PHE GLY LEU LEU GLN SEQRES 32 D 448 VAL LYS THR ILE LEU ALA THR ALA PHE ARG SER TYR ASP SEQRES 33 D 448 PHE GLN LEU LEU ARG ASP GLU VAL PRO ASP PRO ASP TYR SEQRES 34 D 448 HIS THR MET VAL VAL GLY PRO THR ALA SER GLN CYS ARG SEQRES 35 D 448 VAL LYS TYR ILE ARG ARG HET HEM A 501 43 HET VFV A 502 41 HET HEM B 501 43 HET VFV B 502 41 HET HEM C 501 43 HET VFV C 502 41 HET HEM D 501 43 HET VFV D 502 41 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETNAM VFV N-[(1R)-1-(3,4'-DIFLUOROBIPHENYL-4-YL)-2-(1H-IMIDAZOL- HETNAM 2 VFV 1-YL)ETHYL]-4-(5-PHENYL-1,3,4-OXADIAZOL-2-YL)BENZAMIDE HETSYN HEM HEME FORMUL 5 HEM 4(C34 H32 FE N4 O4) FORMUL 6 VFV 4(C32 H23 F2 N5 O2) FORMUL 13 HOH *504(H2 O) HELIX 1 1 HIS A 44 SER A 51 1 8 HELIX 2 2 SER A 51 LEU A 63 1 13 HELIX 3 3 ASP A 82 GLU A 85 5 4 HELIX 4 4 HIS A 86 LEU A 91 1 6 HELIX 5 5 GLU A 101 PHE A 105 5 5 HELIX 6 6 MET A 106 GLY A 111 1 6 HELIX 7 7 VAL A 114 ALA A 118 5 5 HELIX 8 8 PRO A 119 GLU A 133 1 15 HELIX 9 9 LEU A 134 ALA A 137 5 4 HELIX 10 10 LYS A 138 TRP A 158 1 21 HELIX 11 11 LEU A 167 PHE A 184 1 18 HELIX 12 12 GLY A 185 LEU A 192 1 8 HELIX 13 13 ASP A 193 SER A 207 1 15 HELIX 14 14 LEU A 208 PHE A 214 5 7 HELIX 15 15 LEU A 215 LEU A 221 5 7 HELIX 16 16 LEU A 223 LYS A 254 1 32 HELIX 17 17 ASP A 260 SER A 267 1 8 HELIX 18 18 SER A 277 HIS A 309 1 33 HELIX 19 19 ASN A 312 GLU A 324 1 13 HELIX 20 20 ASN A 331 GLU A 338 1 8 HELIX 21 21 MET A 339 ASP A 353 1 15 HELIX 22 22 SER A 383 HIS A 388 1 6 HELIX 23 23 ALA A 417 LYS A 421 5 5 HELIX 24 24 GLY A 424 SER A 442 1 19 HELIX 25 25 ALA A 466 GLN A 468 5 3 HELIX 26 26 HIS B 44 SER B 51 1 8 HELIX 27 27 SER B 51 LYS B 64 1 14 HELIX 28 28 ASP B 82 GLU B 85 5 4 HELIX 29 29 HIS B 86 LEU B 91 1 6 HELIX 30 30 ARG B 100 PHE B 105 5 6 HELIX 31 31 MET B 106 GLY B 111 1 6 HELIX 32 32 VAL B 114 ALA B 118 5 5 HELIX 33 33 PRO B 119 LEU B 134 1 16 HELIX 34 34 THR B 135 ALA B 137 5 3 HELIX 35 35 LYS B 138 TRP B 158 1 21 HELIX 36 36 LEU B 167 PHE B 184 1 18 HELIX 37 37 GLY B 185 LEU B 192 1 8 HELIX 38 38 ASP B 193 LEU B 208 1 16 HELIX 39 39 ILE B 209 PHE B 214 5 6 HELIX 40 40 LEU B 215 LYS B 220 5 6 HELIX 41 41 LEU B 223 GLU B 251 1 29 HELIX 42 42 ASP B 260 SER B 267 1 8 HELIX 43 43 SER B 277 HIS B 309 1 33 HELIX 44 44 ASN B 312 GLU B 324 1 13 HELIX 45 45 ASN B 331 GLU B 338 1 8 HELIX 46 46 MET B 339 ASP B 353 1 15 HELIX 47 47 SER B 383 HIS B 388 1 6 HELIX 48 48 ALA B 417 LYS B 421 5 5 HELIX 49 49 GLY B 424 SER B 442 1 19 HELIX 50 50 ALA B 466 GLN B 468 5 3 HELIX 51 51 HIS C 44 SER C 51 1 8 HELIX 52 52 SER C 51 LEU C 63 1 13 HELIX 53 53 ASP C 82 GLU C 85 5 4 HELIX 54 54 HIS C 86 LEU C 91 1 6 HELIX 55 55 PRO C 99 PHE C 105 5 7 HELIX 56 56 MET C 106 GLY C 111 1 6 HELIX 57 57 VAL C 114 ALA C 118 5 5 HELIX 58 58 PRO C 119 LEU C 134 1 16 HELIX 59 59 LYS C 138 TRP C 158 1 21 HELIX 60 60 LEU C 167 PHE C 184 1 18 HELIX 61 61 GLY C 185 LEU C 192 1 8 HELIX 62 62 ASP C 193 SER C 207 1 15 HELIX 63 63 LEU C 208 PHE C 214 5 7 HELIX 64 64 LEU C 215 LEU C 221 5 7 HELIX 65 65 LEU C 223 LYS C 254 1 32 HELIX 66 66 ASP C 260 SER C 267 1 8 HELIX 67 67 SER C 277 HIS C 309 1 33 HELIX 68 68 ASN C 312 GLU C 324 1 13 HELIX 69 69 ASN C 331 GLU C 338 1 8 HELIX 70 70 MET C 339 ASP C 353 1 15 HELIX 71 71 SER C 383 HIS C 388 1 6 HELIX 72 72 ALA C 417 LYS C 421 5 5 HELIX 73 73 GLY C 424 SER C 442 1 19 HELIX 74 74 ALA C 466 GLN C 468 5 3 HELIX 75 75 HIS D 44 SER D 51 1 8 HELIX 76 76 SER D 51 LYS D 64 1 14 HELIX 77 77 ASP D 82 HIS D 84 5 3 HELIX 78 78 GLU D 85 LEU D 91 1 7 HELIX 79 79 ARG D 100 PHE D 105 5 6 HELIX 80 80 MET D 106 GLY D 111 1 6 HELIX 81 81 VAL D 114 ALA D 118 5 5 HELIX 82 82 PRO D 119 LEU D 134 1 16 HELIX 83 83 THR D 135 ALA D 137 5 3 HELIX 84 84 LYS D 138 TRP D 158 1 21 HELIX 85 85 LEU D 167 PHE D 184 1 18 HELIX 86 86 GLY D 185 LEU D 192 1 8 HELIX 87 87 ASP D 193 SER D 207 1 15 HELIX 88 88 LEU D 208 PHE D 214 5 7 HELIX 89 89 LEU D 215 LEU D 221 5 7 HELIX 90 90 LEU D 223 LYS D 254 1 32 HELIX 91 91 ASP D 260 SER D 267 1 8 HELIX 92 92 SER D 277 MET D 308 1 32 HELIX 93 93 HIS D 309 ALA D 311 5 3 HELIX 94 94 ASN D 312 ILE D 323 1 12 HELIX 95 95 ASN D 331 GLU D 338 1 8 HELIX 96 96 MET D 339 ASP D 353 1 15 HELIX 97 97 SER D 383 HIS D 388 1 6 HELIX 98 98 ALA D 417 LYS D 421 5 5 HELIX 99 99 GLY D 424 TYR D 443 1 20 HELIX 100 100 ALA D 466 GLN D 468 5 3 SHEET 1 A 5 ILE A 67 ILE A 72 0 SHEET 2 A 5 LYS A 75 VAL A 80 -1 O ILE A 79 N PHE A 68 SHEET 3 A 5 ILE A 379 CYS A 382 1 O ALA A 381 N VAL A 80 SHEET 4 A 5 LEU A 359 VAL A 363 -1 N ARG A 361 O ILE A 380 SHEET 5 A 5 LEU A 97 SER A 98 -1 N SER A 98 O LYS A 362 SHEET 1 B 3 GLU A 162 ASN A 166 0 SHEET 2 B 3 ARG A 470 ARG A 475 -1 O VAL A 471 N ILE A 165 SHEET 3 B 3 TYR A 443 LEU A 447 -1 N ASP A 444 O ILE A 474 SHEET 1 C 2 VAL A 367 VAL A 369 0 SHEET 2 C 2 TYR A 372 VAL A 374 -1 O VAL A 374 N VAL A 367 SHEET 1 D 2 PRO A 455 ASP A 456 0 SHEET 2 D 2 GLY A 463 PRO A 464 -1 O GLY A 463 N ASP A 456 SHEET 1 E 5 ILE B 67 ILE B 72 0 SHEET 2 E 5 LYS B 75 VAL B 80 -1 O ILE B 79 N PHE B 68 SHEET 3 E 5 ILE B 379 CYS B 382 1 O ALA B 381 N VAL B 80 SHEET 4 E 5 LEU B 359 VAL B 363 -1 N LEU B 359 O CYS B 382 SHEET 5 E 5 LEU B 97 SER B 98 -1 N SER B 98 O LYS B 362 SHEET 1 F 3 GLU B 162 ASN B 166 0 SHEET 2 F 3 ARG B 470 ARG B 475 -1 O VAL B 471 N ILE B 165 SHEET 3 F 3 TYR B 443 LEU B 447 -1 N ASP B 444 O ILE B 474 SHEET 1 G 2 VAL B 367 VAL B 369 0 SHEET 2 G 2 TYR B 372 VAL B 374 -1 O VAL B 374 N VAL B 367 SHEET 1 H 2 PRO B 455 ASP B 456 0 SHEET 2 H 2 GLY B 463 PRO B 464 -1 O GLY B 463 N ASP B 456 SHEET 1 I 5 ILE C 67 ILE C 72 0 SHEET 2 I 5 LYS C 75 VAL C 80 -1 O VAL C 77 N ILE C 70 SHEET 3 I 5 ILE C 379 CYS C 382 1 O ALA C 381 N VAL C 80 SHEET 4 I 5 LEU C 359 VAL C 363 -1 N ARG C 361 O ILE C 380 SHEET 5 I 5 LEU C 97 SER C 98 -1 N SER C 98 O LYS C 362 SHEET 1 J 3 GLU C 162 ASN C 166 0 SHEET 2 J 3 ARG C 470 ARG C 475 -1 O TYR C 473 N GLY C 163 SHEET 3 J 3 TYR C 443 LEU C 447 -1 N ASP C 444 O ILE C 474 SHEET 1 K 2 VAL C 367 VAL C 369 0 SHEET 2 K 2 TYR C 372 VAL C 374 -1 O VAL C 374 N VAL C 367 SHEET 1 L 2 PRO C 455 ASP C 456 0 SHEET 2 L 2 GLY C 463 PRO C 464 -1 O GLY C 463 N ASP C 456 SHEET 1 M 5 ILE D 67 ILE D 72 0 SHEET 2 M 5 LYS D 75 VAL D 80 -1 O ILE D 79 N PHE D 68 SHEET 3 M 5 ILE D 379 CYS D 382 1 O ALA D 381 N VAL D 80 SHEET 4 M 5 LEU D 359 VAL D 363 -1 N LEU D 359 O CYS D 382 SHEET 5 M 5 LEU D 97 SER D 98 -1 N SER D 98 O LYS D 362 SHEET 1 N 3 GLU D 162 ASN D 166 0 SHEET 2 N 3 ARG D 470 ILE D 474 -1 O VAL D 471 N ILE D 165 SHEET 3 N 3 ASP D 444 LEU D 447 -1 N GLN D 446 O LYS D 472 SHEET 1 O 2 VAL D 367 VAL D 369 0 SHEET 2 O 2 TYR D 372 VAL D 374 -1 O VAL D 374 N VAL D 367 SHEET 1 P 2 PRO D 455 ASP D 456 0 SHEET 2 P 2 GLY D 463 PRO D 464 -1 O GLY D 463 N ASP D 456 LINK FE HEM D 501 NAX VFV D 502 1555 1555 1.94 LINK FE HEM A 501 NAX VFV A 502 1555 1555 1.99 LINK FE HEM C 501 NAX VFV C 502 1555 1555 2.01 LINK FE HEM B 501 NAX VFV B 502 1555 1555 2.07 LINK SG CYS B 422 FE HEM B 501 1555 1555 2.22 LINK SG CYS C 422 FE HEM C 501 1555 1555 2.32 LINK SG CYS A 422 FE HEM A 501 1555 1555 2.42 LINK SG CYS D 422 FE HEM D 501 1555 1555 2.42 SITE 1 AC1 21 TYR A 116 ARG A 124 LEU A 127 ALA A 291 SITE 2 AC1 21 GLY A 292 THR A 295 SER A 296 ARG A 361 SITE 3 AC1 21 GLY A 414 PHE A 415 GLY A 416 VAL A 419 SITE 4 AC1 21 HIS A 420 LYS A 421 CYS A 422 ILE A 423 SITE 5 AC1 21 GLY A 424 VFV A 502 HOH A 602 HOH A 623 SITE 6 AC1 21 HOH A 635 SITE 1 AC2 13 PHE A 48 TYR A 103 ALA A 115 TYR A 116 SITE 2 AC2 13 LEU A 127 MET A 284 ALA A 287 PHE A 290 SITE 3 AC2 13 ALA A 291 LEU A 356 MET A 360 HEM A 501 SITE 4 AC2 13 HOH A 750 SITE 1 AC3 19 TYR B 116 LEU B 127 GLY B 292 THR B 295 SITE 2 AC3 19 SER B 296 LEU B 356 ARG B 361 GLY B 414 SITE 3 AC3 19 PHE B 415 GLY B 416 VAL B 419 HIS B 420 SITE 4 AC3 19 LYS B 421 CYS B 422 GLY B 424 VFV B 502 SITE 5 AC3 19 HOH B 624 HOH B 636 HOH B 652 SITE 1 AC4 15 PHE B 48 TYR B 103 ALA B 115 TYR B 116 SITE 2 AC4 15 LEU B 127 MET B 284 ALA B 287 PHE B 290 SITE 3 AC4 15 ALA B 291 THR B 295 LEU B 356 MET B 360 SITE 4 AC4 15 MET B 460 HEM B 501 HOH B 622 SITE 1 AC5 22 TYR C 116 ARG C 124 LEU C 127 ALA C 291 SITE 2 AC5 22 GLY C 292 THR C 295 SER C 296 LEU C 356 SITE 3 AC5 22 LEU C 359 ARG C 361 GLY C 414 PHE C 415 SITE 4 AC5 22 GLY C 416 VAL C 419 HIS C 420 LYS C 421 SITE 5 AC5 22 CYS C 422 ILE C 423 GLY C 424 VFV C 502 SITE 6 AC5 22 HOH C 610 HOH C 661 SITE 1 AC6 15 TYR C 103 PHE C 105 TYR C 116 LEU C 127 SITE 2 AC6 15 PRO C 210 VAL C 213 PHE C 214 MET C 284 SITE 3 AC6 15 ALA C 287 ALA C 291 LEU C 356 MET C 360 SITE 4 AC6 15 MET C 460 HEM C 501 HOH C 606 SITE 1 AC7 23 TYR D 116 ARG D 124 LEU D 127 ALA D 288 SITE 2 AC7 23 ALA D 291 GLY D 292 THR D 295 SER D 296 SITE 3 AC7 23 LEU D 356 ARG D 361 GLY D 414 PHE D 415 SITE 4 AC7 23 GLY D 416 VAL D 419 HIS D 420 LYS D 421 SITE 5 AC7 23 CYS D 422 ILE D 423 GLY D 424 VFV D 502 SITE 6 AC7 23 HOH D 601 HOH D 613 HOH D 658 SITE 1 AC8 14 PHE D 48 TYR D 103 ALA D 115 TYR D 116 SITE 2 AC8 14 LEU D 127 PHE D 214 MET D 284 ALA D 287 SITE 3 AC8 14 ALA D 291 LEU D 356 MET D 360 HEM D 501 SITE 4 AC8 14 HOH D 645 HOH D 664 CRYST1 59.947 79.706 117.868 74.64 81.20 68.96 P 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 0.016681 -0.006416 -0.001150 0.00000 SCALE2 0.000000 0.013442 -0.003144 0.00000 SCALE3 0.000000 0.000000 0.008817 0.00000 ATOM 1 N GLY A 29 -21.323 -25.273 12.521 1.00 76.81 N ANISOU 1 N GLY A 29 9510 10609 9065 -64 -159 418 N ATOM 2 CA GLY A 29 -20.251 -24.254 12.312 1.00 78.33 C ANISOU 2 CA GLY A 29 9749 9758 10253 199 9 -149 C ATOM 3 C GLY A 29 -18.902 -24.709 12.837 1.00 70.49 C ANISOU 3 C GLY A 29 10038 8982 7763 -539 -661 -572 C ATOM 4 O GLY A 29 -18.421 -25.788 12.485 1.00 89.68 O ANISOU 4 O GLY A 29 14230 8908 10934 2404 1134 3062 O ATOM 5 N LYS A 30 -18.288 -23.872 13.672 1.00 57.03 N ANISOU 5 N LYS A 30 8036 8517 5114 -27 281 571 N ATOM 6 CA LYS A 30 -17.016 -24.187 14.316 1.00 56.41 C ANISOU 6 CA LYS A 30 7798 6923 6711 -93 42 735 C ATOM 7 C LYS A 30 -17.226 -24.328 15.835 1.00 62.30 C ANISOU 7 C LYS A 30 9699 6872 7099 -624 996 566 C ATOM 8 O LYS A 30 -17.247 -23.337 16.583 1.00 53.93 O ANISOU 8 O LYS A 30 8749 5108 6634 682 1680 2173 O ATOM 9 CB LYS A 30 -15.983 -23.107 13.973 1.00 59.20 C ANISOU 9 CB LYS A 30 7894 7640 6956 -604 1077 399 C ATOM 10 CG LYS A 30 -14.653 -23.159 14.721 1.00 63.56 C ANISOU 10 CG LYS A 30 8480 8902 6765 38 692 -156 C ATOM 11 CD LYS A 30 -13.819 -21.928 14.373 1.00 67.22 C ANISOU 11 CD LYS A 30 8302 8288 8947 -388 -901 -1047 C ATOM 12 CE LYS A 30 -12.728 -21.646 15.395 1.00 54.10 C ANISOU 12 CE LYS A 30 7034 6519 7004 -271 772 -575 C ATOM 13 NZ LYS A 30 -11.476 -22.400 15.118 1.00 64.85 N ANISOU 13 NZ LYS A 30 8124 7466 9047 734 3347 1414 N ATOM 14 N LEU A 31 -17.392 -25.571 16.281 1.00 48.57 N ANISOU 14 N LEU A 31 7181 5831 5440 626 1669 -711 N ATOM 15 CA LEU A 31 -17.725 -25.862 17.675 1.00 40.73 C ANISOU 15 CA LEU A 31 5474 4651 5350 -52 -87 506 C ATOM 16 C LEU A 31 -16.515 -25.777 18.577 1.00 37.04 C ANISOU 16 C LEU A 31 5141 4043 4886 306 501 209 C ATOM 17 O LEU A 31 -15.383 -25.941 18.106 1.00 35.51 O ANISOU 17 O LEU A 31 4977 4631 3883 374 816 220 O ATOM 18 CB LEU A 31 -18.317 -27.260 17.779 1.00 42.72 C ANISOU 18 CB LEU A 31 5997 5365 4867 -1114 74 446 C ATOM 19 CG LEU A 31 -19.570 -27.467 16.942 1.00 46.35 C ANISOU 19 CG LEU A 31 4923 6166 6520 -66 52 70 C ATOM 20 CD1 LEU A 31 -19.909 -28.947 16.888 1.00 49.07 C ANISOU 20 CD1 LEU A 31 6656 6057 5930 -114 -882 338 C ATOM 21 CD2 LEU A 31 -20.715 -26.661 17.523 1.00 46.61 C ANISOU 21 CD2 LEU A 31 6740 5259 5709 246 -162 -1317 C ATOM 22 N PRO A 32 -16.734 -25.525 19.885 1.00 35.82 N ANISOU 22 N PRO A 32 4863 4032 4713 217 233 337 N ATOM 23 CA PRO A 32 -15.572 -25.570 20.770 1.00 33.77 C ANISOU 23 CA PRO A 32 5395 3771 3665 -407 96 -216 C ATOM 24 C PRO A 32 -14.904 -26.947 20.692 1.00 31.10 C ANISOU 24 C PRO A 32 4149 4577 3090 -52 363 -12 C ATOM 25 O PRO A 32 -15.548 -27.915 20.300 1.00 35.71 O ANISOU 25 O PRO A 32 5190 4131 4247 -317 865 -231 O ATOM 26 CB PRO A 32 -16.184 -25.340 22.163 1.00 34.56 C ANISOU 26 CB PRO A 32 4890 4415 3823 -24 410 -15 C ATOM 27 CG PRO A 32 -17.451 -24.612 21.906 1.00 37.11 C ANISOU 27 CG PRO A 32 4666 5433 4000 165 430 -487 C ATOM 28 CD PRO A 32 -17.967 -25.149 20.602 1.00 37.41 C ANISOU 28 CD PRO A 32 4695 5129 4389 -743 446 -547 C ATOM 29 N PRO A 33 -13.616 -27.044 21.044 1.00 33.16 N ANISOU 29 N PRO A 33 4291 4156 4152 -798 41 958 N ATOM 30 CA PRO A 33 -13.039 -28.379 21.098 1.00 35.75 C ANISOU 30 CA PRO A 33 4788 4290 4504 -211 422 -382 C ATOM 31 C PRO A 33 -13.664 -29.190 22.258 1.00 45.98 C ANISOU 31 C PRO A 33 7424 5251 4793 -185 1801 -210 C ATOM 32 O PRO A 33 -13.977 -28.635 23.321 1.00 37.98 O ANISOU 32 O PRO A 33 5443 4458 4527 38 809 -132 O ATOM 33 CB PRO A 33 -11.565 -28.113 21.350 1.00 37.16 C ANISOU 33 CB PRO A 33 4639 4278 5201 -323 1354 -331 C ATOM 34 CG PRO A 33 -11.524 -26.779 22.030 1.00 36.73 C ANISOU 34 CG PRO A 33 5102 4230 4622 780 773 -150 C ATOM 35 CD PRO A 33 -12.692 -26.002 21.515 1.00 32.53 C ANISOU 35 CD PRO A 33 4665 4066 3625 -195 14 -222 C ATOM 36 N VAL A 34 -13.839 -30.490 22.028 1.00 49.06 N ANISOU 36 N VAL A 34 7738 5861 5041 -579 1801 -745 N ATOM 37 CA VAL A 34 -14.496 -31.411 22.960 1.00 42.75 C ANISOU 37 CA VAL A 34 5990 5266 4987 139 422 -101 C ATOM 38 C VAL A 34 -13.452 -32.268 23.653 1.00 39.09 C ANISOU 38 C VAL A 34 5951 4106 4795 86 1070 134 C ATOM 39 O VAL A 34 -12.593 -32.868 23.005 1.00 37.53 O ANISOU 39 O VAL A 34 5637 3943 4679 -404 1256 227 O ATOM 40 CB VAL A 34 -15.478 -32.331 22.210 1.00 43.20 C ANISOU 40 CB VAL A 34 5641 5922 4848 158 427 -48 C ATOM 41 CG1 VAL A 34 -16.268 -33.215 23.175 1.00 48.46 C ANISOU 41 CG1 VAL A 34 7400 5038 5973 48 1221 190 C ATOM 42 CG2 VAL A 34 -16.404 -31.503 21.334 1.00 38.92 C ANISOU 42 CG2 VAL A 34 4416 4948 5423 643 1035 -718 C ATOM 43 N TYR A 35 -13.502 -32.324 24.975 1.00 33.35 N ANISOU 43 N TYR A 35 4504 3689 4477 -202 712 89 N ATOM 44 CA TYR A 35 -12.571 -33.167 25.683 1.00 35.21 C ANISOU 44 CA TYR A 35 4388 4315 4674 393 569 -328 C ATOM 45 C TYR A 35 -12.919 -34.623 25.339 1.00 36.77 C ANISOU 45 C TYR A 35 4685 4357 4927 -87 479 367 C ATOM 46 O TYR A 35 -14.108 -34.976 25.263 1.00 38.20 O ANISOU 46 O TYR A 35 5056 4777 4681 -546 661 432 O ATOM 47 CB TYR A 35 -12.633 -32.899 27.176 1.00 36.38 C ANISOU 47 CB TYR A 35 4723 4553 4544 -338 51 -402 C ATOM 48 CG TYR A 35 -11.420 -33.391 27.915 1.00 37.88 C ANISOU 48 CG TYR A 35 5006 4109 5277 161 70 -418 C ATOM 49 CD1 TYR A 35 -10.194 -32.749 27.781 1.00 38.38 C ANISOU 49 CD1 TYR A 35 5539 4605 4436 -112 865 -324 C ATOM 50 CD2 TYR A 35 -11.493 -34.501 28.750 1.00 44.18 C ANISOU 50 CD2 TYR A 35 6178 5781 4826 -113 152 452 C ATOM 51 CE1 TYR A 35 -9.075 -33.197 28.459 1.00 47.30 C ANISOU 51 CE1 TYR A 35 6412 5611 5948 413 -23 -315 C ATOM 52 CE2 TYR A 35 -10.377 -34.960 29.430 1.00 42.25 C ANISOU 52 CE2 TYR A 35 5593 5183 5275 122 593 53 C ATOM 53 CZ TYR A 35 -9.172 -34.305 29.283 1.00 50.07 C ANISOU 53 CZ TYR A 35 6319 6313 6392 -640 233 160 C ATOM 54 OH TYR A 35 -8.057 -34.751 29.959 1.00 54.50 O ANISOU 54 OH TYR A 35 7712 5713 7283 1221 161 204 O ATOM 55 N PRO A 36 -11.894 -35.456 25.060 1.00 37.51 N ANISOU 55 N PRO A 36 4716 4260 5273 -30 243 368 N ATOM 56 CA PRO A 36 -12.215 -36.826 24.641 1.00 37.04 C ANISOU 56 CA PRO A 36 4287 4833 4951 -602 143 -261 C ATOM 57 C PRO A 36 -12.926 -37.596 25.754 1.00 35.17 C ANISOU 57 C PRO A 36 4943 3646 4773 829 -320 626 C ATOM 58 O PRO A 36 -12.536 -37.497 26.918 1.00 37.51 O ANISOU 58 O PRO A 36 5348 4142 4759 963 270 446 O ATOM 59 CB PRO A 36 -10.845 -37.441 24.330 1.00 41.32 C ANISOU 59 CB PRO A 36 5465 4045 6187 212 679 -590 C ATOM 60 CG PRO A 36 -9.924 -36.278 24.118 1.00 43.58 C ANISOU 60 CG PRO A 36 5757 4858 5943 -287 1548 -700 C ATOM 61 CD PRO A 36 -10.441 -35.196 25.030 1.00 34.79 C ANISOU 61 CD PRO A 36 4737 3629 4849 -7 339 276 C ATOM 62 N VAL A 37 -13.988 -38.310 25.387 1.00 41.78 N ANISOU 62 N VAL A 37 5565 4188 6121 251 438 -351 N ATOM 63 CA VAL A 37 -14.730 -39.172 26.307 1.00 51.81 C ANISOU 63 CA VAL A 37 6449 6507 6727 215 1254 610 C ATOM 64 C VAL A 37 -14.087 -40.551 26.288 1.00 55.04 C ANISOU 64 C VAL A 37 8182 5909 6821 -61 -138 -165 C ATOM 65 O VAL A 37 -14.083 -41.211 25.252 1.00 50.14 O ANISOU 65 O VAL A 37 8192 4106 6750 -312 -1095 380 O ATOM 66 CB VAL A 37 -16.206 -39.330 25.872 1.00 59.56 C ANISOU 66 CB VAL A 37 7197 7213 8217 -900 399 9 C ATOM 67 CG1 VAL A 37 -16.988 -40.135 26.904 1.00 62.86 C ANISOU 67 CG1 VAL A 37 9808 5774 8302 93 865 280 C ATOM 68 CG2 VAL A 37 -16.860 -37.974 25.640 1.00 73.23 C ANISOU 68 CG2 VAL A 37 11147 8049 8626 400 854 1590 C ATOM 69 N THR A 38 -13.528 -40.979 27.416 1.00 54.38 N ANISOU 69 N THR A 38 7525 7073 6062 -215 1060 534 N ATOM 70 CA THR A 38 -12.901 -42.300 27.485 1.00 62.32 C ANISOU 70 CA THR A 38 7519 7787 8371 364 73 666 C ATOM 71 C THR A 38 -13.753 -43.306 28.254 1.00 67.94 C ANISOU 71 C THR A 38 8266 7965 9583 -5 1025 594 C ATOM 72 O THR A 38 -13.574 -44.516 28.105 1.00 70.26 O ANISOU 72 O THR A 38 7932 7897 10866 -1739 334 -1162 O ATOM 73 CB THR A 38 -11.469 -42.250 28.062 1.00 64.39 C ANISOU 73 CB THR A 38 8208 7417 8841 306 -678 -279 C ATOM 74 OG1 THR A 38 -11.474 -41.565 29.322 1.00 62.33 O ANISOU 74 OG1 THR A 38 8528 6913 8240 3494 2283 460 O ATOM 75 CG2 THR A 38 -10.518 -41.543 27.090 1.00 67.31 C ANISOU 75 CG2 THR A 38 9159 7960 8454 1180 -208 329 C ATOM 76 N VAL A 39 -14.668 -42.796 29.074 1.00 60.35 N ANISOU 76 N VAL A 39 8564 6475 7889 314 -239 490 N ATOM 77 CA VAL A 39 -15.663 -43.621 29.733 1.00 62.75 C ANISOU 77 CA VAL A 39 7907 7946 7988 -193 200 -333 C ATOM 78 C VAL A 39 -17.046 -43.231 29.272 1.00 62.14 C ANISOU 78 C VAL A 39 8493 6699 8416 130 360 738 C ATOM 79 O VAL A 39 -17.592 -42.229 29.716 1.00 63.90 O ANISOU 79 O VAL A 39 9080 7148 8049 -501 2139 467 O ATOM 80 CB VAL A 39 -15.634 -43.450 31.246 1.00 62.61 C ANISOU 80 CB VAL A 39 7983 7999 7807 -193 57 684 C ATOM 81 CG1 VAL A 39 -16.513 -44.492 31.895 1.00 62.02 C ANISOU 81 CG1 VAL A 39 6844 7403 9315 -174 -552 1086 C ATOM 82 CG2 VAL A 39 -14.221 -43.559 31.757 1.00 70.66 C ANISOU 82 CG2 VAL A 39 8446 7301 11098 -173 -1389 -4 C ATOM 83 N PRO A 40 -17.607 -44.007 28.354 1.00 70.70 N ANISOU 83 N PRO A 40 8456 9011 9394 -878 -95 -139 N ATOM 84 CA PRO A 40 -18.867 -43.620 27.714 1.00 66.84 C ANISOU 84 CA PRO A 40 9727 7173 8492 -121 491 1190 C ATOM 85 C PRO A 40 -20.064 -43.549 28.659 1.00 79.11 C ANISOU 85 C PRO A 40 11158 9611 9288 411 1626 1637 C ATOM 86 O PRO A 40 -20.273 -44.430 29.492 1.00 65.39 O ANISOU 86 O PRO A 40 9682 5898 9263 -1079 1474 818 O ATOM 87 CB PRO A 40 -19.083 -44.731 26.683 1.00 69.75 C ANISOU 87 CB PRO A 40 8824 9084 8591 -256 -652 917 C ATOM 88 CG PRO A 40 -17.708 -45.198 26.350 1.00 74.25 C ANISOU 88 CG PRO A 40 9341 10321 8549 -716 496 -396 C ATOM 89 CD PRO A 40 -16.919 -45.085 27.623 1.00 70.82 C ANISOU 89 CD PRO A 40 8728 9380 8800 -2222 63 -738 C ATOM 90 N ILE A 41 -20.849 -42.490 28.493 1.00 84.35 N ANISOU 90 N ILE A 41 11037 11200 9811 1495 1043 720 N ATOM 91 CA ILE A 41 -22.190 -42.384 29.053 1.00 74.74 C ANISOU 91 CA ILE A 41 9869 9926 8601 -1098 -313 -931 C ATOM 92 C ILE A 41 -22.205 -42.020 30.530 1.00 62.72 C ANISOU 92 C ILE A 41 7918 7560 8350 -570 1007 -69 C ATOM 93 O ILE A 41 -23.247 -41.760 31.088 1.00 54.72 O ANISOU 93 O ILE A 41 7713 4935 8143 -554 399 -540 O ATOM 94 CB ILE A 41 -23.071 -43.585 28.662 1.00 79.45 C ANISOU 94 CB ILE A 41 11189 8851 10146 -372 703 -1755 C ATOM 95 CG1 ILE A 41 -23.430 -43.462 27.174 1.00 79.13 C ANISOU 95 CG1 ILE A 41 11084 8082 10899 -473 100 -190 C ATOM 96 CG2 ILE A 41 -24.344 -43.636 29.483 1.00 76.08 C ANISOU 96 CG2 ILE A 41 11260 9551 8095 529 280 -412 C ATOM 97 CD1 ILE A 41 -24.477 -44.442 26.658 1.00 94.15 C ANISOU 97 CD1 ILE A 41 10356 12455 12960 334 461 552 C ATOM 98 N LEU A 42 -21.049 -42.050 31.154 1.00 59.57 N ANISOU 98 N LEU A 42 7838 8242 6554 120 1289 318 N ATOM 99 CA LEU A 42 -20.794 -41.233 32.295 1.00 56.49 C ANISOU 99 CA LEU A 42 6887 7307 7269 -433 147 392 C ATOM 100 C LEU A 42 -20.269 -39.925 31.794 1.00 64.88 C ANISOU 100 C LEU A 42 9061 7046 8542 0 920 819 C ATOM 101 O LEU A 42 -20.625 -38.881 32.263 1.00 67.68 O ANISOU 101 O LEU A 42 10278 9276 6162 2889 4023 1119 O ATOM 102 CB LEU A 42 -19.750 -41.860 33.199 1.00 54.04 C ANISOU 102 CB LEU A 42 6669 6552 7309 396 818 -72 C ATOM 103 CG LEU A 42 -20.216 -43.012 34.075 1.00 52.20 C ANISOU 103 CG LEU A 42 6799 6705 6327 629 -39 244 C ATOM 104 CD1 LEU A 42 -19.179 -43.324 35.111 1.00 55.69 C ANISOU 104 CD1 LEU A 42 7178 6360 7619 1024 -739 660 C ATOM 105 CD2 LEU A 42 -21.524 -42.709 34.753 1.00 55.29 C ANISOU 105 CD2 LEU A 42 5956 7224 7826 -2997 1558 1782 C ATOM 106 N GLY A 43 -19.384 -40.018 30.820 1.00 68.63 N ANISOU 106 N GLY A 43 9969 7471 8634 -134 1768 -457 N ATOM 107 CA GLY A 43 -18.581 -38.907 30.349 1.00 65.03 C ANISOU 107 CA GLY A 43 7647 7489 9570 559 247 -539 C ATOM 108 C GLY A 43 -17.535 -38.547 31.381 1.00 56.54 C ANISOU 108 C GLY A 43 7679 6345 7458 -139 1101 267 C ATOM 109 O GLY A 43 -16.809 -39.405 31.890 1.00 60.63 O ANISOU 109 O GLY A 43 6905 8754 7376 1391 1980 256 O ATOM 110 N HIS A 44 -17.493 -37.266 31.710 1.00 50.56 N ANISOU 110 N HIS A 44 6621 6824 5765 -416 804 -879 N ATOM 111 CA HIS A 44 -16.435 -36.707 32.517 1.00 41.78 C ANISOU 111 CA HIS A 44 5520 5566 4787 318 746 141 C ATOM 112 C HIS A 44 -16.908 -36.389 33.904 1.00 34.92 C ANISOU 112 C HIS A 44 5073 3730 4464 352 371 985 C ATOM 113 O HIS A 44 -16.158 -35.821 34.714 1.00 39.30 O ANISOU 113 O HIS A 44 5597 4476 4858 662 -390 1115 O ATOM 114 CB HIS A 44 -15.918 -35.449 31.835 1.00 43.88 C ANISOU 114 CB HIS A 44 6014 5160 5499 274 985 -5 C ATOM 115 CG HIS A 44 -15.532 -35.658 30.383 1.00 42.76 C ANISOU 115 CG HIS A 44 5809 5151 5286 -159 221 -548 C ATOM 116 ND1 HIS A 44 -16.267 -35.182 29.356 1.00 47.41 N ANISOU 116 ND1 HIS A 44 7193 5176 5645 262 201 -30 N ATOM 117 CD2 HIS A 44 -14.456 -36.339 29.813 1.00 39.60 C ANISOU 117 CD2 HIS A 44 5491 4151 5403 -609 451 224 C ATOM 118 CE1 HIS A 44 -15.687 -35.525 28.191 1.00 44.15 C ANISOU 118 CE1 HIS A 44 5515 5613 5647 -723 202 271 C ATOM 119 NE2 HIS A 44 -14.582 -36.238 28.471 1.00 43.49 N ANISOU 119 NE2 HIS A 44 5899 5078 5545 -605 478 304 N ATOM 120 N ILE A 45 -18.151 -36.748 34.210 1.00 37.25 N ANISOU 120 N ILE A 45 4996 3780 5375 560 755 180 N ATOM 121 CA ILE A 45 -18.693 -36.470 35.546 1.00 40.36 C ANISOU 121 CA ILE A 45 5621 4623 5090 283 600 73 C ATOM 122 C ILE A 45 -17.799 -37.002 36.673 1.00 42.16 C ANISOU 122 C ILE A 45 5902 4747 5367 167 599 662 C ATOM 123 O ILE A 45 -17.514 -36.293 37.650 1.00 44.94 O ANISOU 123 O ILE A 45 6526 4785 5761 425 805 414 O ATOM 124 CB ILE A 45 -20.159 -36.949 35.691 1.00 45.46 C ANISOU 124 CB ILE A 45 5972 5408 5891 227 1176 158 C ATOM 125 CG1 ILE A 45 -20.817 -36.315 36.927 1.00 46.65 C ANISOU 125 CG1 ILE A 45 7474 5341 4911 -95 621 306 C ATOM 126 CG2 ILE A 45 -20.249 -38.470 35.700 1.00 46.63 C ANISOU 126 CG2 ILE A 45 5866 5195 6653 356 322 478 C ATOM 127 CD1 ILE A 45 -20.502 -34.841 37.088 1.00 42.53 C ANISOU 127 CD1 ILE A 45 6055 4925 5178 1390 1586 -697 C ATOM 128 N ILE A 46 -17.332 -38.238 36.525 1.00 41.91 N ANISOU 128 N ILE A 46 5493 4728 5703 133 438 263 N ATOM 129 CA ILE A 46 -16.503 -38.859 37.560 1.00 45.23 C ANISOU 129 CA ILE A 46 5747 5547 5890 67 -207 273 C ATOM 130 C ILE A 46 -15.192 -38.102 37.759 1.00 42.25 C ANISOU 130 C ILE A 46 6262 4323 5467 4 -90 251 C ATOM 131 O ILE A 46 -14.802 -37.800 38.886 1.00 46.99 O ANISOU 131 O ILE A 46 7168 5208 5476 827 -533 215 O ATOM 132 CB ILE A 46 -16.216 -40.351 37.256 1.00 44.32 C ANISOU 132 CB ILE A 46 5025 5416 6396 226 -14 503 C ATOM 133 CG1 ILE A 46 -17.501 -41.180 37.376 1.00 46.16 C ANISOU 133 CG1 ILE A 46 6393 4887 6255 -451 393 1001 C ATOM 134 CG2 ILE A 46 -15.118 -40.893 38.169 1.00 36.63 C ANISOU 134 CG2 ILE A 46 5809 3433 4676 -220 417 879 C ATOM 135 CD1 ILE A 46 -18.317 -40.898 38.625 1.00 52.31 C ANISOU 135 CD1 ILE A 46 7244 5757 6873 -144 762 -413 C ATOM 136 N GLN A 47 -14.518 -37.795 36.658 1.00 44.78 N ANISOU 136 N GLN A 47 6104 4918 5990 0 343 -76 N ATOM 137 CA GLN A 47 -13.280 -37.035 36.716 1.00 45.32 C ANISOU 137 CA GLN A 47 5760 5541 5919 143 3 -192 C ATOM 138 C GLN A 47 -13.561 -35.666 37.338 1.00 42.69 C ANISOU 138 C GLN A 47 5417 5185 5618 238 242 486 C ATOM 139 O GLN A 47 -12.811 -35.195 38.199 1.00 43.98 O ANISOU 139 O GLN A 47 6190 5106 5413 183 744 -336 O ATOM 140 CB GLN A 47 -12.672 -36.906 35.317 1.00 50.61 C ANISOU 140 CB GLN A 47 6603 5873 6752 109 945 328 C ATOM 141 CG GLN A 47 -12.406 -38.247 34.640 1.00 58.68 C ANISOU 141 CG GLN A 47 7655 6324 8315 -447 896 -661 C ATOM 142 CD GLN A 47 -12.151 -38.127 33.145 1.00 63.13 C ANISOU 142 CD GLN A 47 7709 7501 8777 -549 442 247 C ATOM 143 OE1 GLN A 47 -11.135 -37.581 32.717 1.00 70.37 O ANISOU 143 OE1 GLN A 47 8055 7143 11537 822 1719 2267 O ATOM 144 NE2 GLN A 47 -13.070 -38.658 32.340 1.00 69.06 N ANISOU 144 NE2 GLN A 47 7235 8509 10495 1043 -565 -765 N ATOM 145 N PHE A 48 -14.668 -35.052 36.931 1.00 44.35 N ANISOU 145 N PHE A 48 5505 5773 5574 1310 1455 628 N ATOM 146 CA PHE A 48 -15.041 -33.734 37.450 1.00 45.26 C ANISOU 146 CA PHE A 48 5731 5361 6102 484 575 153 C ATOM 147 C PHE A 48 -15.203 -33.767 38.968 1.00 47.76 C ANISOU 147 C PHE A 48 6037 6051 6059 360 -411 185 C ATOM 148 O PHE A 48 -14.650 -32.922 39.662 1.00 47.90 O ANISOU 148 O PHE A 48 6765 4927 6506 -319 -507 1047 O ATOM 149 CB PHE A 48 -16.320 -33.216 36.781 1.00 44.20 C ANISOU 149 CB PHE A 48 5852 5107 5833 754 1505 1602 C ATOM 150 CG PHE A 48 -16.703 -31.809 37.194 1.00 51.75 C ANISOU 150 CG PHE A 48 6783 5595 7284 72 1227 156 C ATOM 151 CD1 PHE A 48 -17.490 -31.586 38.323 1.00 50.32 C ANISOU 151 CD1 PHE A 48 7887 5043 6187 -733 556 -85 C ATOM 152 CD2 PHE A 48 -16.285 -30.713 36.448 1.00 43.78 C ANISOU 152 CD2 PHE A 48 4850 5428 6355 285 -739 416 C ATOM 153 CE1 PHE A 48 -17.847 -30.302 38.701 1.00 53.97 C ANISOU 153 CE1 PHE A 48 7115 5894 7496 189 1558 -490 C ATOM 154 CE2 PHE A 48 -16.639 -29.425 36.821 1.00 48.68 C ANISOU 154 CE2 PHE A 48 6225 5438 6834 -789 398 -472 C ATOM 155 CZ PHE A 48 -17.420 -29.218 37.949 1.00 54.61 C ANISOU 155 CZ PHE A 48 8338 5117 7291 1368 1089 -59 C ATOM 156 N GLY A 49 -15.951 -34.749 39.476 1.00 51.86 N ANISOU 156 N GLY A 49 6813 6248 6643 508 1044 309 N ATOM 157 CA GLY A 49 -16.172 -34.892 40.920 1.00 48.41 C ANISOU 157 CA GLY A 49 6315 5833 6244 -734 663 -5 C ATOM 158 C GLY A 49 -14.889 -34.965 41.734 1.00 53.36 C ANISOU 158 C GLY A 49 7654 6063 6554 222 -215 476 C ATOM 159 O GLY A 49 -14.776 -34.341 42.799 1.00 51.55 O ANISOU 159 O GLY A 49 7562 6364 5660 -1168 -563 1335 O ATOM 160 N LYS A 50 -13.920 -35.722 41.218 1.00 54.64 N ANISOU 160 N LYS A 50 6736 6273 7751 -321 955 1265 N ATOM 161 CA LYS A 50 -12.631 -35.937 41.876 1.00 53.01 C ANISOU 161 CA LYS A 50 6956 6696 6488 -502 755 1303 C ATOM 162 C LYS A 50 -11.868 -34.648 42.158 1.00 60.96 C ANISOU 162 C LYS A 50 9291 6578 7290 -842 182 393 C ATOM 163 O LYS A 50 -11.404 -34.428 43.277 1.00 72.66 O ANISOU 163 O LYS A 50 11246 8863 7499 65 -394 345 O ATOM 164 CB LYS A 50 -11.759 -36.876 41.037 1.00 57.47 C ANISOU 164 CB LYS A 50 8186 6719 6931 -364 -1128 -1210 C ATOM 165 CG LYS A 50 -11.913 -38.341 41.403 1.00 72.14 C ANISOU 165 CG LYS A 50 11287 7562 8560 729 -90 699 C ATOM 166 CD LYS A 50 -11.208 -38.647 42.716 1.00 78.14 C ANISOU 166 CD LYS A 50 11594 8040 10054 3220 -957 540 C ATOM 167 CE LYS A 50 -11.843 -39.834 43.427 1.00 96.37 C ANISOU 167 CE LYS A 50 12141 10537 13938 -780 332 -290 C ATOM 168 NZ LYS A 50 -11.852 -41.062 42.581 1.00101.50 N ANISOU 168 NZ LYS A 50 12280 12608 13677 -1725 1754 -1388 N ATOM 169 N SER A 51 -11.731 -33.811 41.133 1.00 52.33 N ANISOU 169 N SER A 51 7186 5806 6888 -143 674 -16 N ATOM 170 CA SER A 51 -11.023 -32.539 41.245 1.00 43.80 C ANISOU 170 CA SER A 51 5564 5515 5561 384 210 196 C ATOM 171 C SER A 51 -11.632 -31.575 40.232 1.00 43.63 C ANISOU 171 C SER A 51 5499 5283 5792 259 700 683 C ATOM 172 O SER A 51 -11.178 -31.503 39.095 1.00 43.18 O ANISOU 172 O SER A 51 5592 5041 5771 730 722 213 O ATOM 173 CB SER A 51 -9.524 -32.730 40.977 1.00 41.96 C ANISOU 173 CB SER A 51 5304 5095 5540 299 -571 1497 C ATOM 174 OG SER A 51 -8.815 -31.503 41.097 1.00 46.43 O ANISOU 174 OG SER A 51 4838 6392 6412 26 109 -578 O ATOM 175 N PRO A 52 -12.696 -30.856 40.628 1.00 46.39 N ANISOU 175 N PRO A 52 6108 5812 5705 1175 496 642 N ATOM 176 CA PRO A 52 -13.366 -29.929 39.711 1.00 38.94 C ANISOU 176 CA PRO A 52 5110 4662 5023 392 259 -78 C ATOM 177 C PRO A 52 -12.406 -28.965 39.018 1.00 32.38 C ANISOU 177 C PRO A 52 4005 3949 4349 1103 -75 -275 C ATOM 178 O PRO A 52 -12.398 -28.886 37.794 1.00 37.17 O ANISOU 178 O PRO A 52 5017 4375 4732 606 -60 540 O ATOM 179 CB PRO A 52 -14.345 -29.165 40.621 1.00 42.75 C ANISOU 179 CB PRO A 52 5169 5628 5446 762 878 204 C ATOM 180 CG PRO A 52 -14.058 -29.620 42.013 1.00 44.03 C ANISOU 180 CG PRO A 52 6004 5513 5210 642 584 -277 C ATOM 181 CD PRO A 52 -13.412 -30.964 41.906 1.00 44.78 C ANISOU 181 CD PRO A 52 6524 4999 5488 332 459 420 C ATOM 182 N LEU A 53 -11.594 -28.253 39.795 1.00 31.79 N ANISOU 182 N LEU A 53 4367 3536 4175 1013 -235 329 N ATOM 183 CA LEU A 53 -10.654 -27.289 39.247 1.00 37.04 C ANISOU 183 CA LEU A 53 4040 4802 5230 246 -29 -53 C ATOM 184 C LEU A 53 -9.524 -27.936 38.439 1.00 40.15 C ANISOU 184 C LEU A 53 5252 5124 4878 725 279 -253 C ATOM 185 O LEU A 53 -9.243 -27.520 37.311 1.00 41.43 O ANISOU 185 O LEU A 53 5361 4997 5384 1064 531 86 O ATOM 186 CB LEU A 53 -10.072 -26.422 40.362 1.00 36.52 C ANISOU 186 CB LEU A 53 4405 5336 4134 608 524 -44 C ATOM 187 CG LEU A 53 -9.028 -25.393 39.913 1.00 44.37 C ANISOU 187 CG LEU A 53 5377 5542 5939 -299 -283 511 C ATOM 188 CD1 LEU A 53 -9.590 -24.447 38.854 1.00 46.45 C ANISOU 188 CD1 LEU A 53 5929 6288 5430 387 277 575 C ATOM 189 CD2 LEU A 53 -8.504 -24.620 41.113 1.00 41.70 C ANISOU 189 CD2 LEU A 53 4755 5622 5466 129 1166 -131 C ATOM 190 N GLY A 54 -8.875 -28.936 39.031 1.00 38.78 N ANISOU 190 N GLY A 54 4221 5056 5456 255 -213 -406 N ATOM 191 CA GLY A 54 -7.804 -29.673 38.368 1.00 39.81 C ANISOU 191 CA GLY A 54 5607 5028 4489 917 55 88 C ATOM 192 C GLY A 54 -8.249 -30.235 37.030 1.00 37.16 C ANISOU 192 C GLY A 54 4619 4250 5247 350 -70 -45 C ATOM 193 O GLY A 54 -7.541 -30.106 36.033 1.00 43.05 O ANISOU 193 O GLY A 54 5499 5523 5333 952 265 200 O ATOM 194 N PHE A 55 -9.431 -30.848 37.007 1.00 36.84 N ANISOU 194 N PHE A 55 4640 3930 5427 190 -44 -380 N ATOM 195 CA PHE A 55 -9.990 -31.396 35.777 1.00 31.62 C ANISOU 195 CA PHE A 55 4032 3621 4359 618 430 -204 C ATOM 196 C PHE A 55 -10.231 -30.302 34.748 1.00 39.00 C ANISOU 196 C PHE A 55 5512 4712 4592 432 871 504 C ATOM 197 O PHE A 55 -9.811 -30.426 33.596 1.00 36.33 O ANISOU 197 O PHE A 55 5181 3353 5266 1327 1360 -259 O ATOM 198 CB PHE A 55 -11.301 -32.163 36.049 1.00 31.94 C ANISOU 198 CB PHE A 55 4128 3606 4400 488 193 -363 C ATOM 199 CG PHE A 55 -12.004 -32.623 34.801 1.00 33.77 C ANISOU 199 CG PHE A 55 4264 4475 4089 61 250 240 C ATOM 200 CD1 PHE A 55 -11.443 -33.615 33.987 1.00 40.55 C ANISOU 200 CD1 PHE A 55 5757 4443 5204 455 -363 -713 C ATOM 201 CD2 PHE A 55 -13.209 -32.064 34.422 1.00 35.94 C ANISOU 201 CD2 PHE A 55 4123 4398 5134 -428 79 924 C ATOM 202 CE1 PHE A 55 -12.080 -34.033 32.827 1.00 36.46 C ANISOU 202 CE1 PHE A 55 5175 4223 4454 328 496 -450 C ATOM 203 CE2 PHE A 55 -13.853 -32.477 33.262 1.00 42.21 C ANISOU 203 CE2 PHE A 55 6298 4961 4777 -320 231 94 C ATOM 204 CZ PHE A 55 -13.288 -33.462 32.464 1.00 39.72 C ANISOU 204 CZ PHE A 55 4967 4747 5375 166 724 749 C ATOM 205 N MET A 56 -10.912 -29.231 35.158 1.00 40.97 N ANISOU 205 N MET A 56 5630 4491 5444 354 546 476 N ATOM 206 CA MET A 56 -11.268 -28.176 34.218 1.00 33.38 C ANISOU 206 CA MET A 56 4266 3895 4521 224 650 -173 C ATOM 207 C MET A 56 -10.018 -27.528 33.625 1.00 29.82 C ANISOU 207 C MET A 56 4035 3426 3866 625 640 -670 C ATOM 208 O MET A 56 -9.977 -27.258 32.425 1.00 34.34 O ANISOU 208 O MET A 56 4451 4164 4432 571 1369 10 O ATOM 209 CB MET A 56 -12.197 -27.140 34.869 1.00 33.29 C ANISOU 209 CB MET A 56 4111 4060 4477 575 985 455 C ATOM 210 CG MET A 56 -13.656 -27.589 34.902 1.00 34.45 C ANISOU 210 CG MET A 56 3938 4336 4814 661 285 379 C ATOM 211 SD MET A 56 -14.820 -26.313 35.435 1.00 32.84 S ANISOU 211 SD MET A 56 4502 3788 4186 82 427 -304 S ATOM 212 CE MET A 56 -14.460 -26.278 37.187 1.00 33.88 C ANISOU 212 CE MET A 56 4877 4216 3777 166 627 1042 C ATOM 213 N GLN A 57 -9.005 -27.294 34.457 1.00 33.02 N ANISOU 213 N GLN A 57 3815 4066 4665 942 543 -547 N ATOM 214 CA GLN A 57 -7.745 -26.698 33.989 1.00 39.13 C ANISOU 214 CA GLN A 57 5045 4712 5109 -92 559 -315 C ATOM 215 C GLN A 57 -6.974 -27.647 33.075 1.00 45.49 C ANISOU 215 C GLN A 57 5107 5277 6898 911 972 -337 C ATOM 216 O GLN A 57 -6.216 -27.201 32.210 1.00 47.78 O ANISOU 216 O GLN A 57 6588 4182 7381 781 1291 -208 O ATOM 217 CB GLN A 57 -6.872 -26.270 35.164 1.00 44.41 C ANISOU 217 CB GLN A 57 4580 6087 6204 697 -405 -383 C ATOM 218 CG GLN A 57 -7.331 -24.984 35.831 1.00 45.98 C ANISOU 218 CG GLN A 57 6274 5262 5933 383 66 215 C ATOM 219 CD GLN A 57 -6.514 -24.644 37.057 1.00 47.16 C ANISOU 219 CD GLN A 57 5881 6053 5982 -27 199 254 C ATOM 220 OE1 GLN A 57 -6.023 -25.533 37.752 1.00 49.73 O ANISOU 220 OE1 GLN A 57 5615 6538 6738 1095 539 53 O ATOM 221 NE2 GLN A 57 -6.365 -23.352 37.333 1.00 44.40 N ANISOU 221 NE2 GLN A 57 5695 5488 5685 316 2080 1117 N ATOM 222 N GLU A 58 -7.171 -28.951 33.263 1.00 47.56 N ANISOU 222 N GLU A 58 6209 5116 6746 642 1354 290 N ATOM 223 CA GLU A 58 -6.560 -29.943 32.377 1.00 45.73 C ANISOU 223 CA GLU A 58 6639 5278 5456 84 305 -385 C ATOM 224 C GLU A 58 -7.200 -29.878 30.997 1.00 42.12 C ANISOU 224 C GLU A 58 5456 4714 5832 625 205 294 C ATOM 225 O GLU A 58 -6.505 -29.961 29.981 1.00 44.83 O ANISOU 225 O GLU A 58 5586 5727 5720 272 276 1205 O ATOM 226 CB GLU A 58 -6.671 -31.358 32.961 1.00 51.22 C ANISOU 226 CB GLU A 58 6556 5629 7276 639 1763 246 C ATOM 227 CG GLU A 58 -6.150 -32.467 32.051 1.00 47.63 C ANISOU 227 CG GLU A 58 7054 5577 5462 239 733 344 C ATOM 228 CD GLU A 58 -4.661 -32.353 31.767 1.00 58.85 C ANISOU 228 CD GLU A 58 7062 7808 7488 328 378 87 C ATOM 229 OE1 GLU A 58 -3.897 -31.990 32.688 1.00 63.29 O ANISOU 229 OE1 GLU A 58 7094 8555 8395 276 -263 0 O ATOM 230 OE2 GLU A 58 -4.254 -32.630 30.621 1.00 66.74 O ANISOU 230 OE2 GLU A 58 7780 9510 8066 134 796 -1123 O ATOM 231 N CYS A 59 -8.524 -29.728 30.960 1.00 34.72 N ANISOU 231 N CYS A 59 4581 3521 5087 -502 539 948 N ATOM 232 CA CYS A 59 -9.225 -29.595 29.683 1.00 39.90 C ANISOU 232 CA CYS A 59 5200 4796 5162 -627 -60 -548 C ATOM 233 C CYS A 59 -8.726 -28.354 28.936 1.00 43.83 C ANISOU 233 C CYS A 59 6199 5358 5096 -496 72 -115 C ATOM 234 O CYS A 59 -8.540 -28.380 27.719 1.00 44.35 O ANISOU 234 O CYS A 59 6565 4580 5704 426 925 -702 O ATOM 235 CB CYS A 59 -10.742 -29.492 29.884 1.00 44.30 C ANISOU 235 CB CYS A 59 5495 5079 6257 -234 1223 -10 C ATOM 236 SG CYS A 59 -11.582 -30.948 30.564 1.00 41.29 S ANISOU 236 SG CYS A 59 5377 4695 5616 49 905 29 S ATOM 237 N LYS A 60 -8.502 -27.278 29.693 1.00 39.10 N ANISOU 237 N LYS A 60 4443 4662 5750 -57 1209 -294 N ATOM 238 CA LYS A 60 -8.116 -25.986 29.151 1.00 43.31 C ANISOU 238 CA LYS A 60 5592 5272 5592 -366 794 201 C ATOM 239 C LYS A 60 -6.735 -26.112 28.517 1.00 42.16 C ANISOU 239 C LYS A 60 5421 5416 5182 295 245 -126 C ATOM 240 O LYS A 60 -6.509 -25.676 27.380 1.00 42.62 O ANISOU 240 O LYS A 60 6161 4573 5457 -91 1414 -1020 O ATOM 241 CB LYS A 60 -8.093 -24.960 30.292 1.00 46.98 C ANISOU 241 CB LYS A 60 6744 5116 5991 -145 701 23 C ATOM 242 CG LYS A 60 -8.677 -23.602 29.956 1.00 50.90 C ANISOU 242 CG LYS A 60 7013 5745 6580 788 97 -465 C ATOM 243 CD LYS A 60 -8.545 -22.666 31.151 1.00 46.78 C ANISOU 243 CD LYS A 60 6101 5913 5761 443 1104 -74 C ATOM 244 CE LYS A 60 -8.243 -21.249 30.697 1.00 53.53 C ANISOU 244 CE LYS A 60 7441 6010 6888 -248 1199 -264 C ATOM 245 NZ LYS A 60 -8.193 -20.309 31.852 1.00 55.25 N ANISOU 245 NZ LYS A 60 7167 7046 6776 -1903 -2175 -473 N ATOM 246 N ARG A 61 -5.828 -26.730 29.269 1.00 38.11 N ANISOU 246 N ARG A 61 4845 4459 5173 -245 322 -187 N ATOM 247 CA ARG A 61 -4.458 -26.978 28.834 1.00 43.75 C ANISOU 247 CA ARG A 61 5105 5927 5591 148 417 -2 C ATOM 248 C ARG A 61 -4.410 -27.893 27.612 1.00 47.19 C ANISOU 248 C ARG A 61 5782 5289 6855 -241 1065 -333 C ATOM 249 O ARG A 61 -3.707 -27.609 26.639 1.00 48.34 O ANISOU 249 O ARG A 61 6801 4684 6882 0 718 937 O ATOM 250 CB ARG A 61 -3.687 -27.618 29.978 1.00 42.58 C ANISOU 250 CB ARG A 61 5098 5351 5725 658 781 41 C ATOM 251 CG ARG A 61 -2.214 -27.283 30.013 1.00 51.88 C ANISOU 251 CG ARG A 61 6191 6172 7347 -1476 481 920 C ATOM 252 CD ARG A 61 -1.575 -27.866 31.263 1.00 63.27 C ANISOU 252 CD ARG A 61 8496 8911 6633 -1332 -221 661 C ATOM 253 NE ARG A 61 -2.039 -27.212 32.488 1.00 70.07 N ANISOU 253 NE ARG A 61 8650 8949 9023 -414 670 -206 N ATOM 254 CZ ARG A 61 -2.796 -27.787 33.424 1.00 65.09 C ANISOU 254 CZ ARG A 61 6791 8608 9332 855 1077 -649 C ATOM 255 NH1 ARG A 61 -3.196 -29.052 33.303 1.00 61.74 N ANISOU 255 NH1 ARG A 61 5438 8590 9429 1268 -981 -490 N ATOM 256 NH2 ARG A 61 -3.147 -27.092 34.497 1.00 62.11 N ANISOU 256 NH2 ARG A 61 6693 9694 7210 885 -1042 -338 N ATOM 257 N GLN A 62 -5.161 -28.990 27.662 1.00 43.75 N ANISOU 257 N GLN A 62 5352 5280 5988 -147 1905 181 N ATOM 258 CA GLN A 62 -5.113 -29.976 26.595 1.00 45.27 C ANISOU 258 CA GLN A 62 6203 5782 5215 -148 1156 394 C ATOM 259 C GLN A 62 -5.734 -29.529 25.283 1.00 46.90 C ANISOU 259 C GLN A 62 5509 6233 6077 1129 1138 1040 C ATOM 260 O GLN A 62 -5.210 -29.846 24.214 1.00 48.24 O ANISOU 260 O GLN A 62 7707 5422 5197 596 1053 967 O ATOM 261 CB GLN A 62 -5.707 -31.316 27.027 1.00 47.00 C ANISOU 261 CB GLN A 62 4547 6255 7052 -616 1726 -153 C ATOM 262 CG GLN A 62 -4.639 -32.359 27.306 1.00 55.49 C ANISOU 262 CG GLN A 62 7940 5880 7263 74 119 1479 C ATOM 263 CD GLN A 62 -4.842 -33.616 26.486 1.00 65.39 C ANISOU 263 CD GLN A 62 9257 7518 8070 617 566 -215 C ATOM 264 OE1 GLN A 62 -5.858 -34.303 26.619 1.00 73.54 O ANISOU 264 OE1 GLN A 62 8729 10190 9022 -63 19 -909 O ATOM 265 NE2 GLN A 62 -3.876 -33.921 25.625 1.00 60.28 N ANISOU 265 NE2 GLN A 62 8141 6931 7831 -1378 823 1125 N ATOM 266 N LEU A 63 -6.846 -28.810 25.361 1.00 36.36 N ANISOU 266 N LEU A 63 5441 3676 4696 49 1328 501 N ATOM 267 CA LEU A 63 -7.550 -28.381 24.156 1.00 43.65 C ANISOU 267 CA LEU A 63 5240 5883 5459 -586 152 287 C ATOM 268 C LEU A 63 -7.116 -26.987 23.685 1.00 38.34 C ANISOU 268 C LEU A 63 5284 4932 4351 429 501 -525 C ATOM 269 O LEU A 63 -7.690 -26.438 22.736 1.00 37.92 O ANISOU 269 O LEU A 63 5341 4393 4672 260 1281 551 O ATOM 270 CB LEU A 63 -9.064 -28.434 24.372 1.00 44.59 C ANISOU 270 CB LEU A 63 5444 5147 6348 -385 1259 -404 C ATOM 271 CG LEU A 63 -9.651 -29.787 24.794 1.00 42.38 C ANISOU 271 CG LEU A 63 5600 4986 5516 -718 1499 -1113 C ATOM 272 CD1 LEU A 63 -11.053 -29.564 25.340 1.00 34.91 C ANISOU 272 CD1 LEU A 63 5270 3727 4265 -1298 1384 1029 C ATOM 273 CD2 LEU A 63 -9.650 -30.808 23.647 1.00 35.20 C ANISOU 273 CD2 LEU A 63 5203 3325 4845 -74 597 140 C ATOM 274 N LYS A 64 -6.102 -26.440 24.362 1.00 34.79 N ANISOU 274 N LYS A 64 3543 5267 4408 149 1749 55 N ATOM 275 CA LYS A 64 -5.535 -25.118 24.079 1.00 44.95 C ANISOU 275 CA LYS A 64 5199 5364 6515 88 2167 684 C ATOM 276 C LYS A 64 -6.616 -24.071 23.925 1.00 47.99 C ANISOU 276 C LYS A 64 6205 5780 6247 564 1347 620 C ATOM 277 O LYS A 64 -6.651 -23.364 22.920 1.00 43.45 O ANISOU 277 O LYS A 64 5003 5985 5518 216 2821 -33 O ATOM 278 CB LYS A 64 -4.686 -25.158 22.802 1.00 47.17 C ANISOU 278 CB LYS A 64 6245 5727 5948 879 2077 945 C ATOM 279 CG LYS A 64 -3.445 -26.026 22.902 1.00 44.20 C ANISOU 279 CG LYS A 64 5395 5741 5658 338 1770 557 C ATOM 280 CD LYS A 64 -2.752 -26.133 21.551 1.00 49.13 C ANISOU 280 CD LYS A 64 6156 6836 5672 1309 1423 -348 C ATOM 281 CE LYS A 64 -1.590 -27.104 21.624 1.00 44.42 C ANISOU 281 CE LYS A 64 5626 6045 5207 845 1286 227 C ATOM 282 NZ LYS A 64 -1.105 -27.449 20.257 1.00 48.39 N ANISOU 282 NZ LYS A 64 6695 6122 5567 1840 1789 383 N ATOM 283 N SER A 65 -7.509 -23.974 24.908 1.00 44.97 N ANISOU 283 N SER A 65 5991 5243 5852 348 1099 -130 N ATOM 284 CA SER A 65 -8.706 -23.159 24.746 1.00 40.02 C ANISOU 284 CA SER A 65 5410 5367 4427 15 868 271 C ATOM 285 C SER A 65 -9.395 -22.916 26.083 1.00 44.59 C ANISOU 285 C SER A 65 5935 5576 5431 589 1960 570 C ATOM 286 O SER A 65 -9.583 -23.851 26.852 1.00 37.39 O ANISOU 286 O SER A 65 4625 4405 5175 792 1723 -182 O ATOM 287 CB SER A 65 -9.673 -23.866 23.796 1.00 37.53 C ANISOU 287 CB SER A 65 4863 5062 4335 446 539 705 C ATOM 288 OG SER A 65 -10.686 -22.986 23.340 1.00 35.21 O ANISOU 288 OG SER A 65 4692 4174 4512 -16 784 1157 O ATOM 289 N GLY A 66 -9.758 -21.663 26.356 1.00 44.06 N ANISOU 289 N GLY A 66 5618 5444 5679 773 1654 674 N ATOM 290 CA GLY A 66 -10.552 -21.321 27.550 1.00 37.17 C ANISOU 290 CA GLY A 66 4977 4364 4782 342 300 -516 C ATOM 291 C GLY A 66 -12.019 -21.693 27.369 1.00 37.78 C ANISOU 291 C GLY A 66 5282 4760 4312 -307 486 -313 C ATOM 292 O GLY A 66 -12.768 -21.792 28.336 1.00 39.06 O ANISOU 292 O GLY A 66 4925 4466 5449 -703 1047 -509 O ATOM 293 N ILE A 67 -12.425 -21.898 26.119 1.00 30.90 N ANISOU 293 N ILE A 67 4229 3401 4110 366 378 71 N ATOM 294 CA ILE A 67 -13.778 -22.326 25.784 1.00 33.50 C ANISOU 294 CA ILE A 67 4379 3894 4453 -168 667 108 C ATOM 295 C ILE A 67 -13.715 -23.761 25.267 1.00 41.79 C ANISOU 295 C ILE A 67 6154 4548 5174 -477 1257 -556 C ATOM 296 O ILE A 67 -13.067 -24.037 24.246 1.00 35.81 O ANISOU 296 O ILE A 67 4751 3859 4992 -310 726 20 O ATOM 297 CB ILE A 67 -14.397 -21.402 24.719 1.00 32.43 C ANISOU 297 CB ILE A 67 4216 4645 3459 115 668 -643 C ATOM 298 CG1 ILE A 67 -14.318 -19.941 25.197 1.00 40.98 C ANISOU 298 CG1 ILE A 67 5194 4320 6053 -307 390 -57 C ATOM 299 CG2 ILE A 67 -15.838 -21.801 24.423 1.00 32.26 C ANISOU 299 CG2 ILE A 67 4570 4361 3326 -393 579 -530 C ATOM 300 CD1 ILE A 67 -14.302 -18.923 24.084 1.00 49.27 C ANISOU 300 CD1 ILE A 67 7248 5014 6455 472 -566 556 C ATOM 301 N PHE A 68 -14.380 -24.675 25.973 1.00 38.76 N ANISOU 301 N PHE A 68 4997 4880 4848 78 1537 -399 N ATOM 302 CA PHE A 68 -14.329 -26.098 25.635 1.00 33.11 C ANISOU 302 CA PHE A 68 4277 4463 3841 -86 153 319 C ATOM 303 C PHE A 68 -15.589 -26.815 26.094 1.00 39.08 C ANISOU 303 C PHE A 68 5332 4952 4564 -887 728 -20 C ATOM 304 O PHE A 68 -16.308 -26.324 26.966 1.00 38.99 O ANISOU 304 O PHE A 68 5613 4333 4867 72 661 322 O ATOM 305 CB PHE A 68 -13.099 -26.734 26.270 1.00 32.93 C ANISOU 305 CB PHE A 68 4938 3358 4213 406 282 522 C ATOM 306 CG PHE A 68 -13.023 -26.552 27.763 1.00 30.54 C ANISOU 306 CG PHE A 68 3490 4031 4083 317 467 -351 C ATOM 307 CD1 PHE A 68 -12.505 -25.381 28.310 1.00 29.60 C ANISOU 307 CD1 PHE A 68 3871 3548 3827 -270 139 804 C ATOM 308 CD2 PHE A 68 -13.470 -27.555 28.628 1.00 37.30 C ANISOU 308 CD2 PHE A 68 5397 4632 4141 -99 -160 387 C ATOM 309 CE1 PHE A 68 -12.442 -25.201 29.687 1.00 32.02 C ANISOU 309 CE1 PHE A 68 3472 4678 4013 -197 606 95 C ATOM 310 CE2 PHE A 68 -13.405 -27.384 30.008 1.00 31.63 C ANISOU 310 CE2 PHE A 68 3803 4142 4073 129 496 94 C ATOM 311 CZ PHE A 68 -12.885 -26.211 30.536 1.00 32.20 C ANISOU 311 CZ PHE A 68 4433 3837 3961 479 812 -99 C ATOM 312 N THR A 69 -15.857 -27.975 25.502 1.00 39.81 N ANISOU 312 N THR A 69 6316 4681 4126 -173 2086 -148 N ATOM 313 CA THR A 69 -17.060 -28.734 25.816 1.00 36.44 C ANISOU 313 CA THR A 69 4596 4438 4810 499 402 -408 C ATOM 314 C THR A 69 -16.686 -30.052 26.506 1.00 43.61 C ANISOU 314 C THR A 69 6397 4900 5270 971 1604 538 C ATOM 315 O THR A 69 -15.824 -30.792 26.024 1.00 36.08 O ANISOU 315 O THR A 69 4908 4053 4744 412 239 555 O ATOM 316 CB THR A 69 -17.887 -29.005 24.549 1.00 38.63 C ANISOU 316 CB THR A 69 5047 5253 4378 799 489 -85 C ATOM 317 OG1 THR A 69 -18.195 -27.763 23.907 1.00 42.44 O ANISOU 317 OG1 THR A 69 6323 4327 5473 -63 1728 143 O ATOM 318 CG2 THR A 69 -19.194 -29.741 24.874 1.00 41.57 C ANISOU 318 CG2 THR A 69 6418 4390 4987 372 1703 -423 C ATOM 319 N ILE A 70 -17.307 -30.313 27.655 1.00 37.98 N ANISOU 319 N ILE A 70 5232 4415 4782 672 927 176 N ATOM 320 CA ILE A 70 -17.215 -31.625 28.295 1.00 33.14 C ANISOU 320 CA ILE A 70 4609 4033 3948 122 818 -353 C ATOM 321 C ILE A 70 -18.538 -32.377 28.130 1.00 35.59 C ANISOU 321 C ILE A 70 4568 4580 4374 -119 611 510 C ATOM 322 O ILE A 70 -19.503 -31.851 27.558 1.00 34.24 O ANISOU 322 O ILE A 70 4507 4129 4370 338 1183 -47 O ATOM 323 CB ILE A 70 -16.751 -31.556 29.777 1.00 34.96 C ANISOU 323 CB ILE A 70 4351 4567 4365 122 392 417 C ATOM 324 CG1 ILE A 70 -17.716 -30.725 30.645 1.00 33.30 C ANISOU 324 CG1 ILE A 70 5368 3435 3847 -165 411 300 C ATOM 325 CG2 ILE A 70 -15.333 -31.017 29.863 1.00 36.52 C ANISOU 325 CG2 ILE A 70 4517 4563 4794 186 280 -61 C ATOM 326 CD1 ILE A 70 -17.444 -30.825 32.133 1.00 29.61 C ANISOU 326 CD1 ILE A 70 4115 3211 3925 -133 326 200 C ATOM 327 N ASN A 71 -18.574 -33.624 28.586 1.00 37.28 N ANISOU 327 N ASN A 71 5364 4338 4463 -650 1048 128 N ATOM 328 CA ASN A 71 -19.779 -34.439 28.453 1.00 36.14 C ANISOU 328 CA ASN A 71 4600 4775 4354 -166 266 -43 C ATOM 329 C ASN A 71 -20.218 -34.975 29.825 1.00 37.23 C ANISOU 329 C ASN A 71 4703 4552 4890 136 817 369 C ATOM 330 O ASN A 71 -19.460 -35.673 30.499 1.00 40.90 O ANISOU 330 O ASN A 71 5441 5296 4802 -246 377 1013 O ATOM 331 CB ASN A 71 -19.539 -35.573 27.445 1.00 38.85 C ANISOU 331 CB ASN A 71 5331 4989 4440 -423 1087 -54 C ATOM 332 CG ASN A 71 -20.769 -36.432 27.228 1.00 43.70 C ANISOU 332 CG ASN A 71 6442 4435 5725 -819 288 -391 C ATOM 333 OD1 ASN A 71 -21.230 -37.100 28.144 1.00 52.49 O ANISOU 333 OD1 ASN A 71 7522 5898 6520 -643 1752 -59 O ATOM 334 ND2 ASN A 71 -21.299 -36.424 26.009 1.00 49.12 N ANISOU 334 ND2 ASN A 71 6111 6116 6435 -319 -257 814 N ATOM 335 N ILE A 72 -21.426 -34.610 30.244 1.00 32.82 N ANISOU 335 N ILE A 72 3918 3868 4682 -601 268 158 N ATOM 336 CA ILE A 72 -21.945 -35.014 31.557 1.00 38.64 C ANISOU 336 CA ILE A 72 5300 4733 4646 -342 552 140 C ATOM 337 C ILE A 72 -23.139 -35.939 31.331 1.00 36.95 C ANISOU 337 C ILE A 72 4546 4807 4686 -22 537 123 C ATOM 338 O ILE A 72 -24.201 -35.495 30.893 1.00 36.68 O ANISOU 338 O ILE A 72 4636 4411 4887 195 569 -170 O ATOM 339 CB ILE A 72 -22.358 -33.803 32.438 1.00 39.52 C ANISOU 339 CB ILE A 72 5186 4835 4994 -176 1030 346 C ATOM 340 CG1 ILE A 72 -21.230 -32.769 32.533 1.00 41.36 C ANISOU 340 CG1 ILE A 72 5605 4959 5151 -271 -402 407 C ATOM 341 CG2 ILE A 72 -22.784 -34.255 33.838 1.00 37.85 C ANISOU 341 CG2 ILE A 72 5298 5015 4065 315 -583 628 C ATOM 342 CD1 ILE A 72 -20.078 -33.164 33.431 1.00 38.95 C ANISOU 342 CD1 ILE A 72 5528 4683 4587 -5 447 1675 C ATOM 343 N VAL A 73 -22.948 -37.229 31.597 1.00 39.47 N ANISOU 343 N VAL A 73 4975 4806 5213 -285 347 274 N ATOM 344 CA VAL A 73 -23.992 -38.229 31.348 1.00 40.86 C ANISOU 344 CA VAL A 73 5991 4481 5050 -574 337 -54 C ATOM 345 C VAL A 73 -24.569 -38.072 29.939 1.00 41.08 C ANISOU 345 C VAL A 73 5382 4874 5350 92 238 0 C ATOM 346 O VAL A 73 -25.782 -38.168 29.737 1.00 44.13 O ANISOU 346 O VAL A 73 5459 4369 6937 -1118 601 337 O ATOM 347 CB VAL A 73 -25.137 -38.135 32.385 1.00 48.65 C ANISOU 347 CB VAL A 73 5942 6629 5915 -222 519 -127 C ATOM 348 CG1 VAL A 73 -26.053 -39.351 32.293 1.00 52.93 C ANISOU 348 CG1 VAL A 73 6744 6652 6713 -474 57 170 C ATOM 349 CG2 VAL A 73 -24.580 -38.007 33.792 1.00 45.69 C ANISOU 349 CG2 VAL A 73 5725 6292 5341 -412 978 345 C ATOM 350 N GLY A 74 -23.700 -37.815 28.962 1.00 38.18 N ANISOU 350 N GLY A 74 5000 4439 5065 -470 -11 170 N ATOM 351 CA GLY A 74 -24.140 -37.724 27.574 1.00 43.82 C ANISOU 351 CA GLY A 74 6393 5194 5059 356 -207 110 C ATOM 352 C GLY A 74 -24.674 -36.366 27.164 1.00 44.25 C ANISOU 352 C GLY A 74 6060 5070 5680 233 -255 -229 C ATOM 353 O GLY A 74 -25.166 -36.213 26.051 1.00 45.35 O ANISOU 353 O GLY A 74 7537 4784 4908 -58 460 -243 O ATOM 354 N LYS A 75 -24.595 -35.380 28.056 1.00 37.30 N ANISOU 354 N LYS A 75 5055 4625 4491 -11 880 333 N ATOM 355 CA LYS A 75 -25.012 -34.018 27.713 1.00 35.30 C ANISOU 355 CA LYS A 75 4452 4608 4350 -363 780 453 C ATOM 356 C LYS A 75 -23.793 -33.141 27.513 1.00 30.42 C ANISOU 356 C LYS A 75 4083 3572 3902 0 29 -345 C ATOM 357 O LYS A 75 -22.867 -33.158 28.331 1.00 29.72 O ANISOU 357 O LYS A 75 3743 3549 3999 -213 505 88 O ATOM 358 CB LYS A 75 -25.919 -33.400 28.784 1.00 36.73 C ANISOU 358 CB LYS A 75 5261 4304 4389 25 721 252 C ATOM 359 CG LYS A 75 -27.181 -34.192 29.112 1.00 40.25 C ANISOU 359 CG LYS A 75 4468 5270 5553 0 501 -512 C ATOM 360 CD LYS A 75 -28.030 -34.498 27.882 1.00 49.39 C ANISOU 360 CD LYS A 75 6401 7130 5233 -392 -251 442 C ATOM 361 CE LYS A 75 -29.290 -35.268 28.256 1.00 52.48 C ANISOU 361 CE LYS A 75 6986 5580 7373 -580 -283 -187 C ATOM 362 NZ LYS A 75 -28.966 -36.551 28.948 1.00 45.36 N ANISOU 362 NZ LYS A 75 6032 6111 5088 -384 1206 -159 N ATOM 363 N ARG A 76 -23.799 -32.396 26.410 1.00 33.81 N ANISOU 363 N ARG A 76 4853 3979 4014 -274 618 -139 N ATOM 364 CA ARG A 76 -22.732 -31.451 26.082 1.00 35.87 C ANISOU 364 CA ARG A 76 5111 4532 3983 -915 -2 -400 C ATOM 365 C ARG A 76 -22.804 -30.265 27.033 1.00 30.91 C ANISOU 365 C ARG A 76 4208 3594 3939 -141 -79 366 C ATOM 366 O ARG A 76 -23.849 -29.633 27.173 1.00 34.24 O ANISOU 366 O ARG A 76 4596 3854 4556 -211 1253 222 O ATOM 367 CB ARG A 76 -22.862 -30.970 24.631 1.00 37.25 C ANISOU 367 CB ARG A 76 6355 3501 4296 -763 239 121 C ATOM 368 CG ARG A 76 -22.376 -31.985 23.586 1.00 39.36 C ANISOU 368 CG ARG A 76 6109 4284 4561 -507 711 -61 C ATOM 369 CD ARG A 76 -22.718 -31.561 22.164 1.00 38.48 C ANISOU 369 CD ARG A 76 5927 4268 4425 23 -49 -827 C ATOM 370 NE ARG A 76 -22.392 -30.148 21.931 1.00 42.34 N ANISOU 370 NE ARG A 76 5457 5254 5376 -829 170 -167 N ATOM 371 CZ ARG A 76 -21.200 -29.694 21.560 1.00 40.83 C ANISOU 371 CZ ARG A 76 5206 5399 4907 -166 13 315 C ATOM 372 NH1 ARG A 76 -20.189 -30.536 21.361 1.00 39.92 N ANISOU 372 NH1 ARG A 76 7028 3555 4583 -92 -435 -590 N ATOM 373 NH2 ARG A 76 -21.014 -28.387 21.396 1.00 44.29 N ANISOU 373 NH2 ARG A 76 6780 4933 5115 585 730 373 N ATOM 374 N VAL A 77 -21.697 -29.985 27.704 1.00 30.84 N ANISOU 374 N VAL A 77 3885 3917 3914 -336 236 23 N ATOM 375 CA VAL A 77 -21.626 -28.835 28.574 1.00 29.81 C ANISOU 375 CA VAL A 77 3739 3879 3706 -465 -188 -27 C ATOM 376 C VAL A 77 -20.442 -27.999 28.127 1.00 28.56 C ANISOU 376 C VAL A 77 3779 3972 3098 -13 514 152 C ATOM 377 O VAL A 77 -19.296 -28.410 28.280 1.00 32.12 O ANISOU 377 O VAL A 77 3886 4285 4031 -221 635 397 O ATOM 378 CB VAL A 77 -21.512 -29.247 30.056 1.00 30.68 C ANISOU 378 CB VAL A 77 3804 4062 3789 -549 126 -34 C ATOM 379 CG1 VAL A 77 -21.321 -28.014 30.928 1.00 31.76 C ANISOU 379 CG1 VAL A 77 4122 4469 3474 -1033 1161 -274 C ATOM 380 CG2 VAL A 77 -22.770 -29.999 30.474 1.00 31.91 C ANISOU 380 CG2 VAL A 77 4404 3987 3732 -532 858 567 C ATOM 381 N THR A 78 -20.732 -26.840 27.548 1.00 29.35 N ANISOU 381 N THR A 78 4558 3394 3199 261 842 -350 N ATOM 382 CA THR A 78 -19.689 -25.928 27.065 1.00 31.55 C ANISOU 382 CA THR A 78 4437 3669 3880 30 191 -11 C ATOM 383 C THR A 78 -19.322 -24.877 28.115 1.00 28.15 C ANISOU 383 C THR A 78 3530 3481 3681 -220 112 466 C ATOM 384 O THR A 78 -20.146 -24.047 28.504 1.00 34.73 O ANISOU 384 O THR A 78 5143 3809 4244 180 888 101 O ATOM 385 CB THR A 78 -20.125 -25.241 25.759 1.00 34.43 C ANISOU 385 CB THR A 78 5027 4357 3695 -376 126 249 C ATOM 386 OG1 THR A 78 -20.342 -26.243 24.758 1.00 34.19 O ANISOU 386 OG1 THR A 78 5100 4025 3865 -204 677 251 O ATOM 387 CG2 THR A 78 -19.056 -24.255 25.285 1.00 32.69 C ANISOU 387 CG2 THR A 78 4324 3831 4264 219 113 478 C ATOM 388 N ILE A 79 -18.076 -24.918 28.561 1.00 26.06 N ANISOU 388 N ILE A 79 3480 3094 3325 -217 467 114 N ATOM 389 CA ILE A 79 -17.636 -24.075 29.636 1.00 27.34 C ANISOU 389 CA ILE A 79 3245 3644 3497 127 628 -246 C ATOM 390 C ILE A 79 -16.957 -22.832 29.071 1.00 33.51 C ANISOU 390 C ILE A 79 4534 3893 4304 45 686 322 C ATOM 391 O ILE A 79 -16.046 -22.929 28.238 1.00 33.29 O ANISOU 391 O ILE A 79 4445 4071 4129 250 607 531 O ATOM 392 CB ILE A 79 -16.723 -24.877 30.578 1.00 30.30 C ANISOU 392 CB ILE A 79 3801 3952 3757 -31 477 275 C ATOM 393 CG1 ILE A 79 -17.558 -25.955 31.292 1.00 29.70 C ANISOU 393 CG1 ILE A 79 4205 3377 3702 -49 127 207 C ATOM 394 CG2 ILE A 79 -15.989 -23.967 31.557 1.00 30.98 C ANISOU 394 CG2 ILE A 79 3889 3692 4188 40 398 91 C ATOM 395 CD1 ILE A 79 -16.736 -26.953 32.078 1.00 28.18 C ANISOU 395 CD1 ILE A 79 3766 3816 3122 215 527 131 C ATOM 396 N VAL A 80 -17.437 -21.667 29.496 1.00 33.69 N ANISOU 396 N VAL A 80 4321 3903 4576 61 1137 356 N ATOM 397 CA VAL A 80 -16.815 -20.392 29.143 1.00 32.12 C ANISOU 397 CA VAL A 80 4228 3616 4357 -148 -83 266 C ATOM 398 C VAL A 80 -15.780 -20.144 30.211 1.00 31.49 C ANISOU 398 C VAL A 80 4140 3585 4237 234 208 71 C ATOM 399 O VAL A 80 -16.057 -19.529 31.246 1.00 33.89 O ANISOU 399 O VAL A 80 4774 3509 4593 -313 180 -236 O ATOM 400 CB VAL A 80 -17.858 -19.267 29.075 1.00 30.67 C ANISOU 400 CB VAL A 80 4061 3311 4281 -387 -387 -67 C ATOM 401 CG1 VAL A 80 -17.203 -17.904 28.784 1.00 27.28 C ANISOU 401 CG1 VAL A 80 3518 3466 3381 -183 656 -247 C ATOM 402 CG2 VAL A 80 -18.890 -19.618 28.006 1.00 24.37 C ANISOU 402 CG2 VAL A 80 3097 2735 3425 -126 209 319 C ATOM 403 N GLY A 81 -14.587 -20.674 29.966 1.00 28.30 N ANISOU 403 N GLY A 81 3668 3605 3476 -173 670 450 N ATOM 404 CA GLY A 81 -13.545 -20.737 30.980 1.00 29.12 C ANISOU 404 CA GLY A 81 3615 3574 3876 -343 196 -380 C ATOM 405 C GLY A 81 -12.458 -19.699 30.775 1.00 31.05 C ANISOU 405 C GLY A 81 3792 3647 4356 -419 -3 187 C ATOM 406 O GLY A 81 -11.402 -19.759 31.393 1.00 31.36 O ANISOU 406 O GLY A 81 3547 3881 4487 -559 147 209 O ATOM 407 N ASP A 82 -12.734 -18.740 29.907 1.00 33.84 N ANISOU 407 N ASP A 82 4503 4086 4269 -430 383 473 N ATOM 408 CA ASP A 82 -11.844 -17.607 29.687 1.00 31.76 C ANISOU 408 CA ASP A 82 4258 3753 4056 -3 749 312 C ATOM 409 C ASP A 82 -12.541 -16.368 30.223 1.00 26.59 C ANISOU 409 C ASP A 82 3596 3223 3281 -522 397 441 C ATOM 410 O ASP A 82 -13.588 -15.972 29.688 1.00 29.02 O ANISOU 410 O ASP A 82 3553 3643 3828 -105 512 486 O ATOM 411 CB ASP A 82 -11.588 -17.478 28.189 1.00 30.72 C ANISOU 411 CB ASP A 82 4327 3478 3865 139 1036 -186 C ATOM 412 CG ASP A 82 -10.782 -16.242 27.817 1.00 32.05 C ANISOU 412 CG ASP A 82 4200 4015 3962 -208 382 188 C ATOM 413 OD1 ASP A 82 -10.365 -15.431 28.682 1.00 35.08 O ANISOU 413 OD1 ASP A 82 4639 4323 4367 -1037 333 312 O ATOM 414 OD2 ASP A 82 -10.575 -16.092 26.610 1.00 33.34 O ANISOU 414 OD2 ASP A 82 4452 4083 4130 -471 565 420 O ATOM 415 N PRO A 83 -11.979 -15.757 31.285 1.00 28.82 N ANISOU 415 N PRO A 83 3667 3714 3568 -472 192 318 N ATOM 416 CA PRO A 83 -12.603 -14.568 31.879 1.00 33.53 C ANISOU 416 CA PRO A 83 4185 4272 4281 122 565 279 C ATOM 417 C PRO A 83 -12.850 -13.431 30.884 1.00 35.20 C ANISOU 417 C PRO A 83 4401 4003 4968 14 720 512 C ATOM 418 O PRO A 83 -13.732 -12.606 31.127 1.00 32.79 O ANISOU 418 O PRO A 83 3705 4289 4463 -409 1178 320 O ATOM 419 CB PRO A 83 -11.607 -14.127 32.967 1.00 36.38 C ANISOU 419 CB PRO A 83 4971 3804 5046 -309 260 98 C ATOM 420 CG PRO A 83 -10.729 -15.305 33.217 1.00 38.94 C ANISOU 420 CG PRO A 83 5090 5345 4360 509 -215 470 C ATOM 421 CD PRO A 83 -10.726 -16.137 31.964 1.00 36.20 C ANISOU 421 CD PRO A 83 4484 4486 4784 -29 -558 452 C ATOM 422 N HIS A 84 -12.091 -13.376 29.784 1.00 37.41 N ANISOU 422 N HIS A 84 5559 4526 4129 15 597 236 N ATOM 423 CA HIS A 84 -12.267 -12.289 28.802 1.00 32.05 C ANISOU 423 CA HIS A 84 3877 4194 4104 263 435 -80 C ATOM 424 C HIS A 84 -13.566 -12.425 28.109 1.00 32.01 C ANISOU 424 C HIS A 84 4109 4360 3693 -64 411 177 C ATOM 425 O HIS A 84 -14.090 -11.455 27.567 1.00 39.20 O ANISOU 425 O HIS A 84 5253 3989 5652 -196 582 925 O ATOM 426 CB HIS A 84 -11.116 -12.220 27.788 1.00 32.86 C ANISOU 426 CB HIS A 84 3984 4443 4056 -614 369 486 C ATOM 427 CG HIS A 84 -9.806 -11.798 28.407 1.00 32.23 C ANISOU 427 CG HIS A 84 4019 4692 3533 -106 254 106 C ATOM 428 ND1 HIS A 84 -9.543 -10.518 28.747 1.00 35.37 N ANISOU 428 ND1 HIS A 84 4467 4283 4687 -448 653 1069 N ATOM 429 CD2 HIS A 84 -8.698 -12.542 28.792 1.00 32.63 C ANISOU 429 CD2 HIS A 84 3412 4262 4724 -142 1070 593 C ATOM 430 CE1 HIS A 84 -8.318 -10.444 29.310 1.00 36.26 C ANISOU 430 CE1 HIS A 84 4444 4564 4767 -208 408 594 C ATOM 431 NE2 HIS A 84 -7.802 -11.681 29.340 1.00 40.84 N ANISOU 431 NE2 HIS A 84 5296 4403 5816 -78 541 -681 N ATOM 432 N GLU A 85 -14.125 -13.629 28.144 1.00 30.38 N ANISOU 432 N GLU A 85 4076 4121 3344 97 213 -33 N ATOM 433 CA GLU A 85 -15.400 -13.869 27.484 1.00 28.92 C ANISOU 433 CA GLU A 85 3749 3718 3518 -233 327 65 C ATOM 434 C GLU A 85 -16.603 -13.993 28.422 1.00 29.59 C ANISOU 434 C GLU A 85 3550 3978 3712 84 267 -329 C ATOM 435 O GLU A 85 -17.678 -14.373 27.975 1.00 29.69 O ANISOU 435 O GLU A 85 3634 3759 3888 -20 333 0 O ATOM 436 CB GLU A 85 -15.294 -15.095 26.576 1.00 32.49 C ANISOU 436 CB GLU A 85 4030 4124 4187 122 668 -359 C ATOM 437 CG GLU A 85 -14.154 -14.992 25.556 1.00 30.73 C ANISOU 437 CG GLU A 85 4273 3637 3765 362 571 -103 C ATOM 438 CD GLU A 85 -14.443 -14.024 24.429 1.00 35.17 C ANISOU 438 CD GLU A 85 4897 4520 3945 156 122 204 C ATOM 439 OE1 GLU A 85 -15.597 -13.550 24.294 1.00 36.69 O ANISOU 439 OE1 GLU A 85 4714 4757 4467 -241 295 363 O ATOM 440 OE2 GLU A 85 -13.503 -13.738 23.667 1.00 40.21 O ANISOU 440 OE2 GLU A 85 5124 5024 5128 161 267 1321 O ATOM 441 N HIS A 86 -16.436 -13.671 29.704 1.00 28.24 N ANISOU 441 N HIS A 86 3901 3172 3657 139 377 -278 N ATOM 442 CA HIS A 86 -17.568 -13.710 30.643 1.00 28.97 C ANISOU 442 CA HIS A 86 3648 3728 3629 -294 135 -204 C ATOM 443 C HIS A 86 -18.829 -13.077 30.151 1.00 28.94 C ANISOU 443 C HIS A 86 3940 3451 3605 6 167 -472 C ATOM 444 O HIS A 86 -19.920 -13.639 30.301 1.00 31.52 O ANISOU 444 O HIS A 86 4286 3190 4499 -112 422 -63 O ATOM 445 CB HIS A 86 -17.203 -13.071 31.968 1.00 27.77 C ANISOU 445 CB HIS A 86 3983 3064 3504 -8 10 160 C ATOM 446 CG HIS A 86 -16.411 -13.972 32.852 1.00 26.67 C ANISOU 446 CG HIS A 86 3225 3574 3335 235 144 37 C ATOM 447 ND1 HIS A 86 -15.878 -13.564 34.019 1.00 25.68 N ANISOU 447 ND1 HIS A 86 2703 3428 3625 -397 141 62 N ATOM 448 CD2 HIS A 86 -16.057 -15.306 32.696 1.00 22.60 C ANISOU 448 CD2 HIS A 86 2953 2948 2685 -338 375 533 C ATOM 449 CE1 HIS A 86 -15.226 -14.588 34.588 1.00 23.04 C ANISOU 449 CE1 HIS A 86 2905 2997 2852 -420 340 13 C ATOM 450 NE2 HIS A 86 -15.333 -15.655 33.771 1.00 23.42 N ANISOU 450 NE2 HIS A 86 2763 3001 3131 -166 -176 -105 N ATOM 451 N SER A 87 -18.713 -11.887 29.579 1.00 32.50 N ANISOU 451 N SER A 87 4158 3937 4250 -299 561 119 N ATOM 452 CA SER A 87 -19.905 -11.148 29.195 1.00 33.33 C ANISOU 452 CA SER A 87 4346 3981 4336 -308 -31 -53 C ATOM 453 C SER A 87 -20.760 -11.932 28.215 1.00 28.17 C ANISOU 453 C SER A 87 3736 3762 3204 -150 368 415 C ATOM 454 O SER A 87 -21.960 -11.711 28.149 1.00 27.30 O ANISOU 454 O SER A 87 3758 3559 3055 144 118 183 O ATOM 455 CB SER A 87 -19.551 -9.768 28.631 1.00 43.45 C ANISOU 455 CB SER A 87 6578 4542 5389 275 1061 1121 C ATOM 456 OG SER A 87 -18.914 -9.890 27.379 1.00 41.03 O ANISOU 456 OG SER A 87 6043 4323 5222 -896 729 942 O ATOM 457 N ARG A 88 -20.153 -12.848 27.458 1.00 28.16 N ANISOU 457 N ARG A 88 4281 2947 3471 -101 -80 387 N ATOM 458 CA ARG A 88 -20.927 -13.677 26.521 1.00 30.17 C ANISOU 458 CA ARG A 88 4258 3826 3378 -395 330 44 C ATOM 459 C ARG A 88 -21.842 -14.707 27.231 1.00 27.53 C ANISOU 459 C ARG A 88 3287 3661 3512 6 125 -74 C ATOM 460 O ARG A 88 -22.790 -15.203 26.644 1.00 31.50 O ANISOU 460 O ARG A 88 3958 3937 4070 -659 128 -75 O ATOM 461 CB ARG A 88 -19.996 -14.388 25.522 1.00 31.23 C ANISOU 461 CB ARG A 88 4194 3329 4343 -83 427 32 C ATOM 462 CG ARG A 88 -19.121 -13.459 24.679 1.00 34.41 C ANISOU 462 CG ARG A 88 4378 4685 4008 -290 361 544 C ATOM 463 CD ARG A 88 -19.977 -12.515 23.833 1.00 33.51 C ANISOU 463 CD ARG A 88 4720 4052 3959 -206 159 3 C ATOM 464 NE ARG A 88 -20.749 -13.284 22.868 1.00 31.25 N ANISOU 464 NE ARG A 88 3964 4312 3595 -227 139 680 N ATOM 465 CZ ARG A 88 -22.007 -13.041 22.517 1.00 31.48 C ANISOU 465 CZ ARG A 88 4240 4329 3390 175 389 654 C ATOM 466 NH1 ARG A 88 -22.684 -12.025 23.040 1.00 33.73 N ANISOU 466 NH1 ARG A 88 5494 3541 3780 212 519 829 N ATOM 467 NH2 ARG A 88 -22.600 -13.836 21.641 1.00 35.80 N ANISOU 467 NH2 ARG A 88 4545 4731 4327 -243 620 145 N ATOM 468 N PHE A 89 -21.549 -15.030 28.488 1.00 27.91 N ANISOU 468 N PHE A 89 3575 3479 3547 373 713 413 N ATOM 469 CA PHE A 89 -22.405 -15.920 29.262 1.00 25.86 C ANISOU 469 CA PHE A 89 3487 3142 3194 -82 11 154 C ATOM 470 C PHE A 89 -23.435 -15.074 30.015 1.00 27.45 C ANISOU 470 C PHE A 89 3694 3344 3392 32 -94 122 C ATOM 471 O PHE A 89 -24.631 -15.385 30.042 1.00 31.44 O ANISOU 471 O PHE A 89 3958 3792 4193 -325 -584 130 O ATOM 472 CB PHE A 89 -21.571 -16.768 30.242 1.00 25.70 C ANISOU 472 CB PHE A 89 2885 3556 3321 260 110 4 C ATOM 473 CG PHE A 89 -22.405 -17.596 31.197 1.00 28.16 C ANISOU 473 CG PHE A 89 3788 3594 3317 126 -33 365 C ATOM 474 CD1 PHE A 89 -22.855 -18.863 30.833 1.00 33.00 C ANISOU 474 CD1 PHE A 89 4855 3782 3901 -3 345 -127 C ATOM 475 CD2 PHE A 89 -22.761 -17.098 32.457 1.00 25.93 C ANISOU 475 CD2 PHE A 89 3177 3389 3286 -116 -294 41 C ATOM 476 CE1 PHE A 89 -23.630 -19.628 31.709 1.00 31.95 C ANISOU 476 CE1 PHE A 89 3965 4117 4055 330 440 -77 C ATOM 477 CE2 PHE A 89 -23.538 -17.853 33.330 1.00 26.21 C ANISOU 477 CE2 PHE A 89 4182 3526 2250 49 -344 68 C ATOM 478 CZ PHE A 89 -23.974 -19.121 32.957 1.00 30.83 C ANISOU 478 CZ PHE A 89 4851 3755 3107 -619 -210 247 C ATOM 479 N PHE A 90 -22.961 -13.991 30.625 1.00 28.03 N ANISOU 479 N PHE A 90 3896 3179 3572 26 40 3 N ATOM 480 CA PHE A 90 -23.800 -13.211 31.530 1.00 28.29 C ANISOU 480 CA PHE A 90 3930 3644 3174 -8 -385 -489 C ATOM 481 C PHE A 90 -24.751 -12.221 30.883 1.00 29.43 C ANISOU 481 C PHE A 90 3489 3847 3845 149 207 9 C ATOM 482 O PHE A 90 -25.789 -11.923 31.462 1.00 25.81 O ANISOU 482 O PHE A 90 3440 3126 3240 -323 408 211 O ATOM 483 CB PHE A 90 -22.942 -12.514 32.596 1.00 23.65 C ANISOU 483 CB PHE A 90 2824 3129 3031 -401 179 -43 C ATOM 484 CG PHE A 90 -22.274 -13.475 33.517 1.00 26.36 C ANISOU 484 CG PHE A 90 3127 3338 3548 -190 -92 102 C ATOM 485 CD1 PHE A 90 -23.000 -14.107 34.525 1.00 25.88 C ANISOU 485 CD1 PHE A 90 2608 3651 3574 -120 -41 211 C ATOM 486 CD2 PHE A 90 -20.931 -13.789 33.358 1.00 25.48 C ANISOU 486 CD2 PHE A 90 3112 3281 3288 -34 -274 -373 C ATOM 487 CE1 PHE A 90 -22.396 -15.037 35.359 1.00 25.56 C ANISOU 487 CE1 PHE A 90 3009 3573 3129 -311 -104 240 C ATOM 488 CE2 PHE A 90 -20.320 -14.705 34.199 1.00 24.29 C ANISOU 488 CE2 PHE A 90 2943 3089 3197 -70 125 -169 C ATOM 489 CZ PHE A 90 -21.051 -15.331 35.198 1.00 27.41 C ANISOU 489 CZ PHE A 90 3421 3495 3498 -3 289 230 C ATOM 490 N LEU A 91 -24.420 -11.708 29.698 1.00 29.97 N ANISOU 490 N LEU A 91 4283 3352 3751 -244 103 -42 N ATOM 491 CA LEU A 91 -25.209 -10.595 29.141 1.00 29.23 C ANISOU 491 CA LEU A 91 3693 3862 3549 -170 -3 200 C ATOM 492 C LEU A 91 -26.350 -10.963 28.168 1.00 26.41 C ANISOU 492 C LEU A 91 3412 3467 3153 -119 395 -35 C ATOM 493 O LEU A 91 -27.339 -10.230 28.075 1.00 29.21 O ANISOU 493 O LEU A 91 3954 3444 3697 204 369 -283 O ATOM 494 CB LEU A 91 -24.292 -9.509 28.542 1.00 31.02 C ANISOU 494 CB LEU A 91 4093 3602 4091 -224 322 42 C ATOM 495 CG LEU A 91 -23.267 -8.835 29.463 1.00 30.43 C ANISOU 495 CG LEU A 91 4326 3469 3764 -412 504 138 C ATOM 496 CD1 LEU A 91 -22.568 -7.663 28.757 1.00 32.81 C ANISOU 496 CD1 LEU A 91 4441 3672 4352 -595 905 218 C ATOM 497 CD2 LEU A 91 -23.967 -8.343 30.715 1.00 33.62 C ANISOU 497 CD2 LEU A 91 5117 4237 3418 -388 622 236 C ATOM 498 N PRO A 92 -26.229 -12.088 27.432 1.00 24.37 N ANISOU 498 N PRO A 92 3196 2995 3066 -227 157 239 N ATOM 499 CA PRO A 92 -27.332 -12.367 26.505 1.00 25.42 C ANISOU 499 CA PRO A 92 3504 3230 2924 -284 -18 36 C ATOM 500 C PRO A 92 -28.691 -12.503 27.195 1.00 30.16 C ANISOU 500 C PRO A 92 3523 4154 3781 16 47 253 C ATOM 501 O PRO A 92 -28.768 -13.058 28.287 1.00 32.25 O ANISOU 501 O PRO A 92 3960 4180 4110 -884 466 379 O ATOM 502 CB PRO A 92 -26.913 -13.690 25.871 1.00 26.52 C ANISOU 502 CB PRO A 92 3467 3213 3395 32 -220 114 C ATOM 503 CG PRO A 92 -25.425 -13.600 25.853 1.00 29.30 C ANISOU 503 CG PRO A 92 3696 3543 3894 -252 529 -741 C ATOM 504 CD PRO A 92 -25.064 -12.953 27.166 1.00 27.10 C ANISOU 504 CD PRO A 92 3421 3595 3279 7 169 -15 C ATOM 505 N ARG A 93 -29.741 -11.990 26.558 1.00 26.35 N ANISOU 505 N ARG A 93 3621 2924 3465 -431 -153 348 N ATOM 506 CA ARG A 93 -31.106 -12.060 27.086 1.00 33.79 C ANISOU 506 CA ARG A 93 4203 4166 4470 -145 427 483 C ATOM 507 C ARG A 93 -31.588 -13.500 27.318 1.00 34.46 C ANISOU 507 C ARG A 93 4384 3942 4766 47 395 523 C ATOM 508 O ARG A 93 -31.058 -14.453 26.727 1.00 30.12 O ANISOU 508 O ARG A 93 3425 3903 4115 -417 264 602 O ATOM 509 CB ARG A 93 -32.084 -11.371 26.119 1.00 37.21 C ANISOU 509 CB ARG A 93 5479 3751 4907 -444 -504 437 C ATOM 510 CG ARG A 93 -32.104 -12.001 24.727 1.00 45.35 C ANISOU 510 CG ARG A 93 5837 5946 5447 240 123 -521 C ATOM 511 CD ARG A 93 -33.094 -11.344 23.770 1.00 56.02 C ANISOU 511 CD ARG A 93 7672 6958 6654 1021 -400 991 C ATOM 512 NE ARG A 93 -32.682 -9.993 23.405 1.00 70.06 N ANISOU 512 NE ARG A 93 10539 7974 8106 -316 -653 1810 N ATOM 513 CZ ARG A 93 -33.252 -8.881 23.877 1.00 76.98 C ANISOU 513 CZ ARG A 93 10690 10803 7755 1394 985 737 C ATOM 514 NH1 ARG A 93 -34.276 -8.954 24.729 1.00 84.54 N ANISOU 514 NH1 ARG A 93 8774 12677 10667 1756 -554 3053 N ATOM 515 NH2 ARG A 93 -32.800 -7.693 23.494 1.00 86.11 N ANISOU 515 NH2 ARG A 93 14919 9500 8296 636 811 -1561 N ATOM 516 N ASN A 94 -32.621 -13.627 28.150 1.00 35.17 N ANISOU 516 N ASN A 94 4672 4305 4384 371 530 399 N ATOM 517 CA ASN A 94 -33.296 -14.904 28.436 1.00 40.91 C ANISOU 517 CA ASN A 94 5073 4929 5542 -437 531 461 C ATOM 518 C ASN A 94 -33.752 -15.711 27.223 1.00 40.71 C ANISOU 518 C ASN A 94 4536 5348 5584 -136 356 300 C ATOM 519 O ASN A 94 -33.733 -16.940 27.264 1.00 45.16 O ANISOU 519 O ASN A 94 6101 5475 5581 -452 539 913 O ATOM 520 CB ASN A 94 -34.501 -14.673 29.354 1.00 47.80 C ANISOU 520 CB ASN A 94 5216 6356 6589 76 971 807 C ATOM 521 CG ASN A 94 -34.159 -14.829 30.817 1.00 60.01 C ANISOU 521 CG ASN A 94 7489 8645 6665 -252 853 1253 C ATOM 522 OD1 ASN A 94 -33.422 -15.740 31.205 1.00 58.88 O ANISOU 522 OD1 ASN A 94 6620 7702 8049 750 2578 -618 O ATOM 523 ND2 ASN A 94 -34.709 -13.946 31.646 1.00 66.79 N ANISOU 523 ND2 ASN A 94 8838 5109 11429 -305 464 283 N ATOM 524 N GLU A 95 -34.173 -15.025 26.158 1.00 49.20 N ANISOU 524 N GLU A 95 6146 5746 6800 823 -915 390 N ATOM 525 CA GLU A 95 -34.571 -15.686 24.913 1.00 45.16 C ANISOU 525 CA GLU A 95 6152 4531 6474 -26 334 32 C ATOM 526 C GLU A 95 -33.396 -16.425 24.314 1.00 38.72 C ANISOU 526 C GLU A 95 5275 4059 5376 -561 -106 269 C ATOM 527 O GLU A 95 -33.559 -17.293 23.475 1.00 40.30 O ANISOU 527 O GLU A 95 5596 5388 4328 -600 -1435 126 O ATOM 528 CB GLU A 95 -35.064 -14.674 23.874 1.00 48.46 C ANISOU 528 CB GLU A 95 5764 6250 6396 -266 -808 379 C ATOM 529 CG GLU A 95 -36.468 -14.142 24.103 1.00 58.38 C ANISOU 529 CG GLU A 95 5791 7640 8749 -599 -438 -1187 C ATOM 530 CD GLU A 95 -36.521 -13.008 25.114 1.00 64.20 C ANISOU 530 CD GLU A 95 7724 8234 8432 -843 -639 -1661 C ATOM 531 OE1 GLU A 95 -35.453 -12.527 25.556 1.00 56.02 O ANISOU 531 OE1 GLU A 95 6462 6505 8318 -78 258 -800 O ATOM 532 OE2 GLU A 95 -37.644 -12.591 25.465 1.00 76.10 O ANISOU 532 OE2 GLU A 95 9810 8272 10833 1041 1291 -435 O ATOM 533 N VAL A 96 -32.194 -16.068 24.729 1.00 38.50 N ANISOU 533 N VAL A 96 5167 4303 5155 -101 -31 1182 N ATOM 534 CA VAL A 96 -31.015 -16.644 24.112 1.00 37.81 C ANISOU 534 CA VAL A 96 4317 4670 5379 -274 -241 554 C ATOM 535 C VAL A 96 -30.340 -17.646 25.050 1.00 36.71 C ANISOU 535 C VAL A 96 4866 4522 4560 3 27 145 C ATOM 536 O VAL A 96 -30.017 -18.753 24.637 1.00 37.67 O ANISOU 536 O VAL A 96 5646 4237 4429 -755 -476 25 O ATOM 537 CB VAL A 96 -30.045 -15.546 23.634 1.00 36.49 C ANISOU 537 CB VAL A 96 4802 4285 4775 118 293 980 C ATOM 538 CG1 VAL A 96 -28.751 -16.156 23.126 1.00 34.84 C ANISOU 538 CG1 VAL A 96 4109 4757 4369 -272 -497 544 C ATOM 539 CG2 VAL A 96 -30.703 -14.727 22.538 1.00 36.20 C ANISOU 539 CG2 VAL A 96 4724 4055 4973 -1099 -235 1368 C ATOM 540 N LEU A 97 -30.131 -17.252 26.304 1.00 34.02 N ANISOU 540 N LEU A 97 4640 4371 3913 -624 393 695 N ATOM 541 CA LEU A 97 -29.577 -18.148 27.312 1.00 29.43 C ANISOU 541 CA LEU A 97 3680 3713 3788 -217 164 29 C ATOM 542 C LEU A 97 -30.510 -18.177 28.517 1.00 32.05 C ANISOU 542 C LEU A 97 4229 4019 3926 -179 494 259 C ATOM 543 O LEU A 97 -30.680 -17.170 29.200 1.00 32.29 O ANISOU 543 O LEU A 97 4110 4105 4050 -702 551 204 O ATOM 544 CB LEU A 97 -28.182 -17.705 27.735 1.00 27.86 C ANISOU 544 CB LEU A 97 3701 3923 2961 -406 158 204 C ATOM 545 CG LEU A 97 -27.104 -17.611 26.648 1.00 27.61 C ANISOU 545 CG LEU A 97 3397 3593 3498 -67 283 -87 C ATOM 546 CD1 LEU A 97 -25.774 -17.216 27.274 1.00 26.14 C ANISOU 546 CD1 LEU A 97 3581 3611 2739 -252 283 370 C ATOM 547 CD2 LEU A 97 -26.963 -18.916 25.864 1.00 27.65 C ANISOU 547 CD2 LEU A 97 3276 3649 3578 -59 417 -140 C ATOM 548 N SER A 98 -31.109 -19.335 28.772 1.00 30.89 N ANISOU 548 N SER A 98 4051 3817 3867 -168 254 -83 N ATOM 549 CA SER A 98 -32.152 -19.448 29.801 1.00 34.24 C ANISOU 549 CA SER A 98 3745 5009 4254 -568 271 794 C ATOM 550 C SER A 98 -31.794 -20.462 30.881 1.00 29.97 C ANISOU 550 C SER A 98 3410 3905 4071 -346 399 129 C ATOM 551 O SER A 98 -31.495 -21.611 30.562 1.00 30.65 O ANISOU 551 O SER A 98 3940 3593 4111 -1017 315 420 O ATOM 552 CB SER A 98 -33.495 -19.842 29.182 1.00 35.61 C ANISOU 552 CB SER A 98 3935 5371 4225 -11 -344 831 C ATOM 553 OG SER A 98 -34.494 -19.880 30.210 1.00 39.41 O ANISOU 553 OG SER A 98 3719 5688 5563 -478 275 1585 O ATOM 554 N PRO A 99 -31.826 -20.037 32.162 1.00 34.41 N ANISOU 554 N PRO A 99 5007 3856 4210 -268 216 147 N ATOM 555 CA PRO A 99 -31.557 -20.945 33.272 1.00 31.77 C ANISOU 555 CA PRO A 99 3943 4028 4099 29 -214 -112 C ATOM 556 C PRO A 99 -32.772 -21.790 33.651 1.00 32.60 C ANISOU 556 C PRO A 99 4061 4221 4103 -44 -237 65 C ATOM 557 O PRO A 99 -32.622 -22.748 34.392 1.00 31.82 O ANISOU 557 O PRO A 99 3664 4082 4344 -430 -241 12 O ATOM 558 CB PRO A 99 -31.182 -20.003 34.427 1.00 32.74 C ANISOU 558 CB PRO A 99 4154 3905 4381 226 -442 -314 C ATOM 559 CG PRO A 99 -31.867 -18.726 34.108 1.00 34.47 C ANISOU 559 CG PRO A 99 4726 3871 4498 858 359 -812 C ATOM 560 CD PRO A 99 -32.013 -18.644 32.616 1.00 36.87 C ANISOU 560 CD PRO A 99 4864 4384 4759 671 189 -296 C ATOM 561 N ARG A 100 -33.953 -21.441 33.141 1.00 32.58 N ANISOU 561 N ARG A 100 4070 4325 3983 168 -315 -198 N ATOM 562 CA ARG A 100 -35.203 -22.113 33.530 1.00 38.43 C ANISOU 562 CA ARG A 100 4968 4642 4992 59 467 610 C ATOM 563 C ARG A 100 -35.183 -23.640 33.483 1.00 34.65 C ANISOU 563 C ARG A 100 3828 4679 4657 -433 140 -132 C ATOM 564 O ARG A 100 -35.639 -24.290 34.425 1.00 34.11 O ANISOU 564 O ARG A 100 4552 4513 3893 436 -158 -10 O ATOM 565 CB ARG A 100 -36.380 -21.616 32.694 1.00 47.04 C ANISOU 565 CB ARG A 100 4896 7621 5353 -218 113 923 C ATOM 566 CG ARG A 100 -37.684 -22.292 33.073 1.00 54.48 C ANISOU 566 CG ARG A 100 6348 6284 8067 -1249 1080 298 C ATOM 567 CD ARG A 100 -38.706 -22.224 31.954 1.00 75.57 C ANISOU 567 CD ARG A 100 7630 12061 9020 -4 307 2215 C ATOM 568 NE ARG A 100 -40.056 -22.093 32.491 1.00 60.45 N ANISOU 568 NE ARG A 100 8329 8725 5913 371 336 1816 N ATOM 569 CZ ARG A 100 -40.748 -20.960 32.498 1.00 68.63 C ANISOU 569 CZ ARG A 100 9213 7580 9282 -137 -645 -1048 C ATOM 570 NH1 ARG A 100 -40.225 -19.853 31.985 1.00 79.92 N ANISOU 570 NH1 ARG A 100 10188 10195 9980 -1405 4180 -577 N ATOM 571 NH2 ARG A 100 -41.967 -20.934 33.015 1.00 76.13 N ANISOU 571 NH2 ARG A 100 8365 9065 11493 -1488 -497 -682 N ATOM 572 N GLU A 101 -34.692 -24.210 32.385 1.00 35.98 N ANISOU 572 N GLU A 101 4886 5061 3723 -311 23 320 N ATOM 573 CA GLU A 101 -34.666 -25.671 32.227 1.00 40.21 C ANISOU 573 CA GLU A 101 5466 4950 4860 -502 -274 47 C ATOM 574 C GLU A 101 -33.670 -26.315 33.181 1.00 38.31 C ANISOU 574 C GLU A 101 5027 4883 4647 -254 -73 -452 C ATOM 575 O GLU A 101 -33.868 -27.441 33.645 1.00 38.17 O ANISOU 575 O GLU A 101 5534 4671 4296 -619 -312 -860 O ATOM 576 CB GLU A 101 -34.360 -26.083 30.779 1.00 42.30 C ANISOU 576 CB GLU A 101 5866 5163 5041 -240 239 -105 C ATOM 577 CG GLU A 101 -35.461 -25.735 29.783 1.00 53.89 C ANISOU 577 CG GLU A 101 6580 6881 7014 211 -1009 -132 C ATOM 578 CD GLU A 101 -35.196 -24.447 29.002 1.00 75.65 C ANISOU 578 CD GLU A 101 10777 8753 9214 -1968 -1232 1691 C ATOM 579 OE1 GLU A 101 -34.498 -23.525 29.513 1.00 55.68 O ANISOU 579 OE1 GLU A 101 7330 7257 6566 -234 867 2311 O ATOM 580 OE2 GLU A 101 -35.701 -24.356 27.858 1.00 90.85 O ANISOU 580 OE2 GLU A 101 11699 13296 9522 -2049 -1540 -51 O ATOM 581 N VAL A 102 -32.596 -25.589 33.473 1.00 34.92 N ANISOU 581 N VAL A 102 4504 4189 4574 -42 294 232 N ATOM 582 CA VAL A 102 -31.655 -26.016 34.490 1.00 33.34 C ANISOU 582 CA VAL A 102 4346 4269 4049 15 267 -134 C ATOM 583 C VAL A 102 -32.364 -26.162 35.834 1.00 31.74 C ANISOU 583 C VAL A 102 3928 3940 4189 309 396 36 C ATOM 584 O VAL A 102 -32.069 -27.069 36.604 1.00 32.36 O ANISOU 584 O VAL A 102 4229 3782 4281 -58 737 267 O ATOM 585 CB VAL A 102 -30.486 -25.029 34.612 1.00 34.32 C ANISOU 585 CB VAL A 102 4198 4832 4008 -87 -63 318 C ATOM 586 CG1 VAL A 102 -29.563 -25.423 35.759 1.00 31.09 C ANISOU 586 CG1 VAL A 102 4326 3442 4044 95 164 680 C ATOM 587 CG2 VAL A 102 -29.718 -24.973 33.295 1.00 39.20 C ANISOU 587 CG2 VAL A 102 4291 5947 4653 17 439 827 C ATOM 588 N TYR A 103 -33.301 -25.268 36.115 1.00 30.09 N ANISOU 588 N TYR A 103 3372 3794 4267 17 498 402 N ATOM 589 CA TYR A 103 -33.969 -25.278 37.421 1.00 31.81 C ANISOU 589 CA TYR A 103 4184 3941 3960 90 326 -242 C ATOM 590 C TYR A 103 -35.222 -26.158 37.502 1.00 30.47 C ANISOU 590 C TYR A 103 4164 3530 3882 87 399 -172 C ATOM 591 O TYR A 103 -35.941 -26.122 38.503 1.00 28.61 O ANISOU 591 O TYR A 103 4004 3344 3520 33 94 -260 O ATOM 592 CB TYR A 103 -34.289 -23.845 37.864 1.00 33.10 C ANISOU 592 CB TYR A 103 4466 4052 4056 50 240 -478 C ATOM 593 CG TYR A 103 -33.136 -23.196 38.565 1.00 36.08 C ANISOU 593 CG TYR A 103 4669 4349 4687 -241 70 -441 C ATOM 594 CD1 TYR A 103 -32.143 -22.529 37.846 1.00 36.33 C ANISOU 594 CD1 TYR A 103 4401 5099 4300 132 313 -288 C ATOM 595 CD2 TYR A 103 -33.013 -23.266 39.954 1.00 36.45 C ANISOU 595 CD2 TYR A 103 4244 4998 4604 -104 -100 -126 C ATOM 596 CE1 TYR A 103 -31.067 -21.940 38.490 1.00 34.46 C ANISOU 596 CE1 TYR A 103 4777 4094 4221 -463 641 -295 C ATOM 597 CE2 TYR A 103 -31.942 -22.673 40.608 1.00 34.94 C ANISOU 597 CE2 TYR A 103 4474 4082 4719 -250 55 -328 C ATOM 598 CZ TYR A 103 -30.966 -22.014 39.873 1.00 35.01 C ANISOU 598 CZ TYR A 103 4571 4616 4115 -364 107 -185 C ATOM 599 OH TYR A 103 -29.888 -21.427 40.524 1.00 32.04 O ANISOU 599 OH TYR A 103 3750 4264 4159 -136 485 -237 O ATOM 600 N SER A 104 -35.486 -26.958 36.469 1.00 29.71 N ANISOU 600 N SER A 104 4087 3480 3722 55 121 -76 N ATOM 601 CA SER A 104 -36.669 -27.843 36.486 1.00 31.96 C ANISOU 601 CA SER A 104 4414 3673 4056 -220 344 -140 C ATOM 602 C SER A 104 -36.751 -28.687 37.765 1.00 28.28 C ANISOU 602 C SER A 104 3583 3520 3642 -165 120 -374 C ATOM 603 O SER A 104 -37.833 -28.857 38.343 1.00 27.09 O ANISOU 603 O SER A 104 3730 3150 3410 -560 112 28 O ATOM 604 CB SER A 104 -36.701 -28.760 35.255 1.00 38.80 C ANISOU 604 CB SER A 104 5943 4925 3873 -478 -384 -384 C ATOM 605 OG SER A 104 -37.017 -28.026 34.097 1.00 39.54 O ANISOU 605 OG SER A 104 5061 4679 5280 57 -675 -61 O ATOM 606 N PHE A 105 -35.608 -29.196 38.221 1.00 29.95 N ANISOU 606 N PHE A 105 4213 3249 3917 77 -204 -33 N ATOM 607 CA PHE A 105 -35.593 -30.046 39.419 1.00 28.47 C ANISOU 607 CA PHE A 105 3786 3402 3628 -223 -127 -7 C ATOM 608 C PHE A 105 -36.017 -29.315 40.689 1.00 31.41 C ANISOU 608 C PHE A 105 4263 3908 3762 38 281 104 C ATOM 609 O PHE A 105 -36.282 -29.948 41.706 1.00 31.97 O ANISOU 609 O PHE A 105 3878 3835 4430 194 557 472 O ATOM 610 CB PHE A 105 -34.233 -30.736 39.608 1.00 28.58 C ANISOU 610 CB PHE A 105 3702 3770 3388 -385 78 40 C ATOM 611 CG PHE A 105 -33.175 -29.853 40.191 1.00 29.64 C ANISOU 611 CG PHE A 105 3862 3850 3548 -497 199 -190 C ATOM 612 CD1 PHE A 105 -32.528 -28.915 39.401 1.00 29.51 C ANISOU 612 CD1 PHE A 105 3907 3633 3671 -56 68 165 C ATOM 613 CD2 PHE A 105 -32.819 -29.964 41.532 1.00 30.30 C ANISOU 613 CD2 PHE A 105 3264 4191 4056 -311 45 471 C ATOM 614 CE1 PHE A 105 -31.549 -28.087 39.945 1.00 33.90 C ANISOU 614 CE1 PHE A 105 4160 4768 3951 -911 -15 271 C ATOM 615 CE2 PHE A 105 -31.841 -29.143 42.082 1.00 32.54 C ANISOU 615 CE2 PHE A 105 4600 4072 3690 -459 44 -428 C ATOM 616 CZ PHE A 105 -31.201 -28.202 41.284 1.00 31.47 C ANISOU 616 CZ PHE A 105 4429 3707 3820 -135 51 -270 C ATOM 617 N MET A 106 -36.087 -27.987 40.647 1.00 33.35 N ANISOU 617 N MET A 106 4699 3860 4110 216 433 58 N ATOM 618 CA MET A 106 -36.459 -27.247 41.857 1.00 30.33 C ANISOU 618 CA MET A 106 4004 3407 4111 -173 535 250 C ATOM 619 C MET A 106 -37.896 -26.755 41.822 1.00 33.31 C ANISOU 619 C MET A 106 3857 4602 4197 -179 -1 -57 C ATOM 620 O MET A 106 -38.353 -26.088 42.758 1.00 33.16 O ANISOU 620 O MET A 106 4643 3634 4320 -583 -44 -153 O ATOM 621 CB MET A 106 -35.520 -26.072 42.106 1.00 28.46 C ANISOU 621 CB MET A 106 3727 3925 3158 -171 62 17 C ATOM 622 CG MET A 106 -34.122 -26.493 42.491 1.00 29.53 C ANISOU 622 CG MET A 106 3886 3670 3663 31 245 178 C ATOM 623 SD MET A 106 -33.169 -25.097 43.085 1.00 36.85 S ANISOU 623 SD MET A 106 4572 4600 4827 -539 -99 116 S ATOM 624 CE MET A 106 -34.072 -24.579 44.541 1.00 45.27 C ANISOU 624 CE MET A 106 4836 7161 5200 -849 627 60 C ATOM 625 N VAL A 107 -38.609 -27.087 40.751 1.00 32.00 N ANISOU 625 N VAL A 107 4171 4132 3855 -210 74 -94 N ATOM 626 CA VAL A 107 -40.017 -26.683 40.617 1.00 34.15 C ANISOU 626 CA VAL A 107 4502 4165 4307 123 -171 27 C ATOM 627 C VAL A 107 -40.876 -27.077 41.824 1.00 34.17 C ANISOU 627 C VAL A 107 4242 4293 4446 40 -251 -136 C ATOM 628 O VAL A 107 -41.720 -26.294 42.258 1.00 33.84 O ANISOU 628 O VAL A 107 3936 4384 4536 -358 -280 -609 O ATOM 629 CB VAL A 107 -40.657 -27.226 39.323 1.00 35.44 C ANISOU 629 CB VAL A 107 4669 4376 4420 -390 105 -377 C ATOM 630 CG1 VAL A 107 -42.176 -27.165 39.404 1.00 37.91 C ANISOU 630 CG1 VAL A 107 4555 4365 5484 -631 -338 -626 C ATOM 631 CG2 VAL A 107 -40.167 -26.444 38.119 1.00 32.59 C ANISOU 631 CG2 VAL A 107 4550 3470 4363 -238 -208 -397 C ATOM 632 N PRO A 108 -40.668 -28.293 42.364 1.00 36.54 N ANISOU 632 N PRO A 108 4992 4091 4799 -410 -145 -70 N ATOM 633 CA PRO A 108 -41.411 -28.734 43.550 1.00 38.36 C ANISOU 633 CA PRO A 108 4808 4907 4859 -535 -118 -221 C ATOM 634 C PRO A 108 -41.113 -27.889 44.796 1.00 36.28 C ANISOU 634 C PRO A 108 4712 4296 4776 -465 344 -69 C ATOM 635 O PRO A 108 -41.940 -27.817 45.697 1.00 37.79 O ANISOU 635 O PRO A 108 4170 5056 5131 -85 295 434 O ATOM 636 CB PRO A 108 -40.923 -30.176 43.753 1.00 39.70 C ANISOU 636 CB PRO A 108 5317 4504 5260 -1117 811 413 C ATOM 637 CG PRO A 108 -40.431 -30.612 42.408 1.00 40.15 C ANISOU 637 CG PRO A 108 5511 4645 5099 -776 195 -164 C ATOM 638 CD PRO A 108 -39.829 -29.374 41.805 1.00 39.03 C ANISOU 638 CD PRO A 108 4772 4433 5622 3 307 332 C ATOM 639 N VAL A 109 -39.937 -27.264 44.840 1.00 33.42 N ANISOU 639 N VAL A 109 3989 4112 4594 18 -316 -75 N ATOM 640 CA VAL A 109 -39.579 -26.344 45.923 1.00 36.39 C ANISOU 640 CA VAL A 109 4407 4585 4835 14 -141 -640 C ATOM 641 C VAL A 109 -40.235 -24.969 45.737 1.00 33.28 C ANISOU 641 C VAL A 109 4113 4532 3997 -82 -142 -306 C ATOM 642 O VAL A 109 -40.950 -24.474 46.626 1.00 32.83 O ANISOU 642 O VAL A 109 3801 4243 4428 -178 385 3 O ATOM 643 CB VAL A 109 -38.044 -26.176 46.017 1.00 36.65 C ANISOU 643 CB VAL A 109 4478 4770 4676 176 -803 -372 C ATOM 644 CG1 VAL A 109 -37.676 -24.871 46.707 1.00 39.03 C ANISOU 644 CG1 VAL A 109 4224 5006 5600 -471 73 -811 C ATOM 645 CG2 VAL A 109 -37.425 -27.353 46.747 1.00 37.04 C ANISOU 645 CG2 VAL A 109 4748 4478 4846 462 281 -36 C ATOM 646 N PHE A 110 -39.973 -24.358 44.585 1.00 32.85 N ANISOU 646 N PHE A 110 3498 4471 4511 -161 140 6 N ATOM 647 CA PHE A 110 -40.496 -23.034 44.255 1.00 34.04 C ANISOU 647 CA PHE A 110 3966 4332 4632 78 45 -355 C ATOM 648 C PHE A 110 -42.007 -23.069 44.174 1.00 33.83 C ANISOU 648 C PHE A 110 4166 4319 4368 -124 31 -246 C ATOM 649 O PHE A 110 -42.687 -22.168 44.651 1.00 32.45 O ANISOU 649 O PHE A 110 3439 4374 4512 -116 -310 -188 O ATOM 650 CB PHE A 110 -39.986 -22.568 42.893 1.00 36.99 C ANISOU 650 CB PHE A 110 4278 4861 4914 72 125 -56 C ATOM 651 CG PHE A 110 -38.500 -22.408 42.813 1.00 42.67 C ANISOU 651 CG PHE A 110 4701 5801 5709 -839 237 -122 C ATOM 652 CD1 PHE A 110 -37.783 -21.873 43.881 1.00 41.79 C ANISOU 652 CD1 PHE A 110 4998 5046 5833 -303 -169 30 C ATOM 653 CD2 PHE A 110 -37.813 -22.765 41.645 1.00 40.48 C ANISOU 653 CD2 PHE A 110 5162 4869 5348 -729 188 659 C ATOM 654 CE1 PHE A 110 -36.406 -21.719 43.801 1.00 42.17 C ANISOU 654 CE1 PHE A 110 5365 4924 5732 -722 857 -1042 C ATOM 655 CE2 PHE A 110 -36.435 -22.601 41.560 1.00 38.02 C ANISOU 655 CE2 PHE A 110 4903 5751 3791 324 -75 1009 C ATOM 656 CZ PHE A 110 -35.735 -22.069 42.640 1.00 33.42 C ANISOU 656 CZ PHE A 110 4253 3168 5276 -26 210 54 C ATOM 657 N GLY A 111 -42.521 -24.116 43.542 1.00 31.21 N ANISOU 657 N GLY A 111 4176 4057 3625 -477 64 359 N ATOM 658 CA GLY A 111 -43.937 -24.200 43.241 1.00 36.34 C ANISOU 658 CA GLY A 111 3987 5165 4652 229 -282 -360 C ATOM 659 C GLY A 111 -44.143 -23.725 41.820 1.00 47.99 C ANISOU 659 C GLY A 111 5314 7271 5647 -1097 -1167 1196 C ATOM 660 O GLY A 111 -43.341 -22.947 41.290 1.00 44.75 O ANISOU 660 O GLY A 111 5579 6017 5407 -850 -650 -326 O ATOM 661 N GLU A 112 -45.215 -24.203 41.198 1.00 48.92 N ANISOU 661 N GLU A 112 6361 5995 6231 -1561 -667 -490 N ATOM 662 CA GLU A 112 -45.577 -23.788 39.854 1.00 49.02 C ANISOU 662 CA GLU A 112 6743 5732 6149 -693 -427 -401 C ATOM 663 C GLU A 112 -45.865 -22.290 39.805 1.00 44.05 C ANISOU 663 C GLU A 112 5596 5976 5163 -371 -203 -448 C ATOM 664 O GLU A 112 -46.530 -21.749 40.687 1.00 41.46 O ANISOU 664 O GLU A 112 4634 5984 5133 -429 -542 -522 O ATOM 665 CB GLU A 112 -46.808 -24.570 39.377 1.00 57.65 C ANISOU 665 CB GLU A 112 6547 8072 7285 -1030 -1705 150 C ATOM 666 CG GLU A 112 -46.683 -26.086 39.494 1.00 82.18 C ANISOU 666 CG GLU A 112 11623 8250 11349 202 -212 -594 C ATOM 667 CD GLU A 112 -45.778 -26.705 38.438 1.00 88.68 C ANISOU 667 CD GLU A 112 11245 11090 11358 441 446 318 C ATOM 668 OE1 GLU A 112 -45.432 -26.016 37.451 1.00 77.89 O ANISOU 668 OE1 GLU A 112 8723 11534 9338 -965 -2714 -112 O ATOM 669 OE2 GLU A 112 -45.415 -27.893 38.594 1.00 81.32 O ANISOU 669 OE2 GLU A 112 9765 9851 11280 -1584 -2071 -868 O ATOM 670 N GLY A 113 -45.360 -21.624 38.770 1.00 44.50 N ANISOU 670 N GLY A 113 5659 5516 5730 -418 -500 74 N ATOM 671 CA GLY A 113 -45.598 -20.195 38.592 1.00 41.15 C ANISOU 671 CA GLY A 113 5460 5561 4612 -647 -401 556 C ATOM 672 C GLY A 113 -44.758 -19.336 39.524 1.00 41.23 C ANISOU 672 C GLY A 113 5214 5352 5099 -180 -863 108 C ATOM 673 O GLY A 113 -45.025 -18.140 39.684 1.00 41.75 O ANISOU 673 O GLY A 113 5724 5203 4935 -792 -582 -273 O ATOM 674 N VAL A 114 -43.751 -19.949 40.147 1.00 38.83 N ANISOU 674 N VAL A 114 4486 5416 4852 -614 -437 425 N ATOM 675 CA VAL A 114 -42.828 -19.215 41.002 1.00 31.77 C ANISOU 675 CA VAL A 114 4058 3828 4185 316 51 -144 C ATOM 676 C VAL A 114 -41.421 -19.314 40.433 1.00 33.57 C ANISOU 676 C VAL A 114 4287 4121 4344 91 278 171 C ATOM 677 O VAL A 114 -40.992 -20.389 39.979 1.00 33.32 O ANISOU 677 O VAL A 114 4368 4341 3950 -25 263 -245 O ATOM 678 CB VAL A 114 -42.810 -19.740 42.455 1.00 32.79 C ANISOU 678 CB VAL A 114 3907 4556 3995 -5 1 -354 C ATOM 679 CG1 VAL A 114 -41.894 -18.878 43.324 1.00 31.82 C ANISOU 679 CG1 VAL A 114 3821 3873 4394 -348 256 -117 C ATOM 680 CG2 VAL A 114 -44.212 -19.755 43.048 1.00 33.86 C ANISOU 680 CG2 VAL A 114 3720 4796 4348 -439 -226 726 C ATOM 681 N ALA A 115 -40.709 -18.188 40.472 1.00 32.17 N ANISOU 681 N ALA A 115 4094 4037 4091 227 -101 36 N ATOM 682 CA ALA A 115 -39.303 -18.132 40.088 1.00 34.96 C ANISOU 682 CA ALA A 115 4170 4607 4505 -248 100 217 C ATOM 683 C ALA A 115 -39.106 -18.691 38.678 1.00 33.13 C ANISOU 683 C ALA A 115 4199 3717 4670 -1089 135 117 C ATOM 684 O ALA A 115 -39.797 -18.282 37.743 1.00 38.30 O ANISOU 684 O ALA A 115 5205 4480 4866 -586 -157 414 O ATOM 685 CB ALA A 115 -38.452 -18.876 41.112 1.00 33.69 C ANISOU 685 CB ALA A 115 3337 4309 5154 212 114 -197 C ATOM 686 N TYR A 116 -38.187 -19.637 38.523 1.00 38.09 N ANISOU 686 N TYR A 116 3785 5194 5492 -684 344 -426 N ATOM 687 CA TYR A 116 -37.898 -20.174 37.198 1.00 46.11 C ANISOU 687 CA TYR A 116 5307 6627 5586 274 -33 -891 C ATOM 688 C TYR A 116 -39.048 -20.982 36.609 1.00 47.06 C ANISOU 688 C TYR A 116 5407 6648 5825 3 327 -918 C ATOM 689 O TYR A 116 -39.055 -21.276 35.418 1.00 52.52 O ANISOU 689 O TYR A 116 5086 8444 6423 779 423 -2391 O ATOM 690 CB TYR A 116 -36.601 -20.972 37.210 1.00 47.00 C ANISOU 690 CB TYR A 116 5633 5237 6987 97 -276 -1010 C ATOM 691 CG TYR A 116 -35.395 -20.132 37.576 1.00 47.54 C ANISOU 691 CG TYR A 116 5786 5853 6425 -319 -510 -323 C ATOM 692 CD1 TYR A 116 -34.963 -19.093 36.749 1.00 46.59 C ANISOU 692 CD1 TYR A 116 5576 5598 6525 302 478 -495 C ATOM 693 CD2 TYR A 116 -34.694 -20.372 38.746 1.00 48.72 C ANISOU 693 CD2 TYR A 116 6793 5700 6016 386 -442 -947 C ATOM 694 CE1 TYR A 116 -33.861 -18.317 37.084 1.00 46.40 C ANISOU 694 CE1 TYR A 116 5110 6922 5594 547 392 -1075 C ATOM 695 CE2 TYR A 116 -33.585 -19.613 39.088 1.00 49.66 C ANISOU 695 CE2 TYR A 116 5497 6111 7259 204 76 654 C ATOM 696 CZ TYR A 116 -33.168 -18.589 38.258 1.00 49.16 C ANISOU 696 CZ TYR A 116 6079 6462 6137 -336 120 -23 C ATOM 697 OH TYR A 116 -32.060 -17.847 38.617 1.00 42.78 O ANISOU 697 OH TYR A 116 5944 5563 4744 766 -662 -492 O ATOM 698 N ALA A 117 -40.030 -21.319 37.443 1.00 46.08 N ANISOU 698 N ALA A 117 6429 5026 6052 -519 37 848 N ATOM 699 CA ALA A 117 -41.228 -22.009 36.985 1.00 47.65 C ANISOU 699 CA ALA A 117 5655 5904 6543 -101 265 -24 C ATOM 700 C ALA A 117 -42.276 -21.033 36.436 1.00 50.73 C ANISOU 700 C ALA A 117 6324 6003 6946 -332 -1423 46 C ATOM 701 O ALA A 117 -43.370 -21.445 36.061 1.00 54.55 O ANISOU 701 O ALA A 117 5599 6714 8413 -405 -186 -717 O ATOM 702 CB ALA A 117 -41.817 -22.850 38.114 1.00 43.42 C ANISOU 702 CB ALA A 117 6336 4614 5545 -848 -222 -914 C ATOM 703 N ALA A 118 -41.946 -19.743 36.393 1.00 45.87 N ANISOU 703 N ALA A 118 6324 5417 5686 731 409 33 N ATOM 704 CA ALA A 118 -42.854 -18.751 35.824 1.00 45.47 C ANISOU 704 CA ALA A 118 6082 5988 5206 475 -522 -75 C ATOM 705 C ALA A 118 -42.331 -18.285 34.468 1.00 45.15 C ANISOU 705 C ALA A 118 5165 6189 5800 511 -8 63 C ATOM 706 O ALA A 118 -41.146 -18.444 34.185 1.00 39.69 O ANISOU 706 O ALA A 118 4816 4827 5437 -273 -143 -794 O ATOM 707 CB ALA A 118 -43.006 -17.563 36.767 1.00 44.62 C ANISOU 707 CB ALA A 118 5682 6278 4991 590 137 -18 C ATOM 708 N PRO A 119 -43.213 -17.727 33.613 1.00 42.46 N ANISOU 708 N PRO A 119 5398 5108 5627 -136 -394 -101 N ATOM 709 CA PRO A 119 -42.670 -17.031 32.447 1.00 43.47 C ANISOU 709 CA PRO A 119 5200 5464 5851 280 228 -131 C ATOM 710 C PRO A 119 -41.676 -15.951 32.919 1.00 45.00 C ANISOU 710 C PRO A 119 5336 6135 5625 -102 119 -41 C ATOM 711 O PRO A 119 -41.847 -15.383 34.003 1.00 42.78 O ANISOU 711 O PRO A 119 4881 6273 5100 -661 -207 110 O ATOM 712 CB PRO A 119 -43.912 -16.395 31.806 1.00 46.68 C ANISOU 712 CB PRO A 119 5435 6218 6083 -441 -367 1132 C ATOM 713 CG PRO A 119 -45.060 -17.261 32.240 1.00 41.50 C ANISOU 713 CG PRO A 119 4757 5979 5033 269 -39 639 C ATOM 714 CD PRO A 119 -44.692 -17.721 33.633 1.00 39.89 C ANISOU 714 CD PRO A 119 5145 5294 4717 -107 -177 102 C ATOM 715 N TYR A 120 -40.644 -15.683 32.125 1.00 42.91 N ANISOU 715 N TYR A 120 5577 6117 4610 566 3 -24 N ATOM 716 CA TYR A 120 -39.583 -14.739 32.521 1.00 49.89 C ANISOU 716 CA TYR A 120 6277 5647 7032 55 160 -197 C ATOM 717 C TYR A 120 -40.092 -13.351 32.943 1.00 44.73 C ANISOU 717 C TYR A 120 5575 5711 5709 -57 221 24 C ATOM 718 O TYR A 120 -39.621 -12.813 33.940 1.00 46.14 O ANISOU 718 O TYR A 120 5589 6443 5498 237 521 -126 O ATOM 719 CB TYR A 120 -38.511 -14.627 31.427 1.00 60.81 C ANISOU 719 CB TYR A 120 8874 7752 6478 -1072 707 -12 C ATOM 720 CG TYR A 120 -38.227 -15.947 30.735 1.00 86.24 C ANISOU 720 CG TYR A 120 12907 8658 11199 1805 1704 -1507 C ATOM 721 CD1 TYR A 120 -39.069 -16.416 29.718 1.00 97.10 C ANISOU 721 CD1 TYR A 120 15383 12112 9399 1857 629 -422 C ATOM 722 CD2 TYR A 120 -37.131 -16.733 31.102 1.00 84.36 C ANISOU 722 CD2 TYR A 120 9834 11109 11110 -851 -358 -2509 C ATOM 723 CE1 TYR A 120 -38.828 -17.623 29.084 1.00 94.05 C ANISOU 723 CE1 TYR A 120 15583 11129 9021 -589 -2505 -511 C ATOM 724 CE2 TYR A 120 -36.881 -17.943 30.473 1.00 92.17 C ANISOU 724 CE2 TYR A 120 11797 10331 12889 2311 2342 -273 C ATOM 725 CZ TYR A 120 -37.731 -18.382 29.463 1.00106.30 C ANISOU 725 CZ TYR A 120 14474 11642 14270 1106 907 -262 C ATOM 726 OH TYR A 120 -37.497 -19.580 28.825 1.00 96.69 O ANISOU 726 OH TYR A 120 16441 11122 9172 -1633 -2059 170 O ATOM 727 N PRO A 121 -41.048 -12.768 32.191 1.00 47.44 N ANISOU 727 N PRO A 121 6244 5703 6077 425 -216 -231 N ATOM 728 CA PRO A 121 -41.603 -11.466 32.575 1.00 42.66 C ANISOU 728 CA PRO A 121 5162 6235 4811 623 -152 -374 C ATOM 729 C PRO A 121 -42.213 -11.502 33.971 1.00 36.05 C ANISOU 729 C PRO A 121 4635 4524 4536 659 -644 563 C ATOM 730 O PRO A 121 -41.997 -10.590 34.768 1.00 39.74 O ANISOU 730 O PRO A 121 5292 4818 4989 472 -237 188 O ATOM 731 CB PRO A 121 -42.703 -11.239 31.536 1.00 42.31 C ANISOU 731 CB PRO A 121 5411 5326 5337 1233 -125 536 C ATOM 732 CG PRO A 121 -42.238 -11.992 30.342 1.00 42.41 C ANISOU 732 CG PRO A 121 5475 5125 5513 129 -1201 -678 C ATOM 733 CD PRO A 121 -41.588 -13.225 30.896 1.00 47.49 C ANISOU 733 CD PRO A 121 6434 5478 6130 815 -553 -306 C ATOM 734 N ARG A 122 -42.960 -12.562 34.253 1.00 36.54 N ANISOU 734 N ARG A 122 4393 5036 4455 476 -431 421 N ATOM 735 CA ARG A 122 -43.542 -12.783 35.572 1.00 36.60 C ANISOU 735 CA ARG A 122 4755 4535 4614 353 -257 742 C ATOM 736 C ARG A 122 -42.462 -13.024 36.645 1.00 36.68 C ANISOU 736 C ARG A 122 4550 4911 4476 204 -270 -133 C ATOM 737 O ARG A 122 -42.552 -12.497 37.756 1.00 32.93 O ANISOU 737 O ARG A 122 3955 4377 4180 279 -181 290 O ATOM 738 CB ARG A 122 -44.519 -13.957 35.508 1.00 40.01 C ANISOU 738 CB ARG A 122 4087 5411 5702 115 -106 -198 C ATOM 739 CG ARG A 122 -45.247 -14.252 36.807 1.00 44.37 C ANISOU 739 CG ARG A 122 5147 6186 5522 -707 -239 -99 C ATOM 740 CD ARG A 122 -45.989 -13.019 37.297 1.00 52.73 C ANISOU 740 CD ARG A 122 6947 7204 5882 453 769 -49 C ATOM 741 NE ARG A 122 -47.398 -13.296 37.559 1.00 60.44 N ANISOU 741 NE ARG A 122 7236 9594 6131 970 1282 340 N ATOM 742 CZ ARG A 122 -48.407 -12.604 37.041 1.00 58.86 C ANISOU 742 CZ ARG A 122 8283 8342 5736 -278 -1435 -902 C ATOM 743 NH1 ARG A 122 -48.173 -11.573 36.237 1.00 66.72 N ANISOU 743 NH1 ARG A 122 11165 7553 6630 528 1986 -1080 N ATOM 744 NH2 ARG A 122 -49.654 -12.928 37.345 1.00 73.25 N ANISOU 744 NH2 ARG A 122 9637 10476 7715 -2196 -78 -2154 N ATOM 745 N MET A 123 -41.438 -13.806 36.322 1.00 38.11 N ANISOU 745 N MET A 123 4717 5004 4759 428 -273 79 N ATOM 746 CA MET A 123 -40.360 -14.014 37.292 1.00 34.97 C ANISOU 746 CA MET A 123 4535 4281 4469 218 -65 395 C ATOM 747 C MET A 123 -39.721 -12.685 37.661 1.00 36.05 C ANISOU 747 C MET A 123 4285 4483 4927 288 -81 211 C ATOM 748 O MET A 123 -39.482 -12.408 38.840 1.00 35.03 O ANISOU 748 O MET A 123 4788 3978 4543 253 321 779 O ATOM 749 CB MET A 123 -39.287 -14.977 36.788 1.00 35.76 C ANISOU 749 CB MET A 123 5263 4072 4250 255 258 214 C ATOM 750 CG MET A 123 -38.299 -15.315 37.889 1.00 45.46 C ANISOU 750 CG MET A 123 5824 5809 5639 267 -727 266 C ATOM 751 SD MET A 123 -36.891 -16.341 37.434 1.00 50.89 S ANISOU 751 SD MET A 123 6357 6144 6834 -480 399 199 S ATOM 752 CE MET A 123 -36.021 -15.218 36.331 1.00 84.73 C ANISOU 752 CE MET A 123 11796 10714 9681 -4012 821 2390 C ATOM 753 N ARG A 124 -39.459 -11.859 36.650 1.00 41.17 N ANISOU 753 N ARG A 124 5368 4917 5358 -88 940 378 N ATOM 754 CA ARG A 124 -38.842 -10.553 36.879 1.00 42.12 C ANISOU 754 CA ARG A 124 5179 5420 5404 -247 237 -145 C ATOM 755 C ARG A 124 -39.666 -9.682 37.834 1.00 37.60 C ANISOU 755 C ARG A 124 4627 5054 4602 103 -331 392 C ATOM 756 O ARG A 124 -39.106 -8.978 38.675 1.00 36.37 O ANISOU 756 O ARG A 124 4147 4832 4840 273 -305 451 O ATOM 757 CB ARG A 124 -38.585 -9.843 35.542 1.00 45.54 C ANISOU 757 CB ARG A 124 5196 5896 6211 384 -744 1153 C ATOM 758 CG ARG A 124 -37.783 -8.550 35.629 1.00 52.78 C ANISOU 758 CG ARG A 124 7123 6046 6884 84 -401 -933 C ATOM 759 CD ARG A 124 -36.461 -8.724 36.368 1.00 65.70 C ANISOU 759 CD ARG A 124 6503 8250 10208 1177 -706 -105 C ATOM 760 NE ARG A 124 -35.632 -9.797 35.817 1.00 69.42 N ANISOU 760 NE ARG A 124 8669 7954 9751 1322 591 1031 N ATOM 761 CZ ARG A 124 -34.408 -10.088 36.250 1.00 76.63 C ANISOU 761 CZ ARG A 124 9060 10256 9797 -297 -706 1500 C ATOM 762 NH1 ARG A 124 -33.873 -9.385 37.241 1.00 79.88 N ANISOU 762 NH1 ARG A 124 11469 8007 10875 -1976 -431 1239 N ATOM 763 NH2 ARG A 124 -33.719 -11.081 35.699 1.00 67.84 N ANISOU 763 NH2 ARG A 124 6990 11831 6952 -2811 1647 297 N ATOM 764 N GLU A 125 -40.992 -9.731 37.726 1.00 37.54 N ANISOU 764 N GLU A 125 4615 5404 4244 114 90 322 N ATOM 765 CA GLU A 125 -41.829 -8.946 38.640 1.00 35.84 C ANISOU 765 CA GLU A 125 4676 4800 4142 143 -318 223 C ATOM 766 C GLU A 125 -41.649 -9.467 40.054 1.00 30.84 C ANISOU 766 C GLU A 125 3671 3966 4077 64 -733 -100 C ATOM 767 O GLU A 125 -41.592 -8.695 41.005 1.00 31.97 O ANISOU 767 O GLU A 125 3963 4226 3956 750 -563 -33 O ATOM 768 CB GLU A 125 -43.315 -9.014 38.270 1.00 40.58 C ANISOU 768 CB GLU A 125 4445 5641 5332 10 -185 290 C ATOM 769 CG GLU A 125 -43.725 -8.277 37.000 1.00 46.64 C ANISOU 769 CG GLU A 125 5371 6780 5568 288 -734 797 C ATOM 770 CD GLU A 125 -45.236 -8.283 36.818 1.00 49.49 C ANISOU 770 CD GLU A 125 5792 6983 6027 1465 -1227 -762 C ATOM 771 OE1 GLU A 125 -45.741 -9.127 36.046 1.00 49.02 O ANISOU 771 OE1 GLU A 125 5400 7325 5899 -234 -974 163 O ATOM 772 OE2 GLU A 125 -45.922 -7.472 37.480 1.00 45.08 O ANISOU 772 OE2 GLU A 125 5319 5965 5844 1529 -457 858 O ATOM 773 N GLN A 126 -41.572 -10.785 40.180 1.00 31.69 N ANISOU 773 N GLN A 126 3758 3985 4294 397 -258 377 N ATOM 774 CA GLN A 126 -41.436 -11.426 41.482 1.00 35.71 C ANISOU 774 CA GLN A 126 4887 4525 4153 527 -716 131 C ATOM 775 C GLN A 126 -40.090 -11.082 42.097 1.00 33.00 C ANISOU 775 C GLN A 126 4454 3919 4164 376 -56 1 C ATOM 776 O GLN A 126 -40.012 -10.789 43.288 1.00 30.96 O ANISOU 776 O GLN A 126 3946 3905 3912 406 14 327 O ATOM 777 CB GLN A 126 -41.592 -12.942 41.362 1.00 37.34 C ANISOU 777 CB GLN A 126 5221 4388 4578 -394 -719 1364 C ATOM 778 CG GLN A 126 -43.005 -13.394 41.047 1.00 41.48 C ANISOU 778 CG GLN A 126 4959 5191 5608 -165 -446 222 C ATOM 779 CD GLN A 126 -43.061 -14.859 40.672 1.00 39.49 C ANISOU 779 CD GLN A 126 4993 5196 4814 189 175 511 C ATOM 780 OE1 GLN A 126 -42.023 -15.521 40.526 1.00 35.28 O ANISOU 780 OE1 GLN A 126 4031 4867 4504 -547 34 722 O ATOM 781 NE2 GLN A 126 -44.271 -15.379 40.508 1.00 40.88 N ANISOU 781 NE2 GLN A 126 4807 5590 5135 221 300 861 N ATOM 782 N LEU A 127 -39.036 -11.117 41.282 1.00 34.66 N ANISOU 782 N LEU A 127 4299 4726 4144 -103 95 1325 N ATOM 783 CA LEU A 127 -37.708 -10.701 41.736 1.00 39.65 C ANISOU 783 CA LEU A 127 4720 5361 4981 -137 -66 191 C ATOM 784 C LEU A 127 -37.693 -9.251 42.179 1.00 38.13 C ANISOU 784 C LEU A 127 4389 5260 4836 -183 485 119 C ATOM 785 O LEU A 127 -37.122 -8.934 43.218 1.00 47.08 O ANISOU 785 O LEU A 127 4944 7516 5429 -49 -21 -308 O ATOM 786 CB LEU A 127 -36.655 -10.914 40.646 1.00 39.34 C ANISOU 786 CB LEU A 127 4520 5393 5034 549 -321 231 C ATOM 787 CG LEU A 127 -36.276 -12.365 40.367 1.00 42.00 C ANISOU 787 CG LEU A 127 5160 5786 5009 1175 -269 -5 C ATOM 788 CD1 LEU A 127 -35.450 -12.412 39.099 1.00 44.98 C ANISOU 788 CD1 LEU A 127 5533 7111 4446 889 -679 -804 C ATOM 789 CD2 LEU A 127 -35.510 -12.950 41.543 1.00 37.96 C ANISOU 789 CD2 LEU A 127 4917 4452 5051 -122 -470 225 C ATOM 790 N ASN A 128 -38.310 -8.364 41.401 1.00 40.27 N ANISOU 790 N ASN A 128 5061 4823 5415 -464 -92 293 N ATOM 791 CA ASN A 128 -38.402 -6.971 41.826 1.00 39.53 C ANISOU 791 CA ASN A 128 5352 5082 4584 472 131 -162 C ATOM 792 C ASN A 128 -39.067 -6.895 43.177 1.00 36.89 C ANISOU 792 C ASN A 128 4464 5066 4485 -54 -232 180 C ATOM 793 O ASN A 128 -38.676 -6.084 44.009 1.00 37.56 O ANISOU 793 O ASN A 128 4802 4771 4697 451 -179 -106 O ATOM 794 CB ASN A 128 -39.217 -6.119 40.855 1.00 44.99 C ANISOU 794 CB ASN A 128 5302 6181 5608 -165 -660 667 C ATOM 795 CG ASN A 128 -38.544 -5.947 39.509 1.00 49.11 C ANISOU 795 CG ASN A 128 6156 6278 6226 -713 169 -183 C ATOM 796 OD1 ASN A 128 -37.382 -6.306 39.326 1.00 59.73 O ANISOU 796 OD1 ASN A 128 7120 7341 8232 1109 -13 923 O ATOM 797 ND2 ASN A 128 -39.281 -5.387 38.553 1.00 58.81 N ANISOU 797 ND2 ASN A 128 8745 7016 6583 680 -66 315 N ATOM 798 N PHE A 129 -40.093 -7.721 43.394 1.00 36.34 N ANISOU 798 N PHE A 129 4616 4473 4717 293 -100 864 N ATOM 799 CA PHE A 129 -40.808 -7.671 44.673 1.00 35.12 C ANISOU 799 CA PHE A 129 4331 4268 4745 345 -192 975 C ATOM 800 C PHE A 129 -39.899 -8.130 45.797 1.00 29.88 C ANISOU 800 C PHE A 129 3440 4086 3825 -359 -194 -327 C ATOM 801 O PHE A 129 -39.871 -7.529 46.864 1.00 27.56 O ANISOU 801 O PHE A 129 2843 3880 3746 -374 -80 -47 O ATOM 802 CB PHE A 129 -42.108 -8.485 44.640 1.00 36.42 C ANISOU 802 CB PHE A 129 4388 4643 4806 200 58 1328 C ATOM 803 CG PHE A 129 -43.207 -7.838 43.835 1.00 38.26 C ANISOU 803 CG PHE A 129 3449 5391 5694 107 -833 90 C ATOM 804 CD1 PHE A 129 -43.544 -6.502 44.042 1.00 45.74 C ANISOU 804 CD1 PHE A 129 5769 5553 6056 158 -661 66 C ATOM 805 CD2 PHE A 129 -43.915 -8.565 42.889 1.00 40.05 C ANISOU 805 CD2 PHE A 129 5924 5966 3325 931 -26 -756 C ATOM 806 CE1 PHE A 129 -44.557 -5.903 43.307 1.00 45.58 C ANISOU 806 CE1 PHE A 129 5849 5742 5724 425 -1244 45 C ATOM 807 CE2 PHE A 129 -44.933 -7.973 42.153 1.00 43.92 C ANISOU 807 CE2 PHE A 129 5081 6139 5467 1300 325 -139 C ATOM 808 CZ PHE A 129 -45.252 -6.639 42.362 1.00 41.92 C ANISOU 808 CZ PHE A 129 4737 5796 5392 492 -629 426 C ATOM 809 N LEU A 130 -39.151 -9.196 45.548 1.00 31.06 N ANISOU 809 N LEU A 130 3154 4235 4413 -138 -316 -13 N ATOM 810 CA LEU A 130 -38.175 -9.663 46.513 1.00 32.09 C ANISOU 810 CA LEU A 130 4171 4074 3947 240 -430 32 C ATOM 811 C LEU A 130 -37.118 -8.579 46.798 1.00 36.42 C ANISOU 811 C LEU A 130 4375 5002 4461 -386 -368 187 C ATOM 812 O LEU A 130 -36.839 -8.277 47.954 1.00 38.06 O ANISOU 812 O LEU A 130 4445 5376 4638 -535 -8 -230 O ATOM 813 CB LEU A 130 -37.525 -10.956 46.030 1.00 30.15 C ANISOU 813 CB LEU A 130 4174 3664 3614 -98 -561 -98 C ATOM 814 CG LEU A 130 -36.547 -11.582 47.028 1.00 31.88 C ANISOU 814 CG LEU A 130 3639 4290 4184 685 -193 195 C ATOM 815 CD1 LEU A 130 -37.115 -11.602 48.444 1.00 31.23 C ANISOU 815 CD1 LEU A 130 3627 4275 3964 355 -455 -400 C ATOM 816 CD2 LEU A 130 -36.144 -12.982 46.589 1.00 32.97 C ANISOU 816 CD2 LEU A 130 4203 4409 3912 16 -619 -817 C ATOM 817 N ALA A 131 -36.554 -7.968 45.759 1.00 37.29 N ANISOU 817 N ALA A 131 4185 5384 4599 -543 -138 5 N ATOM 818 CA ALA A 131 -35.525 -6.939 45.978 1.00 37.76 C ANISOU 818 CA ALA A 131 4590 4481 5277 -220 -215 334 C ATOM 819 C ALA A 131 -36.057 -5.758 46.780 1.00 41.31 C ANISOU 819 C ALA A 131 4945 5757 4993 286 -263 -101 C ATOM 820 O ALA A 131 -35.350 -5.191 47.629 1.00 39.99 O ANISOU 820 O ALA A 131 3762 5952 5478 -1074 663 584 O ATOM 821 CB ALA A 131 -34.943 -6.469 44.656 1.00 41.08 C ANISOU 821 CB ALA A 131 4742 5376 5489 -768 -716 1299 C ATOM 822 N GLU A 132 -37.307 -5.383 46.525 1.00 33.63 N ANISOU 822 N GLU A 132 4031 4619 4128 -1145 -386 -80 N ATOM 823 CA GLU A 132 -37.900 -4.303 47.293 1.00 40.80 C ANISOU 823 CA GLU A 132 5258 4778 5465 22 133 354 C ATOM 824 C GLU A 132 -38.035 -4.678 48.770 1.00 43.62 C ANISOU 824 C GLU A 132 6231 4689 5653 -533 131 452 C ATOM 825 O GLU A 132 -38.191 -3.806 49.619 1.00 50.80 O ANISOU 825 O GLU A 132 7076 5322 6901 30 220 -374 O ATOM 826 CB GLU A 132 -39.242 -3.860 46.704 1.00 55.74 C ANISOU 826 CB GLU A 132 6053 6623 8499 -799 -2155 360 C ATOM 827 CG GLU A 132 -39.099 -2.936 45.500 1.00 77.19 C ANISOU 827 CG GLU A 132 10954 10179 8195 -508 129 1205 C ATOM 828 CD GLU A 132 -40.432 -2.474 44.927 1.00 87.76 C ANISOU 828 CD GLU A 132 10564 10828 11951 1255 570 843 C ATOM 829 OE1 GLU A 132 -41.349 -3.312 44.744 1.00 81.98 O ANISOU 829 OE1 GLU A 132 10786 10331 10031 1629 1390 279 O ATOM 830 OE2 GLU A 132 -40.558 -1.264 44.643 1.00109.13 O ANISOU 830 OE2 GLU A 132 17374 10550 13540 685 4014 851 O ATOM 831 N GLU A 133 -37.952 -5.970 49.082 1.00 31.68 N ANISOU 831 N GLU A 133 3493 4320 4225 501 -712 -61 N ATOM 832 CA GLU A 133 -38.031 -6.396 50.478 1.00 31.87 C ANISOU 832 CA GLU A 133 3842 4107 4160 346 -37 -93 C ATOM 833 C GLU A 133 -36.645 -6.400 51.129 1.00 35.66 C ANISOU 833 C GLU A 133 4188 4967 4392 64 -225 -20 C ATOM 834 O GLU A 133 -36.504 -6.635 52.338 1.00 32.15 O ANISOU 834 O GLU A 133 3442 4351 4422 -235 -401 -703 O ATOM 835 CB GLU A 133 -38.677 -7.779 50.606 1.00 34.85 C ANISOU 835 CB GLU A 133 3814 4597 4829 -217 139 -475 C ATOM 836 CG GLU A 133 -40.171 -7.814 50.307 1.00 34.50 C ANISOU 836 CG GLU A 133 3956 4260 4889 -216 -351 -118 C ATOM 837 CD GLU A 133 -40.952 -6.772 51.088 1.00 35.94 C ANISOU 837 CD GLU A 133 3920 4778 4957 -41 -66 -98 C ATOM 838 OE1 GLU A 133 -40.767 -6.658 52.323 1.00 34.93 O ANISOU 838 OE1 GLU A 133 4006 4361 4903 -558 582 443 O ATOM 839 OE2 GLU A 133 -41.752 -6.060 50.456 1.00 40.53 O ANISOU 839 OE2 GLU A 133 4827 4587 5985 -220 -203 803 O ATOM 840 N LEU A 134 -35.634 -6.149 50.306 1.00 37.70 N ANISOU 840 N LEU A 134 4509 5095 4717 -357 -30 407 N ATOM 841 CA LEU A 134 -34.245 -6.098 50.739 1.00 45.64 C ANISOU 841 CA LEU A 134 5220 5896 6223 600 -810 -682 C ATOM 842 C LEU A 134 -33.638 -4.745 50.334 1.00 51.68 C ANISOU 842 C LEU A 134 6129 6719 6786 185 -98 103 C ATOM 843 O LEU A 134 -32.439 -4.648 50.079 1.00 59.23 O ANISOU 843 O LEU A 134 6473 9209 6823 -1126 546 -845 O ATOM 844 CB LEU A 134 -33.452 -7.271 50.131 1.00 39.00 C ANISOU 844 CB LEU A 134 5087 5574 4156 588 -140 651 C ATOM 845 CG LEU A 134 -34.079 -8.672 50.243 1.00 40.29 C ANISOU 845 CG LEU A 134 5269 5445 4594 522 210 -120 C ATOM 846 CD1 LEU A 134 -33.548 -9.597 49.155 1.00 38.43 C ANISOU 846 CD1 LEU A 134 3848 5941 4809 19 448 -400 C ATOM 847 CD2 LEU A 134 -33.907 -9.308 51.626 1.00 32.50 C ANISOU 847 CD2 LEU A 134 3167 4782 4400 60 -579 -488 C ATOM 848 N THR A 135 -34.475 -3.706 50.276 1.00 44.63 N ANISOU 848 N THR A 135 6684 5542 4730 -321 -1572 -604 N ATOM 849 CA THR A 135 -34.006 -2.368 49.922 1.00 48.14 C ANISOU 849 CA THR A 135 4760 6169 7359 -892 532 -776 C ATOM 850 C THR A 135 -33.103 -1.817 51.013 1.00 50.52 C ANISOU 850 C THR A 135 6293 7055 5846 -875 23 92 C ATOM 851 O THR A 135 -33.198 -2.200 52.186 1.00 44.32 O ANISOU 851 O THR A 135 4183 6187 6470 -2050 275 662 O ATOM 852 CB THR A 135 -35.140 -1.336 49.739 1.00 51.59 C ANISOU 852 CB THR A 135 6500 6782 6320 52 -424 -199 C ATOM 853 OG1 THR A 135 -35.794 -1.103 50.998 1.00 48.04 O ANISOU 853 OG1 THR A 135 4866 6355 7029 946 217 246 O ATOM 854 CG2 THR A 135 -36.147 -1.772 48.688 1.00 49.67 C ANISOU 854 CG2 THR A 135 7628 5197 6047 -405 -116 -1184 C ATOM 855 N ILE A 136 -32.247 -0.886 50.613 1.00 61.25 N ANISOU 855 N ILE A 136 7095 7623 8555 -2060 -201 -799 N ATOM 856 CA ILE A 136 -31.327 -0.245 51.528 1.00 51.22 C ANISOU 856 CA ILE A 136 6763 6753 5944 -1070 274 -319 C ATOM 857 C ILE A 136 -32.088 0.418 52.688 1.00 40.38 C ANISOU 857 C ILE A 136 4822 4541 5977 -1487 257 548 C ATOM 858 O ILE A 136 -31.611 0.408 53.822 1.00 49.08 O ANISOU 858 O ILE A 136 6065 6580 6002 -1883 -159 742 O ATOM 859 CB ILE A 136 -30.377 0.723 50.765 1.00 49.42 C ANISOU 859 CB ILE A 136 6264 5961 6549 -675 -169 -234 C ATOM 860 CG1 ILE A 136 -28.915 0.386 51.064 1.00 59.21 C ANISOU 860 CG1 ILE A 136 6489 7926 8083 127 -70 -237 C ATOM 861 CG2 ILE A 136 -30.690 2.182 51.056 1.00 48.65 C ANISOU 861 CG2 ILE A 136 6972 4822 6689 -1066 -1103 1610 C ATOM 862 CD1 ILE A 136 -28.509 -1.012 50.642 1.00 66.83 C ANISOU 862 CD1 ILE A 136 8689 7711 8990 -475 601 -601 C ATOM 863 N ALA A 137 -33.284 0.944 52.412 1.00 45.76 N ANISOU 863 N ALA A 137 6050 4998 6337 -214 -239 581 N ATOM 864 CA ALA A 137 -34.127 1.573 53.445 1.00 50.79 C ANISOU 864 CA ALA A 137 7198 5914 6184 -405 -122 13 C ATOM 865 C ALA A 137 -34.497 0.618 54.570 1.00 52.06 C ANISOU 865 C ALA A 137 7310 6461 6008 -323 584 -88 C ATOM 866 O ALA A 137 -34.698 1.035 55.711 1.00 51.33 O ANISOU 866 O ALA A 137 5686 7004 6811 -164 907 -993 O ATOM 867 CB ALA A 137 -35.392 2.162 52.833 1.00 51.52 C ANISOU 867 CB ALA A 137 6769 5459 7344 -621 -620 -1031 C ATOM 868 N LYS A 138 -34.593 -0.666 54.250 1.00 52.33 N ANISOU 868 N LYS A 138 7161 6398 6322 -1472 -284 209 N ATOM 869 CA LYS A 138 -34.949 -1.640 55.262 1.00 46.23 C ANISOU 869 CA LYS A 138 5525 5998 6040 -72 9 107 C ATOM 870 C LYS A 138 -33.749 -2.055 56.098 1.00 40.04 C ANISOU 870 C LYS A 138 4977 4924 5310 -180 674 212 C ATOM 871 O LYS A 138 -33.913 -2.563 57.205 1.00 40.70 O ANISOU 871 O LYS A 138 5396 4993 5074 0 1467 -237 O ATOM 872 CB LYS A 138 -35.651 -2.837 54.634 1.00 47.80 C ANISOU 872 CB LYS A 138 6001 5801 6359 -339 -234 220 C ATOM 873 CG LYS A 138 -37.027 -2.469 54.108 1.00 45.75 C ANISOU 873 CG LYS A 138 6530 5353 5498 183 55 1148 C ATOM 874 CD LYS A 138 -37.700 -3.632 53.407 1.00 52.60 C ANISOU 874 CD LYS A 138 8191 5632 6162 1014 -223 -461 C ATOM 875 CE LYS A 138 -38.913 -3.165 52.621 1.00 52.17 C ANISOU 875 CE LYS A 138 7051 6563 6206 87 -199 -857 C ATOM 876 NZ LYS A 138 -40.093 -2.921 53.485 1.00 59.85 N ANISOU 876 NZ LYS A 138 8018 5545 9178 903 1264 -992 N ATOM 877 N PHE A 139 -32.544 -1.805 55.583 1.00 35.45 N ANISOU 877 N PHE A 139 4330 4407 4732 38 472 -779 N ATOM 878 CA PHE A 139 -31.316 -2.129 56.310 1.00 38.38 C ANISOU 878 CA PHE A 139 4783 5586 4212 180 491 -60 C ATOM 879 C PHE A 139 -31.199 -1.360 57.629 1.00 38.12 C ANISOU 879 C PHE A 139 5284 4827 4371 571 -10 -58 C ATOM 880 O PHE A 139 -30.501 -1.813 58.545 1.00 33.11 O ANISOU 880 O PHE A 139 3520 4411 4647 79 446 122 O ATOM 881 CB PHE A 139 -30.068 -1.854 55.450 1.00 40.34 C ANISOU 881 CB PHE A 139 4527 6005 4796 720 734 -183 C ATOM 882 CG PHE A 139 -29.788 -2.905 54.400 1.00 40.37 C ANISOU 882 CG PHE A 139 4960 4430 5948 88 273 -324 C ATOM 883 CD1 PHE A 139 -30.799 -3.735 53.919 1.00 38.84 C ANISOU 883 CD1 PHE A 139 4414 5236 5106 455 -376 48 C ATOM 884 CD2 PHE A 139 -28.504 -3.042 53.864 1.00 40.27 C ANISOU 884 CD2 PHE A 139 5166 4543 5589 -753 511 -36 C ATOM 885 CE1 PHE A 139 -30.538 -4.692 52.945 1.00 42.36 C ANISOU 885 CE1 PHE A 139 5212 4898 5984 -245 230 -173 C ATOM 886 CE2 PHE A 139 -28.238 -3.991 52.890 1.00 41.21 C ANISOU 886 CE2 PHE A 139 5356 5175 5125 -227 1819 389 C ATOM 887 CZ PHE A 139 -29.258 -4.821 52.429 1.00 50.46 C ANISOU 887 CZ PHE A 139 5453 7461 6257 -301 578 -342 C ATOM 888 N GLN A 140 -31.867 -0.206 57.734 1.00 36.65 N ANISOU 888 N GLN A 140 4279 4630 5013 94 106 -84 N ATOM 889 CA GLN A 140 -31.812 0.572 58.988 1.00 40.47 C ANISOU 889 CA GLN A 140 5316 4918 5141 -286 -146 -70 C ATOM 890 C GLN A 140 -32.178 -0.312 60.179 1.00 35.43 C ANISOU 890 C GLN A 140 4574 4254 4634 -109 402 -827 C ATOM 891 O GLN A 140 -31.543 -0.250 61.228 1.00 42.57 O ANISOU 891 O GLN A 140 5260 5090 5825 -717 -419 -464 O ATOM 892 CB GLN A 140 -32.717 1.814 58.953 1.00 44.83 C ANISOU 892 CB GLN A 140 5086 5395 6549 -70 -60 -263 C ATOM 893 CG GLN A 140 -32.613 2.658 57.690 1.00 55.00 C ANISOU 893 CG GLN A 140 6685 7023 7190 2 -1674 763 C ATOM 894 CD GLN A 140 -31.257 3.322 57.499 1.00 58.73 C ANISOU 894 CD GLN A 140 7092 7970 7251 -154 1 187 C ATOM 895 OE1 GLN A 140 -30.578 3.687 58.463 1.00 56.91 O ANISOU 895 OE1 GLN A 140 7231 5193 9199 542 -1228 -90 O ATOM 896 NE2 GLN A 140 -30.863 3.495 56.240 1.00 62.71 N ANISOU 896 NE2 GLN A 140 7780 7325 8720 513 1660 2275 N ATOM 897 N ASN A 141 -33.191 -1.155 59.997 1.00 32.51 N ANISOU 897 N ASN A 141 3508 4259 4584 192 310 -198 N ATOM 898 CA ASN A 141 -33.632 -2.061 61.045 1.00 32.95 C ANISOU 898 CA ASN A 141 4057 3990 4470 347 802 -429 C ATOM 899 C ASN A 141 -32.910 -3.386 61.030 1.00 29.54 C ANISOU 899 C ASN A 141 3145 4129 3947 273 97 -170 C ATOM 900 O ASN A 141 -32.808 -4.047 62.055 1.00 30.72 O ANISOU 900 O ASN A 141 3432 4228 4010 147 635 -226 O ATOM 901 CB ASN A 141 -35.130 -2.323 60.914 1.00 45.68 C ANISOU 901 CB ASN A 141 4410 5735 7211 -511 213 -471 C ATOM 902 CG ASN A 141 -35.960 -1.124 61.308 1.00 55.84 C ANISOU 902 CG ASN A 141 6387 7098 7732 786 -67 -1531 C ATOM 903 OD1 ASN A 141 -35.662 -0.446 62.292 1.00 52.12 O ANISOU 903 OD1 ASN A 141 5960 6810 7032 1208 680 -1369 O ATOM 904 ND2 ASN A 141 -37.010 -0.852 60.540 1.00 66.63 N ANISOU 904 ND2 ASN A 141 8943 8834 7537 1181 -882 1049 N ATOM 905 N PHE A 142 -32.432 -3.796 59.862 1.00 29.79 N ANISOU 905 N PHE A 142 2970 3956 4390 -177 406 -590 N ATOM 906 CA PHE A 142 -31.760 -5.093 59.770 1.00 27.47 C ANISOU 906 CA PHE A 142 3505 3649 3283 -13 104 85 C ATOM 907 C PHE A 142 -30.528 -5.135 60.647 1.00 28.52 C ANISOU 907 C PHE A 142 3153 3999 3685 248 268 -30 C ATOM 908 O PHE A 142 -30.327 -6.121 61.341 1.00 31.14 O ANISOU 908 O PHE A 142 3570 4109 4152 -407 713 273 O ATOM 909 CB PHE A 142 -31.392 -5.443 58.331 1.00 26.28 C ANISOU 909 CB PHE A 142 3885 2466 3632 216 187 -515 C ATOM 910 CG PHE A 142 -32.573 -5.789 57.463 1.00 30.38 C ANISOU 910 CG PHE A 142 3555 4170 3817 297 -66 262 C ATOM 911 CD1 PHE A 142 -33.867 -5.814 57.982 1.00 33.88 C ANISOU 911 CD1 PHE A 142 4111 4440 4318 -283 378 -560 C ATOM 912 CD2 PHE A 142 -32.389 -6.128 56.132 1.00 33.60 C ANISOU 912 CD2 PHE A 142 3625 4990 4148 43 245 -465 C ATOM 913 CE1 PHE A 142 -34.952 -6.134 57.179 1.00 30.80 C ANISOU 913 CE1 PHE A 142 4084 3652 3964 -469 429 115 C ATOM 914 CE2 PHE A 142 -33.466 -6.456 55.329 1.00 35.26 C ANISOU 914 CE2 PHE A 142 4084 4733 4578 -413 -92 -170 C ATOM 915 CZ PHE A 142 -34.752 -6.461 55.853 1.00 30.99 C ANISOU 915 CZ PHE A 142 4184 3625 3964 -128 90 -41 C ATOM 916 N VAL A 143 -29.707 -4.075 60.645 1.00 32.32 N ANISOU 916 N VAL A 143 3871 4134 4273 -63 168 -789 N ATOM 917 CA VAL A 143 -28.427 -4.143 61.397 1.00 30.43 C ANISOU 917 CA VAL A 143 3762 3923 3877 298 190 -634 C ATOM 918 C VAL A 143 -28.623 -4.527 62.862 1.00 28.98 C ANISOU 918 C VAL A 143 3193 3769 4048 -552 -174 -241 C ATOM 919 O VAL A 143 -28.012 -5.503 63.324 1.00 30.77 O ANISOU 919 O VAL A 143 3108 4016 4565 3 213 -636 O ATOM 920 CB VAL A 143 -27.513 -2.886 61.270 1.00 34.22 C ANISOU 920 CB VAL A 143 4296 4802 3902 -389 -178 -188 C ATOM 921 CG1 VAL A 143 -26.361 -2.981 62.268 1.00 30.45 C ANISOU 921 CG1 VAL A 143 2750 4449 4368 -987 338 -748 C ATOM 922 CG2 VAL A 143 -26.959 -2.746 59.854 1.00 29.81 C ANISOU 922 CG2 VAL A 143 2692 3888 4742 406 666 268 C ATOM 923 N PRO A 144 -29.474 -3.777 63.606 1.00 32.19 N ANISOU 923 N PRO A 144 3718 4110 4400 161 -441 -394 N ATOM 924 CA PRO A 144 -29.709 -4.151 65.012 1.00 34.51 C ANISOU 924 CA PRO A 144 4312 4419 4381 101 310 -955 C ATOM 925 C PRO A 144 -30.324 -5.547 65.211 1.00 34.56 C ANISOU 925 C PRO A 144 4578 4263 4288 333 -7 -601 C ATOM 926 O PRO A 144 -29.941 -6.270 66.134 1.00 35.31 O ANISOU 926 O PRO A 144 4559 5229 3627 -4 736 -476 O ATOM 927 CB PRO A 144 -30.646 -3.039 65.541 1.00 35.66 C ANISOU 927 CB PRO A 144 4165 4993 4389 892 -169 -354 C ATOM 928 CG PRO A 144 -31.129 -2.296 64.340 1.00 37.23 C ANISOU 928 CG PRO A 144 5321 4049 4773 566 451 437 C ATOM 929 CD PRO A 144 -30.096 -2.483 63.264 1.00 34.62 C ANISOU 929 CD PRO A 144 4223 3609 5320 -59 284 -322 C ATOM 930 N ALA A 145 -31.249 -5.928 64.338 1.00 36.32 N ANISOU 930 N ALA A 145 3718 4877 5204 -189 311 -1032 N ATOM 931 CA ALA A 145 -31.834 -7.273 64.364 1.00 35.51 C ANISOU 931 CA ALA A 145 4615 4498 4376 280 176 158 C ATOM 932 C ALA A 145 -30.772 -8.362 64.250 1.00 31.50 C ANISOU 932 C ALA A 145 3778 4443 3747 -55 -486 283 C ATOM 933 O ALA A 145 -30.796 -9.357 64.988 1.00 27.53 O ANISOU 933 O ALA A 145 3341 3396 3721 -181 332 -381 O ATOM 934 CB ALA A 145 -32.867 -7.424 63.246 1.00 39.03 C ANISOU 934 CB ALA A 145 4660 5484 4684 -37 170 -617 C ATOM 935 N ILE A 146 -29.846 -8.176 63.313 1.00 34.70 N ANISOU 935 N ILE A 146 4120 4801 4261 302 138 -531 N ATOM 936 CA ILE A 146 -28.788 -9.151 63.093 1.00 31.45 C ANISOU 936 CA ILE A 146 4268 4094 3585 139 44 -241 C ATOM 937 C ILE A 146 -27.892 -9.203 64.316 1.00 29.23 C ANISOU 937 C ILE A 146 3388 3979 3736 -133 503 -48 C ATOM 938 O ILE A 146 -27.623 -10.271 64.864 1.00 31.43 O ANISOU 938 O ILE A 146 3837 3923 4181 -172 563 -392 O ATOM 939 CB ILE A 146 -27.958 -8.819 61.827 1.00 30.73 C ANISOU 939 CB ILE A 146 3453 4146 4077 121 7 174 C ATOM 940 CG1 ILE A 146 -28.858 -8.838 60.583 1.00 30.61 C ANISOU 940 CG1 ILE A 146 3938 4074 3615 -74 183 -72 C ATOM 941 CG2 ILE A 146 -26.835 -9.818 61.658 1.00 26.44 C ANISOU 941 CG2 ILE A 146 3424 3253 3366 -351 318 -124 C ATOM 942 CD1 ILE A 146 -28.268 -8.172 59.353 1.00 30.38 C ANISOU 942 CD1 ILE A 146 3975 3794 3773 204 472 -241 C ATOM 943 N GLN A 147 -27.439 -8.044 64.771 1.00 34.26 N ANISOU 943 N GLN A 147 4292 4473 4251 -83 664 -905 N ATOM 944 CA GLN A 147 -26.507 -8.033 65.892 1.00 33.60 C ANISOU 944 CA GLN A 147 4154 4311 4297 -261 505 -536 C ATOM 945 C GLN A 147 -27.158 -8.604 67.161 1.00 34.40 C ANISOU 945 C GLN A 147 4395 4543 4131 217 465 -203 C ATOM 946 O GLN A 147 -26.520 -9.346 67.918 1.00 33.55 O ANISOU 946 O GLN A 147 4266 5192 3287 423 181 -997 O ATOM 947 CB GLN A 147 -25.934 -6.634 66.117 1.00 32.45 C ANISOU 947 CB GLN A 147 3777 4397 4153 -135 217 -1188 C ATOM 948 CG GLN A 147 -24.772 -6.644 67.097 1.00 35.16 C ANISOU 948 CG GLN A 147 4049 4324 4984 560 -320 17 C ATOM 949 CD GLN A 147 -24.101 -5.297 67.211 1.00 42.50 C ANISOU 949 CD GLN A 147 4480 5179 6487 -329 -197 -859 C ATOM 950 OE1 GLN A 147 -24.768 -4.259 67.271 1.00 36.95 O ANISOU 950 OE1 GLN A 147 4626 4407 5003 -856 -45 -397 O ATOM 951 NE2 GLN A 147 -22.772 -5.304 67.238 1.00 38.46 N ANISOU 951 NE2 GLN A 147 4215 5263 5133 95 -951 -113 N ATOM 952 N HIS A 148 -28.435 -8.285 67.369 1.00 32.01 N ANISOU 952 N HIS A 148 3819 4694 3649 -250 275 -730 N ATOM 953 CA HIS A 148 -29.207 -8.898 68.464 1.00 36.28 C ANISOU 953 CA HIS A 148 4493 4612 4680 -625 299 180 C ATOM 954 C HIS A 148 -29.100 -10.410 68.457 1.00 35.39 C ANISOU 954 C HIS A 148 4083 5078 4284 272 204 -225 C ATOM 955 O HIS A 148 -28.689 -11.017 69.452 1.00 35.30 O ANISOU 955 O HIS A 148 4201 5124 4085 -197 570 -129 O ATOM 956 CB HIS A 148 -30.672 -8.446 68.415 1.00 42.46 C ANISOU 956 CB HIS A 148 5224 4877 6029 295 713 191 C ATOM 957 CG HIS A 148 -31.561 -9.140 69.424 1.00 49.63 C ANISOU 957 CG HIS A 148 5827 7030 5999 -141 634 697 C ATOM 958 ND1 HIS A 148 -31.672 -8.722 70.698 1.00 54.50 N ANISOU 958 ND1 HIS A 148 5492 7306 7909 -512 764 -1968 N ATOM 959 CD2 HIS A 148 -32.382 -10.265 69.304 1.00 52.19 C ANISOU 959 CD2 HIS A 148 5652 7605 6573 -70 -122 -799 C ATOM 960 CE1 HIS A 148 -32.521 -9.533 71.364 1.00 64.16 C ANISOU 960 CE1 HIS A 148 8175 7933 8271 -808 1089 -136 C ATOM 961 NE2 HIS A 148 -32.954 -10.477 70.509 1.00 59.94 N ANISOU 961 NE2 HIS A 148 6780 7743 8249 -1475 949 624 N ATOM 962 N GLU A 149 -29.455 -11.039 67.334 1.00 33.33 N ANISOU 962 N GLU A 149 3473 4447 4742 4 169 -495 N ATOM 963 CA GLU A 149 -29.361 -12.489 67.228 1.00 30.34 C ANISOU 963 CA GLU A 149 3365 4008 4152 102 -207 -157 C ATOM 964 C GLU A 149 -27.938 -13.003 67.381 1.00 27.29 C ANISOU 964 C GLU A 149 3230 3649 3488 -348 -519 -243 C ATOM 965 O GLU A 149 -27.730 -14.036 67.995 1.00 30.29 O ANISOU 965 O GLU A 149 3174 4204 4130 128 336 117 O ATOM 966 CB GLU A 149 -29.917 -13.009 65.896 1.00 33.27 C ANISOU 966 CB GLU A 149 4267 4870 3503 29 -132 201 C ATOM 967 CG GLU A 149 -31.430 -13.003 65.782 1.00 39.75 C ANISOU 967 CG GLU A 149 4557 5913 4631 -51 38 -162 C ATOM 968 CD GLU A 149 -32.123 -13.728 66.922 1.00 43.05 C ANISOU 968 CD GLU A 149 4910 5425 6021 -421 560 92 C ATOM 969 OE1 GLU A 149 -31.846 -14.928 67.158 1.00 38.87 O ANISOU 969 OE1 GLU A 149 4174 5325 5267 -143 696 -817 O ATOM 970 OE2 GLU A 149 -32.956 -13.081 67.585 1.00 50.19 O ANISOU 970 OE2 GLU A 149 5374 5881 7813 -363 1327 -224 O ATOM 971 N VAL A 150 -26.963 -12.323 66.792 1.00 28.13 N ANISOU 971 N VAL A 150 3350 3757 3581 -226 -33 -472 N ATOM 972 CA VAL A 150 -25.568 -12.756 66.967 1.00 31.29 C ANISOU 972 CA VAL A 150 3398 4708 3783 -169 197 57 C ATOM 973 C VAL A 150 -25.167 -12.757 68.457 1.00 30.22 C ANISOU 973 C VAL A 150 3563 3997 3923 -561 193 -93 C ATOM 974 O VAL A 150 -24.662 -13.759 68.980 1.00 34.63 O ANISOU 974 O VAL A 150 3640 5123 4392 30 -370 -374 O ATOM 975 CB VAL A 150 -24.601 -11.923 66.098 1.00 30.58 C ANISOU 975 CB VAL A 150 3392 4810 3416 -253 -21 76 C ATOM 976 CG1 VAL A 150 -23.183 -12.437 66.269 1.00 31.61 C ANISOU 976 CG1 VAL A 150 3491 4836 3684 185 295 -544 C ATOM 977 CG2 VAL A 150 -25.004 -12.027 64.629 1.00 25.25 C ANISOU 977 CG2 VAL A 150 2798 3456 3337 -547 184 243 C ATOM 978 N ARG A 151 -25.434 -11.656 69.154 1.00 36.54 N ANISOU 978 N ARG A 151 4279 5360 4242 -1025 374 -1377 N ATOM 979 CA ARG A 151 -25.102 -11.571 70.592 1.00 35.00 C ANISOU 979 CA ARG A 151 4028 4902 4366 -198 -520 -111 C ATOM 980 C ARG A 151 -25.774 -12.666 71.401 1.00 36.93 C ANISOU 980 C ARG A 151 4594 4752 4683 -258 -336 -106 C ATOM 981 O ARG A 151 -25.132 -13.352 72.206 1.00 33.68 O ANISOU 981 O ARG A 151 3243 5148 4404 -698 -514 -572 O ATOM 982 CB ARG A 151 -25.480 -10.203 71.161 1.00 34.81 C ANISOU 982 CB ARG A 151 4873 5013 3340 1 -904 -233 C ATOM 983 CG ARG A 151 -24.715 -9.057 70.525 1.00 44.74 C ANISOU 983 CG ARG A 151 5444 6337 5216 -881 192 -344 C ATOM 984 CD ARG A 151 -24.087 -8.175 71.585 1.00 55.39 C ANISOU 984 CD ARG A 151 6624 7788 6634 -2327 -113 -1237 C ATOM 985 NE ARG A 151 -22.794 -7.673 71.135 1.00 49.29 N ANISOU 985 NE ARG A 151 6522 6350 5855 -1349 -205 -499 N ATOM 986 CZ ARG A 151 -22.609 -6.481 70.582 1.00 49.78 C ANISOU 986 CZ ARG A 151 6935 6311 5666 -620 -535 -238 C ATOM 987 NH1 ARG A 151 -23.637 -5.657 70.418 1.00 52.42 N ANISOU 987 NH1 ARG A 151 5725 7404 6787 -676 -755 -1762 N ATOM 988 NH2 ARG A 151 -21.391 -6.111 70.201 1.00 54.45 N ANISOU 988 NH2 ARG A 151 6897 8180 5610 26 490 -1132 N ATOM 989 N LYS A 152 -27.073 -12.834 71.173 1.00 38.76 N ANISOU 989 N LYS A 152 3978 6017 4729 -260 908 -433 N ATOM 990 CA LYS A 152 -27.842 -13.873 71.841 1.00 35.84 C ANISOU 990 CA LYS A 152 5031 4595 3989 -363 -464 -313 C ATOM 991 C LYS A 152 -27.192 -15.238 71.622 1.00 35.24 C ANISOU 991 C LYS A 152 4095 5064 4227 -200 -184 2 C ATOM 992 O LYS A 152 -27.064 -16.030 72.555 1.00 35.51 O ANISOU 992 O LYS A 152 4126 5237 4126 -234 495 131 O ATOM 993 CB LYS A 152 -29.279 -13.845 71.315 1.00 45.36 C ANISOU 993 CB LYS A 152 4620 7267 5347 -371 -192 -405 C ATOM 994 CG LYS A 152 -30.332 -14.512 72.180 1.00 53.11 C ANISOU 994 CG LYS A 152 6389 8272 5518 -233 -79 2416 C ATOM 995 CD LYS A 152 -31.718 -14.108 71.691 1.00 58.54 C ANISOU 995 CD LYS A 152 5818 8760 7664 -939 -826 569 C ATOM 996 CE LYS A 152 -32.769 -15.132 72.078 1.00 64.30 C ANISOU 996 CE LYS A 152 7144 8824 8462 -1196 -1675 3808 C ATOM 997 NZ LYS A 152 -33.996 -14.981 71.244 1.00 57.34 N ANISOU 997 NZ LYS A 152 5869 9013 6902 678 -378 -937 N ATOM 998 N PHE A 153 -26.755 -15.515 70.396 1.00 32.33 N ANISOU 998 N PHE A 153 2952 4675 4655 -353 -25 -440 N ATOM 999 CA PHE A 153 -26.170 -16.824 70.111 1.00 32.59 C ANISOU 999 CA PHE A 153 4249 4158 3973 -4 -285 231 C ATOM 1000 C PHE A 153 -24.830 -17.013 70.813 1.00 30.75 C ANISOU 1000 C PHE A 153 3972 4003 3705 -59 102 -237 C ATOM 1001 O PHE A 153 -24.551 -18.087 71.370 1.00 31.47 O ANISOU 1001 O PHE A 153 3953 4223 3779 357 319 -370 O ATOM 1002 CB PHE A 153 -25.989 -17.048 68.612 1.00 33.75 C ANISOU 1002 CB PHE A 153 4616 4260 3947 149 110 -4 C ATOM 1003 CG PHE A 153 -25.300 -18.336 68.289 1.00 31.82 C ANISOU 1003 CG PHE A 153 4309 4298 3481 8 419 40 C ATOM 1004 CD1 PHE A 153 -23.905 -18.407 68.256 1.00 32.26 C ANISOU 1004 CD1 PHE A 153 4142 4869 3245 398 -118 235 C ATOM 1005 CD2 PHE A 153 -26.036 -19.489 68.047 1.00 31.58 C ANISOU 1005 CD2 PHE A 153 4126 4408 3465 -248 210 170 C ATOM 1006 CE1 PHE A 153 -23.264 -19.606 67.976 1.00 30.61 C ANISOU 1006 CE1 PHE A 153 3437 4419 3774 -150 -2 138 C ATOM 1007 CE2 PHE A 153 -25.397 -20.692 67.765 1.00 33.94 C ANISOU 1007 CE2 PHE A 153 4293 4629 3972 -217 -543 -494 C ATOM 1008 CZ PHE A 153 -24.008 -20.753 67.729 1.00 32.20 C ANISOU 1008 CZ PHE A 153 4347 4376 3511 -438 378 162 C ATOM 1009 N MET A 154 -23.997 -15.975 70.768 1.00 32.13 N ANISOU 1009 N MET A 154 4125 4485 3597 -515 492 -744 N ATOM 1010 CA MET A 154 -22.684 -16.027 71.397 1.00 36.94 C ANISOU 1010 CA MET A 154 4328 5322 4386 -327 -91 118 C ATOM 1011 C MET A 154 -22.810 -16.155 72.911 1.00 39.91 C ANISOU 1011 C MET A 154 5391 5170 4601 -82 61 -55 C ATOM 1012 O MET A 154 -22.076 -16.926 73.538 1.00 39.17 O ANISOU 1012 O MET A 154 4532 6051 4298 -529 -428 -431 O ATOM 1013 CB MET A 154 -21.880 -14.779 71.046 1.00 37.03 C ANISOU 1013 CB MET A 154 4732 4739 4596 49 25 230 C ATOM 1014 CG MET A 154 -21.623 -14.641 69.564 1.00 36.68 C ANISOU 1014 CG MET A 154 4855 4580 4499 118 -405 204 C ATOM 1015 SD MET A 154 -20.591 -13.232 69.144 1.00 40.39 S ANISOU 1015 SD MET A 154 4643 5540 5161 -380 -962 146 S ATOM 1016 CE MET A 154 -20.315 -13.615 67.425 1.00 57.54 C ANISOU 1016 CE MET A 154 8034 7527 6299 252 466 -655 C ATOM 1017 N ALA A 155 -23.745 -15.403 73.489 1.00 41.93 N ANISOU 1017 N ALA A 155 5007 5455 5467 -399 67 -689 N ATOM 1018 CA ALA A 155 -23.989 -15.446 74.929 1.00 44.42 C ANISOU 1018 CA ALA A 155 5918 5786 5172 672 -324 -651 C ATOM 1019 C ALA A 155 -24.427 -16.838 75.375 1.00 49.86 C ANISOU 1019 C ALA A 155 5916 7086 5940 -1259 -470 -298 C ATOM 1020 O ALA A 155 -23.968 -17.335 76.403 1.00 52.19 O ANISOU 1020 O ALA A 155 5865 8381 5581 -311 -249 -1144 O ATOM 1021 CB ALA A 155 -25.016 -14.401 75.334 1.00 43.97 C ANISOU 1021 CB ALA A 155 5191 6430 5085 713 -658 -705 C ATOM 1022 N ALA A 156 -25.293 -17.480 74.594 1.00 45.81 N ANISOU 1022 N ALA A 156 5614 6577 5214 -385 -510 -28 N ATOM 1023 CA ALA A 156 -25.767 -18.820 74.932 1.00 40.57 C ANISOU 1023 CA ALA A 156 5279 5764 4370 46 5 -533 C ATOM 1024 C ALA A 156 -24.732 -19.924 74.688 1.00 45.33 C ANISOU 1024 C ALA A 156 4682 6298 6242 192 407 309 C ATOM 1025 O ALA A 156 -24.635 -20.863 75.483 1.00 45.31 O ANISOU 1025 O ALA A 156 4871 6719 5623 59 805 -71 O ATOM 1026 CB ALA A 156 -27.059 -19.135 74.181 1.00 45.52 C ANISOU 1026 CB ALA A 156 4241 6902 6150 -694 398 -233 C ATOM 1027 N ASN A 157 -24.103 -19.899 73.513 1.00 40.45 N ANISOU 1027 N ASN A 157 5097 5388 4882 -192 -148 -621 N ATOM 1028 CA ASN A 157 -23.256 -21.008 73.063 1.00 42.71 C ANISOU 1028 CA ASN A 157 5469 5599 5157 41 -154 -861 C ATOM 1029 C ASN A 157 -21.743 -20.793 73.126 1.00 41.21 C ANISOU 1029 C ASN A 157 5704 5350 4603 140 -412 -613 C ATOM 1030 O ASN A 157 -20.970 -21.721 72.889 1.00 43.47 O ANISOU 1030 O ASN A 157 6152 5538 4824 470 -76 1353 O ATOM 1031 CB ASN A 157 -23.656 -21.435 71.647 1.00 40.03 C ANISOU 1031 CB ASN A 157 4936 5592 4679 -213 -54 -50 C ATOM 1032 CG ASN A 157 -25.090 -21.918 71.567 1.00 40.59 C ANISOU 1032 CG ASN A 157 5413 5473 4536 -248 -1240 -223 C ATOM 1033 OD1 ASN A 157 -25.396 -23.053 71.933 1.00 55.66 O ANISOU 1033 OD1 ASN A 157 7221 6307 7619 -1582 -1121 285 O ATOM 1034 ND2 ASN A 157 -25.979 -21.057 71.087 1.00 39.50 N ANISOU 1034 ND2 ASN A 157 3077 5882 6046 -292 35 156 N ATOM 1035 N TRP A 158 -21.327 -19.576 73.448 1.00 41.53 N ANISOU 1035 N TRP A 158 5782 6115 3881 -1117 -571 640 N ATOM 1036 CA TRP A 158 -19.918 -19.258 73.568 1.00 45.13 C ANISOU 1036 CA TRP A 158 5746 6119 5282 -564 -544 434 C ATOM 1037 C TRP A 158 -19.759 -18.558 74.871 1.00 47.71 C ANISOU 1037 C TRP A 158 6485 5892 5748 -1146 554 -523 C ATOM 1038 O TRP A 158 -19.584 -17.321 74.921 1.00 35.72 O ANISOU 1038 O TRP A 158 4238 5105 4227 -122 -83 -367 O ATOM 1039 CB TRP A 158 -19.468 -18.361 72.424 1.00 39.27 C ANISOU 1039 CB TRP A 158 4342 6030 4547 350 964 -552 C ATOM 1040 CG TRP A 158 -19.573 -19.012 71.066 1.00 35.39 C ANISOU 1040 CG TRP A 158 4664 4108 4674 294 403 194 C ATOM 1041 CD1 TRP A 158 -19.972 -20.314 70.777 1.00 36.98 C ANISOU 1041 CD1 TRP A 158 4264 5473 4312 -240 -292 -722 C ATOM 1042 CD2 TRP A 158 -19.274 -18.408 69.759 1.00 32.46 C ANISOU 1042 CD2 TRP A 158 3990 4190 4153 361 266 -46 C ATOM 1043 NE1 TRP A 158 -19.941 -20.547 69.426 1.00 32.08 N ANISOU 1043 NE1 TRP A 158 3665 4320 4200 102 209 177 N ATOM 1044 CE2 TRP A 158 -19.532 -19.447 68.759 1.00 33.67 C ANISOU 1044 CE2 TRP A 158 4496 4355 3943 40 143 176 C ATOM 1045 CE3 TRP A 158 -18.837 -17.162 69.337 1.00 34.49 C ANISOU 1045 CE3 TRP A 158 4197 4510 4396 207 334 450 C ATOM 1046 CZ2 TRP A 158 -19.353 -19.222 67.406 1.00 32.89 C ANISOU 1046 CZ2 TRP A 158 4163 4202 4132 -29 -161 31 C ATOM 1047 CZ3 TRP A 158 -18.660 -16.948 67.968 1.00 34.91 C ANISOU 1047 CZ3 TRP A 158 3944 5275 4045 802 -51 -338 C ATOM 1048 CH2 TRP A 158 -18.913 -17.954 67.028 1.00 29.98 C ANISOU 1048 CH2 TRP A 158 3189 4289 3911 513 -146 235 C ATOM 1049 N ASP A 159 -19.843 -19.325 75.950 1.00 48.33 N ANISOU 1049 N ASP A 159 6118 6165 6080 -104 -53 482 N ATOM 1050 CA ASP A 159 -20.041 -18.736 77.279 1.00 51.46 C ANISOU 1050 CA ASP A 159 6441 7891 5217 -824 -77 573 C ATOM 1051 C ASP A 159 -18.879 -18.873 78.262 1.00 51.97 C ANISOU 1051 C ASP A 159 6491 7079 6173 18 -466 -403 C ATOM 1052 O ASP A 159 -18.905 -18.257 79.321 1.00 56.59 O ANISOU 1052 O ASP A 159 7951 7516 6031 -122 480 -474 O ATOM 1053 CB ASP A 159 -21.355 -19.241 77.914 1.00 48.56 C ANISOU 1053 CB ASP A 159 6266 7470 4713 -94 406 -169 C ATOM 1054 CG ASP A 159 -21.475 -20.770 77.919 1.00 58.61 C ANISOU 1054 CG ASP A 159 6944 7982 7342 -654 86 -315 C ATOM 1055 OD1 ASP A 159 -20.698 -21.460 77.225 1.00 60.50 O ANISOU 1055 OD1 ASP A 159 6444 9265 7276 -718 1436 922 O ATOM 1056 OD2 ASP A 159 -22.369 -21.290 78.621 1.00 55.82 O ANISOU 1056 OD2 ASP A 159 7123 8833 5254 -572 -858 407 O ATOM 1057 N LYS A 160 -17.873 -19.675 77.919 1.00 51.81 N ANISOU 1057 N LYS A 160 6873 7729 5081 197 396 -143 N ATOM 1058 CA LYS A 160 -16.697 -19.845 78.778 1.00 45.29 C ANISOU 1058 CA LYS A 160 6215 6120 4872 243 823 -168 C ATOM 1059 C LYS A 160 -15.630 -18.801 78.449 1.00 51.07 C ANISOU 1059 C LYS A 160 5772 7190 6440 -384 -575 272 C ATOM 1060 O LYS A 160 -15.834 -17.922 77.608 1.00 52.20 O ANISOU 1060 O LYS A 160 6043 6845 6944 -253 0 294 O ATOM 1061 CB LYS A 160 -16.098 -21.248 78.619 1.00 43.61 C ANISOU 1061 CB LYS A 160 6409 6069 4090 565 -55 1183 C ATOM 1062 CG LYS A 160 -17.097 -22.391 78.470 1.00 54.19 C ANISOU 1062 CG LYS A 160 6014 8046 6530 47 -225 -462 C ATOM 1063 CD LYS A 160 -17.717 -22.794 79.801 1.00 69.22 C ANISOU 1063 CD LYS A 160 10104 8906 7289 -456 -470 2905 C ATOM 1064 CE LYS A 160 -18.480 -24.111 79.696 1.00 82.08 C ANISOU 1064 CE LYS A 160 11000 9259 10928 -669 -620 1895 C ATOM 1065 NZ LYS A 160 -18.871 -24.636 81.039 1.00 82.12 N ANISOU 1065 NZ LYS A 160 11002 9029 11171 1397 -272 2225 N ATOM 1066 N ASP A 161 -14.487 -18.905 79.119 1.00 47.87 N ANISOU 1066 N ASP A 161 6026 6702 5460 -381 -511 -110 N ATOM 1067 CA ASP A 161 -13.323 -18.109 78.771 1.00 45.72 C ANISOU 1067 CA ASP A 161 5481 6185 5705 223 164 -601 C ATOM 1068 C ASP A 161 -12.829 -18.583 77.427 1.00 38.39 C ANISOU 1068 C ASP A 161 4881 5445 4258 403 -1638 47 C ATOM 1069 O ASP A 161 -12.390 -17.792 76.593 1.00 47.84 O ANISOU 1069 O ASP A 161 5584 6775 5816 -949 -1168 279 O ATOM 1070 CB ASP A 161 -12.222 -18.288 79.816 1.00 48.13 C ANISOU 1070 CB ASP A 161 6324 6283 5679 240 -55 290 C ATOM 1071 CG ASP A 161 -12.438 -17.426 81.041 1.00 55.84 C ANISOU 1071 CG ASP A 161 7525 7529 6163 -118 384 -371 C ATOM 1072 OD1 ASP A 161 -13.474 -16.728 81.106 1.00 59.28 O ANISOU 1072 OD1 ASP A 161 8792 8195 5537 901 618 -1239 O ATOM 1073 OD2 ASP A 161 -11.566 -17.439 81.935 1.00 62.29 O ANISOU 1073 OD2 ASP A 161 8654 8869 6143 -1008 -54 2366 O ATOM 1074 N GLU A 162 -12.883 -19.896 77.240 1.00 40.88 N ANISOU 1074 N GLU A 162 5320 5618 4593 -102 -682 334 N ATOM 1075 CA GLU A 162 -12.594 -20.497 75.954 1.00 45.44 C ANISOU 1075 CA GLU A 162 5431 6325 5507 -43 -754 -687 C ATOM 1076 C GLU A 162 -13.389 -21.771 75.804 1.00 46.52 C ANISOU 1076 C GLU A 162 6124 5582 5966 -95 295 285 C ATOM 1077 O GLU A 162 -13.939 -22.290 76.782 1.00 44.02 O ANISOU 1077 O GLU A 162 5329 7188 4206 39 -1434 614 O ATOM 1078 CB GLU A 162 -11.096 -20.750 75.763 1.00 46.68 C ANISOU 1078 CB GLU A 162 6016 6143 5577 881 115 -928 C ATOM 1079 CG GLU A 162 -10.440 -21.671 76.775 1.00 56.06 C ANISOU 1079 CG GLU A 162 7827 7934 5537 1189 586 760 C ATOM 1080 CD GLU A 162 -8.928 -21.580 76.702 1.00 78.84 C ANISOU 1080 CD GLU A 162 7983 9332 12641 90 -1815 -671 C ATOM 1081 OE1 GLU A 162 -8.381 -20.497 77.016 1.00 80.54 O ANISOU 1081 OE1 GLU A 162 10098 9649 10852 -621 -2269 87 O ATOM 1082 OE2 GLU A 162 -8.287 -22.584 76.319 1.00 79.81 O ANISOU 1082 OE2 GLU A 162 9396 9982 10943 305 -332 373 O ATOM 1083 N GLY A 163 -13.466 -22.254 74.568 1.00 44.14 N ANISOU 1083 N GLY A 163 5251 5900 5618 229 -339 207 N ATOM 1084 CA GLY A 163 -14.171 -23.481 74.268 1.00 43.35 C ANISOU 1084 CA GLY A 163 5538 5973 4958 6 -1011 495 C ATOM 1085 C GLY A 163 -14.011 -23.882 72.818 1.00 46.17 C ANISOU 1085 C GLY A 163 5777 5586 6177 -104 523 -567 C ATOM 1086 O GLY A 163 -13.569 -23.089 71.973 1.00 48.20 O ANISOU 1086 O GLY A 163 5453 6851 6010 545 660 -70 O ATOM 1087 N GLU A 164 -14.379 -25.125 72.538 1.00 40.67 N ANISOU 1087 N GLU A 164 4853 5466 5134 19 -425 -359 N ATOM 1088 CA GLU A 164 -14.297 -25.676 71.212 1.00 39.54 C ANISOU 1088 CA GLU A 164 4898 5303 4820 579 616 75 C ATOM 1089 C GLU A 164 -15.695 -25.724 70.566 1.00 48.46 C ANISOU 1089 C GLU A 164 5301 7421 5691 -89 183 795 C ATOM 1090 O GLU A 164 -16.676 -26.115 71.208 1.00 41.23 O ANISOU 1090 O GLU A 164 4971 5652 5041 474 -428 1325 O ATOM 1091 CB GLU A 164 -13.650 -27.064 71.277 1.00 34.60 C ANISOU 1091 CB GLU A 164 4022 4722 4402 -305 6 1217 C ATOM 1092 CG GLU A 164 -13.476 -27.725 69.914 1.00 47.37 C ANISOU 1092 CG GLU A 164 6054 5947 5994 308 211 -380 C ATOM 1093 CD GLU A 164 -12.455 -28.847 69.917 1.00 50.89 C ANISOU 1093 CD GLU A 164 6365 6263 6706 664 -433 -374 C ATOM 1094 OE1 GLU A 164 -11.501 -28.786 70.723 1.00 53.31 O ANISOU 1094 OE1 GLU A 164 6595 6800 6859 1127 -632 -460 O ATOM 1095 OE2 GLU A 164 -12.599 -29.781 69.095 1.00 52.35 O ANISOU 1095 OE2 GLU A 164 6746 6212 6933 -430 -1047 -10 O ATOM 1096 N ILE A 165 -15.772 -25.296 69.306 1.00 43.44 N ANISOU 1096 N ILE A 165 4863 6342 5298 923 -85 63 N ATOM 1097 CA ILE A 165 -17.013 -25.282 68.536 1.00 38.28 C ANISOU 1097 CA ILE A 165 4585 5145 4812 -114 214 -25 C ATOM 1098 C ILE A 165 -16.731 -25.767 67.122 1.00 43.43 C ANISOU 1098 C ILE A 165 5278 6227 4993 -801 -194 -770 C ATOM 1099 O ILE A 165 -15.564 -25.831 66.710 1.00 40.95 O ANISOU 1099 O ILE A 165 5062 5988 4507 -441 -694 -89 O ATOM 1100 CB ILE A 165 -17.585 -23.848 68.434 1.00 40.59 C ANISOU 1100 CB ILE A 165 5147 5500 4775 347 564 615 C ATOM 1101 CG1 ILE A 165 -16.534 -22.897 67.846 1.00 39.21 C ANISOU 1101 CG1 ILE A 165 4126 5141 5629 30 -399 201 C ATOM 1102 CG2 ILE A 165 -18.049 -23.346 69.797 1.00 35.16 C ANISOU 1102 CG2 ILE A 165 4051 4580 4729 149 -329 105 C ATOM 1103 CD1 ILE A 165 -17.076 -21.582 67.336 1.00 34.30 C ANISOU 1103 CD1 ILE A 165 4431 4448 4152 -596 -724 -302 C ATOM 1104 N ASN A 166 -17.789 -26.123 66.390 1.00 34.46 N ANISOU 1104 N ASN A 166 3811 5097 4182 -371 388 908 N ATOM 1105 CA ASN A 166 -17.701 -26.288 64.939 1.00 34.73 C ANISOU 1105 CA ASN A 166 4235 4383 4577 25 -129 -68 C ATOM 1106 C ASN A 166 -18.176 -24.968 64.341 1.00 35.33 C ANISOU 1106 C ASN A 166 4117 5049 4257 340 389 572 C ATOM 1107 O ASN A 166 -19.342 -24.571 64.481 1.00 29.86 O ANISOU 1107 O ASN A 166 3595 4488 3263 -164 483 429 O ATOM 1108 CB ASN A 166 -18.508 -27.503 64.433 1.00 33.17 C ANISOU 1108 CB ASN A 166 3772 4580 4249 -177 632 -151 C ATOM 1109 CG ASN A 166 -18.321 -27.763 62.937 1.00 32.03 C ANISOU 1109 CG ASN A 166 3998 3918 4251 74 -197 211 C ATOM 1110 OD1 ASN A 166 -18.711 -26.948 62.110 1.00 31.46 O ANISOU 1110 OD1 ASN A 166 3842 4115 3995 -539 -249 361 O ATOM 1111 ND2 ASN A 166 -17.745 -28.920 62.585 1.00 32.38 N ANISOU 1111 ND2 ASN A 166 3926 4258 4116 345 -109 215 N ATOM 1112 N LEU A 167 -17.250 -24.256 63.712 1.00 33.08 N ANISOU 1112 N LEU A 167 3836 4136 4596 -219 -280 62 N ATOM 1113 CA LEU A 167 -17.536 -22.905 63.253 1.00 31.03 C ANISOU 1113 CA LEU A 167 3881 4232 3674 -139 2 177 C ATOM 1114 C LEU A 167 -18.575 -22.879 62.143 1.00 27.57 C ANISOU 1114 C LEU A 167 3306 3645 3525 -142 291 147 C ATOM 1115 O LEU A 167 -19.388 -21.953 62.065 1.00 27.14 O ANISOU 1115 O LEU A 167 3505 3673 3134 18 43 -214 O ATOM 1116 CB LEU A 167 -16.254 -22.218 62.794 1.00 28.32 C ANISOU 1116 CB LEU A 167 3520 3776 3463 -47 -101 -369 C ATOM 1117 CG LEU A 167 -16.316 -20.732 62.459 1.00 32.53 C ANISOU 1117 CG LEU A 167 4062 4094 4201 -417 576 196 C ATOM 1118 CD1 LEU A 167 -16.762 -19.943 63.684 1.00 32.69 C ANISOU 1118 CD1 LEU A 167 3723 3992 4705 303 -613 -430 C ATOM 1119 CD2 LEU A 167 -14.937 -20.280 61.969 1.00 29.47 C ANISOU 1119 CD2 LEU A 167 3174 3797 4223 101 -182 354 C ATOM 1120 N LEU A 168 -18.539 -23.884 61.275 1.00 28.97 N ANISOU 1120 N LEU A 168 3358 3750 3900 -394 -76 -44 N ATOM 1121 CA LEU A 168 -19.468 -23.924 60.159 1.00 27.76 C ANISOU 1121 CA LEU A 168 3415 3520 3610 -407 -29 -51 C ATOM 1122 C LEU A 168 -20.891 -24.136 60.671 1.00 28.28 C ANISOU 1122 C LEU A 168 3319 3989 3435 126 44 195 C ATOM 1123 O LEU A 168 -21.812 -23.480 60.212 1.00 25.64 O ANISOU 1123 O LEU A 168 3206 3311 3226 -103 425 340 O ATOM 1124 CB LEU A 168 -19.078 -25.008 59.155 1.00 28.67 C ANISOU 1124 CB LEU A 168 3812 3852 3226 -145 353 126 C ATOM 1125 CG LEU A 168 -20.046 -25.189 57.984 1.00 31.28 C ANISOU 1125 CG LEU A 168 4014 3895 3974 51 -97 -171 C ATOM 1126 CD1 LEU A 168 -20.015 -23.973 57.061 1.00 33.93 C ANISOU 1126 CD1 LEU A 168 4616 4277 3996 188 471 -145 C ATOM 1127 CD2 LEU A 168 -19.722 -26.468 57.214 1.00 30.51 C ANISOU 1127 CD2 LEU A 168 3990 3850 3750 -298 325 -122 C ATOM 1128 N GLU A 169 -21.077 -25.045 61.623 1.00 30.94 N ANISOU 1128 N GLU A 169 3815 4240 3699 -266 -14 345 N ATOM 1129 CA GLU A 169 -22.411 -25.225 62.222 1.00 32.10 C ANISOU 1129 CA GLU A 169 3927 4248 4018 -246 130 267 C ATOM 1130 C GLU A 169 -22.911 -23.972 62.920 1.00 29.20 C ANISOU 1130 C GLU A 169 3550 3930 3612 -515 326 506 C ATOM 1131 O GLU A 169 -24.070 -23.582 62.762 1.00 30.44 O ANISOU 1131 O GLU A 169 3588 4193 3784 -804 -346 545 O ATOM 1132 CB GLU A 169 -22.401 -26.338 63.244 1.00 35.98 C ANISOU 1132 CB GLU A 169 4884 4626 4161 -321 -458 496 C ATOM 1133 CG GLU A 169 -22.119 -27.702 62.671 1.00 49.23 C ANISOU 1133 CG GLU A 169 6596 5871 6237 1568 -26 160 C ATOM 1134 CD GLU A 169 -22.221 -28.754 63.745 1.00 55.31 C ANISOU 1134 CD GLU A 169 7470 6629 6917 733 1420 767 C ATOM 1135 OE1 GLU A 169 -22.892 -28.470 64.769 1.00 47.34 O ANISOU 1135 OE1 GLU A 169 6732 5569 5686 -847 304 695 O ATOM 1136 OE2 GLU A 169 -21.626 -29.841 63.570 1.00 55.42 O ANISOU 1136 OE2 GLU A 169 6808 6532 7714 526 -825 1286 O ATOM 1137 N ASP A 170 -22.046 -23.349 63.715 1.00 30.31 N ANISOU 1137 N ASP A 170 3632 4482 3402 -86 34 -6 N ATOM 1138 CA ASP A 170 -22.438 -22.145 64.436 1.00 28.84 C ANISOU 1138 CA ASP A 170 3419 3626 3911 -432 104 82 C ATOM 1139 C ASP A 170 -22.764 -20.972 63.513 1.00 28.08 C ANISOU 1139 C ASP A 170 3241 4064 3362 87 -127 22 C ATOM 1140 O ASP A 170 -23.738 -20.270 63.739 1.00 27.73 O ANISOU 1140 O ASP A 170 3406 3493 3634 -255 522 -535 O ATOM 1141 CB ASP A 170 -21.383 -21.746 65.484 1.00 32.99 C ANISOU 1141 CB ASP A 170 3590 4965 3979 338 -418 81 C ATOM 1142 CG ASP A 170 -21.270 -22.760 66.619 1.00 37.49 C ANISOU 1142 CG ASP A 170 5193 4494 4556 -535 -84 278 C ATOM 1143 OD1 ASP A 170 -21.855 -23.866 66.505 1.00 31.12 O ANISOU 1143 OD1 ASP A 170 3692 4109 4021 -90 576 163 O ATOM 1144 OD2 ASP A 170 -20.589 -22.450 67.625 1.00 38.59 O ANISOU 1144 OD2 ASP A 170 4853 5040 4767 -323 -61 315 O ATOM 1145 N CYS A 171 -21.955 -20.738 62.484 1.00 29.23 N ANISOU 1145 N CYS A 171 3719 4239 3145 353 39 110 N ATOM 1146 CA CYS A 171 -22.297 -19.696 61.508 1.00 30.02 C ANISOU 1146 CA CYS A 171 3226 4076 4102 89 17 525 C ATOM 1147 C CYS A 171 -23.631 -19.973 60.748 1.00 25.52 C ANISOU 1147 C CYS A 171 3069 3237 3389 19 511 6 C ATOM 1148 O CYS A 171 -24.406 -19.051 60.485 1.00 25.99 O ANISOU 1148 O CYS A 171 2820 3863 3192 101 84 146 O ATOM 1149 CB CYS A 171 -21.144 -19.469 60.515 1.00 28.05 C ANISOU 1149 CB CYS A 171 3231 3468 3956 -149 -58 70 C ATOM 1150 SG CYS A 171 -19.707 -18.593 61.223 1.00 28.66 S ANISOU 1150 SG CYS A 171 3156 3880 3851 -259 100 84 S ATOM 1151 N SER A 172 -23.873 -21.227 60.376 1.00 26.97 N ANISOU 1151 N SER A 172 3175 3496 3575 -671 574 41 N ATOM 1152 CA SER A 172 -25.145 -21.613 59.756 1.00 26.77 C ANISOU 1152 CA SER A 172 3519 3653 2997 265 -68 -68 C ATOM 1153 C SER A 172 -26.327 -21.272 60.649 1.00 27.06 C ANISOU 1153 C SER A 172 3183 3596 3501 -82 117 157 C ATOM 1154 O SER A 172 -27.300 -20.703 60.181 1.00 27.80 O ANISOU 1154 O SER A 172 3521 3520 3520 -244 88 603 O ATOM 1155 CB SER A 172 -25.162 -23.102 59.455 1.00 32.25 C ANISOU 1155 CB SER A 172 4381 3683 4186 377 -70 -193 C ATOM 1156 OG SER A 172 -24.068 -23.426 58.621 1.00 36.33 O ANISOU 1156 OG SER A 172 4582 4941 4280 165 101 -73 O ATOM 1157 N THR A 173 -26.233 -21.629 61.929 1.00 28.72 N ANISOU 1157 N THR A 173 3844 3653 3414 -191 301 57 N ATOM 1158 CA THR A 173 -27.269 -21.296 62.930 1.00 30.28 C ANISOU 1158 CA THR A 173 3654 4097 3752 107 328 46 C ATOM 1159 C THR A 173 -27.447 -19.798 63.073 1.00 29.43 C ANISOU 1159 C THR A 173 3829 3943 3411 -122 -6 -38 C ATOM 1160 O THR A 173 -28.576 -19.300 63.106 1.00 30.80 O ANISOU 1160 O THR A 173 3440 4577 3685 -473 226 210 O ATOM 1161 CB THR A 173 -26.925 -21.876 64.313 1.00 31.07 C ANISOU 1161 CB THR A 173 3908 4198 3700 469 737 329 C ATOM 1162 OG1 THR A 173 -26.612 -23.258 64.160 1.00 31.77 O ANISOU 1162 OG1 THR A 173 4270 3792 4009 -337 894 326 O ATOM 1163 CG2 THR A 173 -28.105 -21.704 65.339 1.00 28.34 C ANISOU 1163 CG2 THR A 173 3362 4046 3359 241 351 469 C ATOM 1164 N MET A 174 -26.339 -19.069 63.180 1.00 29.40 N ANISOU 1164 N MET A 174 3667 3722 3779 -349 367 45 N ATOM 1165 CA MET A 174 -26.441 -17.615 63.245 1.00 27.85 C ANISOU 1165 CA MET A 174 3686 3753 3142 -354 -137 -437 C ATOM 1166 C MET A 174 -27.149 -17.039 62.025 1.00 26.40 C ANISOU 1166 C MET A 174 3034 3414 3582 -234 -219 -426 C ATOM 1167 O MET A 174 -28.013 -16.184 62.158 1.00 28.22 O ANISOU 1167 O MET A 174 3483 3636 3602 -78 268 -894 O ATOM 1168 CB MET A 174 -25.065 -16.965 63.443 1.00 27.22 C ANISOU 1168 CB MET A 174 3281 3394 3665 -39 -245 133 C ATOM 1169 CG MET A 174 -24.583 -17.069 64.884 1.00 33.34 C ANISOU 1169 CG MET A 174 4067 5043 3556 -675 -269 -114 C ATOM 1170 SD MET A 174 -23.076 -16.129 65.230 1.00 34.55 S ANISOU 1170 SD MET A 174 3937 4608 4583 -282 -38 -462 S ATOM 1171 CE MET A 174 -21.860 -17.151 64.394 1.00 31.58 C ANISOU 1171 CE MET A 174 4137 4075 3786 269 -570 -112 C ATOM 1172 N ILE A 175 -26.793 -17.517 60.834 1.00 25.19 N ANISOU 1172 N ILE A 175 2616 3734 3220 -502 -110 -75 N ATOM 1173 CA ILE A 175 -27.384 -16.989 59.600 1.00 21.88 C ANISOU 1173 CA ILE A 175 2720 2654 2936 -343 235 199 C ATOM 1174 C ILE A 175 -28.884 -17.274 59.516 1.00 23.77 C ANISOU 1174 C ILE A 175 2877 3147 3005 -110 16 -43 C ATOM 1175 O ILE A 175 -29.645 -16.403 59.093 1.00 25.53 O ANISOU 1175 O ILE A 175 3006 3034 3659 -282 -94 -81 O ATOM 1176 CB ILE A 175 -26.632 -17.476 58.334 1.00 22.95 C ANISOU 1176 CB ILE A 175 2885 2940 2895 -328 -207 -453 C ATOM 1177 CG1 ILE A 175 -25.298 -16.721 58.175 1.00 25.19 C ANISOU 1177 CG1 ILE A 175 2858 3088 3624 -80 550 79 C ATOM 1178 CG2 ILE A 175 -27.463 -17.285 57.067 1.00 20.59 C ANISOU 1178 CG2 ILE A 175 2364 2615 2842 83 224 369 C ATOM 1179 CD1 ILE A 175 -25.434 -15.273 57.721 1.00 22.52 C ANISOU 1179 CD1 ILE A 175 2612 3001 2942 8 55 -218 C ATOM 1180 N ILE A 176 -29.333 -18.465 59.918 1.00 25.05 N ANISOU 1180 N ILE A 176 2985 3109 3422 -287 245 -305 N ATOM 1181 CA ILE A 176 -30.795 -18.680 59.901 1.00 30.56 C ANISOU 1181 CA ILE A 176 3224 3813 4571 -349 40 -339 C ATOM 1182 C ILE A 176 -31.496 -17.780 60.921 1.00 29.39 C ANISOU 1182 C ILE A 176 3307 4116 3741 -161 236 78 C ATOM 1183 O ILE A 176 -32.504 -17.138 60.602 1.00 26.74 O ANISOU 1183 O ILE A 176 3343 3350 3464 -468 186 103 O ATOM 1184 CB ILE A 176 -31.246 -20.158 60.018 1.00 29.11 C ANISOU 1184 CB ILE A 176 3631 3661 3768 -58 -202 76 C ATOM 1185 CG1 ILE A 176 -32.756 -20.251 59.752 1.00 35.01 C ANISOU 1185 CG1 ILE A 176 3765 4354 5181 202 -95 -164 C ATOM 1186 CG2 ILE A 176 -30.889 -20.761 61.373 1.00 26.15 C ANISOU 1186 CG2 ILE A 176 2967 3617 3350 -390 223 -3 C ATOM 1187 CD1 ILE A 176 -33.229 -21.601 59.269 1.00 37.78 C ANISOU 1187 CD1 ILE A 176 4571 5089 4694 -573 203 -541 C ATOM 1188 N ASN A 177 -30.945 -17.703 62.129 1.00 31.90 N ANISOU 1188 N ASN A 177 3781 4647 3690 -690 147 -159 N ATOM 1189 CA ASN A 177 -31.507 -16.814 63.147 1.00 27.65 C ANISOU 1189 CA ASN A 177 3236 3804 3465 -1158 518 223 C ATOM 1190 C ASN A 177 -31.530 -15.363 62.714 1.00 29.22 C ANISOU 1190 C ASN A 177 3426 4137 3537 14 -72 304 C ATOM 1191 O ASN A 177 -32.533 -14.683 62.911 1.00 34.39 O ANISOU 1191 O ASN A 177 3309 5303 4454 -323 1168 -567 O ATOM 1192 CB ASN A 177 -30.751 -16.938 64.477 1.00 30.00 C ANISOU 1192 CB ASN A 177 3363 4305 3728 -95 398 -122 C ATOM 1193 CG ASN A 177 -30.799 -18.344 65.055 1.00 34.73 C ANISOU 1193 CG ASN A 177 4382 4324 4487 -261 -171 -102 C ATOM 1194 OD1 ASN A 177 -31.424 -19.232 64.498 1.00 35.44 O ANISOU 1194 OD1 ASN A 177 4190 4171 5104 -498 177 -226 O ATOM 1195 ND2 ASN A 177 -30.120 -18.549 66.171 1.00 35.54 N ANISOU 1195 ND2 ASN A 177 4789 4682 4033 -106 610 1405 N ATOM 1196 N THR A 178 -30.430 -14.876 62.123 1.00 25.46 N ANISOU 1196 N THR A 178 3049 3396 3228 124 -128 10 N ATOM 1197 CA THR A 178 -30.357 -13.474 61.767 1.00 23.56 C ANISOU 1197 CA THR A 178 2784 3370 2798 -148 98 188 C ATOM 1198 C THR A 178 -31.267 -13.182 60.587 1.00 24.09 C ANISOU 1198 C THR A 178 2483 3288 3381 -266 -172 -66 C ATOM 1199 O THR A 178 -31.955 -12.159 60.591 1.00 24.86 O ANISOU 1199 O THR A 178 2446 3361 3639 -211 324 27 O ATOM 1200 CB THR A 178 -28.920 -12.986 61.418 1.00 26.33 C ANISOU 1200 CB THR A 178 2572 4087 3343 -447 -384 -420 C ATOM 1201 OG1 THR A 178 -28.392 -13.783 60.358 1.00 28.11 O ANISOU 1201 OG1 THR A 178 2554 4290 3835 -976 266 -346 O ATOM 1202 CG2 THR A 178 -27.970 -13.066 62.652 1.00 23.50 C ANISOU 1202 CG2 THR A 178 2842 2883 3204 11 -381 -106 C ATOM 1203 N ALA A 179 -31.250 -14.038 59.562 1.00 26.59 N ANISOU 1203 N ALA A 179 2889 3678 3534 -399 116 -236 N ATOM 1204 CA ALA A 179 -32.147 -13.829 58.416 1.00 26.37 C ANISOU 1204 CA ALA A 179 3217 3614 3188 68 176 -295 C ATOM 1205 C ALA A 179 -33.600 -13.790 58.906 1.00 29.46 C ANISOU 1205 C ALA A 179 3302 3943 3947 -234 328 -38 C ATOM 1206 O ALA A 179 -34.350 -12.889 58.549 1.00 32.05 O ANISOU 1206 O ALA A 179 3402 4206 4568 -64 322 -334 O ATOM 1207 CB ALA A 179 -31.968 -14.907 57.359 1.00 22.00 C ANISOU 1207 CB ALA A 179 2101 3103 3153 247 696 74 C ATOM 1208 N CYS A 180 -33.981 -14.748 59.744 1.00 29.95 N ANISOU 1208 N CYS A 180 3772 3989 3619 -737 258 -317 N ATOM 1209 CA CYS A 180 -35.363 -14.789 60.268 1.00 34.55 C ANISOU 1209 CA CYS A 180 3848 4345 4934 -181 508 -248 C ATOM 1210 C CYS A 180 -35.756 -13.539 61.081 1.00 37.17 C ANISOU 1210 C CYS A 180 4358 4769 4994 245 -176 -773 C ATOM 1211 O CYS A 180 -36.874 -13.009 60.946 1.00 31.80 O ANISOU 1211 O CYS A 180 3631 3866 4583 -567 -81 -53 O ATOM 1212 CB CYS A 180 -35.603 -16.077 61.063 1.00 30.77 C ANISOU 1212 CB CYS A 180 3190 4491 4009 472 1115 -441 C ATOM 1213 SG CYS A 180 -35.718 -17.541 59.997 1.00 34.21 S ANISOU 1213 SG CYS A 180 3649 4719 4628 -709 294 -519 S ATOM 1214 N GLN A 181 -34.828 -13.058 61.902 1.00 37.20 N ANISOU 1214 N GLN A 181 4568 5064 4501 -418 141 -412 N ATOM 1215 CA GLN A 181 -35.058 -11.856 62.703 1.00 35.13 C ANISOU 1215 CA GLN A 181 4201 4872 4273 5 135 -76 C ATOM 1216 C GLN A 181 -35.210 -10.583 61.860 1.00 32.78 C ANISOU 1216 C GLN A 181 3854 4298 4301 -316 -11 -640 C ATOM 1217 O GLN A 181 -35.903 -9.655 62.265 1.00 35.20 O ANISOU 1217 O GLN A 181 4258 4902 4212 -81 307 -880 O ATOM 1218 CB GLN A 181 -33.945 -11.693 63.736 1.00 39.04 C ANISOU 1218 CB GLN A 181 3429 6009 5395 -466 213 -737 C ATOM 1219 CG GLN A 181 -34.230 -10.670 64.821 1.00 42.34 C ANISOU 1219 CG GLN A 181 5040 6150 4895 -248 104 -520 C ATOM 1220 CD GLN A 181 -35.206 -11.174 65.869 1.00 48.39 C ANISOU 1220 CD GLN A 181 5651 6403 6331 194 1260 -379 C ATOM 1221 OE1 GLN A 181 -35.467 -12.375 65.984 1.00 52.14 O ANISOU 1221 OE1 GLN A 181 5361 7446 7003 -1543 15 242 O ATOM 1222 NE2 GLN A 181 -35.742 -10.255 66.647 1.00 46.08 N ANISOU 1222 NE2 GLN A 181 5100 6513 5892 -840 1887 -478 N ATOM 1223 N CYS A 182 -34.583 -10.543 60.683 1.00 31.72 N ANISOU 1223 N CYS A 182 3530 4118 4402 -136 14 -142 N ATOM 1224 CA CYS A 182 -34.721 -9.400 59.793 1.00 33.12 C ANISOU 1224 CA CYS A 182 3728 4736 4117 38 99 154 C ATOM 1225 C CYS A 182 -36.015 -9.448 59.025 1.00 31.82 C ANISOU 1225 C CYS A 182 3193 4218 4678 -189 520 -444 C ATOM 1226 O CYS A 182 -36.649 -8.422 58.804 1.00 34.76 O ANISOU 1226 O CYS A 182 4015 4725 4465 27 402 787 O ATOM 1227 CB CYS A 182 -33.621 -9.389 58.735 1.00 34.75 C ANISOU 1227 CB CYS A 182 3879 4554 4770 -305 469 -340 C ATOM 1228 SG CYS A 182 -32.007 -8.917 59.356 1.00 34.00 S ANISOU 1228 SG CYS A 182 3962 4390 4565 -171 4 -432 S ATOM 1229 N LEU A 183 -36.363 -10.643 58.572 1.00 28.57 N ANISOU 1229 N LEU A 183 2457 4280 4118 -595 824 -413 N ATOM 1230 CA LEU A 183 -37.376 -10.806 57.529 1.00 32.56 C ANISOU 1230 CA LEU A 183 3867 4470 4032 142 18 -492 C ATOM 1231 C LEU A 183 -38.757 -11.183 58.074 1.00 35.89 C ANISOU 1231 C LEU A 183 4281 4865 4489 -287 284 152 C ATOM 1232 O LEU A 183 -39.764 -10.997 57.392 1.00 42.12 O ANISOU 1232 O LEU A 183 4391 5865 5745 -310 -31 127 O ATOM 1233 CB LEU A 183 -36.901 -11.854 56.512 1.00 30.59 C ANISOU 1233 CB LEU A 183 3440 4475 3707 215 298 -177 C ATOM 1234 CG LEU A 183 -35.600 -11.507 55.775 1.00 30.65 C ANISOU 1234 CG LEU A 183 3520 3717 4406 -353 317 -203 C ATOM 1235 CD1 LEU A 183 -35.140 -12.623 54.841 1.00 27.24 C ANISOU 1235 CD1 LEU A 183 2458 4120 3771 -480 351 -60 C ATOM 1236 CD2 LEU A 183 -35.762 -10.205 55.007 1.00 30.11 C ANISOU 1236 CD2 LEU A 183 3104 4314 4020 -302 1012 410 C ATOM 1237 N PHE A 184 -38.808 -11.714 59.293 1.00 37.55 N ANISOU 1237 N PHE A 184 4651 4922 4692 -566 431 293 N ATOM 1238 CA PHE A 184 -40.070 -12.234 59.854 1.00 35.47 C ANISOU 1238 CA PHE A 184 4010 4689 4777 -231 -95 -60 C ATOM 1239 C PHE A 184 -40.505 -11.504 61.113 1.00 37.93 C ANISOU 1239 C PHE A 184 4618 5441 4352 -180 -52 -53 C ATOM 1240 O PHE A 184 -39.694 -11.263 62.011 1.00 34.56 O ANISOU 1240 O PHE A 184 3933 4641 4557 -181 220 -472 O ATOM 1241 CB PHE A 184 -39.955 -13.716 60.213 1.00 33.50 C ANISOU 1241 CB PHE A 184 2934 4645 5147 -1124 663 307 C ATOM 1242 CG PHE A 184 -39.668 -14.625 59.050 1.00 40.29 C ANISOU 1242 CG PHE A 184 4353 5609 5344 -949 62 -206 C ATOM 1243 CD1 PHE A 184 -39.861 -14.212 57.735 1.00 41.92 C ANISOU 1243 CD1 PHE A 184 5008 5703 5216 -2072 526 -75 C ATOM 1244 CD2 PHE A 184 -39.236 -15.925 59.284 1.00 47.94 C ANISOU 1244 CD2 PHE A 184 4752 5718 7743 -423 -155 -699 C ATOM 1245 CE1 PHE A 184 -39.590 -15.065 56.676 1.00 44.97 C ANISOU 1245 CE1 PHE A 184 5373 4353 7359 -1706 514 -682 C ATOM 1246 CE2 PHE A 184 -38.976 -16.784 58.233 1.00 51.14 C ANISOU 1246 CE2 PHE A 184 5355 7528 6546 774 -264 -414 C ATOM 1247 CZ PHE A 184 -39.149 -16.353 56.929 1.00 50.18 C ANISOU 1247 CZ PHE A 184 6064 6285 6716 487 -1274 -469 C ATOM 1248 N GLY A 185 -41.795 -11.194 61.197 1.00 41.19 N ANISOU 1248 N GLY A 185 4782 5963 4906 217 -60 -356 N ATOM 1249 CA GLY A 185 -42.349 -10.588 62.395 1.00 35.51 C ANISOU 1249 CA GLY A 185 3839 4996 4657 -201 47 136 C ATOM 1250 C GLY A 185 -42.190 -11.539 63.560 1.00 29.13 C ANISOU 1250 C GLY A 185 2393 4163 4511 -590 755 -118 C ATOM 1251 O GLY A 185 -42.025 -12.743 63.359 1.00 31.57 O ANISOU 1251 O GLY A 185 2968 4313 4714 -93 628 -895 O ATOM 1252 N GLU A 186 -42.231 -11.011 64.783 1.00 32.24 N ANISOU 1252 N GLU A 186 3414 4510 4326 -775 427 -359 N ATOM 1253 CA GLU A 186 -42.151 -11.866 65.979 1.00 35.50 C ANISOU 1253 CA GLU A 186 4450 4283 4755 -346 -386 65 C ATOM 1254 C GLU A 186 -43.207 -12.980 66.019 1.00 32.41 C ANISOU 1254 C GLU A 186 3995 3991 4326 7 16 51 C ATOM 1255 O GLU A 186 -42.906 -14.103 66.430 1.00 28.70 O ANISOU 1255 O GLU A 186 2798 4256 3848 -470 -148 87 O ATOM 1256 CB GLU A 186 -42.208 -11.050 67.281 1.00 45.35 C ANISOU 1256 CB GLU A 186 5849 6011 5369 -922 170 -1002 C ATOM 1257 CG GLU A 186 -42.009 -11.911 68.530 1.00 60.46 C ANISOU 1257 CG GLU A 186 8108 7802 7060 9 -79 343 C ATOM 1258 CD GLU A 186 -41.819 -11.116 69.817 1.00 76.31 C ANISOU 1258 CD GLU A 186 10350 10386 8256 1818 -1112 -1120 C ATOM 1259 OE1 GLU A 186 -42.463 -10.056 69.986 1.00 69.85 O ANISOU 1259 OE1 GLU A 186 8778 9095 8666 608 684 1272 O ATOM 1260 OE2 GLU A 186 -41.028 -11.567 70.675 1.00 90.78 O ANISOU 1260 OE2 GLU A 186 9719 14195 10577 4008 -445 1815 O ATOM 1261 N ASP A 187 -44.439 -12.675 65.613 1.00 34.86 N ANISOU 1261 N ASP A 187 4152 4834 4259 10 -291 -319 N ATOM 1262 CA ASP A 187 -45.500 -13.692 65.581 1.00 38.83 C ANISOU 1262 CA ASP A 187 4660 4898 5193 -21 -64 -71 C ATOM 1263 C ASP A 187 -45.091 -14.894 64.721 1.00 36.19 C ANISOU 1263 C ASP A 187 5001 4555 4193 -31 -389 283 C ATOM 1264 O ASP A 187 -45.279 -16.051 65.114 1.00 34.67 O ANISOU 1264 O ASP A 187 4607 4645 3918 -1010 -264 -227 O ATOM 1265 CB ASP A 187 -46.839 -13.100 65.094 1.00 37.80 C ANISOU 1265 CB ASP A 187 3676 5488 5196 -480 365 -317 C ATOM 1266 CG ASP A 187 -46.748 -12.455 63.711 1.00 45.90 C ANISOU 1266 CG ASP A 187 5339 6537 5562 71 -559 403 C ATOM 1267 OD1 ASP A 187 -45.639 -12.315 63.129 1.00 49.90 O ANISOU 1267 OD1 ASP A 187 5252 7184 6523 272 -168 264 O ATOM 1268 OD2 ASP A 187 -47.815 -12.070 63.200 1.00 42.15 O ANISOU 1268 OD2 ASP A 187 4049 5695 6270 -431 201 253 O ATOM 1269 N LEU A 188 -44.513 -14.616 63.555 1.00 36.00 N ANISOU 1269 N LEU A 188 3845 4794 5037 -333 585 -118 N ATOM 1270 CA LEU A 188 -44.090 -15.684 62.659 1.00 34.41 C ANISOU 1270 CA LEU A 188 4256 4413 4405 -891 135 -200 C ATOM 1271 C LEU A 188 -42.966 -16.495 63.291 1.00 39.86 C ANISOU 1271 C LEU A 188 5147 4914 5082 -215 -177 -211 C ATOM 1272 O LEU A 188 -43.003 -17.724 63.271 1.00 42.45 O ANISOU 1272 O LEU A 188 5955 5167 5005 -476 485 -296 O ATOM 1273 CB LEU A 188 -43.689 -15.137 61.280 1.00 35.68 C ANISOU 1273 CB LEU A 188 4150 4634 4772 -1160 361 140 C ATOM 1274 CG LEU A 188 -43.210 -16.110 60.187 1.00 41.79 C ANISOU 1274 CG LEU A 188 5705 5426 4747 -743 749 95 C ATOM 1275 CD1 LEU A 188 -43.991 -17.421 60.145 1.00 39.26 C ANISOU 1275 CD1 LEU A 188 5442 3941 5532 663 -172 193 C ATOM 1276 CD2 LEU A 188 -43.265 -15.420 58.830 1.00 39.11 C ANISOU 1276 CD2 LEU A 188 4460 5481 4917 -162 -1495 61 C ATOM 1277 N ARG A 189 -41.981 -15.819 63.876 1.00 39.56 N ANISOU 1277 N ARG A 189 4420 5565 5044 -330 264 -138 N ATOM 1278 CA ARG A 189 -40.881 -16.536 64.522 1.00 41.81 C ANISOU 1278 CA ARG A 189 5102 5772 5011 -245 -10 167 C ATOM 1279 C ARG A 189 -41.344 -17.340 65.731 1.00 45.06 C ANISOU 1279 C ARG A 189 5706 5361 6053 -548 -68 588 C ATOM 1280 O ARG A 189 -40.715 -18.335 66.080 1.00 50.46 O ANISOU 1280 O ARG A 189 6503 6466 6203 660 -976 -167 O ATOM 1281 CB ARG A 189 -39.757 -15.587 64.923 1.00 42.54 C ANISOU 1281 CB ARG A 189 4528 6330 5302 -558 440 774 C ATOM 1282 CG ARG A 189 -39.229 -14.747 63.771 1.00 37.03 C ANISOU 1282 CG ARG A 189 4066 5020 4981 -856 717 -19 C ATOM 1283 CD ARG A 189 -38.021 -13.964 64.239 1.00 42.87 C ANISOU 1283 CD ARG A 189 5502 5670 5117 -1450 -251 499 C ATOM 1284 NE ARG A 189 -38.185 -13.541 65.628 1.00 48.89 N ANISOU 1284 NE ARG A 189 4777 7368 6431 272 160 -483 N ATOM 1285 CZ ARG A 189 -38.580 -12.330 66.018 1.00 51.31 C ANISOU 1285 CZ ARG A 189 4504 7174 7814 -326 1057 -108 C ATOM 1286 NH1 ARG A 189 -38.862 -11.385 65.122 1.00 51.71 N ANISOU 1286 NH1 ARG A 189 4652 7605 7388 -688 66 -17 N ATOM 1287 NH2 ARG A 189 -38.688 -12.063 67.319 1.00 62.52 N ANISOU 1287 NH2 ARG A 189 5612 10649 7491 -1344 -1084 -265 N ATOM 1288 N LYS A 190 -42.432 -16.910 66.372 1.00 45.99 N ANISOU 1288 N LYS A 190 5346 6735 5393 -764 -560 -328 N ATOM 1289 CA LYS A 190 -43.039 -17.717 67.438 1.00 50.20 C ANISOU 1289 CA LYS A 190 6454 6917 5702 -428 40 -204 C ATOM 1290 C LYS A 190 -43.654 -19.017 66.906 1.00 48.44 C ANISOU 1290 C LYS A 190 5952 5839 6611 -71 -327 952 C ATOM 1291 O LYS A 190 -43.394 -20.083 67.446 1.00 48.44 O ANISOU 1291 O LYS A 190 6634 6278 5491 419 175 1019 O ATOM 1292 CB LYS A 190 -44.063 -16.911 68.241 1.00 55.12 C ANISOU 1292 CB LYS A 190 5849 7912 7183 -864 499 -871 C ATOM 1293 CG LYS A 190 -43.447 -16.133 69.392 1.00 60.51 C ANISOU 1293 CG LYS A 190 8730 8717 5542 556 -500 -174 C ATOM 1294 CD LYS A 190 -44.499 -15.461 70.267 1.00 68.94 C ANISOU 1294 CD LYS A 190 6806 10580 8806 -591 1153 -752 C ATOM 1295 CE LYS A 190 -43.931 -15.170 71.655 1.00 69.54 C ANISOU 1295 CE LYS A 190 8254 9362 8803 -1752 1530 -1366 C ATOM 1296 NZ LYS A 190 -44.746 -14.188 72.434 1.00 72.12 N ANISOU 1296 NZ LYS A 190 8323 8043 11035 1338 994 1390 N ATOM 1297 N ARG A 191 -44.450 -18.923 65.843 1.00 50.74 N ANISOU 1297 N ARG A 191 6542 7047 5687 -589 -111 -69 N ATOM 1298 CA ARG A 191 -45.082 -20.096 65.227 1.00 45.19 C ANISOU 1298 CA ARG A 191 6043 5458 5666 68 596 603 C ATOM 1299 C ARG A 191 -44.065 -20.958 64.490 1.00 44.11 C ANISOU 1299 C ARG A 191 5917 5754 5088 -13 271 426 C ATOM 1300 O ARG A 191 -44.219 -22.171 64.379 1.00 54.41 O ANISOU 1300 O ARG A 191 8081 5881 6709 -678 293 375 O ATOM 1301 CB ARG A 191 -46.173 -19.664 64.237 1.00 42.53 C ANISOU 1301 CB ARG A 191 5973 4661 5525 -209 600 717 C ATOM 1302 CG ARG A 191 -47.468 -19.185 64.880 1.00 55.54 C ANISOU 1302 CG ARG A 191 6727 7579 6795 189 1527 -5 C ATOM 1303 CD ARG A 191 -48.514 -20.289 64.986 1.00 67.86 C ANISOU 1303 CD ARG A 191 9866 7857 8058 -1482 1351 -280 C ATOM 1304 NE ARG A 191 -47.941 -21.624 64.810 1.00 70.02 N ANISOU 1304 NE ARG A 191 10903 8968 6732 218 -40 -37 N ATOM 1305 CZ ARG A 191 -48.385 -22.522 63.933 1.00 62.56 C ANISOU 1305 CZ ARG A 191 8862 7577 7331 -836 -282 1088 C ATOM 1306 NH1 ARG A 191 -49.431 -22.242 63.162 1.00 67.32 N ANISOU 1306 NH1 ARG A 191 5759 10594 9223 -2527 882 1039 N ATOM 1307 NH2 ARG A 191 -47.789 -23.706 63.836 1.00 61.91 N ANISOU 1307 NH2 ARG A 191 8869 7321 7331 -1097 -553 1686 N ATOM 1308 N LEU A 192 -43.024 -20.316 63.982 1.00 44.55 N ANISOU 1308 N LEU A 192 5849 5576 5498 -138 82 273 N ATOM 1309 CA LEU A 192 -42.076 -20.968 63.099 1.00 43.22 C ANISOU 1309 CA LEU A 192 5423 5425 5570 -160 -133 422 C ATOM 1310 C LEU A 192 -40.691 -20.463 63.451 1.00 41.52 C ANISOU 1310 C LEU A 192 5571 5208 4996 -484 -20 200 C ATOM 1311 O LEU A 192 -40.190 -19.526 62.834 1.00 39.58 O ANISOU 1311 O LEU A 192 5200 5081 4758 -975 -389 -61 O ATOM 1312 CB LEU A 192 -42.429 -20.649 61.638 1.00 39.83 C ANISOU 1312 CB LEU A 192 4958 5365 4810 -1047 -79 -509 C ATOM 1313 CG LEU A 192 -41.499 -21.105 60.515 1.00 48.16 C ANISOU 1313 CG LEU A 192 5605 6858 5833 979 464 151 C ATOM 1314 CD1 LEU A 192 -41.299 -22.609 60.555 1.00 50.09 C ANISOU 1314 CD1 LEU A 192 6865 6159 6006 -748 854 320 C ATOM 1315 CD2 LEU A 192 -42.046 -20.670 59.165 1.00 51.36 C ANISOU 1315 CD2 LEU A 192 6274 7501 5739 -783 -202 30 C ATOM 1316 N ASP A 193 -40.082 -21.078 64.459 1.00 41.93 N ANISOU 1316 N ASP A 193 5260 5723 4946 286 354 24 N ATOM 1317 CA ASP A 193 -38.780 -20.630 64.919 1.00 48.66 C ANISOU 1317 CA ASP A 193 5453 6677 6359 222 -101 42 C ATOM 1318 C ASP A 193 -37.693 -21.132 63.973 1.00 44.10 C ANISOU 1318 C ASP A 193 6080 5271 5403 -705 177 -291 C ATOM 1319 O ASP A 193 -37.953 -21.959 63.099 1.00 41.14 O ANISOU 1319 O ASP A 193 4781 6040 4810 -614 326 -450 O ATOM 1320 CB ASP A 193 -38.528 -21.034 66.388 1.00 55.13 C ANISOU 1320 CB ASP A 193 7090 7674 6181 398 -482 -457 C ATOM 1321 CG ASP A 193 -38.319 -22.532 66.573 1.00 63.35 C ANISOU 1321 CG ASP A 193 7650 8012 8406 -358 -669 794 C ATOM 1322 OD1 ASP A 193 -39.097 -23.339 66.033 1.00 67.65 O ANISOU 1322 OD1 ASP A 193 9014 8812 7876 -904 -1562 55 O ATOM 1323 OD2 ASP A 193 -37.374 -22.909 67.289 1.00 68.64 O ANISOU 1323 OD2 ASP A 193 9306 9347 7424 388 -1695 1495 O ATOM 1324 N ALA A 194 -36.487 -20.604 64.130 1.00 43.68 N ANISOU 1324 N ALA A 194 5258 6151 5186 295 -673 -1169 N ATOM 1325 CA ALA A 194 -35.378 -20.972 63.265 1.00 48.44 C ANISOU 1325 CA ALA A 194 5967 7115 5324 -361 107 -1265 C ATOM 1326 C ALA A 194 -35.249 -22.493 63.131 1.00 50.12 C ANISOU 1326 C ALA A 194 6474 7003 5566 -256 349 -663 C ATOM 1327 O ALA A 194 -35.123 -23.013 62.029 1.00 45.42 O ANISOU 1327 O ALA A 194 5059 6889 5307 209 1113 -270 O ATOM 1328 CB ALA A 194 -34.085 -20.366 63.783 1.00 46.95 C ANISOU 1328 CB ALA A 194 5800 6307 5730 -1457 1612 -1168 C ATOM 1329 N ARG A 195 -35.307 -23.194 64.259 1.00 46.20 N ANISOU 1329 N ARG A 195 5858 6070 5623 -273 45 -737 N ATOM 1330 CA ARG A 195 -35.133 -24.635 64.299 1.00 46.87 C ANISOU 1330 CA ARG A 195 5977 6032 5797 79 302 119 C ATOM 1331 C ARG A 195 -36.166 -25.392 63.451 1.00 44.97 C ANISOU 1331 C ARG A 195 5525 6227 5334 770 321 5 C ATOM 1332 O ARG A 195 -35.817 -26.296 62.685 1.00 44.90 O ANISOU 1332 O ARG A 195 6419 5592 5048 -355 630 221 O ATOM 1333 CB ARG A 195 -35.189 -25.102 65.749 1.00 45.69 C ANISOU 1333 CB ARG A 195 5899 6189 5272 -481 -349 -345 C ATOM 1334 CG ARG A 195 -34.835 -26.558 65.945 1.00 57.33 C ANISOU 1334 CG ARG A 195 7471 6907 7403 666 799 647 C ATOM 1335 CD ARG A 195 -34.895 -26.926 67.418 1.00 60.78 C ANISOU 1335 CD ARG A 195 8307 7617 7167 163 347 376 C ATOM 1336 NE ARG A 195 -35.648 -28.161 67.616 1.00 74.06 N ANISOU 1336 NE ARG A 195 8359 9854 9924 -935 2164 980 N ATOM 1337 CZ ARG A 195 -35.172 -29.383 67.386 1.00 90.48 C ANISOU 1337 CZ ARG A 195 10480 11301 12595 157 1212 -903 C ATOM 1338 NH1 ARG A 195 -33.931 -29.554 66.944 1.00 93.08 N ANISOU 1338 NH1 ARG A 195 9939 14215 11210 2408 -618 227 N ATOM 1339 NH2 ARG A 195 -35.944 -30.441 67.596 1.00 91.38 N ANISOU 1339 NH2 ARG A 195 12208 10952 11561 724 4811 -150 N ATOM 1340 N ARG A 196 -37.433 -25.023 63.604 1.00 37.32 N ANISOU 1340 N ARG A 196 5231 5643 3304 641 28 -76 N ATOM 1341 CA ARG A 196 -38.525 -25.633 62.864 1.00 45.01 C ANISOU 1341 CA ARG A 196 5763 6256 5082 -527 193 -214 C ATOM 1342 C ARG A 196 -38.449 -25.265 61.390 1.00 45.15 C ANISOU 1342 C ARG A 196 6768 5229 5155 -655 110 -41 C ATOM 1343 O ARG A 196 -38.754 -26.076 60.519 1.00 39.56 O ANISOU 1343 O ARG A 196 5677 4424 4930 -417 54 215 O ATOM 1344 CB ARG A 196 -39.860 -25.153 63.426 1.00 49.78 C ANISOU 1344 CB ARG A 196 6404 7038 5470 -620 1383 190 C ATOM 1345 CG ARG A 196 -41.072 -25.818 62.804 1.00 58.81 C ANISOU 1345 CG ARG A 196 7412 8500 6432 408 -421 -1160 C ATOM 1346 CD ARG A 196 -42.339 -25.395 63.524 1.00 63.13 C ANISOU 1346 CD ARG A 196 6789 9072 8126 685 -268 -388 C ATOM 1347 NE ARG A 196 -43.492 -26.152 63.056 1.00 72.91 N ANISOU 1347 NE ARG A 196 8812 8490 10398 -701 -458 -546 N ATOM 1348 CZ ARG A 196 -44.755 -25.789 63.253 1.00 78.06 C ANISOU 1348 CZ ARG A 196 9507 9579 10571 -279 119 -825 C ATOM 1349 NH1 ARG A 196 -45.034 -24.670 63.908 1.00 71.90 N ANISOU 1349 NH1 ARG A 196 11697 7738 7882 -2093 -176 712 N ATOM 1350 NH2 ARG A 196 -45.743 -26.542 62.789 1.00 78.78 N ANISOU 1350 NH2 ARG A 196 12099 5197 12634 -1358 233 1392 N ATOM 1351 N PHE A 197 -38.056 -24.026 61.122 1.00 43.20 N ANISOU 1351 N PHE A 197 5853 5016 5544 -362 -287 207 N ATOM 1352 CA PHE A 197 -37.941 -23.541 59.756 1.00 38.80 C ANISOU 1352 CA PHE A 197 5464 4331 4947 -467 321 -334 C ATOM 1353 C PHE A 197 -36.825 -24.287 59.044 1.00 34.04 C ANISOU 1353 C PHE A 197 4539 4278 4115 -436 -45 524 C ATOM 1354 O PHE A 197 -37.003 -24.730 57.916 1.00 35.52 O ANISOU 1354 O PHE A 197 5063 4186 4246 -418 -64 446 O ATOM 1355 CB PHE A 197 -37.703 -22.027 59.743 1.00 38.32 C ANISOU 1355 CB PHE A 197 5268 4506 4783 -617 164 274 C ATOM 1356 CG PHE A 197 -37.958 -21.379 58.411 1.00 43.03 C ANISOU 1356 CG PHE A 197 6079 5274 4995 82 -668 59 C ATOM 1357 CD1 PHE A 197 -38.848 -21.937 57.500 1.00 40.30 C ANISOU 1357 CD1 PHE A 197 4798 4907 5605 -567 -258 345 C ATOM 1358 CD2 PHE A 197 -37.326 -20.187 58.077 1.00 55.60 C ANISOU 1358 CD2 PHE A 197 7806 6793 6527 -1744 -444 423 C ATOM 1359 CE1 PHE A 197 -39.084 -21.337 56.273 1.00 37.76 C ANISOU 1359 CE1 PHE A 197 3699 5926 4720 -38 70 -476 C ATOM 1360 CE2 PHE A 197 -37.563 -19.577 56.854 1.00 56.28 C ANISOU 1360 CE2 PHE A 197 7492 6726 7165 -1365 -1441 605 C ATOM 1361 CZ PHE A 197 -38.445 -20.150 55.951 1.00 49.65 C ANISOU 1361 CZ PHE A 197 7171 5666 6025 -153 -830 627 C ATOM 1362 N ALA A 198 -35.689 -24.458 59.712 1.00 33.20 N ANISOU 1362 N ALA A 198 4224 4260 4128 -743 -102 3 N ATOM 1363 CA ALA A 198 -34.581 -25.219 59.135 1.00 38.54 C ANISOU 1363 CA ALA A 198 5121 4922 4601 31 -20 -299 C ATOM 1364 C ALA A 198 -34.973 -26.660 58.798 1.00 39.83 C ANISOU 1364 C ALA A 198 4522 5176 5436 -687 361 -198 C ATOM 1365 O ALA A 198 -34.582 -27.186 57.756 1.00 41.38 O ANISOU 1365 O ALA A 198 5066 5355 5300 -154 240 -6 O ATOM 1366 CB ALA A 198 -33.363 -25.190 60.049 1.00 37.20 C ANISOU 1366 CB ALA A 198 4400 5593 4141 373 572 -992 C ATOM 1367 N GLN A 199 -35.751 -27.289 59.674 1.00 40.53 N ANISOU 1367 N GLN A 199 5873 5045 4480 -179 500 233 N ATOM 1368 CA GLN A 199 -36.234 -28.652 59.443 1.00 40.19 C ANISOU 1368 CA GLN A 199 4973 5239 5059 -237 173 -193 C ATOM 1369 C GLN A 199 -37.110 -28.763 58.200 1.00 37.34 C ANISOU 1369 C GLN A 199 5004 4690 4493 -449 641 80 C ATOM 1370 O GLN A 199 -36.965 -29.701 57.402 1.00 35.04 O ANISOU 1370 O GLN A 199 4694 4305 4312 -315 425 308 O ATOM 1371 CB GLN A 199 -37.008 -29.156 60.663 1.00 43.16 C ANISOU 1371 CB GLN A 199 6654 4917 4825 95 1009 -933 C ATOM 1372 CG GLN A 199 -36.121 -29.502 61.848 1.00 55.40 C ANISOU 1372 CG GLN A 199 7334 7160 6556 527 -162 -709 C ATOM 1373 CD GLN A 199 -36.902 -29.729 63.131 1.00 66.54 C ANISOU 1373 CD GLN A 199 8769 9304 7208 -23 321 222 C ATOM 1374 OE1 GLN A 199 -38.104 -29.996 63.108 1.00 68.06 O ANISOU 1374 OE1 GLN A 199 8534 10256 7067 344 2065 579 O ATOM 1375 NE2 GLN A 199 -36.214 -29.628 64.260 1.00 70.10 N ANISOU 1375 NE2 GLN A 199 10520 9073 7040 -128 20 -1021 N ATOM 1376 N LEU A 200 -38.035 -27.818 58.047 1.00 37.76 N ANISOU 1376 N LEU A 200 5320 4332 4692 -643 283 228 N ATOM 1377 CA LEU A 200 -38.887 -27.771 56.868 1.00 36.70 C ANISOU 1377 CA LEU A 200 4523 4573 4846 -268 183 268 C ATOM 1378 C LEU A 200 -38.040 -27.587 55.622 1.00 35.11 C ANISOU 1378 C LEU A 200 4644 4209 4488 -257 -77 -63 C ATOM 1379 O LEU A 200 -38.247 -28.265 54.611 1.00 32.86 O ANISOU 1379 O LEU A 200 4530 4093 3862 -9 475 451 O ATOM 1380 CB LEU A 200 -39.896 -26.634 56.973 1.00 39.72 C ANISOU 1380 CB LEU A 200 5067 4956 5069 106 955 -797 C ATOM 1381 CG LEU A 200 -41.114 -26.933 57.844 1.00 39.98 C ANISOU 1381 CG LEU A 200 4900 4871 5418 -208 529 333 C ATOM 1382 CD1 LEU A 200 -42.041 -25.723 57.902 1.00 35.09 C ANISOU 1382 CD1 LEU A 200 3701 4988 4643 -609 -631 -197 C ATOM 1383 CD2 LEU A 200 -41.853 -28.163 57.331 1.00 48.00 C ANISOU 1383 CD2 LEU A 200 6622 5579 6036 52 -446 -1198 C ATOM 1384 N LEU A 201 -37.077 -26.675 55.709 1.00 35.67 N ANISOU 1384 N LEU A 201 4575 4563 4412 -511 135 -305 N ATOM 1385 CA LEU A 201 -36.235 -26.359 54.571 1.00 35.20 C ANISOU 1385 CA LEU A 201 4950 4133 4289 -70 143 1 C ATOM 1386 C LEU A 201 -35.340 -27.524 54.221 1.00 33.78 C ANISOU 1386 C LEU A 201 4302 4350 4180 -50 -343 -69 C ATOM 1387 O LEU A 201 -35.159 -27.816 53.047 1.00 32.08 O ANISOU 1387 O LEU A 201 4296 3995 3897 -341 -238 328 O ATOM 1388 CB LEU A 201 -35.417 -25.091 54.820 1.00 34.70 C ANISOU 1388 CB LEU A 201 4699 4089 4394 2 33 -204 C ATOM 1389 CG LEU A 201 -36.297 -23.826 54.854 1.00 36.64 C ANISOU 1389 CG LEU A 201 5358 4496 4064 463 -388 -321 C ATOM 1390 CD1 LEU A 201 -35.560 -22.667 55.511 1.00 39.60 C ANISOU 1390 CD1 LEU A 201 5540 4319 5186 -791 -680 946 C ATOM 1391 CD2 LEU A 201 -36.803 -23.424 53.473 1.00 31.79 C ANISOU 1391 CD2 LEU A 201 4273 3434 4370 121 -219 131 C ATOM 1392 N ALA A 202 -34.797 -28.197 55.234 1.00 31.85 N ANISOU 1392 N ALA A 202 4401 3694 4005 -380 -286 -115 N ATOM 1393 CA ALA A 202 -33.917 -29.337 54.995 1.00 34.37 C ANISOU 1393 CA ALA A 202 4573 4179 4306 -27 -127 -247 C ATOM 1394 C ALA A 202 -34.702 -30.491 54.363 1.00 32.44 C ANISOU 1394 C ALA A 202 3977 4478 3869 -169 191 -158 C ATOM 1395 O ALA A 202 -34.185 -31.221 53.520 1.00 32.52 O ANISOU 1395 O ALA A 202 3895 4293 4167 -76 59 -237 O ATOM 1396 CB ALA A 202 -33.249 -29.785 56.291 1.00 37.33 C ANISOU 1396 CB ALA A 202 4186 4982 5016 51 -829 -350 C ATOM 1397 N LYS A 203 -35.954 -30.657 54.771 1.00 31.31 N ANISOU 1397 N LYS A 203 3503 4269 4124 -56 -123 122 N ATOM 1398 CA LYS A 203 -36.790 -31.686 54.172 1.00 31.84 C ANISOU 1398 CA LYS A 203 3937 4244 3914 -283 20 73 C ATOM 1399 C LYS A 203 -36.982 -31.414 52.673 1.00 33.60 C ANISOU 1399 C LYS A 203 4690 4150 3923 -59 467 342 C ATOM 1400 O LYS A 203 -36.897 -32.331 51.844 1.00 32.56 O ANISOU 1400 O LYS A 203 4525 3550 4297 36 23 509 O ATOM 1401 CB LYS A 203 -38.142 -31.771 54.896 1.00 33.84 C ANISOU 1401 CB LYS A 203 4174 4474 4210 -326 327 265 C ATOM 1402 CG LYS A 203 -39.030 -32.903 54.407 1.00 37.64 C ANISOU 1402 CG LYS A 203 4598 4912 4789 -618 410 -129 C ATOM 1403 CD LYS A 203 -40.299 -33.015 55.245 1.00 38.66 C ANISOU 1403 CD LYS A 203 4347 5033 5306 -402 269 1450 C ATOM 1404 CE LYS A 203 -41.072 -34.260 54.850 1.00 43.15 C ANISOU 1404 CE LYS A 203 5567 5819 5008 -732 267 325 C ATOM 1405 NZ LYS A 203 -42.450 -34.255 55.412 1.00 53.08 N ANISOU 1405 NZ LYS A 203 5792 7947 6429 -478 811 -892 N ATOM 1406 N MET A 204 -37.231 -30.157 52.316 1.00 32.53 N ANISOU 1406 N MET A 204 4604 3643 4112 -26 332 -259 N ATOM 1407 CA MET A 204 -37.316 -29.790 50.898 1.00 32.45 C ANISOU 1407 CA MET A 204 4202 3937 4189 181 -80 135 C ATOM 1408 C MET A 204 -35.963 -29.989 50.218 1.00 34.01 C ANISOU 1408 C MET A 204 4420 4480 4018 -318 18 2 C ATOM 1409 O MET A 204 -35.878 -30.615 49.163 1.00 33.69 O ANISOU 1409 O MET A 204 5261 3623 3914 -546 218 344 O ATOM 1410 CB MET A 204 -37.824 -28.359 50.725 1.00 33.66 C ANISOU 1410 CB MET A 204 4366 4296 4126 509 255 926 C ATOM 1411 CG MET A 204 -39.130 -28.110 51.456 1.00 39.14 C ANISOU 1411 CG MET A 204 5090 4548 5231 -166 1245 245 C ATOM 1412 SD MET A 204 -39.745 -26.409 51.403 1.00 42.74 S ANISOU 1412 SD MET A 204 5369 5236 5634 352 190 956 S ATOM 1413 CE MET A 204 -40.750 -26.528 49.953 1.00 37.45 C ANISOU 1413 CE MET A 204 5025 4968 4234 -95 1083 -165 C ATOM 1414 N GLU A 205 -34.896 -29.507 50.844 1.00 29.37 N ANISOU 1414 N GLU A 205 4141 3307 3710 -230 312 36 N ATOM 1415 CA GLU A 205 -33.574 -29.648 50.253 1.00 31.37 C ANISOU 1415 CA GLU A 205 4005 3872 4041 447 -165 286 C ATOM 1416 C GLU A 205 -33.192 -31.109 50.009 1.00 33.89 C ANISOU 1416 C GLU A 205 5108 3854 3914 178 412 190 C ATOM 1417 O GLU A 205 -32.691 -31.464 48.947 1.00 31.24 O ANISOU 1417 O GLU A 205 4204 3760 3904 -702 397 151 O ATOM 1418 CB GLU A 205 -32.543 -28.980 51.139 1.00 32.65 C ANISOU 1418 CB GLU A 205 4572 3507 4326 -162 -193 316 C ATOM 1419 CG GLU A 205 -31.124 -29.026 50.622 1.00 35.85 C ANISOU 1419 CG GLU A 205 4627 4102 4890 148 73 34 C ATOM 1420 CD GLU A 205 -30.166 -28.493 51.667 1.00 53.31 C ANISOU 1420 CD GLU A 205 6002 7945 6308 -1507 -834 -347 C ATOM 1421 OE1 GLU A 205 -30.293 -28.898 52.843 1.00 57.02 O ANISOU 1421 OE1 GLU A 205 7556 7141 6967 -923 -10 -492 O ATOM 1422 OE2 GLU A 205 -29.303 -27.664 51.324 1.00 61.55 O ANISOU 1422 OE2 GLU A 205 7838 7444 8103 -2071 -702 -158 O ATOM 1423 N SER A 206 -33.419 -31.964 50.991 1.00 31.62 N ANISOU 1423 N SER A 206 4138 3974 3899 10 448 60 N ATOM 1424 CA SER A 206 -32.977 -33.339 50.851 1.00 32.74 C ANISOU 1424 CA SER A 206 4369 4175 3896 281 297 128 C ATOM 1425 C SER A 206 -33.864 -34.090 49.852 1.00 31.35 C ANISOU 1425 C SER A 206 4164 3475 4272 27 291 683 C ATOM 1426 O SER A 206 -33.528 -35.180 49.418 1.00 35.19 O ANISOU 1426 O SER A 206 5535 3705 4131 -93 656 198 O ATOM 1427 CB SER A 206 -32.909 -34.034 52.209 1.00 37.08 C ANISOU 1427 CB SER A 206 4893 4199 4994 1100 862 1181 C ATOM 1428 OG SER A 206 -34.210 -34.424 52.601 1.00 48.03 O ANISOU 1428 OG SER A 206 6319 5980 5951 -1220 1470 410 O ATOM 1429 N SER A 207 -34.973 -33.481 49.448 1.00 28.94 N ANISOU 1429 N SER A 207 3526 3686 3782 -422 481 595 N ATOM 1430 CA SER A 207 -35.792 -34.074 48.402 1.00 32.64 C ANISOU 1430 CA SER A 207 4632 3455 4313 -873 494 -37 C ATOM 1431 C SER A 207 -35.348 -33.721 46.982 1.00 35.59 C ANISOU 1431 C SER A 207 4849 4670 4003 -596 106 -14 C ATOM 1432 O SER A 207 -35.898 -34.268 46.036 1.00 34.62 O ANISOU 1432 O SER A 207 4440 3706 5005 -262 -452 115 O ATOM 1433 CB SER A 207 -37.278 -33.748 48.594 1.00 44.13 C ANISOU 1433 CB SER A 207 5012 5157 6598 -347 472 -559 C ATOM 1434 OG SER A 207 -37.629 -32.514 47.985 1.00 49.08 O ANISOU 1434 OG SER A 207 6936 6674 5038 -1026 312 609 O ATOM 1435 N LEU A 208 -34.373 -32.819 46.827 1.00 33.27 N ANISOU 1435 N LEU A 208 4324 4469 3846 -353 424 -80 N ATOM 1436 CA LEU A 208 -33.893 -32.401 45.489 1.00 34.16 C ANISOU 1436 CA LEU A 208 5241 3352 4386 -196 1072 -128 C ATOM 1437 C LEU A 208 -32.948 -33.402 44.836 1.00 28.25 C ANISOU 1437 C LEU A 208 3726 3181 3825 -291 62 18 C ATOM 1438 O LEU A 208 -32.064 -33.958 45.494 1.00 27.79 O ANISOU 1438 O LEU A 208 3966 2771 3819 163 31 -262 O ATOM 1439 CB LEU A 208 -33.159 -31.051 45.557 1.00 30.34 C ANISOU 1439 CB LEU A 208 4588 3438 3501 -235 779 40 C ATOM 1440 CG LEU A 208 -34.047 -29.890 46.009 1.00 32.74 C ANISOU 1440 CG LEU A 208 4156 3506 4777 169 -61 71 C ATOM 1441 CD1 LEU A 208 -33.214 -28.631 46.173 1.00 32.84 C ANISOU 1441 CD1 LEU A 208 4714 3644 4121 -143 516 -91 C ATOM 1442 CD2 LEU A 208 -35.176 -29.689 45.008 1.00 32.54 C ANISOU 1442 CD2 LEU A 208 4545 3560 4255 200 -39 198 C ATOM 1443 N ILE A 209 -33.113 -33.596 43.532 1.00 27.73 N ANISOU 1443 N ILE A 209 4445 2403 3685 -515 432 -69 N ATOM 1444 CA ILE A 209 -32.190 -34.435 42.780 1.00 32.44 C ANISOU 1444 CA ILE A 209 4723 3641 3960 -88 748 -222 C ATOM 1445 C ILE A 209 -31.576 -33.602 41.664 1.00 30.49 C ANISOU 1445 C ILE A 209 4007 3618 3958 -28 175 44 C ATOM 1446 O ILE A 209 -32.105 -33.582 40.544 1.00 28.41 O ANISOU 1446 O ILE A 209 4299 2712 3781 -214 280 -63 O ATOM 1447 CB ILE A 209 -32.899 -35.692 42.212 1.00 33.50 C ANISOU 1447 CB ILE A 209 4433 4181 4114 -260 275 -374 C ATOM 1448 CG1 ILE A 209 -33.724 -36.374 43.312 1.00 37.35 C ANISOU 1448 CG1 ILE A 209 5259 4224 4708 -478 571 -102 C ATOM 1449 CG2 ILE A 209 -31.877 -36.654 41.615 1.00 33.56 C ANISOU 1449 CG2 ILE A 209 4914 3567 4268 -69 -17 -393 C ATOM 1450 CD1 ILE A 209 -34.485 -37.612 42.874 1.00 34.79 C ANISOU 1450 CD1 ILE A 209 4524 4394 4300 -308 112 107 C ATOM 1451 N PRO A 210 -30.472 -32.887 41.966 1.00 32.75 N ANISOU 1451 N PRO A 210 4299 4020 4122 -44 -136 -464 N ATOM 1452 CA PRO A 210 -29.859 -32.071 40.905 1.00 36.12 C ANISOU 1452 CA PRO A 210 4845 4826 4051 47 -68 -154 C ATOM 1453 C PRO A 210 -29.357 -32.907 39.720 1.00 32.52 C ANISOU 1453 C PRO A 210 3919 4274 4162 -183 504 269 C ATOM 1454 O PRO A 210 -29.169 -32.374 38.651 1.00 32.61 O ANISOU 1454 O PRO A 210 4553 3913 3921 -166 51 -3 O ATOM 1455 CB PRO A 210 -28.705 -31.332 41.599 1.00 39.85 C ANISOU 1455 CB PRO A 210 5330 4471 5340 -936 -7 360 C ATOM 1456 CG PRO A 210 -28.698 -31.763 43.028 1.00 41.34 C ANISOU 1456 CG PRO A 210 4966 5951 4790 -763 173 -64 C ATOM 1457 CD PRO A 210 -29.816 -32.732 43.281 1.00 33.20 C ANISOU 1457 CD PRO A 210 4677 4036 3898 236 -178 347 C ATOM 1458 N ALA A 211 -29.183 -34.213 39.894 1.00 36.13 N ANISOU 1458 N ALA A 211 5001 4506 4221 708 -272 -64 N ATOM 1459 CA ALA A 211 -28.823 -35.071 38.761 1.00 35.03 C ANISOU 1459 CA ALA A 211 4216 4652 4440 298 78 -61 C ATOM 1460 C ALA A 211 -29.838 -34.941 37.624 1.00 31.89 C ANISOU 1460 C ALA A 211 4189 3816 4109 -202 239 -78 C ATOM 1461 O ALA A 211 -29.524 -35.182 36.458 1.00 33.07 O ANISOU 1461 O ALA A 211 4592 3608 4365 -395 789 324 O ATOM 1462 CB ALA A 211 -28.702 -36.519 39.201 1.00 33.95 C ANISOU 1462 CB ALA A 211 3699 4284 4917 -117 353 -303 C ATOM 1463 N ALA A 212 -31.055 -34.545 37.973 1.00 30.70 N ANISOU 1463 N ALA A 212 4186 3675 3801 -259 241 474 N ATOM 1464 CA ALA A 212 -32.122 -34.392 37.003 1.00 30.57 C ANISOU 1464 CA ALA A 212 4098 3415 4099 -361 -32 -322 C ATOM 1465 C ALA A 212 -31.771 -33.347 35.944 1.00 33.44 C ANISOU 1465 C ALA A 212 4407 4367 3931 -431 -93 132 C ATOM 1466 O ALA A 212 -32.371 -33.325 34.880 1.00 33.75 O ANISOU 1466 O ALA A 212 4079 4500 4241 -434 -516 249 O ATOM 1467 CB ALA A 212 -33.435 -34.054 37.696 1.00 34.45 C ANISOU 1467 CB ALA A 212 4591 4017 4480 -322 475 -430 C ATOM 1468 N VAL A 213 -30.784 -32.496 36.219 1.00 32.52 N ANISOU 1468 N VAL A 213 4399 3890 4067 -169 359 -278 N ATOM 1469 CA VAL A 213 -30.348 -31.514 35.212 1.00 36.30 C ANISOU 1469 CA VAL A 213 4620 4524 4645 -564 623 -6 C ATOM 1470 C VAL A 213 -29.865 -32.234 33.947 1.00 36.88 C ANISOU 1470 C VAL A 213 4811 4599 4601 98 247 211 C ATOM 1471 O VAL A 213 -30.136 -31.793 32.827 1.00 38.51 O ANISOU 1471 O VAL A 213 5777 4453 4402 -149 -8 -259 O ATOM 1472 CB VAL A 213 -29.256 -30.568 35.771 1.00 35.46 C ANISOU 1472 CB VAL A 213 4767 4209 4497 -259 451 -194 C ATOM 1473 CG1 VAL A 213 -28.583 -29.768 34.659 1.00 32.20 C ANISOU 1473 CG1 VAL A 213 3906 4031 4295 113 56 -47 C ATOM 1474 CG2 VAL A 213 -29.851 -29.637 36.824 1.00 32.55 C ANISOU 1474 CG2 VAL A 213 3424 4426 4516 -872 857 -177 C ATOM 1475 N PHE A 214 -29.195 -33.369 34.143 1.00 34.96 N ANISOU 1475 N PHE A 214 3989 4548 4745 -122 629 479 N ATOM 1476 CA PHE A 214 -28.530 -34.101 33.068 1.00 37.71 C ANISOU 1476 CA PHE A 214 4888 4830 4609 89 292 -169 C ATOM 1477 C PHE A 214 -29.226 -35.398 32.699 1.00 42.07 C ANISOU 1477 C PHE A 214 4660 5604 5720 -554 568 -574 C ATOM 1478 O PHE A 214 -28.837 -36.085 31.746 1.00 42.37 O ANISOU 1478 O PHE A 214 5422 5548 5127 -336 757 -56 O ATOM 1479 CB PHE A 214 -27.078 -34.367 33.469 1.00 39.44 C ANISOU 1479 CB PHE A 214 4906 5321 4758 -381 -68 -667 C ATOM 1480 CG PHE A 214 -26.282 -33.114 33.627 1.00 40.28 C ANISOU 1480 CG PHE A 214 5538 4612 5151 -198 250 -373 C ATOM 1481 CD1 PHE A 214 -25.883 -32.400 32.509 1.00 40.24 C ANISOU 1481 CD1 PHE A 214 5489 4526 5274 -63 1349 -858 C ATOM 1482 CD2 PHE A 214 -25.981 -32.614 34.889 1.00 35.85 C ANISOU 1482 CD2 PHE A 214 4076 4362 5182 625 -102 31 C ATOM 1483 CE1 PHE A 214 -25.171 -31.224 32.643 1.00 40.16 C ANISOU 1483 CE1 PHE A 214 5265 5289 4704 -928 673 429 C ATOM 1484 CE2 PHE A 214 -25.264 -31.439 35.026 1.00 38.76 C ANISOU 1484 CE2 PHE A 214 5244 4663 4818 -140 1163 -311 C ATOM 1485 CZ PHE A 214 -24.865 -30.736 33.899 1.00 36.82 C ANISOU 1485 CZ PHE A 214 4177 5039 4774 -28 901 -96 C ATOM 1486 N LEU A 215 -30.268 -35.718 33.455 1.00 44.20 N ANISOU 1486 N LEU A 215 5993 5245 5554 -432 1115 221 N ATOM 1487 CA LEU A 215 -31.051 -36.924 33.254 1.00 38.28 C ANISOU 1487 CA LEU A 215 5263 5063 4216 255 513 -20 C ATOM 1488 C LEU A 215 -32.506 -36.494 33.448 1.00 33.14 C ANISOU 1488 C LEU A 215 4445 4133 4014 -997 -224 -288 C ATOM 1489 O LEU A 215 -33.118 -36.802 34.470 1.00 35.68 O ANISOU 1489 O LEU A 215 4618 4274 4662 -1513 235 -116 O ATOM 1490 CB LEU A 215 -30.619 -37.951 34.306 1.00 38.54 C ANISOU 1490 CB LEU A 215 6281 4750 3610 40 727 -239 C ATOM 1491 CG LEU A 215 -30.425 -39.441 34.042 1.00 45.62 C ANISOU 1491 CG LEU A 215 7072 5100 5159 732 528 184 C ATOM 1492 CD1 LEU A 215 -29.720 -39.742 32.727 1.00 41.70 C ANISOU 1492 CD1 LEU A 215 5242 5733 4869 909 395 1818 C ATOM 1493 CD2 LEU A 215 -29.636 -40.016 35.208 1.00 53.97 C ANISOU 1493 CD2 LEU A 215 5013 7991 7500 1112 -804 173 C ATOM 1494 N PRO A 216 -33.054 -35.732 32.483 1.00 38.26 N ANISOU 1494 N PRO A 216 4898 5055 4582 -79 46 137 N ATOM 1495 CA PRO A 216 -34.351 -35.094 32.723 1.00 37.39 C ANISOU 1495 CA PRO A 216 4678 5148 4381 -382 -1 -46 C ATOM 1496 C PRO A 216 -35.513 -36.081 32.833 1.00 38.88 C ANISOU 1496 C PRO A 216 5005 4561 5205 -195 320 176 C ATOM 1497 O PRO A 216 -36.607 -35.706 33.272 1.00 35.38 O ANISOU 1497 O PRO A 216 4894 3798 4751 225 -296 547 O ATOM 1498 CB PRO A 216 -34.529 -34.162 31.520 1.00 38.28 C ANISOU 1498 CB PRO A 216 5804 4290 4451 -929 605 -41 C ATOM 1499 CG PRO A 216 -33.582 -34.671 30.481 1.00 40.79 C ANISOU 1499 CG PRO A 216 5137 5367 4993 513 600 1025 C ATOM 1500 CD PRO A 216 -32.446 -35.314 31.205 1.00 39.51 C ANISOU 1500 CD PRO A 216 5592 4910 4508 169 -40 509 C ATOM 1501 N ILE A 217 -35.269 -37.334 32.463 1.00 39.91 N ANISOU 1501 N ILE A 217 5682 4851 4629 -482 223 -251 N ATOM 1502 CA ILE A 217 -36.276 -38.378 32.627 1.00 40.30 C ANISOU 1502 CA ILE A 217 5677 4524 5109 -123 532 155 C ATOM 1503 C ILE A 217 -36.789 -38.410 34.078 1.00 34.24 C ANISOU 1503 C ILE A 217 4096 4067 4845 336 -37 -312 C ATOM 1504 O ILE A 217 -37.976 -38.626 34.328 1.00 33.21 O ANISOU 1504 O ILE A 217 4617 4005 3995 -356 366 -63 O ATOM 1505 CB ILE A 217 -35.739 -39.764 32.167 1.00 39.88 C ANISOU 1505 CB ILE A 217 5163 4678 5309 110 -632 -245 C ATOM 1506 CG1 ILE A 217 -36.842 -40.826 32.220 1.00 47.27 C ANISOU 1506 CG1 ILE A 217 5006 5925 7027 -108 -123 1630 C ATOM 1507 CG2 ILE A 217 -34.529 -40.199 32.985 1.00 34.84 C ANISOU 1507 CG2 ILE A 217 4727 4023 4485 13 122 207 C ATOM 1508 CD1 ILE A 217 -38.087 -40.452 31.452 1.00 50.28 C ANISOU 1508 CD1 ILE A 217 6915 6618 5569 980 -838 1142 C ATOM 1509 N LEU A 218 -35.890 -38.149 35.025 1.00 36.32 N ANISOU 1509 N LEU A 218 5155 4088 4556 -91 -293 -318 N ATOM 1510 CA LEU A 218 -36.227 -38.181 36.440 1.00 37.57 C ANISOU 1510 CA LEU A 218 5212 4548 4515 -450 -166 -23 C ATOM 1511 C LEU A 218 -37.416 -37.308 36.807 1.00 41.77 C ANISOU 1511 C LEU A 218 5027 5364 5477 133 -725 427 C ATOM 1512 O LEU A 218 -38.190 -37.651 37.700 1.00 49.26 O ANISOU 1512 O LEU A 218 6629 6155 5930 85 445 -153 O ATOM 1513 CB LEU A 218 -35.023 -37.775 37.288 1.00 34.63 C ANISOU 1513 CB LEU A 218 4394 4029 4731 -419 269 165 C ATOM 1514 CG LEU A 218 -33.931 -38.819 37.442 1.00 33.90 C ANISOU 1514 CG LEU A 218 4087 4313 4479 -332 640 266 C ATOM 1515 CD1 LEU A 218 -32.714 -38.182 38.082 1.00 37.80 C ANISOU 1515 CD1 LEU A 218 5155 4914 4294 -548 69 -421 C ATOM 1516 CD2 LEU A 218 -34.407 -40.003 38.269 1.00 34.97 C ANISOU 1516 CD2 LEU A 218 4632 4237 4415 -442 -336 633 C ATOM 1517 N LEU A 219 -37.563 -36.182 36.121 1.00 39.60 N ANISOU 1517 N LEU A 219 5151 4697 5195 -463 -92 -23 N ATOM 1518 CA LEU A 219 -38.624 -35.236 36.454 1.00 45.22 C ANISOU 1518 CA LEU A 219 5069 5652 6461 -380 620 -264 C ATOM 1519 C LEU A 219 -40.015 -35.695 36.017 1.00 45.69 C ANISOU 1519 C LEU A 219 5569 5376 6414 -340 85 -395 C ATOM 1520 O LEU A 219 -41.026 -35.119 36.426 1.00 41.06 O ANISOU 1520 O LEU A 219 5038 4969 5592 -648 -310 -198 O ATOM 1521 CB LEU A 219 -38.285 -33.842 35.920 1.00 48.03 C ANISOU 1521 CB LEU A 219 5661 5186 7400 373 -131 -2 C ATOM 1522 CG LEU A 219 -36.938 -33.374 36.504 1.00 50.50 C ANISOU 1522 CG LEU A 219 6639 5786 6762 -1320 -308 374 C ATOM 1523 CD1 LEU A 219 -36.576 -31.965 36.075 1.00 39.93 C ANISOU 1523 CD1 LEU A 219 4612 4926 5632 18 254 -466 C ATOM 1524 CD2 LEU A 219 -36.932 -33.488 38.025 1.00 48.23 C ANISOU 1524 CD2 LEU A 219 6126 5663 6533 -743 -1125 -900 C ATOM 1525 N LYS A 220 -40.070 -36.746 35.209 1.00 46.06 N ANISOU 1525 N LYS A 220 5931 5623 5944 -706 535 -318 N ATOM 1526 CA LYS A 220 -41.358 -37.308 34.811 1.00 49.62 C ANISOU 1526 CA LYS A 220 6368 6172 6312 -757 -578 154 C ATOM 1527 C LYS A 220 -41.687 -38.637 35.501 1.00 47.69 C ANISOU 1527 C LYS A 220 5701 6243 6176 290 587 286 C ATOM 1528 O LYS A 220 -42.794 -39.140 35.359 1.00 58.38 O ANISOU 1528 O LYS A 220 6853 6174 9154 -1182 502 1353 O ATOM 1529 CB LYS A 220 -41.449 -37.415 33.288 1.00 51.37 C ANISOU 1529 CB LYS A 220 5579 7374 6563 -1548 -1541 377 C ATOM 1530 CG LYS A 220 -41.556 -36.047 32.627 1.00 61.58 C ANISOU 1530 CG LYS A 220 8878 7066 7451 -1376 -655 383 C ATOM 1531 CD LYS A 220 -41.006 -36.037 31.211 1.00 66.52 C ANISOU 1531 CD LYS A 220 9686 8156 7433 175 -648 1192 C ATOM 1532 CE LYS A 220 -42.092 -36.373 30.202 1.00 69.91 C ANISOU 1532 CE LYS A 220 9617 6945 9998 -2360 -933 938 C ATOM 1533 NZ LYS A 220 -41.711 -35.965 28.819 1.00 76.96 N ANISOU 1533 NZ LYS A 220 9926 10182 9130 -1644 -3029 1912 N ATOM 1534 N LEU A 221 -40.731 -39.188 36.253 1.00 45.60 N ANISOU 1534 N LEU A 221 6393 6373 4557 -531 44 277 N ATOM 1535 CA LEU A 221 -40.955 -40.409 37.043 1.00 43.18 C ANISOU 1535 CA LEU A 221 5627 5114 5663 -49 -669 13 C ATOM 1536 C LEU A 221 -41.634 -40.101 38.377 1.00 52.20 C ANISOU 1536 C LEU A 221 7262 6236 6336 -821 393 -277 C ATOM 1537 O LEU A 221 -41.378 -39.055 38.968 1.00 45.80 O ANISOU 1537 O LEU A 221 6618 5303 5478 -599 755 389 O ATOM 1538 CB LEU A 221 -39.629 -41.137 37.308 1.00 33.30 C ANISOU 1538 CB LEU A 221 5138 2803 4711 -711 2 34 C ATOM 1539 CG LEU A 221 -38.829 -41.591 36.084 1.00 35.90 C ANISOU 1539 CG LEU A 221 5108 4369 4163 -411 -8 887 C ATOM 1540 CD1 LEU A 221 -37.646 -42.468 36.467 1.00 35.41 C ANISOU 1540 CD1 LEU A 221 3689 4722 5042 -739 600 447 C ATOM 1541 CD2 LEU A 221 -39.732 -42.337 35.108 1.00 43.56 C ANISOU 1541 CD2 LEU A 221 6119 5093 5337 -895 -618 447 C ATOM 1542 N PRO A 222 -42.515 -41.004 38.853 1.00 57.48 N ANISOU 1542 N PRO A 222 7391 7082 7364 -1443 275 177 N ATOM 1543 CA PRO A 222 -42.969 -40.926 40.248 1.00 53.24 C ANISOU 1543 CA PRO A 222 6342 6991 6894 -940 -705 -1225 C ATOM 1544 C PRO A 222 -41.826 -41.205 41.220 1.00 46.06 C ANISOU 1544 C PRO A 222 6322 5805 5373 -381 280 -343 C ATOM 1545 O PRO A 222 -41.153 -42.234 41.119 1.00 45.86 O ANISOU 1545 O PRO A 222 6280 5694 5448 -340 -399 -113 O ATOM 1546 CB PRO A 222 -44.034 -42.031 40.352 1.00 53.96 C ANISOU 1546 CB PRO A 222 6153 7243 7105 -640 1408 -184 C ATOM 1547 CG PRO A 222 -43.908 -42.845 39.107 1.00 60.66 C ANISOU 1547 CG PRO A 222 7204 8115 7726 -724 1065 -856 C ATOM 1548 CD PRO A 222 -43.334 -41.937 38.061 1.00 63.35 C ANISOU 1548 CD PRO A 222 9578 7192 7300 -1347 213 -755 C ATOM 1549 N LEU A 223 -41.613 -40.282 42.150 1.00 40.87 N ANISOU 1549 N LEU A 223 4526 5977 5024 -954 121 -101 N ATOM 1550 CA LEU A 223 -40.510 -40.383 43.082 1.00 41.47 C ANISOU 1550 CA LEU A 223 5202 5762 4793 -588 -264 -693 C ATOM 1551 C LEU A 223 -41.012 -40.068 44.487 1.00 35.59 C ANISOU 1551 C LEU A 223 3467 5246 4810 -347 229 404 C ATOM 1552 O LEU A 223 -41.784 -39.127 44.662 1.00 39.84 O ANISOU 1552 O LEU A 223 5178 5059 4900 10 127 -619 O ATOM 1553 CB LEU A 223 -39.414 -39.374 42.705 1.00 43.93 C ANISOU 1553 CB LEU A 223 5510 5764 5416 -94 618 153 C ATOM 1554 CG LEU A 223 -38.830 -39.339 41.287 1.00 42.06 C ANISOU 1554 CG LEU A 223 5635 5461 4884 -84 -45 276 C ATOM 1555 CD1 LEU A 223 -38.200 -37.983 40.999 1.00 44.03 C ANISOU 1555 CD1 LEU A 223 5894 6130 4706 -100 1081 1212 C ATOM 1556 CD2 LEU A 223 -37.821 -40.455 41.089 1.00 43.79 C ANISOU 1556 CD2 LEU A 223 5702 6436 4497 253 1256 242 C ATOM 1557 N PRO A 224 -40.551 -40.826 45.500 1.00 39.48 N ANISOU 1557 N PRO A 224 5387 4755 4857 -63 -111 198 N ATOM 1558 CA PRO A 224 -40.908 -40.479 46.897 1.00 38.96 C ANISOU 1558 CA PRO A 224 5184 4654 4962 -154 499 381 C ATOM 1559 C PRO A 224 -40.471 -39.056 47.299 1.00 40.25 C ANISOU 1559 C PRO A 224 5217 5067 5009 -251 418 -149 C ATOM 1560 O PRO A 224 -41.131 -38.430 48.128 1.00 43.85 O ANISOU 1560 O PRO A 224 6045 5336 5278 266 937 164 O ATOM 1561 CB PRO A 224 -40.184 -41.536 47.742 1.00 37.71 C ANISOU 1561 CB PRO A 224 4631 5411 4285 -414 56 179 C ATOM 1562 CG PRO A 224 -39.214 -42.216 46.831 1.00 40.51 C ANISOU 1562 CG PRO A 224 5322 4942 5128 425 -281 -240 C ATOM 1563 CD PRO A 224 -39.628 -41.974 45.404 1.00 40.16 C ANISOU 1563 CD PRO A 224 5476 5047 4735 132 93 -351 C ATOM 1564 N GLN A 225 -39.380 -38.567 46.698 1.00 38.30 N ANISOU 1564 N GLN A 225 4909 4370 5273 -264 308 -186 N ATOM 1565 CA GLN A 225 -38.894 -37.187 46.858 1.00 36.90 C ANISOU 1565 CA GLN A 225 4297 4594 5129 -505 824 -281 C ATOM 1566 C GLN A 225 -39.967 -36.146 46.601 1.00 38.87 C ANISOU 1566 C GLN A 225 4162 5135 5469 -530 43 -433 C ATOM 1567 O GLN A 225 -40.039 -35.135 47.296 1.00 41.61 O ANISOU 1567 O GLN A 225 5391 5523 4895 -976 740 -431 O ATOM 1568 CB GLN A 225 -37.723 -36.911 45.893 1.00 30.16 C ANISOU 1568 CB GLN A 225 3930 3346 4182 -1066 84 -651 C ATOM 1569 CG GLN A 225 -36.401 -37.487 46.357 1.00 33.96 C ANISOU 1569 CG GLN A 225 4032 4075 4795 -702 317 -245 C ATOM 1570 CD GLN A 225 -36.244 -38.975 46.081 1.00 35.03 C ANISOU 1570 CD GLN A 225 5135 3879 4294 -457 -707 510 C ATOM 1571 OE1 GLN A 225 -36.997 -39.578 45.301 1.00 31.34 O ANISOU 1571 OE1 GLN A 225 4496 3359 4053 -458 64 339 O ATOM 1572 NE2 GLN A 225 -35.237 -39.569 46.703 1.00 32.21 N ANISOU 1572 NE2 GLN A 225 3927 3381 4930 -559 -308 -289 N ATOM 1573 N SER A 226 -40.779 -36.382 45.577 1.00 40.71 N ANISOU 1573 N SER A 226 5514 5495 4457 -428 16 63 N ATOM 1574 CA SER A 226 -41.867 -35.468 45.226 1.00 45.21 C ANISOU 1574 CA SER A 226 6375 5461 5339 354 104 -418 C ATOM 1575 C SER A 226 -42.875 -35.280 46.353 1.00 43.16 C ANISOU 1575 C SER A 226 5830 5950 4617 -3 -389 202 C ATOM 1576 O SER A 226 -43.258 -34.148 46.659 1.00 45.85 O ANISOU 1576 O SER A 226 5661 5888 5870 312 -55 622 O ATOM 1577 CB SER A 226 -42.582 -35.935 43.956 1.00 51.70 C ANISOU 1577 CB SER A 226 7914 5709 6019 -1370 -528 33 C ATOM 1578 OG SER A 226 -41.693 -35.898 42.855 1.00 59.16 O ANISOU 1578 OG SER A 226 8457 7887 6134 387 -178 -1337 O ATOM 1579 N ALA A 227 -43.298 -36.378 46.973 1.00 43.50 N ANISOU 1579 N ALA A 227 6160 5200 5168 -767 -121 -829 N ATOM 1580 CA ALA A 227 -44.246 -36.289 48.088 1.00 46.98 C ANISOU 1580 CA ALA A 227 5834 5964 6050 -406 283 -186 C ATOM 1581 C ALA A 227 -43.663 -35.604 49.336 1.00 45.25 C ANISOU 1581 C ALA A 227 5364 5791 6037 194 242 -432 C ATOM 1582 O ALA A 227 -44.377 -34.871 50.019 1.00 45.18 O ANISOU 1582 O ALA A 227 5266 4784 7117 -1029 821 -1020 O ATOM 1583 CB ALA A 227 -44.821 -37.655 48.433 1.00 40.49 C ANISOU 1583 CB ALA A 227 5340 5330 4714 765 -1011 771 C ATOM 1584 N ARG A 228 -42.383 -35.828 49.638 1.00 36.36 N ANISOU 1584 N ARG A 228 4793 4426 4596 -694 850 -117 N ATOM 1585 CA ARG A 228 -41.773 -35.160 50.791 1.00 35.95 C ANISOU 1585 CA ARG A 228 4267 4718 4671 -626 193 389 C ATOM 1586 C ARG A 228 -41.727 -33.663 50.585 1.00 37.73 C ANISOU 1586 C ARG A 228 4470 4865 4999 -254 -134 3 C ATOM 1587 O ARG A 228 -42.076 -32.882 51.482 1.00 39.66 O ANISOU 1587 O ARG A 228 5137 5143 4789 172 -229 163 O ATOM 1588 CB ARG A 228 -40.365 -35.666 51.043 1.00 38.92 C ANISOU 1588 CB ARG A 228 5014 5015 4757 612 551 13 C ATOM 1589 CG ARG A 228 -40.333 -37.126 51.398 1.00 46.30 C ANISOU 1589 CG ARG A 228 6228 5673 5691 389 989 1500 C ATOM 1590 CD ARG A 228 -39.020 -37.508 52.042 1.00 57.83 C ANISOU 1590 CD ARG A 228 6786 7641 7545 1218 505 1176 C ATOM 1591 NE ARG A 228 -38.992 -38.955 52.183 1.00 65.79 N ANISOU 1591 NE ARG A 228 8089 8195 8713 1466 1218 386 N ATOM 1592 CZ ARG A 228 -38.418 -39.784 51.317 1.00 62.05 C ANISOU 1592 CZ ARG A 228 10169 6863 6544 -693 1212 311 C ATOM 1593 NH1 ARG A 228 -37.782 -39.315 50.241 1.00 46.16 N ANISOU 1593 NH1 ARG A 228 4851 6523 6162 -328 -553 9 N ATOM 1594 NH2 ARG A 228 -38.470 -41.089 51.544 1.00 54.77 N ANISOU 1594 NH2 ARG A 228 6972 6643 7195 -386 -63 362 N ATOM 1595 N CYS A 229 -41.287 -33.264 49.398 1.00 38.53 N ANISOU 1595 N CYS A 229 4704 4991 4942 381 -9 -13 N ATOM 1596 CA CYS A 229 -41.170 -31.853 49.087 1.00 39.76 C ANISOU 1596 CA CYS A 229 5200 4774 5131 101 251 -295 C ATOM 1597 C CYS A 229 -42.529 -31.180 49.233 1.00 40.25 C ANISOU 1597 C CYS A 229 5270 4361 5660 101 -134 -637 C ATOM 1598 O CYS A 229 -42.660 -30.207 49.965 1.00 34.67 O ANISOU 1598 O CYS A 229 4362 4130 4679 -576 -342 -271 O ATOM 1599 CB CYS A 229 -40.618 -31.644 47.690 1.00 43.19 C ANISOU 1599 CB CYS A 229 5910 5811 4687 4 -445 211 C ATOM 1600 SG CYS A 229 -39.835 -30.034 47.567 1.00 50.49 S ANISOU 1600 SG CYS A 229 7125 6424 5635 -28 699 515 S ATOM 1601 N HIS A 230 -43.536 -31.726 48.560 1.00 38.31 N ANISOU 1601 N HIS A 230 4930 5166 4459 236 -80 -318 N ATOM 1602 CA HIS A 230 -44.913 -31.260 48.686 1.00 44.34 C ANISOU 1602 CA HIS A 230 5281 5863 5703 621 -212 -82 C ATOM 1603 C HIS A 230 -45.415 -31.207 50.116 1.00 40.99 C ANISOU 1603 C HIS A 230 4957 5082 5534 76 -661 -329 C ATOM 1604 O HIS A 230 -46.056 -30.237 50.504 1.00 41.76 O ANISOU 1604 O HIS A 230 4524 5941 5401 110 -879 -1044 O ATOM 1605 CB HIS A 230 -45.832 -32.114 47.815 1.00 47.75 C ANISOU 1605 CB HIS A 230 6424 5436 6281 -134 695 -849 C ATOM 1606 CG HIS A 230 -47.294 -31.764 47.941 1.00 54.08 C ANISOU 1606 CG HIS A 230 6275 7219 7054 -49 -335 -211 C ATOM 1607 ND1 HIS A 230 -47.852 -30.732 47.278 1.00 51.01 N ANISOU 1607 ND1 HIS A 230 6456 6662 6262 -825 -324 -312 N ATOM 1608 CD2 HIS A 230 -48.314 -32.349 48.693 1.00 53.46 C ANISOU 1608 CD2 HIS A 230 5884 6734 7695 -29 -579 11 C ATOM 1609 CE1 HIS A 230 -49.160 -30.659 47.587 1.00 55.43 C ANISOU 1609 CE1 HIS A 230 6369 6902 7791 -219 -23 -304 C ATOM 1610 NE2 HIS A 230 -49.440 -31.652 48.453 1.00 52.76 N ANISOU 1610 NE2 HIS A 230 5944 7585 6516 829 813 -346 N ATOM 1611 N GLU A 231 -45.132 -32.241 50.910 1.00 39.61 N ANISOU 1611 N GLU A 231 4308 5111 5629 -28 -150 -208 N ATOM 1612 CA GLU A 231 -45.509 -32.267 52.326 1.00 45.39 C ANISOU 1612 CA GLU A 231 4903 6678 5662 -108 -343 -700 C ATOM 1613 C GLU A 231 -44.985 -31.041 53.064 1.00 41.47 C ANISOU 1613 C GLU A 231 4841 4331 6584 327 585 151 C ATOM 1614 O GLU A 231 -45.713 -30.394 53.819 1.00 39.37 O ANISOU 1614 O GLU A 231 4446 5138 5372 -1013 762 -470 O ATOM 1615 CB GLU A 231 -44.921 -33.493 53.027 1.00 55.80 C ANISOU 1615 CB GLU A 231 7613 5888 7698 663 119 -610 C ATOM 1616 CG GLU A 231 -45.709 -34.786 52.937 1.00 66.21 C ANISOU 1616 CG GLU A 231 8334 7989 8832 -1590 1659 1027 C ATOM 1617 CD GLU A 231 -45.013 -35.903 53.699 1.00 75.27 C ANISOU 1617 CD GLU A 231 10710 8672 9214 -66 1189 917 C ATOM 1618 OE1 GLU A 231 -44.952 -35.823 54.949 1.00 77.29 O ANISOU 1618 OE1 GLU A 231 9319 10712 9333 -2125 867 833 O ATOM 1619 OE2 GLU A 231 -44.514 -36.854 53.053 1.00 75.99 O ANISOU 1619 OE2 GLU A 231 9655 9027 10188 -495 2130 1496 O ATOM 1620 N ALA A 232 -43.699 -30.759 52.862 1.00 35.84 N ANISOU 1620 N ALA A 232 4422 4546 4647 25 -284 221 N ATOM 1621 CA ALA A 232 -43.023 -29.708 53.589 1.00 35.96 C ANISOU 1621 CA ALA A 232 4119 4598 4946 -31 -59 1 C ATOM 1622 C ALA A 232 -43.514 -28.341 53.138 1.00 32.16 C ANISOU 1622 C ALA A 232 3378 4484 4356 -101 0 -281 C ATOM 1623 O ALA A 232 -43.776 -27.478 53.971 1.00 32.07 O ANISOU 1623 O ALA A 232 3811 4347 4025 -97 456 -109 O ATOM 1624 CB ALA A 232 -41.509 -29.825 53.420 1.00 35.60 C ANISOU 1624 CB ALA A 232 4131 4198 5196 -21 439 -493 C ATOM 1625 N ARG A 233 -43.639 -28.149 51.823 1.00 31.56 N ANISOU 1625 N ARG A 233 3247 4527 4215 -200 179 -87 N ATOM 1626 CA ARG A 233 -44.093 -26.868 51.283 1.00 34.02 C ANISOU 1626 CA ARG A 233 4099 4331 4496 -423 -364 -385 C ATOM 1627 C ARG A 233 -45.521 -26.584 51.731 1.00 40.42 C ANISOU 1627 C ARG A 233 4654 5145 5557 -414 578 -382 C ATOM 1628 O ARG A 233 -45.853 -25.451 52.093 1.00 38.99 O ANISOU 1628 O ARG A 233 4238 4868 5705 -614 57 -150 O ATOM 1629 CB ARG A 233 -44.000 -26.828 49.750 1.00 35.70 C ANISOU 1629 CB ARG A 233 4226 4755 4582 -6 140 146 C ATOM 1630 CG ARG A 233 -44.073 -25.424 49.152 1.00 36.37 C ANISOU 1630 CG ARG A 233 4613 4636 4567 -961 97 130 C ATOM 1631 CD ARG A 233 -43.936 -25.473 47.633 1.00 38.04 C ANISOU 1631 CD ARG A 233 4833 5063 4556 672 -333 803 C ATOM 1632 NE ARG A 233 -43.902 -24.149 47.003 1.00 34.13 N ANISOU 1632 NE ARG A 233 3694 4625 4647 -218 48 173 N ATOM 1633 CZ ARG A 233 -44.949 -23.326 46.959 1.00 30.31 C ANISOU 1633 CZ ARG A 233 4248 3507 3760 -340 -75 -246 C ATOM 1634 NH1 ARG A 233 -46.084 -23.672 47.547 1.00 35.41 N ANISOU 1634 NH1 ARG A 233 3786 4852 4815 -577 -93 -605 N ATOM 1635 NH2 ARG A 233 -44.870 -22.158 46.359 1.00 28.04 N ANISOU 1635 NH2 ARG A 233 3497 3677 3478 -934 306 -3 N ATOM 1636 N THR A 234 -46.364 -27.612 51.698 1.00 37.84 N ANISOU 1636 N THR A 234 4355 4991 5029 -448 367 711 N ATOM 1637 CA THR A 234 -47.753 -27.456 52.132 1.00 39.34 C ANISOU 1637 CA THR A 234 4868 4869 5210 -504 875 -663 C ATOM 1638 C THR A 234 -47.810 -27.115 53.619 1.00 35.93 C ANISOU 1638 C THR A 234 4498 4356 4797 -534 518 409 C ATOM 1639 O THR A 234 -48.557 -26.224 54.024 1.00 36.40 O ANISOU 1639 O THR A 234 4270 4527 5030 -768 504 88 O ATOM 1640 CB THR A 234 -48.594 -28.707 51.824 1.00 41.41 C ANISOU 1640 CB THR A 234 4325 5975 5431 -667 -428 -951 C ATOM 1641 OG1 THR A 234 -48.512 -28.983 50.424 1.00 40.43 O ANISOU 1641 OG1 THR A 234 5009 5039 5313 83 106 -145 O ATOM 1642 CG2 THR A 234 -50.064 -28.488 52.208 1.00 42.71 C ANISOU 1642 CG2 THR A 234 4966 5359 5902 -1020 815 -178 C ATOM 1643 N GLU A 235 -47.004 -27.804 54.427 1.00 38.26 N ANISOU 1643 N GLU A 235 4342 5167 5025 -321 -57 35 N ATOM 1644 CA GLU A 235 -46.947 -27.499 55.849 1.00 37.03 C ANISOU 1644 CA GLU A 235 4607 4779 4682 -211 620 465 C ATOM 1645 C GLU A 235 -46.548 -26.049 56.075 1.00 41.32 C ANISOU 1645 C GLU A 235 4698 5471 5531 -733 1038 -88 C ATOM 1646 O GLU A 235 -47.135 -25.359 56.920 1.00 37.56 O ANISOU 1646 O GLU A 235 4617 4698 4955 -1152 1305 716 O ATOM 1647 CB GLU A 235 -45.971 -28.410 56.574 1.00 40.17 C ANISOU 1647 CB GLU A 235 5050 4707 5503 -12 406 498 C ATOM 1648 CG GLU A 235 -45.862 -28.088 58.053 1.00 52.22 C ANISOU 1648 CG GLU A 235 6533 7060 6245 -8 -110 -350 C ATOM 1649 CD GLU A 235 -45.075 -29.125 58.822 1.00 66.24 C ANISOU 1649 CD GLU A 235 8953 7939 8277 962 -553 714 C ATOM 1650 OE1 GLU A 235 -44.997 -28.999 60.063 1.00 64.73 O ANISOU 1650 OE1 GLU A 235 9373 7309 7912 -162 1079 2839 O ATOM 1651 OE2 GLU A 235 -44.538 -30.064 58.192 1.00 68.69 O ANISOU 1651 OE2 GLU A 235 8550 9060 8486 51 -795 -626 O ATOM 1652 N LEU A 236 -45.548 -25.583 55.323 1.00 33.85 N ANISOU 1652 N LEU A 236 4106 4195 4557 -354 158 305 N ATOM 1653 CA LEU A 236 -45.091 -24.216 55.480 1.00 27.54 C ANISOU 1653 CA LEU A 236 3222 4032 3208 -225 -21 -38 C ATOM 1654 C LEU A 236 -46.174 -23.236 55.059 1.00 30.76 C ANISOU 1654 C LEU A 236 3537 4395 3756 164 -84 -276 C ATOM 1655 O LEU A 236 -46.425 -22.241 55.758 1.00 31.05 O ANISOU 1655 O LEU A 236 3441 4009 4347 -661 -153 -422 O ATOM 1656 CB LEU A 236 -43.812 -23.955 54.667 1.00 33.61 C ANISOU 1656 CB LEU A 236 3854 4348 4566 -951 730 238 C ATOM 1657 CG LEU A 236 -43.472 -22.472 54.496 1.00 27.99 C ANISOU 1657 CG LEU A 236 3578 3876 3178 -9 169 179 C ATOM 1658 CD1 LEU A 236 -43.235 -21.779 55.830 1.00 27.15 C ANISOU 1658 CD1 LEU A 236 2671 3795 3849 -553 280 -346 C ATOM 1659 CD2 LEU A 236 -42.245 -22.322 53.614 1.00 32.40 C ANISOU 1659 CD2 LEU A 236 4063 4714 3532 -416 698 -462 C ATOM 1660 N GLN A 237 -46.821 -23.509 53.923 1.00 27.27 N ANISOU 1660 N GLN A 237 2816 4026 3517 -587 107 218 N ATOM 1661 CA GLN A 237 -47.872 -22.613 53.454 1.00 30.03 C ANISOU 1661 CA GLN A 237 3626 3706 4076 -150 -127 -17 C ATOM 1662 C GLN A 237 -49.029 -22.551 54.473 1.00 30.16 C ANISOU 1662 C GLN A 237 3725 3939 3792 -331 -242 -154 C ATOM 1663 O GLN A 237 -49.633 -21.499 54.693 1.00 34.83 O ANISOU 1663 O GLN A 237 3101 4620 5512 -158 -167 -560 O ATOM 1664 CB GLN A 237 -48.358 -23.016 52.051 1.00 35.68 C ANISOU 1664 CB GLN A 237 4340 5198 4016 45 -393 60 C ATOM 1665 CG GLN A 237 -49.205 -21.952 51.371 1.00 38.81 C ANISOU 1665 CG GLN A 237 5085 4574 5086 267 -247 46 C ATOM 1666 CD GLN A 237 -49.588 -22.310 49.944 1.00 44.19 C ANISOU 1666 CD GLN A 237 5211 6156 5420 201 -386 -299 C ATOM 1667 OE1 GLN A 237 -48.734 -22.608 49.104 1.00 42.46 O ANISOU 1667 OE1 GLN A 237 5042 5205 5885 -1122 143 -79 O ATOM 1668 NE2 GLN A 237 -50.883 -22.273 49.661 1.00 41.54 N ANISOU 1668 NE2 GLN A 237 4990 5612 5181 -26 -203 86 N ATOM 1669 N LYS A 238 -49.299 -23.673 55.123 1.00 30.89 N ANISOU 1669 N LYS A 238 3562 4328 3845 -618 -173 33 N ATOM 1670 CA LYS A 238 -50.348 -23.750 56.142 1.00 38.09 C ANISOU 1670 CA LYS A 238 4189 5967 4316 -241 299 -316 C ATOM 1671 C LYS A 238 -50.036 -22.839 57.330 1.00 40.67 C ANISOU 1671 C LYS A 238 4684 4874 5896 -391 -275 -500 C ATOM 1672 O LYS A 238 -50.892 -22.083 57.794 1.00 41.07 O ANISOU 1672 O LYS A 238 4048 5407 6147 -572 6 272 O ATOM 1673 CB LYS A 238 -50.495 -25.202 56.605 1.00 46.77 C ANISOU 1673 CB LYS A 238 5906 5761 6102 -520 265 -131 C ATOM 1674 CG LYS A 238 -51.416 -25.420 57.793 1.00 60.11 C ANISOU 1674 CG LYS A 238 7917 7932 6987 -2359 1094 15 C ATOM 1675 CD LYS A 238 -51.111 -26.764 58.442 1.00 78.34 C ANISOU 1675 CD LYS A 238 10167 8618 10981 -14 176 680 C ATOM 1676 CE LYS A 238 -52.113 -27.116 59.532 1.00 91.20 C ANISOU 1676 CE LYS A 238 10296 12191 12162 -1583 969 -1601 C ATOM 1677 NZ LYS A 238 -53.474 -27.356 58.972 1.00 89.94 N ANISOU 1677 NZ LYS A 238 8124 13268 12779 926 2691 -2933 N ATOM 1678 N ILE A 239 -48.802 -22.922 57.823 1.00 36.66 N ANISOU 1678 N ILE A 239 4616 4581 4731 286 258 -553 N ATOM 1679 CA ILE A 239 -48.348 -22.062 58.903 1.00 33.35 C ANISOU 1679 CA ILE A 239 3846 4505 4319 -110 -50 28 C ATOM 1680 C ILE A 239 -48.480 -20.586 58.530 1.00 30.31 C ANISOU 1680 C ILE A 239 3171 4436 3907 -135 -422 -89 C ATOM 1681 O ILE A 239 -48.931 -19.776 59.340 1.00 35.20 O ANISOU 1681 O ILE A 239 3969 4880 4526 -256 283 -527 O ATOM 1682 CB ILE A 239 -46.888 -22.360 59.295 1.00 38.21 C ANISOU 1682 CB ILE A 239 4273 5234 5010 213 -566 -71 C ATOM 1683 CG1 ILE A 239 -46.767 -23.766 59.904 1.00 40.44 C ANISOU 1683 CG1 ILE A 239 5032 5113 5217 139 -486 -182 C ATOM 1684 CG2 ILE A 239 -46.364 -21.276 60.239 1.00 35.86 C ANISOU 1684 CG2 ILE A 239 3835 4929 4859 283 499 -345 C ATOM 1685 CD1 ILE A 239 -45.343 -24.287 59.934 1.00 43.27 C ANISOU 1685 CD1 ILE A 239 5925 6100 4412 1391 -383 158 C ATOM 1686 N LEU A 240 -48.092 -20.235 57.307 1.00 28.05 N ANISOU 1686 N LEU A 240 2667 4013 3976 139 -294 -218 N ATOM 1687 CA LEU A 240 -48.214 -18.860 56.840 1.00 29.29 C ANISOU 1687 CA LEU A 240 3411 3827 3891 -201 -78 -265 C ATOM 1688 C LEU A 240 -49.673 -18.418 56.771 1.00 34.51 C ANISOU 1688 C LEU A 240 3609 4257 5244 -138 -179 -1022 C ATOM 1689 O LEU A 240 -50.012 -17.282 57.098 1.00 31.20 O ANISOU 1689 O LEU A 240 2764 4063 5024 -36 -561 -39 O ATOM 1690 CB LEU A 240 -47.601 -18.710 55.460 1.00 31.61 C ANISOU 1690 CB LEU A 240 3596 4552 3860 -171 9 -508 C ATOM 1691 CG LEU A 240 -46.091 -18.879 55.312 1.00 33.97 C ANISOU 1691 CG LEU A 240 3655 4987 4263 -28 121 -599 C ATOM 1692 CD1 LEU A 240 -45.736 -18.604 53.861 1.00 31.46 C ANISOU 1692 CD1 LEU A 240 2666 4816 4468 169 454 -266 C ATOM 1693 CD2 LEU A 240 -45.311 -17.959 56.244 1.00 32.74 C ANISOU 1693 CD2 LEU A 240 3244 4999 4194 511 156 -858 C ATOM 1694 N SER A 241 -50.532 -19.324 56.323 1.00 30.73 N ANISOU 1694 N SER A 241 3370 4513 3792 -661 309 -169 N ATOM 1695 CA SER A 241 -51.955 -19.037 56.247 1.00 32.96 C ANISOU 1695 CA SER A 241 3714 4840 3968 -326 -244 -601 C ATOM 1696 C SER A 241 -52.468 -18.667 57.641 1.00 28.09 C ANISOU 1696 C SER A 241 2132 4202 4336 -275 5 -123 C ATOM 1697 O SER A 241 -53.158 -17.669 57.812 1.00 34.51 O ANISOU 1697 O SER A 241 4035 3498 5577 -401 92 -754 O ATOM 1698 CB SER A 241 -52.681 -20.262 55.692 1.00 37.24 C ANISOU 1698 CB SER A 241 3923 4958 5269 -922 -374 -106 C ATOM 1699 OG SER A 241 -54.076 -20.110 55.811 1.00 42.04 O ANISOU 1699 OG SER A 241 4713 5943 5318 298 -614 -75 O ATOM 1700 N GLU A 242 -52.089 -19.461 58.636 1.00 28.72 N ANISOU 1700 N GLU A 242 2944 3991 3974 -1111 359 287 N ATOM 1701 CA GLU A 242 -52.496 -19.243 60.025 1.00 33.93 C ANISOU 1701 CA GLU A 242 4035 4459 4396 -415 762 -225 C ATOM 1702 C GLU A 242 -51.924 -17.974 60.652 1.00 37.09 C ANISOU 1702 C GLU A 242 4148 4948 4996 -762 801 -465 C ATOM 1703 O GLU A 242 -52.584 -17.316 61.462 1.00 34.17 O ANISOU 1703 O GLU A 242 2779 5269 4932 -1069 1143 131 O ATOM 1704 CB GLU A 242 -52.130 -20.467 60.862 1.00 39.45 C ANISOU 1704 CB GLU A 242 4093 5317 5578 279 335 231 C ATOM 1705 CG GLU A 242 -52.890 -21.720 60.430 1.00 43.88 C ANISOU 1705 CG GLU A 242 4974 5684 6015 -107 565 -282 C ATOM 1706 CD GLU A 242 -52.324 -22.992 61.023 1.00 51.48 C ANISOU 1706 CD GLU A 242 6378 6520 6661 489 1237 432 C ATOM 1707 OE1 GLU A 242 -51.408 -22.910 61.870 1.00 62.84 O ANISOU 1707 OE1 GLU A 242 8705 8049 7120 567 -12 -290 O ATOM 1708 OE2 GLU A 242 -52.794 -24.082 60.638 1.00 62.19 O ANISOU 1708 OE2 GLU A 242 6075 8907 8645 -825 -116 -1054 O ATOM 1709 N ILE A 243 -50.693 -17.633 60.293 1.00 32.70 N ANISOU 1709 N ILE A 243 3673 4474 4276 -113 850 -629 N ATOM 1710 CA ILE A 243 -50.144 -16.334 60.656 1.00 33.62 C ANISOU 1710 CA ILE A 243 3207 4343 5225 -139 88 -281 C ATOM 1711 C ILE A 243 -50.938 -15.171 60.064 1.00 31.10 C ANISOU 1711 C ILE A 243 3093 4556 4168 95 227 -488 C ATOM 1712 O ILE A 243 -51.193 -14.188 60.749 1.00 32.29 O ANISOU 1712 O ILE A 243 3069 4464 4733 -397 230 -843 O ATOM 1713 CB ILE A 243 -48.656 -16.192 60.239 1.00 32.39 C ANISOU 1713 CB ILE A 243 3521 4207 4578 -469 416 220 C ATOM 1714 CG1 ILE A 243 -47.769 -16.921 61.257 1.00 37.31 C ANISOU 1714 CG1 ILE A 243 3376 5941 4858 -15 -347 -310 C ATOM 1715 CG2 ILE A 243 -48.277 -14.717 60.112 1.00 30.95 C ANISOU 1715 CG2 ILE A 243 2532 4039 5186 119 1256 -201 C ATOM 1716 CD1 ILE A 243 -47.850 -16.374 62.682 1.00 36.14 C ANISOU 1716 CD1 ILE A 243 3336 5480 4914 -22 837 -139 C ATOM 1717 N ILE A 244 -51.299 -15.268 58.788 1.00 27.22 N ANISOU 1717 N ILE A 244 2334 4103 3904 -415 358 10 N ATOM 1718 CA ILE A 244 -52.043 -14.201 58.144 1.00 31.29 C ANISOU 1718 CA ILE A 244 3990 4053 3844 -461 541 945 C ATOM 1719 C ILE A 244 -53.382 -13.980 58.847 1.00 38.75 C ANISOU 1719 C ILE A 244 4260 4759 5704 -4 900 -102 C ATOM 1720 O ILE A 244 -53.799 -12.841 59.074 1.00 34.65 O ANISOU 1720 O ILE A 244 3324 5000 4838 125 -261 -543 O ATOM 1721 CB ILE A 244 -52.327 -14.531 56.669 1.00 35.76 C ANISOU 1721 CB ILE A 244 4343 4662 4581 261 -89 -176 C ATOM 1722 CG1 ILE A 244 -51.036 -14.489 55.856 1.00 37.18 C ANISOU 1722 CG1 ILE A 244 4518 4756 4851 252 122 -247 C ATOM 1723 CG2 ILE A 244 -53.372 -13.572 56.086 1.00 31.54 C ANISOU 1723 CG2 ILE A 244 3693 3675 4614 -278 800 286 C ATOM 1724 CD1 ILE A 244 -51.178 -15.121 54.487 1.00 37.96 C ANISOU 1724 CD1 ILE A 244 5314 4451 4656 -330 144 105 C ATOM 1725 N ILE A 245 -54.054 -15.077 59.182 1.00 40.25 N ANISOU 1725 N ILE A 245 4449 5520 5323 -644 796 43 N ATOM 1726 CA ILE A 245 -55.346 -14.994 59.855 1.00 38.68 C ANISOU 1726 CA ILE A 245 4493 5623 4580 -668 530 -41 C ATOM 1727 C ILE A 245 -55.173 -14.371 61.243 1.00 40.89 C ANISOU 1727 C ILE A 245 4650 5312 5572 -6 39 -885 C ATOM 1728 O ILE A 245 -55.898 -13.441 61.595 1.00 39.65 O ANISOU 1728 O ILE A 245 4394 4849 5823 -435 416 -569 O ATOM 1729 CB ILE A 245 -56.038 -16.369 59.930 1.00 32.87 C ANISOU 1729 CB ILE A 245 3708 4497 4284 232 226 -536 C ATOM 1730 CG1 ILE A 245 -56.504 -16.793 58.538 1.00 29.67 C ANISOU 1730 CG1 ILE A 245 2904 4153 4215 415 658 -790 C ATOM 1731 CG2 ILE A 245 -57.234 -16.323 60.871 1.00 37.07 C ANISOU 1731 CG2 ILE A 245 4220 5493 4372 -425 640 24 C ATOM 1732 CD1 ILE A 245 -56.913 -18.255 58.454 1.00 34.58 C ANISOU 1732 CD1 ILE A 245 3502 4326 5310 21 -169 332 C ATOM 1733 N ALA A 246 -54.196 -14.862 62.010 1.00 40.23 N ANISOU 1733 N ALA A 246 5255 5337 4692 -972 212 588 N ATOM 1734 CA ALA A 246 -53.881 -14.286 63.326 1.00 37.27 C ANISOU 1734 CA ALA A 246 3965 5548 4648 -39 600 334 C ATOM 1735 C ALA A 246 -53.559 -12.789 63.305 1.00 42.85 C ANISOU 1735 C ALA A 246 4824 5745 5711 -488 -177 -218 C ATOM 1736 O ALA A 246 -53.983 -12.062 64.210 1.00 44.75 O ANISOU 1736 O ALA A 246 4397 6749 5854 -38 197 56 O ATOM 1737 CB ALA A 246 -52.771 -15.068 64.018 1.00 38.25 C ANISOU 1737 CB ALA A 246 4298 5643 4592 301 512 119 C ATOM 1738 N ARG A 247 -52.814 -12.346 62.296 1.00 38.05 N ANISOU 1738 N ARG A 247 4439 5038 4979 119 -651 17 N ATOM 1739 CA ARG A 247 -52.475 -10.934 62.156 1.00 39.83 C ANISOU 1739 CA ARG A 247 4879 5132 5120 -245 -419 688 C ATOM 1740 C ARG A 247 -53.738 -10.107 61.949 1.00 42.91 C ANISOU 1740 C ARG A 247 4146 5948 6207 135 167 -833 C ATOM 1741 O ARG A 247 -53.886 -9.025 62.516 1.00 44.69 O ANISOU 1741 O ARG A 247 4430 6081 6469 -1144 187 -1308 O ATOM 1742 CB ARG A 247 -51.510 -10.726 60.987 1.00 40.51 C ANISOU 1742 CB ARG A 247 5574 4754 5061 257 401 -487 C ATOM 1743 CG ARG A 247 -50.331 -11.685 60.978 1.00 47.03 C ANISOU 1743 CG ARG A 247 5456 5975 6435 824 180 -1084 C ATOM 1744 CD ARG A 247 -49.015 -10.943 61.153 1.00 48.99 C ANISOU 1744 CD ARG A 247 7149 5433 6032 -1439 783 -72 C ATOM 1745 NE ARG A 247 -48.380 -10.646 59.872 1.00 41.16 N ANISOU 1745 NE ARG A 247 5770 4300 5566 -203 1085 -966 N ATOM 1746 CZ ARG A 247 -47.109 -10.912 59.589 1.00 34.13 C ANISOU 1746 CZ ARG A 247 4856 4114 3998 -195 -160 -164 C ATOM 1747 NH1 ARG A 247 -46.331 -11.484 60.498 1.00 30.97 N ANISOU 1747 NH1 ARG A 247 4261 3684 3822 -920 55 -267 N ATOM 1748 NH2 ARG A 247 -46.616 -10.607 58.397 1.00 32.21 N ANISOU 1748 NH2 ARG A 247 2695 5179 4363 -268 871 232 N ATOM 1749 N LYS A 248 -54.649 -10.633 61.137 1.00 41.06 N ANISOU 1749 N LYS A 248 4139 5355 6105 -561 853 -600 N ATOM 1750 CA LYS A 248 -55.955 -10.013 60.933 1.00 39.77 C ANISOU 1750 CA LYS A 248 5189 4773 5148 -36 -291 -618 C ATOM 1751 C LYS A 248 -56.698 -9.839 62.267 1.00 36.42 C ANISOU 1751 C LYS A 248 3779 4803 5253 -86 -514 56 C ATOM 1752 O LYS A 248 -57.279 -8.784 62.525 1.00 42.28 O ANISOU 1752 O LYS A 248 4973 5504 5587 252 -366 -1021 O ATOM 1753 CB LYS A 248 -56.776 -10.820 59.935 1.00 40.21 C ANISOU 1753 CB LYS A 248 3218 7168 4890 17 -634 -285 C ATOM 1754 CG LYS A 248 -56.295 -10.637 58.509 1.00 44.89 C ANISOU 1754 CG LYS A 248 4975 7301 4778 97 -54 -494 C ATOM 1755 CD LYS A 248 -57.244 -11.265 57.508 1.00 46.23 C ANISOU 1755 CD LYS A 248 5768 6479 5317 -1146 -12 -132 C ATOM 1756 CE LYS A 248 -56.815 -10.877 56.105 1.00 43.07 C ANISOU 1756 CE LYS A 248 5129 6346 4889 530 -378 15 C ATOM 1757 NZ LYS A 248 -57.483 -11.729 55.096 1.00 45.17 N ANISOU 1757 NZ LYS A 248 5006 6271 5884 546 1117 -1765 N ATOM 1758 N GLU A 249 -56.649 -10.861 63.119 1.00 31.77 N ANISOU 1758 N GLU A 249 3209 4709 4152 -898 -693 -350 N ATOM 1759 CA GLU A 249 -57.234 -10.782 64.464 1.00 37.84 C ANISOU 1759 CA GLU A 249 4190 5512 4674 -433 191 -298 C ATOM 1760 C GLU A 249 -56.542 -9.760 65.371 1.00 41.94 C ANISOU 1760 C GLU A 249 5123 5211 5599 -54 -141 -891 C ATOM 1761 O GLU A 249 -57.214 -9.053 66.128 1.00 42.59 O ANISOU 1761 O GLU A 249 3776 7022 5384 732 -365 -524 O ATOM 1762 CB GLU A 249 -57.232 -12.159 65.138 1.00 46.14 C ANISOU 1762 CB GLU A 249 5712 5486 6332 904 -1111 -110 C ATOM 1763 CG GLU A 249 -58.454 -13.010 64.831 1.00 59.94 C ANISOU 1763 CG GLU A 249 6144 7247 9382 -1227 857 1546 C ATOM 1764 CD GLU A 249 -58.143 -14.497 64.747 1.00 70.57 C ANISOU 1764 CD GLU A 249 9206 8624 8980 812 392 13 C ATOM 1765 OE1 GLU A 249 -57.400 -15.009 65.610 1.00 83.04 O ANISOU 1765 OE1 GLU A 249 10502 10131 10916 2264 147 2508 O ATOM 1766 OE2 GLU A 249 -58.650 -15.157 63.813 1.00 79.76 O ANISOU 1766 OE2 GLU A 249 9219 9510 11576 -221 2911 -3337 O ATOM 1767 N GLU A 250 -55.210 -9.691 65.313 1.00 45.19 N ANISOU 1767 N GLU A 250 4932 6498 5739 -57 506 -1317 N ATOM 1768 CA GLU A 250 -54.456 -8.674 66.062 1.00 45.98 C ANISOU 1768 CA GLU A 250 5622 5187 6660 -224 360 -798 C ATOM 1769 C GLU A 250 -54.892 -7.282 65.648 1.00 41.70 C ANISOU 1769 C GLU A 250 3783 6245 5816 389 -372 -337 C ATOM 1770 O GLU A 250 -55.072 -6.407 66.496 1.00 45.03 O ANISOU 1770 O GLU A 250 4850 6657 5603 191 -605 -189 O ATOM 1771 CB GLU A 250 -52.947 -8.750 65.794 1.00 55.39 C ANISOU 1771 CB GLU A 250 5802 7298 7943 765 662 -1151 C ATOM 1772 CG GLU A 250 -52.194 -9.952 66.333 1.00 58.59 C ANISOU 1772 CG GLU A 250 8420 7359 6480 -54 -1338 -348 C ATOM 1773 CD GLU A 250 -50.818 -10.084 65.683 1.00 75.52 C ANISOU 1773 CD GLU A 250 7336 9216 12142 -626 -809 965 C ATOM 1774 OE1 GLU A 250 -50.308 -9.081 65.126 1.00 69.45 O ANISOU 1774 OE1 GLU A 250 5645 10647 10095 -880 -1207 956 O ATOM 1775 OE2 GLU A 250 -50.246 -11.195 65.714 1.00 83.10 O ANISOU 1775 OE2 GLU A 250 6545 11254 13773 812 -3271 1807 O ATOM 1776 N GLU A 251 -55.013 -7.061 64.339 1.00 39.04 N ANISOU 1776 N GLU A 251 4128 5406 5296 -45 298 -1076 N ATOM 1777 CA GLU A 251 -55.391 -5.745 63.826 1.00 45.62 C ANISOU 1777 CA GLU A 251 5019 6365 5947 -8 -1 27 C ATOM 1778 C GLU A 251 -56.789 -5.353 64.300 1.00 47.68 C ANISOU 1778 C GLU A 251 5382 6151 6581 7 406 -677 C ATOM 1779 O GLU A 251 -57.025 -4.203 64.652 1.00 45.53 O ANISOU 1779 O GLU A 251 4158 5952 7189 -922 -1105 -1500 O ATOM 1780 CB GLU A 251 -55.329 -5.698 62.299 1.00 47.15 C ANISOU 1780 CB GLU A 251 5670 6411 5834 -772 47 -2098 C ATOM 1781 CG GLU A 251 -53.926 -5.715 61.716 1.00 59.10 C ANISOU 1781 CG GLU A 251 6937 8674 6841 -732 1799 -1408 C ATOM 1782 CD GLU A 251 -53.917 -6.103 60.251 1.00 64.49 C ANISOU 1782 CD GLU A 251 8702 9368 6430 239 -38 -531 C ATOM 1783 OE1 GLU A 251 -54.950 -5.914 59.575 1.00 63.94 O ANISOU 1783 OE1 GLU A 251 7600 8701 7993 -1548 -125 622 O ATOM 1784 OE2 GLU A 251 -52.875 -6.604 59.779 1.00 65.43 O ANISOU 1784 OE2 GLU A 251 9190 9772 5895 488 508 196 O ATOM 1785 N VAL A 252 -57.709 -6.310 64.322 1.00 50.22 N ANISOU 1785 N VAL A 252 5873 7176 6031 -921 649 -1046 N ATOM 1786 CA VAL A 252 -59.083 -6.026 64.760 1.00 49.58 C ANISOU 1786 CA VAL A 252 5938 6418 6482 -457 754 -641 C ATOM 1787 C VAL A 252 -59.185 -5.697 66.260 1.00 48.41 C ANISOU 1787 C VAL A 252 5326 6629 6436 -240 -354 -939 C ATOM 1788 O VAL A 252 -59.809 -4.701 66.631 1.00 50.30 O ANISOU 1788 O VAL A 252 6020 6499 6591 -300 -1139 -1469 O ATOM 1789 CB VAL A 252 -60.040 -7.173 64.383 1.00 46.79 C ANISOU 1789 CB VAL A 252 4650 7909 5219 -473 -168 -581 C ATOM 1790 CG1 VAL A 252 -61.388 -7.023 65.093 1.00 41.92 C ANISOU 1790 CG1 VAL A 252 4487 6309 5129 -207 -493 -503 C ATOM 1791 CG2 VAL A 252 -60.213 -7.226 62.871 1.00 37.87 C ANISOU 1791 CG2 VAL A 252 2808 6449 5130 -730 451 -1564 C ATOM 1792 N ASN A 253 -58.568 -6.523 67.105 1.00 58.64 N ANISOU 1792 N ASN A 253 6591 7799 7890 466 -24 321 N ATOM 1793 CA ASN A 253 -58.641 -6.369 68.570 1.00 66.35 C ANISOU 1793 CA ASN A 253 8218 8695 8294 -416 215 185 C ATOM 1794 C ASN A 253 -57.803 -5.225 69.139 1.00 76.29 C ANISOU 1794 C ASN A 253 10097 9831 9055 -800 82 -915 C ATOM 1795 O ASN A 253 -58.264 -4.484 70.005 1.00 82.12 O ANISOU 1795 O ASN A 253 10557 13301 7344 214 295 -1040 O ATOM 1796 CB ASN A 253 -58.287 -7.687 69.271 1.00 73.37 C ANISOU 1796 CB ASN A 253 10324 9753 7800 1241 1307 477 C ATOM 1797 CG ASN A 253 -59.182 -8.837 68.839 1.00 78.18 C ANISOU 1797 CG ASN A 253 8970 11054 9680 668 1910 1362 C ATOM 1798 OD1 ASN A 253 -60.115 -8.653 68.058 1.00 88.87 O ANISOU 1798 OD1 ASN A 253 9986 13079 10700 2033 729 1556 O ATOM 1799 ND2 ASN A 253 -58.898 -10.031 69.344 1.00 80.01 N ANISOU 1799 ND2 ASN A 253 8721 12531 9145 1660 1361 2770 N ATOM 1800 N LYS A 254 -56.564 -5.108 68.666 1.00 79.61 N ANISOU 1800 N LYS A 254 10672 12836 6740 -384 614 -1326 N ATOM 1801 CA LYS A 254 -55.720 -3.947 68.937 1.00 81.74 C ANISOU 1801 CA LYS A 254 9925 12243 8888 248 -176 -2050 C ATOM 1802 C LYS A 254 -55.472 -3.308 67.580 1.00 80.00 C ANISOU 1802 C LYS A 254 8937 11176 10283 -352 2190 -2342 C ATOM 1803 O LYS A 254 -56.025 -3.762 66.590 1.00 77.51 O ANISOU 1803 O LYS A 254 8488 11462 9498 158 201 -711 O ATOM 1804 CB LYS A 254 -54.403 -4.386 69.585 1.00 79.25 C ANISOU 1804 CB LYS A 254 11440 14258 4412 40 -1653 -3615 C ATOM 1805 CG LYS A 254 -53.423 -3.260 69.919 1.00110.68 C ANISOU 1805 CG LYS A 254 15928 13560 12562 -2243 1625 -797 C ATOM 1806 CD LYS A 254 -54.001 -2.240 70.897 1.00122.23 C ANISOU 1806 CD LYS A 254 17122 13001 16319 104 1945 -772 C ATOM 1807 CE LYS A 254 -52.986 -1.142 71.230 1.00107.45 C ANISOU 1807 CE LYS A 254 15169 13722 11932 1162 -1792 494 C ATOM 1808 NZ LYS A 254 -52.024 -1.552 72.315 1.00 75.01 N ANISOU 1808 NZ LYS A 254 11236 8181 9083 -1156 391 -2148 N ATOM 1809 N ASP A 255 -54.666 -2.257 67.504 1.00 93.28 N ANISOU 1809 N ASP A 255 11165 11903 12373 -2172 1313 -187 N ATOM 1810 CA ASP A 255 -54.269 -1.793 66.180 1.00100.90 C ANISOU 1810 CA ASP A 255 13755 12590 11993 -1965 -470 947 C ATOM 1811 C ASP A 255 -52.897 -2.366 65.796 1.00105.95 C ANISOU 1811 C ASP A 255 14221 12285 13748 -1267 -1448 337 C ATOM 1812 O ASP A 255 -52.245 -1.870 64.871 1.00127.85 O ANISOU 1812 O ASP A 255 18647 13551 16379 -3008 -384 2979 O ATOM 1813 CB ASP A 255 -54.317 -0.264 66.068 1.00101.60 C ANISOU 1813 CB ASP A 255 12330 12683 13588 -464 -489 406 C ATOM 1814 CG ASP A 255 -54.774 0.204 64.687 1.00105.45 C ANISOU 1814 CG ASP A 255 10900 14106 15060 667 -3247 -1254 C ATOM 1815 OD1 ASP A 255 -55.039 -0.659 63.815 1.00107.47 O ANISOU 1815 OD1 ASP A 255 10324 13310 17199 -775 -1589 -1802 O ATOM 1816 OD2 ASP A 255 -54.875 1.437 64.471 1.00114.69 O ANISOU 1816 OD2 ASP A 255 8038 13341 22198 7599 -1263 -3983 O ATOM 1817 N SER A 256 -52.478 -3.418 66.504 1.00 94.17 N ANISOU 1817 N SER A 256 12998 10473 12309 -1215 -849 -1641 N ATOM 1818 CA SER A 256 -51.208 -4.098 66.228 1.00 95.43 C ANISOU 1818 CA SER A 256 13068 11045 12144 -1313 692 -834 C ATOM 1819 C SER A 256 -51.112 -4.475 64.754 1.00 87.59 C ANISOU 1819 C SER A 256 11700 9513 12066 -847 948 -706 C ATOM 1820 O SER A 256 -52.020 -5.107 64.210 1.00 85.66 O ANISOU 1820 O SER A 256 6991 12974 12580 2437 863 -3356 O ATOM 1821 CB SER A 256 -51.055 -5.362 67.088 1.00 94.09 C ANISOU 1821 CB SER A 256 11689 12236 11825 1223 -793 -947 C ATOM 1822 OG SER A 256 -51.339 -5.106 68.461 1.00 98.35 O ANISOU 1822 OG SER A 256 12625 12937 11805 -1211 970 413 O ATOM 1823 N SER A 257 -50.015 -4.074 64.114 1.00 84.48 N ANISOU 1823 N SER A 257 10504 10995 10597 -2221 -1229 -313 N ATOM 1824 CA SER A 257 -49.763 -4.407 62.714 1.00 78.80 C ANISOU 1824 CA SER A 257 8727 10020 11192 -117 690 412 C ATOM 1825 C SER A 257 -48.291 -4.729 62.508 1.00 70.72 C ANISOU 1825 C SER A 257 9208 7856 9806 870 250 -1409 C ATOM 1826 O SER A 257 -47.417 -3.921 62.816 1.00 76.66 O ANISOU 1826 O SER A 257 6973 10606 11548 836 -790 -816 O ATOM 1827 CB SER A 257 -50.174 -3.256 61.798 1.00 81.57 C ANISOU 1827 CB SER A 257 9574 10808 10610 526 3016 1159 C ATOM 1828 OG SER A 257 -49.348 -2.127 62.018 1.00 85.71 O ANISOU 1828 OG SER A 257 9965 11317 11284 373 1569 1656 O ATOM 1829 N THR A 258 -48.030 -5.913 61.975 1.00 53.40 N ANISOU 1829 N THR A 258 6002 7161 7126 -1404 -251 -1423 N ATOM 1830 CA THR A 258 -46.675 -6.408 61.796 1.00 52.37 C ANISOU 1830 CA THR A 258 6872 6650 6374 185 -619 -400 C ATOM 1831 C THR A 258 -46.206 -6.167 60.368 1.00 50.94 C ANISOU 1831 C THR A 258 5086 6975 7291 260 651 -701 C ATOM 1832 O THR A 258 -46.870 -6.562 59.413 1.00 56.45 O ANISOU 1832 O THR A 258 6627 8030 6791 777 1036 -1862 O ATOM 1833 CB THR A 258 -46.619 -7.905 62.139 1.00 47.26 C ANISOU 1833 CB THR A 258 4927 6692 6335 -1053 -208 445 C ATOM 1834 OG1 THR A 258 -46.902 -8.059 63.531 1.00 48.75 O ANISOU 1834 OG1 THR A 258 6263 6481 5779 663 56 -1158 O ATOM 1835 CG2 THR A 258 -45.251 -8.512 61.827 1.00 51.90 C ANISOU 1835 CG2 THR A 258 6330 6900 6488 -120 600 -425 C ATOM 1836 N SER A 259 -45.066 -5.504 60.227 1.00 38.57 N ANISOU 1836 N SER A 259 5015 4355 5283 511 -463 -1114 N ATOM 1837 CA SER A 259 -44.529 -5.203 58.916 1.00 42.97 C ANISOU 1837 CA SER A 259 5200 5429 5697 -495 -335 -279 C ATOM 1838 C SER A 259 -43.299 -6.068 58.664 1.00 46.31 C ANISOU 1838 C SER A 259 5796 5851 5947 -48 -166 -991 C ATOM 1839 O SER A 259 -42.285 -5.930 59.356 1.00 49.66 O ANISOU 1839 O SER A 259 5378 7178 6312 -487 91 -584 O ATOM 1840 CB SER A 259 -44.163 -3.727 58.842 1.00 48.86 C ANISOU 1840 CB SER A 259 7236 5011 6314 183 741 269 C ATOM 1841 OG SER A 259 -44.629 -3.168 57.628 1.00 58.66 O ANISOU 1841 OG SER A 259 7473 8510 6302 -256 224 999 O ATOM 1842 N ASP A 260 -43.386 -6.973 57.691 1.00 36.14 N ANISOU 1842 N ASP A 260 4093 4707 4931 0 331 68 N ATOM 1843 CA ASP A 260 -42.259 -7.862 57.398 1.00 32.91 C ANISOU 1843 CA ASP A 260 3625 4413 4466 -12 -571 177 C ATOM 1844 C ASP A 260 -42.216 -8.322 55.948 1.00 33.96 C ANISOU 1844 C ASP A 260 4212 4307 4382 83 449 170 C ATOM 1845 O ASP A 260 -42.928 -7.786 55.091 1.00 35.68 O ANISOU 1845 O ASP A 260 3793 4746 5017 -731 -118 533 O ATOM 1846 CB ASP A 260 -42.208 -9.049 58.381 1.00 31.63 C ANISOU 1846 CB ASP A 260 3437 4462 4117 326 -49 -40 C ATOM 1847 CG ASP A 260 -43.372 -10.055 58.206 1.00 34.78 C ANISOU 1847 CG ASP A 260 4223 4262 4729 114 -104 0 C ATOM 1848 OD1 ASP A 260 -44.292 -9.872 57.372 1.00 32.70 O ANISOU 1848 OD1 ASP A 260 3548 4617 4258 184 362 -130 O ATOM 1849 OD2 ASP A 260 -43.347 -11.068 58.928 1.00 36.38 O ANISOU 1849 OD2 ASP A 260 3770 5065 4987 -340 1005 448 O ATOM 1850 N LEU A 261 -41.377 -9.307 55.660 1.00 30.83 N ANISOU 1850 N LEU A 261 3694 3978 4041 -288 -31 339 N ATOM 1851 CA LEU A 261 -41.280 -9.815 54.292 1.00 33.03 C ANISOU 1851 CA LEU A 261 4418 3619 4511 -224 -105 -438 C ATOM 1852 C LEU A 261 -42.613 -10.427 53.848 1.00 33.60 C ANISOU 1852 C LEU A 261 3629 5109 4026 16 20 455 C ATOM 1853 O LEU A 261 -43.021 -10.305 52.687 1.00 29.33 O ANISOU 1853 O LEU A 261 3039 4172 3932 -298 341 -14 O ATOM 1854 CB LEU A 261 -40.190 -10.879 54.206 1.00 33.59 C ANISOU 1854 CB LEU A 261 3129 4858 4775 -205 138 -242 C ATOM 1855 CG LEU A 261 -40.206 -11.783 52.965 1.00 36.85 C ANISOU 1855 CG LEU A 261 4795 5007 4198 -82 271 63 C ATOM 1856 CD1 LEU A 261 -39.753 -11.002 51.746 1.00 37.54 C ANISOU 1856 CD1 LEU A 261 5033 4694 4536 -586 185 115 C ATOM 1857 CD2 LEU A 261 -39.319 -13.000 53.160 1.00 39.10 C ANISOU 1857 CD2 LEU A 261 6058 4449 4346 -83 -168 -386 C ATOM 1858 N LEU A 262 -43.266 -11.118 54.780 1.00 32.23 N ANISOU 1858 N LEU A 262 3873 4067 4303 -28 346 -70 N ATOM 1859 CA LEU A 262 -44.555 -11.736 54.509 1.00 32.14 C ANISOU 1859 CA LEU A 262 3795 4178 4237 -125 569 451 C ATOM 1860 C LEU A 262 -45.596 -10.655 54.139 1.00 33.56 C ANISOU 1860 C LEU A 262 3919 4717 4115 149 339 145 C ATOM 1861 O LEU A 262 -46.131 -10.657 53.026 1.00 35.57 O ANISOU 1861 O LEU A 262 3418 5048 5048 113 -131 466 O ATOM 1862 CB LEU A 262 -44.983 -12.628 55.697 1.00 27.82 C ANISOU 1862 CB LEU A 262 2978 3871 3720 25 -802 595 C ATOM 1863 CG LEU A 262 -46.377 -13.286 55.627 1.00 26.43 C ANISOU 1863 CG LEU A 262 3326 2840 3873 -16 -182 140 C ATOM 1864 CD1 LEU A 262 -46.551 -14.125 54.365 1.00 26.56 C ANISOU 1864 CD1 LEU A 262 2699 3850 3542 -176 204 17 C ATOM 1865 CD2 LEU A 262 -46.670 -14.117 56.865 1.00 24.18 C ANISOU 1865 CD2 LEU A 262 2823 3221 3141 -20 260 -553 C ATOM 1866 N SER A 263 -45.839 -9.709 55.044 1.00 35.80 N ANISOU 1866 N SER A 263 4144 4429 5030 72 -588 -392 N ATOM 1867 CA SER A 263 -46.782 -8.626 54.774 1.00 36.55 C ANISOU 1867 CA SER A 263 4524 4665 4699 203 -414 305 C ATOM 1868 C SER A 263 -46.412 -7.879 53.494 1.00 36.40 C ANISOU 1868 C SER A 263 4279 4624 4926 -281 -337 413 C ATOM 1869 O SER A 263 -47.279 -7.503 52.709 1.00 34.15 O ANISOU 1869 O SER A 263 3966 4305 4701 281 -263 -269 O ATOM 1870 CB SER A 263 -46.838 -7.652 55.945 1.00 41.33 C ANISOU 1870 CB SER A 263 5018 5077 5607 373 595 -249 C ATOM 1871 OG SER A 263 -45.628 -6.917 56.047 1.00 45.46 O ANISOU 1871 OG SER A 263 6036 5345 5890 -327 -244 -16 O ATOM 1872 N GLY A 264 -45.118 -7.680 53.277 1.00 34.30 N ANISOU 1872 N GLY A 264 3819 4482 4729 419 -28 146 N ATOM 1873 CA GLY A 264 -44.651 -6.992 52.069 1.00 33.75 C ANISOU 1873 CA GLY A 264 4285 3997 4539 167 518 -409 C ATOM 1874 C GLY A 264 -44.985 -7.724 50.787 1.00 31.76 C ANISOU 1874 C GLY A 264 3586 4217 4265 -79 148 123 C ATOM 1875 O GLY A 264 -45.511 -7.132 49.856 1.00 38.72 O ANISOU 1875 O GLY A 264 4770 4664 5276 1385 297 509 O ATOM 1876 N LEU A 265 -44.684 -9.017 50.715 1.00 31.06 N ANISOU 1876 N LEU A 265 3134 4011 4655 -441 194 -502 N ATOM 1877 CA LEU A 265 -45.005 -9.756 49.492 1.00 30.43 C ANISOU 1877 CA LEU A 265 3857 3807 3897 326 -96 -19 C ATOM 1878 C LEU A 265 -46.519 -9.868 49.270 1.00 32.17 C ANISOU 1878 C LEU A 265 4050 4074 4096 460 -33 -102 C ATOM 1879 O LEU A 265 -47.001 -9.824 48.140 1.00 36.24 O ANISOU 1879 O LEU A 265 4382 4678 4708 355 -798 -191 O ATOM 1880 CB LEU A 265 -44.360 -11.139 49.508 1.00 30.84 C ANISOU 1880 CB LEU A 265 3445 3998 4272 477 413 -471 C ATOM 1881 CG LEU A 265 -42.832 -11.081 49.406 1.00 30.15 C ANISOU 1881 CG LEU A 265 3426 3933 4097 -79 -151 0 C ATOM 1882 CD1 LEU A 265 -42.239 -12.475 49.560 1.00 30.24 C ANISOU 1882 CD1 LEU A 265 3779 3662 4048 -94 -295 -767 C ATOM 1883 CD2 LEU A 265 -42.424 -10.440 48.077 1.00 34.21 C ANISOU 1883 CD2 LEU A 265 3877 4728 4390 -688 370 -116 C ATOM 1884 N LEU A 266 -47.260 -10.009 50.360 1.00 35.03 N ANISOU 1884 N LEU A 266 4259 4318 4731 -63 229 -4 N ATOM 1885 CA LEU A 266 -48.715 -10.128 50.293 1.00 40.41 C ANISOU 1885 CA LEU A 266 4362 5666 5324 408 -248 662 C ATOM 1886 C LEU A 266 -49.384 -8.875 49.738 1.00 42.39 C ANISOU 1886 C LEU A 266 4681 5460 5964 347 -34 818 C ATOM 1887 O LEU A 266 -50.457 -8.964 49.171 1.00 43.91 O ANISOU 1887 O LEU A 266 4617 6477 5587 386 273 478 O ATOM 1888 CB LEU A 266 -49.291 -10.453 51.666 1.00 33.90 C ANISOU 1888 CB LEU A 266 2851 4990 5039 802 -442 -183 C ATOM 1889 CG LEU A 266 -49.205 -11.892 52.166 1.00 38.43 C ANISOU 1889 CG LEU A 266 4228 5142 5231 -229 90 -43 C ATOM 1890 CD1 LEU A 266 -49.590 -11.909 53.638 1.00 37.09 C ANISOU 1890 CD1 LEU A 266 3849 5407 4833 -728 -415 -227 C ATOM 1891 CD2 LEU A 266 -50.074 -12.841 51.344 1.00 38.81 C ANISOU 1891 CD2 LEU A 266 4135 4937 5675 133 170 -382 C ATOM 1892 N SER A 267 -48.744 -7.719 49.893 1.00 44.00 N ANISOU 1892 N SER A 267 6185 5338 5193 524 -3 -428 N ATOM 1893 CA SER A 267 -49.278 -6.471 49.349 1.00 45.69 C ANISOU 1893 CA SER A 267 5407 5811 6139 344 -442 101 C ATOM 1894 C SER A 267 -48.817 -6.190 47.901 1.00 48.35 C ANISOU 1894 C SER A 267 5590 6227 6553 784 199 229 C ATOM 1895 O SER A 267 -49.170 -5.162 47.315 1.00 51.11 O ANISOU 1895 O SER A 267 6380 5579 7460 500 610 326 O ATOM 1896 CB SER A 267 -48.909 -5.302 50.261 1.00 48.87 C ANISOU 1896 CB SER A 267 5991 6251 6325 626 -1623 47 C ATOM 1897 OG SER A 267 -47.517 -5.054 50.194 1.00 56.13 O ANISOU 1897 OG SER A 267 6719 7406 7200 -273 -1865 78 O ATOM 1898 N ALA A 268 -48.035 -7.100 47.326 1.00 47.16 N ANISOU 1898 N ALA A 268 6311 6307 5300 463 -586 -723 N ATOM 1899 CA ALA A 268 -47.555 -6.938 45.950 1.00 45.49 C ANISOU 1899 CA ALA A 268 5761 5936 5585 788 -158 -581 C ATOM 1900 C ALA A 268 -48.688 -7.125 44.939 1.00 43.17 C ANISOU 1900 C ALA A 268 5280 5301 5820 1044 -86 435 C ATOM 1901 O ALA A 268 -49.491 -8.054 45.052 1.00 45.31 O ANISOU 1901 O ALA A 268 5161 6215 5837 578 -255 720 O ATOM 1902 CB ALA A 268 -46.431 -7.925 45.664 1.00 41.01 C ANISOU 1902 CB ALA A 268 4687 6574 4318 741 -778 247 C ATOM 1903 N VAL A 269 -48.746 -6.242 43.949 1.00 42.91 N ANISOU 1903 N VAL A 269 5920 5587 4796 413 202 128 N ATOM 1904 CA VAL A 269 -49.712 -6.377 42.861 1.00 42.74 C ANISOU 1904 CA VAL A 269 5366 5542 5330 486 247 -347 C ATOM 1905 C VAL A 269 -48.957 -6.411 41.531 1.00 38.93 C ANISOU 1905 C VAL A 269 5451 4314 5024 690 -64 70 C ATOM 1906 O VAL A 269 -48.151 -5.527 41.260 1.00 45.14 O ANISOU 1906 O VAL A 269 5898 5526 5726 250 536 456 O ATOM 1907 CB VAL A 269 -50.724 -5.215 42.845 1.00 46.99 C ANISOU 1907 CB VAL A 269 4514 7045 6293 941 -267 -593 C ATOM 1908 CG1 VAL A 269 -51.861 -5.536 41.889 1.00 45.40 C ANISOU 1908 CG1 VAL A 269 5235 6262 5752 1147 -512 -424 C ATOM 1909 CG2 VAL A 269 -51.262 -4.945 44.247 1.00 43.73 C ANISOU 1909 CG2 VAL A 269 4936 6035 5645 1021 -1366 -997 C ATOM 1910 N TYR A 270 -49.188 -7.443 40.721 1.00 34.35 N ANISOU 1910 N TYR A 270 3907 5128 4016 692 -1050 149 N ATOM 1911 CA TYR A 270 -48.491 -7.561 39.442 1.00 37.07 C ANISOU 1911 CA TYR A 270 4592 4706 4784 1021 -178 -169 C ATOM 1912 C TYR A 270 -48.991 -6.463 38.541 1.00 45.14 C ANISOU 1912 C TYR A 270 6340 5279 5532 320 140 1326 C ATOM 1913 O TYR A 270 -50.007 -5.831 38.838 1.00 51.93 O ANISOU 1913 O TYR A 270 6528 5710 7493 528 -30 1258 O ATOM 1914 CB TYR A 270 -48.758 -8.914 38.780 1.00 40.39 C ANISOU 1914 CB TYR A 270 5008 5318 5018 2 -1490 -104 C ATOM 1915 CG TYR A 270 -48.185 -10.100 39.521 1.00 43.08 C ANISOU 1915 CG TYR A 270 5528 4926 5915 304 -477 188 C ATOM 1916 CD1 TYR A 270 -46.804 -10.295 39.617 1.00 46.74 C ANISOU 1916 CD1 TYR A 270 5520 6155 6081 604 701 875 C ATOM 1917 CD2 TYR A 270 -49.025 -11.034 40.119 1.00 40.50 C ANISOU 1917 CD2 TYR A 270 4833 5425 5128 397 -422 -77 C ATOM 1918 CE1 TYR A 270 -46.283 -11.389 40.298 1.00 43.80 C ANISOU 1918 CE1 TYR A 270 5036 5593 6011 359 373 440 C ATOM 1919 CE2 TYR A 270 -48.513 -12.126 40.794 1.00 41.71 C ANISOU 1919 CE2 TYR A 270 5340 5361 5145 7 405 929 C ATOM 1920 CZ TYR A 270 -47.147 -12.299 40.880 1.00 38.92 C ANISOU 1920 CZ TYR A 270 5217 5020 4548 259 -228 31 C ATOM 1921 OH TYR A 270 -46.661 -13.390 41.556 1.00 38.17 O ANISOU 1921 OH TYR A 270 5057 4663 4781 -77 -458 -30 O ATOM 1922 N ARG A 271 -48.295 -6.235 37.437 1.00 45.10 N ANISOU 1922 N ARG A 271 4586 6912 5636 70 106 119 N ATOM 1923 CA ARG A 271 -48.712 -5.202 36.496 1.00 48.22 C ANISOU 1923 CA ARG A 271 6349 6076 5895 99 328 80 C ATOM 1924 C ARG A 271 -50.077 -5.492 35.879 1.00 53.74 C ANISOU 1924 C ARG A 271 6566 6515 7337 478 -665 1570 C ATOM 1925 O ARG A 271 -50.836 -4.572 35.615 1.00 55.68 O ANISOU 1925 O ARG A 271 5411 7649 8094 731 -2662 471 O ATOM 1926 CB ARG A 271 -47.652 -4.980 35.423 1.00 48.30 C ANISOU 1926 CB ARG A 271 5611 6628 6110 -39 -314 1916 C ATOM 1927 CG ARG A 271 -46.560 -4.026 35.877 1.00 57.06 C ANISOU 1927 CG ARG A 271 7297 6383 7999 -229 -695 -327 C ATOM 1928 CD ARG A 271 -45.265 -4.295 35.141 1.00 71.21 C ANISOU 1928 CD ARG A 271 9035 9348 8670 -74 1116 12 C ATOM 1929 NE ARG A 271 -45.462 -4.278 33.697 1.00 77.34 N ANISOU 1929 NE ARG A 271 11110 9607 8666 -86 1127 1035 N ATOM 1930 CZ ARG A 271 -44.875 -5.122 32.856 1.00 82.65 C ANISOU 1930 CZ ARG A 271 11351 9628 10422 1696 -299 -153 C ATOM 1931 NH1 ARG A 271 -44.061 -6.065 33.319 1.00 89.01 N ANISOU 1931 NH1 ARG A 271 8863 10783 14172 279 239 1050 N ATOM 1932 NH2 ARG A 271 -45.113 -5.033 31.553 1.00 85.17 N ANISOU 1932 NH2 ARG A 271 11024 10533 10802 1305 -777 1887 N ATOM 1933 N ASP A 272 -50.391 -6.769 35.675 1.00 59.96 N ANISOU 1933 N ASP A 272 6728 7308 8742 60 -1802 614 N ATOM 1934 CA ASP A 272 -51.691 -7.162 35.143 1.00 50.03 C ANISOU 1934 CA ASP A 272 6689 6085 6233 -297 -869 458 C ATOM 1935 C ASP A 272 -52.813 -6.990 36.170 1.00 53.28 C ANISOU 1935 C ASP A 272 6904 6350 6988 -158 -542 -204 C ATOM 1936 O ASP A 272 -53.929 -7.454 35.951 1.00 55.23 O ANISOU 1936 O ASP A 272 6676 8088 6219 138 -1801 1103 O ATOM 1937 CB ASP A 272 -51.657 -8.609 34.652 1.00 54.49 C ANISOU 1937 CB ASP A 272 7789 6364 6549 517 474 189 C ATOM 1938 CG ASP A 272 -51.805 -9.615 35.785 1.00 51.14 C ANISOU 1938 CG ASP A 272 6107 6945 6378 431 -1105 477 C ATOM 1939 OD1 ASP A 272 -51.741 -9.216 36.972 1.00 46.16 O ANISOU 1939 OD1 ASP A 272 4827 6668 6041 676 847 317 O ATOM 1940 OD2 ASP A 272 -51.994 -10.813 35.485 1.00 58.10 O ANISOU 1940 OD2 ASP A 272 6967 7870 7235 217 -1650 -340 O ATOM 1941 N GLY A 273 -52.513 -6.357 37.303 1.00 56.10 N ANISOU 1941 N GLY A 273 7028 8452 5835 -36 253 -294 N ATOM 1942 CA GLY A 273 -53.552 -6.017 38.280 1.00 47.96 C ANISOU 1942 CA GLY A 273 5555 6452 6212 1255 -778 574 C ATOM 1943 C GLY A 273 -53.841 -7.051 39.358 1.00 52.71 C ANISOU 1943 C GLY A 273 6239 7016 6770 1029 -20 862 C ATOM 1944 O GLY A 273 -54.432 -6.715 40.385 1.00 52.43 O ANISOU 1944 O GLY A 273 5750 7164 7005 2182 -373 1117 O ATOM 1945 N THR A 274 -53.431 -8.301 39.137 1.00 53.98 N ANISOU 1945 N THR A 274 7550 6857 6102 391 -206 -502 N ATOM 1946 CA THR A 274 -53.621 -9.379 40.127 1.00 52.27 C ANISOU 1946 CA THR A 274 5249 7001 7610 654 -210 262 C ATOM 1947 C THR A 274 -52.630 -9.264 41.305 1.00 53.26 C ANISOU 1947 C THR A 274 6574 7104 6558 -136 -152 1091 C ATOM 1948 O THR A 274 -51.562 -8.657 41.162 1.00 49.14 O ANISOU 1948 O THR A 274 5577 6355 6735 411 -1179 172 O ATOM 1949 CB THR A 274 -53.486 -10.774 39.477 1.00 60.15 C ANISOU 1949 CB THR A 274 7165 7553 8134 -290 -908 -536 C ATOM 1950 OG1 THR A 274 -52.131 -10.982 39.055 1.00 72.14 O ANISOU 1950 OG1 THR A 274 8842 9566 9001 2281 348 403 O ATOM 1951 CG2 THR A 274 -54.410 -10.910 38.270 1.00 61.92 C ANISOU 1951 CG2 THR A 274 6307 9440 7778 1004 -615 815 C ATOM 1952 N PRO A 275 -52.978 -9.834 42.478 1.00 46.69 N ANISOU 1952 N PRO A 275 5042 6475 6224 1754 195 579 N ATOM 1953 CA PRO A 275 -52.010 -9.812 43.557 1.00 47.11 C ANISOU 1953 CA PRO A 275 5442 6156 6301 423 228 94 C ATOM 1954 C PRO A 275 -51.259 -11.141 43.608 1.00 48.52 C ANISOU 1954 C PRO A 275 5907 5858 6670 152 -1371 -212 C ATOM 1955 O PRO A 275 -51.730 -12.143 43.072 1.00 46.28 O ANISOU 1955 O PRO A 275 4471 6358 6754 -49 -1306 -163 O ATOM 1956 CB PRO A 275 -52.893 -9.672 44.792 1.00 46.99 C ANISOU 1956 CB PRO A 275 5596 6144 6114 353 -13 -685 C ATOM 1957 CG PRO A 275 -54.131 -10.434 44.434 1.00 49.13 C ANISOU 1957 CG PRO A 275 6316 6241 6110 -401 -193 406 C ATOM 1958 CD PRO A 275 -54.257 -10.422 42.922 1.00 53.34 C ANISOU 1958 CD PRO A 275 6702 7397 6167 -490 -283 472 C ATOM 1959 N MET A 276 -50.097 -11.147 44.243 1.00 43.50 N ANISOU 1959 N MET A 276 4966 5946 5613 198 -282 -309 N ATOM 1960 CA MET A 276 -49.379 -12.389 44.473 1.00 41.57 C ANISOU 1960 CA MET A 276 5204 5981 4608 -43 -653 619 C ATOM 1961 C MET A 276 -50.245 -13.302 45.333 1.00 36.45 C ANISOU 1961 C MET A 276 3726 5082 5040 -118 -762 -258 C ATOM 1962 O MET A 276 -50.776 -12.863 46.355 1.00 40.46 O ANISOU 1962 O MET A 276 4648 5552 5172 644 498 853 O ATOM 1963 CB MET A 276 -48.065 -12.086 45.194 1.00 45.47 C ANISOU 1963 CB MET A 276 4851 6369 6057 99 -743 -69 C ATOM 1964 CG MET A 276 -46.992 -13.135 45.010 1.00 47.07 C ANISOU 1964 CG MET A 276 5832 6060 5989 189 -1233 -1510 C ATOM 1965 SD MET A 276 -45.408 -12.553 45.638 1.00 46.18 S ANISOU 1965 SD MET A 276 4607 6353 6583 -240 -282 386 S ATOM 1966 CE MET A 276 -45.094 -11.156 44.573 1.00 45.73 C ANISOU 1966 CE MET A 276 5406 5920 6048 1131 -620 559 C ATOM 1967 N SER A 277 -50.388 -14.561 44.925 1.00 38.48 N ANISOU 1967 N SER A 277 4711 5087 4819 298 -354 -315 N ATOM 1968 CA SER A 277 -51.147 -15.552 45.703 1.00 38.44 C ANISOU 1968 CA SER A 277 4397 5284 4924 228 -273 -103 C ATOM 1969 C SER A 277 -50.332 -15.989 46.910 1.00 38.98 C ANISOU 1969 C SER A 277 4319 5594 4895 -211 71 834 C ATOM 1970 O SER A 277 -49.129 -15.777 46.947 1.00 36.26 O ANISOU 1970 O SER A 277 4122 4967 4687 -304 -230 245 O ATOM 1971 CB SER A 277 -51.468 -16.773 44.845 1.00 38.84 C ANISOU 1971 CB SER A 277 4739 5275 4744 394 -242 -81 C ATOM 1972 OG SER A 277 -50.284 -17.431 44.434 1.00 37.83 O ANISOU 1972 OG SER A 277 4131 5298 4945 -225 -458 -540 O ATOM 1973 N LEU A 278 -50.974 -16.610 47.894 1.00 33.15 N ANISOU 1973 N LEU A 278 2873 4851 4871 194 243 275 N ATOM 1974 CA LEU A 278 -50.237 -17.156 49.024 1.00 36.87 C ANISOU 1974 CA LEU A 278 4375 4951 4683 234 -104 295 C ATOM 1975 C LEU A 278 -49.258 -18.241 48.552 1.00 36.52 C ANISOU 1975 C LEU A 278 4835 4793 4248 -41 -55 -223 C ATOM 1976 O LEU A 278 -48.160 -18.386 49.098 1.00 37.06 O ANISOU 1976 O LEU A 278 4413 4675 4991 -168 315 545 O ATOM 1977 CB LEU A 278 -51.177 -17.708 50.099 1.00 37.83 C ANISOU 1977 CB LEU A 278 4569 4926 4879 46 -86 313 C ATOM 1978 CG LEU A 278 -50.454 -18.339 51.303 1.00 40.34 C ANISOU 1978 CG LEU A 278 4700 5601 5024 -127 -331 441 C ATOM 1979 CD1 LEU A 278 -49.576 -17.329 52.038 1.00 40.80 C ANISOU 1979 CD1 LEU A 278 5327 4360 5812 125 -64 249 C ATOM 1980 CD2 LEU A 278 -51.429 -18.999 52.268 1.00 44.53 C ANISOU 1980 CD2 LEU A 278 5189 6085 5644 -513 151 352 C ATOM 1981 N HIS A 279 -49.662 -18.994 47.536 1.00 31.46 N ANISOU 1981 N HIS A 279 3262 4241 4449 -377 118 -49 N ATOM 1982 CA HIS A 279 -48.808 -19.994 46.908 1.00 35.54 C ANISOU 1982 CA HIS A 279 4475 4566 4464 -258 294 -791 C ATOM 1983 C HIS A 279 -47.497 -19.401 46.431 1.00 34.49 C ANISOU 1983 C HIS A 279 4374 4060 4669 109 89 33 C ATOM 1984 O HIS A 279 -46.416 -20.006 46.554 1.00 31.85 O ANISOU 1984 O HIS A 279 3946 4065 4091 -422 -262 128 O ATOM 1985 CB HIS A 279 -49.566 -20.611 45.739 1.00 35.06 C ANISOU 1985 CB HIS A 279 3498 5017 4804 140 -41 -758 C ATOM 1986 CG HIS A 279 -48.727 -21.523 44.888 1.00 32.37 C ANISOU 1986 CG HIS A 279 3934 4516 3847 68 -164 -616 C ATOM 1987 ND1 HIS A 279 -48.333 -22.739 45.306 1.00 35.33 N ANISOU 1987 ND1 HIS A 279 4751 4687 3985 0 -410 -171 N ATOM 1988 CD2 HIS A 279 -48.213 -21.359 43.609 1.00 30.76 C ANISOU 1988 CD2 HIS A 279 3525 4316 3847 -398 -425 204 C ATOM 1989 CE1 HIS A 279 -47.597 -23.330 44.344 1.00 33.22 C ANISOU 1989 CE1 HIS A 279 3966 4692 3964 -607 -191 -2 C ATOM 1990 NE2 HIS A 279 -47.525 -22.485 43.303 1.00 33.08 N ANISOU 1990 NE2 HIS A 279 4289 4050 4228 -582 -736 -80 N ATOM 1991 N GLU A 280 -47.587 -18.197 45.880 1.00 31.93 N ANISOU 1991 N GLU A 280 3751 4234 4145 -275 -500 145 N ATOM 1992 CA GLU A 280 -46.438 -17.541 45.281 1.00 32.11 C ANISOU 1992 CA GLU A 280 4299 4137 3762 -286 -210 416 C ATOM 1993 C GLU A 280 -45.573 -16.897 46.355 1.00 32.10 C ANISOU 1993 C GLU A 280 3912 3954 4328 -283 -38 -108 C ATOM 1994 O GLU A 280 -44.349 -16.991 46.301 1.00 33.43 O ANISOU 1994 O GLU A 280 3656 4762 4281 6 31 412 O ATOM 1995 CB GLU A 280 -46.909 -16.523 44.253 1.00 30.87 C ANISOU 1995 CB GLU A 280 3524 4121 4084 100 -534 187 C ATOM 1996 CG GLU A 280 -47.380 -17.200 42.978 1.00 34.42 C ANISOU 1996 CG GLU A 280 3990 5226 3861 279 -370 -82 C ATOM 1997 CD GLU A 280 -48.219 -16.301 42.096 1.00 37.33 C ANISOU 1997 CD GLU A 280 4776 4795 4610 784 -268 99 C ATOM 1998 OE1 GLU A 280 -48.574 -15.189 42.529 1.00 34.50 O ANISOU 1998 OE1 GLU A 280 4196 4630 4282 -251 -909 -332 O ATOM 1999 OE2 GLU A 280 -48.524 -16.717 40.957 1.00 40.96 O ANISOU 1999 OE2 GLU A 280 4630 5653 5277 538 -1201 60 O ATOM 2000 N VAL A 281 -46.219 -16.263 47.332 1.00 29.37 N ANISOU 2000 N VAL A 281 3260 4113 3784 -387 -133 200 N ATOM 2001 CA VAL A 281 -45.521 -15.680 48.473 1.00 32.42 C ANISOU 2001 CA VAL A 281 4492 4200 3624 246 -386 -299 C ATOM 2002 C VAL A 281 -44.730 -16.760 49.211 1.00 32.37 C ANISOU 2002 C VAL A 281 3952 4069 4276 -66 -103 97 C ATOM 2003 O VAL A 281 -43.585 -16.552 49.586 1.00 32.46 O ANISOU 2003 O VAL A 281 3803 4196 4332 -343 62 181 O ATOM 2004 CB VAL A 281 -46.494 -15.013 49.464 1.00 32.04 C ANISOU 2004 CB VAL A 281 4101 4226 3847 611 -313 100 C ATOM 2005 CG1 VAL A 281 -45.759 -14.623 50.748 1.00 29.97 C ANISOU 2005 CG1 VAL A 281 3841 3889 3655 -404 434 -26 C ATOM 2006 CG2 VAL A 281 -47.137 -13.787 48.838 1.00 28.68 C ANISOU 2006 CG2 VAL A 281 3546 4007 3343 -102 71 617 C ATOM 2007 N CYS A 282 -45.356 -17.914 49.419 1.00 30.87 N ANISOU 2007 N CYS A 282 3762 3772 4192 134 217 -27 N ATOM 2008 CA CYS A 282 -44.706 -19.020 50.100 1.00 29.01 C ANISOU 2008 CA CYS A 282 3473 3754 3793 -62 -19 -111 C ATOM 2009 C CYS A 282 -43.472 -19.493 49.322 1.00 29.08 C ANISOU 2009 C CYS A 282 3726 3670 3651 147 -46 -82 C ATOM 2010 O CYS A 282 -42.420 -19.761 49.908 1.00 27.87 O ANISOU 2010 O CYS A 282 3185 3721 3683 72 504 -432 O ATOM 2011 CB CYS A 282 -45.689 -20.184 50.282 1.00 32.16 C ANISOU 2011 CB CYS A 282 3592 4050 4576 -41 40 469 C ATOM 2012 SG CYS A 282 -44.899 -21.667 50.947 1.00 34.61 S ANISOU 2012 SG CYS A 282 3985 4200 4962 266 -32 74 S ATOM 2013 N GLY A 283 -43.621 -19.593 48.004 1.00 27.37 N ANISOU 2013 N GLY A 283 3538 3228 3633 -99 35 -133 N ATOM 2014 CA GLY A 283 -42.566 -20.083 47.134 1.00 31.87 C ANISOU 2014 CA GLY A 283 3670 4351 4087 -166 484 28 C ATOM 2015 C GLY A 283 -41.398 -19.123 47.097 1.00 30.74 C ANISOU 2015 C GLY A 283 3938 3775 3964 -151 -166 24 C ATOM 2016 O GLY A 283 -40.241 -19.540 47.084 1.00 31.96 O ANISOU 2016 O GLY A 283 3949 4033 4160 -93 74 509 O ATOM 2017 N MET A 284 -41.715 -17.834 47.077 1.00 29.32 N ANISOU 2017 N MET A 284 3728 3755 3656 -35 -201 -227 N ATOM 2018 CA MET A 284 -40.706 -16.785 47.120 1.00 29.46 C ANISOU 2018 CA MET A 284 3854 3549 3788 -12 -287 465 C ATOM 2019 C MET A 284 -39.924 -16.792 48.428 1.00 27.69 C ANISOU 2019 C MET A 284 3617 3528 3375 -90 85 -419 C ATOM 2020 O MET A 284 -38.701 -16.582 48.434 1.00 29.14 O ANISOU 2020 O MET A 284 3541 4152 3378 -464 320 -451 O ATOM 2021 CB MET A 284 -41.351 -15.415 46.891 1.00 27.60 C ANISOU 2021 CB MET A 284 2570 3889 4027 376 -332 -94 C ATOM 2022 CG MET A 284 -41.811 -15.198 45.455 1.00 31.59 C ANISOU 2022 CG MET A 284 3906 4276 3819 -483 -288 -59 C ATOM 2023 SD MET A 284 -40.517 -15.448 44.220 1.00 37.98 S ANISOU 2023 SD MET A 284 4497 5133 4799 -71 -458 132 S ATOM 2024 CE MET A 284 -39.560 -13.951 44.477 1.00 39.67 C ANISOU 2024 CE MET A 284 5130 4891 5051 -748 101 1467 C ATOM 2025 N ILE A 285 -40.621 -17.043 49.532 1.00 26.48 N ANISOU 2025 N ILE A 285 2985 3471 3606 -326 117 -372 N ATOM 2026 CA ILE A 285 -39.970 -17.062 50.843 1.00 28.07 C ANISOU 2026 CA ILE A 285 3375 3975 3314 378 17 385 C ATOM 2027 C ILE A 285 -39.020 -18.246 50.886 1.00 26.75 C ANISOU 2027 C ILE A 285 3674 3221 3267 30 105 -141 C ATOM 2028 O ILE A 285 -37.856 -18.139 51.334 1.00 28.59 O ANISOU 2028 O ILE A 285 3588 3757 3516 -602 30 110 O ATOM 2029 CB ILE A 285 -40.979 -17.149 52.007 1.00 26.54 C ANISOU 2029 CB ILE A 285 2883 3708 3490 -219 -112 169 C ATOM 2030 CG1 ILE A 285 -41.741 -15.824 52.182 1.00 29.66 C ANISOU 2030 CG1 ILE A 285 3552 4001 3714 24 546 127 C ATOM 2031 CG2 ILE A 285 -40.262 -17.508 53.307 1.00 27.35 C ANISOU 2031 CG2 ILE A 285 3560 3857 2972 -49 287 383 C ATOM 2032 CD1 ILE A 285 -42.875 -15.901 53.207 1.00 27.44 C ANISOU 2032 CD1 ILE A 285 3180 3884 3360 292 196 15 C ATOM 2033 N VAL A 286 -39.510 -19.371 50.390 1.00 23.75 N ANISOU 2033 N VAL A 286 2420 3425 3176 -309 310 122 N ATOM 2034 CA VAL A 286 -38.711 -20.587 50.348 1.00 26.91 C ANISOU 2034 CA VAL A 286 3572 3183 3470 -35 291 -210 C ATOM 2035 C VAL A 286 -37.476 -20.395 49.456 1.00 25.74 C ANISOU 2035 C VAL A 286 3248 2850 3680 -306 -75 -71 C ATOM 2036 O VAL A 286 -36.358 -20.764 49.825 1.00 27.61 O ANISOU 2036 O VAL A 286 3190 3166 4133 -375 218 88 O ATOM 2037 CB VAL A 286 -39.534 -21.769 49.812 1.00 27.29 C ANISOU 2037 CB VAL A 286 3038 3652 3678 -222 331 -64 C ATOM 2038 CG1 VAL A 286 -38.631 -22.972 49.586 1.00 29.70 C ANISOU 2038 CG1 VAL A 286 4029 2709 4546 -456 326 262 C ATOM 2039 CG2 VAL A 286 -40.636 -22.126 50.787 1.00 29.00 C ANISOU 2039 CG2 VAL A 286 3772 4272 2973 -366 383 117 C ATOM 2040 N ALA A 287 -37.700 -19.828 48.277 1.00 27.75 N ANISOU 2040 N ALA A 287 3415 3555 3574 -789 102 202 N ATOM 2041 CA ALA A 287 -36.639 -19.587 47.323 1.00 29.00 C ANISOU 2041 CA ALA A 287 3364 4163 3491 -107 175 267 C ATOM 2042 C ALA A 287 -35.559 -18.659 47.919 1.00 28.15 C ANISOU 2042 C ALA A 287 3760 3419 3516 31 246 -122 C ATOM 2043 O ALA A 287 -34.356 -18.930 47.804 1.00 31.46 O ANISOU 2043 O ALA A 287 3567 4001 4385 -376 -74 331 O ATOM 2044 CB ALA A 287 -37.222 -19.008 46.047 1.00 28.75 C ANISOU 2044 CB ALA A 287 2746 4309 3867 692 -25 35 C ATOM 2045 N ALA A 288 -36.000 -17.586 48.567 1.00 24.53 N ANISOU 2045 N ALA A 288 2950 3170 3200 -34 226 116 N ATOM 2046 CA ALA A 288 -35.101 -16.644 49.236 1.00 28.22 C ANISOU 2046 CA ALA A 288 3383 3579 3761 -250 -122 87 C ATOM 2047 C ALA A 288 -34.207 -17.295 50.302 1.00 29.19 C ANISOU 2047 C ALA A 288 4037 3501 3551 -160 -166 174 C ATOM 2048 O ALA A 288 -33.003 -17.017 50.363 1.00 33.25 O ANISOU 2048 O ALA A 288 4171 4085 4375 -265 340 973 O ATOM 2049 CB ALA A 288 -35.894 -15.483 49.832 1.00 30.10 C ANISOU 2049 CB ALA A 288 3240 3866 4330 -450 -373 -470 C ATOM 2050 N MET A 289 -34.791 -18.162 51.127 1.00 28.75 N ANISOU 2050 N MET A 289 3400 3978 3544 -354 307 1 N ATOM 2051 CA MET A 289 -34.052 -18.889 52.177 1.00 31.45 C ANISOU 2051 CA MET A 289 3732 4159 4058 -144 271 340 C ATOM 2052 C MET A 289 -33.059 -19.879 51.590 1.00 35.08 C ANISOU 2052 C MET A 289 4132 4300 4895 -27 -185 -459 C ATOM 2053 O MET A 289 -31.931 -20.008 52.070 1.00 36.48 O ANISOU 2053 O MET A 289 4610 4451 4799 -78 -537 567 O ATOM 2054 CB MET A 289 -35.023 -19.653 53.082 1.00 31.80 C ANISOU 2054 CB MET A 289 4296 4048 3739 -564 30 154 C ATOM 2055 CG MET A 289 -35.873 -18.748 53.949 1.00 38.32 C ANISOU 2055 CG MET A 289 4592 4846 5119 -137 661 -6 C ATOM 2056 SD MET A 289 -34.842 -17.826 55.110 1.00 49.55 S ANISOU 2056 SD MET A 289 5626 6980 6219 -473 37 -416 S ATOM 2057 CE MET A 289 -35.726 -16.273 55.175 1.00 54.98 C ANISOU 2057 CE MET A 289 6805 5867 8217 -832 781 779 C ATOM 2058 N PHE A 290 -33.506 -20.600 50.569 1.00 32.14 N ANISOU 2058 N PHE A 290 3909 4525 3777 -324 59 119 N ATOM 2059 CA PHE A 290 -32.643 -21.485 49.813 1.00 35.49 C ANISOU 2059 CA PHE A 290 4306 4552 4626 -226 365 44 C ATOM 2060 C PHE A 290 -31.469 -20.720 49.193 1.00 36.55 C ANISOU 2060 C PHE A 290 4124 3969 5792 -29 -164 1038 C ATOM 2061 O PHE A 290 -30.346 -21.207 49.180 1.00 33.46 O ANISOU 2061 O PHE A 290 3608 3640 5462 -400 -321 292 O ATOM 2062 CB PHE A 290 -33.432 -22.166 48.694 1.00 37.83 C ANISOU 2062 CB PHE A 290 4489 4959 4923 -1285 616 173 C ATOM 2063 CG PHE A 290 -33.852 -23.575 49.009 1.00 39.44 C ANISOU 2063 CG PHE A 290 5284 4433 5269 -312 21 323 C ATOM 2064 CD1 PHE A 290 -35.055 -23.835 49.663 1.00 43.79 C ANISOU 2064 CD1 PHE A 290 5595 5128 5912 -517 264 238 C ATOM 2065 CD2 PHE A 290 -33.055 -24.647 48.625 1.00 41.72 C ANISOU 2065 CD2 PHE A 290 5757 5078 5016 336 -520 -19 C ATOM 2066 CE1 PHE A 290 -35.451 -25.142 49.941 1.00 35.67 C ANISOU 2066 CE1 PHE A 290 3259 5251 5041 -139 1143 35 C ATOM 2067 CE2 PHE A 290 -33.439 -25.948 48.904 1.00 44.21 C ANISOU 2067 CE2 PHE A 290 6228 4998 5571 -240 610 -1460 C ATOM 2068 CZ PHE A 290 -34.642 -26.197 49.559 1.00 37.31 C ANISOU 2068 CZ PHE A 290 5363 3506 5306 -435 -423 -1109 C ATOM 2069 N ALA A 291 -31.726 -19.537 48.648 1.00 28.65 N ANISOU 2069 N ALA A 291 3671 3620 3593 -383 -135 256 N ATOM 2070 CA ALA A 291 -30.623 -18.776 48.065 1.00 27.56 C ANISOU 2070 CA ALA A 291 3111 3593 3768 4 -309 361 C ATOM 2071 C ALA A 291 -29.691 -18.374 49.197 1.00 29.71 C ANISOU 2071 C ALA A 291 3742 3578 3966 -409 -204 -404 C ATOM 2072 O ALA A 291 -28.513 -18.725 49.202 1.00 31.78 O ANISOU 2072 O ALA A 291 3924 4030 4120 -163 -672 -252 O ATOM 2073 CB ALA A 291 -31.123 -17.549 47.309 1.00 24.69 C ANISOU 2073 CB ALA A 291 2481 3361 3539 -226 469 570 C ATOM 2074 N GLY A 292 -30.253 -17.685 50.180 1.00 31.24 N ANISOU 2074 N GLY A 292 3945 3741 4180 -385 261 -266 N ATOM 2075 CA GLY A 292 -29.467 -17.029 51.212 1.00 33.35 C ANISOU 2075 CA GLY A 292 4693 4065 3913 223 -461 3 C ATOM 2076 C GLY A 292 -28.780 -17.863 52.278 1.00 28.03 C ANISOU 2076 C GLY A 292 3358 3631 3659 119 36 -267 C ATOM 2077 O GLY A 292 -27.762 -17.444 52.788 1.00 30.55 O ANISOU 2077 O GLY A 292 3659 4025 3923 -538 118 -222 O ATOM 2078 N GLN A 293 -29.316 -19.034 52.622 1.00 25.98 N ANISOU 2078 N GLN A 293 3121 3544 3206 36 570 92 N ATOM 2079 CA GLN A 293 -28.825 -19.738 53.803 1.00 29.40 C ANISOU 2079 CA GLN A 293 3323 3776 4069 -199 -176 606 C ATOM 2080 C GLN A 293 -27.371 -20.210 53.659 1.00 32.16 C ANISOU 2080 C GLN A 293 3905 4163 4151 233 190 -820 C ATOM 2081 O GLN A 293 -26.466 -19.646 54.291 1.00 31.81 O ANISOU 2081 O GLN A 293 3524 4121 4441 -32 372 -258 O ATOM 2082 CB GLN A 293 -29.765 -20.888 54.211 1.00 26.91 C ANISOU 2082 CB GLN A 293 2911 3499 3814 84 104 73 C ATOM 2083 CG GLN A 293 -29.282 -21.695 55.423 1.00 33.62 C ANISOU 2083 CG GLN A 293 3935 5176 3662 131 365 675 C ATOM 2084 CD GLN A 293 -29.201 -20.884 56.723 1.00 37.26 C ANISOU 2084 CD GLN A 293 4850 4554 4753 -51 -452 198 C ATOM 2085 OE1 GLN A 293 -29.957 -19.923 56.918 1.00 38.58 O ANISOU 2085 OE1 GLN A 293 4455 5012 5189 -349 275 103 O ATOM 2086 NE2 GLN A 293 -28.290 -21.282 57.631 1.00 29.91 N ANISOU 2086 NE2 GLN A 293 3627 3725 4012 19 179 -547 N ATOM 2087 N HIS A 294 -27.133 -21.214 52.821 1.00 23.79 N ANISOU 2087 N HIS A 294 2681 2935 3423 -729 -67 -129 N ATOM 2088 CA HIS A 294 -25.797 -21.803 52.760 1.00 28.07 C ANISOU 2088 CA HIS A 294 3353 3346 3966 -333 298 35 C ATOM 2089 C HIS A 294 -24.727 -20.836 52.311 1.00 24.06 C ANISOU 2089 C HIS A 294 3041 3164 2935 -100 41 35 C ATOM 2090 O HIS A 294 -23.659 -20.776 52.917 1.00 23.55 O ANISOU 2090 O HIS A 294 2864 3264 2818 -542 318 -30 O ATOM 2091 CB HIS A 294 -25.775 -23.069 51.910 1.00 32.38 C ANISOU 2091 CB HIS A 294 4531 3958 3811 -127 161 -341 C ATOM 2092 CG HIS A 294 -26.625 -24.189 52.464 1.00 36.57 C ANISOU 2092 CG HIS A 294 4722 4473 4699 -299 293 -122 C ATOM 2093 ND1 HIS A 294 -26.557 -24.583 53.749 1.00 42.38 N ANISOU 2093 ND1 HIS A 294 6030 5174 4898 -1372 -358 38 N ATOM 2094 CD2 HIS A 294 -27.562 -25.018 51.850 1.00 35.79 C ANISOU 2094 CD2 HIS A 294 4103 4723 4770 79 409 -61 C ATOM 2095 CE1 HIS A 294 -27.414 -25.594 53.955 1.00 43.08 C ANISOU 2095 CE1 HIS A 294 5917 4955 5495 -964 -505 258 C ATOM 2096 NE2 HIS A 294 -28.028 -25.863 52.791 1.00 42.73 N ANISOU 2096 NE2 HIS A 294 6044 5242 4946 -651 -244 509 N ATOM 2097 N THR A 295 -25.007 -20.074 51.261 1.00 23.90 N ANISOU 2097 N THR A 295 2906 2931 3243 -222 -213 47 N ATOM 2098 CA THR A 295 -24.025 -19.140 50.700 1.00 23.78 C ANISOU 2098 CA THR A 295 2656 3123 3252 46 41 95 C ATOM 2099 C THR A 295 -23.534 -18.153 51.765 1.00 25.72 C ANISOU 2099 C THR A 295 3146 3319 3304 67 140 -211 C ATOM 2100 O THR A 295 -22.321 -17.936 51.916 1.00 25.91 O ANISOU 2100 O THR A 295 3118 3279 3446 156 367 225 O ATOM 2101 CB THR A 295 -24.587 -18.355 49.508 1.00 23.17 C ANISOU 2101 CB THR A 295 2942 2866 2995 -218 32 33 C ATOM 2102 OG1 THR A 295 -25.834 -17.764 49.885 1.00 27.38 O ANISOU 2102 OG1 THR A 295 3434 3203 3766 259 5 -67 O ATOM 2103 CG2 THR A 295 -24.785 -19.252 48.280 1.00 24.81 C ANISOU 2103 CG2 THR A 295 3332 3037 3054 64 38 -129 C ATOM 2104 N SER A 296 -24.463 -17.565 52.518 1.00 24.93 N ANISOU 2104 N SER A 296 2999 3058 3413 -145 216 -272 N ATOM 2105 CA SER A 296 -24.077 -16.588 53.523 1.00 24.61 C ANISOU 2105 CA SER A 296 3104 3448 2797 354 77 -277 C ATOM 2106 C SER A 296 -23.326 -17.207 54.668 1.00 23.46 C ANISOU 2106 C SER A 296 2802 2705 3407 498 92 -180 C ATOM 2107 O SER A 296 -22.389 -16.603 55.172 1.00 25.05 O ANISOU 2107 O SER A 296 3064 2935 3518 21 -55 372 O ATOM 2108 CB SER A 296 -25.294 -15.818 54.045 1.00 24.88 C ANISOU 2108 CB SER A 296 3118 3142 3191 429 -78 -171 C ATOM 2109 OG SER A 296 -25.879 -15.136 52.958 1.00 26.43 O ANISOU 2109 OG SER A 296 2996 3098 3948 375 29 323 O ATOM 2110 N SER A 297 -23.749 -18.398 55.095 1.00 22.76 N ANISOU 2110 N SER A 297 2374 3030 3243 149 374 -149 N ATOM 2111 CA SER A 297 -23.075 -19.121 56.176 1.00 23.27 C ANISOU 2111 CA SER A 297 2805 2705 3328 50 115 -37 C ATOM 2112 C SER A 297 -21.640 -19.512 55.783 1.00 22.99 C ANISOU 2112 C SER A 297 2718 3374 2641 -410 305 -114 C ATOM 2113 O SER A 297 -20.715 -19.466 56.592 1.00 23.22 O ANISOU 2113 O SER A 297 2592 3125 3104 -523 254 46 O ATOM 2114 CB SER A 297 -23.813 -20.429 56.502 1.00 25.26 C ANISOU 2114 CB SER A 297 3326 3395 2876 -429 495 185 C ATOM 2115 OG SER A 297 -25.182 -20.219 56.762 1.00 33.33 O ANISOU 2115 OG SER A 297 3829 4096 4736 72 265 -429 O ATOM 2116 N ILE A 298 -21.498 -19.995 54.559 1.00 19.74 N ANISOU 2116 N ILE A 298 2388 2414 2697 -485 315 -84 N ATOM 2117 CA ILE A 298 -20.227 -20.468 54.044 1.00 20.36 C ANISOU 2117 CA ILE A 298 2548 2420 2768 -104 158 -339 C ATOM 2118 C ILE A 298 -19.265 -19.274 53.928 1.00 22.93 C ANISOU 2118 C ILE A 298 2807 2804 3100 -306 138 194 C ATOM 2119 O ILE A 298 -18.112 -19.374 54.343 1.00 26.31 O ANISOU 2119 O ILE A 298 2967 3471 3558 -302 96 -74 O ATOM 2120 CB ILE A 298 -20.444 -21.192 52.695 1.00 20.73 C ANISOU 2120 CB ILE A 298 2451 2733 2690 -377 81 -322 C ATOM 2121 CG1 ILE A 298 -21.021 -22.596 52.959 1.00 23.97 C ANISOU 2121 CG1 ILE A 298 3285 2534 3286 -287 10 -340 C ATOM 2122 CG2 ILE A 298 -19.160 -21.240 51.865 1.00 22.03 C ANISOU 2122 CG2 ILE A 298 3008 2699 2660 149 439 42 C ATOM 2123 CD1 ILE A 298 -21.791 -23.182 51.780 1.00 24.63 C ANISOU 2123 CD1 ILE A 298 2893 3542 2921 -289 70 -116 C ATOM 2124 N THR A 299 -19.771 -18.141 53.433 1.00 21.72 N ANISOU 2124 N THR A 299 2870 2522 2858 -200 49 -20 N ATOM 2125 CA THR A 299 -18.950 -16.941 53.229 1.00 22.95 C ANISOU 2125 CA THR A 299 2848 2681 3189 -244 53 65 C ATOM 2126 C THR A 299 -18.472 -16.415 54.566 1.00 24.46 C ANISOU 2126 C THR A 299 3107 3030 3157 -106 144 -124 C ATOM 2127 O THR A 299 -17.302 -16.053 54.718 1.00 24.10 O ANISOU 2127 O THR A 299 2760 2980 3416 35 919 -64 O ATOM 2128 CB THR A 299 -19.712 -15.849 52.452 1.00 22.73 C ANISOU 2128 CB THR A 299 2867 2774 2995 -267 1 51 C ATOM 2129 OG1 THR A 299 -20.036 -16.339 51.144 1.00 23.03 O ANISOU 2129 OG1 THR A 299 2917 2767 3064 -307 565 -227 O ATOM 2130 CG2 THR A 299 -18.884 -14.544 52.331 1.00 22.67 C ANISOU 2130 CG2 THR A 299 2573 2910 3129 -151 421 166 C ATOM 2131 N THR A 300 -19.367 -16.388 55.551 1.00 23.59 N ANISOU 2131 N THR A 300 2925 2926 3111 -233 228 183 N ATOM 2132 CA THR A 300 -18.990 -16.040 56.919 1.00 23.27 C ANISOU 2132 CA THR A 300 2921 3016 2903 109 273 -108 C ATOM 2133 C THR A 300 -17.942 -17.008 57.520 1.00 25.80 C ANISOU 2133 C THR A 300 2912 3270 3619 109 -67 -141 C ATOM 2134 O THR A 300 -16.934 -16.582 58.105 1.00 25.83 O ANISOU 2134 O THR A 300 3227 3735 2851 -210 -157 -62 O ATOM 2135 CB THR A 300 -20.237 -16.023 57.828 1.00 23.21 C ANISOU 2135 CB THR A 300 2798 3298 2721 177 127 201 C ATOM 2136 OG1 THR A 300 -21.217 -15.152 57.262 1.00 22.97 O ANISOU 2136 OG1 THR A 300 2310 2980 3434 -185 156 284 O ATOM 2137 CG2 THR A 300 -19.883 -15.533 59.242 1.00 23.71 C ANISOU 2137 CG2 THR A 300 2734 3055 3220 -51 -106 -304 C ATOM 2138 N THR A 301 -18.177 -18.308 57.376 1.00 23.33 N ANISOU 2138 N THR A 301 2539 3012 3313 37 640 26 N ATOM 2139 CA THR A 301 -17.239 -19.307 57.900 1.00 26.57 C ANISOU 2139 CA THR A 301 2920 3281 3891 -80 270 486 C ATOM 2140 C THR A 301 -15.835 -19.172 57.261 1.00 25.71 C ANISOU 2140 C THR A 301 3001 3600 3167 208 177 -104 C ATOM 2141 O THR A 301 -14.842 -19.053 57.971 1.00 27.12 O ANISOU 2141 O THR A 301 3079 3698 3526 -495 359 -187 O ATOM 2142 CB THR A 301 -17.803 -20.734 57.741 1.00 24.77 C ANISOU 2142 CB THR A 301 2660 3200 3548 188 142 262 C ATOM 2143 OG1 THR A 301 -19.126 -20.778 58.314 1.00 23.99 O ANISOU 2143 OG1 THR A 301 2894 3210 3010 -19 274 -293 O ATOM 2144 CG2 THR A 301 -16.899 -21.757 58.442 1.00 24.10 C ANISOU 2144 CG2 THR A 301 3131 2646 3377 -123 -71 363 C ATOM 2145 N TRP A 302 -15.753 -19.175 55.936 1.00 22.05 N ANISOU 2145 N TRP A 302 2786 2529 3063 -212 71 47 N ATOM 2146 CA TRP A 302 -14.453 -19.001 55.282 1.00 27.72 C ANISOU 2146 CA TRP A 302 3239 3904 3389 -307 297 -198 C ATOM 2147 C TRP A 302 -13.773 -17.743 55.757 1.00 28.32 C ANISOU 2147 C TRP A 302 3373 3580 3807 -19 -184 -42 C ATOM 2148 O TRP A 302 -12.601 -17.766 56.096 1.00 27.80 O ANISOU 2148 O TRP A 302 3304 3498 3759 637 -125 -482 O ATOM 2149 CB TRP A 302 -14.592 -18.906 53.780 1.00 26.37 C ANISOU 2149 CB TRP A 302 3338 3469 3212 -145 -93 -289 C ATOM 2150 CG TRP A 302 -14.694 -20.207 53.025 1.00 25.08 C ANISOU 2150 CG TRP A 302 3134 3249 3143 -96 292 -123 C ATOM 2151 CD1 TRP A 302 -15.714 -20.595 52.173 1.00 22.56 C ANISOU 2151 CD1 TRP A 302 2597 2990 2982 -299 664 78 C ATOM 2152 CD2 TRP A 302 -13.706 -21.308 52.964 1.00 26.57 C ANISOU 2152 CD2 TRP A 302 3208 3160 3726 -152 -135 7 C ATOM 2153 NE1 TRP A 302 -15.454 -21.822 51.618 1.00 25.81 N ANISOU 2153 NE1 TRP A 302 2986 3121 3699 62 546 -237 N ATOM 2154 CE2 TRP A 302 -14.265 -22.303 52.049 1.00 28.06 C ANISOU 2154 CE2 TRP A 302 3696 3243 3723 92 -326 -130 C ATOM 2155 CE3 TRP A 302 -12.465 -21.553 53.551 1.00 26.02 C ANISOU 2155 CE3 TRP A 302 3509 3020 3355 430 211 850 C ATOM 2156 CZ2 TRP A 302 -13.597 -23.483 51.744 1.00 27.17 C ANISOU 2156 CZ2 TRP A 302 3452 3209 3661 113 -62 327 C ATOM 2157 CZ3 TRP A 302 -11.810 -22.751 53.243 1.00 26.51 C ANISOU 2157 CZ3 TRP A 302 3080 3335 3657 0 258 -186 C ATOM 2158 CH2 TRP A 302 -12.368 -23.692 52.363 1.00 27.07 C ANISOU 2158 CH2 TRP A 302 2927 3867 3492 -322 321 -161 C ATOM 2159 N SER A 303 -14.503 -16.627 55.771 1.00 28.04 N ANISOU 2159 N SER A 303 3684 3415 3555 33 235 -320 N ATOM 2160 CA SER A 303 -13.922 -15.365 56.210 1.00 26.26 C ANISOU 2160 CA SER A 303 2868 3271 3836 12 366 257 C ATOM 2161 C SER A 303 -13.263 -15.442 57.586 1.00 31.95 C ANISOU 2161 C SER A 303 4213 3976 3950 -688 -45 89 C ATOM 2162 O SER A 303 -12.148 -14.933 57.763 1.00 32.31 O ANISOU 2162 O SER A 303 3197 4472 4604 152 48 16 O ATOM 2163 CB SER A 303 -14.933 -14.225 56.142 1.00 23.06 C ANISOU 2163 CB SER A 303 2931 2791 3038 -122 284 -4 C ATOM 2164 OG SER A 303 -15.345 -14.031 54.793 1.00 25.25 O ANISOU 2164 OG SER A 303 3330 2860 3400 -464 -277 -339 O ATOM 2165 N MET A 304 -13.934 -16.095 58.539 1.00 26.31 N ANISOU 2165 N MET A 304 2939 3364 3692 -91 127 -296 N ATOM 2166 CA MET A 304 -13.418 -16.234 59.890 1.00 27.92 C ANISOU 2166 CA MET A 304 2887 4091 3628 -76 67 237 C ATOM 2167 C MET A 304 -12.219 -17.183 59.940 1.00 27.08 C ANISOU 2167 C MET A 304 3552 3005 3730 -100 74 -81 C ATOM 2168 O MET A 304 -11.219 -16.893 60.617 1.00 28.86 O ANISOU 2168 O MET A 304 3430 3861 3672 106 -268 529 O ATOM 2169 CB MET A 304 -14.520 -16.681 60.864 1.00 28.22 C ANISOU 2169 CB MET A 304 2866 3880 3977 -97 294 -164 C ATOM 2170 CG MET A 304 -15.659 -15.670 61.021 1.00 29.24 C ANISOU 2170 CG MET A 304 3524 3559 4024 92 197 -338 C ATOM 2171 SD MET A 304 -16.902 -16.173 62.249 1.00 30.51 S ANISOU 2171 SD MET A 304 3359 4327 3904 5 158 -96 S ATOM 2172 CE MET A 304 -15.969 -15.953 63.749 1.00 32.04 C ANISOU 2172 CE MET A 304 4220 4783 3169 635 291 -643 C ATOM 2173 N LEU A 305 -12.316 -18.295 59.220 1.00 24.35 N ANISOU 2173 N LEU A 305 2829 3415 3006 -228 133 -158 N ATOM 2174 CA LEU A 305 -11.217 -19.276 59.126 1.00 27.91 C ANISOU 2174 CA LEU A 305 3598 3399 3604 -5 -55 -276 C ATOM 2175 C LEU A 305 -9.937 -18.575 58.664 1.00 31.35 C ANISOU 2175 C LEU A 305 3880 4058 3974 -130 171 -238 C ATOM 2176 O LEU A 305 -8.895 -18.717 59.291 1.00 38.64 O ANISOU 2176 O LEU A 305 4331 5317 5031 82 -34 -134 O ATOM 2177 CB LEU A 305 -11.576 -20.453 58.184 1.00 27.29 C ANISOU 2177 CB LEU A 305 3317 3327 3726 -397 325 -229 C ATOM 2178 CG LEU A 305 -12.689 -21.405 58.680 1.00 23.86 C ANISOU 2178 CG LEU A 305 3141 2990 2932 -255 -25 -240 C ATOM 2179 CD1 LEU A 305 -13.172 -22.366 57.594 1.00 22.65 C ANISOU 2179 CD1 LEU A 305 2211 3146 3247 -581 126 -292 C ATOM 2180 CD2 LEU A 305 -12.252 -22.172 59.921 1.00 24.66 C ANISOU 2180 CD2 LEU A 305 2719 3359 3290 311 200 63 C ATOM 2181 N HIS A 306 -10.042 -17.803 57.581 1.00 29.93 N ANISOU 2181 N HIS A 306 3610 3623 4137 -49 534 -58 N ATOM 2182 CA HIS A 306 -8.932 -17.005 57.074 1.00 29.80 C ANISOU 2182 CA HIS A 306 3776 3354 4191 33 270 242 C ATOM 2183 C HIS A 306 -8.420 -16.008 58.079 1.00 33.90 C ANISOU 2183 C HIS A 306 4105 4596 4179 561 -224 -502 C ATOM 2184 O HIS A 306 -7.221 -15.983 58.375 1.00 32.20 O ANISOU 2184 O HIS A 306 3556 4006 4669 -341 -40 -308 O ATOM 2185 CB HIS A 306 -9.317 -16.279 55.785 1.00 26.82 C ANISOU 2185 CB HIS A 306 2942 3522 3724 -450 -452 -234 C ATOM 2186 CG HIS A 306 -9.571 -17.192 54.612 1.00 25.71 C ANISOU 2186 CG HIS A 306 3167 3285 3314 -178 137 -119 C ATOM 2187 ND1 HIS A 306 -8.639 -18.045 54.134 1.00 26.09 N ANISOU 2187 ND1 HIS A 306 3001 3823 3088 130 63 133 N ATOM 2188 CD2 HIS A 306 -10.707 -17.362 53.819 1.00 26.51 C ANISOU 2188 CD2 HIS A 306 3344 3761 2967 365 -62 161 C ATOM 2189 CE1 HIS A 306 -9.152 -18.733 53.098 1.00 26.70 C ANISOU 2189 CE1 HIS A 306 3295 3332 3515 -380 398 21 C ATOM 2190 NE2 HIS A 306 -10.422 -18.309 52.903 1.00 29.36 N ANISOU 2190 NE2 HIS A 306 3784 3332 4040 44 355 -41 N ATOM 2191 N LEU A 307 -9.316 -15.174 58.607 1.00 28.69 N ANISOU 2191 N LEU A 307 3158 3941 3801 -163 -49 -177 N ATOM 2192 CA LEU A 307 -8.920 -14.131 59.543 1.00 29.90 C ANISOU 2192 CA LEU A 307 3704 3944 3710 -40 116 -354 C ATOM 2193 C LEU A 307 -8.233 -14.652 60.812 1.00 33.25 C ANISOU 2193 C LEU A 307 3859 4230 4544 84 -415 30 C ATOM 2194 O LEU A 307 -7.393 -13.958 61.398 1.00 30.35 O ANISOU 2194 O LEU A 307 3791 3770 3968 444 -44 -642 O ATOM 2195 CB LEU A 307 -10.116 -13.240 59.905 1.00 27.99 C ANISOU 2195 CB LEU A 307 3059 3237 4338 -478 -454 -84 C ATOM 2196 CG LEU A 307 -10.486 -12.251 58.801 1.00 30.50 C ANISOU 2196 CG LEU A 307 3600 3437 4548 149 243 188 C ATOM 2197 CD1 LEU A 307 -11.920 -11.802 58.963 1.00 25.74 C ANISOU 2197 CD1 LEU A 307 2917 3225 3638 -1001 126 325 C ATOM 2198 CD2 LEU A 307 -9.523 -11.051 58.765 1.00 30.02 C ANISOU 2198 CD2 LEU A 307 3192 3707 4504 151 783 -813 C ATOM 2199 N MET A 308 -8.567 -15.867 61.235 1.00 33.32 N ANISOU 2199 N MET A 308 3713 4232 4713 515 269 80 N ATOM 2200 CA MET A 308 -7.986 -16.405 62.472 1.00 36.25 C ANISOU 2200 CA MET A 308 4680 4619 4473 196 266 440 C ATOM 2201 C MET A 308 -6.653 -17.140 62.285 1.00 35.10 C ANISOU 2201 C MET A 308 3587 5437 4310 -512 -36 -204 C ATOM 2202 O MET A 308 -5.975 -17.450 63.263 1.00 37.22 O ANISOU 2202 O MET A 308 3744 5400 4997 -557 -266 181 O ATOM 2203 CB MET A 308 -8.978 -17.326 63.188 1.00 33.99 C ANISOU 2203 CB MET A 308 3485 4409 5017 4 42 -219 C ATOM 2204 CG MET A 308 -9.080 -18.730 62.602 1.00 33.17 C ANISOU 2204 CG MET A 308 3905 4581 4118 247 541 -383 C ATOM 2205 SD MET A 308 -10.267 -19.780 63.480 1.00 33.18 S ANISOU 2205 SD MET A 308 3847 4172 4586 -108 -341 2 S ATOM 2206 CE MET A 308 -11.817 -18.937 63.107 1.00 28.46 C ANISOU 2206 CE MET A 308 3389 3480 3943 -271 -276 -145 C ATOM 2207 N HIS A 309 -6.312 -17.449 61.038 1.00 32.36 N ANISOU 2207 N HIS A 309 3218 4585 4491 -528 133 -74 N ATOM 2208 CA HIS A 309 -5.078 -18.163 60.702 1.00 34.65 C ANISOU 2208 CA HIS A 309 4241 4299 4624 38 -90 -551 C ATOM 2209 C HIS A 309 -3.895 -17.248 60.889 1.00 32.23 C ANISOU 2209 C HIS A 309 3991 4331 3924 11 109 -134 C ATOM 2210 O HIS A 309 -3.965 -16.089 60.486 1.00 34.62 O ANISOU 2210 O HIS A 309 3847 4513 4792 -472 177 233 O ATOM 2211 CB HIS A 309 -5.152 -18.632 59.253 1.00 37.89 C ANISOU 2211 CB HIS A 309 4842 4626 4928 263 81 -1021 C ATOM 2212 CG HIS A 309 -4.051 -19.591 58.864 1.00 37.01 C ANISOU 2212 CG HIS A 309 4880 4626 4555 176 408 -606 C ATOM 2213 ND1 HIS A 309 -2.790 -19.180 58.592 1.00 37.75 N ANISOU 2213 ND1 HIS A 309 4632 5057 4652 336 1 -222 N ATOM 2214 CD2 HIS A 309 -4.060 -20.979 58.707 1.00 29.41 C ANISOU 2214 CD2 HIS A 309 3492 4086 3597 -792 -215 59 C ATOM 2215 CE1 HIS A 309 -2.032 -20.252 58.272 1.00 37.25 C ANISOU 2215 CE1 HIS A 309 3605 5207 5340 127 97 -80 C ATOM 2216 NE2 HIS A 309 -2.811 -21.352 58.343 1.00 38.35 N ANISOU 2216 NE2 HIS A 309 4766 4304 5501 540 484 -814 N ATOM 2217 N PRO A 310 -2.793 -17.743 61.501 1.00 34.90 N ANISOU 2217 N PRO A 310 3906 4430 4923 95 42 221 N ATOM 2218 CA PRO A 310 -1.699 -16.816 61.838 1.00 34.17 C ANISOU 2218 CA PRO A 310 4202 3977 4801 216 -123 154 C ATOM 2219 C PRO A 310 -1.072 -16.112 60.619 1.00 30.51 C ANISOU 2219 C PRO A 310 3099 4178 4315 620 -22 -252 C ATOM 2220 O PRO A 310 -0.591 -14.987 60.747 1.00 35.56 O ANISOU 2220 O PRO A 310 3449 4817 5245 -24 -11 -539 O ATOM 2221 CB PRO A 310 -0.670 -17.703 62.568 1.00 36.56 C ANISOU 2221 CB PRO A 310 4328 4456 5104 39 -821 263 C ATOM 2222 CG PRO A 310 -1.387 -18.967 62.912 1.00 37.90 C ANISOU 2222 CG PRO A 310 4771 5280 4348 -291 -85 789 C ATOM 2223 CD PRO A 310 -2.472 -19.132 61.877 1.00 35.50 C ANISOU 2223 CD PRO A 310 4147 4096 5243 -246 -107 106 C ATOM 2224 N ALA A 311 -1.111 -16.741 59.446 1.00 32.13 N ANISOU 2224 N ALA A 311 3397 4661 4149 380 253 -289 N ATOM 2225 CA ALA A 311 -0.573 -16.121 58.227 1.00 32.42 C ANISOU 2225 CA ALA A 311 3587 4267 4465 -234 -213 -52 C ATOM 2226 C ALA A 311 -1.262 -14.801 57.870 1.00 37.57 C ANISOU 2226 C ALA A 311 4539 4786 4949 107 398 762 C ATOM 2227 O ALA A 311 -0.711 -13.987 57.135 1.00 30.57 O ANISOU 2227 O ALA A 311 2878 4092 4646 -194 -83 55 O ATOM 2228 CB ALA A 311 -0.637 -17.092 57.050 1.00 30.26 C ANISOU 2228 CB ALA A 311 2658 4882 3957 110 73 -78 C ATOM 2229 N ASN A 312 -2.465 -14.593 58.398 1.00 37.85 N ANISOU 2229 N ASN A 312 4368 4827 5186 368 -27 -425 N ATOM 2230 CA ASN A 312 -3.278 -13.443 58.033 1.00 31.38 C ANISOU 2230 CA ASN A 312 3262 4436 4223 -284 -352 -277 C ATOM 2231 C ASN A 312 -3.426 -12.444 59.185 1.00 32.00 C ANISOU 2231 C ASN A 312 3676 4096 4383 -319 -121 -193 C ATOM 2232 O ASN A 312 -4.356 -11.635 59.200 1.00 35.36 O ANISOU 2232 O ASN A 312 4042 4853 4539 129 -816 -85 O ATOM 2233 CB ASN A 312 -4.655 -13.935 57.569 1.00 28.88 C ANISOU 2233 CB ASN A 312 3182 3698 4094 -303 -194 -16 C ATOM 2234 CG ASN A 312 -4.567 -14.841 56.361 1.00 32.93 C ANISOU 2234 CG ASN A 312 4284 3759 4465 -61 160 -77 C ATOM 2235 OD1 ASN A 312 -3.885 -14.519 55.378 1.00 35.78 O ANISOU 2235 OD1 ASN A 312 4118 4699 4775 -262 -31 483 O ATOM 2236 ND2 ASN A 312 -5.250 -15.986 56.421 1.00 28.62 N ANISOU 2236 ND2 ASN A 312 3110 4031 3729 -66 88 -67 N ATOM 2237 N VAL A 313 -2.501 -12.497 60.143 1.00 34.02 N ANISOU 2237 N VAL A 313 3866 5107 3950 330 132 -27 N ATOM 2238 CA VAL A 313 -2.533 -11.611 61.316 1.00 35.71 C ANISOU 2238 CA VAL A 313 4246 4645 4676 -278 -403 -225 C ATOM 2239 C VAL A 313 -2.619 -10.132 60.931 1.00 38.25 C ANISOU 2239 C VAL A 313 4715 4873 4944 285 116 -263 C ATOM 2240 O VAL A 313 -3.250 -9.346 61.641 1.00 39.33 O ANISOU 2240 O VAL A 313 4971 6281 3688 -240 116 -1034 O ATOM 2241 CB VAL A 313 -1.324 -11.861 62.252 1.00 38.03 C ANISOU 2241 CB VAL A 313 4444 5713 4293 -535 -346 -251 C ATOM 2242 CG1 VAL A 313 -0.012 -11.445 61.578 1.00 34.47 C ANISOU 2242 CG1 VAL A 313 3786 4511 4800 -37 -307 -860 C ATOM 2243 CG2 VAL A 313 -1.518 -11.157 63.589 1.00 33.14 C ANISOU 2243 CG2 VAL A 313 3288 4815 4486 169 -44 63 C ATOM 2244 N LYS A 314 -2.003 -9.757 59.806 1.00 36.55 N ANISOU 2244 N LYS A 314 3935 5032 4920 429 13 -322 N ATOM 2245 CA LYS A 314 -2.099 -8.381 59.299 1.00 38.35 C ANISOU 2245 CA LYS A 314 4296 5032 5243 -153 -203 -61 C ATOM 2246 C LYS A 314 -3.544 -8.024 58.954 1.00 38.60 C ANISOU 2246 C LYS A 314 4441 4752 5473 -7 -458 -760 C ATOM 2247 O LYS A 314 -3.980 -6.882 59.135 1.00 32.35 O ANISOU 2247 O LYS A 314 3052 4437 4799 -598 -265 -775 O ATOM 2248 CB LYS A 314 -1.232 -8.176 58.047 1.00 39.05 C ANISOU 2248 CB LYS A 314 4561 4880 5396 160 319 -947 C ATOM 2249 CG LYS A 314 0.266 -8.351 58.255 1.00 43.83 C ANISOU 2249 CG LYS A 314 4690 5300 6664 -619 -627 -501 C ATOM 2250 CD LYS A 314 0.816 -7.465 59.368 1.00 49.05 C ANISOU 2250 CD LYS A 314 6672 6147 5815 -432 -747 -1168 C ATOM 2251 CE LYS A 314 1.508 -6.213 58.845 1.00 52.87 C ANISOU 2251 CE LYS A 314 7203 6755 6129 -261 -740 -205 C ATOM 2252 NZ LYS A 314 2.405 -5.587 59.869 1.00 43.22 N ANISOU 2252 NZ LYS A 314 4767 6458 5196 1109 335 -534 N ATOM 2253 N HIS A 315 -4.280 -8.999 58.431 1.00 35.27 N ANISOU 2253 N HIS A 315 3710 4917 4772 -412 286 -261 N ATOM 2254 CA HIS A 315 -5.648 -8.738 57.984 1.00 34.59 C ANISOU 2254 CA HIS A 315 4102 4506 4533 -521 -214 -812 C ATOM 2255 C HIS A 315 -6.594 -8.639 59.151 1.00 30.28 C ANISOU 2255 C HIS A 315 3440 4064 4001 -519 -674 -570 C ATOM 2256 O HIS A 315 -7.495 -7.798 59.169 1.00 36.72 O ANISOU 2256 O HIS A 315 4554 4004 5393 -165 -581 -1411 O ATOM 2257 CB HIS A 315 -6.079 -9.804 56.992 1.00 28.94 C ANISOU 2257 CB HIS A 315 3107 4345 3543 -185 -308 -165 C ATOM 2258 CG HIS A 315 -5.211 -9.865 55.773 1.00 26.68 C ANISOU 2258 CG HIS A 315 3186 3787 3160 -178 -695 -301 C ATOM 2259 ND1 HIS A 315 -4.920 -8.774 55.049 1.00 33.34 N ANISOU 2259 ND1 HIS A 315 3923 4261 4482 -391 87 -147 N ATOM 2260 CD2 HIS A 315 -4.568 -10.935 55.154 1.00 31.63 C ANISOU 2260 CD2 HIS A 315 3412 4483 4123 483 5 -61 C ATOM 2261 CE1 HIS A 315 -4.135 -9.124 54.007 1.00 32.73 C ANISOU 2261 CE1 HIS A 315 3509 4281 4644 -680 156 -85 C ATOM 2262 NE2 HIS A 315 -3.919 -10.445 54.074 1.00 34.44 N ANISOU 2262 NE2 HIS A 315 3994 4235 4857 22 501 -83 N ATOM 2263 N LEU A 316 -6.373 -9.490 60.143 1.00 31.85 N ANISOU 2263 N LEU A 316 3777 4173 4149 -780 -78 -239 N ATOM 2264 CA LEU A 316 -7.106 -9.434 61.403 1.00 34.58 C ANISOU 2264 CA LEU A 316 4053 4489 4594 -103 490 11 C ATOM 2265 C LEU A 316 -6.900 -8.084 62.089 1.00 40.17 C ANISOU 2265 C LEU A 316 4969 5239 5053 -629 369 -686 C ATOM 2266 O LEU A 316 -7.872 -7.468 62.537 1.00 40.15 O ANISOU 2266 O LEU A 316 3787 5354 6113 -931 11 -420 O ATOM 2267 CB LEU A 316 -6.713 -10.594 62.325 1.00 32.95 C ANISOU 2267 CB LEU A 316 3720 4579 4218 159 -6 -175 C ATOM 2268 CG LEU A 316 -7.436 -10.626 63.684 1.00 35.96 C ANISOU 2268 CG LEU A 316 4080 4995 4584 -98 344 279 C ATOM 2269 CD1 LEU A 316 -8.937 -10.747 63.487 1.00 34.02 C ANISOU 2269 CD1 LEU A 316 4283 3952 4690 -707 275 -691 C ATOM 2270 CD2 LEU A 316 -6.935 -11.743 64.591 1.00 33.79 C ANISOU 2270 CD2 LEU A 316 3797 4610 4429 -358 -525 -329 C ATOM 2271 N GLU A 317 -5.650 -7.614 62.152 1.00 38.48 N ANISOU 2271 N GLU A 317 4341 5030 5249 -256 240 -619 N ATOM 2272 CA GLU A 317 -5.376 -6.264 62.645 1.00 32.28 C ANISOU 2272 CA GLU A 317 3889 4485 3890 -502 318 -25 C ATOM 2273 C GLU A 317 -6.140 -5.198 61.868 1.00 30.03 C ANISOU 2273 C GLU A 317 2482 4667 4261 -980 -281 -228 C ATOM 2274 O GLU A 317 -6.674 -4.258 62.467 1.00 41.39 O ANISOU 2274 O GLU A 317 4001 5774 5951 -1058 269 -1622 O ATOM 2275 CB GLU A 317 -3.875 -5.925 62.602 1.00 43.64 C ANISOU 2275 CB GLU A 317 3981 5615 6985 -594 624 -170 C ATOM 2276 CG GLU A 317 -3.580 -4.435 62.813 1.00 43.73 C ANISOU 2276 CG GLU A 317 5383 5883 5347 -142 1228 -1456 C ATOM 2277 CD GLU A 317 -2.121 -4.056 62.582 1.00 55.47 C ANISOU 2277 CD GLU A 317 6066 7678 7330 -1559 777 -724 C ATOM 2278 OE1 GLU A 317 -1.579 -4.329 61.480 1.00 47.74 O ANISOU 2278 OE1 GLU A 317 4010 7282 6845 -643 340 647 O ATOM 2279 OE2 GLU A 317 -1.517 -3.459 63.503 1.00 61.39 O ANISOU 2279 OE2 GLU A 317 7702 7633 7988 162 -287 -1454 O ATOM 2280 N ALA A 318 -6.184 -5.314 60.541 1.00 27.96 N ANISOU 2280 N ALA A 318 2508 4031 4085 -787 522 -216 N ATOM 2281 CA ALA A 318 -6.886 -4.304 59.727 1.00 33.38 C ANISOU 2281 CA ALA A 318 3810 4638 4234 -409 247 344 C ATOM 2282 C ALA A 318 -8.401 -4.329 59.977 1.00 41.53 C ANISOU 2282 C ALA A 318 4227 5060 6490 -5 1010 578 C ATOM 2283 O ALA A 318 -9.092 -3.294 59.913 1.00 37.27 O ANISOU 2283 O ALA A 318 3702 4414 6042 -475 158 -767 O ATOM 2284 CB ALA A 318 -6.591 -4.492 58.243 1.00 32.45 C ANISOU 2284 CB ALA A 318 3186 4576 4567 -132 268 -965 C ATOM 2285 N LEU A 319 -8.918 -5.521 60.245 1.00 37.45 N ANISOU 2285 N LEU A 319 4154 4856 5218 -445 1079 -499 N ATOM 2286 CA LEU A 319 -10.329 -5.652 60.582 1.00 36.29 C ANISOU 2286 CA LEU A 319 4280 4603 4904 -570 966 -471 C ATOM 2287 C LEU A 319 -10.588 -5.011 61.938 1.00 33.38 C ANISOU 2287 C LEU A 319 4015 4310 4358 -563 -7 -263 C ATOM 2288 O LEU A 319 -11.478 -4.177 62.064 1.00 39.98 O ANISOU 2288 O LEU A 319 5056 4215 5919 -453 -452 -1196 O ATOM 2289 CB LEU A 319 -10.756 -7.119 60.612 1.00 31.56 C ANISOU 2289 CB LEU A 319 3435 4533 4022 -451 -94 -85 C ATOM 2290 CG LEU A 319 -12.209 -7.328 61.054 1.00 32.96 C ANISOU 2290 CG LEU A 319 3728 4084 4711 -617 12 765 C ATOM 2291 CD1 LEU A 319 -13.163 -6.706 60.046 1.00 29.40 C ANISOU 2291 CD1 LEU A 319 2395 4349 4424 -813 300 386 C ATOM 2292 CD2 LEU A 319 -12.484 -8.813 61.230 1.00 28.04 C ANISOU 2292 CD2 LEU A 319 3583 3741 3329 -89 557 314 C ATOM 2293 N ARG A 320 -9.802 -5.414 62.939 1.00 31.23 N ANISOU 2293 N ARG A 320 3634 4185 4048 -467 417 24 N ATOM 2294 CA ARG A 320 -9.948 -4.929 64.315 1.00 36.47 C ANISOU 2294 CA ARG A 320 4655 4753 4449 -129 -464 -681 C ATOM 2295 C ARG A 320 -9.805 -3.424 64.381 1.00 39.08 C ANISOU 2295 C ARG A 320 5165 4910 4773 -48 -463 185 C ATOM 2296 O ARG A 320 -10.504 -2.764 65.152 1.00 46.35 O ANISOU 2296 O ARG A 320 5617 5991 6000 -343 -412 -1156 O ATOM 2297 CB ARG A 320 -8.909 -5.571 65.230 1.00 36.25 C ANISOU 2297 CB ARG A 320 4243 4772 4757 -86 378 461 C ATOM 2298 CG ARG A 320 -9.188 -7.019 65.569 1.00 41.96 C ANISOU 2298 CG ARG A 320 5421 5052 5469 -1491 735 -307 C ATOM 2299 CD ARG A 320 -9.812 -7.096 66.938 1.00 44.81 C ANISOU 2299 CD ARG A 320 5454 6308 5264 -478 420 273 C ATOM 2300 NE ARG A 320 -10.351 -8.416 67.260 1.00 42.55 N ANISOU 2300 NE ARG A 320 5125 5259 5783 201 -86 -835 N ATOM 2301 CZ ARG A 320 -9.614 -9.489 67.513 1.00 43.62 C ANISOU 2301 CZ ARG A 320 6045 4625 5903 -132 -221 -538 C ATOM 2302 NH1 ARG A 320 -8.288 -9.430 67.439 1.00 54.97 N ANISOU 2302 NH1 ARG A 320 6035 7313 7538 -377 -894 -1055 N ATOM 2303 NH2 ARG A 320 -10.206 -10.628 67.822 1.00 41.60 N ANISOU 2303 NH2 ARG A 320 5376 5588 4841 -771 -370 64 N ATOM 2304 N LYS A 321 -8.894 -2.885 63.572 1.00 39.68 N ANISOU 2304 N LYS A 321 4516 5332 5227 228 36 -430 N ATOM 2305 CA LYS A 321 -8.751 -1.438 63.443 1.00 42.86 C ANISOU 2305 CA LYS A 321 5212 5185 5884 -397 -515 -851 C ATOM 2306 C LYS A 321 -9.980 -0.814 62.797 1.00 44.79 C ANISOU 2306 C LYS A 321 5450 5634 5931 272 -586 -1191 C ATOM 2307 O LYS A 321 -10.447 0.231 63.238 1.00 43.81 O ANISOU 2307 O LYS A 321 4068 5473 7102 -859 -520 -1962 O ATOM 2308 CB LYS A 321 -7.515 -1.072 62.626 1.00 53.02 C ANISOU 2308 CB LYS A 321 7087 6473 6585 -113 1541 -1467 C ATOM 2309 CG LYS A 321 -7.470 0.403 62.260 1.00 62.83 C ANISOU 2309 CG LYS A 321 7342 7593 8937 1501 -234 578 C ATOM 2310 CD LYS A 321 -6.267 0.756 61.401 1.00 69.83 C ANISOU 2310 CD LYS A 321 8377 8704 9449 1015 968 -627 C ATOM 2311 CE LYS A 321 -6.026 2.260 61.441 1.00 72.21 C ANISOU 2311 CE LYS A 321 9520 8380 9536 2182 -1825 -1413 C ATOM 2312 NZ LYS A 321 -6.070 2.761 62.848 1.00 68.23 N ANISOU 2312 NZ LYS A 321 9602 7530 8791 -784 -1212 -281 N ATOM 2313 N GLU A 322 -10.490 -1.446 61.743 1.00 40.20 N ANISOU 2313 N GLU A 322 4040 5720 5512 -698 409 -822 N ATOM 2314 CA GLU A 322 -11.656 -0.919 61.042 1.00 40.81 C ANISOU 2314 CA GLU A 322 5431 5315 4760 215 262 -844 C ATOM 2315 C GLU A 322 -12.863 -0.784 61.964 1.00 31.82 C ANISOU 2315 C GLU A 322 3606 3908 4576 -785 -920 -849 C ATOM 2316 O GLU A 322 -13.668 0.112 61.785 1.00 39.12 O ANISOU 2316 O GLU A 322 3903 5013 5948 -35 -935 -1846 O ATOM 2317 CB GLU A 322 -12.031 -1.812 59.867 1.00 43.52 C ANISOU 2317 CB GLU A 322 5391 6717 4426 73 -325 -735 C ATOM 2318 CG GLU A 322 -13.213 -1.297 59.064 1.00 43.98 C ANISOU 2318 CG GLU A 322 5199 5768 5740 676 -183 -767 C ATOM 2319 CD GLU A 322 -13.423 -2.083 57.788 1.00 42.64 C ANISOU 2319 CD GLU A 322 5589 5628 4983 2 32 110 C ATOM 2320 OE1 GLU A 322 -13.943 -3.224 57.847 1.00 41.54 O ANISOU 2320 OE1 GLU A 322 4521 5426 5836 482 250 -671 O ATOM 2321 OE2 GLU A 322 -13.075 -1.553 56.721 1.00 38.31 O ANISOU 2321 OE2 GLU A 322 4522 4756 5275 -245 553 -545 O ATOM 2322 N ILE A 323 -12.976 -1.668 62.950 1.00 37.43 N ANISOU 2322 N ILE A 323 4311 5250 4659 -1427 -160 -405 N ATOM 2323 CA ILE A 323 -14.167 -1.702 63.801 1.00 41.00 C ANISOU 2323 CA ILE A 323 4842 5642 5091 -1273 238 -979 C ATOM 2324 C ILE A 323 -13.948 -1.052 65.162 1.00 46.20 C ANISOU 2324 C ILE A 323 5361 6563 5628 -531 744 -2255 C ATOM 2325 O ILE A 323 -14.906 -0.837 65.899 1.00 41.33 O ANISOU 2325 O ILE A 323 3995 5766 5941 -763 461 -1020 O ATOM 2326 CB ILE A 323 -14.689 -3.145 63.987 1.00 34.09 C ANISOU 2326 CB ILE A 323 3988 4810 4153 47 511 -333 C ATOM 2327 CG1 ILE A 323 -13.752 -3.944 64.900 1.00 37.16 C ANISOU 2327 CG1 ILE A 323 4264 4783 5072 282 109 -422 C ATOM 2328 CG2 ILE A 323 -14.904 -3.806 62.622 1.00 34.00 C ANISOU 2328 CG2 ILE A 323 3619 4215 5081 -1315 424 -919 C ATOM 2329 CD1 ILE A 323 -14.216 -5.354 65.197 1.00 40.89 C ANISOU 2329 CD1 ILE A 323 4940 5390 5204 -420 -55 -99 C ATOM 2330 N GLU A 324 -12.685 -0.742 65.467 1.00 50.89 N ANISOU 2330 N GLU A 324 5206 6904 7223 -1235 1101 -1504 N ATOM 2331 CA GLU A 324 -12.236 -0.205 66.766 1.00 48.15 C ANISOU 2331 CA GLU A 324 5690 6985 5618 41 1092 -530 C ATOM 2332 C GLU A 324 -13.116 0.875 67.400 1.00 35.48 C ANISOU 2332 C GLU A 324 3759 5030 4689 -1208 -269 -259 C ATOM 2333 O GLU A 324 -13.343 0.850 68.601 1.00 43.19 O ANISOU 2333 O GLU A 324 3672 7235 5502 -634 1321 -920 O ATOM 2334 CB GLU A 324 -10.799 0.326 66.643 1.00 54.42 C ANISOU 2334 CB GLU A 324 5727 7599 7348 -277 -59 -2064 C ATOM 2335 CG GLU A 324 -10.120 0.630 67.970 1.00 66.47 C ANISOU 2335 CG GLU A 324 8501 9396 7358 65 -1257 -2001 C ATOM 2336 CD GLU A 324 -8.823 1.408 67.808 1.00 78.78 C ANISOU 2336 CD GLU A 324 9550 10522 9858 -309 1181 -1049 C ATOM 2337 OE1 GLU A 324 -8.322 1.537 66.664 1.00 69.88 O ANISOU 2337 OE1 GLU A 324 9313 8563 8673 -104 178 -1886 O ATOM 2338 OE2 GLU A 324 -8.302 1.895 68.835 1.00 86.74 O ANISOU 2338 OE2 GLU A 324 7704 13116 12137 1144 -2832 355 O ATOM 2339 N GLU A 325 -13.579 1.833 66.604 1.00 41.87 N ANISOU 2339 N GLU A 325 4410 4947 6550 -530 -401 -288 N ATOM 2340 CA GLU A 325 -14.348 2.953 67.139 1.00 48.44 C ANISOU 2340 CA GLU A 325 5515 5996 6893 -622 521 -1108 C ATOM 2341 C GLU A 325 -15.857 2.738 66.990 1.00 55.67 C ANISOU 2341 C GLU A 325 5713 5799 9640 -1013 -100 -501 C ATOM 2342 O GLU A 325 -16.631 3.696 67.066 1.00 53.54 O ANISOU 2342 O GLU A 325 6165 6454 7723 -492 402 -2269 O ATOM 2343 CB GLU A 325 -13.901 4.281 66.499 1.00 51.45 C ANISOU 2343 CB GLU A 325 6320 6225 7003 -373 1243 -929 C ATOM 2344 CG GLU A 325 -12.384 4.480 66.529 1.00 57.80 C ANISOU 2344 CG GLU A 325 6481 6730 8747 -110 1793 -2055 C ATOM 2345 CD GLU A 325 -11.948 5.935 66.470 1.00 55.49 C ANISOU 2345 CD GLU A 325 6379 7548 7156 -744 380 592 C ATOM 2346 OE1 GLU A 325 -10.966 6.277 67.158 1.00 60.46 O ANISOU 2346 OE1 GLU A 325 6152 10498 6323 905 -291 1241 O ATOM 2347 OE2 GLU A 325 -12.571 6.740 65.744 1.00 54.77 O ANISOU 2347 OE2 GLU A 325 6129 7796 6884 931 1552 -62 O ATOM 2348 N PHE A 326 -16.270 1.483 66.790 1.00 45.14 N ANISOU 2348 N PHE A 326 5203 5833 6113 -298 -272 -1698 N ATOM 2349 CA PHE A 326 -17.701 1.176 66.631 1.00 46.52 C ANISOU 2349 CA PHE A 326 6018 5718 5937 -2101 859 -1203 C ATOM 2350 C PHE A 326 -18.427 1.145 67.980 1.00 38.13 C ANISOU 2350 C PHE A 326 4969 4564 4952 -752 -153 -1145 C ATOM 2351 O PHE A 326 -17.893 0.638 68.967 1.00 38.29 O ANISOU 2351 O PHE A 326 3924 5098 5526 -454 -692 -1107 O ATOM 2352 CB PHE A 326 -17.927 -0.158 65.880 1.00 41.05 C ANISOU 2352 CB PHE A 326 5113 5555 4928 -1924 -409 -490 C ATOM 2353 CG PHE A 326 -17.730 -0.077 64.379 1.00 40.27 C ANISOU 2353 CG PHE A 326 4671 5286 5340 -85 905 -940 C ATOM 2354 CD1 PHE A 326 -17.577 1.155 63.736 1.00 44.61 C ANISOU 2354 CD1 PHE A 326 6181 5498 5270 -885 380 -1017 C ATOM 2355 CD2 PHE A 326 -17.736 -1.240 63.601 1.00 33.11 C ANISOU 2355 CD2 PHE A 326 2928 5261 4391 -83 -391 -592 C ATOM 2356 CE1 PHE A 326 -17.395 1.230 62.367 1.00 42.43 C ANISOU 2356 CE1 PHE A 326 5270 5829 5022 -908 -462 -225 C ATOM 2357 CE2 PHE A 326 -17.560 -1.170 62.224 1.00 31.22 C ANISOU 2357 CE2 PHE A 326 3179 4195 4485 312 -99 -753 C ATOM 2358 CZ PHE A 326 -17.389 0.063 61.608 1.00 44.32 C ANISOU 2358 CZ PHE A 326 6017 4939 5881 37 119 225 C ATOM 2359 N PRO A 327 -19.664 1.667 68.031 1.00 44.79 N ANISOU 2359 N PRO A 327 6368 5252 5398 651 -410 -580 N ATOM 2360 CA PRO A 327 -20.425 1.542 69.282 1.00 44.86 C ANISOU 2360 CA PRO A 327 4896 5597 6551 -297 178 -918 C ATOM 2361 C PRO A 327 -20.767 0.081 69.591 1.00 45.05 C ANISOU 2361 C PRO A 327 5443 6234 5439 -301 59 7 C ATOM 2362 O PRO A 327 -20.712 -0.773 68.700 1.00 53.28 O ANISOU 2362 O PRO A 327 6311 6669 7265 137 -324 -1054 O ATOM 2363 CB PRO A 327 -21.692 2.342 69.001 1.00 44.50 C ANISOU 2363 CB PRO A 327 5481 5743 5681 150 318 -505 C ATOM 2364 CG PRO A 327 -21.826 2.335 67.518 1.00 46.35 C ANISOU 2364 CG PRO A 327 6462 5719 5430 -588 832 -72 C ATOM 2365 CD PRO A 327 -20.426 2.364 66.983 1.00 42.11 C ANISOU 2365 CD PRO A 327 5303 4774 5923 135 -574 -849 C ATOM 2366 N ALA A 328 -21.104 -0.207 70.842 1.00 39.09 N ANISOU 2366 N ALA A 328 4485 5280 5087 -56 -143 -855 N ATOM 2367 CA ALA A 328 -21.536 -1.544 71.226 1.00 47.19 C ANISOU 2367 CA ALA A 328 5975 5837 6116 -218 -333 113 C ATOM 2368 C ALA A 328 -22.702 -1.984 70.342 1.00 47.32 C ANISOU 2368 C ALA A 328 6440 5327 6213 -226 -276 -773 C ATOM 2369 O ALA A 328 -22.877 -3.168 70.072 1.00 44.59 O ANISOU 2369 O ALA A 328 4701 6316 5924 -1231 -381 -1769 O ATOM 2370 CB ALA A 328 -21.944 -1.565 72.691 1.00 52.03 C ANISOU 2370 CB ALA A 328 5599 8006 6163 -363 -230 -232 C ATOM 2371 N GLN A 329 -23.489 -1.012 69.898 1.00 47.24 N ANISOU 2371 N GLN A 329 5576 6291 6080 -155 -719 -1011 N ATOM 2372 CA GLN A 329 -24.640 -1.270 69.063 1.00 46.84 C ANISOU 2372 CA GLN A 329 5628 7058 5110 -652 -189 -1405 C ATOM 2373 C GLN A 329 -24.431 -0.649 67.701 1.00 42.73 C ANISOU 2373 C GLN A 329 4245 5635 6355 -88 729 -651 C ATOM 2374 O GLN A 329 -24.554 0.567 67.525 1.00 43.06 O ANISOU 2374 O GLN A 329 5032 5143 6186 -735 737 -1477 O ATOM 2375 CB GLN A 329 -25.911 -0.730 69.712 1.00 51.83 C ANISOU 2375 CB GLN A 329 7149 6272 6271 -542 921 -2230 C ATOM 2376 CG GLN A 329 -26.213 -1.375 71.054 1.00 67.62 C ANISOU 2376 CG GLN A 329 8275 9637 7779 -2203 551 -204 C ATOM 2377 CD GLN A 329 -27.587 -1.009 71.580 1.00 82.65 C ANISOU 2377 CD GLN A 329 10114 11205 10083 600 1793 284 C ATOM 2378 OE1 GLN A 329 -28.320 -0.230 70.963 1.00 93.63 O ANISOU 2378 OE1 GLN A 329 12096 10318 13158 479 1794 2347 O ATOM 2379 NE2 GLN A 329 -27.946 -1.574 72.727 1.00 94.16 N ANISOU 2379 NE2 GLN A 329 12893 11479 11403 -2783 -192 1788 N ATOM 2380 N LEU A 330 -24.119 -1.506 66.736 1.00 39.63 N ANISOU 2380 N LEU A 330 4337 5401 5319 -141 218 -247 N ATOM 2381 CA LEU A 330 -23.802 -1.075 65.385 1.00 34.00 C ANISOU 2381 CA LEU A 330 3738 4529 4650 -850 -453 -790 C ATOM 2382 C LEU A 330 -25.002 -0.459 64.746 1.00 31.19 C ANISOU 2382 C LEU A 330 4600 2943 4306 227 342 -1024 C ATOM 2383 O LEU A 330 -26.125 -0.790 65.078 1.00 39.30 O ANISOU 2383 O LEU A 330 4514 4870 5547 798 1239 -1260 O ATOM 2384 CB LEU A 330 -23.372 -2.271 64.538 1.00 33.29 C ANISOU 2384 CB LEU A 330 3830 4439 4379 14 -114 -141 C ATOM 2385 CG LEU A 330 -22.041 -2.875 64.937 1.00 33.77 C ANISOU 2385 CG LEU A 330 3714 3958 5157 188 78 -316 C ATOM 2386 CD1 LEU A 330 -21.853 -4.164 64.161 1.00 31.51 C ANISOU 2386 CD1 LEU A 330 4093 3961 3918 187 341 97 C ATOM 2387 CD2 LEU A 330 -20.956 -1.865 64.613 1.00 40.28 C ANISOU 2387 CD2 LEU A 330 4588 5006 5708 -303 1329 -138 C ATOM 2388 N ASN A 331 -24.779 0.407 63.784 1.00 38.07 N ANISOU 2388 N ASN A 331 5172 3705 5588 -766 -257 69 N ATOM 2389 CA ASN A 331 -25.904 0.955 63.076 1.00 41.53 C ANISOU 2389 CA ASN A 331 5351 4767 5659 -394 -721 -738 C ATOM 2390 C ASN A 331 -25.622 0.868 61.600 1.00 37.66 C ANISOU 2390 C ASN A 331 4861 3478 5969 -101 130 -407 C ATOM 2391 O ASN A 331 -24.541 0.422 61.192 1.00 37.71 O ANISOU 2391 O ASN A 331 3903 3852 6571 -781 165 -38 O ATOM 2392 CB ASN A 331 -26.152 2.398 63.504 1.00 45.73 C ANISOU 2392 CB ASN A 331 5328 5609 6436 -21 485 -1741 C ATOM 2393 CG ASN A 331 -24.940 3.270 63.291 1.00 50.70 C ANISOU 2393 CG ASN A 331 7109 5718 6437 -1129 -22 53 C ATOM 2394 OD1 ASN A 331 -24.533 3.517 62.157 1.00 55.26 O ANISOU 2394 OD1 ASN A 331 7337 6810 6849 -876 1097 -770 O ATOM 2395 ND2 ASN A 331 -24.347 3.736 64.385 1.00 51.39 N ANISOU 2395 ND2 ASN A 331 5908 6622 6994 -339 82 -853 N ATOM 2396 N TYR A 332 -26.597 1.296 60.805 1.00 39.36 N ANISOU 2396 N TYR A 332 4565 4911 5479 -47 403 294 N ATOM 2397 CA TYR A 332 -26.498 1.230 59.362 1.00 42.91 C ANISOU 2397 CA TYR A 332 5462 5640 5199 424 468 -165 C ATOM 2398 C TYR A 332 -25.187 1.808 58.820 1.00 47.74 C ANISOU 2398 C TYR A 332 5583 5743 6809 -789 319 -1109 C ATOM 2399 O TYR A 332 -24.581 1.221 57.921 1.00 45.00 O ANISOU 2399 O TYR A 332 5624 4992 6478 -435 -73 -881 O ATOM 2400 CB TYR A 332 -27.706 1.905 58.702 1.00 48.42 C ANISOU 2400 CB TYR A 332 5362 7731 5303 350 440 799 C ATOM 2401 CG TYR A 332 -27.559 2.043 57.202 1.00 40.30 C ANISOU 2401 CG TYR A 332 5027 5056 5227 463 1245 -782 C ATOM 2402 CD1 TYR A 332 -26.841 3.099 56.662 1.00 38.45 C ANISOU 2402 CD1 TYR A 332 5061 4185 5364 809 891 -1067 C ATOM 2403 CD2 TYR A 332 -28.118 1.115 56.330 1.00 40.48 C ANISOU 2403 CD2 TYR A 332 4124 5915 5342 191 -214 -153 C ATOM 2404 CE1 TYR A 332 -26.687 3.239 55.299 1.00 43.68 C ANISOU 2404 CE1 TYR A 332 5695 5364 5537 424 277 -224 C ATOM 2405 CE2 TYR A 332 -27.967 1.246 54.952 1.00 40.55 C ANISOU 2405 CE2 TYR A 332 4519 5093 5792 476 -155 733 C ATOM 2406 CZ TYR A 332 -27.248 2.313 54.444 1.00 41.87 C ANISOU 2406 CZ TYR A 332 4656 5588 5663 -143 18 213 C ATOM 2407 OH TYR A 332 -27.072 2.487 53.086 1.00 42.61 O ANISOU 2407 OH TYR A 332 5577 5229 5384 1131 -231 -367 O ATOM 2408 N ASN A 333 -24.754 2.953 59.351 1.00 45.33 N ANISOU 2408 N ASN A 333 5120 4938 7162 101 774 -1187 N ATOM 2409 CA ASN A 333 -23.532 3.610 58.852 1.00 46.42 C ANISOU 2409 CA ASN A 333 5516 4874 7247 145 845 -247 C ATOM 2410 C ASN A 333 -22.298 2.749 59.048 1.00 33.88 C ANISOU 2410 C ASN A 333 4768 3648 4455 -898 21 -578 C ATOM 2411 O ASN A 333 -21.492 2.585 58.131 1.00 40.35 O ANISOU 2411 O ASN A 333 5004 3990 6335 -1284 1171 -355 O ATOM 2412 CB ASN A 333 -23.304 4.969 59.530 1.00 44.48 C ANISOU 2412 CB ASN A 333 5693 5658 5549 -564 393 -168 C ATOM 2413 CG ASN A 333 -24.330 6.007 59.126 1.00 57.94 C ANISOU 2413 CG ASN A 333 7876 6055 8082 249 325 1008 C ATOM 2414 OD1 ASN A 333 -24.789 6.035 57.982 1.00 71.47 O ANISOU 2414 OD1 ASN A 333 9784 9224 8147 -2325 -179 842 O ATOM 2415 ND2 ASN A 333 -24.686 6.880 60.064 1.00 57.23 N ANISOU 2415 ND2 ASN A 333 7657 7310 6777 -40 -306 657 N ATOM 2416 N ASN A 334 -22.159 2.203 60.254 1.00 33.32 N ANISOU 2416 N ASN A 334 4829 3254 4575 -323 181 -727 N ATOM 2417 CA ASN A 334 -21.038 1.342 60.590 1.00 36.99 C ANISOU 2417 CA ASN A 334 4316 4562 5173 -601 -546 -391 C ATOM 2418 C ASN A 334 -20.854 0.224 59.562 1.00 43.71 C ANISOU 2418 C ASN A 334 5271 5373 5960 -580 397 -1014 C ATOM 2419 O ASN A 334 -19.804 0.132 58.931 1.00 42.30 O ANISOU 2419 O ASN A 334 5176 4837 6058 -1237 403 -1702 O ATOM 2420 CB ASN A 334 -21.220 0.725 61.977 1.00 41.09 C ANISOU 2420 CB ASN A 334 5437 5148 5025 -889 -223 -800 C ATOM 2421 CG ASN A 334 -21.403 1.761 63.074 1.00 44.40 C ANISOU 2421 CG ASN A 334 5797 5172 5901 -691 1205 -991 C ATOM 2422 OD1 ASN A 334 -22.192 1.552 63.991 1.00 40.75 O ANISOU 2422 OD1 ASN A 334 5436 4263 5782 -579 921 -969 O ATOM 2423 ND2 ASN A 334 -20.656 2.866 63.004 1.00 37.87 N ANISOU 2423 ND2 ASN A 334 6001 3595 4790 270 1413 -1630 N ATOM 2424 N VAL A 335 -21.888 -0.605 59.387 1.00 40.87 N ANISOU 2424 N VAL A 335 4951 4678 5898 -331 517 -497 N ATOM 2425 CA VAL A 335 -21.789 -1.797 58.544 1.00 35.14 C ANISOU 2425 CA VAL A 335 4490 4466 4394 -502 511 -13 C ATOM 2426 C VAL A 335 -21.773 -1.460 57.062 1.00 33.08 C ANISOU 2426 C VAL A 335 3912 4275 4379 -17 132 68 C ATOM 2427 O VAL A 335 -20.980 -2.017 56.308 1.00 31.83 O ANISOU 2427 O VAL A 335 4031 3924 4138 -39 -35 -52 O ATOM 2428 CB VAL A 335 -22.917 -2.825 58.820 1.00 33.02 C ANISOU 2428 CB VAL A 335 4274 4136 4134 -517 449 -764 C ATOM 2429 CG1 VAL A 335 -22.709 -4.087 57.980 1.00 28.31 C ANISOU 2429 CG1 VAL A 335 2894 3856 4005 10 773 -319 C ATOM 2430 CG2 VAL A 335 -22.970 -3.180 60.301 1.00 29.56 C ANISOU 2430 CG2 VAL A 335 3611 3327 4291 69 -31 325 C ATOM 2431 N MET A 336 -22.643 -0.550 56.646 1.00 29.17 N ANISOU 2431 N MET A 336 3378 3073 4631 -469 627 -428 N ATOM 2432 CA MET A 336 -22.776 -0.228 55.234 1.00 37.14 C ANISOU 2432 CA MET A 336 5201 4250 4658 -190 68 -266 C ATOM 2433 C MET A 336 -21.680 0.685 54.701 1.00 42.98 C ANISOU 2433 C MET A 336 5405 5058 5867 -355 719 -46 C ATOM 2434 O MET A 336 -21.218 0.501 53.576 1.00 45.49 O ANISOU 2434 O MET A 336 5642 5328 6313 -813 1712 555 O ATOM 2435 CB MET A 336 -24.156 0.363 54.927 1.00 47.14 C ANISOU 2435 CB MET A 336 5049 5230 7631 176 60 -655 C ATOM 2436 CG MET A 336 -25.283 -0.655 54.976 1.00 48.79 C ANISOU 2436 CG MET A 336 4792 6434 7309 -144 -533 -361 C ATOM 2437 SD MET A 336 -25.064 -2.018 53.815 1.00 54.13 S ANISOU 2437 SD MET A 336 6315 6813 7435 -394 559 -332 S ATOM 2438 CE MET A 336 -25.149 -1.178 52.241 1.00 44.56 C ANISOU 2438 CE MET A 336 4326 6017 6587 241 -210 -457 C ATOM 2439 N ASP A 337 -21.278 1.677 55.489 1.00 45.29 N ANISOU 2439 N ASP A 337 5686 5173 6346 -679 -547 384 N ATOM 2440 CA ASP A 337 -20.361 2.700 54.978 1.00 46.94 C ANISOU 2440 CA ASP A 337 5219 5880 6733 -462 196 233 C ATOM 2441 C ASP A 337 -18.964 2.574 55.572 1.00 40.10 C ANISOU 2441 C ASP A 337 5376 4193 5667 286 333 -407 C ATOM 2442 O ASP A 337 -17.992 3.006 54.958 1.00 49.13 O ANISOU 2442 O ASP A 337 6294 5924 6448 123 1710 -1098 O ATOM 2443 CB ASP A 337 -20.903 4.122 55.229 1.00 53.78 C ANISOU 2443 CB ASP A 337 6164 5967 8304 -678 257 -367 C ATOM 2444 CG ASP A 337 -22.189 4.438 54.441 1.00 56.59 C ANISOU 2444 CG ASP A 337 7109 6282 8109 769 505 496 C ATOM 2445 OD1 ASP A 337 -22.372 3.991 53.275 1.00 53.67 O ANISOU 2445 OD1 ASP A 337 7322 5804 7264 863 1333 1377 O ATOM 2446 OD2 ASP A 337 -23.024 5.174 55.008 1.00 61.05 O ANISOU 2446 OD2 ASP A 337 7977 6341 8875 240 2802 1125 O ATOM 2447 N GLU A 338 -18.859 1.982 56.759 1.00 40.53 N ANISOU 2447 N GLU A 338 5443 4656 5300 344 320 -717 N ATOM 2448 CA GLU A 338 -17.592 1.982 57.496 1.00 41.44 C ANISOU 2448 CA GLU A 338 5640 4780 5324 -210 92 -630 C ATOM 2449 C GLU A 338 -16.889 0.625 57.574 1.00 39.70 C ANISOU 2449 C GLU A 338 4848 5020 5214 -235 359 -61 C ATOM 2450 O GLU A 338 -16.034 0.412 58.427 1.00 38.86 O ANISOU 2450 O GLU A 338 4639 4613 5511 -1286 -205 -1205 O ATOM 2451 CB GLU A 338 -17.792 2.596 58.893 1.00 39.24 C ANISOU 2451 CB GLU A 338 4802 4868 5237 -904 826 -453 C ATOM 2452 CG GLU A 338 -18.181 4.069 58.827 1.00 45.31 C ANISOU 2452 CG GLU A 338 5754 5248 6210 -296 593 -142 C ATOM 2453 CD GLU A 338 -18.800 4.605 60.105 1.00 50.05 C ANISOU 2453 CD GLU A 338 6498 6591 5926 29 47 -396 C ATOM 2454 OE1 GLU A 338 -18.394 4.195 61.209 1.00 48.42 O ANISOU 2454 OE1 GLU A 338 6495 6102 5799 504 469 -163 O ATOM 2455 OE2 GLU A 338 -19.696 5.462 60.003 1.00 63.74 O ANISOU 2455 OE2 GLU A 338 7419 6762 10038 654 -202 -32 O ATOM 2456 N MET A 339 -17.229 -0.292 56.675 1.00 45.41 N ANISOU 2456 N MET A 339 5507 5339 6407 24 1149 -1068 N ATOM 2457 CA MET A 339 -16.595 -1.615 56.697 1.00 39.84 C ANISOU 2457 CA MET A 339 4708 5056 5373 -245 885 -355 C ATOM 2458 C MET A 339 -16.065 -2.089 55.335 1.00 39.29 C ANISOU 2458 C MET A 339 4521 4948 5459 -566 1020 -528 C ATOM 2459 O MET A 339 -16.292 -3.239 54.966 1.00 35.95 O ANISOU 2459 O MET A 339 3496 4965 5197 -473 972 -566 O ATOM 2460 CB MET A 339 -17.541 -2.671 57.302 1.00 33.81 C ANISOU 2460 CB MET A 339 4119 4405 4321 186 33 9 C ATOM 2461 CG MET A 339 -17.832 -2.488 58.786 1.00 33.82 C ANISOU 2461 CG MET A 339 4735 4021 4093 910 131 313 C ATOM 2462 SD MET A 339 -18.692 -3.857 59.596 1.00 36.79 S ANISOU 2462 SD MET A 339 4244 4426 5308 -256 329 -697 S ATOM 2463 CE MET A 339 -17.418 -5.119 59.672 1.00 32.41 C ANISOU 2463 CE MET A 339 4234 4157 3924 -202 -978 260 C ATOM 2464 N PRO A 340 -15.323 -1.226 54.598 1.00 38.80 N ANISOU 2464 N PRO A 340 5578 4198 4965 -111 1032 -87 N ATOM 2465 CA PRO A 340 -14.858 -1.683 53.277 1.00 31.70 C ANISOU 2465 CA PRO A 340 4564 3509 3970 -174 -181 210 C ATOM 2466 C PRO A 340 -13.894 -2.872 53.346 1.00 27.03 C ANISOU 2466 C PRO A 340 2839 3671 3758 -684 414 72 C ATOM 2467 O PRO A 340 -13.854 -3.682 52.428 1.00 34.24 O ANISOU 2467 O PRO A 340 4131 4372 4504 86 802 -464 O ATOM 2468 CB PRO A 340 -14.131 -0.456 52.717 1.00 31.42 C ANISOU 2468 CB PRO A 340 4307 4159 3469 -112 300 397 C ATOM 2469 CG PRO A 340 -13.635 0.262 53.927 1.00 35.57 C ANISOU 2469 CG PRO A 340 4573 4259 4682 -737 709 -784 C ATOM 2470 CD PRO A 340 -14.758 0.101 54.932 1.00 39.17 C ANISOU 2470 CD PRO A 340 4646 4938 5299 -522 980 -509 C ATOM 2471 N PHE A 341 -13.132 -2.978 54.425 1.00 31.61 N ANISOU 2471 N PHE A 341 4025 3801 4185 -196 -240 -1 N ATOM 2472 CA PHE A 341 -12.158 -4.056 54.542 1.00 35.83 C ANISOU 2472 CA PHE A 341 4088 4207 5318 -15 115 2 C ATOM 2473 C PHE A 341 -12.788 -5.399 54.883 1.00 33.40 C ANISOU 2473 C PHE A 341 3766 4188 4734 -229 98 -447 C ATOM 2474 O PHE A 341 -12.359 -6.428 54.381 1.00 32.50 O ANISOU 2474 O PHE A 341 3364 4190 4792 -737 578 -473 O ATOM 2475 CB PHE A 341 -11.057 -3.750 55.562 1.00 33.86 C ANISOU 2475 CB PHE A 341 4308 4256 4299 56 558 -338 C ATOM 2476 CG PHE A 341 -10.003 -4.813 55.610 1.00 33.29 C ANISOU 2476 CG PHE A 341 3852 4221 4574 -152 -203 148 C ATOM 2477 CD1 PHE A 341 -9.061 -4.916 54.586 1.00 39.29 C ANISOU 2477 CD1 PHE A 341 4458 4250 6218 185 1015 -666 C ATOM 2478 CD2 PHE A 341 -9.991 -5.756 56.626 1.00 29.52 C ANISOU 2478 CD2 PHE A 341 3513 3927 3777 -696 -298 -379 C ATOM 2479 CE1 PHE A 341 -8.091 -5.916 54.603 1.00 31.76 C ANISOU 2479 CE1 PHE A 341 3678 3677 4712 -528 -438 -123 C ATOM 2480 CE2 PHE A 341 -9.030 -6.761 56.644 1.00 34.52 C ANISOU 2480 CE2 PHE A 341 3751 3979 5383 -616 235 -674 C ATOM 2481 CZ PHE A 341 -8.081 -6.838 55.632 1.00 33.04 C ANISOU 2481 CZ PHE A 341 4636 3951 3967 91 -190 -453 C ATOM 2482 N ALA A 342 -13.774 -5.386 55.771 1.00 35.29 N ANISOU 2482 N ALA A 342 4562 4705 4141 -645 330 75 N ATOM 2483 CA ALA A 342 -14.534 -6.584 56.075 1.00 32.52 C ANISOU 2483 CA ALA A 342 4249 4490 3617 -518 543 -407 C ATOM 2484 C ALA A 342 -15.180 -7.042 54.791 1.00 25.04 C ANISOU 2484 C ALA A 342 2498 3622 3393 -33 890 223 C ATOM 2485 O ALA A 342 -15.252 -8.230 54.490 1.00 32.02 O ANISOU 2485 O ALA A 342 3342 4104 4719 -130 944 -226 O ATOM 2486 CB ALA A 342 -15.602 -6.273 57.110 1.00 31.41 C ANISOU 2486 CB ALA A 342 4016 3462 4455 -48 632 -485 C ATOM 2487 N GLU A 343 -15.657 -6.084 54.020 1.00 23.93 N ANISOU 2487 N GLU A 343 2532 3395 3162 -203 750 107 N ATOM 2488 CA GLU A 343 -16.259 -6.413 52.747 1.00 26.51 C ANISOU 2488 CA GLU A 343 2581 3753 3739 -597 242 -185 C ATOM 2489 C GLU A 343 -15.292 -7.087 51.771 1.00 32.97 C ANISOU 2489 C GLU A 343 3772 4202 4551 -113 354 -1092 C ATOM 2490 O GLU A 343 -15.680 -8.011 51.045 1.00 29.11 O ANISOU 2490 O GLU A 343 3361 3633 4064 -896 450 -178 O ATOM 2491 CB GLU A 343 -16.885 -5.190 52.098 1.00 29.37 C ANISOU 2491 CB GLU A 343 3377 4004 3775 365 878 -155 C ATOM 2492 CG GLU A 343 -17.385 -5.496 50.698 1.00 38.88 C ANISOU 2492 CG GLU A 343 4830 5591 4350 111 -34 -354 C ATOM 2493 CD GLU A 343 -18.822 -5.082 50.468 1.00 51.08 C ANISOU 2493 CD GLU A 343 5217 7645 6543 1149 -208 -1083 C ATOM 2494 OE1 GLU A 343 -19.531 -4.758 51.448 1.00 52.55 O ANISOU 2494 OE1 GLU A 343 6065 7716 6185 508 568 -9 O ATOM 2495 OE2 GLU A 343 -19.246 -5.099 49.294 1.00 56.30 O ANISOU 2495 OE2 GLU A 343 6904 7823 6663 1303 -477 413 O ATOM 2496 N ARG A 344 -14.052 -6.598 51.729 1.00 35.04 N ANISOU 2496 N ARG A 344 3664 4532 5117 -215 648 -464 N ATOM 2497 CA ARG A 344 -13.001 -7.230 50.924 1.00 34.46 C ANISOU 2497 CA ARG A 344 3911 3694 5486 -65 770 -219 C ATOM 2498 C ARG A 344 -12.734 -8.654 51.419 1.00 24.26 C ANISOU 2498 C ARG A 344 2516 3411 3290 -859 470 -218 C ATOM 2499 O ARG A 344 -12.499 -9.547 50.626 1.00 25.71 O ANISOU 2499 O ARG A 344 2875 3176 3717 -213 426 -75 O ATOM 2500 CB ARG A 344 -11.694 -6.410 50.965 1.00 35.77 C ANISOU 2500 CB ARG A 344 4109 4217 5262 -626 1299 45 C ATOM 2501 CG ARG A 344 -11.670 -5.190 50.053 1.00 32.97 C ANISOU 2501 CG ARG A 344 3188 4419 4919 44 799 231 C ATOM 2502 CD ARG A 344 -10.344 -4.431 50.141 1.00 31.94 C ANISOU 2502 CD ARG A 344 3796 4114 4224 -358 -67 590 C ATOM 2503 NE ARG A 344 -10.187 -3.578 48.959 1.00 28.99 N ANISOU 2503 NE ARG A 344 3549 3479 3984 -216 -391 222 N ATOM 2504 CZ ARG A 344 -9.674 -3.981 47.800 1.00 32.19 C ANISOU 2504 CZ ARG A 344 3230 4342 4656 -534 349 100 C ATOM 2505 NH1 ARG A 344 -9.223 -5.225 47.659 1.00 39.32 N ANISOU 2505 NH1 ARG A 344 3799 4457 6682 -330 382 -301 N ATOM 2506 NH2 ARG A 344 -9.610 -3.140 46.773 1.00 32.51 N ANISOU 2506 NH2 ARG A 344 3728 4003 4621 -473 -138 -111 N ATOM 2507 N CYS A 345 -12.771 -8.859 52.733 1.00 23.85 N ANISOU 2507 N CYS A 345 2337 3361 3361 -582 -258 66 N ATOM 2508 CA CYS A 345 -12.517 -10.182 53.285 1.00 26.81 C ANISOU 2508 CA CYS A 345 3211 3262 3712 -21 -108 -27 C ATOM 2509 C CYS A 345 -13.583 -11.163 52.830 1.00 27.18 C ANISOU 2509 C CYS A 345 3242 3436 3646 -118 120 5 C ATOM 2510 O CYS A 345 -13.272 -12.306 52.478 1.00 26.76 O ANISOU 2510 O CYS A 345 2495 3746 3925 -352 808 -242 O ATOM 2511 CB CYS A 345 -12.469 -10.155 54.812 1.00 32.62 C ANISOU 2511 CB CYS A 345 4278 4447 3667 -435 -4 -990 C ATOM 2512 SG CYS A 345 -11.095 -9.220 55.536 1.00 33.10 S ANISOU 2512 SG CYS A 345 3538 4241 4795 -333 -121 -437 S ATOM 2513 N ALA A 346 -14.838 -10.715 52.849 1.00 29.30 N ANISOU 2513 N ALA A 346 3221 3646 4265 -27 -211 -451 N ATOM 2514 CA ALA A 346 -15.951 -11.544 52.408 1.00 25.47 C ANISOU 2514 CA ALA A 346 2860 3296 3521 178 88 -437 C ATOM 2515 C ALA A 346 -15.827 -11.891 50.928 1.00 23.55 C ANISOU 2515 C ALA A 346 2418 3076 3454 321 614 -78 C ATOM 2516 O ALA A 346 -15.972 -13.048 50.549 1.00 25.06 O ANISOU 2516 O ALA A 346 2428 3177 3915 -322 313 -7 O ATOM 2517 CB ALA A 346 -17.277 -10.843 52.679 1.00 25.41 C ANISOU 2517 CB ALA A 346 2589 2994 4070 -67 291 133 C ATOM 2518 N ARG A 347 -15.566 -10.894 50.084 1.00 23.01 N ANISOU 2518 N ARG A 347 2565 2645 3533 627 372 -179 N ATOM 2519 CA ARG A 347 -15.562 -11.126 48.647 1.00 28.69 C ANISOU 2519 CA ARG A 347 3496 3867 3537 658 103 -32 C ATOM 2520 C ARG A 347 -14.388 -12.000 48.199 1.00 27.24 C ANISOU 2520 C ARG A 347 3305 3554 3491 355 -77 -241 C ATOM 2521 O ARG A 347 -14.516 -12.813 47.281 1.00 23.60 O ANISOU 2521 O ARG A 347 2513 3135 3318 -385 425 117 O ATOM 2522 CB ARG A 347 -15.583 -9.803 47.883 1.00 33.01 C ANISOU 2522 CB ARG A 347 3797 3490 5252 -549 -350 139 C ATOM 2523 CG ARG A 347 -16.918 -9.085 48.003 1.00 40.86 C ANISOU 2523 CG ARG A 347 4823 5322 5377 475 213 -952 C ATOM 2524 CD ARG A 347 -16.853 -7.629 47.561 1.00 48.85 C ANISOU 2524 CD ARG A 347 5933 6350 6276 -545 -109 78 C ATOM 2525 NE ARG A 347 -16.412 -7.485 46.177 1.00 56.19 N ANISOU 2525 NE ARG A 347 7059 7511 6778 -483 -480 1287 N ATOM 2526 CZ ARG A 347 -17.206 -7.574 45.112 1.00 56.80 C ANISOU 2526 CZ ARG A 347 7179 7274 7126 -1015 -484 338 C ATOM 2527 NH1 ARG A 347 -18.516 -7.814 45.251 1.00 50.57 N ANISOU 2527 NH1 ARG A 347 6519 4181 8512 1470 1303 889 N ATOM 2528 NH2 ARG A 347 -16.682 -7.424 43.896 1.00 53.15 N ANISOU 2528 NH2 ARG A 347 7144 4627 8422 -1269 1433 -708 N ATOM 2529 N GLU A 348 -13.248 -11.817 48.851 1.00 27.68 N ANISOU 2529 N GLU A 348 3141 3495 3880 80 -51 -134 N ATOM 2530 CA GLU A 348 -12.069 -12.621 48.549 1.00 27.12 C ANISOU 2530 CA GLU A 348 3174 3441 3688 100 37 -138 C ATOM 2531 C GLU A 348 -12.269 -14.073 49.019 1.00 26.07 C ANISOU 2531 C GLU A 348 3099 3530 3276 128 -5 -127 C ATOM 2532 O GLU A 348 -11.724 -15.006 48.427 1.00 26.00 O ANISOU 2532 O GLU A 348 2980 3545 3350 217 314 -40 O ATOM 2533 CB GLU A 348 -10.810 -11.963 49.139 1.00 27.02 C ANISOU 2533 CB GLU A 348 3511 2866 3887 224 -319 -393 C ATOM 2534 CG GLU A 348 -9.545 -12.818 49.143 1.00 27.95 C ANISOU 2534 CG GLU A 348 2913 3747 3958 57 393 -312 C ATOM 2535 CD GLU A 348 -8.969 -13.104 47.755 1.00 26.99 C ANISOU 2535 CD GLU A 348 3357 3520 3376 162 6 209 C ATOM 2536 OE1 GLU A 348 -9.573 -12.752 46.721 1.00 23.31 O ANISOU 2536 OE1 GLU A 348 2461 3272 3120 -496 112 -109 O ATOM 2537 OE2 GLU A 348 -7.871 -13.683 47.699 1.00 30.65 O ANISOU 2537 OE2 GLU A 348 3596 3469 4579 391 385 -346 O ATOM 2538 N SER A 349 -13.081 -14.282 50.055 1.00 24.89 N ANISOU 2538 N SER A 349 2802 3461 3194 43 -170 195 N ATOM 2539 CA SER A 349 -13.365 -15.661 50.500 1.00 24.65 C ANISOU 2539 CA SER A 349 2986 3243 3135 27 -8 72 C ATOM 2540 C SER A 349 -14.201 -16.383 49.467 1.00 25.34 C ANISOU 2540 C SER A 349 3220 3199 3206 58 28 -88 C ATOM 2541 O SER A 349 -14.001 -17.577 49.199 1.00 26.17 O ANISOU 2541 O SER A 349 2983 3024 3935 54 160 35 O ATOM 2542 CB SER A 349 -14.108 -15.684 51.839 1.00 25.17 C ANISOU 2542 CB SER A 349 3354 3054 3156 367 163 -5 C ATOM 2543 OG SER A 349 -13.290 -15.230 52.903 1.00 27.63 O ANISOU 2543 OG SER A 349 2857 3822 3816 325 16 -105 O ATOM 2544 N ILE A 350 -15.149 -15.642 48.897 1.00 24.27 N ANISOU 2544 N ILE A 350 2883 3222 3114 -270 58 91 N ATOM 2545 CA ILE A 350 -15.961 -16.125 47.802 1.00 21.74 C ANISOU 2545 CA ILE A 350 2704 2836 2720 8 13 286 C ATOM 2546 C ILE A 350 -15.117 -16.244 46.547 1.00 23.92 C ANISOU 2546 C ILE A 350 3143 2891 3054 -120 218 -151 C ATOM 2547 O ILE A 350 -15.351 -17.110 45.726 1.00 23.73 O ANISOU 2547 O ILE A 350 2990 3001 3023 -193 457 -179 O ATOM 2548 CB ILE A 350 -17.110 -15.151 47.496 1.00 21.46 C ANISOU 2548 CB ILE A 350 2525 2996 2631 220 -2 -217 C ATOM 2549 CG1 ILE A 350 -18.047 -15.052 48.705 1.00 21.43 C ANISOU 2549 CG1 ILE A 350 2583 2613 2945 43 205 -175 C ATOM 2550 CG2 ILE A 350 -17.874 -15.618 46.261 1.00 22.09 C ANISOU 2550 CG2 ILE A 350 2845 2518 3028 -68 -355 -35 C ATOM 2551 CD1 ILE A 350 -19.072 -13.917 48.620 1.00 20.25 C ANISOU 2551 CD1 ILE A 350 2513 2673 2508 52 -258 -34 C ATOM 2552 N ARG A 351 -14.166 -15.324 46.383 1.00 25.08 N ANISOU 2552 N ARG A 351 2527 3616 3384 -218 74 80 N ATOM 2553 CA ARG A 351 -13.249 -15.331 45.238 1.00 25.98 C ANISOU 2553 CA ARG A 351 3383 3145 3342 -129 321 203 C ATOM 2554 C ARG A 351 -12.314 -16.543 45.191 1.00 23.56 C ANISOU 2554 C ARG A 351 2875 3206 2869 -212 309 -94 C ATOM 2555 O ARG A 351 -12.110 -17.141 44.135 1.00 23.51 O ANISOU 2555 O ARG A 351 2484 2981 3466 -328 251 -324 O ATOM 2556 CB ARG A 351 -12.429 -14.039 45.206 1.00 27.44 C ANISOU 2556 CB ARG A 351 3082 3344 3999 -97 250 432 C ATOM 2557 CG ARG A 351 -11.536 -13.900 43.983 1.00 33.59 C ANISOU 2557 CG ARG A 351 4054 4338 4370 -1755 315 770 C ATOM 2558 CD ARG A 351 -10.069 -14.052 44.351 1.00 38.74 C ANISOU 2558 CD ARG A 351 4190 4909 5617 558 904 -166 C ATOM 2559 NE ARG A 351 -9.499 -15.290 43.828 1.00 32.21 N ANISOU 2559 NE ARG A 351 3970 3567 4700 -143 1215 967 N ATOM 2560 CZ ARG A 351 -8.586 -16.018 44.462 1.00 30.16 C ANISOU 2560 CZ ARG A 351 3630 4197 3632 -317 -3 -113 C ATOM 2561 NH1 ARG A 351 -8.134 -15.633 45.647 1.00 23.56 N ANISOU 2561 NH1 ARG A 351 2653 3153 3142 -582 1142 -315 N ATOM 2562 NH2 ARG A 351 -8.123 -17.132 43.910 1.00 29.20 N ANISOU 2562 NH2 ARG A 351 2820 3363 4912 252 940 365 N ATOM 2563 N ARG A 352 -11.758 -16.903 46.345 1.00 25.52 N ANISOU 2563 N ARG A 352 2876 3459 3361 -229 31 187 N ATOM 2564 CA ARG A 352 -10.944 -18.111 46.484 1.00 26.50 C ANISOU 2564 CA ARG A 352 3092 3425 3549 35 300 147 C ATOM 2565 C ARG A 352 -11.736 -19.435 46.493 1.00 29.03 C ANISOU 2565 C ARG A 352 3528 3609 3893 -10 377 -394 C ATOM 2566 O ARG A 352 -11.286 -20.441 45.912 1.00 25.64 O ANISOU 2566 O ARG A 352 3064 3399 3276 293 488 377 O ATOM 2567 CB ARG A 352 -10.109 -17.995 47.755 1.00 28.46 C ANISOU 2567 CB ARG A 352 3469 3605 3738 357 9 -136 C ATOM 2568 CG ARG A 352 -9.081 -19.095 47.935 1.00 26.56 C ANISOU 2568 CG ARG A 352 3246 3283 3560 52 107 128 C ATOM 2569 CD ARG A 352 -8.530 -19.055 49.346 1.00 29.62 C ANISOU 2569 CD ARG A 352 3922 3791 3539 165 -48 243 C ATOM 2570 NE ARG A 352 -7.453 -20.021 49.593 1.00 29.11 N ANISOU 2570 NE ARG A 352 3331 3795 3932 77 704 210 N ATOM 2571 CZ ARG A 352 -7.596 -21.159 50.273 1.00 33.86 C ANISOU 2571 CZ ARG A 352 3841 3829 5194 260 767 679 C ATOM 2572 NH1 ARG A 352 -8.786 -21.519 50.754 1.00 28.32 N ANISOU 2572 NH1 ARG A 352 3093 4096 3569 226 -11 32 N ATOM 2573 NH2 ARG A 352 -6.543 -21.952 50.465 1.00 29.88 N ANISOU 2573 NH2 ARG A 352 3112 3882 4359 -150 231 -59 N ATOM 2574 N ASP A 353 -12.903 -19.441 47.150 1.00 26.75 N ANISOU 2574 N ASP A 353 3648 3154 3360 68 406 93 N ATOM 2575 CA ASP A 353 -13.719 -20.647 47.256 1.00 26.57 C ANISOU 2575 CA ASP A 353 3106 3634 3353 2 194 283 C ATOM 2576 C ASP A 353 -15.200 -20.337 47.046 1.00 22.93 C ANISOU 2576 C ASP A 353 3348 2518 2845 322 82 -29 C ATOM 2577 O ASP A 353 -15.959 -20.255 48.013 1.00 23.68 O ANISOU 2577 O ASP A 353 2641 2909 3444 267 356 314 O ATOM 2578 CB ASP A 353 -13.488 -21.313 48.620 1.00 25.88 C ANISOU 2578 CB ASP A 353 3219 3261 3352 64 62 236 C ATOM 2579 CG ASP A 353 -12.037 -21.696 48.830 1.00 27.41 C ANISOU 2579 CG ASP A 353 3358 3589 3467 236 116 -166 C ATOM 2580 OD1 ASP A 353 -11.587 -22.662 48.177 1.00 26.78 O ANISOU 2580 OD1 ASP A 353 3215 3428 3530 86 421 -68 O ATOM 2581 OD2 ASP A 353 -11.348 -21.022 49.636 1.00 27.02 O ANISOU 2581 OD2 ASP A 353 2988 3461 3813 96 227 -41 O ATOM 2582 N PRO A 354 -15.608 -20.150 45.782 1.00 22.45 N ANISOU 2582 N PRO A 354 3024 2643 2863 -25 44 -147 N ATOM 2583 CA PRO A 354 -16.983 -19.756 45.477 1.00 25.01 C ANISOU 2583 CA PRO A 354 2932 3396 3172 -56 437 -12 C ATOM 2584 C PRO A 354 -17.956 -20.886 45.820 1.00 28.65 C ANISOU 2584 C PRO A 354 3512 3371 4000 -185 663 116 C ATOM 2585 O PRO A 354 -17.719 -22.046 45.452 1.00 28.11 O ANISOU 2585 O PRO A 354 3594 3468 3618 -685 524 -118 O ATOM 2586 CB PRO A 354 -16.958 -19.460 43.972 1.00 20.91 C ANISOU 2586 CB PRO A 354 2448 2629 2866 -249 -72 -344 C ATOM 2587 CG PRO A 354 -15.762 -20.215 43.459 1.00 23.09 C ANISOU 2587 CG PRO A 354 3197 3004 2571 68 186 -522 C ATOM 2588 CD PRO A 354 -14.763 -20.253 44.573 1.00 23.91 C ANISOU 2588 CD PRO A 354 3265 2834 2984 -171 71 172 C ATOM 2589 N PRO A 355 -19.022 -20.553 46.558 1.00 26.86 N ANISOU 2589 N PRO A 355 3293 3209 3700 5 353 -4 N ATOM 2590 CA PRO A 355 -20.007 -21.547 47.000 1.00 26.31 C ANISOU 2590 CA PRO A 355 3168 3301 3526 1 483 -197 C ATOM 2591 C PRO A 355 -20.762 -22.184 45.830 1.00 26.32 C ANISOU 2591 C PRO A 355 3393 3257 3350 294 146 -32 C ATOM 2592 O PRO A 355 -21.186 -23.337 45.926 1.00 26.68 O ANISOU 2592 O PRO A 355 3288 3413 3435 34 84 211 O ATOM 2593 CB PRO A 355 -20.972 -20.752 47.897 1.00 23.95 C ANISOU 2593 CB PRO A 355 3031 2982 3085 228 196 180 C ATOM 2594 CG PRO A 355 -20.402 -19.395 48.043 1.00 28.85 C ANISOU 2594 CG PRO A 355 3545 3403 4013 -233 666 -585 C ATOM 2595 CD PRO A 355 -19.323 -19.189 47.024 1.00 25.19 C ANISOU 2595 CD PRO A 355 3270 2867 3433 -115 148 249 C ATOM 2596 N LEU A 356 -20.920 -21.439 44.737 1.00 25.57 N ANISOU 2596 N LEU A 356 3142 3332 3239 -9 252 -36 N ATOM 2597 CA LEU A 356 -21.530 -21.975 43.524 1.00 24.97 C ANISOU 2597 CA LEU A 356 3175 3137 3173 93 197 211 C ATOM 2598 C LEU A 356 -20.440 -22.203 42.468 1.00 28.94 C ANISOU 2598 C LEU A 356 3847 3548 3598 -10 619 -124 C ATOM 2599 O LEU A 356 -19.846 -21.253 41.961 1.00 27.27 O ANISOU 2599 O LEU A 356 3323 3401 3638 191 525 14 O ATOM 2600 CB LEU A 356 -22.625 -21.026 43.023 1.00 23.30 C ANISOU 2600 CB LEU A 356 2378 3301 3173 -97 280 108 C ATOM 2601 CG LEU A 356 -23.754 -20.790 44.065 1.00 24.29 C ANISOU 2601 CG LEU A 356 2992 2875 3359 200 594 73 C ATOM 2602 CD1 LEU A 356 -24.651 -19.623 43.675 1.00 22.64 C ANISOU 2602 CD1 LEU A 356 2589 3007 3005 7 616 221 C ATOM 2603 CD2 LEU A 356 -24.603 -22.045 44.247 1.00 26.15 C ANISOU 2603 CD2 LEU A 356 3490 3124 3320 63 720 849 C ATOM 2604 N LEU A 357 -20.178 -23.470 42.147 1.00 31.34 N ANISOU 2604 N LEU A 357 4276 3537 4093 341 304 284 N ATOM 2605 CA LEU A 357 -19.052 -23.840 41.276 1.00 31.16 C ANISOU 2605 CA LEU A 357 4035 3867 3936 79 155 45 C ATOM 2606 C LEU A 357 -19.303 -23.595 39.797 1.00 29.76 C ANISOU 2606 C LEU A 357 3805 3464 4035 335 -143 282 C ATOM 2607 O LEU A 357 -18.365 -23.294 39.047 1.00 33.16 O ANISOU 2607 O LEU A 357 4198 3823 4579 154 98 676 O ATOM 2608 CB LEU A 357 -18.703 -25.321 41.454 1.00 33.64 C ANISOU 2608 CB LEU A 357 3882 4548 4351 1080 -119 463 C ATOM 2609 CG LEU A 357 -18.374 -25.824 42.857 1.00 32.18 C ANISOU 2609 CG LEU A 357 4114 3717 4396 24 -464 480 C ATOM 2610 CD1 LEU A 357 -17.811 -27.223 42.713 1.00 34.82 C ANISOU 2610 CD1 LEU A 357 4401 4477 4352 746 -256 -556 C ATOM 2611 CD2 LEU A 357 -17.400 -24.903 43.581 1.00 28.08 C ANISOU 2611 CD2 LEU A 357 3518 3432 3717 316 571 -214 C ATOM 2612 N MET A 358 -20.562 -23.758 39.388 1.00 27.58 N ANISOU 2612 N MET A 358 3611 3193 3675 -194 -86 125 N ATOM 2613 CA MET A 358 -20.964 -23.764 37.973 1.00 29.71 C ANISOU 2613 CA MET A 358 3770 3940 3577 56 -252 -120 C ATOM 2614 C MET A 358 -22.316 -23.096 37.734 1.00 29.48 C ANISOU 2614 C MET A 358 3948 3511 3739 289 303 271 C ATOM 2615 O MET A 358 -23.354 -23.609 38.169 1.00 33.06 O ANISOU 2615 O MET A 358 4253 4213 4093 -354 292 655 O ATOM 2616 CB MET A 358 -21.094 -25.209 37.473 1.00 31.24 C ANISOU 2616 CB MET A 358 3966 3580 4321 -235 702 167 C ATOM 2617 CG MET A 358 -19.802 -25.992 37.481 1.00 42.94 C ANISOU 2617 CG MET A 358 5246 5199 5868 1378 571 -80 C ATOM 2618 SD MET A 358 -18.924 -25.720 35.937 1.00 49.64 S ANISOU 2618 SD MET A 358 6101 6284 6474 -1329 942 422 S ATOM 2619 CE MET A 358 -20.203 -26.193 34.806 1.00 43.33 C ANISOU 2619 CE MET A 358 6853 6016 3594 801 7 1032 C ATOM 2620 N LEU A 359 -22.317 -21.986 37.000 1.00 25.65 N ANISOU 2620 N LEU A 359 2965 3179 3601 -254 262 124 N ATOM 2621 CA LEU A 359 -23.567 -21.324 36.610 1.00 23.27 C ANISOU 2621 CA LEU A 359 3319 2690 2830 -126 68 134 C ATOM 2622 C LEU A 359 -23.911 -21.847 35.239 1.00 23.64 C ANISOU 2622 C LEU A 359 3113 2732 3138 -48 64 -194 C ATOM 2623 O LEU A 359 -23.020 -22.017 34.409 1.00 24.67 O ANISOU 2623 O LEU A 359 3421 3186 2763 86 185 -164 O ATOM 2624 CB LEU A 359 -23.379 -19.803 36.576 1.00 19.57 C ANISOU 2624 CB LEU A 359 2820 2363 2251 378 401 242 C ATOM 2625 CG LEU A 359 -22.660 -19.302 37.831 1.00 23.29 C ANISOU 2625 CG LEU A 359 3083 2746 3019 -171 -6 159 C ATOM 2626 CD1 LEU A 359 -22.295 -17.818 37.777 1.00 22.59 C ANISOU 2626 CD1 LEU A 359 2806 2742 3032 -305 -140 226 C ATOM 2627 CD2 LEU A 359 -23.460 -19.647 39.098 1.00 24.65 C ANISOU 2627 CD2 LEU A 359 3598 2606 3163 -256 481 -433 C ATOM 2628 N MET A 360 -25.186 -22.120 35.000 1.00 24.03 N ANISOU 2628 N MET A 360 3144 2891 3095 -30 102 64 N ATOM 2629 CA MET A 360 -25.568 -22.808 33.785 1.00 26.63 C ANISOU 2629 CA MET A 360 3536 3115 3465 28 -265 -71 C ATOM 2630 C MET A 360 -26.746 -22.144 33.123 1.00 25.65 C ANISOU 2630 C MET A 360 3272 3018 3455 -168 23 206 C ATOM 2631 O MET A 360 -27.583 -21.543 33.796 1.00 28.28 O ANISOU 2631 O MET A 360 3896 3066 3781 -356 545 55 O ATOM 2632 CB MET A 360 -25.885 -24.271 34.105 1.00 28.17 C ANISOU 2632 CB MET A 360 3475 3134 4093 3 554 -136 C ATOM 2633 CG MET A 360 -24.625 -25.053 34.448 1.00 30.93 C ANISOU 2633 CG MET A 360 3797 3894 4059 36 64 592 C ATOM 2634 SD MET A 360 -24.895 -26.805 34.735 1.00 34.94 S ANISOU 2634 SD MET A 360 4884 3857 4533 74 451 141 S ATOM 2635 CE MET A 360 -25.856 -26.688 36.255 1.00 27.51 C ANISOU 2635 CE MET A 360 3847 2802 3800 188 21 915 C ATOM 2636 N ARG A 361 -26.787 -22.249 31.799 1.00 25.72 N ANISOU 2636 N ARG A 361 3184 3056 3532 -186 26 -24 N ATOM 2637 CA ARG A 361 -27.940 -21.850 31.015 1.00 26.44 C ANISOU 2637 CA ARG A 361 3635 3214 3195 136 83 191 C ATOM 2638 C ARG A 361 -28.174 -22.893 29.934 1.00 27.36 C ANISOU 2638 C ARG A 361 3750 3097 3547 37 -220 304 C ATOM 2639 O ARG A 361 -27.239 -23.577 29.517 1.00 30.92 O ANISOU 2639 O ARG A 361 4465 3674 3610 145 507 435 O ATOM 2640 CB ARG A 361 -27.688 -20.505 30.324 1.00 25.98 C ANISOU 2640 CB ARG A 361 3929 2868 3071 101 439 -84 C ATOM 2641 CG ARG A 361 -27.151 -19.400 31.213 1.00 26.58 C ANISOU 2641 CG ARG A 361 3725 3418 2954 -315 111 17 C ATOM 2642 CD ARG A 361 -28.250 -18.715 32.020 1.00 28.52 C ANISOU 2642 CD ARG A 361 3638 3171 4025 -93 121 -28 C ATOM 2643 NE ARG A 361 -27.691 -17.617 32.814 1.00 27.05 N ANISOU 2643 NE ARG A 361 3511 3430 3336 -129 -43 159 N ATOM 2644 CZ ARG A 361 -27.267 -17.710 34.075 1.00 28.32 C ANISOU 2644 CZ ARG A 361 3966 3297 3497 -472 -303 -88 C ATOM 2645 NH1 ARG A 361 -27.341 -18.866 34.755 1.00 26.58 N ANISOU 2645 NH1 ARG A 361 3250 3340 3506 -405 405 17 N ATOM 2646 NH2 ARG A 361 -26.757 -16.626 34.661 1.00 21.91 N ANISOU 2646 NH2 ARG A 361 2403 2882 3040 178 593 -243 N ATOM 2647 N LYS A 362 -29.410 -23.001 29.463 1.00 27.85 N ANISOU 2647 N LYS A 362 3684 3442 3455 -893 -82 409 N ATOM 2648 CA LYS A 362 -29.682 -23.773 28.254 1.00 30.70 C ANISOU 2648 CA LYS A 362 4019 3961 3684 -246 -122 31 C ATOM 2649 C LYS A 362 -29.448 -22.856 27.062 1.00 33.07 C ANISOU 2649 C LYS A 362 4353 4145 4065 -210 379 176 C ATOM 2650 O LYS A 362 -29.945 -21.719 27.033 1.00 33.02 O ANISOU 2650 O LYS A 362 4468 4358 3716 118 319 135 O ATOM 2651 CB LYS A 362 -31.138 -24.250 28.233 1.00 37.14 C ANISOU 2651 CB LYS A 362 4597 4621 4893 -1348 209 -5 C ATOM 2652 CG LYS A 362 -31.431 -25.325 27.194 1.00 37.76 C ANISOU 2652 CG LYS A 362 5009 5038 4298 -487 73 -65 C ATOM 2653 CD LYS A 362 -30.803 -26.651 27.612 1.00 53.41 C ANISOU 2653 CD LYS A 362 7530 5510 7253 441 -1151 -18 C ATOM 2654 CE LYS A 362 -31.036 -27.748 26.582 1.00 58.78 C ANISOU 2654 CE LYS A 362 7502 7614 7217 -1744 -807 -721 C ATOM 2655 NZ LYS A 362 -32.487 -27.955 26.314 1.00 57.46 N ANISOU 2655 NZ LYS A 362 6933 6613 8286 -1716 332 200 N ATOM 2656 N VAL A 363 -28.704 -23.336 26.073 1.00 31.72 N ANISOU 2656 N VAL A 363 3882 4041 4128 -209 -167 -219 N ATOM 2657 CA VAL A 363 -28.542 -22.553 24.854 1.00 34.54 C ANISOU 2657 CA VAL A 363 4656 4297 4168 -120 186 -193 C ATOM 2658 C VAL A 363 -29.801 -22.634 23.989 1.00 38.24 C ANISOU 2658 C VAL A 363 5080 4578 4871 119 -369 -93 C ATOM 2659 O VAL A 363 -30.106 -23.679 23.401 1.00 32.57 O ANISOU 2659 O VAL A 363 4720 3812 3840 134 81 637 O ATOM 2660 CB VAL A 363 -27.282 -22.967 24.087 1.00 34.56 C ANISOU 2660 CB VAL A 363 4174 4465 4489 77 -77 388 C ATOM 2661 CG1 VAL A 363 -27.124 -22.132 22.826 1.00 35.87 C ANISOU 2661 CG1 VAL A 363 5109 4399 4120 -599 -704 91 C ATOM 2662 CG2 VAL A 363 -26.076 -22.787 24.992 1.00 31.15 C ANISOU 2662 CG2 VAL A 363 4347 3319 4167 -276 -46 204 C ATOM 2663 N MET A 364 -30.539 -21.526 23.927 1.00 35.79 N ANISOU 2663 N MET A 364 4976 4295 4326 -227 0 -284 N ATOM 2664 CA MET A 364 -31.816 -21.485 23.208 1.00 39.74 C ANISOU 2664 CA MET A 364 5037 5418 4642 216 -69 -309 C ATOM 2665 C MET A 364 -31.654 -21.177 21.711 1.00 43.19 C ANISOU 2665 C MET A 364 5563 5543 5304 -477 -7 818 C ATOM 2666 O MET A 364 -32.583 -21.357 20.922 1.00 47.39 O ANISOU 2666 O MET A 364 6280 6929 4797 373 -199 85 O ATOM 2667 CB MET A 364 -32.767 -20.478 23.855 1.00 39.95 C ANISOU 2667 CB MET A 364 5908 4200 5068 -113 420 28 C ATOM 2668 CG MET A 364 -32.946 -20.663 25.358 1.00 43.63 C ANISOU 2668 CG MET A 364 5773 5801 5000 -355 -277 323 C ATOM 2669 SD MET A 364 -33.544 -22.314 25.797 1.00 48.33 S ANISOU 2669 SD MET A 364 5908 6118 6336 -303 -798 1015 S ATOM 2670 CE MET A 364 -35.211 -22.241 25.118 1.00 46.06 C ANISOU 2670 CE MET A 364 5483 5444 6574 -287 -943 723 C ATOM 2671 N ALA A 365 -30.466 -20.722 21.336 1.00 41.98 N ANISOU 2671 N ALA A 365 5269 5353 5329 -185 -68 630 N ATOM 2672 CA ALA A 365 -30.153 -20.354 19.957 1.00 44.99 C ANISOU 2672 CA ALA A 365 5716 6011 5364 1015 -256 1021 C ATOM 2673 C ALA A 365 -28.641 -20.242 19.853 1.00 42.69 C ANISOU 2673 C ALA A 365 5847 5300 5070 -342 113 292 C ATOM 2674 O ALA A 365 -27.985 -19.815 20.810 1.00 41.69 O ANISOU 2674 O ALA A 365 5984 4914 4941 -776 177 520 O ATOM 2675 CB ALA A 365 -30.815 -19.023 19.590 1.00 37.41 C ANISOU 2675 CB ALA A 365 5933 4423 3858 -247 -485 211 C ATOM 2676 N ASP A 366 -28.088 -20.639 18.708 1.00 37.44 N ANISOU 2676 N ASP A 366 5480 3656 5088 -171 -356 -77 N ATOM 2677 CA ASP A 366 -26.639 -20.637 18.502 1.00 41.92 C ANISOU 2677 CA ASP A 366 5568 4911 5447 -156 470 196 C ATOM 2678 C ASP A 366 -26.002 -19.339 18.979 1.00 39.36 C ANISOU 2678 C ASP A 366 5418 5280 4256 416 -245 -480 C ATOM 2679 O ASP A 366 -26.487 -18.261 18.660 1.00 43.35 O ANISOU 2679 O ASP A 366 6441 4796 5231 -308 619 628 O ATOM 2680 CB ASP A 366 -26.314 -20.839 17.022 1.00 43.97 C ANISOU 2680 CB ASP A 366 6612 5138 4956 838 227 976 C ATOM 2681 CG ASP A 366 -26.519 -22.265 16.570 1.00 61.59 C ANISOU 2681 CG ASP A 366 9238 6841 7322 -1103 518 -1042 C ATOM 2682 OD1 ASP A 366 -27.001 -23.088 17.380 1.00 64.54 O ANISOU 2682 OD1 ASP A 366 9379 7747 7397 660 168 638 O ATOM 2683 OD2 ASP A 366 -26.196 -22.566 15.400 1.00 58.99 O ANISOU 2683 OD2 ASP A 366 7572 7307 7534 320 1096 -74 O ATOM 2684 N VAL A 367 -24.921 -19.428 19.743 1.00 35.42 N ANISOU 2684 N VAL A 367 4582 5369 3506 -403 549 -218 N ATOM 2685 CA VAL A 367 -24.270 -18.201 20.217 1.00 40.02 C ANISOU 2685 CA VAL A 367 5185 5130 4889 -942 922 226 C ATOM 2686 C VAL A 367 -22.788 -18.228 19.967 1.00 39.00 C ANISOU 2686 C VAL A 367 4921 4699 5198 -499 294 167 C ATOM 2687 O VAL A 367 -22.115 -19.235 20.206 1.00 40.91 O ANISOU 2687 O VAL A 367 5676 4643 5226 -247 -15 161 O ATOM 2688 CB VAL A 367 -24.498 -17.898 21.714 1.00 38.23 C ANISOU 2688 CB VAL A 367 5221 4550 4753 -202 876 678 C ATOM 2689 CG1 VAL A 367 -25.904 -17.378 21.942 1.00 38.98 C ANISOU 2689 CG1 VAL A 367 5463 4398 4949 205 459 555 C ATOM 2690 CG2 VAL A 367 -24.212 -19.125 22.567 1.00 37.71 C ANISOU 2690 CG2 VAL A 367 5800 5600 2928 574 701 607 C ATOM 2691 N LYS A 368 -22.294 -17.092 19.501 1.00 36.78 N ANISOU 2691 N LYS A 368 5357 4922 3695 -497 634 130 N ATOM 2692 CA LYS A 368 -20.893 -16.928 19.193 1.00 36.67 C ANISOU 2692 CA LYS A 368 4622 4249 5059 -119 43 -170 C ATOM 2693 C LYS A 368 -20.136 -16.607 20.464 1.00 36.41 C ANISOU 2693 C LYS A 368 5018 4802 4011 253 451 838 C ATOM 2694 O LYS A 368 -20.425 -15.611 21.126 1.00 43.67 O ANISOU 2694 O LYS A 368 6010 5545 5037 276 1160 80 O ATOM 2695 CB LYS A 368 -20.744 -15.755 18.226 1.00 45.45 C ANISOU 2695 CB LYS A 368 7141 5453 4673 -437 44 376 C ATOM 2696 CG LYS A 368 -19.891 -16.049 17.016 1.00 46.49 C ANISOU 2696 CG LYS A 368 5889 4632 7142 656 1137 915 C ATOM 2697 CD LYS A 368 -18.419 -16.059 17.350 1.00 53.44 C ANISOU 2697 CD LYS A 368 6746 6904 6653 -551 -310 136 C ATOM 2698 CE LYS A 368 -17.635 -16.574 16.156 1.00 60.79 C ANISOU 2698 CE LYS A 368 7617 7126 8352 251 814 251 C ATOM 2699 NZ LYS A 368 -16.410 -15.755 15.972 1.00 61.10 N ANISOU 2699 NZ LYS A 368 7065 8789 7359 737 2371 1477 N ATOM 2700 N VAL A 369 -19.152 -17.428 20.805 1.00 33.88 N ANISOU 2700 N VAL A 369 4679 3840 4355 -74 717 424 N ATOM 2701 CA VAL A 369 -18.329 -17.156 21.974 1.00 38.00 C ANISOU 2701 CA VAL A 369 5310 4537 4590 453 106 147 C ATOM 2702 C VAL A 369 -16.852 -17.280 21.633 1.00 45.03 C ANISOU 2702 C VAL A 369 5840 5886 5383 0 645 376 C ATOM 2703 O VAL A 369 -16.366 -18.373 21.314 1.00 48.55 O ANISOU 2703 O VAL A 369 7136 5804 5506 -146 1142 71 O ATOM 2704 CB VAL A 369 -18.640 -18.113 23.136 1.00 37.57 C ANISOU 2704 CB VAL A 369 4689 5009 4576 -122 286 86 C ATOM 2705 CG1 VAL A 369 -17.832 -17.705 24.358 1.00 41.50 C ANISOU 2705 CG1 VAL A 369 5259 5603 4904 844 -415 96 C ATOM 2706 CG2 VAL A 369 -20.127 -18.119 23.451 1.00 31.27 C ANISOU 2706 CG2 VAL A 369 4348 3811 3722 663 -137 144 C ATOM 2707 N GLY A 370 -16.128 -16.169 21.726 1.00 49.41 N ANISOU 2707 N GLY A 370 6788 6289 5696 -499 261 -191 N ATOM 2708 CA GLY A 370 -14.749 -16.149 21.259 1.00 52.13 C ANISOU 2708 CA GLY A 370 6800 6661 6344 -90 226 120 C ATOM 2709 C GLY A 370 -14.780 -16.551 19.798 1.00 49.61 C ANISOU 2709 C GLY A 370 6413 6189 6246 -145 207 403 C ATOM 2710 O GLY A 370 -15.580 -16.021 19.020 1.00 45.28 O ANISOU 2710 O GLY A 370 6068 5385 5751 -750 175 -15 O ATOM 2711 N SER A 371 -13.952 -17.514 19.413 1.00 51.42 N ANISOU 2711 N SER A 371 6304 6807 6425 -321 627 -49 N ATOM 2712 CA SER A 371 -13.934 -17.905 18.010 1.00 51.37 C ANISOU 2712 CA SER A 371 6979 6179 6357 -404 1088 216 C ATOM 2713 C SER A 371 -14.884 -19.060 17.684 1.00 47.68 C ANISOU 2713 C SER A 371 6145 6056 5915 225 300 17 C ATOM 2714 O SER A 371 -14.824 -19.614 16.592 1.00 47.45 O ANISOU 2714 O SER A 371 6906 6045 5077 869 1071 1111 O ATOM 2715 CB SER A 371 -12.504 -18.189 17.537 1.00 55.15 C ANISOU 2715 CB SER A 371 6685 7404 6864 191 210 -228 C ATOM 2716 OG SER A 371 -11.981 -19.349 18.147 1.00 63.74 O ANISOU 2716 OG SER A 371 7467 7568 9182 -423 -898 1194 O ATOM 2717 N TYR A 372 -15.777 -19.410 18.613 1.00 44.09 N ANISOU 2717 N TYR A 372 6212 5007 5531 222 387 -259 N ATOM 2718 CA TYR A 372 -16.647 -20.568 18.409 1.00 37.39 C ANISOU 2718 CA TYR A 372 5007 4517 4682 458 1242 186 C ATOM 2719 C TYR A 372 -18.126 -20.251 18.350 1.00 35.03 C ANISOU 2719 C TYR A 372 5080 4119 4109 94 -146 608 C ATOM 2720 O TYR A 372 -18.568 -19.204 18.812 1.00 44.81 O ANISOU 2720 O TYR A 372 7351 4015 5660 -525 1165 -101 O ATOM 2721 CB TYR A 372 -16.407 -21.624 19.501 1.00 37.76 C ANISOU 2721 CB TYR A 372 4991 5268 4088 956 1246 171 C ATOM 2722 CG TYR A 372 -14.955 -21.958 19.701 1.00 40.82 C ANISOU 2722 CG TYR A 372 4762 5952 4792 155 146 -24 C ATOM 2723 CD1 TYR A 372 -14.296 -22.841 18.844 1.00 40.72 C ANISOU 2723 CD1 TYR A 372 5065 4705 5699 83 627 234 C ATOM 2724 CD2 TYR A 372 -14.232 -21.378 20.737 1.00 39.30 C ANISOU 2724 CD2 TYR A 372 5399 5088 4442 330 1373 -1335 C ATOM 2725 CE1 TYR A 372 -12.951 -23.144 19.022 1.00 33.85 C ANISOU 2725 CE1 TYR A 372 5006 3319 4532 220 564 143 C ATOM 2726 CE2 TYR A 372 -12.892 -21.668 20.928 1.00 45.73 C ANISOU 2726 CE2 TYR A 372 6325 5350 5699 967 398 284 C ATOM 2727 CZ TYR A 372 -12.257 -22.552 20.069 1.00 40.99 C ANISOU 2727 CZ TYR A 372 4945 5455 5171 119 115 -251 C ATOM 2728 OH TYR A 372 -10.933 -22.834 20.278 1.00 40.82 O ANISOU 2728 OH TYR A 372 5444 4593 5473 829 518 606 O ATOM 2729 N VAL A 373 -18.889 -21.179 17.778 1.00 33.26 N ANISOU 2729 N VAL A 373 4692 4021 3925 170 356 419 N ATOM 2730 CA VAL A 373 -20.338 -21.178 17.903 1.00 35.44 C ANISOU 2730 CA VAL A 373 4637 4640 4189 277 438 248 C ATOM 2731 C VAL A 373 -20.758 -22.232 18.937 1.00 40.40 C ANISOU 2731 C VAL A 373 6094 4486 4770 364 911 444 C ATOM 2732 O VAL A 373 -20.412 -23.411 18.808 1.00 37.55 O ANISOU 2732 O VAL A 373 5258 4555 4454 391 930 97 O ATOM 2733 CB VAL A 373 -21.033 -21.485 16.558 1.00 40.46 C ANISOU 2733 CB VAL A 373 5080 5399 4891 -480 116 -271 C ATOM 2734 CG1 VAL A 373 -22.526 -21.645 16.751 1.00 34.93 C ANISOU 2734 CG1 VAL A 373 4931 4591 3750 -154 952 759 C ATOM 2735 CG2 VAL A 373 -20.764 -20.378 15.546 1.00 52.62 C ANISOU 2735 CG2 VAL A 373 7672 6865 5455 -167 2056 1106 C ATOM 2736 N VAL A 374 -21.483 -21.799 19.968 1.00 36.70 N ANISOU 2736 N VAL A 374 5185 4335 4421 -80 195 195 N ATOM 2737 CA VAL A 374 -22.101 -22.725 20.915 1.00 36.32 C ANISOU 2737 CA VAL A 374 4641 4885 4274 -588 732 -445 C ATOM 2738 C VAL A 374 -23.531 -22.936 20.442 1.00 33.90 C ANISOU 2738 C VAL A 374 4620 4391 3869 -72 484 144 C ATOM 2739 O VAL A 374 -24.314 -21.993 20.390 1.00 40.00 O ANISOU 2739 O VAL A 374 4931 5265 5000 286 559 -588 O ATOM 2740 CB VAL A 374 -22.054 -22.216 22.373 1.00 33.69 C ANISOU 2740 CB VAL A 374 4702 4355 3743 -382 20 334 C ATOM 2741 CG1 VAL A 374 -22.666 -23.250 23.319 1.00 29.40 C ANISOU 2741 CG1 VAL A 374 4435 3617 3117 -72 -199 -11 C ATOM 2742 CG2 VAL A 374 -20.618 -21.898 22.769 1.00 33.51 C ANISOU 2742 CG2 VAL A 374 4297 4766 3670 -382 723 599 C ATOM 2743 N PRO A 375 -23.855 -24.182 20.065 1.00 33.30 N ANISOU 2743 N PRO A 375 4281 4465 3906 193 282 -202 N ATOM 2744 CA PRO A 375 -25.083 -24.585 19.400 1.00 33.49 C ANISOU 2744 CA PRO A 375 4961 4426 3337 -116 16 100 C ATOM 2745 C PRO A 375 -26.284 -24.684 20.309 1.00 32.46 C ANISOU 2745 C PRO A 375 4680 3514 4139 -129 4 -490 C ATOM 2746 O PRO A 375 -26.154 -25.078 21.462 1.00 38.55 O ANISOU 2746 O PRO A 375 6514 3765 4367 -347 451 -263 O ATOM 2747 CB PRO A 375 -24.743 -25.972 18.844 1.00 36.88 C ANISOU 2747 CB PRO A 375 4836 3856 5320 189 186 705 C ATOM 2748 CG PRO A 375 -23.672 -26.483 19.728 1.00 37.02 C ANISOU 2748 CG PRO A 375 5492 4507 4065 -570 -34 909 C ATOM 2749 CD PRO A 375 -22.898 -25.293 20.204 1.00 33.67 C ANISOU 2749 CD PRO A 375 5550 3470 3773 144 241 767 C ATOM 2750 N LYS A 376 -27.448 -24.344 19.771 1.00 33.70 N ANISOU 2750 N LYS A 376 4720 3595 4488 -280 -153 -346 N ATOM 2751 CA LYS A 376 -28.709 -24.585 20.442 1.00 42.41 C ANISOU 2751 CA LYS A 376 5760 5307 5047 -535 639 48 C ATOM 2752 C LYS A 376 -28.660 -25.983 21.050 1.00 45.88 C ANISOU 2752 C LYS A 376 6254 5303 5872 596 1010 240 C ATOM 2753 O LYS A 376 -28.085 -26.900 20.454 1.00 41.64 O ANISOU 2753 O LYS A 376 5532 5617 4670 -920 823 -929 O ATOM 2754 CB LYS A 376 -29.856 -24.478 19.435 1.00 46.21 C ANISOU 2754 CB LYS A 376 6316 5402 5840 193 150 -820 C ATOM 2755 CG LYS A 376 -31.246 -24.534 20.045 1.00 50.98 C ANISOU 2755 CG LYS A 376 6056 6377 6936 147 -72 568 C ATOM 2756 CD LYS A 376 -32.320 -24.430 18.976 1.00 52.19 C ANISOU 2756 CD LYS A 376 7132 6842 5854 -27 -114 188 C ATOM 2757 CE LYS A 376 -33.705 -24.378 19.606 1.00 54.35 C ANISOU 2757 CE LYS A 376 6383 5917 8350 -319 -513 -1063 C ATOM 2758 NZ LYS A 376 -34.702 -23.753 18.691 1.00 58.22 N ANISOU 2758 NZ LYS A 376 7797 8078 6246 -135 -832 -793 N ATOM 2759 N GLY A 377 -29.223 -26.136 22.247 1.00 41.10 N ANISOU 2759 N GLY A 377 5792 4973 4851 -83 137 -348 N ATOM 2760 CA GLY A 377 -29.315 -27.447 22.894 1.00 40.48 C ANISOU 2760 CA GLY A 377 5895 4599 4883 140 -180 -424 C ATOM 2761 C GLY A 377 -28.180 -27.744 23.853 1.00 39.11 C ANISOU 2761 C GLY A 377 4914 4797 5146 -86 312 -190 C ATOM 2762 O GLY A 377 -28.324 -28.562 24.770 1.00 40.03 O ANISOU 2762 O GLY A 377 5610 4127 5469 -1317 752 -570 O ATOM 2763 N ASP A 378 -27.034 -27.097 23.660 1.00 35.82 N ANISOU 2763 N ASP A 378 5384 3984 4242 -292 113 89 N ATOM 2764 CA ASP A 378 -25.981 -27.215 24.648 1.00 32.31 C ANISOU 2764 CA ASP A 378 4006 3760 4507 -20 278 -296 C ATOM 2765 C ASP A 378 -26.477 -26.689 25.986 1.00 31.16 C ANISOU 2765 C ASP A 378 4082 3720 4037 -231 -179 -52 C ATOM 2766 O ASP A 378 -27.427 -25.891 26.062 1.00 31.01 O ANISOU 2766 O ASP A 378 3785 3985 4011 -498 308 -477 O ATOM 2767 CB ASP A 378 -24.731 -26.431 24.237 1.00 34.37 C ANISOU 2767 CB ASP A 378 4851 4021 4186 -125 546 527 C ATOM 2768 CG ASP A 378 -23.736 -27.279 23.468 1.00 38.66 C ANISOU 2768 CG ASP A 378 5276 4830 4581 348 149 -232 C ATOM 2769 OD1 ASP A 378 -24.158 -28.289 22.865 1.00 38.76 O ANISOU 2769 OD1 ASP A 378 6344 4495 3885 -163 295 247 O ATOM 2770 OD2 ASP A 378 -22.533 -26.939 23.471 1.00 43.62 O ANISOU 2770 OD2 ASP A 378 5902 5347 5323 -239 813 237 O ATOM 2771 N ILE A 379 -25.844 -27.172 27.044 1.00 31.40 N ANISOU 2771 N ILE A 379 4449 3726 3754 -651 -81 115 N ATOM 2772 CA ILE A 379 -25.823 -26.424 28.278 1.00 33.62 C ANISOU 2772 CA ILE A 379 4692 4216 3865 -605 319 114 C ATOM 2773 C ILE A 379 -24.544 -25.606 28.212 1.00 33.24 C ANISOU 2773 C ILE A 379 4444 3888 4296 -301 -227 -74 C ATOM 2774 O ILE A 379 -23.460 -26.132 27.922 1.00 35.68 O ANISOU 2774 O ILE A 379 4799 3715 5043 -702 444 201 O ATOM 2775 CB ILE A 379 -25.854 -27.335 29.517 1.00 31.39 C ANISOU 2775 CB ILE A 379 4143 4170 3613 -288 -181 -45 C ATOM 2776 CG1 ILE A 379 -27.228 -28.023 29.615 1.00 33.99 C ANISOU 2776 CG1 ILE A 379 4213 4549 4151 -348 206 5 C ATOM 2777 CG2 ILE A 379 -25.578 -26.524 30.771 1.00 28.14 C ANISOU 2777 CG2 ILE A 379 4161 3157 3373 -102 -17 377 C ATOM 2778 CD1 ILE A 379 -27.284 -29.169 30.613 1.00 38.94 C ANISOU 2778 CD1 ILE A 379 5528 4393 4873 -577 401 310 C ATOM 2779 N ILE A 380 -24.680 -24.306 28.422 1.00 30.33 N ANISOU 2779 N ILE A 380 4098 3836 3589 -9 602 203 N ATOM 2780 CA ILE A 380 -23.509 -23.446 28.509 1.00 32.04 C ANISOU 2780 CA ILE A 380 4567 3928 3678 -247 -293 69 C ATOM 2781 C ILE A 380 -23.296 -23.099 29.974 1.00 24.93 C ANISOU 2781 C ILE A 380 3392 2483 3596 -103 -45 40 C ATOM 2782 O ILE A 380 -24.257 -22.916 30.713 1.00 30.98 O ANISOU 2782 O ILE A 380 4207 3536 4026 42 336 -90 O ATOM 2783 CB ILE A 380 -23.632 -22.200 27.592 1.00 30.64 C ANISOU 2783 CB ILE A 380 3953 3678 4011 -76 173 121 C ATOM 2784 CG1 ILE A 380 -22.294 -21.489 27.445 1.00 31.48 C ANISOU 2784 CG1 ILE A 380 4210 3777 3972 -43 968 378 C ATOM 2785 CG2 ILE A 380 -24.680 -21.222 28.090 1.00 28.95 C ANISOU 2785 CG2 ILE A 380 3475 3787 3736 -145 430 585 C ATOM 2786 CD1 ILE A 380 -22.317 -20.458 26.335 1.00 31.12 C ANISOU 2786 CD1 ILE A 380 3982 3914 3925 25 -153 444 C ATOM 2787 N ALA A 381 -22.036 -23.053 30.394 1.00 25.95 N ANISOU 2787 N ALA A 381 3424 3205 3228 476 -67 241 N ATOM 2788 CA ALA A 381 -21.694 -22.860 31.792 1.00 26.44 C ANISOU 2788 CA ALA A 381 3566 3279 3198 96 0 239 C ATOM 2789 C ALA A 381 -20.597 -21.857 31.898 1.00 31.02 C ANISOU 2789 C ALA A 381 4416 3460 3909 -395 377 -322 C ATOM 2790 O ALA A 381 -19.770 -21.699 30.984 1.00 30.01 O ANISOU 2790 O ALA A 381 4415 3294 3694 402 394 15 O ATOM 2791 CB ALA A 381 -21.208 -24.167 32.416 1.00 23.90 C ANISOU 2791 CB ALA A 381 3141 2891 3047 221 184 -333 C ATOM 2792 N CYS A 382 -20.558 -21.214 33.052 1.00 28.77 N ANISOU 2792 N CYS A 382 3798 3364 3765 178 264 -206 N ATOM 2793 CA CYS A 382 -19.455 -20.356 33.389 1.00 29.22 C ANISOU 2793 CA CYS A 382 3791 3560 3751 113 32 56 C ATOM 2794 C CYS A 382 -19.162 -20.693 34.826 1.00 27.05 C ANISOU 2794 C CYS A 382 3430 3365 3482 -200 130 -50 C ATOM 2795 O CYS A 382 -20.062 -20.685 35.657 1.00 29.18 O ANISOU 2795 O CYS A 382 3854 3406 3825 60 546 -63 O ATOM 2796 CB CYS A 382 -19.843 -18.889 33.230 1.00 28.79 C ANISOU 2796 CB CYS A 382 3476 3374 4089 81 468 27 C ATOM 2797 SG CYS A 382 -18.403 -17.813 33.302 1.00 31.77 S ANISOU 2797 SG CYS A 382 3965 3930 4176 -144 825 -286 S ATOM 2798 N SER A 383 -17.910 -21.022 35.109 1.00 26.31 N ANISOU 2798 N SER A 383 3510 3010 3476 -221 210 157 N ATOM 2799 CA SER A 383 -17.536 -21.544 36.407 1.00 28.55 C ANISOU 2799 CA SER A 383 3536 3805 3507 -145 -156 200 C ATOM 2800 C SER A 383 -16.758 -20.567 37.287 1.00 28.04 C ANISOU 2800 C SER A 383 3675 3242 3736 -51 421 -222 C ATOM 2801 O SER A 383 -15.574 -20.276 37.035 1.00 27.81 O ANISOU 2801 O SER A 383 3697 3261 3606 140 494 -296 O ATOM 2802 CB SER A 383 -16.745 -22.843 36.227 1.00 30.55 C ANISOU 2802 CB SER A 383 3865 4009 3731 133 -112 70 C ATOM 2803 OG SER A 383 -16.091 -23.210 37.428 1.00 28.03 O ANISOU 2803 OG SER A 383 3541 3500 3609 443 228 -5 O ATOM 2804 N PRO A 384 -17.405 -20.068 38.352 1.00 27.10 N ANISOU 2804 N PRO A 384 3366 3307 3624 -81 407 -223 N ATOM 2805 CA PRO A 384 -16.625 -19.214 39.241 1.00 24.33 C ANISOU 2805 CA PRO A 384 3022 3209 3012 11 168 228 C ATOM 2806 C PRO A 384 -15.385 -19.910 39.800 1.00 27.47 C ANISOU 2806 C PRO A 384 3307 3165 3964 330 -18 -133 C ATOM 2807 O PRO A 384 -14.364 -19.253 40.048 1.00 26.27 O ANISOU 2807 O PRO A 384 3177 3198 3604 318 253 -243 O ATOM 2808 CB PRO A 384 -17.622 -18.853 40.353 1.00 24.73 C ANISOU 2808 CB PRO A 384 3305 3292 2797 -24 181 161 C ATOM 2809 CG PRO A 384 -18.956 -18.902 39.665 1.00 26.14 C ANISOU 2809 CG PRO A 384 2917 3736 3279 -157 567 180 C ATOM 2810 CD PRO A 384 -18.844 -20.067 38.699 1.00 29.12 C ANISOU 2810 CD PRO A 384 3563 3641 3858 -110 549 60 C ATOM 2811 N LEU A 385 -15.438 -21.222 39.991 1.00 24.82 N ANISOU 2811 N LEU A 385 3095 3143 3192 86 560 231 N ATOM 2812 CA LEU A 385 -14.241 -21.903 40.490 1.00 27.46 C ANISOU 2812 CA LEU A 385 3213 3355 3864 218 378 241 C ATOM 2813 C LEU A 385 -13.075 -21.800 39.480 1.00 26.11 C ANISOU 2813 C LEU A 385 3482 3104 3332 194 122 442 C ATOM 2814 O LEU A 385 -11.934 -21.462 39.838 1.00 29.72 O ANISOU 2814 O LEU A 385 3260 3620 4411 246 1046 -180 O ATOM 2815 CB LEU A 385 -14.550 -23.364 40.791 1.00 26.47 C ANISOU 2815 CB LEU A 385 3510 3531 3016 32 783 721 C ATOM 2816 CG LEU A 385 -13.373 -24.171 41.320 1.00 29.32 C ANISOU 2816 CG LEU A 385 3555 3757 3828 70 -86 -87 C ATOM 2817 CD1 LEU A 385 -12.968 -23.694 42.707 1.00 25.01 C ANISOU 2817 CD1 LEU A 385 2579 3482 3442 -176 205 243 C ATOM 2818 CD2 LEU A 385 -13.763 -25.640 41.332 1.00 32.18 C ANISOU 2818 CD2 LEU A 385 4321 3453 4453 270 294 303 C ATOM 2819 N LEU A 386 -13.378 -22.090 38.222 1.00 28.05 N ANISOU 2819 N LEU A 386 3810 3379 3468 238 198 -119 N ATOM 2820 CA LEU A 386 -12.397 -21.979 37.142 1.00 32.50 C ANISOU 2820 CA LEU A 386 4362 4040 3947 -158 592 -8 C ATOM 2821 C LEU A 386 -11.904 -20.545 36.941 1.00 31.20 C ANISOU 2821 C LEU A 386 3849 3946 4060 7 78 118 C ATOM 2822 O LEU A 386 -10.706 -20.274 37.028 1.00 29.68 O ANISOU 2822 O LEU A 386 3387 3714 4174 434 708 -4 O ATOM 2823 CB LEU A 386 -12.976 -22.521 35.840 1.00 31.13 C ANISOU 2823 CB LEU A 386 3821 4039 3966 -191 334 156 C ATOM 2824 CG LEU A 386 -11.972 -22.662 34.688 1.00 31.04 C ANISOU 2824 CG LEU A 386 3946 4192 3655 131 20 -348 C ATOM 2825 CD1 LEU A 386 -10.760 -23.516 35.062 1.00 29.06 C ANISOU 2825 CD1 LEU A 386 3995 3686 3358 -48 161 -332 C ATOM 2826 CD2 LEU A 386 -12.698 -23.245 33.494 1.00 27.89 C ANISOU 2826 CD2 LEU A 386 3823 3575 3197 -378 349 189 C ATOM 2827 N SER A 387 -12.830 -19.629 36.684 1.00 29.85 N ANISOU 2827 N SER A 387 3786 3941 3614 142 803 340 N ATOM 2828 CA SER A 387 -12.464 -18.232 36.444 1.00 26.77 C ANISOU 2828 CA SER A 387 3112 3571 3488 244 264 -153 C ATOM 2829 C SER A 387 -11.669 -17.574 37.578 1.00 27.33 C ANISOU 2829 C SER A 387 3704 3179 3501 202 517 -561 C ATOM 2830 O SER A 387 -10.746 -16.802 37.306 1.00 30.17 O ANISOU 2830 O SER A 387 3864 3769 3826 -19 729 -359 O ATOM 2831 CB SER A 387 -13.690 -17.417 36.066 1.00 26.34 C ANISOU 2831 CB SER A 387 3218 3374 3414 102 210 258 C ATOM 2832 OG SER A 387 -14.266 -17.956 34.888 1.00 26.65 O ANISOU 2832 OG SER A 387 3028 3335 3762 -297 382 292 O ATOM 2833 N HIS A 388 -11.995 -17.902 38.830 1.00 25.14 N ANISOU 2833 N HIS A 388 2859 3434 3256 767 22 85 N ATOM 2834 CA HIS A 388 -11.346 -17.285 39.992 1.00 27.11 C ANISOU 2834 CA HIS A 388 3168 3666 3467 341 345 -247 C ATOM 2835 C HIS A 388 -9.973 -17.842 40.239 1.00 24.56 C ANISOU 2835 C HIS A 388 2791 3494 3045 -285 632 223 C ATOM 2836 O HIS A 388 -9.278 -17.392 41.142 1.00 26.43 O ANISOU 2836 O HIS A 388 2665 3771 3604 185 484 88 O ATOM 2837 CB HIS A 388 -12.180 -17.461 41.274 1.00 29.30 C ANISOU 2837 CB HIS A 388 3086 3811 4236 -184 719 260 C ATOM 2838 CG HIS A 388 -13.506 -16.736 41.256 1.00 29.99 C ANISOU 2838 CG HIS A 388 3675 3872 3847 406 463 39 C ATOM 2839 ND1 HIS A 388 -14.411 -16.863 42.249 1.00 29.92 N ANISOU 2839 ND1 HIS A 388 3546 4020 3803 -17 336 -37 N ATOM 2840 CD2 HIS A 388 -14.076 -15.879 40.309 1.00 29.23 C ANISOU 2840 CD2 HIS A 388 3704 3644 3758 102 263 -62 C ATOM 2841 CE1 HIS A 388 -15.497 -16.105 41.963 1.00 29.10 C ANISOU 2841 CE1 HIS A 388 3457 3909 3690 -200 414 394 C ATOM 2842 NE2 HIS A 388 -15.292 -15.507 40.777 1.00 27.47 N ANISOU 2842 NE2 HIS A 388 3392 3539 3506 -434 279 59 N ATOM 2843 N HIS A 389 -9.589 -18.833 39.440 1.00 28.59 N ANISOU 2843 N HIS A 389 3512 3111 4237 51 976 226 N ATOM 2844 CA HIS A 389 -8.262 -19.440 39.511 1.00 31.57 C ANISOU 2844 CA HIS A 389 3825 4074 4094 350 37 442 C ATOM 2845 C HIS A 389 -7.461 -19.247 38.247 1.00 35.93 C ANISOU 2845 C HIS A 389 4287 4779 4584 -89 415 788 C ATOM 2846 O HIS A 389 -6.351 -19.777 38.115 1.00 37.04 O ANISOU 2846 O HIS A 389 4754 4715 4603 14 1118 344 O ATOM 2847 CB HIS A 389 -8.374 -20.915 39.892 1.00 29.82 C ANISOU 2847 CB HIS A 389 3467 3891 3972 -94 75 221 C ATOM 2848 CG HIS A 389 -8.756 -21.113 41.330 1.00 31.36 C ANISOU 2848 CG HIS A 389 4081 3860 3971 -438 73 -100 C ATOM 2849 ND1 HIS A 389 -10.032 -21.063 41.748 1.00 33.81 N ANISOU 2849 ND1 HIS A 389 4408 3912 4526 877 702 1259 N ATOM 2850 CD2 HIS A 389 -7.971 -21.278 42.471 1.00 31.13 C ANISOU 2850 CD2 HIS A 389 4034 3470 4322 655 272 918 C ATOM 2851 CE1 HIS A 389 -10.069 -21.209 43.083 1.00 32.76 C ANISOU 2851 CE1 HIS A 389 4233 4335 3880 -118 67 -171 C ATOM 2852 NE2 HIS A 389 -8.809 -21.350 43.523 1.00 34.66 N ANISOU 2852 NE2 HIS A 389 4368 4637 4164 576 371 -123 N ATOM 2853 N ASP A 390 -8.018 -18.485 37.309 1.00 34.42 N ANISOU 2853 N ASP A 390 3730 4709 4637 -108 107 361 N ATOM 2854 CA ASP A 390 -7.265 -18.007 36.157 1.00 36.08 C ANISOU 2854 CA ASP A 390 4861 4946 3901 -93 36 -60 C ATOM 2855 C ASP A 390 -6.079 -17.177 36.647 1.00 36.69 C ANISOU 2855 C ASP A 390 4761 4422 4756 -330 542 -21 C ATOM 2856 O ASP A 390 -6.256 -16.210 37.381 1.00 33.32 O ANISOU 2856 O ASP A 390 3724 4435 4501 -238 1204 53 O ATOM 2857 CB ASP A 390 -8.157 -17.159 35.255 1.00 40.03 C ANISOU 2857 CB ASP A 390 5364 5139 4705 672 522 469 C ATOM 2858 CG ASP A 390 -7.454 -16.740 33.984 1.00 42.91 C ANISOU 2858 CG ASP A 390 5310 5815 5178 -612 946 -283 C ATOM 2859 OD1 ASP A 390 -6.688 -15.755 34.031 1.00 40.95 O ANISOU 2859 OD1 ASP A 390 5330 5357 4869 -255 1955 33 O ATOM 2860 OD2 ASP A 390 -7.663 -17.404 32.944 1.00 39.57 O ANISOU 2860 OD2 ASP A 390 5020 5743 4271 126 1237 144 O ATOM 2861 N GLU A 391 -4.868 -17.544 36.246 1.00 39.19 N ANISOU 2861 N GLU A 391 5058 4631 5199 289 120 78 N ATOM 2862 CA GLU A 391 -3.689 -16.912 36.845 1.00 37.21 C ANISOU 2862 CA GLU A 391 4548 4375 5213 237 640 -81 C ATOM 2863 C GLU A 391 -3.354 -15.514 36.321 1.00 32.99 C ANISOU 2863 C GLU A 391 3497 4980 4054 -257 446 -49 C ATOM 2864 O GLU A 391 -2.661 -14.746 36.988 1.00 35.01 O ANISOU 2864 O GLU A 391 3395 4659 5245 -713 651 -115 O ATOM 2865 CB GLU A 391 -2.500 -17.857 36.826 1.00 41.90 C ANISOU 2865 CB GLU A 391 4520 5557 5843 642 208 41 C ATOM 2866 CG GLU A 391 -2.560 -18.838 37.984 1.00 50.55 C ANISOU 2866 CG GLU A 391 6395 5920 6891 -234 1784 655 C ATOM 2867 CD GLU A 391 -1.564 -19.970 37.861 1.00 59.48 C ANISOU 2867 CD GLU A 391 7558 7193 7847 1157 284 801 C ATOM 2868 OE1 GLU A 391 -1.094 -20.244 36.736 1.00 65.29 O ANISOU 2868 OE1 GLU A 391 9095 6719 8991 1855 826 -15 O ATOM 2869 OE2 GLU A 391 -1.262 -20.594 38.894 1.00 58.14 O ANISOU 2869 OE2 GLU A 391 6418 8374 7299 2629 341 181 O ATOM 2870 N GLU A 392 -3.899 -15.162 35.164 1.00 32.74 N ANISOU 2870 N GLU A 392 4003 4375 4059 899 984 370 N ATOM 2871 CA GLU A 392 -3.809 -13.789 34.683 1.00 33.67 C ANISOU 2871 CA GLU A 392 3781 4173 4839 -175 604 88 C ATOM 2872 C GLU A 392 -4.744 -12.885 35.500 1.00 36.19 C ANISOU 2872 C GLU A 392 4465 4488 4798 -318 544 -580 C ATOM 2873 O GLU A 392 -4.336 -11.813 35.945 1.00 32.75 O ANISOU 2873 O GLU A 392 3223 4498 4721 -585 979 -36 O ATOM 2874 CB GLU A 392 -4.157 -13.710 33.193 1.00 39.42 C ANISOU 2874 CB GLU A 392 4901 5537 4538 -41 1352 316 C ATOM 2875 CG GLU A 392 -3.985 -12.311 32.617 1.00 44.74 C ANISOU 2875 CG GLU A 392 5922 5319 5755 210 694 311 C ATOM 2876 CD GLU A 392 -4.832 -12.052 31.387 1.00 49.15 C ANISOU 2876 CD GLU A 392 6312 6365 5997 152 235 -305 C ATOM 2877 OE1 GLU A 392 -4.845 -10.894 30.931 1.00 55.25 O ANISOU 2877 OE1 GLU A 392 7137 6943 6911 -632 -248 281 O ATOM 2878 OE2 GLU A 392 -5.486 -12.989 30.878 1.00 54.97 O ANISOU 2878 OE2 GLU A 392 5859 7557 7468 -1461 1768 -593 O ATOM 2879 N ALA A 393 -5.989 -13.330 35.699 1.00 35.95 N ANISOU 2879 N ALA A 393 4147 4452 5058 -89 444 -195 N ATOM 2880 CA ALA A 393 -6.974 -12.607 36.520 1.00 34.20 C ANISOU 2880 CA ALA A 393 3849 4508 4636 -189 256 34 C ATOM 2881 C ALA A 393 -6.588 -12.512 38.001 1.00 30.76 C ANISOU 2881 C ALA A 393 2755 4200 4733 -768 938 205 C ATOM 2882 O ALA A 393 -6.702 -11.441 38.615 1.00 33.14 O ANISOU 2882 O ALA A 393 3342 4341 4908 -1102 892 -144 O ATOM 2883 CB ALA A 393 -8.357 -13.251 36.384 1.00 35.33 C ANISOU 2883 CB ALA A 393 3766 4795 4862 -307 705 677 C ATOM 2884 N PHE A 394 -6.151 -13.636 38.570 1.00 31.91 N ANISOU 2884 N PHE A 394 3262 4356 4504 -316 958 345 N ATOM 2885 CA PHE A 394 -5.913 -13.749 40.003 1.00 32.12 C ANISOU 2885 CA PHE A 394 3961 3866 4375 -165 220 -17 C ATOM 2886 C PHE A 394 -4.577 -14.447 40.265 1.00 36.38 C ANISOU 2886 C PHE A 394 4005 4629 5188 43 374 -175 C ATOM 2887 O PHE A 394 -4.536 -15.661 40.519 1.00 34.61 O ANISOU 2887 O PHE A 394 3836 4737 4575 -145 1001 306 O ATOM 2888 CB PHE A 394 -7.080 -14.511 40.687 1.00 31.34 C ANISOU 2888 CB PHE A 394 3667 3840 4401 413 625 -79 C ATOM 2889 CG PHE A 394 -8.427 -13.835 40.529 1.00 27.88 C ANISOU 2889 CG PHE A 394 3189 3350 4052 -287 266 399 C ATOM 2890 CD1 PHE A 394 -8.739 -12.706 41.272 1.00 26.56 C ANISOU 2890 CD1 PHE A 394 2809 4159 3121 -264 1126 244 C ATOM 2891 CD2 PHE A 394 -9.373 -14.315 39.628 1.00 32.79 C ANISOU 2891 CD2 PHE A 394 3938 4139 4382 -195 -235 257 C ATOM 2892 CE1 PHE A 394 -9.966 -12.067 41.128 1.00 26.82 C ANISOU 2892 CE1 PHE A 394 4051 3122 3017 176 -489 697 C ATOM 2893 CE2 PHE A 394 -10.615 -13.679 39.478 1.00 28.48 C ANISOU 2893 CE2 PHE A 394 3526 3078 4213 -527 594 285 C ATOM 2894 CZ PHE A 394 -10.914 -12.561 40.244 1.00 24.39 C ANISOU 2894 CZ PHE A 394 2536 3207 3524 58 129 560 C ATOM 2895 N PRO A 395 -3.467 -13.692 40.200 1.00 40.22 N ANISOU 2895 N PRO A 395 4621 5131 5527 -517 657 378 N ATOM 2896 CA PRO A 395 -2.168 -14.329 40.459 1.00 41.84 C ANISOU 2896 CA PRO A 395 5220 5284 5393 -250 -72 207 C ATOM 2897 C PRO A 395 -2.129 -15.011 41.827 1.00 39.60 C ANISOU 2897 C PRO A 395 5062 4685 5298 76 246 -3 C ATOM 2898 O PRO A 395 -2.643 -14.461 42.812 1.00 35.87 O ANISOU 2898 O PRO A 395 3966 4323 5339 -590 523 84 O ATOM 2899 CB PRO A 395 -1.178 -13.152 40.398 1.00 39.78 C ANISOU 2899 CB PRO A 395 3992 5494 5627 41 -590 -40 C ATOM 2900 CG PRO A 395 -1.835 -12.169 39.489 1.00 39.77 C ANISOU 2900 CG PRO A 395 4465 5257 5388 -211 703 951 C ATOM 2901 CD PRO A 395 -3.316 -12.284 39.791 1.00 38.56 C ANISOU 2901 CD PRO A 395 4596 4785 5267 261 985 53 C ATOM 2902 N GLU A 396 -1.536 -16.203 41.882 1.00 34.56 N ANISOU 2902 N GLU A 396 3380 4944 4804 23 1300 -26 N ATOM 2903 CA GLU A 396 -1.453 -16.966 43.123 1.00 38.44 C ANISOU 2903 CA GLU A 396 4199 5342 5063 -684 624 343 C ATOM 2904 C GLU A 396 -2.856 -17.143 43.712 1.00 36.14 C ANISOU 2904 C GLU A 396 3914 5275 4542 348 378 -471 C ATOM 2905 O GLU A 396 -3.122 -16.727 44.832 1.00 35.24 O ANISOU 2905 O GLU A 396 3158 5356 4874 748 1067 -198 O ATOM 2906 CB GLU A 396 -0.545 -16.263 44.124 1.00 36.92 C ANISOU 2906 CB GLU A 396 3894 5052 5079 -392 1029 18 C ATOM 2907 CG GLU A 396 0.070 -17.192 45.161 1.00 55.15 C ANISOU 2907 CG GLU A 396 7021 8547 5385 465 45 1250 C ATOM 2908 CD GLU A 396 1.111 -16.495 46.016 1.00 68.14 C ANISOU 2908 CD GLU A 396 8245 8451 9194 -1706 -483 1306 C ATOM 2909 OE1 GLU A 396 1.634 -15.448 45.581 1.00 66.28 O ANISOU 2909 OE1 GLU A 396 7390 7855 9935 -399 1524 743 O ATOM 2910 OE2 GLU A 396 1.409 -16.994 47.123 1.00 71.35 O ANISOU 2910 OE2 GLU A 396 5687 12014 9405 2101 -32 975 O ATOM 2911 N PRO A 397 -3.753 -17.770 42.945 1.00 35.18 N ANISOU 2911 N PRO A 397 3942 4798 4626 109 282 -137 N ATOM 2912 CA PRO A 397 -5.175 -17.835 43.285 1.00 35.78 C ANISOU 2912 CA PRO A 397 4274 4962 4357 8 586 -230 C ATOM 2913 C PRO A 397 -5.527 -18.598 44.576 1.00 34.21 C ANISOU 2913 C PRO A 397 4281 3589 5127 253 533 276 C ATOM 2914 O PRO A 397 -6.582 -18.323 45.141 1.00 32.35 O ANISOU 2914 O PRO A 397 3995 3717 4578 362 -128 182 O ATOM 2915 CB PRO A 397 -5.800 -18.489 42.054 1.00 35.23 C ANISOU 2915 CB PRO A 397 3619 4612 5151 -287 67 -139 C ATOM 2916 CG PRO A 397 -4.686 -19.264 41.429 1.00 34.99 C ANISOU 2916 CG PRO A 397 4038 5095 4162 -284 213 -169 C ATOM 2917 CD PRO A 397 -3.468 -18.419 41.655 1.00 33.99 C ANISOU 2917 CD PRO A 397 3729 4928 4257 -28 245 -44 C ATOM 2918 N ARG A 398 -4.673 -19.518 45.048 1.00 28.89 N ANISOU 2918 N ARG A 398 2976 4316 3684 127 299 -80 N ATOM 2919 CA ARG A 398 -4.939 -20.207 46.321 1.00 28.57 C ANISOU 2919 CA ARG A 398 3164 3563 4127 14 198 61 C ATOM 2920 C ARG A 398 -4.570 -19.360 47.528 1.00 30.20 C ANISOU 2920 C ARG A 398 3708 3762 4005 290 410 121 C ATOM 2921 O ARG A 398 -4.906 -19.712 48.650 1.00 29.79 O ANISOU 2921 O ARG A 398 3655 4088 3575 654 262 138 O ATOM 2922 CB ARG A 398 -4.257 -21.593 46.443 1.00 31.75 C ANISOU 2922 CB ARG A 398 3884 3885 4292 387 -395 202 C ATOM 2923 CG ARG A 398 -4.870 -22.746 45.624 1.00 31.85 C ANISOU 2923 CG ARG A 398 3687 3629 4784 234 -106 181 C ATOM 2924 CD ARG A 398 -6.400 -22.693 45.512 1.00 32.04 C ANISOU 2924 CD ARG A 398 3690 3968 4513 67 -131 961 C ATOM 2925 NE ARG A 398 -7.100 -23.124 46.726 1.00 31.95 N ANISOU 2925 NE ARG A 398 3797 4053 4288 -73 118 122 N ATOM 2926 CZ ARG A 398 -8.393 -22.907 46.977 1.00 35.69 C ANISOU 2926 CZ ARG A 398 4294 5502 3762 835 343 278 C ATOM 2927 NH1 ARG A 398 -9.147 -22.222 46.115 1.00 30.13 N ANISOU 2927 NH1 ARG A 398 3630 3693 4122 -85 266 49 N ATOM 2928 NH2 ARG A 398 -8.932 -23.371 48.105 1.00 31.01 N ANISOU 2928 NH2 ARG A 398 3519 4156 4105 -151 -110 223 N ATOM 2929 N ARG A 399 -3.864 -18.256 47.311 1.00 29.31 N ANISOU 2929 N ARG A 399 3302 3365 4467 516 248 -338 N ATOM 2930 CA ARG A 399 -3.575 -17.362 48.416 1.00 32.35 C ANISOU 2930 CA ARG A 399 4010 4469 3810 199 120 -257 C ATOM 2931 C ARG A 399 -4.759 -16.434 48.660 1.00 31.14 C ANISOU 2931 C ARG A 399 3419 4279 4131 -229 13 145 C ATOM 2932 O ARG A 399 -5.195 -15.692 47.762 1.00 30.04 O ANISOU 2932 O ARG A 399 2515 4399 4499 -76 252 109 O ATOM 2933 CB ARG A 399 -2.303 -16.546 48.171 1.00 37.90 C ANISOU 2933 CB ARG A 399 3818 5229 5351 -62 -326 102 C ATOM 2934 CG ARG A 399 -2.080 -15.448 49.204 1.00 45.74 C ANISOU 2934 CG ARG A 399 4915 5712 6753 348 568 -1137 C ATOM 2935 CD ARG A 399 -0.642 -14.936 49.210 1.00 62.73 C ANISOU 2935 CD ARG A 399 6336 8720 8777 -1771 -898 -996 C ATOM 2936 NE ARG A 399 0.263 -15.885 49.857 1.00 74.73 N ANISOU 2936 NE ARG A 399 7407 8983 12003 1059 376 -1443 N ATOM 2937 CZ ARG A 399 1.320 -15.544 50.592 1.00 89.20 C ANISOU 2937 CZ ARG A 399 7920 11459 14509 1026 -851 -940 C ATOM 2938 NH1 ARG A 399 1.619 -14.266 50.792 1.00 97.92 N ANISOU 2938 NH1 ARG A 399 6562 12614 18026 -1644 -3223 394 N ATOM 2939 NH2 ARG A 399 2.075 -16.486 51.140 1.00 92.30 N ANISOU 2939 NH2 ARG A 399 9802 10774 14493 1066 -328 1356 N ATOM 2940 N TRP A 400 -5.274 -16.480 49.882 1.00 32.42 N ANISOU 2940 N TRP A 400 3853 4346 4116 -5 137 -319 N ATOM 2941 CA TRP A 400 -6.324 -15.579 50.297 1.00 33.07 C ANISOU 2941 CA TRP A 400 4268 4040 4254 -8 674 -56 C ATOM 2942 C TRP A 400 -5.696 -14.246 50.568 1.00 32.23 C ANISOU 2942 C TRP A 400 4143 4070 4032 -14 -3 85 C ATOM 2943 O TRP A 400 -4.876 -14.125 51.480 1.00 30.62 O ANISOU 2943 O TRP A 400 3308 4063 4260 -665 477 8 O ATOM 2944 CB TRP A 400 -6.951 -16.111 51.562 1.00 29.60 C ANISOU 2944 CB TRP A 400 3378 3831 4037 372 -43 446 C ATOM 2945 CG TRP A 400 -8.159 -15.347 52.027 1.00 28.92 C ANISOU 2945 CG TRP A 400 3580 4099 3307 166 187 -103 C ATOM 2946 CD1 TRP A 400 -9.452 -15.423 51.524 1.00 26.73 C ANISOU 2946 CD1 TRP A 400 3228 3245 3683 -3 304 239 C ATOM 2947 CD2 TRP A 400 -8.233 -14.379 53.127 1.00 27.54 C ANISOU 2947 CD2 TRP A 400 3239 3672 3553 -13 323 -63 C ATOM 2948 NE1 TRP A 400 -10.302 -14.595 52.224 1.00 24.69 N ANISOU 2948 NE1 TRP A 400 3369 2888 3121 -323 228 151 N ATOM 2949 CE2 TRP A 400 -9.638 -13.943 53.196 1.00 26.62 C ANISOU 2949 CE2 TRP A 400 3427 3326 3362 274 -318 -24 C ATOM 2950 CE3 TRP A 400 -7.320 -13.860 54.036 1.00 29.36 C ANISOU 2950 CE3 TRP A 400 2716 4514 3925 68 335 -259 C ATOM 2951 CZ2 TRP A 400 -10.074 -13.014 54.132 1.00 28.33 C ANISOU 2951 CZ2 TRP A 400 3049 3960 3755 364 329 -99 C ATOM 2952 CZ3 TRP A 400 -7.776 -12.933 54.984 1.00 29.73 C ANISOU 2952 CZ3 TRP A 400 3793 2716 4787 283 -282 -95 C ATOM 2953 CH2 TRP A 400 -9.121 -12.520 55.026 1.00 31.67 C ANISOU 2953 CH2 TRP A 400 3634 3887 4511 -72 361 -812 C ATOM 2954 N ASP A 401 -6.067 -13.242 49.779 1.00 29.53 N ANISOU 2954 N ASP A 401 3147 3706 4368 -517 824 513 N ATOM 2955 CA ASP A 401 -5.551 -11.878 49.961 1.00 30.81 C ANISOU 2955 CA ASP A 401 3624 3595 4486 72 296 -404 C ATOM 2956 C ASP A 401 -6.648 -10.830 49.760 1.00 25.86 C ANISOU 2956 C ASP A 401 3050 3557 3216 -408 105 296 C ATOM 2957 O ASP A 401 -6.973 -10.475 48.638 1.00 21.65 O ANISOU 2957 O ASP A 401 2095 2966 3165 -440 255 137 O ATOM 2958 CB ASP A 401 -4.383 -11.611 48.997 1.00 29.05 C ANISOU 2958 CB ASP A 401 3585 3546 3905 -243 -130 -253 C ATOM 2959 CG ASP A 401 -3.897 -10.178 49.055 1.00 37.02 C ANISOU 2959 CG ASP A 401 4828 4187 5048 -1243 307 -285 C ATOM 2960 OD1 ASP A 401 -4.342 -9.415 49.950 1.00 38.47 O ANISOU 2960 OD1 ASP A 401 4400 4707 5506 -520 426 -299 O ATOM 2961 OD2 ASP A 401 -3.068 -9.819 48.201 1.00 41.05 O ANISOU 2961 OD2 ASP A 401 5450 5428 4717 -704 764 -496 O ATOM 2962 N PRO A 402 -7.230 -10.330 50.855 1.00 29.00 N ANISOU 2962 N PRO A 402 3491 3783 3742 17 15 -328 N ATOM 2963 CA PRO A 402 -8.354 -9.411 50.683 1.00 30.15 C ANISOU 2963 CA PRO A 402 3732 3658 4065 170 146 -28 C ATOM 2964 C PRO A 402 -7.965 -8.117 49.966 1.00 33.85 C ANISOU 2964 C PRO A 402 3942 4660 4258 -159 201 695 C ATOM 2965 O PRO A 402 -8.832 -7.415 49.451 1.00 32.88 O ANISOU 2965 O PRO A 402 2913 4567 5012 -268 395 446 O ATOM 2966 CB PRO A 402 -8.810 -9.122 52.118 1.00 29.91 C ANISOU 2966 CB PRO A 402 3470 3880 4014 -8 457 69 C ATOM 2967 CG PRO A 402 -7.736 -9.649 53.014 1.00 35.68 C ANISOU 2967 CG PRO A 402 4383 4566 4605 586 -103 134 C ATOM 2968 CD PRO A 402 -7.021 -10.722 52.256 1.00 31.17 C ANISOU 2968 CD PRO A 402 3873 3691 4278 -405 335 597 C ATOM 2969 N GLU A 403 -6.669 -7.812 49.917 1.00 33.77 N ANISOU 2969 N GLU A 403 3899 4487 4444 -226 -317 -164 N ATOM 2970 CA GLU A 403 -6.220 -6.590 49.259 1.00 33.41 C ANISOU 2970 CA GLU A 403 3914 4178 4600 348 -156 -155 C ATOM 2971 C GLU A 403 -6.151 -6.706 47.735 1.00 32.19 C ANISOU 2971 C GLU A 403 3617 4115 4496 284 191 -168 C ATOM 2972 O GLU A 403 -6.043 -5.691 47.051 1.00 34.37 O ANISOU 2972 O GLU A 403 3651 4064 5342 -247 -218 253 O ATOM 2973 CB GLU A 403 -4.878 -6.093 49.835 1.00 34.76 C ANISOU 2973 CB GLU A 403 4356 3862 4989 -694 186 -254 C ATOM 2974 CG GLU A 403 -4.873 -5.849 51.342 1.00 39.13 C ANISOU 2974 CG GLU A 403 5391 4935 4538 -699 -893 544 C ATOM 2975 CD GLU A 403 -5.570 -4.561 51.778 1.00 55.68 C ANISOU 2975 CD GLU A 403 7161 6415 7577 833 18 336 C ATOM 2976 OE1 GLU A 403 -6.306 -3.948 50.974 1.00 54.70 O ANISOU 2976 OE1 GLU A 403 7756 6463 6562 371 -435 -447 O ATOM 2977 OE2 GLU A 403 -5.385 -4.154 52.950 1.00 67.69 O ANISOU 2977 OE2 GLU A 403 9399 7472 8847 -1404 -198 -718 O ATOM 2978 N ARG A 404 -6.226 -7.921 47.189 1.00 32.31 N ANISOU 2978 N ARG A 404 3862 4094 4317 -368 522 -209 N ATOM 2979 CA ARG A 404 -6.101 -8.077 45.729 1.00 29.85 C ANISOU 2979 CA ARG A 404 3810 3686 3842 -277 69 317 C ATOM 2980 C ARG A 404 -7.290 -7.444 45.043 1.00 32.19 C ANISOU 2980 C ARG A 404 3702 4153 4375 47 97 102 C ATOM 2981 O ARG A 404 -8.329 -7.230 45.674 1.00 32.16 O ANISOU 2981 O ARG A 404 4131 3554 4533 -392 682 -214 O ATOM 2982 CB ARG A 404 -6.004 -9.553 45.309 1.00 31.92 C ANISOU 2982 CB ARG A 404 3862 4006 4260 -228 -237 -260 C ATOM 2983 CG ARG A 404 -7.334 -10.308 45.364 1.00 33.58 C ANISOU 2983 CG ARG A 404 3931 3729 5099 -127 140 90 C ATOM 2984 CD ARG A 404 -7.285 -11.668 44.672 1.00 29.58 C ANISOU 2984 CD ARG A 404 3424 3951 3865 -57 383 375 C ATOM 2985 NE ARG A 404 -6.479 -12.685 45.370 1.00 29.34 N ANISOU 2985 NE ARG A 404 3639 3616 3891 95 21 -193 N ATOM 2986 CZ ARG A 404 -5.406 -13.275 44.836 1.00 32.27 C ANISOU 2986 CZ ARG A 404 3888 4080 4290 623 214 581 C ATOM 2987 NH1 ARG A 404 -4.999 -12.947 43.607 1.00 28.14 N ANISOU 2987 NH1 ARG A 404 1874 4575 4243 251 644 -430 N ATOM 2988 NH2 ARG A 404 -4.739 -14.199 45.518 1.00 29.74 N ANISOU 2988 NH2 ARG A 404 2685 4121 4491 537 -165 -153 N ATOM 2989 N ASP A 405 -7.115 -7.118 43.764 1.00 32.28 N ANISOU 2989 N ASP A 405 3719 4154 4391 -363 446 28 N ATOM 2990 CA ASP A 405 -8.214 -6.781 42.866 1.00 38.64 C ANISOU 2990 CA ASP A 405 4919 4625 5136 538 -166 -1 C ATOM 2991 C ASP A 405 -8.057 -7.685 41.667 1.00 36.59 C ANISOU 2991 C ASP A 405 4793 4032 5077 -63 158 222 C ATOM 2992 O ASP A 405 -6.946 -8.135 41.364 1.00 37.29 O ANISOU 2992 O ASP A 405 4291 4869 5007 -161 265 431 O ATOM 2993 CB ASP A 405 -8.144 -5.325 42.377 1.00 43.82 C ANISOU 2993 CB ASP A 405 6365 4998 5283 -126 -57 603 C ATOM 2994 CG ASP A 405 -7.978 -4.319 43.507 1.00 50.97 C ANISOU 2994 CG ASP A 405 7122 6264 5980 115 1070 -680 C ATOM 2995 OD1 ASP A 405 -8.755 -4.366 44.482 1.00 43.07 O ANISOU 2995 OD1 ASP A 405 4432 5443 6489 -74 303 237 O ATOM 2996 OD2 ASP A 405 -7.071 -3.461 43.407 1.00 72.51 O ANISOU 2996 OD2 ASP A 405 9345 8127 10078 -1575 1544 114 O ATOM 2997 N GLU A 406 -9.159 -7.947 40.979 1.00 34.13 N ANISOU 2997 N GLU A 406 3928 4721 4318 -80 792 461 N ATOM 2998 CA GLU A 406 -9.116 -8.704 39.746 1.00 33.38 C ANISOU 2998 CA GLU A 406 4274 4131 4276 -207 35 356 C ATOM 2999 C GLU A 406 -8.205 -7.987 38.760 1.00 38.51 C ANISOU 2999 C GLU A 406 4599 4333 5698 -575 1119 122 C ATOM 3000 O GLU A 406 -8.149 -6.761 38.745 1.00 34.01 O ANISOU 3000 O GLU A 406 3632 4052 5238 -813 902 289 O ATOM 3001 CB GLU A 406 -10.510 -8.823 39.151 1.00 30.11 C ANISOU 3001 CB GLU A 406 3452 3471 4515 -573 737 697 C ATOM 3002 CG GLU A 406 -11.208 -7.507 38.844 1.00 32.77 C ANISOU 3002 CG GLU A 406 3823 3558 5066 -450 408 601 C ATOM 3003 CD GLU A 406 -12.649 -7.723 38.411 1.00 35.10 C ANISOU 3003 CD GLU A 406 4299 4136 4900 8 -346 319 C ATOM 3004 OE1 GLU A 406 -13.200 -8.809 38.679 1.00 32.82 O ANISOU 3004 OE1 GLU A 406 3874 4099 4495 192 188 199 O ATOM 3005 OE2 GLU A 406 -13.242 -6.822 37.796 1.00 30.60 O ANISOU 3005 OE2 GLU A 406 3481 3562 4583 -263 604 330 O ATOM 3006 N LYS A 407 -7.501 -8.758 37.941 1.00 42.36 N ANISOU 3006 N LYS A 407 4984 5482 5630 -23 886 -174 N ATOM 3007 CA LYS A 407 -6.610 -8.180 36.942 1.00 41.44 C ANISOU 3007 CA LYS A 407 5431 5099 5216 -645 34 298 C ATOM 3008 C LYS A 407 -7.148 -8.356 35.531 1.00 41.53 C ANISOU 3008 C LYS A 407 4967 5626 5184 -851 395 67 C ATOM 3009 O LYS A 407 -6.560 -7.882 34.565 1.00 40.54 O ANISOU 3009 O LYS A 407 5314 4468 5620 -1261 368 269 O ATOM 3010 CB LYS A 407 -5.180 -8.693 37.121 1.00 41.19 C ANISOU 3010 CB LYS A 407 4914 5735 5001 -777 1172 260 C ATOM 3011 CG LYS A 407 -4.571 -8.090 38.379 1.00 44.24 C ANISOU 3011 CG LYS A 407 5563 5861 5385 -1019 664 451 C ATOM 3012 CD LYS A 407 -3.097 -8.365 38.542 1.00 54.11 C ANISOU 3012 CD LYS A 407 6224 8456 5877 -343 -92 509 C ATOM 3013 CE LYS A 407 -2.522 -7.397 39.563 1.00 59.82 C ANISOU 3013 CE LYS A 407 7655 8022 7051 -1665 325 34 C ATOM 3014 NZ LYS A 407 -1.164 -7.803 40.016 1.00 67.33 N ANISOU 3014 NZ LYS A 407 9323 7741 8519 -829 -457 1814 N ATOM 3015 N VAL A 408 -8.282 -9.040 35.426 1.00 34.39 N ANISOU 3015 N VAL A 408 4409 4199 4456 -166 562 463 N ATOM 3016 CA VAL A 408 -9.094 -8.997 34.220 1.00 31.17 C ANISOU 3016 CA VAL A 408 3640 4046 4154 -891 846 323 C ATOM 3017 C VAL A 408 -10.461 -8.473 34.651 1.00 37.21 C ANISOU 3017 C VAL A 408 4461 4835 4840 429 663 1051 C ATOM 3018 O VAL A 408 -11.082 -9.005 35.573 1.00 32.76 O ANISOU 3018 O VAL A 408 4011 3876 4557 379 750 379 O ATOM 3019 CB VAL A 408 -9.209 -10.385 33.566 1.00 31.24 C ANISOU 3019 CB VAL A 408 3563 4232 4072 -549 805 190 C ATOM 3020 CG1 VAL A 408 -10.101 -10.327 32.332 1.00 35.03 C ANISOU 3020 CG1 VAL A 408 3916 5180 4211 -580 646 1194 C ATOM 3021 CG2 VAL A 408 -7.821 -10.922 33.205 1.00 33.25 C ANISOU 3021 CG2 VAL A 408 3935 4038 4659 154 279 48 C ATOM 3022 N GLU A 409 -10.915 -7.407 34.007 1.00 32.95 N ANISOU 3022 N GLU A 409 3986 3676 4856 -913 1143 1076 N ATOM 3023 CA GLU A 409 -12.171 -6.780 34.371 1.00 32.77 C ANISOU 3023 CA GLU A 409 3816 3694 4941 -339 73 331 C ATOM 3024 C GLU A 409 -13.344 -7.768 34.234 1.00 29.79 C ANISOU 3024 C GLU A 409 3909 3426 3984 -361 582 -182 C ATOM 3025 O GLU A 409 -13.510 -8.395 33.195 1.00 29.84 O ANISOU 3025 O GLU A 409 3753 4183 3398 -542 679 -3 O ATOM 3026 CB GLU A 409 -12.402 -5.575 33.472 1.00 40.73 C ANISOU 3026 CB GLU A 409 5527 4434 5514 -775 485 1331 C ATOM 3027 CG GLU A 409 -13.538 -4.675 33.911 1.00 52.32 C ANISOU 3027 CG GLU A 409 5923 6333 7622 14 150 573 C ATOM 3028 CD GLU A 409 -13.729 -3.502 32.968 1.00 69.87 C ANISOU 3028 CD GLU A 409 9040 7257 10250 383 -422 2464 C ATOM 3029 OE1 GLU A 409 -12.723 -3.010 32.407 1.00 75.79 O ANISOU 3029 OE1 GLU A 409 11499 7947 9350 319 1686 2171 O ATOM 3030 OE2 GLU A 409 -14.887 -3.077 32.783 1.00 81.12 O ANISOU 3030 OE2 GLU A 409 9824 8217 12779 1676 -100 847 O ATOM 3031 N GLY A 410 -14.160 -7.905 35.276 1.00 28.13 N ANISOU 3031 N GLY A 410 3680 2933 4074 -168 487 458 N ATOM 3032 CA GLY A 410 -15.293 -8.855 35.211 1.00 28.45 C ANISOU 3032 CA GLY A 410 3239 3601 3970 -131 799 -141 C ATOM 3033 C GLY A 410 -14.947 -10.314 35.552 1.00 31.02 C ANISOU 3033 C GLY A 410 3568 3745 4474 -64 -238 192 C ATOM 3034 O GLY A 410 -15.822 -11.192 35.512 1.00 28.75 O ANISOU 3034 O GLY A 410 3463 3484 3974 95 222 253 O ATOM 3035 N ALA A 411 -13.686 -10.592 35.897 1.00 26.82 N ANISOU 3035 N ALA A 411 3181 3853 3157 193 726 1366 N ATOM 3036 CA ALA A 411 -13.296 -11.987 36.187 1.00 28.50 C ANISOU 3036 CA ALA A 411 3492 3353 3983 244 720 463 C ATOM 3037 C ALA A 411 -13.901 -12.529 37.493 1.00 28.13 C ANISOU 3037 C ALA A 411 3685 3448 3554 77 798 -72 C ATOM 3038 O ALA A 411 -14.153 -13.741 37.623 1.00 27.61 O ANISOU 3038 O ALA A 411 3511 3551 3429 -75 557 -288 O ATOM 3039 CB ALA A 411 -11.790 -12.141 36.228 1.00 27.64 C ANISOU 3039 CB ALA A 411 3425 3748 3327 156 910 822 C ATOM 3040 N PHE A 412 -14.097 -11.647 38.470 1.00 25.01 N ANISOU 3040 N PHE A 412 3017 3098 3388 -310 454 -60 N ATOM 3041 CA PHE A 412 -14.808 -12.040 39.680 1.00 26.16 C ANISOU 3041 CA PHE A 412 3596 3351 2992 59 346 -64 C ATOM 3042 C PHE A 412 -16.303 -12.188 39.389 1.00 28.11 C ANISOU 3042 C PHE A 412 3381 3489 3811 16 450 147 C ATOM 3043 O PHE A 412 -16.972 -11.225 39.009 1.00 27.23 O ANISOU 3043 O PHE A 412 3313 3339 3694 -173 303 121 O ATOM 3044 CB PHE A 412 -14.620 -11.035 40.806 1.00 29.22 C ANISOU 3044 CB PHE A 412 3493 4316 3293 -808 16 -363 C ATOM 3045 CG PHE A 412 -15.423 -11.376 42.033 1.00 29.97 C ANISOU 3045 CG PHE A 412 3928 3915 3543 369 423 180 C ATOM 3046 CD1 PHE A 412 -15.004 -12.390 42.889 1.00 26.21 C ANISOU 3046 CD1 PHE A 412 3435 3110 3410 -463 -130 -333 C ATOM 3047 CD2 PHE A 412 -16.609 -10.718 42.308 1.00 25.83 C ANISOU 3047 CD2 PHE A 412 3275 3005 3532 -329 203 127 C ATOM 3048 CE1 PHE A 412 -15.744 -12.715 44.018 1.00 28.60 C ANISOU 3048 CE1 PHE A 412 3283 3696 3887 -113 233 -349 C ATOM 3049 CE2 PHE A 412 -17.349 -11.034 43.434 1.00 25.04 C ANISOU 3049 CE2 PHE A 412 3164 2969 3380 21 193 18 C ATOM 3050 CZ PHE A 412 -16.917 -12.028 44.292 1.00 24.45 C ANISOU 3050 CZ PHE A 412 3121 2996 3170 -244 -71 -124 C ATOM 3051 N ILE A 413 -16.823 -13.393 39.581 1.00 28.27 N ANISOU 3051 N ILE A 413 3338 3303 4097 -27 178 -251 N ATOM 3052 CA ILE A 413 -18.209 -13.684 39.262 1.00 25.45 C ANISOU 3052 CA ILE A 413 3235 2993 3438 -67 188 33 C ATOM 3053 C ILE A 413 -18.861 -14.412 40.435 1.00 27.20 C ANISOU 3053 C ILE A 413 3363 3792 3177 -145 72 -89 C ATOM 3054 O ILE A 413 -19.778 -15.220 40.265 1.00 26.30 O ANISOU 3054 O ILE A 413 3512 3028 3450 -8 447 327 O ATOM 3055 CB ILE A 413 -18.328 -14.511 37.964 1.00 25.39 C ANISOU 3055 CB ILE A 413 3361 3277 3007 224 100 162 C ATOM 3056 CG1 ILE A 413 -17.294 -15.637 37.941 1.00 25.57 C ANISOU 3056 CG1 ILE A 413 3436 2932 3347 64 543 -300 C ATOM 3057 CG2 ILE A 413 -18.123 -13.620 36.744 1.00 27.16 C ANISOU 3057 CG2 ILE A 413 3548 3182 3588 -100 612 270 C ATOM 3058 CD1 ILE A 413 -17.510 -16.593 36.793 1.00 25.33 C ANISOU 3058 CD1 ILE A 413 3582 2736 3304 258 562 -247 C ATOM 3059 N GLY A 414 -18.383 -14.095 41.630 1.00 24.11 N ANISOU 3059 N GLY A 414 2611 3378 3171 232 137 -200 N ATOM 3060 CA GLY A 414 -18.874 -14.708 42.843 1.00 27.10 C ANISOU 3060 CA GLY A 414 3188 3393 3715 -145 109 288 C ATOM 3061 C GLY A 414 -20.366 -14.514 43.040 1.00 26.74 C ANISOU 3061 C GLY A 414 3068 3149 3941 144 -244 388 C ATOM 3062 O GLY A 414 -21.040 -15.392 43.583 1.00 24.70 O ANISOU 3062 O GLY A 414 2980 3290 3114 163 50 -93 O ATOM 3063 N PHE A 415 -20.880 -13.370 42.605 1.00 24.73 N ANISOU 3063 N PHE A 415 3016 2925 3453 187 381 273 N ATOM 3064 CA PHE A 415 -22.306 -13.080 42.723 1.00 23.99 C ANISOU 3064 CA PHE A 415 2861 2929 3322 -186 84 -64 C ATOM 3065 C PHE A 415 -22.969 -13.046 41.362 1.00 25.14 C ANISOU 3065 C PHE A 415 2952 3405 3195 -323 142 -21 C ATOM 3066 O PHE A 415 -24.034 -12.452 41.206 1.00 26.75 O ANISOU 3066 O PHE A 415 3735 3104 3322 215 316 851 O ATOM 3067 CB PHE A 415 -22.526 -11.730 43.416 1.00 23.60 C ANISOU 3067 CB PHE A 415 2572 3154 3239 407 287 -54 C ATOM 3068 CG PHE A 415 -22.125 -11.711 44.865 1.00 25.96 C ANISOU 3068 CG PHE A 415 3331 3138 3393 81 129 -271 C ATOM 3069 CD1 PHE A 415 -22.909 -12.344 45.828 1.00 26.66 C ANISOU 3069 CD1 PHE A 415 3636 3181 3312 218 53 77 C ATOM 3070 CD2 PHE A 415 -20.983 -11.034 45.276 1.00 26.93 C ANISOU 3070 CD2 PHE A 415 2896 3670 3665 592 -325 -288 C ATOM 3071 CE1 PHE A 415 -22.556 -12.319 47.166 1.00 23.81 C ANISOU 3071 CE1 PHE A 415 2942 2760 3344 246 155 -280 C ATOM 3072 CE2 PHE A 415 -20.631 -11.000 46.623 1.00 26.86 C ANISOU 3072 CE2 PHE A 415 2750 3932 3521 283 -110 339 C ATOM 3073 CZ PHE A 415 -21.417 -11.643 47.564 1.00 23.92 C ANISOU 3073 CZ PHE A 415 2860 3020 3205 433 -245 -63 C ATOM 3074 N GLY A 416 -22.354 -13.692 40.375 1.00 23.78 N ANISOU 3074 N GLY A 416 3036 2767 3229 -778 185 -88 N ATOM 3075 CA GLY A 416 -22.894 -13.669 39.014 1.00 22.74 C ANISOU 3075 CA GLY A 416 2978 2665 2995 -297 111 191 C ATOM 3076 C GLY A 416 -22.782 -12.284 38.380 1.00 21.70 C ANISOU 3076 C GLY A 416 2649 2833 2762 44 183 204 C ATOM 3077 O GLY A 416 -22.058 -11.417 38.870 1.00 24.51 O ANISOU 3077 O GLY A 416 3425 2892 2995 -278 722 -357 O ATOM 3078 N ALA A 417 -23.510 -12.065 37.295 1.00 21.16 N ANISOU 3078 N ALA A 417 2567 3102 2369 476 659 121 N ATOM 3079 CA ALA A 417 -23.470 -10.777 36.600 1.00 24.42 C ANISOU 3079 CA ALA A 417 3103 3016 3157 432 373 108 C ATOM 3080 C ALA A 417 -24.594 -10.708 35.593 1.00 25.93 C ANISOU 3080 C ALA A 417 3363 3417 3069 -94 221 87 C ATOM 3081 O ALA A 417 -25.228 -11.714 35.285 1.00 23.97 O ANISOU 3081 O ALA A 417 3037 3131 2936 128 399 -27 O ATOM 3082 CB ALA A 417 -22.136 -10.582 35.888 1.00 26.64 C ANISOU 3082 CB ALA A 417 3150 3093 3880 -290 324 568 C ATOM 3083 N GLY A 418 -24.826 -9.510 35.070 1.00 28.22 N ANISOU 3083 N GLY A 418 3441 3585 3694 874 343 0 N ATOM 3084 CA GLY A 418 -25.747 -9.335 33.963 1.00 28.72 C ANISOU 3084 CA GLY A 418 3743 3787 3382 643 218 -302 C ATOM 3085 C GLY A 418 -27.179 -9.692 34.280 1.00 29.63 C ANISOU 3085 C GLY A 418 4165 3401 3692 69 45 346 C ATOM 3086 O GLY A 418 -27.696 -9.326 35.329 1.00 31.19 O ANISOU 3086 O GLY A 418 4153 3897 3798 535 132 415 O ATOM 3087 N VAL A 419 -27.816 -10.409 33.359 1.00 30.77 N ANISOU 3087 N VAL A 419 4061 3656 3974 -55 -276 464 N ATOM 3088 CA VAL A 419 -29.243 -10.687 33.433 1.00 33.42 C ANISOU 3088 CA VAL A 419 4040 4670 3985 79 -246 212 C ATOM 3089 C VAL A 419 -29.681 -11.352 34.750 1.00 32.33 C ANISOU 3089 C VAL A 419 4193 4032 4057 619 294 72 C ATOM 3090 O VAL A 419 -30.732 -11.001 35.308 1.00 26.46 O ANISOU 3090 O VAL A 419 3206 3078 3770 30 -209 260 O ATOM 3091 CB VAL A 419 -29.715 -11.504 32.201 1.00 33.09 C ANISOU 3091 CB VAL A 419 4289 3967 4316 202 144 -132 C ATOM 3092 CG1 VAL A 419 -31.224 -11.766 32.255 1.00 34.96 C ANISOU 3092 CG1 VAL A 419 4327 3898 5056 -136 325 713 C ATOM 3093 CG2 VAL A 419 -29.352 -10.764 30.911 1.00 35.94 C ANISOU 3093 CG2 VAL A 419 4305 4869 4479 -767 297 -48 C ATOM 3094 N HIS A 420 -28.878 -12.289 35.253 1.00 33.23 N ANISOU 3094 N HIS A 420 4114 4306 4205 522 170 316 N ATOM 3095 CA HIS A 420 -29.250 -13.041 36.451 1.00 31.23 C ANISOU 3095 CA HIS A 420 4049 3931 3886 196 302 -140 C ATOM 3096 C HIS A 420 -28.325 -12.794 37.594 1.00 29.43 C ANISOU 3096 C HIS A 420 3446 3762 3974 104 458 59 C ATOM 3097 O HIS A 420 -28.051 -13.687 38.388 1.00 33.10 O ANISOU 3097 O HIS A 420 4569 3883 4124 552 444 183 O ATOM 3098 CB HIS A 420 -29.332 -14.529 36.137 1.00 30.76 C ANISOU 3098 CB HIS A 420 3489 3864 4332 93 348 82 C ATOM 3099 CG HIS A 420 -30.344 -14.852 35.074 1.00 32.09 C ANISOU 3099 CG HIS A 420 4431 3652 4107 -53 168 -318 C ATOM 3100 ND1 HIS A 420 -31.662 -14.948 35.337 1.00 33.44 N ANISOU 3100 ND1 HIS A 420 4328 3511 4866 -139 -237 -30 N ATOM 3101 CD2 HIS A 420 -30.199 -15.060 33.706 1.00 33.13 C ANISOU 3101 CD2 HIS A 420 4585 3831 4172 -158 162 -496 C ATOM 3102 CE1 HIS A 420 -32.325 -15.221 34.197 1.00 32.20 C ANISOU 3102 CE1 HIS A 420 4479 3567 4186 408 135 116 C ATOM 3103 NE2 HIS A 420 -31.430 -15.290 33.202 1.00 32.47 N ANISOU 3103 NE2 HIS A 420 4459 4093 3786 249 -61 -358 N ATOM 3104 N LYS A 421 -27.837 -11.567 37.704 1.00 27.57 N ANISOU 3104 N LYS A 421 3255 3548 3672 342 491 -429 N ATOM 3105 CA LYS A 421 -26.961 -11.227 38.816 1.00 28.72 C ANISOU 3105 CA LYS A 421 3519 3729 3663 175 -82 340 C ATOM 3106 C LYS A 421 -27.717 -11.371 40.132 1.00 28.32 C ANISOU 3106 C LYS A 421 3454 3438 3866 74 -104 176 C ATOM 3107 O LYS A 421 -28.949 -11.272 40.169 1.00 26.58 O ANISOU 3107 O LYS A 421 3294 3259 3546 286 167 -102 O ATOM 3108 CB LYS A 421 -26.410 -9.812 38.671 1.00 29.70 C ANISOU 3108 CB LYS A 421 3812 3655 3815 -7 -134 180 C ATOM 3109 CG LYS A 421 -27.445 -8.701 38.779 1.00 32.23 C ANISOU 3109 CG LYS A 421 4152 4056 4037 132 411 -79 C ATOM 3110 CD LYS A 421 -26.742 -7.359 38.950 1.00 41.32 C ANISOU 3110 CD LYS A 421 5776 4365 5557 -477 -162 554 C ATOM 3111 CE LYS A 421 -27.524 -6.252 38.270 1.00 48.03 C ANISOU 3111 CE LYS A 421 6991 5663 5592 7 -853 1036 C ATOM 3112 NZ LYS A 421 -27.508 -6.474 36.793 1.00 48.61 N ANISOU 3112 NZ LYS A 421 6539 6157 5773 -11 1231 -31 N ATOM 3113 N CYS A 422 -26.972 -11.630 41.201 1.00 26.07 N ANISOU 3113 N CYS A 422 3608 2996 3299 28 3 -350 N ATOM 3114 CA CYS A 422 -27.548 -11.874 42.502 1.00 25.25 C ANISOU 3114 CA CYS A 422 3176 2950 3465 -27 -72 318 C ATOM 3115 C CYS A 422 -28.315 -10.659 43.018 1.00 31.39 C ANISOU 3115 C CYS A 422 3757 3757 4413 3 527 -581 C ATOM 3116 O CYS A 422 -27.777 -9.554 43.048 1.00 30.79 O ANISOU 3116 O CYS A 422 3869 3177 4652 347 730 23 O ATOM 3117 CB CYS A 422 -26.442 -12.202 43.487 1.00 23.90 C ANISOU 3117 CB CYS A 422 2794 3124 3163 181 102 -86 C ATOM 3118 SG CYS A 422 -27.071 -12.618 45.114 1.00 25.48 S ANISOU 3118 SG CYS A 422 2829 3486 3366 179 218 29 S ATOM 3119 N ILE A 423 -29.560 -10.853 43.432 1.00 31.09 N ANISOU 3119 N ILE A 423 3576 3954 4280 -60 284 5 N ATOM 3120 CA ILE A 423 -30.281 -9.761 44.086 1.00 30.59 C ANISOU 3120 CA ILE A 423 3718 3983 3918 292 -238 41 C ATOM 3121 C ILE A 423 -30.100 -9.794 45.596 1.00 27.16 C ANISOU 3121 C ILE A 423 2825 3513 3981 -156 -90 -294 C ATOM 3122 O ILE A 423 -30.469 -8.848 46.273 1.00 29.85 O ANISOU 3122 O ILE A 423 3275 3532 4533 31 17 -425 O ATOM 3123 CB ILE A 423 -31.799 -9.716 43.757 1.00 33.87 C ANISOU 3123 CB ILE A 423 3667 4846 4355 487 -106 -7 C ATOM 3124 CG1 ILE A 423 -32.514 -10.962 44.254 1.00 37.20 C ANISOU 3124 CG1 ILE A 423 4187 4309 5635 208 -153 -549 C ATOM 3125 CG2 ILE A 423 -32.037 -9.486 42.274 1.00 36.32 C ANISOU 3125 CG2 ILE A 423 3843 5841 4115 304 -699 -1224 C ATOM 3126 CD1 ILE A 423 -34.014 -10.781 44.357 1.00 42.56 C ANISOU 3126 CD1 ILE A 423 4779 5360 6030 1764 -125 352 C ATOM 3127 N GLY A 424 -29.545 -10.876 46.137 1.00 26.24 N ANISOU 3127 N GLY A 424 2673 3690 3605 -61 106 -133 N ATOM 3128 CA GLY A 424 -29.333 -10.934 47.583 1.00 27.81 C ANISOU 3128 CA GLY A 424 3080 4016 3468 -105 134 582 C ATOM 3129 C GLY A 424 -27.951 -10.516 48.064 1.00 25.77 C ANISOU 3129 C GLY A 424 3421 3244 3126 -257 145 -44 C ATOM 3130 O GLY A 424 -27.684 -10.519 49.263 1.00 24.60 O ANISOU 3130 O GLY A 424 3206 3000 3141 0 147 74 O ATOM 3131 N GLN A 425 -27.060 -10.159 47.143 1.00 24.34 N ANISOU 3131 N GLN A 425 2949 3058 3241 -134 177 -15 N ATOM 3132 CA GLN A 425 -25.655 -9.875 47.508 1.00 25.00 C ANISOU 3132 CA GLN A 425 3088 3129 3282 -427 322 -113 C ATOM 3133 C GLN A 425 -25.507 -8.874 48.681 1.00 22.03 C ANISOU 3133 C GLN A 425 2476 2904 2988 -292 262 299 C ATOM 3134 O GLN A 425 -24.786 -9.115 49.649 1.00 25.46 O ANISOU 3134 O GLN A 425 2809 3343 3519 -451 26 489 O ATOM 3135 CB GLN A 425 -24.882 -9.397 46.264 1.00 26.75 C ANISOU 3135 CB GLN A 425 3306 3763 3094 -32 971 -918 C ATOM 3136 CG GLN A 425 -23.790 -8.386 46.580 1.00 34.85 C ANISOU 3136 CG GLN A 425 4130 4519 4592 -828 631 -530 C ATOM 3137 CD GLN A 425 -22.898 -8.060 45.398 1.00 39.23 C ANISOU 3137 CD GLN A 425 4787 5598 4519 -31 599 119 C ATOM 3138 OE1 GLN A 425 -23.280 -8.253 44.243 1.00 36.70 O ANISOU 3138 OE1 GLN A 425 4294 4930 4718 -104 224 645 O ATOM 3139 NE2 GLN A 425 -21.687 -7.566 45.686 1.00 41.39 N ANISOU 3139 NE2 GLN A 425 5281 4643 5802 27 210 -250 N ATOM 3140 N LYS A 426 -26.212 -7.755 48.605 1.00 22.80 N ANISOU 3140 N LYS A 426 2672 2833 3157 -232 87 26 N ATOM 3141 CA LYS A 426 -26.119 -6.744 49.654 1.00 23.92 C ANISOU 3141 CA LYS A 426 2773 3162 3154 -233 218 -109 C ATOM 3142 C LYS A 426 -26.605 -7.209 51.010 1.00 24.51 C ANISOU 3142 C LYS A 426 3211 2746 3353 14 75 79 C ATOM 3143 O LYS A 426 -25.987 -6.915 52.028 1.00 25.41 O ANISOU 3143 O LYS A 426 2841 3289 3523 -93 183 -176 O ATOM 3144 CB LYS A 426 -26.855 -5.476 49.246 1.00 26.22 C ANISOU 3144 CB LYS A 426 3466 3209 3286 92 191 -219 C ATOM 3145 CG LYS A 426 -26.164 -4.736 48.107 1.00 36.38 C ANISOU 3145 CG LYS A 426 5162 4544 4116 -576 981 177 C ATOM 3146 CD LYS A 426 -26.996 -3.552 47.646 1.00 46.30 C ANISOU 3146 CD LYS A 426 5943 5446 6202 -538 6 1313 C ATOM 3147 CE LYS A 426 -26.429 -2.935 46.375 1.00 64.95 C ANISOU 3147 CE LYS A 426 8295 9225 7156 -973 2274 1472 C ATOM 3148 NZ LYS A 426 -24.976 -2.618 46.510 1.00 68.52 N ANISOU 3148 NZ LYS A 426 9571 9104 7358 -2544 698 1991 N ATOM 3149 N PHE A 427 -27.718 -7.933 51.027 1.00 27.34 N ANISOU 3149 N PHE A 427 2854 3451 4083 24 300 84 N ATOM 3150 CA PHE A 427 -28.244 -8.468 52.280 1.00 25.99 C ANISOU 3150 CA PHE A 427 2923 3241 3709 27 51 116 C ATOM 3151 C PHE A 427 -27.341 -9.568 52.834 1.00 23.64 C ANISOU 3151 C PHE A 427 2285 3413 3282 -230 -176 -132 C ATOM 3152 O PHE A 427 -27.060 -9.607 54.038 1.00 24.95 O ANISOU 3152 O PHE A 427 2798 3669 3012 -538 838 23 O ATOM 3153 CB PHE A 427 -29.686 -8.993 52.079 1.00 27.56 C ANISOU 3153 CB PHE A 427 3086 3251 4133 -177 -94 19 C ATOM 3154 CG PHE A 427 -30.274 -9.606 53.312 1.00 31.50 C ANISOU 3154 CG PHE A 427 3619 4197 4151 -133 35 264 C ATOM 3155 CD1 PHE A 427 -30.588 -8.820 54.413 1.00 34.30 C ANISOU 3155 CD1 PHE A 427 4131 4852 4048 445 -297 106 C ATOM 3156 CD2 PHE A 427 -30.507 -10.970 53.377 1.00 36.82 C ANISOU 3156 CD2 PHE A 427 4236 4141 5613 -17 270 75 C ATOM 3157 CE1 PHE A 427 -31.127 -9.390 55.559 1.00 38.59 C ANISOU 3157 CE1 PHE A 427 4062 5198 5401 -1087 292 183 C ATOM 3158 CE2 PHE A 427 -31.039 -11.546 54.521 1.00 40.36 C ANISOU 3158 CE2 PHE A 427 4816 5613 4904 -229 361 -244 C ATOM 3159 CZ PHE A 427 -31.350 -10.755 55.615 1.00 39.01 C ANISOU 3159 CZ PHE A 427 4333 4750 5738 -511 415 -550 C ATOM 3160 N GLY A 428 -26.891 -10.474 51.963 1.00 24.75 N ANISOU 3160 N GLY A 428 2764 3306 3331 78 -36 79 N ATOM 3161 CA GLY A 428 -25.924 -11.506 52.377 1.00 24.46 C ANISOU 3161 CA GLY A 428 2871 2718 3705 -155 -76 150 C ATOM 3162 C GLY A 428 -24.671 -10.915 53.028 1.00 23.51 C ANISOU 3162 C GLY A 428 2926 2892 3113 2 183 -249 C ATOM 3163 O GLY A 428 -24.231 -11.373 54.080 1.00 27.34 O ANISOU 3163 O GLY A 428 3251 3771 3366 128 231 -147 O ATOM 3164 N LEU A 429 -24.086 -9.901 52.395 1.00 26.30 N ANISOU 3164 N LEU A 429 3368 2878 3746 -483 408 -384 N ATOM 3165 CA LEU A 429 -22.864 -9.262 52.929 1.00 26.30 C ANISOU 3165 CA LEU A 429 3186 3459 3348 -94 -87 52 C ATOM 3166 C LEU A 429 -23.148 -8.458 54.211 1.00 27.47 C ANISOU 3166 C LEU A 429 3579 3456 3400 -37 48 -12 C ATOM 3167 O LEU A 429 -22.307 -8.367 55.114 1.00 25.52 O ANISOU 3167 O LEU A 429 2710 3438 3545 -245 561 41 O ATOM 3168 CB LEU A 429 -22.212 -8.379 51.849 1.00 27.50 C ANISOU 3168 CB LEU A 429 3143 3586 3716 -325 429 -231 C ATOM 3169 CG LEU A 429 -21.631 -9.205 50.696 1.00 28.19 C ANISOU 3169 CG LEU A 429 3684 3604 3422 -138 103 -249 C ATOM 3170 CD1 LEU A 429 -21.120 -8.342 49.556 1.00 29.06 C ANISOU 3170 CD1 LEU A 429 3720 4067 3255 -1113 -212 -499 C ATOM 3171 CD2 LEU A 429 -20.525 -10.091 51.237 1.00 30.98 C ANISOU 3171 CD2 LEU A 429 3542 3736 4492 125 93 -449 C ATOM 3172 N LEU A 430 -24.342 -7.880 54.304 1.00 28.83 N ANISOU 3172 N LEU A 430 3647 3235 4070 -22 757 -479 N ATOM 3173 CA LEU A 430 -24.716 -7.173 55.541 1.00 25.13 C ANISOU 3173 CA LEU A 430 2962 3158 3426 34 615 -56 C ATOM 3174 C LEU A 430 -24.662 -8.135 56.725 1.00 23.81 C ANISOU 3174 C LEU A 430 2749 3158 3138 118 178 -401 C ATOM 3175 O LEU A 430 -24.115 -7.809 57.792 1.00 23.52 O ANISOU 3175 O LEU A 430 2959 2678 3297 -304 246 -322 O ATOM 3176 CB LEU A 430 -26.115 -6.574 55.410 1.00 26.86 C ANISOU 3176 CB LEU A 430 2945 3263 3995 15 -106 -404 C ATOM 3177 CG LEU A 430 -26.576 -5.682 56.571 1.00 30.93 C ANISOU 3177 CG LEU A 430 3432 3886 4432 -62 492 -746 C ATOM 3178 CD1 LEU A 430 -25.986 -4.285 56.404 1.00 28.61 C ANISOU 3178 CD1 LEU A 430 2749 3820 4300 169 475 -1085 C ATOM 3179 CD2 LEU A 430 -28.102 -5.612 56.622 1.00 30.44 C ANISOU 3179 CD2 LEU A 430 3480 3676 4407 -210 1058 -172 C ATOM 3180 N GLN A 431 -25.215 -9.339 56.543 1.00 23.24 N ANISOU 3180 N GLN A 431 2778 2909 3140 146 138 -183 N ATOM 3181 CA GLN A 431 -25.140 -10.338 57.593 1.00 23.14 C ANISOU 3181 CA GLN A 431 2848 2718 3224 127 396 -130 C ATOM 3182 C GLN A 431 -23.686 -10.768 57.837 1.00 24.32 C ANISOU 3182 C GLN A 431 2692 3482 3065 -405 13 -235 C ATOM 3183 O GLN A 431 -23.243 -10.871 58.982 1.00 24.26 O ANISOU 3183 O GLN A 431 3219 3008 2989 -517 31 -325 O ATOM 3184 CB GLN A 431 -25.967 -11.585 57.241 1.00 27.43 C ANISOU 3184 CB GLN A 431 3035 3608 3777 -207 -115 -565 C ATOM 3185 CG GLN A 431 -27.480 -11.387 57.157 1.00 29.57 C ANISOU 3185 CG GLN A 431 3146 3876 4213 139 135 -489 C ATOM 3186 CD GLN A 431 -28.174 -12.665 56.743 1.00 31.52 C ANISOU 3186 CD GLN A 431 3560 4254 4159 -381 -381 13 C ATOM 3187 OE1 GLN A 431 -28.646 -13.452 57.589 1.00 30.52 O ANISOU 3187 OE1 GLN A 431 3447 3694 4455 -230 61 -144 O ATOM 3188 NE2 GLN A 431 -28.204 -12.910 55.435 1.00 33.05 N ANISOU 3188 NE2 GLN A 431 3511 4929 4116 -960 201 -10 N ATOM 3189 N VAL A 432 -22.950 -11.077 56.772 1.00 22.19 N ANISOU 3189 N VAL A 432 2524 2626 3277 -191 152 -135 N ATOM 3190 CA VAL A 432 -21.565 -11.536 56.969 1.00 22.96 C ANISOU 3190 CA VAL A 432 2648 2906 3167 20 -99 -614 C ATOM 3191 C VAL A 432 -20.771 -10.480 57.755 1.00 21.32 C ANISOU 3191 C VAL A 432 2276 2841 2984 -273 207 -236 C ATOM 3192 O VAL A 432 -20.091 -10.783 58.732 1.00 23.73 O ANISOU 3192 O VAL A 432 2759 3286 2968 -310 402 -137 O ATOM 3193 CB VAL A 432 -20.850 -11.799 55.629 1.00 22.14 C ANISOU 3193 CB VAL A 432 2755 2572 3082 1 -120 -575 C ATOM 3194 CG1 VAL A 432 -19.385 -12.194 55.871 1.00 25.59 C ANISOU 3194 CG1 VAL A 432 2784 3582 3356 106 -2 -197 C ATOM 3195 CG2 VAL A 432 -21.587 -12.868 54.815 1.00 19.53 C ANISOU 3195 CG2 VAL A 432 1986 2566 2865 -80 159 -364 C ATOM 3196 N LYS A 433 -20.884 -9.234 57.322 1.00 25.99 N ANISOU 3196 N LYS A 433 2765 2981 4128 -323 545 -212 N ATOM 3197 CA LYS A 433 -20.088 -8.144 57.922 1.00 27.47 C ANISOU 3197 CA LYS A 433 3546 3498 3391 -98 -245 -414 C ATOM 3198 C LYS A 433 -20.499 -7.856 59.345 1.00 28.23 C ANISOU 3198 C LYS A 433 3442 3807 3475 138 125 -242 C ATOM 3199 O LYS A 433 -19.643 -7.641 60.203 1.00 29.84 O ANISOU 3199 O LYS A 433 2828 4260 4247 -441 292 -905 O ATOM 3200 CB LYS A 433 -20.145 -6.881 57.071 1.00 26.36 C ANISOU 3200 CB LYS A 433 3208 3147 3661 -136 -271 -359 C ATOM 3201 CG LYS A 433 -19.399 -7.043 55.762 1.00 28.37 C ANISOU 3201 CG LYS A 433 2705 4221 3851 -290 -159 20 C ATOM 3202 CD LYS A 433 -19.890 -6.080 54.708 1.00 33.40 C ANISOU 3202 CD LYS A 433 4293 3651 4746 -129 -1 387 C ATOM 3203 CE LYS A 433 -19.524 -4.655 55.050 1.00 30.87 C ANISOU 3203 CE LYS A 433 3813 3827 4089 -200 136 91 C ATOM 3204 NZ LYS A 433 -20.096 -3.775 53.989 1.00 33.14 N ANISOU 3204 NZ LYS A 433 4353 4365 3872 -186 -319 -158 N ATOM 3205 N THR A 434 -21.803 -7.889 59.610 1.00 27.74 N ANISOU 3205 N THR A 434 3119 3678 3743 -142 103 -325 N ATOM 3206 CA THR A 434 -22.278 -7.681 60.972 1.00 26.13 C ANISOU 3206 CA THR A 434 2834 3626 3466 -72 -64 -137 C ATOM 3207 C THR A 434 -21.762 -8.780 61.893 1.00 25.79 C ANISOU 3207 C THR A 434 2573 3534 3692 -216 75 -57 C ATOM 3208 O THR A 434 -21.323 -8.503 63.020 1.00 27.58 O ANISOU 3208 O THR A 434 2836 4047 3597 -571 610 -676 O ATOM 3209 CB THR A 434 -23.820 -7.560 61.042 1.00 25.88 C ANISOU 3209 CB THR A 434 2787 3846 3197 -362 153 343 C ATOM 3210 OG1 THR A 434 -24.249 -6.514 60.155 1.00 26.65 O ANISOU 3210 OG1 THR A 434 2895 3311 3918 110 -134 -95 O ATOM 3211 CG2 THR A 434 -24.271 -7.213 62.456 1.00 27.91 C ANISOU 3211 CG2 THR A 434 3462 3627 3513 -711 -317 -949 C ATOM 3212 N ILE A 435 -21.803 -10.028 61.422 1.00 25.84 N ANISOU 3212 N ILE A 435 2443 3547 3827 142 86 -279 N ATOM 3213 CA ILE A 435 -21.309 -11.143 62.227 1.00 24.93 C ANISOU 3213 CA ILE A 435 2958 2952 3562 -475 202 18 C ATOM 3214 C ILE A 435 -19.798 -10.993 62.453 1.00 26.24 C ANISOU 3214 C ILE A 435 3142 3417 3411 -350 61 80 C ATOM 3215 O ILE A 435 -19.311 -11.218 63.559 1.00 27.93 O ANISOU 3215 O ILE A 435 3163 3747 3699 -149 11 -119 O ATOM 3216 CB ILE A 435 -21.603 -12.528 61.589 1.00 25.03 C ANISOU 3216 CB ILE A 435 2788 3324 3399 -322 -238 -426 C ATOM 3217 CG1 ILE A 435 -23.096 -12.898 61.683 1.00 25.08 C ANISOU 3217 CG1 ILE A 435 2956 3279 3294 -722 -87 -537 C ATOM 3218 CG2 ILE A 435 -20.802 -13.610 62.296 1.00 24.63 C ANISOU 3218 CG2 ILE A 435 3238 2852 3265 -104 129 -475 C ATOM 3219 CD1 ILE A 435 -23.480 -14.037 60.739 1.00 22.88 C ANISOU 3219 CD1 ILE A 435 2292 3270 3129 -785 590 -781 C ATOM 3220 N LEU A 436 -19.053 -10.607 61.420 1.00 26.19 N ANISOU 3220 N LEU A 436 2951 3389 3609 -316 451 -344 N ATOM 3221 CA LEU A 436 -17.585 -10.457 61.583 1.00 27.86 C ANISOU 3221 CA LEU A 436 3207 3967 3412 -59 27 42 C ATOM 3222 C LEU A 436 -17.227 -9.404 62.640 1.00 30.53 C ANISOU 3222 C LEU A 436 3685 3937 3978 -372 -166 24 C ATOM 3223 O LEU A 436 -16.376 -9.632 63.500 1.00 31.34 O ANISOU 3223 O LEU A 436 3472 4281 4155 -144 120 475 O ATOM 3224 CB LEU A 436 -16.904 -10.127 60.249 1.00 24.15 C ANISOU 3224 CB LEU A 436 2279 3538 3356 -77 -13 -199 C ATOM 3225 CG LEU A 436 -16.865 -11.221 59.164 1.00 24.45 C ANISOU 3225 CG LEU A 436 3024 3117 3147 -103 133 85 C ATOM 3226 CD1 LEU A 436 -16.279 -10.669 57.866 1.00 23.07 C ANISOU 3226 CD1 LEU A 436 2804 3226 2733 -399 -238 -130 C ATOM 3227 CD2 LEU A 436 -16.059 -12.413 59.660 1.00 27.15 C ANISOU 3227 CD2 LEU A 436 3528 2831 3957 447 55 -710 C ATOM 3228 N ALA A 437 -17.892 -8.253 62.570 1.00 34.51 N ANISOU 3228 N ALA A 437 4433 4018 4661 -85 736 -353 N ATOM 3229 CA ALA A 437 -17.650 -7.160 63.511 1.00 33.53 C ANISOU 3229 CA ALA A 437 4109 4050 4578 -93 497 -192 C ATOM 3230 C ALA A 437 -18.049 -7.531 64.934 1.00 34.94 C ANISOU 3230 C ALA A 437 4227 4726 4321 -540 -332 120 C ATOM 3231 O ALA A 437 -17.405 -7.130 65.901 1.00 34.53 O ANISOU 3231 O ALA A 437 3215 4901 5002 -1034 -204 -63 O ATOM 3232 CB ALA A 437 -18.410 -5.921 63.071 1.00 30.36 C ANISOU 3232 CB ALA A 437 3882 3992 3660 -648 419 439 C ATOM 3233 N THR A 438 -19.131 -8.285 65.065 1.00 34.22 N ANISOU 3233 N THR A 438 4278 4290 4433 -465 -34 405 N ATOM 3234 CA THR A 438 -19.642 -8.621 66.383 1.00 30.71 C ANISOU 3234 CA THR A 438 3962 3738 3968 -415 -53 -524 C ATOM 3235 C THR A 438 -18.792 -9.729 67.006 1.00 35.18 C ANISOU 3235 C THR A 438 3882 4934 4550 241 -437 -451 C ATOM 3236 O THR A 438 -18.488 -9.688 68.198 1.00 36.80 O ANISOU 3236 O THR A 438 4858 4792 4330 -425 67 -332 O ATOM 3237 CB THR A 438 -21.131 -9.054 66.314 1.00 29.57 C ANISOU 3237 CB THR A 438 3413 4014 3805 136 203 -149 C ATOM 3238 OG1 THR A 438 -21.907 -8.020 65.689 1.00 26.00 O ANISOU 3238 OG1 THR A 438 2932 3773 3173 -110 213 -506 O ATOM 3239 CG2 THR A 438 -21.674 -9.346 67.701 1.00 30.03 C ANISOU 3239 CG2 THR A 438 3636 4240 3534 -35 92 -524 C ATOM 3240 N ALA A 439 -18.409 -10.711 66.191 1.00 32.83 N ANISOU 3240 N ALA A 439 3820 4298 4354 -7 -281 -266 N ATOM 3241 CA ALA A 439 -17.620 -11.845 66.669 1.00 32.35 C ANISOU 3241 CA ALA A 439 4194 4612 3485 134 85 77 C ATOM 3242 C ALA A 439 -16.204 -11.427 67.047 1.00 38.42 C ANISOU 3242 C ALA A 439 4599 5099 4900 -702 1 531 C ATOM 3243 O ALA A 439 -15.714 -11.777 68.135 1.00 37.19 O ANISOU 3243 O ALA A 439 4652 5183 4292 -378 109 -531 O ATOM 3244 CB ALA A 439 -17.585 -12.958 65.630 1.00 36.19 C ANISOU 3244 CB ALA A 439 5025 4063 4663 -75 -29 -231 C ATOM 3245 N PHE A 440 -15.545 -10.690 66.151 1.00 31.68 N ANISOU 3245 N PHE A 440 4089 3526 4421 -97 181 -355 N ATOM 3246 CA PHE A 440 -14.155 -10.283 66.401 1.00 35.13 C ANISOU 3246 CA PHE A 440 4267 5046 4033 -251 -14 158 C ATOM 3247 C PHE A 440 -13.980 -9.142 67.401 1.00 37.76 C ANISOU 3247 C PHE A 440 4887 4655 4802 -98 -308 68 C ATOM 3248 O PHE A 440 -12.869 -8.902 67.864 1.00 41.92 O ANISOU 3248 O PHE A 440 4717 6164 5045 79 -40 -1095 O ATOM 3249 CB PHE A 440 -13.405 -9.996 65.098 1.00 30.37 C ANISOU 3249 CB PHE A 440 2849 4028 4660 -443 155 -105 C ATOM 3250 CG PHE A 440 -13.016 -11.235 64.362 1.00 32.59 C ANISOU 3250 CG PHE A 440 3881 4245 4257 -77 291 -92 C ATOM 3251 CD1 PHE A 440 -12.089 -12.124 64.917 1.00 31.87 C ANISOU 3251 CD1 PHE A 440 3413 4246 4448 -575 233 118 C ATOM 3252 CD2 PHE A 440 -13.588 -11.540 63.138 1.00 32.97 C ANISOU 3252 CD2 PHE A 440 3961 4333 4232 289 -73 318 C ATOM 3253 CE1 PHE A 440 -11.732 -13.284 64.250 1.00 34.26 C ANISOU 3253 CE1 PHE A 440 3864 4576 4577 -485 342 -133 C ATOM 3254 CE2 PHE A 440 -13.230 -12.697 62.456 1.00 37.59 C ANISOU 3254 CE2 PHE A 440 4841 4142 5298 206 -83 69 C ATOM 3255 CZ PHE A 440 -12.301 -13.570 63.014 1.00 34.45 C ANISOU 3255 CZ PHE A 440 4011 4499 4578 139 123 -309 C ATOM 3256 N ARG A 441 -15.059 -8.447 67.742 1.00 40.98 N ANISOU 3256 N ARG A 441 4799 5507 5263 -16 -481 -826 N ATOM 3257 CA ARG A 441 -14.983 -7.462 68.814 1.00 40.69 C ANISOU 3257 CA ARG A 441 5148 5157 5153 298 365 -665 C ATOM 3258 C ARG A 441 -14.813 -8.159 70.157 1.00 43.58 C ANISOU 3258 C ARG A 441 5502 5153 5902 -241 -331 -242 C ATOM 3259 O ARG A 441 -14.082 -7.676 71.025 1.00 42.05 O ANISOU 3259 O ARG A 441 4895 5420 5661 -51 272 -651 O ATOM 3260 CB ARG A 441 -16.228 -6.579 68.846 1.00 44.60 C ANISOU 3260 CB ARG A 441 4706 6386 5854 409 -534 -899 C ATOM 3261 CG ARG A 441 -16.337 -5.708 70.097 1.00 45.23 C ANISOU 3261 CG ARG A 441 4866 6043 6275 -847 -391 -1168 C ATOM 3262 CD ARG A 441 -17.734 -5.121 70.226 1.00 50.45 C ANISOU 3262 CD ARG A 441 5463 6302 7402 -69 -452 -985 C ATOM 3263 NE ARG A 441 -17.828 -4.064 71.232 1.00 58.51 N ANISOU 3263 NE ARG A 441 7542 7242 7446 -102 -513 -1286 N ATOM 3264 CZ ARG A 441 -17.864 -2.763 70.953 1.00 64.13 C ANISOU 3264 CZ ARG A 441 8865 7647 7852 -726 -121 -363 C ATOM 3265 NH1 ARG A 441 -17.814 -2.338 69.695 1.00 57.89 N ANISOU 3265 NH1 ARG A 441 6142 8601 7250 -384 -252 -1099 N ATOM 3266 NH2 ARG A 441 -17.956 -1.880 71.938 1.00 68.86 N ANISOU 3266 NH2 ARG A 441 8273 9307 8581 -3738 -1152 -1871 N ATOM 3267 N SER A 442 -15.474 -9.299 70.332 1.00 40.46 N ANISOU 3267 N SER A 442 4725 5542 5103 -395 -473 -235 N ATOM 3268 CA SER A 442 -15.493 -9.928 71.647 1.00 38.86 C ANISOU 3268 CA SER A 442 4828 4880 5056 -220 396 -488 C ATOM 3269 C SER A 442 -14.700 -11.224 71.765 1.00 39.73 C ANISOU 3269 C SER A 442 4685 5262 5146 33 216 -338 C ATOM 3270 O SER A 442 -14.488 -11.720 72.867 1.00 43.81 O ANISOU 3270 O SER A 442 5601 6196 4847 -484 252 -382 O ATOM 3271 CB SER A 442 -16.930 -10.133 72.115 1.00 36.21 C ANISOU 3271 CB SER A 442 4341 4489 4926 -356 -277 -497 C ATOM 3272 OG SER A 442 -17.649 -8.921 71.999 1.00 38.59 O ANISOU 3272 OG SER A 442 4542 5026 5093 150 129 -677 O ATOM 3273 N TYR A 443 -14.260 -11.777 70.642 1.00 37.88 N ANISOU 3273 N TYR A 443 4160 4888 5345 -481 -403 -1255 N ATOM 3274 CA TYR A 443 -13.583 -13.070 70.683 1.00 37.25 C ANISOU 3274 CA TYR A 443 4403 4668 5081 -301 -235 -665 C ATOM 3275 C TYR A 443 -12.369 -13.124 69.783 1.00 38.25 C ANISOU 3275 C TYR A 443 4677 4517 5339 134 98 13 C ATOM 3276 O TYR A 443 -12.305 -12.431 68.761 1.00 39.16 O ANISOU 3276 O TYR A 443 4831 5189 4858 -289 -480 -296 O ATOM 3277 CB TYR A 443 -14.523 -14.191 70.230 1.00 35.01 C ANISOU 3277 CB TYR A 443 4149 4653 4498 -636 55 162 C ATOM 3278 CG TYR A 443 -15.703 -14.433 71.128 1.00 35.39 C ANISOU 3278 CG TYR A 443 4234 5065 4145 -226 177 48 C ATOM 3279 CD1 TYR A 443 -16.869 -13.682 70.992 1.00 36.48 C ANISOU 3279 CD1 TYR A 443 4630 4794 4436 -50 -7 -824 C ATOM 3280 CD2 TYR A 443 -15.664 -15.429 72.102 1.00 32.42 C ANISOU 3280 CD2 TYR A 443 3911 3985 4422 -725 -349 -402 C ATOM 3281 CE1 TYR A 443 -17.964 -13.905 71.816 1.00 36.79 C ANISOU 3281 CE1 TYR A 443 4454 4847 4678 -327 -197 -50 C ATOM 3282 CE2 TYR A 443 -16.749 -15.657 72.931 1.00 38.36 C ANISOU 3282 CE2 TYR A 443 4345 5572 4655 -58 328 -626 C ATOM 3283 CZ TYR A 443 -17.898 -14.894 72.780 1.00 37.94 C ANISOU 3283 CZ TYR A 443 4793 5093 4527 10 134 -15 C ATOM 3284 OH TYR A 443 -18.981 -15.127 73.599 1.00 40.15 O ANISOU 3284 OH TYR A 443 4570 6094 4590 -194 187 -662 O ATOM 3285 N ASP A 444 -11.419 -13.973 70.161 1.00 34.57 N ANISOU 3285 N ASP A 444 3411 5211 4511 -315 -524 -117 N ATOM 3286 CA ASP A 444 -10.427 -14.445 69.220 1.00 38.01 C ANISOU 3286 CA ASP A 444 4502 4743 5195 425 -194 -272 C ATOM 3287 C ASP A 444 -10.758 -15.886 68.967 1.00 35.90 C ANISOU 3287 C ASP A 444 4108 5191 4340 -341 -544 -538 C ATOM 3288 O ASP A 444 -11.543 -16.494 69.707 1.00 37.78 O ANISOU 3288 O ASP A 444 4225 5649 4481 617 -213 358 O ATOM 3289 CB ASP A 444 -9.009 -14.331 69.786 1.00 43.74 C ANISOU 3289 CB ASP A 444 4751 6194 5671 -508 -339 -581 C ATOM 3290 CG ASP A 444 -8.515 -12.907 69.806 1.00 46.79 C ANISOU 3290 CG ASP A 444 4883 6423 6469 -1000 -275 -1 C ATOM 3291 OD1 ASP A 444 -8.484 -12.270 68.729 1.00 49.51 O ANISOU 3291 OD1 ASP A 444 5478 6385 6945 -838 963 371 O ATOM 3292 OD2 ASP A 444 -8.166 -12.425 70.899 1.00 51.57 O ANISOU 3292 OD2 ASP A 444 6625 6500 6466 -619 43 -705 O ATOM 3293 N PHE A 445 -10.164 -16.430 67.916 1.00 35.86 N ANISOU 3293 N PHE A 445 4099 4970 4554 -132 122 -142 N ATOM 3294 CA PHE A 445 -10.369 -17.820 67.563 1.00 36.70 C ANISOU 3294 CA PHE A 445 4110 4918 4914 -291 239 -409 C ATOM 3295 C PHE A 445 -9.029 -18.395 67.170 1.00 35.13 C ANISOU 3295 C PHE A 445 4307 4217 4820 125 -269 -358 C ATOM 3296 O PHE A 445 -8.156 -17.679 66.662 1.00 36.66 O ANISOU 3296 O PHE A 445 3823 5545 4558 -78 -342 -264 O ATOM 3297 CB PHE A 445 -11.362 -17.953 66.398 1.00 37.12 C ANISOU 3297 CB PHE A 445 4284 5471 4349 669 249 -166 C ATOM 3298 CG PHE A 445 -12.686 -17.313 66.665 1.00 32.21 C ANISOU 3298 CG PHE A 445 3736 4519 3982 141 -472 -121 C ATOM 3299 CD1 PHE A 445 -12.905 -15.972 66.341 1.00 31.80 C ANISOU 3299 CD1 PHE A 445 3802 4233 4047 -524 -463 14 C ATOM 3300 CD2 PHE A 445 -13.715 -18.042 67.254 1.00 30.75 C ANISOU 3300 CD2 PHE A 445 4203 4416 3061 208 -502 144 C ATOM 3301 CE1 PHE A 445 -14.125 -15.365 66.609 1.00 33.29 C ANISOU 3301 CE1 PHE A 445 4018 4494 4133 -368 -306 118 C ATOM 3302 CE2 PHE A 445 -14.937 -17.440 67.523 1.00 32.60 C ANISOU 3302 CE2 PHE A 445 3577 4597 4210 -250 -435 298 C ATOM 3303 CZ PHE A 445 -15.144 -16.104 67.203 1.00 30.18 C ANISOU 3303 CZ PHE A 445 3528 4440 3497 -116 -562 70 C ATOM 3304 N GLN A 446 -8.871 -19.684 67.411 1.00 33.89 N ANISOU 3304 N GLN A 446 4191 4371 4314 9 -409 312 N ATOM 3305 CA GLN A 446 -7.702 -20.395 66.947 1.00 41.16 C ANISOU 3305 CA GLN A 446 4732 4898 6007 456 -180 -159 C ATOM 3306 C GLN A 446 -8.123 -21.641 66.158 1.00 38.26 C ANISOU 3306 C GLN A 446 3915 5691 4929 98 -362 -64 C ATOM 3307 O GLN A 446 -8.884 -22.468 66.664 1.00 40.35 O ANISOU 3307 O GLN A 446 4970 5331 5030 65 -449 720 O ATOM 3308 CB GLN A 446 -6.837 -20.751 68.160 1.00 48.31 C ANISOU 3308 CB GLN A 446 6666 6497 5190 1034 34 329 C ATOM 3309 CG GLN A 446 -5.776 -21.806 67.930 1.00 52.97 C ANISOU 3309 CG GLN A 446 6175 7071 6878 1019 137 434 C ATOM 3310 CD GLN A 446 -5.398 -22.517 69.215 1.00 61.48 C ANISOU 3310 CD GLN A 446 8742 7911 6704 2103 -892 -149 C ATOM 3311 OE1 GLN A 446 -5.251 -21.892 70.270 1.00 57.90 O ANISOU 3311 OE1 GLN A 446 5892 9189 6918 1137 -2543 29 O ATOM 3312 NE2 GLN A 446 -5.244 -23.835 69.136 1.00 68.72 N ANISOU 3312 NE2 GLN A 446 8824 6966 10320 -659 -1678 1564 N ATOM 3313 N LEU A 447 -7.649 -21.752 64.912 1.00 35.60 N ANISOU 3313 N LEU A 447 3364 5755 4405 181 -888 449 N ATOM 3314 CA LEU A 447 -7.794 -22.984 64.118 1.00 43.43 C ANISOU 3314 CA LEU A 447 5874 5474 5153 -382 158 330 C ATOM 3315 C LEU A 447 -7.176 -24.179 64.834 1.00 48.11 C ANISOU 3315 C LEU A 447 5836 5736 6705 34 -677 203 C ATOM 3316 O LEU A 447 -6.172 -24.036 65.522 1.00 49.00 O ANISOU 3316 O LEU A 447 5522 6064 7029 164 -358 -747 O ATOM 3317 CB LEU A 447 -7.111 -22.849 62.751 1.00 42.06 C ANISOU 3317 CB LEU A 447 3519 6605 5856 -1356 255 -114 C ATOM 3318 CG LEU A 447 -7.892 -22.775 61.439 1.00 45.05 C ANISOU 3318 CG LEU A 447 5792 6157 5166 -192 354 985 C ATOM 3319 CD1 LEU A 447 -6.954 -23.122 60.293 1.00 46.23 C ANISOU 3319 CD1 LEU A 447 4388 6863 6312 871 11 406 C ATOM 3320 CD2 LEU A 447 -9.081 -23.726 61.441 1.00 46.62 C ANISOU 3320 CD2 LEU A 447 6051 6497 5165 -624 -465 -123 C ATOM 3321 N LEU A 448 -7.764 -25.358 64.662 1.00 46.40 N ANISOU 3321 N LEU A 448 5983 5480 6164 290 80 -639 N ATOM 3322 CA LEU A 448 -7.230 -26.563 65.299 1.00 47.97 C ANISOU 3322 CA LEU A 448 5988 6310 5925 -43 -6 174 C ATOM 3323 C LEU A 448 -6.540 -27.485 64.290 1.00 47.65 C ANISOU 3323 C LEU A 448 5468 6086 6547 -233 479 286 C ATOM 3324 O LEU A 448 -6.612 -28.710 64.389 1.00 54.95 O ANISOU 3324 O LEU A 448 7724 6096 7057 404 -775 93 O ATOM 3325 CB LEU A 448 -8.323 -27.291 66.093 1.00 45.38 C ANISOU 3325 CB LEU A 448 6157 5856 5228 -39 -369 440 C ATOM 3326 CG LEU A 448 -8.873 -26.462 67.259 1.00 48.52 C ANISOU 3326 CG LEU A 448 6070 6299 6066 -73 -145 -221 C ATOM 3327 CD1 LEU A 448 -9.953 -27.214 68.021 1.00 47.50 C ANISOU 3327 CD1 LEU A 448 5388 5733 6925 -49 -962 268 C ATOM 3328 CD2 LEU A 448 -7.756 -26.018 68.202 1.00 44.36 C ANISOU 3328 CD2 LEU A 448 4368 5856 6631 1320 -342 827 C ATOM 3329 N ARG A 449 -5.872 -26.865 63.321 1.00 41.68 N ANISOU 3329 N ARG A 449 5591 5835 4408 879 -615 572 N ATOM 3330 CA ARG A 449 -5.064 -27.555 62.323 1.00 44.42 C ANISOU 3330 CA ARG A 449 5334 5836 5704 143 182 135 C ATOM 3331 C ARG A 449 -4.146 -26.514 61.697 1.00 44.13 C ANISOU 3331 C ARG A 449 5291 5766 5710 377 286 334 C ATOM 3332 O ARG A 449 -4.346 -25.312 61.892 1.00 44.78 O ANISOU 3332 O ARG A 449 4598 6048 6366 1093 -611 -285 O ATOM 3333 CB ARG A 449 -5.937 -28.226 61.260 1.00 47.35 C ANISOU 3333 CB ARG A 449 6622 5106 6262 304 -131 -339 C ATOM 3334 CG ARG A 449 -7.180 -27.444 60.869 1.00 53.26 C ANISOU 3334 CG ARG A 449 5672 7565 6999 526 -455 -783 C ATOM 3335 CD ARG A 449 -7.983 -28.220 59.843 1.00 52.34 C ANISOU 3335 CD ARG A 449 6522 7169 6196 4 -361 147 C ATOM 3336 NE ARG A 449 -7.468 -27.983 58.503 1.00 51.07 N ANISOU 3336 NE ARG A 449 6965 6429 6011 1507 -604 470 N ATOM 3337 CZ ARG A 449 -7.347 -28.913 57.563 1.00 44.29 C ANISOU 3337 CZ ARG A 449 4540 5713 6573 -93 -1143 349 C ATOM 3338 NH1 ARG A 449 -7.682 -30.169 57.815 1.00 48.57 N ANISOU 3338 NH1 ARG A 449 5894 5887 6672 378 -1181 1997 N ATOM 3339 NH2 ARG A 449 -6.869 -28.588 56.370 1.00 51.48 N ANISOU 3339 NH2 ARG A 449 4899 7624 7035 1486 98 62 N ATOM 3340 N ASP A 450 -3.138 -26.969 60.961 1.00 41.53 N ANISOU 3340 N ASP A 450 5936 5039 4802 682 192 690 N ATOM 3341 CA ASP A 450 -2.120 -26.070 60.419 1.00 43.57 C ANISOU 3341 CA ASP A 450 4879 6248 5428 -214 -675 258 C ATOM 3342 C ASP A 450 -2.672 -25.114 59.365 1.00 46.70 C ANISOU 3342 C ASP A 450 6105 5072 6567 -38 -821 380 C ATOM 3343 O ASP A 450 -2.300 -23.945 59.333 1.00 42.36 O ANISOU 3343 O ASP A 450 5800 5230 5062 49 -790 20 O ATOM 3344 CB ASP A 450 -0.960 -26.872 59.818 1.00 53.14 C ANISOU 3344 CB ASP A 450 6193 6850 7145 605 -466 -110 C ATOM 3345 CG ASP A 450 -0.268 -27.757 60.837 1.00 64.57 C ANISOU 3345 CG ASP A 450 7920 8912 7701 1729 -1133 677 C ATOM 3346 OD1 ASP A 450 -0.268 -27.408 62.041 1.00 66.40 O ANISOU 3346 OD1 ASP A 450 6555 10151 8523 590 -2258 -259 O ATOM 3347 OD2 ASP A 450 0.282 -28.804 60.429 1.00 66.63 O ANISOU 3347 OD2 ASP A 450 8834 8289 8192 704 -2512 -388 O ATOM 3348 N GLU A 451 -3.552 -25.625 58.507 1.00 42.91 N ANISOU 3348 N GLU A 451 5164 5527 5610 488 -374 235 N ATOM 3349 CA GLU A 451 -4.030 -24.886 57.344 1.00 39.39 C ANISOU 3349 CA GLU A 451 4949 5607 4410 -304 -28 -56 C ATOM 3350 C GLU A 451 -5.539 -24.724 57.396 1.00 40.54 C ANISOU 3350 C GLU A 451 5161 5496 4744 620 -172 13 C ATOM 3351 O GLU A 451 -6.231 -25.498 58.069 1.00 43.84 O ANISOU 3351 O GLU A 451 4764 5467 6425 131 -417 460 O ATOM 3352 CB GLU A 451 -3.635 -25.624 56.060 1.00 41.15 C ANISOU 3352 CB GLU A 451 5616 4829 5188 270 196 -67 C ATOM 3353 CG GLU A 451 -2.163 -26.020 55.993 1.00 49.27 C ANISOU 3353 CG GLU A 451 6049 6079 6589 736 -334 -324 C ATOM 3354 CD GLU A 451 -1.230 -24.843 55.777 1.00 63.78 C ANISOU 3354 CD GLU A 451 7822 7804 8606 -691 -23 365 C ATOM 3355 OE1 GLU A 451 -1.435 -24.086 54.804 1.00 66.07 O ANISOU 3355 OE1 GLU A 451 7217 8306 9579 27 -61 1180 O ATOM 3356 OE2 GLU A 451 -0.278 -24.684 56.572 1.00 73.83 O ANISOU 3356 OE2 GLU A 451 10319 10466 7266 -1476 -1021 -431 O ATOM 3357 N VAL A 452 -6.059 -23.717 56.698 1.00 42.43 N ANISOU 3357 N VAL A 452 5294 5126 5700 154 -300 408 N ATOM 3358 CA VAL A 452 -7.512 -23.573 56.600 1.00 41.61 C ANISOU 3358 CA VAL A 452 5139 4808 5860 -129 -578 253 C ATOM 3359 C VAL A 452 -8.074 -24.848 55.957 1.00 36.00 C ANISOU 3359 C VAL A 452 4107 4820 4749 -35 210 120 C ATOM 3360 O VAL A 452 -7.348 -25.558 55.246 1.00 33.10 O ANISOU 3360 O VAL A 452 4101 4157 4317 -383 215 319 O ATOM 3361 CB VAL A 452 -7.931 -22.303 55.825 1.00 39.22 C ANISOU 3361 CB VAL A 452 5044 4908 4949 -149 236 314 C ATOM 3362 CG1 VAL A 452 -7.235 -21.076 56.405 1.00 39.07 C ANISOU 3362 CG1 VAL A 452 4857 4149 5837 849 -333 156 C ATOM 3363 CG2 VAL A 452 -7.616 -22.442 54.343 1.00 37.59 C ANISOU 3363 CG2 VAL A 452 5062 4423 4796 -145 -381 -670 C ATOM 3364 N PRO A 453 -9.352 -25.171 56.228 1.00 30.01 N ANISOU 3364 N PRO A 453 3820 3839 3743 -4 242 -92 N ATOM 3365 CA PRO A 453 -9.928 -26.387 55.667 1.00 26.94 C ANISOU 3365 CA PRO A 453 3056 3767 3410 -315 190 206 C ATOM 3366 C PRO A 453 -9.899 -26.454 54.145 1.00 27.88 C ANISOU 3366 C PRO A 453 3534 3422 3635 -207 687 76 C ATOM 3367 O PRO A 453 -9.944 -25.418 53.475 1.00 27.55 O ANISOU 3367 O PRO A 453 3326 3512 3629 -123 544 -151 O ATOM 3368 CB PRO A 453 -11.389 -26.302 56.108 1.00 25.59 C ANISOU 3368 CB PRO A 453 3177 2912 3632 488 161 -328 C ATOM 3369 CG PRO A 453 -11.315 -25.608 57.421 1.00 27.60 C ANISOU 3369 CG PRO A 453 3564 3508 3413 205 18 -176 C ATOM 3370 CD PRO A 453 -10.259 -24.544 57.207 1.00 29.64 C ANISOU 3370 CD PRO A 453 3653 4095 3511 -75 203 82 C ATOM 3371 N ASP A 454 -9.862 -27.672 53.613 1.00 28.71 N ANISOU 3371 N ASP A 454 3715 3465 3727 357 232 -110 N ATOM 3372 CA ASP A 454 -10.092 -27.904 52.193 1.00 31.26 C ANISOU 3372 CA ASP A 454 3827 3962 4086 143 -440 -278 C ATOM 3373 C ASP A 454 -11.560 -27.689 51.925 1.00 29.77 C ANISOU 3373 C ASP A 454 3726 3615 3968 578 369 41 C ATOM 3374 O ASP A 454 -12.392 -28.053 52.754 1.00 27.98 O ANISOU 3374 O ASP A 454 3494 3544 3594 574 28 -45 O ATOM 3375 CB ASP A 454 -9.780 -29.363 51.810 1.00 31.98 C ANISOU 3375 CB ASP A 454 3983 3712 4454 72 -345 172 C ATOM 3376 CG ASP A 454 -8.435 -29.821 52.300 1.00 36.13 C ANISOU 3376 CG ASP A 454 4050 4358 5319 481 -207 283 C ATOM 3377 OD1 ASP A 454 -7.450 -29.079 52.124 1.00 39.98 O ANISOU 3377 OD1 ASP A 454 4203 5305 5681 -26 51 252 O ATOM 3378 OD2 ASP A 454 -8.364 -30.925 52.872 1.00 36.95 O ANISOU 3378 OD2 ASP A 454 4052 4568 5419 2 -396 288 O ATOM 3379 N PRO A 455 -11.882 -27.114 50.756 1.00 32.95 N ANISOU 3379 N PRO A 455 4125 4100 4294 285 26 403 N ATOM 3380 CA PRO A 455 -13.268 -27.078 50.304 1.00 32.51 C ANISOU 3380 CA PRO A 455 4147 4209 3995 -146 174 -28 C ATOM 3381 C PRO A 455 -13.804 -28.489 50.127 1.00 33.95 C ANISOU 3381 C PRO A 455 4074 4170 4653 -200 337 374 C ATOM 3382 O PRO A 455 -13.048 -29.406 49.795 1.00 39.05 O ANISOU 3382 O PRO A 455 5607 4571 4658 604 616 359 O ATOM 3383 CB PRO A 455 -13.185 -26.384 48.939 1.00 33.60 C ANISOU 3383 CB PRO A 455 4112 4364 4287 170 -112 378 C ATOM 3384 CG PRO A 455 -11.730 -26.361 48.571 1.00 36.77 C ANISOU 3384 CG PRO A 455 4246 4816 4907 -104 -161 973 C ATOM 3385 CD PRO A 455 -10.983 -26.358 49.864 1.00 33.28 C ANISOU 3385 CD PRO A 455 4229 4383 4032 -403 354 -640 C ATOM 3386 N ASP A 456 -15.093 -28.668 50.361 1.00 28.84 N ANISOU 3386 N ASP A 456 3795 3381 3780 -130 -167 728 N ATOM 3387 CA ASP A 456 -15.716 -29.972 50.117 1.00 29.54 C ANISOU 3387 CA ASP A 456 4140 3524 3559 -214 -177 126 C ATOM 3388 C ASP A 456 -16.672 -29.832 48.944 1.00 27.61 C ANISOU 3388 C ASP A 456 3533 3133 3822 -653 -11 -58 C ATOM 3389 O ASP A 456 -17.761 -29.267 49.072 1.00 30.31 O ANISOU 3389 O ASP A 456 4276 3369 3870 -279 537 -148 O ATOM 3390 CB ASP A 456 -16.397 -30.478 51.398 1.00 30.02 C ANISOU 3390 CB ASP A 456 3216 3887 4300 -69 156 427 C ATOM 3391 CG ASP A 456 -17.216 -31.763 51.194 1.00 32.69 C ANISOU 3391 CG ASP A 456 4511 3718 4189 -232 536 92 C ATOM 3392 OD1 ASP A 456 -17.303 -32.328 50.087 1.00 37.90 O ANISOU 3392 OD1 ASP A 456 5212 4563 4625 -16 220 -398 O ATOM 3393 OD2 ASP A 456 -17.810 -32.205 52.180 1.00 33.34 O ANISOU 3393 OD2 ASP A 456 5214 3436 4016 -260 11 585 O ATOM 3394 N TYR A 457 -16.236 -30.338 47.788 1.00 30.82 N ANISOU 3394 N TYR A 457 4009 3482 4217 156 165 -118 N ATOM 3395 CA TYR A 457 -16.963 -30.189 46.531 1.00 32.12 C ANISOU 3395 CA TYR A 457 4442 3550 4210 -104 288 233 C ATOM 3396 C TYR A 457 -18.146 -31.129 46.318 1.00 33.39 C ANISOU 3396 C TYR A 457 4243 4167 4274 -25 -165 -325 C ATOM 3397 O TYR A 457 -18.749 -31.100 45.257 1.00 36.20 O ANISOU 3397 O TYR A 457 3857 5144 4753 -473 -508 -968 O ATOM 3398 CB TYR A 457 -15.999 -30.310 45.350 1.00 35.20 C ANISOU 3398 CB TYR A 457 4847 3582 4945 -8 832 -10 C ATOM 3399 CG TYR A 457 -14.941 -29.223 45.329 1.00 37.03 C ANISOU 3399 CG TYR A 457 4326 4452 5292 -218 233 -28 C ATOM 3400 CD1 TYR A 457 -15.304 -27.876 45.262 1.00 35.50 C ANISOU 3400 CD1 TYR A 457 4910 4219 4357 -400 212 353 C ATOM 3401 CD2 TYR A 457 -13.584 -29.540 45.377 1.00 34.80 C ANISOU 3401 CD2 TYR A 457 4434 4252 4534 119 -220 22 C ATOM 3402 CE1 TYR A 457 -14.343 -26.874 45.233 1.00 33.05 C ANISOU 3402 CE1 TYR A 457 4255 3647 4655 193 -361 -740 C ATOM 3403 CE2 TYR A 457 -12.615 -28.546 45.351 1.00 34.24 C ANISOU 3403 CE2 TYR A 457 4922 4085 4002 49 55 -80 C ATOM 3404 CZ TYR A 457 -13.003 -27.213 45.281 1.00 30.99 C ANISOU 3404 CZ TYR A 457 4088 3980 3706 -333 282 -152 C ATOM 3405 OH TYR A 457 -12.057 -26.215 45.262 1.00 28.33 O ANISOU 3405 OH TYR A 457 3433 3555 3776 40 295 -118 O ATOM 3406 N HIS A 458 -18.486 -31.946 47.309 1.00 37.56 N ANISOU 3406 N HIS A 458 4941 4543 4784 30 587 -104 N ATOM 3407 CA HIS A 458 -19.555 -32.932 47.124 1.00 42.77 C ANISOU 3407 CA HIS A 458 5361 5685 5203 -175 -394 -568 C ATOM 3408 C HIS A 458 -20.942 -32.379 47.261 1.00 43.57 C ANISOU 3408 C HIS A 458 5353 5622 5579 22 38 -559 C ATOM 3409 O HIS A 458 -21.900 -33.049 46.892 1.00 47.40 O ANISOU 3409 O HIS A 458 7208 4439 6363 -280 -105 -1798 O ATOM 3410 CB HIS A 458 -19.383 -34.117 48.066 1.00 47.42 C ANISOU 3410 CB HIS A 458 6968 4110 6941 -887 -805 -925 C ATOM 3411 CG HIS A 458 -18.089 -34.861 47.873 1.00 60.79 C ANISOU 3411 CG HIS A 458 7117 8044 7935 35 931 -74 C ATOM 3412 ND1 HIS A 458 -17.146 -34.933 48.831 1.00 64.99 N ANISOU 3412 ND1 HIS A 458 8498 8871 7324 -161 725 -1213 N ATOM 3413 CD2 HIS A 458 -17.593 -35.563 46.777 1.00 71.47 C ANISOU 3413 CD2 HIS A 458 9145 8021 9990 1458 894 -999 C ATOM 3414 CE1 HIS A 458 -16.103 -35.649 48.378 1.00 74.63 C ANISOU 3414 CE1 HIS A 458 8933 9380 10041 830 47 -1582 C ATOM 3415 NE2 HIS A 458 -16.377 -36.034 47.121 1.00 74.92 N ANISOU 3415 NE2 HIS A 458 8355 11576 8534 3182 2800 -2040 N ATOM 3416 N THR A 459 -21.080 -31.164 47.791 1.00 39.80 N ANISOU 3416 N THR A 459 5317 4891 4914 -66 212 206 N ATOM 3417 CA THR A 459 -22.418 -30.576 48.000 1.00 38.86 C ANISOU 3417 CA THR A 459 5473 4643 4648 -40 143 -490 C ATOM 3418 C THR A 459 -22.841 -29.601 46.886 1.00 37.34 C ANISOU 3418 C THR A 459 4938 4355 4894 -151 -26 -460 C ATOM 3419 O THR A 459 -21.988 -29.103 46.139 1.00 39.08 O ANISOU 3419 O THR A 459 6308 4400 4140 222 910 -561 O ATOM 3420 CB THR A 459 -22.524 -29.882 49.378 1.00 36.24 C ANISOU 3420 CB THR A 459 4999 4758 4009 -580 404 104 C ATOM 3421 OG1 THR A 459 -21.559 -28.817 49.473 1.00 32.34 O ANISOU 3421 OG1 THR A 459 4262 3994 4031 115 10 -433 O ATOM 3422 CG2 THR A 459 -22.298 -30.896 50.501 1.00 37.26 C ANISOU 3422 CG2 THR A 459 5223 4117 4814 140 351 125 C ATOM 3423 N MET A 460 -24.149 -29.342 46.782 1.00 36.73 N ANISOU 3423 N MET A 460 4235 4088 5631 -804 -222 -479 N ATOM 3424 CA MET A 460 -24.722 -28.376 45.827 1.00 39.27 C ANISOU 3424 CA MET A 460 5250 4593 5076 -230 172 -307 C ATOM 3425 C MET A 460 -24.108 -26.984 46.021 1.00 39.57 C ANISOU 3425 C MET A 460 5584 5069 4379 -980 317 -70 C ATOM 3426 O MET A 460 -23.715 -26.315 45.068 1.00 32.84 O ANISOU 3426 O MET A 460 4465 4493 3518 -596 43 -677 O ATOM 3427 CB MET A 460 -26.243 -28.252 46.039 1.00 47.26 C ANISOU 3427 CB MET A 460 4891 7070 5994 -660 -131 429 C ATOM 3428 CG MET A 460 -27.151 -28.912 45.012 1.00 58.00 C ANISOU 3428 CG MET A 460 7432 8375 6228 -2043 -328 -611 C ATOM 3429 SD MET A 460 -28.925 -28.693 45.367 1.00 66.54 S ANISOU 3429 SD MET A 460 7284 8712 9285 -1615 -571 -222 S ATOM 3430 CE MET A 460 -29.095 -26.915 45.587 1.00 71.72 C ANISOU 3430 CE MET A 460 10337 8098 8813 -944 820 1919 C ATOM 3431 N VAL A 461 -24.072 -26.540 47.272 1.00 33.46 N ANISOU 3431 N VAL A 461 4210 4160 4341 -361 -117 -394 N ATOM 3432 CA VAL A 461 -23.465 -25.267 47.629 1.00 29.36 C ANISOU 3432 CA VAL A 461 3412 3712 4031 -76 125 -201 C ATOM 3433 C VAL A 461 -22.215 -25.641 48.432 1.00 29.85 C ANISOU 3433 C VAL A 461 3795 3929 3614 -261 111 503 C ATOM 3434 O VAL A 461 -22.312 -26.323 49.459 1.00 26.84 O ANISOU 3434 O VAL A 461 3503 3583 3110 -113 347 27 O ATOM 3435 CB VAL A 461 -24.456 -24.378 48.422 1.00 28.03 C ANISOU 3435 CB VAL A 461 3345 3507 3795 -342 -258 -767 C ATOM 3436 CG1 VAL A 461 -23.893 -22.981 48.662 1.00 21.73 C ANISOU 3436 CG1 VAL A 461 2871 2864 2519 68 285 71 C ATOM 3437 CG2 VAL A 461 -25.795 -24.289 47.684 1.00 25.90 C ANISOU 3437 CG2 VAL A 461 3107 3321 3409 666 179 196 C ATOM 3438 N VAL A 462 -21.050 -25.226 47.929 1.00 25.69 N ANISOU 3438 N VAL A 462 3264 3572 2924 86 189 -97 N ATOM 3439 CA VAL A 462 -19.761 -25.699 48.423 1.00 25.58 C ANISOU 3439 CA VAL A 462 3286 3291 3140 -148 -49 118 C ATOM 3440 C VAL A 462 -19.207 -24.780 49.497 1.00 25.61 C ANISOU 3440 C VAL A 462 3367 3308 3052 -86 -59 162 C ATOM 3441 O VAL A 462 -19.138 -23.557 49.316 1.00 25.21 O ANISOU 3441 O VAL A 462 2967 3160 3451 -50 125 -31 O ATOM 3442 CB VAL A 462 -18.716 -25.815 47.286 1.00 29.44 C ANISOU 3442 CB VAL A 462 3306 4329 3550 28 22 -473 C ATOM 3443 CG1 VAL A 462 -17.354 -26.212 47.843 1.00 27.43 C ANISOU 3443 CG1 VAL A 462 3234 3462 3722 141 358 -194 C ATOM 3444 CG2 VAL A 462 -19.175 -26.824 46.249 1.00 29.09 C ANISOU 3444 CG2 VAL A 462 4164 3544 3344 222 679 -449 C ATOM 3445 N GLY A 463 -18.809 -25.388 50.612 1.00 22.54 N ANISOU 3445 N GLY A 463 2663 2952 2946 -250 55 143 N ATOM 3446 CA GLY A 463 -18.208 -24.666 51.714 1.00 22.46 C ANISOU 3446 CA GLY A 463 3284 2484 2765 -251 179 120 C ATOM 3447 C GLY A 463 -16.993 -25.439 52.182 1.00 22.95 C ANISOU 3447 C GLY A 463 2707 3217 2793 -318 392 230 C ATOM 3448 O GLY A 463 -16.639 -26.457 51.586 1.00 26.66 O ANISOU 3448 O GLY A 463 3282 3379 3465 45 -77 -13 O ATOM 3449 N PRO A 464 -16.354 -24.978 53.264 1.00 25.06 N ANISOU 3449 N PRO A 464 3102 3214 3204 -262 71 -259 N ATOM 3450 CA PRO A 464 -15.214 -25.688 53.850 1.00 27.74 C ANISOU 3450 CA PRO A 464 3462 3469 3610 197 -24 -280 C ATOM 3451 C PRO A 464 -15.640 -27.058 54.401 1.00 31.82 C ANISOU 3451 C PRO A 464 3993 3948 4147 214 332 245 C ATOM 3452 O PRO A 464 -16.789 -27.235 54.821 1.00 29.84 O ANISOU 3452 O PRO A 464 3524 4028 3785 342 209 -294 O ATOM 3453 CB PRO A 464 -14.775 -24.759 54.989 1.00 25.47 C ANISOU 3453 CB PRO A 464 2739 3509 3427 180 73 -128 C ATOM 3454 CG PRO A 464 -16.032 -24.040 55.379 1.00 25.17 C ANISOU 3454 CG PRO A 464 3174 3193 3193 549 57 214 C ATOM 3455 CD PRO A 464 -16.795 -23.845 54.094 1.00 24.63 C ANISOU 3455 CD PRO A 464 2766 3260 3329 168 7 -169 C ATOM 3456 N THR A 465 -14.730 -28.025 54.371 1.00 32.02 N ANISOU 3456 N THR A 465 4215 3995 3956 462 -166 155 N ATOM 3457 CA THR A 465 -15.011 -29.362 54.906 1.00 32.24 C ANISOU 3457 CA THR A 465 4241 3911 4094 584 2 -158 C ATOM 3458 C THR A 465 -15.424 -29.281 56.373 1.00 32.20 C ANISOU 3458 C THR A 465 3829 4053 4350 117 324 130 C ATOM 3459 O THR A 465 -14.648 -28.817 57.222 1.00 33.24 O ANISOU 3459 O THR A 465 4096 4433 4099 158 -75 298 O ATOM 3460 CB THR A 465 -13.786 -30.280 54.733 1.00 33.30 C ANISOU 3460 CB THR A 465 4846 3468 4337 714 647 -132 C ATOM 3461 OG1 THR A 465 -13.534 -30.434 53.332 1.00 35.98 O ANISOU 3461 OG1 THR A 465 4459 4744 4467 466 876 451 O ATOM 3462 CG2 THR A 465 -14.043 -31.648 55.345 1.00 31.18 C ANISOU 3462 CG2 THR A 465 3737 4123 3984 395 102 304 C ATOM 3463 N ALA A 466 -16.646 -29.727 56.659 1.00 29.90 N ANISOU 3463 N ALA A 466 3637 3292 4428 302 -72 673 N ATOM 3464 CA ALA A 466 -17.305 -29.481 57.951 1.00 32.63 C ANISOU 3464 CA ALA A 466 3978 4223 4195 -321 -109 22 C ATOM 3465 C ALA A 466 -16.548 -30.063 59.132 1.00 35.03 C ANISOU 3465 C ALA A 466 4498 4181 4631 147 -302 188 C ATOM 3466 O ALA A 466 -16.470 -29.449 60.203 1.00 37.22 O ANISOU 3466 O ALA A 466 5444 3937 4757 62 78 133 O ATOM 3467 CB ALA A 466 -18.755 -30.001 57.929 1.00 32.13 C ANISOU 3467 CB ALA A 466 3942 3898 4368 -471 880 162 C ATOM 3468 N SER A 467 -15.995 -31.256 58.937 1.00 34.55 N ANISOU 3468 N SER A 467 4167 4476 4484 314 305 42 N ATOM 3469 CA SER A 467 -15.268 -31.960 59.995 1.00 35.51 C ANISOU 3469 CA SER A 467 4656 4797 4038 445 -184 -379 C ATOM 3470 C SER A 467 -13.922 -31.291 60.269 1.00 40.98 C ANISOU 3470 C SER A 467 5262 5278 5031 -531 -3 281 C ATOM 3471 O SER A 467 -13.265 -31.579 61.282 1.00 40.83 O ANISOU 3471 O SER A 467 5702 4535 5277 2 161 721 O ATOM 3472 CB SER A 467 -15.053 -33.419 59.599 1.00 35.69 C ANISOU 3472 CB SER A 467 5430 4226 3903 749 -468 910 C ATOM 3473 OG SER A 467 -14.227 -33.502 58.442 1.00 40.49 O ANISOU 3473 OG SER A 467 4732 5326 5325 796 231 192 O ATOM 3474 N GLN A 468 -13.503 -30.409 59.362 1.00 35.22 N ANISOU 3474 N GLN A 468 5020 3923 4438 -46 -233 -390 N ATOM 3475 CA GLN A 468 -12.256 -29.656 59.547 1.00 33.02 C ANISOU 3475 CA GLN A 468 4146 4154 4244 187 531 226 C ATOM 3476 C GLN A 468 -12.508 -28.260 60.106 1.00 34.13 C ANISOU 3476 C GLN A 468 4453 4099 4412 -73 225 -12 C ATOM 3477 O GLN A 468 -11.588 -27.435 60.179 1.00 34.22 O ANISOU 3477 O GLN A 468 3928 4235 4838 140 -212 486 O ATOM 3478 CB GLN A 468 -11.516 -29.514 58.227 1.00 30.53 C ANISOU 3478 CB GLN A 468 3788 4044 3765 543 92 344 C ATOM 3479 CG GLN A 468 -11.087 -30.817 57.595 1.00 32.74 C ANISOU 3479 CG GLN A 468 4342 4104 3991 259 -486 -217 C ATOM 3480 CD GLN A 468 -10.514 -30.603 56.206 1.00 42.07 C ANISOU 3480 CD GLN A 468 6017 4993 4975 -154 936 -568 C ATOM 3481 OE1 GLN A 468 -10.299 -29.468 55.767 1.00 42.21 O ANISOU 3481 OE1 GLN A 468 5441 5164 5432 455 -17 107 O ATOM 3482 NE2 GLN A 468 -10.271 -31.693 55.504 1.00 35.33 N ANISOU 3482 NE2 GLN A 468 5067 4301 4053 450 369 410 N ATOM 3483 N CYS A 469 -13.748 -27.992 60.503 1.00 32.80 N ANISOU 3483 N CYS A 469 4132 3891 4440 55 -34 152 N ATOM 3484 CA CYS A 469 -14.121 -26.647 60.958 1.00 31.99 C ANISOU 3484 CA CYS A 469 4118 3905 4130 116 -252 52 C ATOM 3485 C CYS A 469 -14.225 -26.469 62.473 1.00 33.24 C ANISOU 3485 C CYS A 469 4054 4425 4150 35 -35 218 C ATOM 3486 O CYS A 469 -14.748 -25.462 62.950 1.00 36.80 O ANISOU 3486 O CYS A 469 4777 4254 4950 260 -223 271 O ATOM 3487 CB CYS A 469 -15.406 -26.182 60.265 1.00 33.66 C ANISOU 3487 CB CYS A 469 3831 4702 4253 599 296 284 C ATOM 3488 SG CYS A 469 -15.176 -25.755 58.519 1.00 33.09 S ANISOU 3488 SG CYS A 469 4135 4223 4213 383 -6 220 S ATOM 3489 N ARG A 470 -13.720 -27.428 63.243 1.00 32.96 N ANISOU 3489 N ARG A 470 3588 4372 4560 -342 2 503 N ATOM 3490 CA ARG A 470 -13.667 -27.221 64.691 1.00 38.79 C ANISOU 3490 CA ARG A 470 5189 4614 4935 321 -20 -374 C ATOM 3491 C ARG A 470 -12.618 -26.170 65.047 1.00 37.29 C ANISOU 3491 C ARG A 470 4716 4807 4645 306 50 -29 C ATOM 3492 O ARG A 470 -11.473 -26.247 64.611 1.00 40.21 O ANISOU 3492 O ARG A 470 5141 5846 4291 127 449 317 O ATOM 3493 CB ARG A 470 -13.445 -28.536 65.452 1.00 42.73 C ANISOU 3493 CB ARG A 470 5938 5954 4341 -168 -11 747 C ATOM 3494 CG ARG A 470 -14.535 -29.566 65.181 1.00 44.70 C ANISOU 3494 CG ARG A 470 6167 5111 5703 241 -324 231 C ATOM 3495 CD ARG A 470 -14.581 -30.672 66.220 1.00 51.89 C ANISOU 3495 CD ARG A 470 7744 5705 6266 570 170 862 C ATOM 3496 NE ARG A 470 -14.957 -30.201 67.555 1.00 53.17 N ANISOU 3496 NE ARG A 470 7089 5773 7339 1161 -233 -208 N ATOM 3497 CZ ARG A 470 -16.199 -29.908 67.940 1.00 54.21 C ANISOU 3497 CZ ARG A 470 6714 7273 6608 -260 189 -416 C ATOM 3498 NH1 ARG A 470 -17.215 -30.008 67.088 1.00 54.54 N ANISOU 3498 NH1 ARG A 470 5908 6045 8769 -2492 -20 -24 N ATOM 3499 NH2 ARG A 470 -16.426 -29.499 69.183 1.00 48.69 N ANISOU 3499 NH2 ARG A 470 7085 5275 6137 -715 -239 324 N ATOM 3500 N VAL A 471 -13.027 -25.166 65.812 1.00 32.89 N ANISOU 3500 N VAL A 471 4384 4248 3861 16 -38 240 N ATOM 3501 CA VAL A 471 -12.110 -24.120 66.249 1.00 35.52 C ANISOU 3501 CA VAL A 471 4310 4802 4383 -215 -299 217 C ATOM 3502 C VAL A 471 -12.253 -23.831 67.740 1.00 37.22 C ANISOU 3502 C VAL A 471 5046 4546 4550 -271 102 -100 C ATOM 3503 O VAL A 471 -13.253 -24.209 68.361 1.00 35.77 O ANISOU 3503 O VAL A 471 4565 4491 4533 -27 -13 -222 O ATOM 3504 CB VAL A 471 -12.306 -22.796 65.470 1.00 35.87 C ANISOU 3504 CB VAL A 471 4705 5133 3788 875 -108 80 C ATOM 3505 CG1 VAL A 471 -12.270 -23.040 63.961 1.00 30.52 C ANISOU 3505 CG1 VAL A 471 4034 3755 3806 -450 123 -251 C ATOM 3506 CG2 VAL A 471 -13.594 -22.097 65.896 1.00 33.74 C ANISOU 3506 CG2 VAL A 471 3482 5281 4053 -270 8 140 C ATOM 3507 N LYS A 472 -11.252 -23.152 68.306 1.00 36.46 N ANISOU 3507 N LYS A 472 4170 5318 4365 276 -432 319 N ATOM 3508 CA LYS A 472 -11.321 -22.689 69.695 1.00 41.04 C ANISOU 3508 CA LYS A 472 5268 5261 5064 462 -235 -614 C ATOM 3509 C LYS A 472 -11.670 -21.204 69.751 1.00 38.82 C ANISOU 3509 C LYS A 472 4604 5113 5031 246 -349 -614 C ATOM 3510 O LYS A 472 -10.958 -20.383 69.172 1.00 46.90 O ANISOU 3510 O LYS A 472 5380 6257 6180 -322 -382 14 O ATOM 3511 CB LYS A 472 -9.999 -22.949 70.439 1.00 42.59 C ANISOU 3511 CB LYS A 472 4971 6186 5025 387 276 407 C ATOM 3512 CG LYS A 472 -9.978 -22.379 71.853 1.00 49.19 C ANISOU 3512 CG LYS A 472 6831 5935 5923 -347 -361 -376 C ATOM 3513 CD LYS A 472 -8.885 -22.978 72.723 1.00 59.83 C ANISOU 3513 CD LYS A 472 5954 8618 8158 488 -684 -532 C ATOM 3514 CE LYS A 472 -7.729 -22.012 72.916 1.00 62.93 C ANISOU 3514 CE LYS A 472 7386 7435 9089 136 -473 -372 C ATOM 3515 NZ LYS A 472 -6.790 -22.509 73.960 1.00 70.36 N ANISOU 3515 NZ LYS A 472 9931 10168 6632 -85 -632 361 N ATOM 3516 N TYR A 473 -12.773 -20.860 70.419 1.00 35.52 N ANISOU 3516 N TYR A 473 4813 4848 3832 231 -273 -341 N ATOM 3517 CA TYR A 473 -13.044 -19.455 70.719 1.00 35.64 C ANISOU 3517 CA TYR A 473 4497 4567 4476 -85 154 294 C ATOM 3518 C TYR A 473 -12.402 -19.083 72.029 1.00 37.91 C ANISOU 3518 C TYR A 473 4401 5094 4907 155 -138 96 C ATOM 3519 O TYR A 473 -12.335 -19.887 72.949 1.00 41.65 O ANISOU 3519 O TYR A 473 5518 5539 4767 390 -719 81 O ATOM 3520 CB TYR A 473 -14.540 -19.124 70.780 1.00 36.11 C ANISOU 3520 CB TYR A 473 4321 4968 4430 -407 -202 -76 C ATOM 3521 CG TYR A 473 -15.281 -19.644 72.006 1.00 39.28 C ANISOU 3521 CG TYR A 473 4875 5358 4688 138 689 -295 C ATOM 3522 CD1 TYR A 473 -15.259 -18.950 73.218 1.00 42.45 C ANISOU 3522 CD1 TYR A 473 5216 5832 5080 -487 -69 -731 C ATOM 3523 CD2 TYR A 473 -16.035 -20.817 71.935 1.00 38.36 C ANISOU 3523 CD2 TYR A 473 5104 5496 3973 -12 -75 -20 C ATOM 3524 CE1 TYR A 473 -15.952 -19.427 74.327 1.00 43.31 C ANISOU 3524 CE1 TYR A 473 5921 5486 5046 -260 -172 -167 C ATOM 3525 CE2 TYR A 473 -16.728 -21.298 73.029 1.00 37.83 C ANISOU 3525 CE2 TYR A 473 3786 6056 4531 -382 -148 70 C ATOM 3526 CZ TYR A 473 -16.685 -20.606 74.223 1.00 42.44 C ANISOU 3526 CZ TYR A 473 5216 5733 5173 -315 275 -297 C ATOM 3527 OH TYR A 473 -17.391 -21.104 75.302 1.00 39.66 O ANISOU 3527 OH TYR A 473 5170 5753 4144 -67 -653 -243 O ATOM 3528 N ILE A 474 -11.955 -17.840 72.104 1.00 43.65 N ANISOU 3528 N ILE A 474 4828 5715 6039 -603 -187 -524 N ATOM 3529 CA ILE A 474 -11.314 -17.322 73.287 1.00 45.51 C ANISOU 3529 CA ILE A 474 5954 5956 5382 280 -224 -513 C ATOM 3530 C ILE A 474 -11.921 -15.962 73.541 1.00 43.77 C ANISOU 3530 C ILE A 474 4738 6169 5724 415 -476 -428 C ATOM 3531 O ILE A 474 -11.781 -15.049 72.713 1.00 44.82 O ANISOU 3531 O ILE A 474 5196 6262 5569 -826 -880 -582 O ATOM 3532 CB ILE A 474 -9.797 -17.162 73.081 1.00 49.01 C ANISOU 3532 CB ILE A 474 5912 6440 6268 -319 -66 -663 C ATOM 3533 CG1 ILE A 474 -9.181 -18.494 72.636 1.00 49.51 C ANISOU 3533 CG1 ILE A 474 6062 6493 6254 -497 313 -867 C ATOM 3534 CG2 ILE A 474 -9.141 -16.652 74.357 1.00 45.60 C ANISOU 3534 CG2 ILE A 474 4575 5698 7052 -1471 -59 -382 C ATOM 3535 CD1 ILE A 474 -7.973 -18.351 71.738 1.00 54.32 C ANISOU 3535 CD1 ILE A 474 6329 8212 6097 -1844 223 -1002 C ATOM 3536 N ARG A 475 -12.606 -15.842 74.675 1.00 42.40 N ANISOU 3536 N ARG A 475 4108 6245 5756 -515 -462 -839 N ATOM 3537 CA ARG A 475 -13.219 -14.581 75.078 1.00 45.69 C ANISOU 3537 CA ARG A 475 6187 5632 5540 57 -119 -231 C ATOM 3538 C ARG A 475 -12.125 -13.539 75.277 1.00 48.51 C ANISOU 3538 C ARG A 475 5935 6037 6458 -17 105 -196 C ATOM 3539 O ARG A 475 -11.090 -13.831 75.874 1.00 52.74 O ANISOU 3539 O ARG A 475 6554 6343 7142 277 -679 -1156 O ATOM 3540 CB ARG A 475 -14.032 -14.768 76.369 1.00 44.62 C ANISOU 3540 CB ARG A 475 5478 5485 5989 -555 161 -656 C ATOM 3541 CG ARG A 475 -14.763 -13.516 76.840 1.00 48.96 C ANISOU 3541 CG ARG A 475 5406 6183 7013 360 -274 -424 C ATOM 3542 CD ARG A 475 -15.647 -12.969 75.728 1.00 55.85 C ANISOU 3542 CD ARG A 475 7415 7928 5877 728 -559 -581 C ATOM 3543 NE ARG A 475 -16.428 -11.810 76.143 1.00 61.04 N ANISOU 3543 NE ARG A 475 7077 8833 7281 725 -772 -1528 N ATOM 3544 CZ ARG A 475 -17.555 -11.882 76.845 1.00 63.96 C ANISOU 3544 CZ ARG A 475 7307 8165 8828 -282 -206 -882 C ATOM 3545 NH1 ARG A 475 -18.038 -13.064 77.224 1.00 60.31 N ANISOU 3545 NH1 ARG A 475 6559 9070 7284 138 -779 452 N ATOM 3546 NH2 ARG A 475 -18.198 -10.770 77.173 1.00 62.59 N ANISOU 3546 NH2 ARG A 475 6811 8883 8085 542 34 395 N ATOM 3547 N ARG A 476 -12.342 -12.331 74.766 1.00 49.88 N ANISOU 3547 N ARG A 476 6140 5891 6919 247 -199 -420 N ATOM 3548 CA ARG A 476 -11.344 -11.278 74.911 1.00 50.36 C ANISOU 3548 CA ARG A 476 7210 5590 6334 -293 980 -23 C ATOM 3549 C ARG A 476 -11.428 -10.583 76.272 1.00 53.15 C ANISOU 3549 C ARG A 476 7120 6614 6458 1457 1125 -419 C ATOM 3550 O ARG A 476 -12.503 -10.168 76.695 1.00 46.07 O ANISOU 3550 O ARG A 476 5893 7079 4532 -152 1046 -697 O ATOM 3551 CB ARG A 476 -11.459 -10.275 73.765 1.00 50.57 C ANISOU 3551 CB ARG A 476 5610 7179 6423 278 324 461 C ATOM 3552 CG ARG A 476 -10.793 -10.776 72.495 1.00 51.61 C ANISOU 3552 CG ARG A 476 6061 7260 6289 399 -527 -518 C ATOM 3553 CD ARG A 476 -11.184 -9.981 71.264 1.00 52.00 C ANISOU 3553 CD ARG A 476 6540 6603 6612 306 -851 -694 C ATOM 3554 NE ARG A 476 -10.567 -8.653 71.181 1.00 61.07 N ANISOU 3554 NE ARG A 476 7179 7983 8041 -1302 1012 -1736 N ATOM 3555 CZ ARG A 476 -9.276 -8.420 70.946 1.00 56.04 C ANISOU 3555 CZ ARG A 476 6696 6855 7738 -984 -610 -2194 C ATOM 3556 NH1 ARG A 476 -8.412 -9.421 70.801 1.00 56.00 N ANISOU 3556 NH1 ARG A 476 7954 5845 7477 -842 -456 -299 N ATOM 3557 NH2 ARG A 476 -8.843 -7.169 70.871 1.00 48.61 N ANISOU 3557 NH2 ARG A 476 6870 5996 5604 827 -303 -1216 N TER 3558 ARG A 476 HETATM14233 CHA HEM A 501 -28.124 -15.117 41.657 1.00 24.12 C ANISOU14233 CHA HEM A 501 2977 3111 3074 -9 -37 -84 C HETATM14234 CHB HEM A 501 -24.194 -15.968 44.638 1.00 20.36 C ANISOU14234 CHB HEM A 501 2757 2283 2693 -470 88 12 C HETATM14235 CHC HEM A 501 -26.705 -14.359 48.493 1.00 22.71 C ANISOU14235 CHC HEM A 501 2677 3169 2780 181 66 16 C HETATM14236 CHD HEM A 501 -30.801 -14.379 45.654 1.00 25.50 C ANISOU14236 CHD HEM A 501 3505 2951 3233 -595 -3 104 C HETATM14237 C1A HEM A 501 -26.830 -15.439 42.204 1.00 20.56 C ANISOU14237 C1A HEM A 501 2689 2186 2934 -444 42 -183 C HETATM14238 C2A HEM A 501 -25.780 -15.914 41.287 1.00 22.21 C ANISOU14238 C2A HEM A 501 3045 2564 2828 295 -8 215 C HETATM14239 C3A HEM A 501 -24.620 -16.161 42.136 1.00 23.30 C ANISOU14239 C3A HEM A 501 2800 3203 2848 -13 -204 -387 C HETATM14240 C4A HEM A 501 -25.081 -15.814 43.511 1.00 21.28 C ANISOU14240 C4A HEM A 501 2798 2345 2939 -41 -21 -18 C HETATM14241 CMA HEM A 501 -23.289 -16.672 41.675 1.00 21.67 C ANISOU14241 CMA HEM A 501 2772 2490 2972 39 -79 -22 C HETATM14242 CAA HEM A 501 -25.875 -16.103 39.808 1.00 20.92 C ANISOU14242 CAA HEM A 501 2429 2803 2714 129 169 220 C HETATM14243 CBA HEM A 501 -26.660 -17.349 39.519 1.00 24.25 C ANISOU14243 CBA HEM A 501 3034 2843 3336 -87 114 85 C HETATM14244 CGA HEM A 501 -26.555 -17.659 38.054 1.00 28.33 C ANISOU14244 CGA HEM A 501 3660 3753 3351 -311 256 -25 C HETATM14245 O1A HEM A 501 -25.861 -16.909 37.331 1.00 27.46 O ANISOU14245 O1A HEM A 501 3690 3135 3607 -80 479 -129 O HETATM14246 O2A HEM A 501 -27.177 -18.659 37.632 1.00 28.61 O ANISOU14246 O2A HEM A 501 3848 2994 4026 80 429 -307 O HETATM14247 C1B HEM A 501 -24.538 -15.602 45.973 1.00 22.26 C ANISOU14247 C1B HEM A 501 2940 2488 3030 -132 26 -154 C HETATM14248 C2B HEM A 501 -23.505 -15.630 47.022 1.00 22.99 C ANISOU14248 C2B HEM A 501 2917 2985 2833 184 -73 -207 C HETATM14249 C3B HEM A 501 -24.297 -15.146 48.128 1.00 21.99 C ANISOU14249 C3B HEM A 501 2534 2724 3097 -100 318 252 C HETATM14250 C4B HEM A 501 -25.650 -14.904 47.613 1.00 23.26 C ANISOU14250 C4B HEM A 501 3029 2982 2825 164 273 -66 C HETATM14251 CMB HEM A 501 -22.051 -16.037 47.027 1.00 19.57 C ANISOU14251 CMB HEM A 501 2386 2238 2810 -235 801 -104 C HETATM14252 CAB HEM A 501 -23.779 -14.957 49.500 1.00 25.90 C ANISOU14252 CAB HEM A 501 4296 2755 2788 -131 331 306 C HETATM14253 CBB HEM A 501 -24.541 -14.301 50.342 1.00 31.15 C ANISOU14253 CBB HEM A 501 4181 3986 3667 61 591 -372 C HETATM14254 C1C HEM A 501 -28.103 -14.297 48.135 1.00 21.47 C ANISOU14254 C1C HEM A 501 2867 2479 2809 -388 231 80 C HETATM14255 C2C HEM A 501 -29.221 -14.018 49.096 1.00 24.12 C ANISOU14255 C2C HEM A 501 2890 3265 3008 -391 279 381 C HETATM14256 C3C HEM A 501 -30.411 -14.037 48.201 1.00 26.36 C ANISOU14256 C3C HEM A 501 3365 3304 3344 -80 -22 27 C HETATM14257 C4C HEM A 501 -29.933 -14.287 46.821 1.00 25.43 C ANISOU14257 C4C HEM A 501 3176 3187 3297 -359 143 179 C HETATM14258 CMC HEM A 501 -29.080 -13.808 50.596 1.00 23.15 C ANISOU14258 CMC HEM A 501 3053 2858 2882 458 829 -135 C HETATM14259 CAC HEM A 501 -31.847 -13.865 48.551 1.00 32.61 C ANISOU14259 CAC HEM A 501 3850 3813 4724 -352 793 24 C HETATM14260 CBC HEM A 501 -32.182 -13.215 49.649 1.00 36.46 C ANISOU14260 CBC HEM A 501 4262 4544 5045 295 1519 29 C HETATM14261 C1D HEM A 501 -30.403 -14.612 44.261 1.00 29.14 C ANISOU14261 C1D HEM A 501 3415 3918 3737 226 242 -85 C HETATM14262 C2D HEM A 501 -31.427 -14.565 43.199 1.00 27.79 C ANISOU14262 C2D HEM A 501 3325 3699 3533 -140 9 -493 C HETATM14263 C3D HEM A 501 -30.626 -14.784 42.004 1.00 29.22 C ANISOU14263 C3D HEM A 501 3165 4306 3628 -217 217 -288 C HETATM14264 C4D HEM A 501 -29.261 -14.944 42.533 1.00 26.54 C ANISOU14264 C4D HEM A 501 3569 3391 3124 279 150 -3 C HETATM14265 CMD HEM A 501 -32.918 -14.350 43.291 1.00 26.67 C ANISOU14265 CMD HEM A 501 3165 3567 3398 325 101 -214 C HETATM14266 CAD HEM A 501 -31.087 -14.920 40.582 1.00 26.81 C ANISOU14266 CAD HEM A 501 2986 3892 3309 -62 163 -61 C HETATM14267 CBD HEM A 501 -31.408 -13.634 39.916 1.00 33.55 C ANISOU14267 CBD HEM A 501 3861 4239 4646 218 -125 332 C HETATM14268 CGD HEM A 501 -31.924 -13.988 38.543 1.00 34.51 C ANISOU14268 CGD HEM A 501 4117 4724 4268 154 494 -367 C HETATM14269 O1D HEM A 501 -32.076 -15.189 38.181 1.00 33.56 O ANISOU14269 O1D HEM A 501 3969 4264 4519 134 -85 440 O HETATM14270 O2D HEM A 501 -32.175 -13.008 37.818 1.00 46.35 O ANISOU14270 O2D HEM A 501 5454 6179 5976 372 -350 1053 O HETATM14271 NA HEM A 501 -26.407 -15.250 43.584 1.00 22.00 N ANISOU14271 NA HEM A 501 2987 2549 2820 12 -83 -46 N HETATM14272 NB HEM A 501 -25.778 -15.173 46.294 1.00 23.98 N ANISOU14272 NB HEM A 501 3222 2849 3040 -190 206 -227 N HETATM14273 NC HEM A 501 -28.496 -14.300 46.754 1.00 25.47 N ANISOU14273 NC HEM A 501 3281 3300 3097 -323 15 -285 N HETATM14274 ND HEM A 501 -29.123 -14.802 43.851 1.00 24.28 N ANISOU14274 ND HEM A 501 3443 2577 3204 95 221 254 N HETATM14275 FE HEM A 501 -27.545 -14.985 45.188 1.00 25.13 FE ANISOU14275 FE HEM A 501 3099 3184 3266 -114 297 -90 FE HETATM14276 CAO VFV A 502 -34.404 -17.627 41.670 1.00 39.64 C ANISOU14276 CAO VFV A 502 5375 4322 5363 -745 -697 527 C HETATM14277 CAK VFV A 502 -35.497 -16.828 41.355 1.00 40.47 C ANISOU14277 CAK VFV A 502 5245 4524 5606 -394 180 352 C HETATM14278 CBD VFV A 502 -36.278 -16.281 42.367 1.00 42.14 C ANISOU14278 CBD VFV A 502 5086 5550 5373 -413 403 599 C HETATM14279 FAB VFV A 502 -37.356 -15.487 42.032 1.00 43.32 F ANISOU14279 FAB VFV A 502 5319 5477 5660 -781 -207 929 F HETATM14280 CAJ VFV A 502 -35.961 -16.530 43.704 1.00 37.05 C ANISOU14280 CAJ VFV A 502 3753 4834 5488 -1442 421 1641 C HETATM14281 CAN VFV A 502 -34.866 -17.337 44.018 1.00 38.04 C ANISOU14281 CAN VFV A 502 4383 4494 5576 -379 639 402 C HETATM14282 CBG VFV A 502 -34.089 -17.899 43.000 1.00 35.61 C ANISOU14282 CBG VFV A 502 3942 4894 4693 -66 -172 -72 C HETATM14283 CBJ VFV A 502 -32.973 -18.694 43.279 1.00 30.48 C ANISOU14283 CBJ VFV A 502 3923 3863 3792 -198 83 41 C HETATM14284 CAV VFV A 502 -32.943 -19.546 44.378 1.00 23.99 C ANISOU14284 CAV VFV A 502 3011 2790 3311 -510 24 -512 C HETATM14285 CBE VFV A 502 -31.797 -20.303 44.616 1.00 27.75 C ANISOU14285 CBE VFV A 502 3581 3224 3738 12 33 -25 C HETATM14286 FAC VFV A 502 -31.765 -21.098 45.645 1.00 28.31 F ANISOU14286 FAC VFV A 502 3715 3534 3505 -789 43 -85 F HETATM14287 CAR VFV A 502 -31.851 -18.606 42.437 1.00 27.84 C ANISOU14287 CAR VFV A 502 3650 3601 3324 328 -51 -1015 C HETATM14288 CAS VFV A 502 -30.710 -19.377 42.683 1.00 28.94 C ANISOU14288 CAS VFV A 502 3569 3931 3495 207 -243 89 C HETATM14289 CBK VFV A 502 -30.684 -20.242 43.776 1.00 27.21 C ANISOU14289 CBK VFV A 502 3417 3051 3871 -52 76 56 C HETATM14290 CBN VFV A 502 -29.541 -21.018 44.093 1.00 27.28 C ANISOU14290 CBN VFV A 502 2800 3483 4080 -207 134 -190 C HETATM14291 CAW VFV A 502 -28.242 -20.201 43.877 1.00 25.17 C ANISOU14291 CAW VFV A 502 3119 3084 3359 -246 140 47 C HETATM14292 NBO VFV A 502 -28.069 -19.005 44.699 1.00 26.62 N ANISOU14292 NBO VFV A 502 3295 3435 3382 -277 113 -96 N HETATM14293 CAT VFV A 502 -27.767 -18.961 45.996 1.00 21.84 C ANISOU14293 CAT VFV A 502 2156 2980 3160 465 202 -249 C HETATM14294 CAG VFV A 502 -27.672 -17.680 46.340 1.00 23.76 C ANISOU14294 CAG VFV A 502 2670 3050 3305 -80 -403 -62 C HETATM14295 NAX VFV A 502 -27.897 -16.946 45.260 1.00 25.33 N ANISOU14295 NAX VFV A 502 3142 3119 3364 282 40 79 N HETATM14296 CAU VFV A 502 -28.147 -17.761 44.234 1.00 25.38 C ANISOU14296 CAU VFV A 502 3004 3196 3443 307 467 -111 C HETATM14297 NBA VFV A 502 -29.288 -22.218 43.273 1.00 27.01 N ANISOU14297 NBA VFV A 502 2451 3226 4584 -505 -3 -291 N HETATM14298 CBC VFV A 502 -28.606 -23.255 43.834 1.00 31.43 C ANISOU14298 CBC VFV A 502 3752 3995 4194 69 244 389 C HETATM14299 OAA VFV A 502 -28.195 -23.198 44.996 1.00 34.73 O ANISOU14299 OAA VFV A 502 4097 4859 4238 -343 684 -25 O HETATM14300 CBF VFV A 502 -28.186 -24.295 42.982 1.00 31.46 C ANISOU14300 CBF VFV A 502 3973 4202 3776 -96 331 189 C HETATM14301 CAM VFV A 502 -26.914 -24.817 43.217 1.00 34.63 C ANISOU14301 CAM VFV A 502 4211 4315 4629 237 407 -18 C HETATM14302 CAQ VFV A 502 -26.381 -25.819 42.404 1.00 38.17 C ANISOU14302 CAQ VFV A 502 6276 3958 4269 438 -219 -299 C HETATM14303 CAL VFV A 502 -28.914 -24.777 41.891 1.00 30.41 C ANISOU14303 CAL VFV A 502 3566 3955 4031 -512 751 -202 C HETATM14304 CAP VFV A 502 -28.378 -25.783 41.070 1.00 32.43 C ANISOU14304 CAP VFV A 502 4227 3320 4774 -417 30 -489 C HETATM14305 CBI VFV A 502 -27.114 -26.327 41.333 1.00 35.90 C ANISOU14305 CBI VFV A 502 4348 4338 4955 -230 32 129 C HETATM14306 CBM VFV A 502 -26.547 -27.267 40.552 1.00 40.08 C ANISOU14306 CBM VFV A 502 5273 5168 4786 310 -169 -374 C HETATM14307 OBB VFV A 502 -25.130 -27.402 40.406 1.00 39.98 O ANISOU14307 OBB VFV A 502 5241 5441 4508 -181 505 158 O HETATM14308 NAZ VFV A 502 -27.141 -28.152 39.745 1.00 39.33 N ANISOU14308 NAZ VFV A 502 4323 4564 6057 -1099 864 -63 N HETATM14309 NAY VFV A 502 -26.160 -28.844 39.145 1.00 43.23 N ANISOU14309 NAY VFV A 502 5948 5218 5259 -251 973 -299 N HETATM14310 CBL VFV A 502 -24.962 -28.381 39.549 1.00 43.07 C ANISOU14310 CBL VFV A 502 5754 4869 5740 590 202 194 C HETATM14311 CBH VFV A 502 -23.743 -28.806 39.167 1.00 45.52 C ANISOU14311 CBH VFV A 502 5857 5690 5746 810 127 300 C HETATM14312 CAI VFV A 502 -22.625 -28.480 39.946 1.00 43.20 C ANISOU14312 CAI VFV A 502 5570 5158 5685 -682 978 169 C HETATM14313 CAF VFV A 502 -21.340 -28.896 39.589 1.00 39.20 C ANISOU14313 CAF VFV A 502 5573 4326 4992 -58 353 529 C HETATM14314 CAD VFV A 502 -21.169 -29.648 38.425 1.00 40.79 C ANISOU14314 CAD VFV A 502 4955 5931 4609 -312 779 246 C HETATM14315 CAE VFV A 502 -22.271 -29.971 37.633 1.00 45.87 C ANISOU14315 CAE VFV A 502 5393 6266 5767 -727 398 -505 C HETATM14316 CAH VFV A 502 -23.557 -29.552 37.999 1.00 49.54 C ANISOU14316 CAH VFV A 502 6749 6282 5788 1047 766 316 C CONECT 311814275 CONECT 667614359 CONECT1023414443 CONECT1379214527 CONECT142331423714264 CONECT142341424014247 CONECT142351425014254 CONECT142361425714261 CONECT14237142331423814271 CONECT14238142371423914242 CONECT14239142381424014241 CONECT14240142341423914271 CONECT1424114239 CONECT142421423814243 CONECT142431424214244 CONECT14244142431424514246 CONECT1424514244 CONECT1424614244 CONECT14247142341424814272 CONECT14248142471424914251 CONECT14249142481425014252 CONECT14250142351424914272 CONECT1425114248 CONECT142521424914253 CONECT1425314252 CONECT14254142351425514273 CONECT14255142541425614258 CONECT14256142551425714259 CONECT14257142361425614273 CONECT1425814255 CONECT142591425614260 CONECT1426014259 CONECT14261142361426214274 CONECT14262142611426314265 CONECT14263142621426414266 CONECT14264142331426314274 CONECT1426514262 CONECT142661426314267 CONECT142671426614268 CONECT14268142671426914270 CONECT1426914268 CONECT1427014268 CONECT14271142371424014275 CONECT14272142471425014275 CONECT14273142541425714275 CONECT14274142611426414275 CONECT14275 3118142711427214273 CONECT142751427414295 CONECT142761427714282 CONECT142771427614278 CONECT14278142771427914280 CONECT1427914278 CONECT142801427814281 CONECT142811428014282 CONECT14282142761428114283 CONECT14283142821428414287 CONECT142841428314285 CONECT14285142841428614289 CONECT1428614285 CONECT142871428314288 CONECT142881428714289 CONECT14289142851428814290 CONECT14290142891429114297 CONECT142911429014292 CONECT14292142911429314296 CONECT142931429214294 CONECT142941429314295 CONECT14295142751429414296 CONECT142961429214295 CONECT142971429014298 CONECT14298142971429914300 CONECT1429914298 CONECT14300142981430114303 CONECT143011430014302 CONECT143021430114305 CONECT143031430014304 CONECT143041430314305 CONECT14305143021430414306 CONECT14306143051430714308 CONECT143071430614310 CONECT143081430614309 CONECT143091430814310 CONECT14310143071430914311 CONECT14311143101431214316 CONECT143121431114313 CONECT143131431214314 CONECT143141431314315 CONECT143151431414316 CONECT143161431114315 CONECT143171432114348 CONECT143181432414331 CONECT143191433414338 CONECT143201434114345 CONECT14321143171432214355 CONECT14322143211432314326 CONECT14323143221432414325 CONECT14324143181432314355 CONECT1432514323 CONECT143261432214327 CONECT143271432614328 CONECT14328143271432914330 CONECT1432914328 CONECT1433014328 CONECT14331143181433214356 CONECT14332143311433314335 CONECT14333143321433414336 CONECT14334143191433314356 CONECT1433514332 CONECT143361433314337 CONECT1433714336 CONECT14338143191433914357 CONECT14339143381434014342 CONECT14340143391434114343 CONECT14341143201434014357 CONECT1434214339 CONECT143431434014344 CONECT1434414343 CONECT14345143201434614358 CONECT14346143451434714349 CONECT14347143461434814350 CONECT14348143171434714358 CONECT1434914346 CONECT143501434714351 CONECT143511435014352 CONECT14352143511435314354 CONECT1435314352 CONECT1435414352 CONECT14355143211432414359 CONECT14356143311433414359 CONECT14357143381434114359 CONECT14358143451434814359 CONECT14359 6676143551435614357 CONECT143591435814379 CONECT143601436114366 CONECT143611436014362 CONECT14362143611436314364 CONECT1436314362 CONECT143641436214365 CONECT143651436414366 CONECT14366143601436514367 CONECT14367143661436814371 CONECT143681436714369 CONECT14369143681437014373 CONECT1437014369 CONECT143711436714372 CONECT143721437114373 CONECT14373143691437214374 CONECT14374143731437514381 CONECT143751437414376 CONECT14376143751437714380 CONECT143771437614378 CONECT143781437714379 CONECT14379143591437814380 CONECT143801437614379 CONECT143811437414382 CONECT14382143811438314384 CONECT1438314382 CONECT14384143821438514387 CONECT143851438414386 CONECT143861438514389 CONECT143871438414388 CONECT143881438714389 CONECT14389143861438814390 CONECT14390143891439114392 CONECT143911439014394 CONECT143921439014393 CONECT143931439214394 CONECT14394143911439314395 CONECT14395143941439614400 CONECT143961439514397 CONECT143971439614398 CONECT143981439714399 CONECT143991439814400 CONECT144001439514399 CONECT144011440514432 CONECT144021440814415 CONECT144031441814422 CONECT144041442514429 CONECT14405144011440614439 CONECT14406144051440714410 CONECT14407144061440814409 CONECT14408144021440714439 CONECT1440914407 CONECT144101440614411 CONECT144111441014412 CONECT14412144111441314414 CONECT1441314412 CONECT1441414412 CONECT14415144021441614440 CONECT14416144151441714419 CONECT14417144161441814420 CONECT14418144031441714440 CONECT1441914416 CONECT144201441714421 CONECT1442114420 CONECT14422144031442314441 CONECT14423144221442414426 CONECT14424144231442514427 CONECT14425144041442414441 CONECT1442614423 CONECT144271442414428 CONECT1442814427 CONECT14429144041443014442 CONECT14430144291443114433 CONECT14431144301443214434 CONECT14432144011443114442 CONECT1443314430 CONECT144341443114435 CONECT144351443414436 CONECT14436144351443714438 CONECT1443714436 CONECT1443814436 CONECT14439144051440814443 CONECT14440144151441814443 CONECT14441144221442514443 CONECT14442144291443214443 CONECT1444310234144391444014441 CONECT144431444214463 CONECT144441444514450 CONECT144451444414446 CONECT14446144451444714448 CONECT1444714446 CONECT144481444614449 CONECT144491444814450 CONECT14450144441444914451 CONECT14451144501445214455 CONECT144521445114453 CONECT14453144521445414457 CONECT1445414453 CONECT144551445114456 CONECT144561445514457 CONECT14457144531445614458 CONECT14458144571445914465 CONECT144591445814460 CONECT14460144591446114464 CONECT144611446014462 CONECT144621446114463 CONECT14463144431446214464 CONECT144641446014463 CONECT144651445814466 CONECT14466144651446714468 CONECT1446714466 CONECT14468144661446914471 CONECT144691446814470 CONECT144701446914473 CONECT144711446814472 CONECT144721447114473 CONECT14473144701447214474 CONECT14474144731447514476 CONECT144751447414478 CONECT144761447414477 CONECT144771447614478 CONECT14478144751447714479 CONECT14479144781448014484 CONECT144801447914481 CONECT144811448014482 CONECT144821448114483 CONECT144831448214484 CONECT144841447914483 CONECT144851448914516 CONECT144861449214499 CONECT144871450214506 CONECT144881450914513 CONECT14489144851449014523 CONECT14490144891449114494 CONECT14491144901449214493 CONECT14492144861449114523 CONECT1449314491 CONECT144941449014495 CONECT144951449414496 CONECT14496144951449714498 CONECT1449714496 CONECT1449814496 CONECT14499144861450014524 CONECT14500144991450114503 CONECT14501145001450214504 CONECT14502144871450114524 CONECT1450314500 CONECT145041450114505 CONECT1450514504 CONECT14506144871450714525 CONECT14507145061450814510 CONECT14508145071450914511 CONECT14509144881450814525 CONECT1451014507 CONECT145111450814512 CONECT1451214511 CONECT14513144881451414526 CONECT14514145131451514517 CONECT14515145141451614518 CONECT14516144851451514526 CONECT1451714514 CONECT145181451514519 CONECT145191451814520 CONECT14520145191452114522 CONECT1452114520 CONECT1452214520 CONECT14523144891449214527 CONECT14524144991450214527 CONECT14525145061450914527 CONECT14526145131451614527 CONECT1452713792145231452414525 CONECT145271452614547 CONECT145281452914534 CONECT145291452814530 CONECT14530145291453114532 CONECT1453114530 CONECT145321453014533 CONECT145331453214534 CONECT14534145281453314535 CONECT14535145341453614539 CONECT145361453514537 CONECT14537145361453814541 CONECT1453814537 CONECT145391453514540 CONECT145401453914541 CONECT14541145371454014542 CONECT14542145411454314549 CONECT145431454214544 CONECT14544145431454514548 CONECT145451454414546 CONECT145461454514547 CONECT14547145271454614548 CONECT145481454414547 CONECT145491454214550 CONECT14550145491455114552 CONECT1455114550 CONECT14552145501455314555 CONECT145531455214554 CONECT145541455314557 CONECT145551455214556 CONECT145561455514557 CONECT14557145541455614558 CONECT14558145571455914560 CONECT145591455814562 CONECT145601455814561 CONECT145611456014562 CONECT14562145591456114563 CONECT14563145621456414568 CONECT145641456314565 CONECT145651456414566 CONECT145661456514567 CONECT145671456614568 CONECT145681456314567 MASTER 365 0 8 100 48 0 39 615068 4 344 140 END