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*** l ***elNémo ID: 2402130202012570896Job options:ID = 2402130202012570896 JOBID = l USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER l HEADER HYDROLASE 16-MAR-18 5ZIO TITLE CRYSTAL STRUCTURE OF NDM-1 IN COMPLEX WITH L-CAPTOPRIL COMPND MOL_ID: 1; COMPND 2 MOLECULE: METALLO-BETA-LACTAMASE TYPE 2; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: B2 METALLO-BETA-LACTAMASE,BETA-LACTAMASE TYPE II,METALLO- COMPND 5 BETA-LACTAMASE NDM-1,METALLO-BETA-LACTAMASE TYPE II,NEW DELHI COMPND 6 METALLO-BETA-LACTAMASE-1,NDM-1; COMPND 7 EC: 3.5.2.6; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: KLEBSIELLA PNEUMONIAE; SOURCE 3 ORGANISM_TAXID: 573; SOURCE 4 GENE: BLANDM-1; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRHISMBP KEYWDS NDM-1, METALLO-BETA-LACTAMASE, ANTIBIOTIC RESISTENT, INHIBITOR, THIO KEYWDS 2 COMPOUNDS, HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR H.ZHANG,Q.HAO REVDAT 3 22-NOV-23 5ZIO 1 REMARK REVDAT 2 16-DEC-20 5ZIO 1 JRNL REVDAT 1 20-MAR-19 5ZIO 0 JRNL AUTH G.MA,S.WANG,K.WU,W.ZHANG,A.AHMAD,Q.HAO,X.LEI,H.ZHANG JRNL TITL STRUCTURE-GUIDED OPTIMIZATION OF D-CAPTOPRIL FOR DISCOVERY JRNL TITL 2 OF POTENT NDM-1 INHIBITORS JRNL REF BIOORG.MED.CHEM. V. 29 2020 JRNL REFN ESSN 1464-3391 JRNL DOI 10.1016/J.BMC.2020.115902 REMARK 2 REMARK 2 RESOLUTION. 0.98 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.7.0029 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 0.98 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.13 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 90.2 REMARK 3 NUMBER OF REFLECTIONS : 99642 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) : 0.124 REMARK 3 R VALUE (WORKING SET) : 0.124 REMARK 3 FREE R VALUE : 0.137 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 5281 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) : 0.98 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.01 REMARK 3 REFLECTION IN BIN (WORKING SET) : 4693 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 57.55 REMARK 3 BIN R VALUE (WORKING SET) : 0.1860 REMARK 3 BIN FREE R VALUE SET COUNT : 246 REMARK 3 BIN FREE R VALUE : 0.1820 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1697 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 16 REMARK 3 SOLVENT ATOMS : 281 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.19 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.14000 REMARK 3 B22 (A**2) : -0.27000 REMARK 3 B33 (A**2) : 0.37000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.14000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.020 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.020 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.012 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.451 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.983 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.980 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1836 ; 0.009 ; 0.019 REMARK 3 BOND LENGTHS OTHERS (A): 1735 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2504 ; 1.261 ; 1.941 REMARK 3 BOND ANGLES OTHERS (DEGREES): 3996 ; 0.745 ; 3.001 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 248 ; 6.381 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 80 ;31.750 ;24.500 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 286 ;11.718 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;15.438 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 278 ; 0.076 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2152 ; 0.006 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): 427 ; 0.001 ; 0.020 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 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): 1836 ; 1.888 ; 3.000 REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 1778 ; 7.493 ; 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 : NULL 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY REMARK 4 REMARK 4 5ZIO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-MAR-18. REMARK 100 THE DEPOSITION ID IS D_1300007149. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-JAN-12 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL17U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97924 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 104952 REMARK 200 RESOLUTION RANGE HIGH (A) : 0.980 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 90.2 REMARK 200 DATA REDUNDANCY : 7.000 REMARK 200 R MERGE (I) : 0.07300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.98 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.02 REMARK 200 COMPLETENESS FOR SHELL (%) : 63.4 REMARK 200 DATA REDUNDANCY IN SHELL : 3.90 REMARK 200 R MERGE FOR SHELL (I) : 0.26800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 3Q6X REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 39.53 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH5.5, 15% PEG 3350, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 29.97400 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A 2 REMARK 465 GLU A 3 REMARK 465 ILE A 4 REMARK 465 ARG A 5 REMARK 465 PRO A 6 REMARK 465 THR A 7 REMARK 465 ILE A 8 REMARK 465 GLY A 9 REMARK 465 GLN A 10 REMARK 465 GLN A 11 REMARK 465 MET A 12 REMARK 465 GLU A 13 REMARK 465 THR A 14 REMARK 465 GLY A 15 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 ASP A 63 142.89 75.72 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 ZN A 301 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 93 NE2 REMARK 620 2 HIS A 95 ND1 99.3 REMARK 620 3 HIS A 162 NE2 100.5 116.0 REMARK 620 4 X8Z A 303 S 135.6 110.4 95.2 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 302 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 97 OD2 REMARK 620 2 CYS A 181 SG 110.6 REMARK 620 3 HIS A 223 NE2 92.3 106.5 REMARK 620 4 X8Z A 303 S 118.2 110.5 117.2 REMARK 620 N 1 2 3 REMARK 630 REMARK 630 MOLECULE TYPE: NULL REMARK 630 MOLECULE NAME: L-CAPTOPRIL REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 630 REMARK 630 M RES C SSSEQI REMARK 630 X8Z A 303 REMARK 630 SOURCE: NULL REMARK 630 TAXONOMY: NULL REMARK 630 SUBCOMP: PRO CC8 REMARK 630 DETAILS: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue X8Z A 303 DBREF 5ZIO A 2 243 UNP C7C422 BLAN1_KLEPN 29 270 SEQRES 1 A 242 GLY GLU ILE ARG PRO THR ILE GLY GLN GLN MET GLU THR SEQRES 2 A 242 GLY ASP GLN ARG PHE GLY ASP LEU VAL PHE ARG GLN LEU SEQRES 3 A 242 ALA PRO ASN VAL TRP GLN HIS THR SER TYR LEU ASP MET SEQRES 4 A 242 PRO GLY PHE GLY ALA VAL ALA SER ASN GLY LEU ILE VAL SEQRES 5 A 242 ARG ASP GLY GLY ARG VAL LEU VAL VAL ASP THR ALA TRP SEQRES 6 A 242 THR ASP ASP GLN THR ALA GLN ILE LEU ASN TRP ILE LYS SEQRES 7 A 242 GLN GLU ILE ASN LEU PRO VAL ALA LEU ALA VAL VAL THR SEQRES 8 A 242 HIS ALA HIS GLN ASP LYS MET GLY GLY MET ASP ALA LEU SEQRES 9 A 242 HIS ALA ALA GLY ILE ALA THR TYR ALA ASN ALA LEU SER SEQRES 10 A 242 ASN GLN LEU ALA PRO GLN GLU GLY MET VAL ALA ALA GLN SEQRES 11 A 242 HIS SER LEU THR PHE ALA ALA ASN GLY TRP VAL GLU PRO SEQRES 12 A 242 ALA THR ALA PRO ASN PHE GLY PRO LEU LYS VAL PHE TYR SEQRES 13 A 242 PRO GLY PRO GLY HIS THR SER ASP ASN ILE THR VAL GLY SEQRES 14 A 242 ILE ASP GLY THR ASP ILE ALA PHE GLY GLY CYS LEU ILE SEQRES 15 A 242 LYS ASP SER LYS ALA LYS SER LEU GLY ASN LEU GLY ASP SEQRES 16 A 242 ALA ASP THR GLU HIS TYR ALA ALA SER ALA ARG ALA PHE SEQRES 17 A 242 GLY ALA ALA PHE PRO LYS ALA SER MET ILE VAL MET SER SEQRES 18 A 242 HIS SER ALA PRO ASP SER ARG ALA ALA ILE THR HIS THR SEQRES 19 A 242 ALA ARG MET ALA ASP LYS LEU ARG HET ZN A 301 1 HET ZN A 302 1 HET X8Z A 303 14 HETNAM ZN ZINC ION HETNAM X8Z L-CAPTOPRIL FORMUL 2 ZN 2(ZN 2+) FORMUL 4 X8Z C9 H15 N O3 S FORMUL 5 HOH *281(H2 O) HELIX 1 AA1 THR A 67 ILE A 82 1 16 HELIX 2 AA2 HIS A 95 GLY A 100 1 6 HELIX 3 AA3 GLY A 101 ALA A 108 1 8 HELIX 4 AA4 ALA A 116 ALA A 122 1 7 HELIX 5 AA5 GLU A 143 ALA A 147 5 5 HELIX 6 AA6 GLY A 180 ILE A 183 5 4 HELIX 7 AA7 HIS A 201 PHE A 213 1 13 HELIX 8 AA8 ARG A 229 LYS A 241 1 13 SHEET 1 AA1 8 GLN A 17 PHE A 19 0 SHEET 2 AA1 8 LEU A 22 ALA A 28 -1 O PHE A 24 N GLN A 17 SHEET 3 AA1 8 VAL A 31 MET A 40 -1 O GLN A 33 N ARG A 25 SHEET 4 AA1 8 GLY A 44 ASP A 55 -1 O VAL A 46 N LEU A 38 SHEET 5 AA1 8 ARG A 58 VAL A 62 -1 O ARG A 58 N ASP A 55 SHEET 6 AA1 8 VAL A 86 VAL A 91 1 O VAL A 90 N VAL A 61 SHEET 7 AA1 8 ALA A 111 ASN A 115 1 O TYR A 113 N VAL A 91 SHEET 8 AA1 8 HIS A 132 LEU A 134 1 O LEU A 134 N ALA A 114 SHEET 1 AA2 4 LEU A 153 PHE A 156 0 SHEET 2 AA2 4 THR A 168 ILE A 171 -1 O GLY A 170 N LYS A 154 SHEET 3 AA2 4 ILE A 176 PHE A 178 -1 O PHE A 178 N VAL A 169 SHEET 4 AA2 4 MET A 218 VAL A 220 1 O VAL A 220 N ALA A 177 LINK NE2 HIS A 93 ZN ZN A 301 1555 1555 2.07 LINK ND1 HIS A 95 ZN ZN A 301 1555 1555 2.06 LINK OD2 ASP A 97 ZN ZN A 302 1555 1555 1.95 LINK NE2 HIS A 162 ZN ZN A 301 1555 1555 2.09 LINK SG CYS A 181 ZN ZN A 302 1555 1555 2.29 LINK NE2 HIS A 223 ZN ZN A 302 1555 1555 2.10 LINK ZN ZN A 301 S X8Z A 303 1555 1555 2.32 LINK ZN ZN A 302 S X8Z A 303 1555 1555 2.33 SITE 1 AC1 4 HIS A 93 HIS A 95 HIS A 162 X8Z A 303 SITE 1 AC2 4 ASP A 97 CYS A 181 HIS A 223 X8Z A 303 SITE 1 AC3 10 VAL A 46 HIS A 95 ASP A 97 HIS A 162 SITE 2 AC3 10 GLY A 192 ASN A 193 HIS A 223 ZN A 301 SITE 3 AC3 10 ZN A 302 HOH A 405 CRYST1 41.506 59.948 41.904 90.00 98.06 90.00 P 1 21 1 2 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 0.024093 0.000000 0.003411 0.00000 SCALE2 0.000000 0.016681 0.000000 0.00000 SCALE3 0.000000 0.000000 0.024102 0.00000 ATOM 1 N ASP A 16 1.107 21.340 34.694 1.00 20.17 N ANISOU 1 N ASP A 16 2336 2981 2345 7 783 618 N ATOM 2 CA ASP A 16 -0.021 21.764 35.569 1.00 17.22 C ANISOU 2 CA ASP A 16 2280 2504 1757 161 432 764 C ATOM 3 C ASP A 16 -1.331 21.755 34.805 1.00 16.16 C ANISOU 3 C ASP A 16 2482 2151 1507 120 268 565 C ATOM 4 O ASP A 16 -1.414 22.233 33.684 1.00 19.19 O ANISOU 4 O ASP A 16 3148 2628 1516 132 408 713 O ATOM 5 CB ASP A 16 0.206 23.178 36.121 1.00 19.93 C ANISOU 5 CB ASP A 16 2507 2880 2182 278 810 99 C ATOM 6 CG ASP A 16 1.268 23.236 37.197 1.00 21.13 C ANISOU 6 CG ASP A 16 2566 2979 2481 108 710 271 C ATOM 7 OD1 ASP A 16 1.588 22.190 37.784 1.00 23.35 O ANISOU 7 OD1 ASP A 16 2897 3555 2419 36 886 925 O ATOM 8 OD2 ASP A 16 1.784 24.344 37.460 1.00 25.05 O ANISOU 8 OD2 ASP A 16 3672 3091 2755 -121 573 142 O ATOM 9 N GLN A 17 -2.360 21.233 35.439 1.00 14.85 N ANISOU 9 N GLN A 17 2357 2096 1187 285 310 372 N ATOM 10 CA GLN A 17 -3.701 21.286 34.913 1.00 14.77 C ANISOU 10 CA GLN A 17 2592 1792 1225 415 -14 271 C ATOM 11 C GLN A 17 -4.520 22.261 35.734 1.00 13.59 C ANISOU 11 C GLN A 17 2387 1722 1052 278 -3 342 C ATOM 12 O GLN A 17 -4.754 22.029 36.918 1.00 14.23 O ANISOU 12 O GLN A 17 2551 1756 1097 154 21 433 O ATOM 13 CB GLN A 17 -4.301 19.892 34.972 1.00 16.31 C ANISOU 13 CB GLN A 17 2941 1782 1474 400 86 78 C ATOM 14 CG GLN A 17 -5.561 19.700 34.159 1.00 20.21 C ANISOU 14 CG GLN A 17 2872 2750 2057 248 8 161 C ATOM 15 CD GLN A 17 -6.220 18.355 34.417 1.00 21.81 C ANISOU 15 CD GLN A 17 3142 2691 2453 141 -168 94 C ATOM 16 OE1 GLN A 17 -5.583 17.408 34.896 1.00 20.44 O ANISOU 16 OE1 GLN A 17 3245 2345 2174 43 209 104 O ATOM 17 NE2 GLN A 17 -7.512 18.268 34.117 1.00 24.98 N ANISOU 17 NE2 GLN A 17 3129 3278 3083 53 -167 66 N ATOM 18 N ARG A 18 -4.941 23.356 35.113 1.00 13.29 N ANISOU 18 N ARG A 18 2341 1763 946 263 -14 366 N ATOM 19 CA ARG A 18 -5.835 24.296 35.755 1.00 13.32 C ANISOU 19 CA ARG A 18 2125 1678 1255 232 -23 411 C ATOM 20 C ARG A 18 -7.233 23.732 35.626 1.00 13.58 C ANISOU 20 C ARG A 18 2267 1766 1127 49 -94 372 C ATOM 21 O ARG A 18 -7.666 23.367 34.542 1.00 18.87 O ANISOU 21 O ARG A 18 2786 3134 1247 -288 -160 77 O ATOM 22 CB ARG A 18 -5.744 25.682 35.103 1.00 14.25 C ANISOU 22 CB ARG A 18 2430 1703 1280 320 -12 497 C ATOM 23 CG ARG A 18 -4.367 26.321 35.195 1.00 14.26 C ANISOU 23 CG ARG A 18 2574 1733 1110 160 165 399 C ATOM 24 CD ARG A 18 -4.368 27.761 34.716 1.00 14.56 C ANISOU 24 CD ARG A 18 2686 1585 1258 169 70 214 C ATOM 25 NE ARG A 18 -4.673 27.865 33.294 1.00 14.09 N ANISOU 25 NE ARG A 18 2630 1442 1279 124 78 234 N ATOM 26 CZ ARG A 18 -3.779 27.843 32.307 1.00 13.26 C ANISOU 26 CZ ARG A 18 2497 1199 1340 83 16 142 C ATOM 27 NH1 ARG A 18 -2.479 27.714 32.542 1.00 16.12 N ANISOU 27 NH1 ARG A 18 2482 1781 1861 144 86 47 N ATOM 28 NH2 ARG A 18 -4.201 27.955 31.065 1.00 14.21 N ANISOU 28 NH2 ARG A 18 2732 1417 1246 410 114 153 N ATOM 29 N PHE A 19 -7.927 23.637 36.749 1.00 12.86 N ANISOU 29 N PHE A 19 1983 1695 1209 74 -121 327 N ATOM 30 CA PHE A 19 -9.258 23.062 36.779 1.00 13.02 C ANISOU 30 CA PHE A 19 2041 1687 1216 -10 -343 316 C ATOM 31 C PHE A 19 -10.074 23.942 37.696 1.00 14.24 C ANISOU 31 C PHE A 19 2080 1726 1604 121 -357 189 C ATOM 32 O PHE A 19 -9.890 23.928 38.911 1.00 13.77 O ANISOU 32 O PHE A 19 1975 1693 1561 42 -36 3 O ATOM 33 CB PHE A 19 -9.186 21.621 37.267 1.00 13.78 C ANISOU 33 CB PHE A 19 2160 1625 1450 78 -360 221 C ATOM 34 CG PHE A 19 -10.507 20.902 37.284 1.00 13.85 C ANISOU 34 CG PHE A 19 2252 1716 1292 -28 -355 316 C ATOM 35 CD1 PHE A 19 -11.313 20.947 38.413 1.00 13.75 C ANISOU 35 CD1 PHE A 19 2223 1672 1329 18 -335 251 C ATOM 36 CD2 PHE A 19 -10.925 20.142 36.199 1.00 15.83 C ANISOU 36 CD2 PHE A 19 2452 1980 1579 -102 -319 54 C ATOM 37 CE1 PHE A 19 -12.521 20.274 38.457 1.00 15.49 C ANISOU 37 CE1 PHE A 19 2215 1998 1673 -83 -268 236 C ATOM 38 CE2 PHE A 19 -12.133 19.460 36.240 1.00 17.21 C ANISOU 38 CE2 PHE A 19 2500 2221 1818 -204 -310 -20 C ATOM 39 CZ PHE A 19 -12.932 19.529 37.369 1.00 16.23 C ANISOU 39 CZ PHE A 19 2217 2027 1920 -155 -338 148 C ATOM 40 N GLY A 20 -10.942 24.748 37.095 1.00 16.85 N ANISOU 40 N GLY A 20 2271 1980 2150 424 -679 -84 N ATOM 41 CA GLY A 20 -11.531 25.876 37.787 1.00 16.89 C ANISOU 41 CA GLY A 20 2153 2171 2091 422 -417 -77 C ATOM 42 C GLY A 20 -10.418 26.709 38.386 1.00 15.18 C ANISOU 42 C GLY A 20 2109 1943 1716 667 -442 -113 C ATOM 43 O GLY A 20 -9.437 27.043 37.715 1.00 16.77 O ANISOU 43 O GLY A 20 2545 2061 1765 631 -321 101 O ATOM 44 N ASP A 21 -10.542 26.992 39.673 1.00 13.23 N ANISOU 44 N ASP A 21 1751 1614 1660 380 -272 35 N ATOM 45 CA ASP A 21 -9.589 27.834 40.373 1.00 11.64 C ANISOU 45 CA ASP A 21 1605 1376 1443 249 -139 296 C ATOM 46 C ASP A 21 -8.506 27.033 41.095 1.00 10.07 C ANISOU 46 C ASP A 21 1344 1236 1246 136 13 249 C ATOM 47 O ASP A 21 -7.762 27.607 41.886 1.00 11.16 O ANISOU 47 O ASP A 21 1557 1347 1333 116 -120 180 O ATOM 48 CB ASP A 21 -10.335 28.729 41.367 1.00 11.93 C ANISOU 48 CB ASP A 21 1584 1354 1593 174 -36 267 C ATOM 49 CG ASP A 21 -9.609 30.023 41.658 1.00 11.80 C ANISOU 49 CG ASP A 21 1714 1332 1436 184 -4 274 C ATOM 50 OD1 ASP A 21 -9.145 30.682 40.707 1.00 12.29 O ANISOU 50 OD1 ASP A 21 1717 1502 1448 164 112 297 O ATOM 51 OD2 ASP A 21 -9.524 30.390 42.847 1.00 13.02 O ANISOU 51 OD2 ASP A 21 1874 1631 1440 65 252 217 O ATOM 52 N LEU A 22 -8.422 25.729 40.820 1.00 9.76 N ANISOU 52 N LEU A 22 1339 1275 1093 159 48 222 N ATOM 53 CA LEU A 22 -7.438 24.847 41.424 1.00 10.00 C ANISOU 53 CA LEU A 22 1363 1346 1089 183 37 278 C ATOM 54 C LEU A 22 -6.423 24.409 40.375 1.00 10.08 C ANISOU 54 C LEU A 22 1512 1284 1033 254 29 287 C ATOM 55 O LEU A 22 -6.618 24.598 39.169 1.00 10.66 O ANISOU 55 O LEU A 22 1508 1518 1022 179 26 312 O ATOM 56 CB LEU A 22 -8.123 23.627 42.049 1.00 10.74 C ANISOU 56 CB LEU A 22 1449 1346 1282 182 237 209 C ATOM 57 CG LEU A 22 -8.845 23.869 43.384 1.00 11.93 C ANISOU 57 CG LEU A 22 1617 1453 1462 116 413 196 C ATOM 58 CD1 LEU A 22 -10.177 24.582 43.184 1.00 13.53 C ANISOU 58 CD1 LEU A 22 1730 1542 1866 248 411 176 C ATOM 59 CD2 LEU A 22 -9.047 22.544 44.105 1.00 13.47 C ANISOU 59 CD2 LEU A 22 1945 1474 1696 208 408 249 C ATOM 60 N VAL A 23 -5.324 23.835 40.852 1.00 10.06 N ANISOU 60 N VAL A 23 1450 1440 932 320 158 319 N ATOM 61 CA VAL A 23 -4.275 23.315 39.984 1.00 10.08 C ANISOU 61 CA VAL A 23 1551 1302 975 307 197 302 C ATOM 62 C VAL A 23 -3.938 21.884 40.419 1.00 10.32 C ANISOU 62 C VAL A 23 1761 1321 837 290 6 300 C ATOM 63 O VAL A 23 -3.846 21.600 41.610 1.00 10.27 O ANISOU 63 O VAL A 23 1753 1332 814 388 88 233 O ATOM 64 CB VAL A 23 -3.015 24.219 39.994 1.00 10.81 C ANISOU 64 CB VAL A 23 1512 1487 1108 225 285 312 C ATOM 65 CG1 VAL A 23 -1.911 23.622 39.127 1.00 12.74 C ANISOU 65 CG1 VAL A 23 1674 1727 1437 161 515 209 C ATOM 66 CG2 VAL A 23 -3.358 25.630 39.516 1.00 11.99 C ANISOU 66 CG2 VAL A 23 1754 1490 1307 185 46 366 C ATOM 67 N PHE A 24 -3.796 20.996 39.440 1.00 10.30 N ANISOU 67 N PHE A 24 1727 1315 869 258 108 288 N ATOM 68 CA PHE A 24 -3.468 19.593 39.674 1.00 10.42 C ANISOU 68 CA PHE A 24 1727 1362 870 359 223 114 C ATOM 69 C PHE A 24 -2.199 19.256 38.911 1.00 10.46 C ANISOU 69 C PHE A 24 1710 1403 858 232 265 180 C ATOM 70 O PHE A 24 -2.024 19.676 37.771 1.00 12.52 O ANISOU 70 O PHE A 24 2069 1779 906 458 379 307 O ATOM 71 CB PHE A 24 -4.625 18.687 39.249 1.00 10.89 C ANISOU 71 CB PHE A 24 1788 1460 888 323 82 96 C ATOM 72 CG PHE A 24 -5.876 18.942 40.028 1.00 10.50 C ANISOU 72 CG PHE A 24 1701 1473 815 274 38 79 C ATOM 73 CD1 PHE A 24 -6.724 19.987 39.676 1.00 11.49 C ANISOU 73 CD1 PHE A 24 1760 1586 1016 316 15 229 C ATOM 74 CD2 PHE A 24 -6.173 18.203 41.165 1.00 10.31 C ANISOU 74 CD2 PHE A 24 1641 1336 940 135 57 90 C ATOM 75 CE1 PHE A 24 -7.854 20.258 40.431 1.00 11.93 C ANISOU 75 CE1 PHE A 24 1674 1728 1128 318 23 251 C ATOM 76 CE2 PHE A 24 -7.306 18.467 41.909 1.00 10.73 C ANISOU 76 CE2 PHE A 24 1519 1647 909 10 78 169 C ATOM 77 CZ PHE A 24 -8.140 19.500 41.543 1.00 11.34 C ANISOU 77 CZ PHE A 24 1579 1651 1077 74 2 127 C ATOM 78 N ARG A 25 -1.305 18.499 39.540 1.00 10.67 N ANISOU 78 N ARG A 25 1774 1426 851 347 431 275 N ATOM 79 CA AARG A 25 -0.028 18.132 38.936 0.56 11.16 C ANISOU 79 CA AARG A 25 1785 1431 1022 325 454 203 C ATOM 80 CA BARG A 25 -0.032 18.134 38.931 0.44 11.23 C ANISOU 80 CA BARG A 25 1787 1444 1036 345 452 222 C ATOM 81 C ARG A 25 0.266 16.670 39.216 1.00 10.62 C ANISOU 81 C ARG A 25 1661 1396 978 237 416 216 C ATOM 82 O ARG A 25 0.323 16.259 40.372 1.00 10.60 O ANISOU 82 O ARG A 25 1663 1411 952 280 381 157 O ATOM 83 CB AARG A 25 1.103 18.986 39.518 0.56 12.95 C ANISOU 83 CB AARG A 25 1922 1398 1599 92 552 173 C ATOM 84 CB BARG A 25 1.092 19.010 39.495 0.44 13.41 C ANISOU 84 CB BARG A 25 2002 1457 1635 127 445 213 C ATOM 85 CG AARG A 25 2.486 18.618 38.990 0.56 15.23 C ANISOU 85 CG AARG A 25 1945 1814 2025 56 646 84 C ATOM 86 CG BARG A 25 2.455 18.773 38.857 0.44 15.93 C ANISOU 86 CG BARG A 25 2032 1917 2102 147 552 252 C ATOM 87 CD AARG A 25 3.603 19.393 39.673 0.56 16.51 C ANISOU 87 CD AARG A 25 1966 2062 2245 80 491 37 C ATOM 88 CD BARG A 25 3.565 19.537 39.565 0.44 19.48 C ANISOU 88 CD BARG A 25 2369 2425 2606 -31 286 92 C ATOM 89 NE AARG A 25 3.624 20.794 39.265 0.56 17.24 N ANISOU 89 NE AARG A 25 2283 2030 2238 0 417 -2 N ATOM 90 NE BARG A 25 4.826 18.798 39.547 0.44 22.98 N ANISOU 90 NE BARG A 25 2430 3042 3259 163 209 -42 N ATOM 91 CZ AARG A 25 4.532 21.691 39.651 0.56 19.03 C ANISOU 91 CZ AARG A 25 2347 2310 2573 -78 40 118 C ATOM 92 CZ BARG A 25 5.973 19.251 40.046 0.44 23.06 C ANISOU 92 CZ BARG A 25 2536 2702 3523 66 149 35 C ATOM 93 NH1AARG A 25 5.523 21.352 40.475 0.56 20.19 N ANISOU 93 NH1AARG A 25 2635 2515 2520 -30 -35 267 N ATOM 94 NH1BARG A 25 6.034 20.455 40.598 0.44 22.99 N ANISOU 94 NH1BARG A 25 2528 2854 3353 124 219 -86 N ATOM 95 NH2AARG A 25 4.445 22.944 39.216 0.56 19.43 N ANISOU 95 NH2AARG A 25 2302 2291 2787 -67 -83 137 N ATOM 96 NH2BARG A 25 7.063 18.500 39.987 0.44 24.83 N ANISOU 96 NH2BARG A 25 2358 3016 4060 68 -36 104 N ATOM 97 N GLN A 26 0.467 15.876 38.170 1.00 11.68 N ANISOU 97 N GLN A 26 1936 1512 989 302 393 142 N ATOM 98 CA GLN A 26 0.840 14.489 38.355 1.00 10.88 C ANISOU 98 CA GLN A 26 1754 1462 916 198 393 77 C ATOM 99 C GLN A 26 2.289 14.406 38.823 1.00 10.99 C ANISOU 99 C GLN A 26 1707 1339 1130 37 355 -7 C ATOM 100 O GLN A 26 3.185 14.989 38.202 1.00 13.57 O ANISOU 100 O GLN A 26 1844 1725 1585 77 560 365 O ATOM 101 CB GLN A 26 0.666 13.683 37.083 1.00 11.91 C ANISOU 101 CB GLN A 26 1801 1696 1024 239 319 -63 C ATOM 102 CG GLN A 26 0.849 12.203 37.345 1.00 13.17 C ANISOU 102 CG GLN A 26 2065 1655 1281 208 68 -178 C ATOM 103 CD GLN A 26 0.438 11.346 36.181 1.00 15.53 C ANISOU 103 CD GLN A 26 2537 1854 1508 327 -151 -350 C ATOM 104 OE1 GLN A 26 0.384 11.805 35.040 1.00 19.25 O ANISOU 104 OE1 GLN A 26 3489 2246 1577 86 -148 -198 O ATOM 105 NE2 GLN A 26 0.153 10.086 36.459 1.00 17.96 N ANISOU 105 NE2 GLN A 26 2712 1908 2204 67 -221 -397 N ATOM 106 N LEU A 27 2.503 13.670 39.914 1.00 9.98 N ANISOU 106 N LEU A 27 1340 1232 1220 45 272 -29 N ATOM 107 CA LEU A 27 3.834 13.483 40.494 1.00 10.58 C ANISOU 107 CA LEU A 27 1335 1335 1346 70 211 -123 C ATOM 108 C LEU A 27 4.428 12.105 40.256 1.00 11.58 C ANISOU 108 C LEU A 27 1344 1482 1570 116 232 -288 C ATOM 109 O LEU A 27 5.643 11.944 40.305 1.00 14.19 O ANISOU 109 O LEU A 27 1369 1715 2305 161 292 -367 O ATOM 110 CB LEU A 27 3.798 13.700 42.002 1.00 11.13 C ANISOU 110 CB LEU A 27 1326 1531 1370 168 122 -209 C ATOM 111 CG LEU A 27 3.254 15.040 42.482 1.00 11.52 C ANISOU 111 CG LEU A 27 1466 1554 1356 208 -39 -302 C ATOM 112 CD1 LEU A 27 3.408 15.131 43.992 1.00 12.02 C ANISOU 112 CD1 LEU A 27 1334 1853 1378 303 -60 -198 C ATOM 113 CD2 LEU A 27 3.962 16.195 41.795 1.00 13.23 C ANISOU 113 CD2 LEU A 27 1884 1478 1665 87 -158 -259 C ATOM 114 N ALA A 28 3.571 11.121 40.023 1.00 11.61 N ANISOU 114 N ALA A 28 1455 1358 1596 99 258 -180 N ATOM 115 CA ALA A 28 3.969 9.728 39.842 1.00 12.25 C ANISOU 115 CA ALA A 28 1675 1458 1519 223 374 -301 C ATOM 116 C ALA A 28 2.801 9.042 39.167 1.00 11.89 C ANISOU 116 C ALA A 28 1800 1242 1475 25 461 -199 C ATOM 117 O ALA A 28 1.723 9.608 39.107 1.00 12.30 O ANISOU 117 O ALA A 28 1696 1436 1539 -20 478 -321 O ATOM 118 CB ALA A 28 4.267 9.074 41.189 1.00 13.41 C ANISOU 118 CB ALA A 28 1832 1495 1768 311 229 -147 C ATOM 119 N PRO A 29 2.982 7.810 38.671 1.00 13.01 N ANISOU 119 N PRO A 29 1919 1507 1515 178 615 -467 N ATOM 120 CA PRO A 29 1.882 7.145 37.958 1.00 14.69 C ANISOU 120 CA PRO A 29 2088 1633 1860 -62 586 -484 C ATOM 121 C PRO A 29 0.506 7.161 38.671 1.00 13.11 C ANISOU 121 C PRO A 29 1914 1692 1373 -14 193 -365 C ATOM 122 O PRO A 29 -0.538 7.312 38.036 1.00 14.48 O ANISOU 122 O PRO A 29 2223 2000 1276 40 34 -358 O ATOM 123 CB PRO A 29 2.427 5.728 37.777 1.00 15.74 C ANISOU 123 CB PRO A 29 2329 1716 1934 -13 908 -655 C ATOM 124 CG PRO A 29 3.893 5.956 37.566 1.00 16.09 C ANISOU 124 CG PRO A 29 2164 1637 2310 225 559 -543 C ATOM 125 CD PRO A 29 4.237 7.040 38.556 1.00 14.57 C ANISOU 125 CD PRO A 29 2077 1528 1931 313 611 -394 C ATOM 126 N ASN A 30 0.522 7.035 39.991 1.00 11.86 N ANISOU 126 N ASN A 30 1856 1290 1361 -1 377 -251 N ATOM 127 CA ASN A 30 -0.701 6.947 40.798 1.00 11.16 C ANISOU 127 CA ASN A 30 1684 1284 1272 -5 244 -288 C ATOM 128 C ASN A 30 -0.837 8.088 41.819 1.00 9.75 C ANISOU 128 C ASN A 30 1397 1168 1138 87 251 -137 C ATOM 129 O ASN A 30 -1.614 7.964 42.765 1.00 10.42 O ANISOU 129 O ASN A 30 1499 1134 1325 -149 407 -250 O ATOM 130 CB ASN A 30 -0.731 5.615 41.566 1.00 11.38 C ANISOU 130 CB ASN A 30 1662 1142 1518 -55 334 -318 C ATOM 131 CG ASN A 30 -0.961 4.400 40.674 1.00 12.65 C ANISOU 131 CG ASN A 30 2028 1206 1572 -114 265 -354 C ATOM 132 OD1 ASN A 30 -0.507 4.343 39.530 1.00 14.93 O ANISOU 132 OD1 ASN A 30 2566 1482 1625 -374 409 -471 O ATOM 133 ND2 ASN A 30 -1.655 3.407 41.215 1.00 13.41 N ANISOU 133 ND2 ASN A 30 2082 1364 1649 -236 279 -345 N ATOM 134 N VAL A 31 -0.093 9.181 41.648 1.00 9.36 N ANISOU 134 N VAL A 31 1338 1183 1034 120 307 -180 N ATOM 135 CA VAL A 31 -0.083 10.265 42.630 1.00 9.21 C ANISOU 135 CA VAL A 31 1323 1085 1088 35 151 -134 C ATOM 136 C VAL A 31 -0.160 11.624 41.943 1.00 8.70 C ANISOU 136 C VAL A 31 1252 1120 933 58 125 -90 C ATOM 137 O VAL A 31 0.622 11.910 41.022 1.00 9.52 O ANISOU 137 O VAL A 31 1343 1172 1102 47 247 -58 O ATOM 138 CB VAL A 31 1.183 10.226 43.515 1.00 9.74 C ANISOU 138 CB VAL A 31 1307 1215 1179 40 157 -39 C ATOM 139 CG1 VAL A 31 1.117 11.296 44.600 1.00 9.72 C ANISOU 139 CG1 VAL A 31 1289 1312 1091 -25 113 -35 C ATOM 140 CG2 VAL A 31 1.366 8.851 44.149 1.00 10.45 C ANISOU 140 CG2 VAL A 31 1371 1301 1296 91 45 73 C ATOM 141 N TRP A 32 -1.080 12.455 42.437 1.00 8.96 N ANISOU 141 N TRP A 32 1311 1120 970 119 165 -31 N ATOM 142 CA TRP A 32 -1.242 13.820 41.966 1.00 8.85 C ANISOU 142 CA TRP A 32 1252 1139 971 84 284 -14 C ATOM 143 C TRP A 32 -1.247 14.770 43.154 1.00 8.68 C ANISOU 143 C TRP A 32 1218 1092 985 88 265 19 C ATOM 144 O TRP A 32 -1.722 14.426 44.250 1.00 9.50 O ANISOU 144 O TRP A 32 1415 1134 1060 -54 428 -40 O ATOM 145 CB TRP A 32 -2.560 13.979 41.204 1.00 9.96 C ANISOU 145 CB TRP A 32 1432 1314 1039 183 116 -85 C ATOM 146 CG TRP A 32 -2.704 13.108 39.994 1.00 11.30 C ANISOU 146 CG TRP A 32 1502 1728 1063 183 115 -211 C ATOM 147 CD1 TRP A 32 -2.521 13.484 38.693 1.00 12.99 C ANISOU 147 CD1 TRP A 32 1701 2147 1086 3 48 -99 C ATOM 148 CD2 TRP A 32 -3.081 11.720 39.962 1.00 12.35 C ANISOU 148 CD2 TRP A 32 1498 1776 1416 130 58 -379 C ATOM 149 NE1 TRP A 32 -2.755 12.422 37.858 1.00 15.56 N ANISOU 149 NE1 TRP A 32 2031 2646 1233 -62 99 -464 N ATOM 150 CE2 TRP A 32 -3.109 11.330 38.607 1.00 14.59 C ANISOU 150 CE2 TRP A 32 1806 2247 1488 178 168 -584 C ATOM 151 CE3 TRP A 32 -3.411 10.775 40.947 1.00 12.97 C ANISOU 151 CE3 TRP A 32 1328 1865 1735 105 95 -197 C ATOM 152 CZ2 TRP A 32 -3.436 10.031 38.209 1.00 17.58 C ANISOU 152 CZ2 TRP A 32 2275 2385 2019 34 18 -762 C ATOM 153 CZ3 TRP A 32 -3.746 9.486 40.548 1.00 15.03 C ANISOU 153 CZ3 TRP A 32 1673 1860 2177 83 12 -216 C ATOM 154 CH2 TRP A 32 -3.748 9.126 39.188 1.00 16.99 C ANISOU 154 CH2 TRP A 32 1991 2063 2398 217 96 -686 C ATOM 155 N GLN A 33 -0.742 15.977 42.939 1.00 8.65 N ANISOU 155 N GLN A 33 1360 1068 858 146 290 159 N ATOM 156 CA GLN A 33 -0.818 17.071 43.902 1.00 8.18 C ANISOU 156 CA GLN A 33 1209 1091 806 189 289 175 C ATOM 157 C GLN A 33 -1.997 17.971 43.554 1.00 8.10 C ANISOU 157 C GLN A 33 1219 945 910 148 133 135 C ATOM 158 O GLN A 33 -2.120 18.399 42.406 1.00 9.09 O ANISOU 158 O GLN A 33 1239 1263 948 324 235 236 O ATOM 159 CB GLN A 33 0.481 17.868 43.854 1.00 9.23 C ANISOU 159 CB GLN A 33 1170 1111 1225 184 33 110 C ATOM 160 CG GLN A 33 0.563 18.967 44.890 1.00 8.96 C ANISOU 160 CG GLN A 33 1063 1179 1160 136 114 128 C ATOM 161 CD GLN A 33 1.843 19.752 44.770 1.00 9.28 C ANISOU 161 CD GLN A 33 1030 1241 1254 128 128 119 C ATOM 162 OE1 GLN A 33 2.731 19.634 45.606 1.00 10.94 O ANISOU 162 OE1 GLN A 33 1154 1628 1375 -59 18 254 O ATOM 163 NE2 GLN A 33 1.970 20.521 43.695 1.00 10.38 N ANISOU 163 NE2 GLN A 33 1212 1377 1355 8 -6 272 N ATOM 164 N HIS A 34 -2.843 18.260 44.547 1.00 7.91 N ANISOU 164 N HIS A 34 1105 939 959 167 106 87 N ATOM 165 CA HIS A 34 -3.886 19.269 44.409 1.00 7.87 C ANISOU 165 CA HIS A 34 1025 1016 947 148 28 175 C ATOM 166 C HIS A 34 -3.445 20.555 45.043 1.00 7.52 C ANISOU 166 C HIS A 34 958 1047 850 155 104 208 C ATOM 167 O HIS A 34 -2.802 20.532 46.088 1.00 7.91 O ANISOU 167 O HIS A 34 1091 959 955 101 -22 182 O ATOM 168 CB HIS A 34 -5.235 18.767 44.962 1.00 8.01 C ANISOU 168 CB HIS A 34 1064 1099 879 78 19 43 C ATOM 169 CG HIS A 34 -5.335 18.530 46.449 1.00 7.38 C ANISOU 169 CG HIS A 34 943 927 931 93 -52 73 C ATOM 170 ND1 HIS A 34 -5.497 19.547 47.369 1.00 7.03 N ANISOU 170 ND1 HIS A 34 890 897 882 44 48 140 N ATOM 171 CD2 HIS A 34 -5.474 17.365 47.132 1.00 7.41 C ANISOU 171 CD2 HIS A 34 1006 969 839 105 -10 58 C ATOM 172 CE1 HIS A 34 -5.698 19.001 48.558 1.00 6.98 C ANISOU 172 CE1 HIS A 34 845 901 903 39 19 115 C ATOM 173 NE2 HIS A 34 -5.686 17.683 48.443 1.00 7.45 N ANISOU 173 NE2 HIS A 34 1026 926 878 99 -21 101 N ATOM 174 N THR A 35 -3.778 21.677 44.399 1.00 7.76 N ANISOU 174 N THR A 35 1091 1069 788 162 48 210 N ATOM 175 CA THR A 35 -3.411 22.978 44.901 1.00 8.22 C ANISOU 175 CA THR A 35 1177 1033 912 176 48 210 C ATOM 176 C THR A 35 -4.632 23.896 44.853 1.00 8.02 C ANISOU 176 C THR A 35 1151 991 904 130 97 275 C ATOM 177 O THR A 35 -5.307 24.006 43.813 1.00 9.20 O ANISOU 177 O THR A 35 1357 1256 880 361 50 221 O ATOM 178 CB THR A 35 -2.279 23.605 44.066 1.00 8.92 C ANISOU 178 CB THR A 35 1203 1157 1027 227 85 299 C ATOM 179 OG1 THR A 35 -1.167 22.700 44.025 1.00 9.34 O ANISOU 179 OG1 THR A 35 1153 1180 1213 182 211 170 O ATOM 180 CG2 THR A 35 -1.839 24.944 44.622 1.00 9.19 C ANISOU 180 CG2 THR A 35 1184 1163 1143 187 268 293 C ATOM 181 N SER A 36 -4.870 24.586 45.962 1.00 8.05 N ANISOU 181 N SER A 36 1165 919 973 219 2 208 N ATOM 182 CA SER A 36 -5.975 25.527 46.092 1.00 7.87 C ANISOU 182 CA SER A 36 1097 976 918 218 97 271 C ATOM 183 C SER A 36 -5.457 26.806 46.729 1.00 7.87 C ANISOU 183 C SER A 36 1068 999 923 181 177 291 C ATOM 184 O SER A 36 -4.412 26.811 47.380 1.00 8.17 O ANISOU 184 O SER A 36 1115 927 1061 152 87 282 O ATOM 185 CB SER A 36 -7.113 24.922 46.915 1.00 8.18 C ANISOU 185 CB SER A 36 1140 948 1019 99 63 257 C ATOM 186 OG SER A 36 -6.725 24.579 48.240 1.00 7.94 O ANISOU 186 OG SER A 36 1083 1007 924 154 219 229 O ATOM 187 N TYR A 37 -6.202 27.892 46.535 1.00 8.54 N ANISOU 187 N TYR A 37 1212 959 1074 157 43 343 N ATOM 188 CA TYR A 37 -5.748 29.234 46.905 1.00 9.40 C ANISOU 188 CA TYR A 37 1396 944 1229 160 57 265 C ATOM 189 C TYR A 37 -6.766 29.948 47.757 1.00 9.52 C ANISOU 189 C TYR A 37 1377 811 1428 217 48 267 C ATOM 190 O TYR A 37 -7.968 29.887 47.481 1.00 10.40 O ANISOU 190 O TYR A 37 1348 1121 1482 275 22 155 O ATOM 191 CB TYR A 37 -5.513 30.085 45.634 1.00 10.47 C ANISOU 191 CB TYR A 37 1637 893 1445 260 41 443 C ATOM 192 CG TYR A 37 -4.424 29.527 44.767 1.00 11.31 C ANISOU 192 CG TYR A 37 1856 1166 1273 348 160 569 C ATOM 193 CD1 TYR A 37 -4.693 28.532 43.838 1.00 13.04 C ANISOU 193 CD1 TYR A 37 2507 1092 1353 446 178 514 C ATOM 194 CD2 TYR A 37 -3.109 29.960 44.907 1.00 13.85 C ANISOU 194 CD2 TYR A 37 1854 1826 1581 282 120 874 C ATOM 195 CE1 TYR A 37 -3.681 27.962 43.086 1.00 15.06 C ANISOU 195 CE1 TYR A 37 2958 1375 1388 580 448 600 C ATOM 196 CE2 TYR A 37 -2.091 29.410 44.145 1.00 16.13 C ANISOU 196 CE2 TYR A 37 2119 2225 1785 650 262 1053 C ATOM 197 CZ TYR A 37 -2.386 28.406 43.244 1.00 16.07 C ANISOU 197 CZ TYR A 37 2588 1791 1727 966 557 1098 C ATOM 198 OH TYR A 37 -1.383 27.860 42.480 1.00 21.34 O ANISOU 198 OH TYR A 37 3198 2354 2553 1468 1000 1141 O ATOM 199 N LEU A 38 -6.290 30.696 48.746 1.00 10.03 N ANISOU 199 N LEU A 38 1488 952 1370 199 118 203 N ATOM 200 CA LEU A 38 -7.157 31.546 49.538 1.00 10.79 C ANISOU 200 CA LEU A 38 1705 909 1482 264 210 228 C ATOM 201 C LEU A 38 -6.522 32.906 49.689 1.00 12.03 C ANISOU 201 C LEU A 38 1847 938 1783 244 259 229 C ATOM 202 O LEU A 38 -5.347 33.015 50.046 1.00 13.50 O ANISOU 202 O LEU A 38 1907 1045 2175 134 136 27 O ATOM 203 CB LEU A 38 -7.381 30.957 50.927 1.00 11.50 C ANISOU 203 CB LEU A 38 2000 950 1416 294 90 178 C ATOM 204 CG LEU A 38 -8.419 31.693 51.785 1.00 13.19 C ANISOU 204 CG LEU A 38 2156 1205 1647 381 264 122 C ATOM 205 CD1 LEU A 38 -9.807 31.573 51.177 1.00 15.98 C ANISOU 205 CD1 LEU A 38 2093 2077 1898 459 292 199 C ATOM 206 CD2 LEU A 38 -8.423 31.185 53.218 1.00 14.46 C ANISOU 206 CD2 LEU A 38 2281 1605 1604 510 381 151 C ATOM 207 N ASP A 39 -7.306 33.942 49.407 1.00 14.71 N ANISOU 207 N ASP A 39 2210 978 2402 374 236 387 N ATOM 208 CA AASP A 39 -6.899 35.306 49.686 0.33 17.74 C ANISOU 208 CA AASP A 39 2561 1173 3006 140 428 152 C ATOM 209 CA BASP A 39 -6.903 35.308 49.701 0.67 17.31 C ANISOU 209 CA BASP A 39 2544 1005 3027 325 480 271 C ATOM 210 C ASP A 39 -6.864 35.479 51.201 1.00 20.14 C ANISOU 210 C ASP A 39 3064 1517 3069 96 780 -56 C ATOM 211 O ASP A 39 -7.888 35.352 51.872 1.00 25.08 O ANISOU 211 O ASP A 39 3452 2387 3687 -505 1245 -1038 O ATOM 212 CB AASP A 39 -7.874 36.302 49.052 0.33 20.64 C ANISOU 212 CB AASP A 39 2798 1676 3365 339 232 307 C ATOM 213 CB BASP A 39 -7.886 36.320 49.121 0.67 20.27 C ANISOU 213 CB BASP A 39 3015 1123 3563 518 410 478 C ATOM 214 CG AASP A 39 -7.971 36.153 47.537 0.33 21.26 C ANISOU 214 CG AASP A 39 2912 1803 3360 344 128 393 C ATOM 215 CG BASP A 39 -7.552 37.757 49.522 0.67 20.44 C ANISOU 215 CG BASP A 39 3354 1099 3312 243 638 706 C ATOM 216 OD1AASP A 39 -7.005 35.669 46.911 0.33 23.98 O ANISOU 216 OD1AASP A 39 2994 2177 3940 416 78 -186 O ATOM 217 OD1BASP A 39 -6.349 38.080 49.650 0.67 18.16 O ANISOU 217 OD1BASP A 39 3644 1120 2134 125 135 167 O ATOM 218 OD2AASP A 39 -9.019 36.526 46.969 0.33 24.29 O ANISOU 218 OD2AASP A 39 2868 2598 3760 451 -13 153 O ATOM 219 OD2BASP A 39 -8.488 38.564 49.707 0.67 26.91 O ANISOU 219 OD2BASP A 39 3524 1888 4810 502 762 77 O ATOM 220 N MET A 40 -5.684 35.734 51.732 1.00 19.08 N ANISOU 220 N MET A 40 3171 1598 2478 539 639 694 N ATOM 221 CA MET A 40 -5.536 35.984 53.143 1.00 23.06 C ANISOU 221 CA MET A 40 4068 2041 2652 674 585 398 C ATOM 222 C MET A 40 -5.189 37.452 53.236 1.00 21.76 C ANISOU 222 C MET A 40 3653 2141 2473 697 563 -85 C ATOM 223 O MET A 40 -4.043 37.829 52.981 1.00 23.95 O ANISOU 223 O MET A 40 3801 2857 2442 368 542 -782 O ATOM 224 CB MET A 40 -4.443 35.100 53.725 1.00 25.75 C ANISOU 224 CB MET A 40 4505 2159 3117 920 457 488 C ATOM 225 CG MET A 40 -4.866 33.646 53.855 1.00 30.72 C ANISOU 225 CG MET A 40 5357 2212 4103 712 819 588 C ATOM 226 SD MET A 40 -3.657 32.626 54.713 1.00 32.60 S ANISOU 226 SD MET A 40 6349 2765 3270 1190 819 511 S ATOM 227 CE MET A 40 -3.515 33.504 56.265 1.00 32.24 C ANISOU 227 CE MET A 40 5578 1799 4870 -68 1295 -561 C ATOM 228 N PRO A 41 -6.189 38.296 53.555 1.00 20.35 N ANISOU 228 N PRO A 41 3546 2003 2182 508 533 -387 N ATOM 229 CA PRO A 41 -5.932 39.720 53.577 1.00 21.10 C ANISOU 229 CA PRO A 41 3414 2120 2482 323 671 -608 C ATOM 230 C PRO A 41 -4.672 40.010 54.386 1.00 26.25 C ANISOU 230 C PRO A 41 3802 3348 2823 332 123 -126 C ATOM 231 O PRO A 41 -4.538 39.526 55.511 1.00 28.62 O ANISOU 231 O PRO A 41 4524 3968 2381 186 681 -247 O ATOM 232 CB PRO A 41 -7.185 40.283 54.243 1.00 20.97 C ANISOU 232 CB PRO A 41 3424 2053 2490 373 592 -727 C ATOM 233 CG PRO A 41 -8.262 39.342 53.832 1.00 22.28 C ANISOU 233 CG PRO A 41 3352 2251 2863 362 643 -738 C ATOM 234 CD PRO A 41 -7.609 37.992 53.820 1.00 22.30 C ANISOU 234 CD PRO A 41 3597 2175 2699 406 691 -455 C ATOM 235 N GLY A 42 -3.739 40.741 53.780 1.00 27.28 N ANISOU 235 N GLY A 42 4083 3079 3202 64 338 -554 N ATOM 236 CA GLY A 42 -2.451 41.038 54.404 1.00 30.08 C ANISOU 236 CA GLY A 42 4067 3808 3551 125 130 -415 C ATOM 237 C GLY A 42 -1.321 40.098 54.007 1.00 29.36 C ANISOU 237 C GLY A 42 4248 3570 3335 132 -7 -538 C ATOM 238 O GLY A 42 -0.184 40.291 54.434 1.00 32.41 O ANISOU 238 O GLY A 42 4385 4156 3774 214 -421 -306 O ATOM 239 N PHE A 43 -1.624 39.083 53.198 1.00 29.70 N ANISOU 239 N PHE A 43 4479 4009 2793 0 -179 -527 N ATOM 240 CA PHE A 43 -0.608 38.135 52.729 1.00 31.26 C ANISOU 240 CA PHE A 43 3950 4620 3307 120 -206 -283 C ATOM 241 C PHE A 43 -0.616 37.934 51.209 1.00 29.68 C ANISOU 241 C PHE A 43 3309 4589 3377 -75 -412 -576 C ATOM 242 O PHE A 43 0.442 37.767 50.602 1.00 35.05 O ANISOU 242 O PHE A 43 4000 5960 3354 222 105 -632 O ATOM 243 CB PHE A 43 -0.781 36.787 53.437 1.00 34.07 C ANISOU 243 CB PHE A 43 4149 4907 3887 0 -349 24 C ATOM 244 CG PHE A 43 -0.550 36.849 54.922 1.00 35.99 C ANISOU 244 CG PHE A 43 4160 5615 3900 -7 -290 57 C ATOM 245 CD1 PHE A 43 0.735 36.773 55.442 1.00 37.15 C ANISOU 245 CD1 PHE A 43 4021 5989 4102 -147 -193 -11 C ATOM 246 CD2 PHE A 43 -1.617 36.986 55.802 1.00 36.29 C ANISOU 246 CD2 PHE A 43 4092 5780 3916 -322 -263 292 C ATOM 247 CE1 PHE A 43 0.953 36.831 56.811 1.00 39.98 C ANISOU 247 CE1 PHE A 43 4468 6696 4026 -267 54 180 C ATOM 248 CE2 PHE A 43 -1.407 37.045 57.171 1.00 38.88 C ANISOU 248 CE2 PHE A 43 4241 6554 3976 -271 -228 89 C ATOM 249 CZ PHE A 43 -0.120 36.967 57.677 1.00 39.18 C ANISOU 249 CZ PHE A 43 4110 6675 4099 -378 -121 167 C ATOM 250 N GLY A 44 -1.798 37.961 50.597 1.00 20.73 N ANISOU 250 N GLY A 44 3069 2414 2391 -391 -20 -611 N ATOM 251 CA GLY A 44 -1.951 37.649 49.180 1.00 17.65 C ANISOU 251 CA GLY A 44 2790 1750 2162 -248 5 -231 C ATOM 252 C GLY A 44 -2.725 36.360 49.055 1.00 13.88 C ANISOU 252 C GLY A 44 2510 1330 1432 95 -57 153 C ATOM 253 O GLY A 44 -3.308 35.884 50.030 1.00 14.46 O ANISOU 253 O GLY A 44 2651 1416 1428 231 37 189 O ATOM 254 N ALA A 45 -2.721 35.789 47.859 1.00 12.99 N ANISOU 254 N ALA A 45 2409 1191 1336 139 45 295 N ATOM 255 CA ALA A 45 -3.441 34.551 47.582 1.00 12.54 C ANISOU 255 CA ALA A 45 2397 1045 1320 228 92 345 C ATOM 256 C ALA A 45 -2.522 33.364 47.823 1.00 12.89 C ANISOU 256 C ALA A 45 2366 1126 1404 213 182 542 C ATOM 257 O ALA A 45 -1.636 33.075 47.033 1.00 16.42 O ANISOU 257 O ALA A 45 2626 1780 1830 444 542 589 O ATOM 258 CB ALA A 45 -3.948 34.538 46.152 1.00 14.69 C ANISOU 258 CB ALA A 45 2828 1315 1438 63 -105 385 C ATOM 259 N VAL A 46 -2.765 32.665 48.916 1.00 10.62 N ANISOU 259 N VAL A 46 1769 960 1303 40 58 387 N ATOM 260 CA VAL A 46 -1.848 31.653 49.424 1.00 10.61 C ANISOU 260 CA VAL A 46 1628 1045 1358 -3 13 372 C ATOM 261 C VAL A 46 -2.210 30.276 48.888 1.00 9.36 C ANISOU 261 C VAL A 46 1398 939 1218 32 102 478 C ATOM 262 O VAL A 46 -3.339 29.809 49.059 1.00 9.87 O ANISOU 262 O VAL A 46 1356 1055 1338 8 59 291 O ATOM 263 CB VAL A 46 -1.893 31.645 50.970 1.00 12.16 C ANISOU 263 CB VAL A 46 1932 1305 1383 7 -158 294 C ATOM 264 CG1 VAL A 46 -0.942 30.599 51.534 1.00 12.80 C ANISOU 264 CG1 VAL A 46 1868 1542 1451 -47 -114 553 C ATOM 265 CG2 VAL A 46 -1.555 33.026 51.521 1.00 14.46 C ANISOU 265 CG2 VAL A 46 2321 1509 1661 -37 -165 40 C ATOM 266 N ALA A 47 -1.239 29.615 48.264 1.00 9.91 N ANISOU 266 N ALA A 47 1311 937 1515 -57 116 379 N ATOM 267 CA ALA A 47 -1.403 28.245 47.795 1.00 9.46 C ANISOU 267 CA ALA A 47 1212 878 1503 7 135 392 C ATOM 268 C ALA A 47 -1.271 27.251 48.933 1.00 8.62 C ANISOU 268 C ALA A 47 1031 913 1330 52 112 297 C ATOM 269 O ALA A 47 -0.417 27.414 49.811 1.00 9.72 O ANISOU 269 O ALA A 47 1264 980 1448 -149 -32 409 O ATOM 270 CB ALA A 47 -0.340 27.931 46.761 1.00 11.25 C ANISOU 270 CB ALA A 47 1411 1162 1700 7 275 275 C ATOM 271 N SER A 48 -2.065 26.184 48.865 1.00 7.83 N ANISOU 271 N SER A 48 978 853 1142 91 67 268 N ATOM 272 CA SER A 48 -1.889 25.019 49.725 1.00 7.45 C ANISOU 272 CA SER A 48 953 832 1046 68 85 239 C ATOM 273 C SER A 48 -1.993 23.770 48.874 1.00 7.16 C ANISOU 273 C SER A 48 949 888 883 63 74 231 C ATOM 274 O SER A 48 -2.922 23.644 48.072 1.00 7.20 O ANISOU 274 O SER A 48 941 828 966 95 86 144 O ATOM 275 CB SER A 48 -2.950 24.968 50.831 1.00 7.88 C ANISOU 275 CB SER A 48 1045 906 1042 15 104 245 C ATOM 276 OG SER A 48 -2.725 23.856 51.678 1.00 8.29 O ANISOU 276 OG SER A 48 1166 910 1072 35 79 258 O ATOM 277 N ASN A 49 -1.077 22.835 49.114 1.00 7.29 N ANISOU 277 N ASN A 49 959 875 935 65 27 143 N ATOM 278 CA ASN A 49 -1.023 21.567 48.401 1.00 7.16 C ANISOU 278 CA ASN A 49 917 854 950 71 -3 139 C ATOM 279 C ASN A 49 -1.442 20.397 49.285 1.00 7.00 C ANISOU 279 C ASN A 49 910 872 875 99 2 143 C ATOM 280 O ASN A 49 -1.075 20.335 50.465 1.00 7.25 O ANISOU 280 O ASN A 49 1005 850 898 1 -42 120 O ATOM 281 CB ASN A 49 0.406 21.261 47.925 1.00 7.79 C ANISOU 281 CB ASN A 49 966 929 1062 83 60 141 C ATOM 282 CG ASN A 49 1.012 22.367 47.096 1.00 8.46 C ANISOU 282 CG ASN A 49 1065 1007 1142 131 137 193 C ATOM 283 OD1 ASN A 49 0.359 22.952 46.234 1.00 9.73 O ANISOU 283 OD1 ASN A 49 1149 1359 1186 54 166 488 O ATOM 284 ND2 ASN A 49 2.274 22.668 47.365 1.00 10.43 N ANISOU 284 ND2 ASN A 49 1036 1424 1502 -33 214 530 N ATOM 285 N GLY A 50 -2.140 19.452 48.667 1.00 6.74 N ANISOU 285 N GLY A 50 945 885 728 36 64 175 N ATOM 286 CA GLY A 50 -2.358 18.123 49.217 1.00 6.74 C ANISOU 286 CA GLY A 50 862 851 845 13 42 153 C ATOM 287 C GLY A 50 -2.137 17.077 48.138 1.00 6.81 C ANISOU 287 C GLY A 50 926 832 827 52 6 186 C ATOM 288 O GLY A 50 -1.596 17.377 47.067 1.00 7.42 O ANISOU 288 O GLY A 50 1027 899 890 45 93 152 O ATOM 289 N LEU A 51 -2.549 15.843 48.402 1.00 6.78 N ANISOU 289 N LEU A 51 889 858 828 18 92 85 N ATOM 290 CA LEU A 51 -2.294 14.733 47.503 1.00 7.04 C ANISOU 290 CA LEU A 51 957 888 828 42 122 72 C ATOM 291 C LEU A 51 -3.549 13.929 47.197 1.00 6.96 C ANISOU 291 C LEU A 51 940 822 882 89 46 18 C ATOM 292 O LEU A 51 -4.506 13.897 47.981 1.00 7.23 O ANISOU 292 O LEU A 51 966 962 817 8 49 49 O ATOM 293 CB LEU A 51 -1.228 13.797 48.078 1.00 7.77 C ANISOU 293 CB LEU A 51 1012 1050 888 150 59 -15 C ATOM 294 CG LEU A 51 0.184 14.382 48.115 1.00 9.24 C ANISOU 294 CG LEU A 51 1090 1193 1226 106 -45 -123 C ATOM 295 CD1 LEU A 51 1.114 13.494 48.916 1.00 12.24 C ANISOU 295 CD1 LEU A 51 1070 2001 1578 271 -30 198 C ATOM 296 CD2 LEU A 51 0.763 14.592 46.724 1.00 9.88 C ANISOU 296 CD2 LEU A 51 1031 1336 1386 -17 44 -99 C ATOM 297 N ILE A 52 -3.495 13.250 46.062 1.00 7.32 N ANISOU 297 N ILE A 52 972 914 895 27 166 -42 N ATOM 298 CA ILE A 52 -4.510 12.320 45.606 1.00 7.68 C ANISOU 298 CA ILE A 52 1102 970 843 5 81 -132 C ATOM 299 C ILE A 52 -3.730 11.081 45.154 1.00 7.96 C ANISOU 299 C ILE A 52 1115 939 968 -3 36 -120 C ATOM 300 O ILE A 52 -2.786 11.197 44.358 1.00 8.99 O ANISOU 300 O ILE A 52 1290 1004 1121 81 238 -34 O ATOM 301 CB ILE A 52 -5.287 12.898 44.399 1.00 8.08 C ANISOU 301 CB ILE A 52 1167 1016 884 92 62 -68 C ATOM 302 CG1 ILE A 52 -5.923 14.242 44.774 1.00 8.97 C ANISOU 302 CG1 ILE A 52 1190 1073 1145 144 6 -118 C ATOM 303 CG2 ILE A 52 -6.314 11.889 43.895 1.00 9.00 C ANISOU 303 CG2 ILE A 52 1272 1154 992 51 35 -202 C ATOM 304 CD1 ILE A 52 -6.522 14.997 43.609 1.00 9.56 C ANISOU 304 CD1 ILE A 52 1215 1225 1188 96 -31 -33 C ATOM 305 N VAL A 53 -4.122 9.914 45.649 1.00 7.88 N ANISOU 305 N VAL A 53 1041 965 988 1 115 -146 N ATOM 306 CA VAL A 53 -3.423 8.661 45.376 1.00 7.99 C ANISOU 306 CA VAL A 53 1127 980 929 5 128 -177 C ATOM 307 C VAL A 53 -4.419 7.624 44.887 1.00 8.33 C ANISOU 307 C VAL A 53 1210 907 1046 8 94 -242 C ATOM 308 O VAL A 53 -5.427 7.376 45.539 1.00 9.19 O ANISOU 308 O VAL A 53 1179 1112 1200 -90 141 -280 O ATOM 309 CB VAL A 53 -2.727 8.133 46.644 1.00 8.80 C ANISOU 309 CB VAL A 53 1250 1039 1052 3 74 -60 C ATOM 310 CG1 VAL A 53 -2.012 6.818 46.363 1.00 10.02 C ANISOU 310 CG1 VAL A 53 1406 1124 1276 121 97 -26 C ATOM 311 CG2 VAL A 53 -1.751 9.152 47.198 1.00 8.78 C ANISOU 311 CG2 VAL A 53 1167 1142 1024 32 29 -21 C ATOM 312 N ARG A 54 -4.152 7.021 43.733 1.00 8.95 N ANISOU 312 N ARG A 54 1333 1048 1017 -61 200 -220 N ATOM 313 CA ARG A 54 -4.939 5.874 43.311 1.00 9.39 C ANISOU 313 CA ARG A 54 1392 1113 1061 -101 269 -342 C ATOM 314 C ARG A 54 -4.284 4.601 43.844 1.00 9.61 C ANISOU 314 C ARG A 54 1481 1061 1106 -116 98 -447 C ATOM 315 O ARG A 54 -3.087 4.365 43.635 1.00 10.67 O ANISOU 315 O ARG A 54 1478 1105 1471 -37 108 -257 O ATOM 316 CB ARG A 54 -5.093 5.771 41.786 1.00 10.18 C ANISOU 316 CB ARG A 54 1570 1207 1091 -55 204 -287 C ATOM 317 CG ARG A 54 -5.985 4.591 41.411 1.00 10.75 C ANISOU 317 CG ARG A 54 1611 1273 1201 -53 8 -433 C ATOM 318 CD ARG A 54 -6.208 4.417 39.911 1.00 11.12 C ANISOU 318 CD ARG A 54 1706 1355 1162 -110 70 -326 C ATOM 319 NE ARG A 54 -4.990 4.108 39.161 1.00 11.79 N ANISOU 319 NE ARG A 54 1819 1521 1139 -56 130 -401 N ATOM 320 CZ ARG A 54 -4.342 2.943 39.199 1.00 12.05 C ANISOU 320 CZ ARG A 54 1699 1508 1371 -120 1 -535 C ATOM 321 NH1 ARG A 54 -4.784 1.935 39.940 1.00 12.09 N ANISOU 321 NH1 ARG A 54 1752 1402 1438 -77 81 -610 N ATOM 322 NH2 ARG A 54 -3.235 2.789 38.476 1.00 14.20 N ANISOU 322 NH2 ARG A 54 1932 1772 1691 -164 312 -637 N ATOM 323 N ASP A 55 -5.084 3.799 44.541 1.00 9.99 N ANISOU 323 N ASP A 55 1471 1123 1200 -140 68 -354 N ATOM 324 CA ASP A 55 -4.654 2.499 45.039 1.00 10.20 C ANISOU 324 CA ASP A 55 1659 1136 1078 -174 112 -320 C ATOM 325 C ASP A 55 -5.590 1.459 44.440 1.00 10.29 C ANISOU 325 C ASP A 55 1570 1191 1146 -99 -16 -315 C ATOM 326 O ASP A 55 -6.686 1.229 44.941 1.00 11.01 O ANISOU 326 O ASP A 55 1699 1193 1290 -256 90 -407 O ATOM 327 CB ASP A 55 -4.738 2.470 46.562 1.00 11.43 C ANISOU 327 CB ASP A 55 1854 1400 1086 -344 59 -232 C ATOM 328 CG ASP A 55 -4.448 1.101 47.142 1.00 12.07 C ANISOU 328 CG ASP A 55 1930 1525 1130 -338 40 -103 C ATOM 329 OD1 ASP A 55 -3.622 0.370 46.572 1.00 13.77 O ANISOU 329 OD1 ASP A 55 2236 1697 1296 -64 254 99 O ATOM 330 OD2 ASP A 55 -5.049 0.769 48.176 1.00 14.20 O ANISOU 330 OD2 ASP A 55 2448 1713 1234 -379 251 -72 O ATOM 331 N GLY A 56 -5.166 0.864 43.331 1.00 10.99 N ANISOU 331 N GLY A 56 1667 1322 1185 -105 52 -351 N ATOM 332 CA GLY A 56 -6.006 -0.076 42.614 1.00 11.71 C ANISOU 332 CA GLY A 56 1807 1349 1293 6 -40 -524 C ATOM 333 C GLY A 56 -7.288 0.580 42.147 1.00 10.70 C ANISOU 333 C GLY A 56 1715 1198 1152 -103 -17 -507 C ATOM 334 O GLY A 56 -7.262 1.538 41.369 1.00 11.37 O ANISOU 334 O GLY A 56 1753 1214 1351 -111 -90 -381 O ATOM 335 N GLY A 57 -8.412 0.050 42.612 1.00 11.57 N ANISOU 335 N GLY A 57 1776 1282 1338 -151 114 -516 N ATOM 336 CA GLY A 57 -9.720 0.544 42.217 1.00 11.92 C ANISOU 336 CA GLY A 57 1794 1250 1484 -251 -27 -511 C ATOM 337 C GLY A 57 -10.328 1.616 43.100 1.00 11.28 C ANISOU 337 C GLY A 57 1700 1303 1282 -274 75 -386 C ATOM 338 O GLY A 57 -11.533 1.839 43.038 1.00 12.76 O ANISOU 338 O GLY A 57 1767 1507 1574 -89 -32 -557 O ATOM 339 N ARG A 58 -9.518 2.286 43.912 1.00 11.24 N ANISOU 339 N ARG A 58 1649 1168 1452 -247 79 -439 N ATOM 340 CA ARG A 58 -10.033 3.358 44.745 1.00 11.33 C ANISOU 340 CA ARG A 58 1716 1155 1434 -226 70 -440 C ATOM 341 C ARG A 58 -9.026 4.491 44.831 1.00 9.71 C ANISOU 341 C ARG A 58 1492 1135 1060 -112 46 -367 C ATOM 342 O ARG A 58 -7.860 4.339 44.462 1.00 10.51 O ANISOU 342 O ARG A 58 1488 1140 1363 -98 100 -333 O ATOM 343 CB ARG A 58 -10.366 2.829 46.133 1.00 12.42 C ANISOU 343 CB ARG A 58 1890 1320 1507 -290 25 -317 C ATOM 344 CG ARG A 58 -9.130 2.497 46.927 1.00 12.16 C ANISOU 344 CG ARG A 58 1868 1397 1354 -302 30 -383 C ATOM 345 CD ARG A 58 -9.280 1.312 47.864 1.00 15.09 C ANISOU 345 CD ARG A 58 2354 1705 1674 -206 -327 -98 C ATOM 346 NE ARG A 58 -8.035 1.205 48.600 1.00 14.06 N ANISOU 346 NE ARG A 58 2356 1650 1337 -176 -194 -160 N ATOM 347 CZ ARG A 58 -7.857 1.465 49.892 1.00 12.07 C ANISOU 347 CZ ARG A 58 2344 976 1263 -247 -85 -42 C ATOM 348 NH1 ARG A 58 -8.870 1.735 50.721 1.00 12.55 N ANISOU 348 NH1 ARG A 58 2026 1286 1456 -282 -98 225 N ATOM 349 NH2 ARG A 58 -6.623 1.418 50.365 1.00 12.27 N ANISOU 349 NH2 ARG A 58 2317 1198 1147 -124 -113 -21 N ATOM 350 N VAL A 59 -9.507 5.624 45.325 1.00 9.02 N ANISOU 350 N VAL A 59 1280 1120 1025 -156 26 -377 N ATOM 351 CA VAL A 59 -8.714 6.833 45.460 1.00 8.98 C ANISOU 351 CA VAL A 59 1238 1079 1094 -114 -34 -331 C ATOM 352 C VAL A 59 -8.662 7.239 46.935 1.00 8.50 C ANISOU 352 C VAL A 59 1147 1016 1064 -112 -40 -249 C ATOM 353 O VAL A 59 -9.643 7.096 47.671 1.00 9.14 O ANISOU 353 O VAL A 59 1211 1143 1118 -189 0 -319 O ATOM 354 CB VAL A 59 -9.308 7.956 44.594 1.00 8.91 C ANISOU 354 CB VAL A 59 1221 1183 980 13 87 -299 C ATOM 355 CG1 VAL A 59 -8.562 9.266 44.783 1.00 9.80 C ANISOU 355 CG1 VAL A 59 1359 1159 1206 -11 -111 -179 C ATOM 356 CG2 VAL A 59 -9.266 7.543 43.133 1.00 10.95 C ANISOU 356 CG2 VAL A 59 1749 1359 1050 67 23 -360 C ATOM 357 N LEU A 60 -7.506 7.739 47.354 1.00 7.97 N ANISOU 357 N LEU A 60 1074 963 990 -85 99 -218 N ATOM 358 CA LEU A 60 -7.257 8.202 48.715 1.00 7.75 C ANISOU 358 CA LEU A 60 1097 913 935 -109 70 -189 C ATOM 359 C LEU A 60 -6.818 9.663 48.622 1.00 7.23 C ANISOU 359 C LEU A 60 1032 898 816 -121 96 -159 C ATOM 360 O LEU A 60 -6.029 10.013 47.761 1.00 8.95 O ANISOU 360 O LEU A 60 1292 999 1110 -131 390 -232 O ATOM 361 CB LEU A 60 -6.149 7.370 49.363 1.00 8.17 C ANISOU 361 CB LEU A 60 1124 1009 971 -126 30 -96 C ATOM 362 CG LEU A 60 -6.230 5.865 49.121 1.00 9.87 C ANISOU 362 CG LEU A 60 1462 1036 1249 -40 -50 -213 C ATOM 363 CD1 LEU A 60 -4.979 5.167 49.622 1.00 10.48 C ANISOU 363 CD1 LEU A 60 1523 1129 1330 45 0 -73 C ATOM 364 CD2 LEU A 60 -7.481 5.260 49.738 1.00 11.33 C ANISOU 364 CD2 LEU A 60 1708 1018 1579 -127 69 17 C ATOM 365 N VAL A 61 -7.307 10.503 49.519 1.00 6.89 N ANISOU 365 N VAL A 61 1004 858 756 -66 65 -115 N ATOM 366 CA VAL A 61 -6.980 11.918 49.519 1.00 7.27 C ANISOU 366 CA VAL A 61 1041 868 852 -63 -12 -110 C ATOM 367 C VAL A 61 -6.229 12.291 50.792 1.00 6.61 C ANISOU 367 C VAL A 61 928 771 810 -17 25 -6 C ATOM 368 O VAL A 61 -6.589 11.844 51.889 1.00 7.04 O ANISOU 368 O VAL A 61 1030 826 817 -132 4 -13 O ATOM 369 CB VAL A 61 -8.265 12.766 49.356 1.00 7.66 C ANISOU 369 CB VAL A 61 1052 991 866 13 -19 -168 C ATOM 370 CG1 VAL A 61 -7.994 14.254 49.538 1.00 8.63 C ANISOU 370 CG1 VAL A 61 1118 994 1165 96 -168 -106 C ATOM 371 CG2 VAL A 61 -8.902 12.507 48.002 1.00 9.14 C ANISOU 371 CG2 VAL A 61 1255 1262 955 16 -195 -100 C ATOM 372 N VAL A 62 -5.197 13.119 50.636 1.00 6.26 N ANISOU 372 N VAL A 62 906 715 757 5 76 -2 N ATOM 373 CA VAL A 62 -4.482 13.720 51.750 1.00 6.23 C ANISOU 373 CA VAL A 62 818 674 873 4 23 29 C ATOM 374 C VAL A 62 -4.746 15.235 51.705 1.00 5.91 C ANISOU 374 C VAL A 62 764 667 814 -12 -42 78 C ATOM 375 O VAL A 62 -4.363 15.905 50.761 1.00 6.36 O ANISOU 375 O VAL A 62 876 727 814 29 56 66 O ATOM 376 CB VAL A 62 -2.969 13.440 51.688 1.00 6.95 C ANISOU 376 CB VAL A 62 844 792 1002 24 30 168 C ATOM 377 CG1 VAL A 62 -2.274 14.058 52.896 1.00 8.06 C ANISOU 377 CG1 VAL A 62 890 905 1268 28 -150 68 C ATOM 378 CG2 VAL A 62 -2.697 11.946 51.620 1.00 7.89 C ANISOU 378 CG2 VAL A 62 1025 848 1124 133 56 67 C ATOM 379 N ASP A 63 -5.436 15.707 52.748 1.00 6.17 N ANISOU 379 N ASP A 63 799 694 851 9 -49 24 N ATOM 380 CA ASP A 63 -5.814 17.105 52.986 1.00 6.11 C ANISOU 380 CA ASP A 63 774 701 843 -6 -56 50 C ATOM 381 C ASP A 63 -6.968 17.562 52.112 1.00 5.89 C ANISOU 381 C ASP A 63 688 762 788 0 31 60 C ATOM 382 O ASP A 63 -7.098 17.169 50.952 1.00 6.57 O ANISOU 382 O ASP A 63 864 796 835 56 -68 66 O ATOM 383 CB ASP A 63 -4.621 18.058 52.886 1.00 5.99 C ANISOU 383 CB ASP A 63 759 742 775 11 79 63 C ATOM 384 CG ASP A 63 -3.638 17.858 54.036 1.00 6.77 C ANISOU 384 CG ASP A 63 799 746 1027 73 -67 -17 C ATOM 385 OD1 ASP A 63 -4.072 17.378 55.102 1.00 8.62 O ANISOU 385 OD1 ASP A 63 1438 889 947 -38 -279 113 O ATOM 386 OD2 ASP A 63 -2.460 18.188 53.860 1.00 8.95 O ANISOU 386 OD2 ASP A 63 781 1003 1614 69 -80 -164 O ATOM 387 N THR A 64 -7.821 18.387 52.708 1.00 6.11 N ANISOU 387 N THR A 64 756 769 794 45 5 65 N ATOM 388 CA THR A 64 -8.806 19.101 51.920 1.00 6.48 C ANISOU 388 CA THR A 64 784 796 881 45 -50 75 C ATOM 389 C THR A 64 -8.144 20.292 51.216 1.00 6.46 C ANISOU 389 C THR A 64 788 800 864 111 86 64 C ATOM 390 O THR A 64 -6.958 20.539 51.391 1.00 7.14 O ANISOU 390 O THR A 64 791 836 1084 71 6 111 O ATOM 391 CB THR A 64 -10.023 19.556 52.764 1.00 7.00 C ANISOU 391 CB THR A 64 784 897 976 45 -67 55 C ATOM 392 OG1 THR A 64 -9.682 20.650 53.617 1.00 7.23 O ANISOU 392 OG1 THR A 64 877 851 1019 110 3 29 O ATOM 393 CG2 THR A 64 -10.566 18.447 53.638 1.00 7.46 C ANISOU 393 CG2 THR A 64 833 917 1082 4 25 37 C ATOM 394 N ALA A 65 -8.961 21.020 50.457 1.00 7.26 N ANISOU 394 N ALA A 65 836 888 1033 94 15 189 N ATOM 395 CA ALA A 65 -8.622 22.372 50.040 1.00 7.43 C ANISOU 395 CA ALA A 65 856 900 1065 96 26 269 C ATOM 396 C ALA A 65 -9.023 23.346 51.147 1.00 7.59 C ANISOU 396 C ALA A 65 877 885 1121 45 -17 240 C ATOM 397 O ALA A 65 -9.565 22.945 52.193 1.00 8.02 O ANISOU 397 O ALA A 65 997 873 1176 53 85 193 O ATOM 398 CB ALA A 65 -9.307 22.712 48.716 1.00 8.01 C ANISOU 398 CB ALA A 65 1041 1000 1002 149 83 268 C ATOM 399 N TRP A 66 -8.821 24.640 50.929 1.00 7.86 N ANISOU 399 N TRP A 66 963 881 1142 78 50 210 N ATOM 400 CA TRP A 66 -9.178 25.616 51.946 1.00 7.87 C ANISOU 400 CA TRP A 66 1068 904 1018 89 14 267 C ATOM 401 C TRP A 66 -10.680 25.642 52.262 1.00 7.84 C ANISOU 401 C TRP A 66 1072 893 1011 132 55 225 C ATOM 402 O TRP A 66 -11.070 25.956 53.386 1.00 8.94 O ANISOU 402 O TRP A 66 1143 1216 1037 182 30 110 O ATOM 403 CB TRP A 66 -8.802 27.024 51.514 1.00 8.43 C ANISOU 403 CB TRP A 66 1239 862 1100 108 102 204 C ATOM 404 CG TRP A 66 -7.347 27.303 51.275 1.00 8.32 C ANISOU 404 CG TRP A 66 1241 786 1134 143 123 261 C ATOM 405 CD1 TRP A 66 -6.673 27.190 50.085 1.00 8.78 C ANISOU 405 CD1 TRP A 66 1324 877 1133 219 159 317 C ATOM 406 CD2 TRP A 66 -6.411 27.840 52.213 1.00 8.35 C ANISOU 406 CD2 TRP A 66 1119 704 1349 38 222 239 C ATOM 407 NE1 TRP A 66 -5.379 27.601 50.238 1.00 9.59 N ANISOU 407 NE1 TRP A 66 1291 975 1375 213 255 373 N ATOM 408 CE2 TRP A 66 -5.196 28.028 51.524 1.00 9.18 C ANISOU 408 CE2 TRP A 66 1164 850 1471 52 250 355 C ATOM 409 CE3 TRP A 66 -6.496 28.229 53.556 1.00 9.02 C ANISOU 409 CE3 TRP A 66 1206 828 1390 121 73 149 C ATOM 410 CZ2 TRP A 66 -4.068 28.564 52.137 1.00 10.36 C ANISOU 410 CZ2 TRP A 66 1201 1019 1714 -5 157 433 C ATOM 411 CZ3 TRP A 66 -5.376 28.765 54.166 1.00 10.66 C ANISOU 411 CZ3 TRP A 66 1389 1031 1630 -99 29 41 C ATOM 412 CH2 TRP A 66 -4.174 28.923 53.456 1.00 11.02 C ANISOU 412 CH2 TRP A 66 1275 1080 1829 -124 -15 178 C ATOM 413 N THR A 67 -11.520 25.408 51.256 1.00 8.28 N ANISOU 413 N THR A 67 1030 983 1130 186 40 109 N ATOM 414 CA THR A 67 -12.960 25.553 51.427 1.00 8.66 C ANISOU 414 CA THR A 67 1056 1097 1135 233 51 117 C ATOM 415 C THR A 67 -13.710 24.318 50.963 1.00 8.22 C ANISOU 415 C THR A 67 953 1117 1052 259 -30 122 C ATOM 416 O THR A 67 -13.200 23.475 50.215 1.00 8.44 O ANISOU 416 O THR A 67 960 1153 1093 245 31 140 O ATOM 417 CB THR A 67 -13.509 26.762 50.642 1.00 9.42 C ANISOU 417 CB THR A 67 1149 1096 1332 327 29 101 C ATOM 418 OG1 THR A 67 -13.471 26.455 49.245 1.00 9.66 O ANISOU 418 OG1 THR A 67 1223 1186 1261 311 32 204 O ATOM 419 CG2 THR A 67 -12.711 28.029 50.928 1.00 10.14 C ANISOU 419 CG2 THR A 67 1423 1054 1375 281 -38 151 C ATOM 420 N ASP A 68 -14.964 24.246 51.377 1.00 9.02 N ANISOU 420 N ASP A 68 953 1206 1266 225 -8 76 N ATOM 421 CA ASP A 68 -15.846 23.191 50.918 1.00 9.22 C ANISOU 421 CA ASP A 68 888 1264 1349 182 38 98 C ATOM 422 C ASP A 68 -16.009 23.212 49.400 1.00 9.50 C ANISOU 422 C ASP A 68 857 1392 1359 269 -58 52 C ATOM 423 O ASP A 68 -15.930 22.167 48.757 1.00 9.86 O ANISOU 423 O ASP A 68 967 1437 1341 267 -27 -3 O ATOM 424 CB ASP A 68 -17.218 23.299 51.584 1.00 10.25 C ANISOU 424 CB ASP A 68 904 1464 1526 209 41 56 C ATOM 425 CG ASP A 68 -17.171 23.049 53.075 1.00 10.84 C ANISOU 425 CG ASP A 68 791 1748 1579 156 229 195 C ATOM 426 OD1 ASP A 68 -16.453 22.132 53.519 1.00 10.76 O ANISOU 426 OD1 ASP A 68 989 1756 1344 169 137 184 O ATOM 427 OD2 ASP A 68 -17.884 23.771 53.802 1.00 14.02 O ANISOU 427 OD2 ASP A 68 1747 1900 1678 453 440 150 O ATOM 428 N ASP A 69 -16.250 24.389 48.830 1.00 9.97 N ANISOU 428 N ASP A 69 952 1449 1385 383 -46 87 N ATOM 429 CA ASP A 69 -16.438 24.472 47.379 1.00 10.74 C ANISOU 429 CA ASP A 69 1116 1596 1365 412 -101 213 C ATOM 430 C ASP A 69 -15.194 23.992 46.616 1.00 9.85 C ANISOU 430 C ASP A 69 1106 1420 1214 357 -165 168 C ATOM 431 O ASP A 69 -15.303 23.264 45.630 1.00 10.82 O ANISOU 431 O ASP A 69 1189 1701 1218 337 -214 64 O ATOM 432 CB ASP A 69 -16.780 25.900 46.950 1.00 12.83 C ANISOU 432 CB ASP A 69 1562 1769 1541 631 -254 293 C ATOM 433 CG ASP A 69 -18.203 26.309 47.298 1.00 16.69 C ANISOU 433 CG ASP A 69 1719 2421 2198 846 -113 282 C ATOM 434 OD1 ASP A 69 -19.032 25.454 47.677 1.00 19.55 O ANISOU 434 OD1 ASP A 69 1540 2895 2994 752 7 248 O ATOM 435 OD2 ASP A 69 -18.491 27.514 47.172 1.00 21.51 O ANISOU 435 OD2 ASP A 69 2247 2594 3330 1186 -244 281 O ATOM 436 N GLN A 70 -14.015 24.384 47.083 1.00 9.44 N ANISOU 436 N GLN A 70 1052 1361 1172 301 -53 233 N ATOM 437 CA GLN A 70 -12.783 23.948 46.433 1.00 9.22 C ANISOU 437 CA GLN A 70 1184 1269 1051 304 2 246 C ATOM 438 C GLN A 70 -12.605 22.441 46.578 1.00 8.59 C ANISOU 438 C GLN A 70 1043 1244 974 248 -92 133 C ATOM 439 O GLN A 70 -12.123 21.764 45.674 1.00 9.12 O ANISOU 439 O GLN A 70 1162 1279 1022 231 6 94 O ATOM 440 CB GLN A 70 -11.572 24.644 47.038 1.00 8.66 C ANISOU 440 CB GLN A 70 1161 1245 881 277 91 241 C ATOM 441 CG GLN A 70 -11.479 26.123 46.737 1.00 9.40 C ANISOU 441 CG GLN A 70 1150 1259 1161 284 192 305 C ATOM 442 CD GLN A 70 -10.470 26.804 47.625 1.00 9.86 C ANISOU 442 CD GLN A 70 1273 1154 1318 253 122 238 C ATOM 443 OE1 GLN A 70 -9.936 26.206 48.559 1.00 10.46 O ANISOU 443 OE1 GLN A 70 1366 1150 1456 288 -44 205 O ATOM 444 NE2 GLN A 70 -10.213 28.065 47.353 1.00 11.48 N ANISOU 444 NE2 GLN A 70 1631 1236 1494 73 10 318 N ATOM 445 N THR A 71 -12.967 21.910 47.736 1.00 8.38 N ANISOU 445 N THR A 71 973 1141 1068 217 -49 112 N ATOM 446 CA THR A 71 -12.831 20.481 47.988 1.00 8.15 C ANISOU 446 CA THR A 71 979 1129 987 166 -37 89 C ATOM 447 C THR A 71 -13.797 19.673 47.113 1.00 8.63 C ANISOU 447 C THR A 71 1020 1227 1028 163 -124 84 C ATOM 448 O THR A 71 -13.432 18.627 46.584 1.00 9.11 O ANISOU 448 O THR A 71 1066 1338 1056 213 -92 30 O ATOM 449 CB THR A 71 -12.993 20.204 49.488 1.00 7.92 C ANISOU 449 CB THR A 71 799 1203 1006 87 -2 99 C ATOM 450 OG1 THR A 71 -11.998 20.940 50.209 1.00 7.86 O ANISOU 450 OG1 THR A 71 877 1099 1009 77 -57 144 O ATOM 451 CG2 THR A 71 -12.838 18.742 49.827 1.00 8.73 C ANISOU 451 CG2 THR A 71 912 1189 1214 136 7 86 C ATOM 452 N ALA A 72 -15.013 20.181 46.923 1.00 9.53 N ANISOU 452 N ALA A 72 959 1450 1210 184 -137 9 N ATOM 453 CA ALA A 72 -15.922 19.562 45.972 1.00 10.11 C ANISOU 453 CA ALA A 72 1051 1456 1331 184 -177 -75 C ATOM 454 C ALA A 72 -15.308 19.562 44.563 1.00 10.31 C ANISOU 454 C ALA A 72 1207 1507 1203 298 -332 28 C ATOM 455 O ALA A 72 -15.492 18.609 43.808 1.00 11.67 O ANISOU 455 O ALA A 72 1402 1724 1306 302 -332 -194 O ATOM 456 CB ALA A 72 -17.254 20.287 45.966 1.00 11.34 C ANISOU 456 CB ALA A 72 1015 1738 1555 241 -183 -204 C ATOM 457 N GLN A 73 -14.572 20.618 44.215 1.00 10.66 N ANISOU 457 N GLN A 73 1340 1546 1162 341 -239 69 N ATOM 458 CA GLN A 73 -13.875 20.656 42.929 1.00 11.09 C ANISOU 458 CA GLN A 73 1533 1573 1105 302 -237 5 C ATOM 459 C GLN A 73 -12.771 19.597 42.822 1.00 10.65 C ANISOU 459 C GLN A 73 1543 1432 1072 243 -169 -46 C ATOM 460 O GLN A 73 -12.576 19.023 41.749 1.00 11.31 O ANISOU 460 O GLN A 73 1747 1545 1004 293 -170 -23 O ATOM 461 CB GLN A 73 -13.313 22.047 42.646 1.00 12.28 C ANISOU 461 CB GLN A 73 1977 1562 1126 332 -103 145 C ATOM 462 CG GLN A 73 -14.365 23.039 42.209 1.00 16.62 C ANISOU 462 CG GLN A 73 2489 1825 2000 537 -360 428 C ATOM 463 CD GLN A 73 -14.713 22.860 40.747 1.00 19.54 C ANISOU 463 CD GLN A 73 2882 2319 2222 287 -812 523 C ATOM 464 OE1 GLN A 73 -15.241 21.825 40.339 1.00 20.56 O ANISOU 464 OE1 GLN A 73 3064 2525 2223 115 -960 492 O ATOM 465 NE2 GLN A 73 -14.402 23.862 39.944 1.00 22.15 N ANISOU 465 NE2 GLN A 73 3478 2721 2217 157 -625 716 N ATOM 466 N ILE A 74 -12.047 19.335 43.908 1.00 9.53 N ANISOU 466 N ILE A 74 1394 1229 998 145 -86 0 N ATOM 467 CA ILE A 74 -11.102 18.222 43.918 1.00 9.44 C ANISOU 467 CA ILE A 74 1335 1271 978 155 -56 -23 C ATOM 468 C ILE A 74 -11.843 16.932 43.574 1.00 8.79 C ANISOU 468 C ILE A 74 1134 1304 898 202 -105 -93 C ATOM 469 O ILE A 74 -11.386 16.146 42.750 1.00 9.45 O ANISOU 469 O ILE A 74 1268 1413 909 188 -13 -103 O ATOM 470 CB ILE A 74 -10.399 18.074 45.284 1.00 9.07 C ANISOU 470 CB ILE A 74 1146 1270 1029 101 -61 -14 C ATOM 471 CG1 ILE A 74 -9.485 19.271 45.552 1.00 9.45 C ANISOU 471 CG1 ILE A 74 1016 1292 1280 92 87 32 C ATOM 472 CG2 ILE A 74 -9.633 16.755 45.344 1.00 9.86 C ANISOU 472 CG2 ILE A 74 1201 1316 1227 139 -89 -104 C ATOM 473 CD1 ILE A 74 -8.891 19.297 46.943 1.00 9.99 C ANISOU 473 CD1 ILE A 74 1000 1368 1428 122 -56 -194 C ATOM 474 N LEU A 75 -12.991 16.706 44.196 1.00 8.98 N ANISOU 474 N LEU A 75 1120 1282 1009 175 -117 -52 N ATOM 475 CA LEU A 75 -13.742 15.487 43.933 1.00 9.43 C ANISOU 475 CA LEU A 75 1086 1389 1105 142 -192 -133 C ATOM 476 C LEU A 75 -14.241 15.436 42.481 1.00 10.46 C ANISOU 476 C LEU A 75 1189 1634 1152 173 -243 -208 C ATOM 477 O LEU A 75 -14.278 14.367 41.874 1.00 11.22 O ANISOU 477 O LEU A 75 1358 1678 1225 154 -305 -276 O ATOM 478 CB LEU A 75 -14.887 15.342 44.936 1.00 9.99 C ANISOU 478 CB LEU A 75 984 1465 1343 114 -163 -130 C ATOM 479 CG LEU A 75 -14.463 15.329 46.409 1.00 9.95 C ANISOU 479 CG LEU A 75 1059 1448 1273 90 -48 -75 C ATOM 480 CD1 LEU A 75 -15.681 15.151 47.298 1.00 11.08 C ANISOU 480 CD1 LEU A 75 1219 1546 1442 127 90 -31 C ATOM 481 CD2 LEU A 75 -13.440 14.243 46.673 1.00 10.23 C ANISOU 481 CD2 LEU A 75 1192 1526 1169 146 49 15 C ATOM 482 N ASN A 76 -14.598 16.590 41.921 1.00 11.33 N ANISOU 482 N ASN A 76 1299 1736 1269 267 -331 -161 N ATOM 483 CA ASN A 76 -14.980 16.673 40.512 1.00 12.04 C ANISOU 483 CA ASN A 76 1438 1836 1299 132 -358 -1 C ATOM 484 C ASN A 76 -13.822 16.334 39.585 1.00 11.87 C ANISOU 484 C ASN A 76 1551 1732 1224 268 -414 -117 C ATOM 485 O ASN A 76 -14.001 15.606 38.613 1.00 12.87 O ANISOU 485 O ASN A 76 1727 1973 1189 294 -470 -192 O ATOM 486 CB ASN A 76 -15.510 18.071 40.179 1.00 13.25 C ANISOU 486 CB ASN A 76 1628 2051 1354 448 -504 -14 C ATOM 487 CG ASN A 76 -16.835 18.378 40.853 1.00 17.24 C ANISOU 487 CG ASN A 76 1829 2502 2216 405 -176 -140 C ATOM 488 OD1 ASN A 76 -17.575 17.475 41.229 1.00 19.84 O ANISOU 488 OD1 ASN A 76 1765 2873 2898 301 -162 55 O ATOM 489 ND2 ASN A 76 -17.139 19.662 41.004 1.00 18.89 N ANISOU 489 ND2 ASN A 76 2148 2620 2408 764 -117 84 N ATOM 490 N TRP A 77 -12.634 16.850 39.892 1.00 11.31 N ANISOU 490 N TRP A 77 1553 1572 1171 230 -314 -30 N ATOM 491 CA TRP A 77 -11.441 16.511 39.117 1.00 11.42 C ANISOU 491 CA TRP A 77 1694 1568 1075 239 -245 -89 C ATOM 492 C TRP A 77 -11.177 15.007 39.192 1.00 10.70 C ANISOU 492 C TRP A 77 1579 1520 965 201 -269 -182 C ATOM 493 O TRP A 77 -10.887 14.384 38.173 1.00 11.43 O ANISOU 493 O TRP A 77 1704 1626 1012 168 -169 -193 O ATOM 494 CB TRP A 77 -10.224 17.316 39.598 1.00 11.28 C ANISOU 494 CB TRP A 77 1663 1579 1040 157 -69 -13 C ATOM 495 CG TRP A 77 -8.965 17.006 38.848 1.00 11.51 C ANISOU 495 CG TRP A 77 1684 1618 1070 45 43 -31 C ATOM 496 CD1 TRP A 77 -8.463 17.679 37.775 1.00 12.30 C ANISOU 496 CD1 TRP A 77 1972 1575 1124 31 84 26 C ATOM 497 CD2 TRP A 77 -8.043 15.943 39.122 1.00 10.97 C ANISOU 497 CD2 TRP A 77 1547 1640 981 35 34 -77 C ATOM 498 NE1 TRP A 77 -7.294 17.097 37.359 1.00 12.67 N ANISOU 498 NE1 TRP A 77 1997 1658 1158 3 239 -117 N ATOM 499 CE2 TRP A 77 -7.014 16.027 38.164 1.00 11.83 C ANISOU 499 CE2 TRP A 77 1653 1719 1123 42 183 -162 C ATOM 500 CE3 TRP A 77 -7.993 14.923 40.077 1.00 11.30 C ANISOU 500 CE3 TRP A 77 1455 1756 1082 34 12 17 C ATOM 501 CZ2 TRP A 77 -5.947 15.124 38.127 1.00 12.81 C ANISOU 501 CZ2 TRP A 77 1708 1826 1332 122 133 -270 C ATOM 502 CZ3 TRP A 77 -6.935 14.026 40.041 1.00 12.69 C ANISOU 502 CZ3 TRP A 77 1662 1870 1287 203 -75 -52 C ATOM 503 CH2 TRP A 77 -5.928 14.132 39.071 1.00 13.11 C ANISOU 503 CH2 TRP A 77 1502 1922 1556 160 -54 -129 C ATOM 504 N ILE A 78 -11.286 14.424 40.382 1.00 10.14 N ANISOU 504 N ILE A 78 1412 1433 1007 142 -253 -155 N ATOM 505 CA ILE A 78 -11.088 12.990 40.546 1.00 9.95 C ANISOU 505 CA ILE A 78 1339 1433 1009 129 -193 -227 C ATOM 506 C ILE A 78 -12.080 12.210 39.677 1.00 10.79 C ANISOU 506 C ILE A 78 1522 1558 1020 98 -264 -286 C ATOM 507 O ILE A 78 -11.701 11.253 38.999 1.00 11.36 O ANISOU 507 O ILE A 78 1592 1642 1081 157 -210 -352 O ATOM 508 CB ILE A 78 -11.185 12.565 42.026 1.00 9.85 C ANISOU 508 CB ILE A 78 1266 1415 1059 92 -193 -173 C ATOM 509 CG1 ILE A 78 -9.992 13.135 42.804 1.00 9.36 C ANISOU 509 CG1 ILE A 78 1218 1334 1004 140 -132 -154 C ATOM 510 CG2 ILE A 78 -11.228 11.043 42.132 1.00 10.24 C ANISOU 510 CG2 ILE A 78 1316 1410 1163 64 -94 -179 C ATOM 511 CD1 ILE A 78 -10.094 12.999 44.307 1.00 9.12 C ANISOU 511 CD1 ILE A 78 1191 1262 1012 96 -83 -136 C ATOM 512 N LYS A 79 -13.343 12.617 39.691 1.00 11.87 N ANISOU 512 N LYS A 79 1543 1788 1179 151 -307 -388 N ATOM 513 CA ALYS A 79 -14.361 11.958 38.882 0.55 13.25 C ANISOU 513 CA ALYS A 79 1687 2063 1285 105 -436 -464 C ATOM 514 CA BLYS A 79 -14.356 11.947 38.881 0.45 13.05 C ANISOU 514 CA BLYS A 79 1701 1959 1297 101 -415 -446 C ATOM 515 C LYS A 79 -13.993 11.980 37.396 1.00 13.51 C ANISOU 515 C LYS A 79 1819 2050 1261 94 -518 -376 C ATOM 516 O LYS A 79 -14.134 10.974 36.701 1.00 15.41 O ANISOU 516 O LYS A 79 2310 2174 1372 56 -594 -523 O ATOM 517 CB ALYS A 79 -15.719 12.626 39.117 0.55 14.38 C ANISOU 517 CB ALYS A 79 1490 2450 1522 109 -650 -388 C ATOM 518 CB BLYS A 79 -15.731 12.577 39.106 0.45 14.61 C ANISOU 518 CB BLYS A 79 1758 2181 1609 223 -295 -208 C ATOM 519 CG ALYS A 79 -16.840 12.146 38.209 0.55 15.28 C ANISOU 519 CG ALYS A 79 1486 2607 1711 -59 -615 -456 C ATOM 520 CG BLYS A 79 -16.879 11.782 38.505 0.45 16.10 C ANISOU 520 CG BLYS A 79 2041 2246 1830 119 -505 -204 C ATOM 521 CD ALYS A 79 -17.143 10.669 38.396 0.55 17.92 C ANISOU 521 CD ALYS A 79 1977 2612 2218 -48 -292 -423 C ATOM 522 CD BLYS A 79 -18.218 12.441 38.785 0.45 18.73 C ANISOU 522 CD BLYS A 79 1972 2945 2197 144 -356 -242 C ATOM 523 CE ALYS A 79 -18.309 10.245 37.520 0.55 19.93 C ANISOU 523 CE ALYS A 79 2102 2947 2522 -124 -438 -451 C ATOM 524 CE BLYS A 79 -19.360 11.643 38.179 0.45 20.81 C ANISOU 524 CE BLYS A 79 2225 3090 2590 -18 -433 -347 C ATOM 525 NZ ALYS A 79 -18.581 8.784 37.593 0.55 21.66 N ANISOU 525 NZ ALYS A 79 2524 2965 2738 -204 -108 -477 N ATOM 526 NZ BLYS A 79 -20.680 12.295 38.399 0.45 22.43 N ANISOU 526 NZ BLYS A 79 2237 3420 2864 4 -236 -307 N ATOM 527 N GLN A 80 -13.513 13.129 36.922 1.00 14.22 N ANISOU 527 N GLN A 80 2093 2112 1195 118 -600 -257 N ATOM 528 CA AGLN A 80 -13.164 13.323 35.510 0.60 15.18 C ANISOU 528 CA AGLN A 80 2299 2333 1133 139 -596 -320 C ATOM 529 CA BGLN A 80 -13.188 13.289 35.507 0.40 15.32 C ANISOU 529 CA BGLN A 80 2321 2301 1199 124 -521 -296 C ATOM 530 C GLN A 80 -11.893 12.583 35.096 1.00 15.39 C ANISOU 530 C GLN A 80 2541 2277 1030 185 -323 -300 C ATOM 531 O GLN A 80 -11.845 11.967 34.035 1.00 17.51 O ANISOU 531 O GLN A 80 2925 2640 1085 -2 -370 -504 O ATOM 532 CB AGLN A 80 -12.998 14.823 35.217 0.60 16.51 C ANISOU 532 CB AGLN A 80 2643 2394 1233 275 -413 -149 C ATOM 533 CB BGLN A 80 -13.133 14.773 35.135 0.40 17.05 C ANISOU 533 CB BGLN A 80 2570 2375 1533 215 -441 -129 C ATOM 534 CG AGLN A 80 -12.477 15.157 33.823 0.60 17.47 C ANISOU 534 CG AGLN A 80 2750 2689 1197 159 -440 -133 C ATOM 535 CG BGLN A 80 -14.489 15.460 35.199 0.40 18.45 C ANISOU 535 CG BGLN A 80 2594 2583 1833 283 -532 -92 C ATOM 536 CD AGLN A 80 -12.387 16.652 33.572 0.60 20.22 C ANISOU 536 CD AGLN A 80 3119 2754 1809 212 -292 33 C ATOM 537 CD BGLN A 80 -14.454 16.879 34.668 0.40 20.90 C ANISOU 537 CD BGLN A 80 2955 2615 2368 182 -393 13 C ATOM 538 OE1AGLN A 80 -13.405 17.335 33.466 0.60 23.60 O ANISOU 538 OE1AGLN A 80 3409 3158 2399 456 -519 53 O ATOM 539 OE1BGLN A 80 -13.608 17.224 33.846 0.40 23.84 O ANISOU 539 OE1BGLN A 80 3405 3152 2498 140 -174 167 O ATOM 540 NE2AGLN A 80 -11.164 17.169 33.470 0.60 20.20 N ANISOU 540 NE2AGLN A 80 3031 2659 1984 412 -89 17 N ATOM 541 NE2BGLN A 80 -15.382 17.707 35.132 0.40 20.78 N ANISOU 541 NE2BGLN A 80 2691 2823 2381 141 -389 65 N ATOM 542 N GLU A 81 -10.857 12.666 35.928 1.00 13.74 N ANISOU 542 N GLU A 81 2334 1936 949 221 -156 -235 N ATOM 543 CA GLU A 81 -9.522 12.204 35.540 1.00 13.88 C ANISOU 543 CA GLU A 81 2436 1736 1101 227 28 -178 C ATOM 544 C GLU A 81 -9.157 10.809 36.030 1.00 13.45 C ANISOU 544 C GLU A 81 2380 1622 1109 163 155 -239 C ATOM 545 O GLU A 81 -8.238 10.200 35.495 1.00 16.62 O ANISOU 545 O GLU A 81 2927 1861 1524 427 600 -97 O ATOM 546 CB GLU A 81 -8.468 13.210 36.004 1.00 14.65 C ANISOU 546 CB GLU A 81 2631 1837 1095 103 -28 -168 C ATOM 547 CG GLU A 81 -8.646 14.606 35.423 1.00 16.42 C ANISOU 547 CG GLU A 81 3026 1835 1375 137 -85 -149 C ATOM 548 CD GLU A 81 -8.349 14.696 33.938 1.00 19.25 C ANISOU 548 CD GLU A 81 3650 2056 1606 -8 229 256 C ATOM 549 OE1 GLU A 81 -7.724 13.770 33.383 1.00 22.50 O ANISOU 549 OE1 GLU A 81 4320 2532 1694 96 503 -59 O ATOM 550 OE2 GLU A 81 -8.743 15.708 33.328 1.00 22.61 O ANISOU 550 OE2 GLU A 81 4197 2429 1962 80 -142 562 O ATOM 551 N ILE A 82 -9.862 10.305 37.040 1.00 12.28 N ANISOU 551 N ILE A 82 2043 1599 1022 223 13 -230 N ATOM 552 CA ILE A 82 -9.607 8.961 37.567 1.00 12.14 C ANISOU 552 CA ILE A 82 1968 1556 1088 147 5 -278 C ATOM 553 C ILE A 82 -10.864 8.097 37.502 1.00 12.54 C ANISOU 553 C ILE A 82 2024 1594 1145 132 -104 -271 C ATOM 554 O ILE A 82 -10.794 6.942 37.103 1.00 13.34 O ANISOU 554 O ILE A 82 2169 1585 1315 16 -56 -409 O ATOM 555 CB ILE A 82 -9.057 9.000 39.009 1.00 11.51 C ANISOU 555 CB ILE A 82 1787 1500 1085 141 14 -249 C ATOM 556 CG1 ILE A 82 -7.800 9.883 39.071 1.00 12.59 C ANISOU 556 CG1 ILE A 82 1832 1690 1260 66 85 -300 C ATOM 557 CG2 ILE A 82 -8.749 7.587 39.482 1.00 12.34 C ANISOU 557 CG2 ILE A 82 1946 1498 1243 127 -115 -241 C ATOM 558 CD1 ILE A 82 -7.263 10.120 40.466 1.00 12.51 C ANISOU 558 CD1 ILE A 82 1712 1686 1353 129 3 -242 C ATOM 559 N ASN A 83 -12.006 8.650 37.903 1.00 12.59 N ANISOU 559 N ASN A 83 1850 1761 1170 -18 -200 -365 N ATOM 560 CA ASN A 83 -13.294 7.965 37.796 1.00 13.91 C ANISOU 560 CA ASN A 83 1916 1836 1532 -86 -376 -379 C ATOM 561 C ASN A 83 -13.338 6.663 38.597 1.00 13.36 C ANISOU 561 C ASN A 83 1876 1815 1382 -215 -272 -451 C ATOM 562 O ASN A 83 -13.772 5.620 38.103 1.00 14.40 O ANISOU 562 O ASN A 83 2147 1873 1450 -325 -226 -506 O ATOM 563 CB ASN A 83 -13.657 7.713 36.329 1.00 15.93 C ANISOU 563 CB ASN A 83 2398 2126 1527 -201 -397 -371 C ATOM 564 CG ASN A 83 -15.104 7.317 36.154 1.00 18.00 C ANISOU 564 CG ASN A 83 2414 2567 1856 -179 -647 -399 C ATOM 565 OD1 ASN A 83 -15.961 7.673 36.962 1.00 18.61 O ANISOU 565 OD1 ASN A 83 2120 2693 2258 -156 -733 -684 O ATOM 566 ND2 ASN A 83 -15.386 6.567 35.102 1.00 20.93 N ANISOU 566 ND2 ASN A 83 2765 3199 1987 -383 -831 -611 N ATOM 567 N LEU A 84 -12.872 6.750 39.841 1.00 12.92 N ANISOU 567 N LEU A 84 1738 1770 1400 -165 -267 -402 N ATOM 568 CA LEU A 84 -12.991 5.673 40.819 1.00 12.65 C ANISOU 568 CA LEU A 84 1694 1734 1376 -238 -207 -490 C ATOM 569 C LEU A 84 -13.437 6.276 42.143 1.00 13.13 C ANISOU 569 C LEU A 84 1690 1845 1454 -212 -119 -513 C ATOM 570 O LEU A 84 -13.210 7.454 42.389 1.00 13.10 O ANISOU 570 O LEU A 84 1677 1768 1533 -49 -216 -511 O ATOM 571 CB LEU A 84 -11.650 4.958 41.001 1.00 12.53 C ANISOU 571 CB LEU A 84 1696 1713 1349 -213 -139 -302 C ATOM 572 CG LEU A 84 -11.145 4.162 39.793 1.00 12.81 C ANISOU 572 CG LEU A 84 1724 1739 1402 -145 -108 -324 C ATOM 573 CD1 LEU A 84 -9.677 3.803 39.959 1.00 13.20 C ANISOU 573 CD1 LEU A 84 1793 1650 1571 -120 -19 -213 C ATOM 574 CD2 LEU A 84 -11.987 2.910 39.578 1.00 13.91 C ANISOU 574 CD2 LEU A 84 1949 1703 1630 -125 -122 -513 C ATOM 575 N PRO A 85 -14.056 5.467 43.015 1.00 13.04 N ANISOU 575 N PRO A 85 1665 1867 1419 -256 -57 -588 N ATOM 576 CA PRO A 85 -14.530 5.985 44.293 1.00 12.65 C ANISOU 576 CA PRO A 85 1373 2022 1409 -277 42 -449 C ATOM 577 C PRO A 85 -13.403 6.443 45.198 1.00 11.46 C ANISOU 577 C PRO A 85 1422 1618 1312 -202 7 -345 C ATOM 578 O PRO A 85 -12.336 5.835 45.217 1.00 11.89 O ANISOU 578 O PRO A 85 1436 1635 1444 -157 -22 -481 O ATOM 579 CB PRO A 85 -15.242 4.781 44.926 1.00 15.18 C ANISOU 579 CB PRO A 85 1741 2175 1849 -637 -85 -425 C ATOM 580 CG PRO A 85 -14.688 3.586 44.233 1.00 17.28 C ANISOU 580 CG PRO A 85 2279 2177 2109 -543 370 -292 C ATOM 581 CD PRO A 85 -14.397 4.042 42.838 1.00 14.55 C ANISOU 581 CD PRO A 85 1802 1946 1781 -447 56 -556 C ATOM 582 N VAL A 86 -13.659 7.510 45.947 1.00 10.89 N ANISOU 582 N VAL A 86 1213 1613 1312 -102 72 -302 N ATOM 583 CA VAL A 86 -12.735 7.985 46.969 1.00 10.54 C ANISOU 583 CA VAL A 86 1228 1422 1352 -118 125 -395 C ATOM 584 C VAL A 86 -13.049 7.250 48.264 1.00 10.87 C ANISOU 584 C VAL A 86 1247 1425 1457 -277 149 -391 C ATOM 585 O VAL A 86 -14.094 7.480 48.879 1.00 12.91 O ANISOU 585 O VAL A 86 1394 1879 1630 -219 328 -263 O ATOM 586 CB VAL A 86 -12.812 9.507 47.153 1.00 10.86 C ANISOU 586 CB VAL A 86 1160 1414 1551 -4 132 -269 C ATOM 587 CG1 VAL A 86 -11.832 9.959 48.225 1.00 11.09 C ANISOU 587 CG1 VAL A 86 1249 1347 1617 -91 181 -404 C ATOM 588 CG2 VAL A 86 -12.504 10.210 45.840 1.00 11.98 C ANISOU 588 CG2 VAL A 86 1413 1447 1691 73 251 -146 C ATOM 589 N ALA A 87 -12.145 6.358 48.665 1.00 10.01 N ANISOU 589 N ALA A 87 1297 1303 1200 -387 146 -375 N ATOM 590 CA ALA A 87 -12.374 5.504 49.826 1.00 10.88 C ANISOU 590 CA ALA A 87 1490 1436 1205 -542 184 -370 C ATOM 591 C ALA A 87 -12.219 6.224 51.157 1.00 10.94 C ANISOU 591 C ALA A 87 1508 1472 1174 -592 87 -315 C ATOM 592 O ALA A 87 -12.908 5.900 52.117 1.00 14.22 O ANISOU 592 O ALA A 87 1995 2136 1270 -1082 253 -395 O ATOM 593 CB ALA A 87 -11.438 4.314 49.796 1.00 12.10 C ANISOU 593 CB ALA A 87 1894 1338 1362 -430 99 -275 C ATOM 594 N LEU A 88 -11.293 7.172 51.232 1.00 9.03 N ANISOU 594 N LEU A 88 1172 1163 1095 -277 41 -249 N ATOM 595 CA LEU A 88 -11.025 7.864 52.482 1.00 8.24 C ANISOU 595 CA LEU A 88 1084 1006 1037 -180 61 -183 C ATOM 596 C LEU A 88 -10.183 9.095 52.210 1.00 7.41 C ANISOU 596 C LEU A 88 935 942 936 -95 -54 -98 C ATOM 597 O LEU A 88 -9.538 9.216 51.161 1.00 7.90 O ANISOU 597 O LEU A 88 1001 1043 957 -144 -9 -161 O ATOM 598 CB LEU A 88 -10.314 6.956 53.491 1.00 9.23 C ANISOU 598 CB LEU A 88 1402 924 1179 -180 16 -137 C ATOM 599 CG LEU A 88 -8.932 6.446 53.090 1.00 10.89 C ANISOU 599 CG LEU A 88 1580 1206 1349 146 -89 -183 C ATOM 600 CD1 LEU A 88 -7.808 7.343 53.582 1.00 11.36 C ANISOU 600 CD1 LEU A 88 1459 1352 1505 107 -120 -14 C ATOM 601 CD2 LEU A 88 -8.726 5.035 53.611 1.00 13.57 C ANISOU 601 CD2 LEU A 88 1913 1215 2026 168 -321 -97 C ATOM 602 N ALA A 89 -10.175 9.978 53.195 1.00 7.30 N ANISOU 602 N ALA A 89 926 959 887 -126 61 -109 N ATOM 603 CA ALA A 89 -9.259 11.110 53.250 1.00 7.39 C ANISOU 603 CA ALA A 89 1026 843 935 -83 -17 -115 C ATOM 604 C ALA A 89 -8.639 11.184 54.625 1.00 7.03 C ANISOU 604 C ALA A 89 1004 742 924 -103 -12 -26 C ATOM 605 O ALA A 89 -9.309 10.907 55.636 1.00 7.99 O ANISOU 605 O ALA A 89 1121 987 925 -266 3 -30 O ATOM 606 CB ALA A 89 -9.975 12.410 52.955 1.00 7.92 C ANISOU 606 CB ALA A 89 1148 965 893 14 59 34 C ATOM 607 N VAL A 90 -7.367 11.564 54.660 1.00 6.75 N ANISOU 607 N VAL A 90 1004 834 726 -126 24 -21 N ATOM 608 CA VAL A 90 -6.666 11.860 55.905 1.00 6.79 C ANISOU 608 CA VAL A 90 1040 761 778 -103 -49 9 C ATOM 609 C VAL A 90 -6.209 13.313 55.818 1.00 6.06 C ANISOU 609 C VAL A 90 768 745 789 -36 -17 79 C ATOM 610 O VAL A 90 -5.725 13.748 54.769 1.00 6.72 O ANISOU 610 O VAL A 90 944 753 853 -72 117 92 O ATOM 611 CB VAL A 90 -5.508 10.869 56.173 1.00 7.62 C ANISOU 611 CB VAL A 90 1148 775 969 -54 -104 95 C ATOM 612 CG1 VAL A 90 -4.493 10.835 55.036 1.00 8.41 C ANISOU 612 CG1 VAL A 90 1114 929 1151 68 -15 195 C ATOM 613 CG2 VAL A 90 -4.851 11.164 57.510 1.00 8.53 C ANISOU 613 CG2 VAL A 90 1337 938 963 19 -170 107 C ATOM 614 N VAL A 91 -6.367 14.040 56.917 1.00 6.41 N ANISOU 614 N VAL A 91 891 711 834 -96 45 70 N ATOM 615 CA VAL A 91 -6.043 15.460 56.966 1.00 6.26 C ANISOU 615 CA VAL A 91 925 711 740 -82 75 49 C ATOM 616 C VAL A 91 -4.965 15.664 58.023 1.00 6.43 C ANISOU 616 C VAL A 91 984 611 847 -45 -46 80 C ATOM 617 O VAL A 91 -4.964 14.976 59.049 1.00 7.42 O ANISOU 617 O VAL A 91 1200 800 817 -193 -57 123 O ATOM 618 CB VAL A 91 -7.302 16.313 57.214 1.00 7.90 C ANISOU 618 CB VAL A 91 1008 940 1052 27 132 171 C ATOM 619 CG1 VAL A 91 -8.289 16.104 56.072 1.00 8.86 C ANISOU 619 CG1 VAL A 91 832 1208 1326 -3 39 392 C ATOM 620 CG2 VAL A 91 -7.970 15.982 58.544 1.00 9.06 C ANISOU 620 CG2 VAL A 91 1269 1061 1109 193 292 174 C ATOM 621 N THR A 92 -4.048 16.604 57.775 1.00 6.35 N ANISOU 621 N THR A 92 952 668 793 -61 -57 71 N ATOM 622 CA THR A 92 -2.763 16.580 58.473 1.00 6.70 C ANISOU 622 CA THR A 92 990 718 838 1 -104 77 C ATOM 623 C THR A 92 -2.563 17.578 59.610 1.00 6.62 C ANISOU 623 C THR A 92 924 773 816 -43 -46 63 C ATOM 624 O THR A 92 -1.523 17.522 60.247 1.00 7.46 O ANISOU 624 O THR A 92 966 958 909 55 -106 -52 O ATOM 625 CB THR A 92 -1.581 16.588 57.469 1.00 7.21 C ANISOU 625 CB THR A 92 905 847 987 20 -115 104 C ATOM 626 OG1 THR A 92 -1.577 17.810 56.729 1.00 7.09 O ANISOU 626 OG1 THR A 92 887 886 919 -26 -82 116 O ATOM 627 CG2 THR A 92 -1.623 15.400 56.524 1.00 7.60 C ANISOU 627 CG2 THR A 92 1051 965 871 63 -63 72 C ATOM 628 N HIS A 93 -3.533 18.458 59.858 1.00 6.82 N ANISOU 628 N HIS A 93 1017 736 838 -25 -94 0 N ATOM 629 CA HIS A 93 -3.691 19.165 61.142 1.00 7.08 C ANISOU 629 CA HIS A 93 1079 735 875 -55 -26 -13 C ATOM 630 C HIS A 93 -4.907 20.076 61.039 1.00 7.08 C ANISOU 630 C HIS A 93 1065 704 920 -91 -45 9 C ATOM 631 O HIS A 93 -5.473 20.278 59.959 1.00 7.41 O ANISOU 631 O HIS A 93 1042 853 921 -44 -32 36 O ATOM 632 CB HIS A 93 -2.453 19.952 61.619 1.00 7.54 C ANISOU 632 CB HIS A 93 1104 866 895 2 -175 -93 C ATOM 633 CG HIS A 93 -2.025 21.054 60.725 1.00 7.38 C ANISOU 633 CG HIS A 93 983 883 937 -63 -138 -114 C ATOM 634 ND1 HIS A 93 -1.250 20.839 59.610 1.00 8.08 N ANISOU 634 ND1 HIS A 93 996 1006 1068 -82 -68 -124 N ATOM 635 CD2 HIS A 93 -2.218 22.391 60.805 1.00 8.04 C ANISOU 635 CD2 HIS A 93 1189 856 1008 -149 -137 25 C ATOM 636 CE1 HIS A 93 -1.006 21.999 59.031 1.00 8.41 C ANISOU 636 CE1 HIS A 93 1033 1045 1115 -174 -90 -89 C ATOM 637 NE2 HIS A 93 -1.581 22.953 59.737 1.00 8.28 N ANISOU 637 NE2 HIS A 93 1128 891 1126 -181 -142 -45 N ATOM 638 N ALA A 94 -5.285 20.644 62.177 1.00 7.84 N ANISOU 638 N ALA A 94 1204 841 932 7 -24 -20 N ATOM 639 CA ALA A 94 -6.478 21.478 62.288 1.00 7.85 C ANISOU 639 CA ALA A 94 1205 818 957 -59 59 46 C ATOM 640 C ALA A 94 -6.193 22.953 61.978 1.00 8.35 C ANISOU 640 C ALA A 94 1401 789 982 -96 31 -51 C ATOM 641 O ALA A 94 -6.290 23.812 62.849 1.00 10.31 O ANISOU 641 O ALA A 94 1908 977 1030 -173 375 -146 O ATOM 642 CB ALA A 94 -7.109 21.320 63.672 1.00 8.87 C ANISOU 642 CB ALA A 94 1468 887 1016 -25 173 74 C ATOM 643 N HIS A 95 -5.831 23.206 60.717 1.00 7.89 N ANISOU 643 N HIS A 95 1332 709 955 -5 -15 13 N ATOM 644 CA HIS A 95 -5.841 24.543 60.134 1.00 7.77 C ANISOU 644 CA HIS A 95 1239 729 982 -47 78 43 C ATOM 645 C HIS A 95 -6.668 24.491 58.850 1.00 6.87 C ANISOU 645 C HIS A 95 935 749 926 -32 206 31 C ATOM 646 O HIS A 95 -6.875 23.422 58.264 1.00 7.04 O ANISOU 646 O HIS A 95 1008 743 922 -42 19 57 O ATOM 647 CB HIS A 95 -4.418 25.056 59.824 1.00 8.19 C ANISOU 647 CB HIS A 95 1217 803 1089 -75 9 -9 C ATOM 648 CG HIS A 95 -3.673 25.580 61.014 1.00 8.53 C ANISOU 648 CG HIS A 95 1371 787 1081 -123 -16 14 C ATOM 649 ND1 HIS A 95 -2.317 25.732 61.016 1.00 9.09 N ANISOU 649 ND1 HIS A 95 1336 961 1156 -224 -48 22 N ATOM 650 CD2 HIS A 95 -4.088 26.014 62.229 1.00 9.07 C ANISOU 650 CD2 HIS A 95 1324 958 1161 -86 69 -60 C ATOM 651 CE1 HIS A 95 -1.912 26.254 62.150 1.00 9.35 C ANISOU 651 CE1 HIS A 95 1331 920 1299 -202 -112 -44 C ATOM 652 NE2 HIS A 95 -2.971 26.442 62.912 1.00 9.74 N ANISOU 652 NE2 HIS A 95 1558 1013 1128 -99 -67 -172 N ATOM 653 N GLN A 96 -7.117 25.658 58.400 1.00 7.60 N ANISOU 653 N GLN A 96 1062 709 1114 -3 89 13 N ATOM 654 CA GLN A 96 -8.094 25.742 57.309 1.00 7.92 C ANISOU 654 CA GLN A 96 1038 762 1208 41 86 155 C ATOM 655 C GLN A 96 -7.630 25.145 56.001 1.00 7.32 C ANISOU 655 C GLN A 96 964 656 1161 50 -6 147 C ATOM 656 O GLN A 96 -8.427 24.586 55.251 1.00 8.02 O ANISOU 656 O GLN A 96 889 973 1185 -44 0 164 O ATOM 657 CB GLN A 96 -8.519 27.185 57.063 1.00 8.72 C ANISOU 657 CB GLN A 96 1200 864 1249 192 323 251 C ATOM 658 CG GLN A 96 -9.711 27.246 56.109 1.00 10.75 C ANISOU 658 CG GLN A 96 1472 1250 1362 431 145 330 C ATOM 659 CD GLN A 96 -10.100 28.608 55.654 1.00 12.05 C ANISOU 659 CD GLN A 96 1922 1256 1399 658 429 293 C ATOM 660 OE1 GLN A 96 -9.703 29.595 56.243 1.00 14.61 O ANISOU 660 OE1 GLN A 96 2939 1131 1481 541 406 195 O ATOM 661 NE2 GLN A 96 -10.918 28.668 54.604 1.00 14.62 N ANISOU 661 NE2 GLN A 96 2180 1793 1581 699 241 446 N ATOM 662 N ASP A 97 -6.345 25.306 55.692 1.00 7.31 N ANISOU 662 N ASP A 97 928 736 1114 31 -43 41 N ATOM 663 CA ASP A 97 -5.830 24.782 54.448 1.00 6.99 C ANISOU 663 CA ASP A 97 892 743 1020 57 -23 134 C ATOM 664 C ASP A 97 -5.900 23.264 54.348 1.00 6.32 C ANISOU 664 C ASP A 97 704 751 943 15 56 120 C ATOM 665 O ASP A 97 -5.909 22.716 53.257 1.00 7.36 O ANISOU 665 O ASP A 97 997 852 944 36 -23 89 O ATOM 666 CB ASP A 97 -4.416 25.294 54.155 1.00 7.52 C ANISOU 666 CB ASP A 97 850 851 1155 58 0 83 C ATOM 667 CG ASP A 97 -3.414 25.118 55.276 1.00 7.92 C ANISOU 667 CG ASP A 97 954 835 1217 -36 -65 123 C ATOM 668 OD1 ASP A 97 -3.751 25.006 56.473 1.00 9.40 O ANISOU 668 OD1 ASP A 97 1091 1275 1203 -166 -192 230 O ATOM 669 OD2 ASP A 97 -2.237 25.163 54.897 1.00 9.59 O ANISOU 669 OD2 ASP A 97 980 1334 1326 16 -100 41 O ATOM 670 N LYS A 98 -5.912 22.599 55.502 1.00 6.55 N ANISOU 670 N LYS A 98 893 711 883 50 -5 62 N ATOM 671 CA LYS A 98 -5.888 21.131 55.583 1.00 6.55 C ANISOU 671 CA LYS A 98 910 702 876 31 -7 32 C ATOM 672 C LYS A 98 -7.250 20.506 55.887 1.00 6.56 C ANISOU 672 C LYS A 98 909 726 855 33 -76 42 C ATOM 673 O LYS A 98 -7.489 19.358 55.505 1.00 6.75 O ANISOU 673 O LYS A 98 958 708 896 -4 -24 50 O ATOM 674 CB LYS A 98 -4.891 20.680 56.666 1.00 7.26 C ANISOU 674 CB LYS A 98 933 742 1083 6 -87 105 C ATOM 675 CG LYS A 98 -3.510 21.348 56.638 1.00 7.35 C ANISOU 675 CG LYS A 98 899 891 1003 16 -95 93 C ATOM 676 CD LYS A 98 -2.583 20.889 55.518 1.00 7.52 C ANISOU 676 CD LYS A 98 819 895 1142 -15 -39 151 C ATOM 677 CE LYS A 98 -2.839 21.516 54.156 1.00 7.42 C ANISOU 677 CE LYS A 98 917 908 992 46 -60 7 C ATOM 678 NZ LYS A 98 -2.058 20.823 53.098 1.00 7.72 N ANISOU 678 NZ LYS A 98 868 1005 1058 46 -9 10 N ATOM 679 N MET A 99 -8.103 21.244 56.608 1.00 6.86 N ANISOU 679 N MET A 99 933 704 966 -32 -14 20 N ATOM 680 CA AMET A 99 -9.387 20.708 57.096 0.72 6.79 C ANISOU 680 CA AMET A 99 999 748 833 -47 79 -15 C ATOM 681 CA BMET A 99 -9.353 20.734 57.133 0.28 7.14 C ANISOU 681 CA BMET A 99 978 806 925 -62 8 45 C ATOM 682 C MET A 99 -10.572 21.594 56.750 1.00 7.35 C ANISOU 682 C MET A 99 941 871 979 -62 -28 2 C ATOM 683 O MET A 99 -11.695 21.276 57.128 1.00 8.63 O ANISOU 683 O MET A 99 971 1087 1220 -110 -18 132 O ATOM 684 CB AMET A 99 -9.380 20.469 58.615 0.72 7.00 C ANISOU 684 CB AMET A 99 1160 649 851 -13 104 -11 C ATOM 685 CB BMET A 99 -9.209 20.673 58.649 0.28 7.86 C ANISOU 685 CB BMET A 99 1179 867 937 -29 -6 56 C ATOM 686 CG AMET A 99 -8.506 19.326 59.039 0.72 6.88 C ANISOU 686 CG AMET A 99 895 777 942 -58 171 112 C ATOM 687 CG BMET A 99 -9.936 19.540 59.316 0.28 7.90 C ANISOU 687 CG BMET A 99 1078 904 1019 -2 38 85 C ATOM 688 SD AMET A 99 -8.452 18.965 60.798 0.72 7.57 S ANISOU 688 SD AMET A 99 1080 860 935 -126 -23 115 S ATOM 689 SD BMET A 99 -9.289 19.313 60.980 0.28 8.98 S ANISOU 689 SD BMET A 99 1395 1034 980 -195 44 174 S ATOM 690 CE AMET A 99 -10.040 18.143 61.020 0.72 8.09 C ANISOU 690 CE AMET A 99 1113 897 1061 -69 101 172 C ATOM 691 CE BMET A 99 -10.204 17.846 61.446 0.28 8.11 C ANISOU 691 CE BMET A 99 1144 1133 802 -135 161 238 C ATOM 692 N GLY A 100 -10.361 22.676 56.004 1.00 7.19 N ANISOU 692 N GLY A 100 878 830 1021 0 15 42 N ATOM 693 CA GLY A 100 -11.436 23.607 55.685 1.00 7.88 C ANISOU 693 CA GLY A 100 895 898 1200 83 72 -10 C ATOM 694 C GLY A 100 -12.573 23.025 54.869 1.00 7.84 C ANISOU 694 C GLY A 100 827 1042 1110 90 69 90 C ATOM 695 O GLY A 100 -13.672 23.583 54.864 1.00 9.40 O ANISOU 695 O GLY A 100 902 1237 1432 216 39 -8 O ATOM 696 N GLY A 101 -12.321 21.925 54.162 1.00 7.62 N ANISOU 696 N GLY A 101 696 1086 1112 78 72 66 N ATOM 697 CA GLY A 101 -13.319 21.310 53.303 1.00 8.13 C ANISOU 697 CA GLY A 101 744 1188 1156 76 18 52 C ATOM 698 C GLY A 101 -13.905 20.019 53.816 1.00 7.78 C ANISOU 698 C GLY A 101 686 1169 1099 91 -26 -11 C ATOM 699 O GLY A 101 -14.467 19.253 53.035 1.00 8.51 O ANISOU 699 O GLY A 101 754 1352 1126 44 -109 -73 O ATOM 700 N MET A 102 -13.846 19.780 55.124 1.00 7.54 N ANISOU 700 N MET A 102 723 1007 1135 49 -39 -4 N ATOM 701 CA AMET A 102 -14.348 18.516 55.688 0.47 7.92 C ANISOU 701 CA AMET A 102 831 1050 1127 33 -35 14 C ATOM 702 CA BMET A 102 -14.338 18.536 55.691 0.53 7.95 C ANISOU 702 CA BMET A 102 858 1058 1104 16 -72 18 C ATOM 703 C MET A 102 -15.804 18.259 55.327 1.00 8.05 C ANISOU 703 C MET A 102 839 1127 1091 -18 -6 1 C ATOM 704 O MET A 102 -16.165 17.132 55.002 1.00 8.83 O ANISOU 704 O MET A 102 940 1166 1249 -70 -68 -25 O ATOM 705 CB AMET A 102 -14.226 18.462 57.212 0.47 7.86 C ANISOU 705 CB AMET A 102 794 1083 1110 48 90 -12 C ATOM 706 CB BMET A 102 -14.163 18.565 57.205 0.53 8.47 C ANISOU 706 CB BMET A 102 967 1155 1094 -12 -11 6 C ATOM 707 CG AMET A 102 -12.816 18.525 57.760 0.47 8.29 C ANISOU 707 CG AMET A 102 888 1141 1119 23 -16 -70 C ATOM 708 CG BMET A 102 -14.361 17.228 57.874 0.53 8.21 C ANISOU 708 CG BMET A 102 977 1064 1076 -65 -68 -92 C ATOM 709 SD AMET A 102 -11.640 17.372 57.039 0.47 7.83 S ANISOU 709 SD AMET A 102 887 972 1114 -8 0 97 S ATOM 710 SD BMET A 102 -13.155 15.983 57.378 0.53 8.77 S ANISOU 710 SD BMET A 102 1220 972 1140 62 -115 -32 S ATOM 711 CE AMET A 102 -12.182 15.851 57.793 0.47 9.32 C ANISOU 711 CE AMET A 102 1157 1084 1299 -162 345 38 C ATOM 712 CE BMET A 102 -11.673 16.649 58.129 0.53 9.09 C ANISOU 712 CE BMET A 102 995 1321 1137 -29 58 123 C ATOM 713 N ASP A 103 -16.649 19.284 55.395 1.00 8.23 N ANISOU 713 N ASP A 103 799 1160 1167 -10 1 4 N ATOM 714 CA ASP A 103 -18.063 19.090 55.093 1.00 9.20 C ANISOU 714 CA ASP A 103 806 1289 1398 -26 -52 15 C ATOM 715 C ASP A 103 -18.267 18.576 53.670 1.00 9.09 C ANISOU 715 C ASP A 103 688 1296 1467 19 17 -42 C ATOM 716 O ASP A 103 -19.165 17.781 53.432 1.00 9.70 O ANISOU 716 O ASP A 103 658 1401 1624 -42 37 -141 O ATOM 717 CB ASP A 103 -18.864 20.392 55.283 1.00 9.71 C ANISOU 717 CB ASP A 103 755 1464 1470 42 -50 -115 C ATOM 718 CG ASP A 103 -19.363 20.631 56.729 1.00 10.62 C ANISOU 718 CG ASP A 103 1004 1530 1499 -20 -42 -192 C ATOM 719 OD1 ASP A 103 -19.436 19.708 57.552 1.00 11.81 O ANISOU 719 OD1 ASP A 103 1213 1759 1515 -167 24 -77 O ATOM 720 OD2 ASP A 103 -19.769 21.774 57.027 1.00 12.74 O ANISOU 720 OD2 ASP A 103 1351 1823 1666 237 179 -323 O ATOM 721 N ALA A 104 -17.470 19.040 52.714 1.00 8.75 N ANISOU 721 N ALA A 104 692 1268 1364 -12 -82 -17 N ATOM 722 CA ALA A 104 -17.585 18.540 51.343 1.00 8.99 C ANISOU 722 CA ALA A 104 691 1410 1311 56 -25 20 C ATOM 723 C ALA A 104 -17.252 17.060 51.247 1.00 8.96 C ANISOU 723 C ALA A 104 749 1365 1289 -9 -15 23 C ATOM 724 O ALA A 104 -17.909 16.316 50.514 1.00 9.82 O ANISOU 724 O ALA A 104 873 1444 1415 39 -137 -71 O ATOM 725 CB ALA A 104 -16.716 19.341 50.393 1.00 9.86 C ANISOU 725 CB ALA A 104 795 1522 1427 90 -9 122 C ATOM 726 N LEU A 105 -16.247 16.617 51.992 1.00 8.67 N ANISOU 726 N LEU A 105 699 1256 1337 33 14 -40 N ATOM 727 CA LEU A 105 -15.925 15.190 52.010 1.00 8.86 C ANISOU 727 CA LEU A 105 821 1250 1293 14 -48 -77 C ATOM 728 C LEU A 105 -17.094 14.395 52.612 1.00 8.81 C ANISOU 728 C LEU A 105 840 1206 1302 9 -96 -97 C ATOM 729 O LEU A 105 -17.473 13.336 52.103 1.00 9.71 O ANISOU 729 O LEU A 105 886 1333 1469 -37 -40 -251 O ATOM 730 CB LEU A 105 -14.650 14.926 52.798 1.00 8.84 C ANISOU 730 CB LEU A 105 840 1162 1356 31 -59 22 C ATOM 731 CG LEU A 105 -13.376 15.569 52.242 1.00 8.78 C ANISOU 731 CG LEU A 105 818 1072 1444 80 -3 26 C ATOM 732 CD1 LEU A 105 -12.215 15.195 53.148 1.00 9.30 C ANISOU 732 CD1 LEU A 105 730 1099 1702 -57 -54 158 C ATOM 733 CD2 LEU A 105 -13.081 15.165 50.798 1.00 10.40 C ANISOU 733 CD2 LEU A 105 1077 1346 1526 -23 134 -38 C ATOM 734 N HIS A 106 -17.645 14.895 53.711 1.00 9.17 N ANISOU 734 N HIS A 106 904 1179 1401 -103 -71 -167 N ATOM 735 CA HIS A 106 -18.751 14.214 54.370 1.00 9.87 C ANISOU 735 CA HIS A 106 858 1286 1603 -168 -7 -223 C ATOM 736 C HIS A 106 -19.995 14.174 53.501 1.00 10.28 C ANISOU 736 C HIS A 106 891 1468 1544 -224 15 -182 C ATOM 737 O HIS A 106 -20.669 13.140 53.432 1.00 11.63 O ANISOU 737 O HIS A 106 950 1600 1866 -329 108 -227 O ATOM 738 CB HIS A 106 -19.020 14.831 55.729 1.00 9.79 C ANISOU 738 CB HIS A 106 983 1219 1516 -111 22 -120 C ATOM 739 CG HIS A 106 -17.884 14.645 56.677 1.00 9.49 C ANISOU 739 CG HIS A 106 1064 1144 1398 -56 61 -78 C ATOM 740 ND1 HIS A 106 -17.738 15.368 57.835 1.00 9.95 N ANISOU 740 ND1 HIS A 106 1140 1332 1307 103 159 -115 N ATOM 741 CD2 HIS A 106 -16.814 13.819 56.612 1.00 9.76 C ANISOU 741 CD2 HIS A 106 1155 1224 1328 17 52 -26 C ATOM 742 CE1 HIS A 106 -16.641 14.971 58.458 1.00 10.85 C ANISOU 742 CE1 HIS A 106 1389 1427 1306 242 -5 -142 C ATOM 743 NE2 HIS A 106 -16.050 14.043 57.727 1.00 10.43 N ANISOU 743 NE2 HIS A 106 1364 1284 1315 258 -58 -57 N ATOM 744 N ALA A 107 -20.281 15.269 52.809 1.00 10.20 N ANISOU 744 N ALA A 107 755 1488 1631 -80 -37 -228 N ATOM 745 CA ALA A 107 -21.422 15.310 51.902 1.00 10.99 C ANISOU 745 CA ALA A 107 696 1791 1687 -15 -21 -297 C ATOM 746 C ALA A 107 -21.281 14.279 50.788 1.00 11.34 C ANISOU 746 C ALA A 107 737 1746 1824 -34 -85 -367 C ATOM 747 O ALA A 107 -22.267 13.734 50.300 1.00 12.92 O ANISOU 747 O ALA A 107 817 2138 1952 -46 -156 -608 O ATOM 748 CB ALA A 107 -21.585 16.704 51.323 1.00 11.66 C ANISOU 748 CB ALA A 107 815 1795 1819 -21 -109 -287 C ATOM 749 N ALA A 108 -20.041 13.998 50.401 1.00 10.92 N ANISOU 749 N ALA A 108 811 1768 1570 8 -77 -380 N ATOM 750 CA ALA A 108 -19.739 13.037 49.348 1.00 12.03 C ANISOU 750 CA ALA A 108 921 1816 1832 54 -69 -497 C ATOM 751 C ALA A 108 -19.693 11.589 49.843 1.00 12.24 C ANISOU 751 C ALA A 108 1023 1795 1831 -67 -176 -516 C ATOM 752 O ALA A 108 -19.492 10.683 49.044 1.00 14.06 O ANISOU 752 O ALA A 108 1375 1933 2031 -144 -19 -672 O ATOM 753 CB ALA A 108 -18.412 13.402 48.685 1.00 12.30 C ANISOU 753 CB ALA A 108 1089 1850 1732 91 -15 -339 C ATOM 754 N GLY A 109 -19.872 11.374 51.147 1.00 11.64 N ANISOU 754 N GLY A 109 918 1596 1906 -188 -118 -374 N ATOM 755 CA GLY A 109 -19.874 10.031 51.728 1.00 13.19 C ANISOU 755 CA GLY A 109 1153 1649 2209 -321 -100 -269 C ATOM 756 C GLY A 109 -18.495 9.429 51.946 1.00 12.32 C ANISOU 756 C GLY A 109 1167 1458 2055 -308 -39 -320 C ATOM 757 O GLY A 109 -18.362 8.215 52.064 1.00 14.69 O ANISOU 757 O GLY A 109 1356 1448 2776 -350 -125 -216 O ATOM 758 N ILE A 110 -17.471 10.273 52.016 1.00 10.28 N ANISOU 758 N ILE A 110 1028 1257 1618 -168 -14 -240 N ATOM 759 CA ILE A 110 -16.093 9.815 52.153 1.00 10.08 C ANISOU 759 CA ILE A 110 1121 1194 1514 -116 -14 -265 C ATOM 760 C ILE A 110 -15.730 9.696 53.635 1.00 9.90 C ANISOU 760 C ILE A 110 1093 1162 1505 -210 38 -233 C ATOM 761 O ILE A 110 -15.991 10.604 54.413 1.00 11.32 O ANISOU 761 O ILE A 110 1470 1318 1510 9 119 -257 O ATOM 762 CB ILE A 110 -15.142 10.788 51.430 1.00 9.60 C ANISOU 762 CB ILE A 110 1021 1237 1387 0 45 -249 C ATOM 763 CG1 ILE A 110 -15.433 10.780 49.924 1.00 10.25 C ANISOU 763 CG1 ILE A 110 1012 1469 1411 18 64 -274 C ATOM 764 CG2 ILE A 110 -13.681 10.438 51.709 1.00 9.86 C ANISOU 764 CG2 ILE A 110 1055 1361 1327 -8 -37 -112 C ATOM 765 CD1 ILE A 110 -14.839 11.944 49.169 1.00 10.81 C ANISOU 765 CD1 ILE A 110 1099 1538 1468 118 85 -118 C ATOM 766 N ALA A 111 -15.126 8.572 54.014 1.00 9.67 N ANISOU 766 N ALA A 111 1172 1111 1392 -259 32 -233 N ATOM 767 CA ALA A 111 -14.655 8.360 55.384 1.00 9.67 C ANISOU 767 CA ALA A 111 1185 1128 1357 -277 91 -129 C ATOM 768 C ALA A 111 -13.438 9.230 55.663 1.00 8.47 C ANISOU 768 C ALA A 111 1079 958 1178 -183 115 -71 C ATOM 769 O ALA A 111 -12.486 9.222 54.881 1.00 9.24 O ANISOU 769 O ALA A 111 1076 1187 1245 -263 139 -239 O ATOM 770 CB ALA A 111 -14.303 6.902 55.604 1.00 10.27 C ANISOU 770 CB ALA A 111 1341 1126 1435 -392 38 -9 C ATOM 771 N THR A 112 -13.454 9.957 56.775 1.00 8.16 N ANISOU 771 N THR A 112 1023 941 1135 -199 110 -31 N ATOM 772 CA THR A 112 -12.397 10.913 57.074 1.00 8.01 C ANISOU 772 CA THR A 112 1043 831 1167 -121 31 -69 C ATOM 773 C THR A 112 -11.662 10.585 58.368 1.00 7.74 C ANISOU 773 C THR A 112 1143 693 1103 -197 84 -30 C ATOM 774 O THR A 112 -12.244 10.099 59.343 1.00 8.02 O ANISOU 774 O THR A 112 1142 808 1095 -129 105 -1 O ATOM 775 CB THR A 112 -12.948 12.333 57.126 1.00 8.27 C ANISOU 775 CB THR A 112 1172 871 1098 -49 71 -16 C ATOM 776 OG1 THR A 112 -13.953 12.388 58.141 1.00 8.84 O ANISOU 776 OG1 THR A 112 1212 1042 1102 84 135 -69 O ATOM 777 CG2 THR A 112 -13.514 12.732 55.770 1.00 9.08 C ANISOU 777 CG2 THR A 112 1320 1010 1118 2 22 -3 C ATOM 778 N TYR A 113 -10.367 10.891 58.348 1.00 6.95 N ANISOU 778 N TYR A 113 1124 677 838 -132 106 -38 N ATOM 779 CA TYR A 113 -9.421 10.550 59.407 1.00 6.95 C ANISOU 779 CA TYR A 113 1031 738 871 -117 166 5 C ATOM 780 C TYR A 113 -8.525 11.744 59.715 1.00 6.97 C ANISOU 780 C TYR A 113 1128 735 783 -108 139 -26 C ATOM 781 O TYR A 113 -8.085 12.446 58.803 1.00 7.69 O ANISOU 781 O TYR A 113 1269 871 779 -268 83 2 O ATOM 782 CB TYR A 113 -8.525 9.378 58.963 1.00 7.51 C ANISOU 782 CB TYR A 113 1096 749 1006 -107 138 -37 C ATOM 783 CG TYR A 113 -9.310 8.112 58.725 1.00 7.83 C ANISOU 783 CG TYR A 113 1137 744 1091 -94 223 -64 C ATOM 784 CD1 TYR A 113 -9.974 7.907 57.521 1.00 8.30 C ANISOU 784 CD1 TYR A 113 1256 761 1134 -94 173 -100 C ATOM 785 CD2 TYR A 113 -9.434 7.148 59.715 1.00 8.71 C ANISOU 785 CD2 TYR A 113 1302 802 1203 -6 273 24 C ATOM 786 CE1 TYR A 113 -10.754 6.785 57.317 1.00 9.24 C ANISOU 786 CE1 TYR A 113 1156 929 1424 -141 176 -216 C ATOM 787 CE2 TYR A 113 -10.208 6.015 59.514 1.00 9.92 C ANISOU 787 CE2 TYR A 113 1510 776 1480 -51 355 1 C ATOM 788 CZ TYR A 113 -10.875 5.852 58.317 1.00 10.14 C ANISOU 788 CZ TYR A 113 1368 869 1613 -223 359 -173 C ATOM 789 OH TYR A 113 -11.667 4.746 58.096 1.00 12.60 O ANISOU 789 OH TYR A 113 1630 972 2184 -393 418 -280 O ATOM 790 N ALA A 114 -8.230 11.934 60.996 1.00 6.94 N ANISOU 790 N ALA A 114 1094 752 788 -109 128 6 N ATOM 791 CA ALA A 114 -7.266 12.938 61.433 1.00 7.07 C ANISOU 791 CA ALA A 114 1139 794 751 -112 97 -7 C ATOM 792 C ALA A 114 -6.650 12.457 62.730 1.00 7.19 C ANISOU 792 C ALA A 114 1253 730 746 -72 93 15 C ATOM 793 O ALA A 114 -7.238 11.647 63.444 1.00 7.91 O ANISOU 793 O ALA A 114 1313 766 926 -86 42 136 O ATOM 794 CB ALA A 114 -7.949 14.285 61.661 1.00 7.54 C ANISOU 794 CB ALA A 114 1207 771 887 -122 21 -2 C ATOM 795 N ASN A 115 -5.488 12.993 63.069 1.00 7.27 N ANISOU 795 N ASN A 115 1208 788 766 -50 48 46 N ATOM 796 CA ASN A 115 -4.942 12.831 64.408 1.00 7.97 C ANISOU 796 CA ASN A 115 1434 759 834 -8 -33 64 C ATOM 797 C ASN A 115 -6.053 13.118 65.438 1.00 8.00 C ANISOU 797 C ASN A 115 1404 782 852 -43 -5 13 C ATOM 798 O ASN A 115 -6.778 14.110 65.297 1.00 7.86 O ANISOU 798 O ASN A 115 1435 789 761 -21 59 61 O ATOM 799 CB ASN A 115 -3.781 13.830 64.556 1.00 8.47 C ANISOU 799 CB ASN A 115 1445 872 898 -46 -117 122 C ATOM 800 CG ASN A 115 -3.020 13.736 65.866 1.00 9.09 C ANISOU 800 CG ASN A 115 1531 979 942 -79 -189 163 C ATOM 801 OD1 ASN A 115 -3.399 13.040 66.795 1.00 10.38 O ANISOU 801 OD1 ASN A 115 1652 1284 1007 -125 -254 324 O ATOM 802 ND2 ASN A 115 -1.924 14.478 65.936 1.00 10.04 N ANISOU 802 ND2 ASN A 115 1555 1142 1117 -168 -311 74 N ATOM 803 N ALA A 116 -6.182 12.275 66.455 1.00 8.56 N ANISOU 803 N ALA A 116 1578 775 896 96 29 50 N ATOM 804 CA ALA A 116 -7.110 12.535 67.560 1.00 9.25 C ANISOU 804 CA ALA A 116 1685 887 943 -19 97 113 C ATOM 805 C ALA A 116 -7.004 13.990 68.028 1.00 8.98 C ANISOU 805 C ALA A 116 1812 958 638 -1 109 109 C ATOM 806 O ALA A 116 -8.020 14.629 68.301 1.00 9.61 O ANISOU 806 O ALA A 116 1866 914 872 11 164 74 O ATOM 807 CB ALA A 116 -6.841 11.596 68.724 1.00 10.27 C ANISOU 807 CB ALA A 116 1991 969 940 -84 182 196 C ATOM 808 N LEU A 117 -5.783 14.499 68.162 1.00 9.39 N ANISOU 808 N LEU A 117 1838 905 824 -12 60 43 N ATOM 809 CA LEU A 117 -5.597 15.858 68.650 1.00 9.66 C ANISOU 809 CA LEU A 117 1880 923 867 -5 -61 -17 C ATOM 810 C LEU A 117 -6.161 16.880 67.661 1.00 9.03 C ANISOU 810 C LEU A 117 1744 876 810 -92 -35 -20 C ATOM 811 O LEU A 117 -6.714 17.897 68.074 1.00 9.50 O ANISOU 811 O LEU A 117 1865 933 809 -24 -5 -41 O ATOM 812 CB LEU A 117 -4.125 16.136 68.952 1.00 10.72 C ANISOU 812 CB LEU A 117 1882 1138 1050 -23 -121 117 C ATOM 813 CG LEU A 117 -3.796 17.512 69.539 1.00 11.54 C ANISOU 813 CG LEU A 117 1943 1349 1092 -44 -122 -114 C ATOM 814 CD1 LEU A 117 -4.572 17.791 70.821 1.00 13.01 C ANISOU 814 CD1 LEU A 117 2208 1678 1055 -161 -99 -281 C ATOM 815 CD2 LEU A 117 -2.302 17.615 69.793 1.00 13.29 C ANISOU 815 CD2 LEU A 117 1974 1747 1327 -232 -245 -82 C ATOM 816 N SER A 118 -6.030 16.627 66.360 1.00 8.28 N ANISOU 816 N SER A 118 1546 802 795 -10 -9 10 N ATOM 817 CA SER A 118 -6.638 17.503 65.366 1.00 7.85 C ANISOU 817 CA SER A 118 1453 747 780 -61 -1 7 C ATOM 818 C SER A 118 -8.154 17.536 65.515 1.00 7.88 C ANISOU 818 C SER A 118 1507 753 735 -33 73 44 C ATOM 819 O SER A 118 -8.768 18.592 65.396 1.00 8.73 O ANISOU 819 O SER A 118 1491 840 984 35 117 42 O ATOM 820 CB SER A 118 -6.295 17.063 63.941 1.00 7.76 C ANISOU 820 CB SER A 118 1430 742 774 -71 5 63 C ATOM 821 OG SER A 118 -4.903 16.966 63.713 1.00 8.11 O ANISOU 821 OG SER A 118 1379 886 815 -73 -20 20 O ATOM 822 N ASN A 119 -8.769 16.376 65.737 1.00 8.04 N ANISOU 822 N ASN A 119 1471 750 833 -5 115 9 N ATOM 823 CA ASN A 119 -10.217 16.341 65.927 1.00 8.58 C ANISOU 823 CA ASN A 119 1490 854 915 -31 97 46 C ATOM 824 C ASN A 119 -10.626 17.075 67.190 1.00 8.97 C ANISOU 824 C ASN A 119 1668 792 946 -44 194 80 C ATOM 825 O ASN A 119 -11.641 17.768 67.205 1.00 10.09 O ANISOU 825 O ASN A 119 1726 925 1182 33 180 -33 O ATOM 826 CB ASN A 119 -10.723 14.911 65.929 1.00 8.54 C ANISOU 826 CB ASN A 119 1424 821 1000 -4 122 26 C ATOM 827 CG ASN A 119 -10.691 14.308 64.548 1.00 8.24 C ANISOU 827 CG ASN A 119 1299 844 984 -73 129 30 C ATOM 828 OD1 ASN A 119 -10.772 15.026 63.543 1.00 8.65 O ANISOU 828 OD1 ASN A 119 1393 959 933 -91 24 55 O ATOM 829 ND2 ASN A 119 -10.551 12.992 64.480 1.00 9.03 N ANISOU 829 ND2 ASN A 119 1579 858 993 -79 249 51 N ATOM 830 N GLN A 120 -9.828 16.956 68.248 1.00 9.43 N ANISOU 830 N GLN A 120 1782 895 906 40 213 19 N ATOM 831 CA GLN A 120 -10.087 17.698 69.469 1.00 10.08 C ANISOU 831 CA GLN A 120 1964 970 894 -49 191 -30 C ATOM 832 C GLN A 120 -10.033 19.209 69.232 1.00 9.75 C ANISOU 832 C GLN A 120 1938 995 770 -56 253 -42 C ATOM 833 O GLN A 120 -10.875 19.939 69.749 1.00 11.30 O ANISOU 833 O GLN A 120 2103 1096 1094 18 480 -11 O ATOM 834 CB GLN A 120 -9.080 17.298 70.540 1.00 11.02 C ANISOU 834 CB GLN A 120 2252 1038 896 -47 118 127 C ATOM 835 CG GLN A 120 -9.304 17.957 71.885 1.00 13.78 C ANISOU 835 CG GLN A 120 2756 1423 1054 44 33 -115 C ATOM 836 CD GLN A 120 -8.118 17.747 72.804 1.00 15.27 C ANISOU 836 CD GLN A 120 2835 1766 1198 -8 -54 -17 C ATOM 837 OE1 GLN A 120 -7.678 16.619 73.015 1.00 18.56 O ANISOU 837 OE1 GLN A 120 3368 1905 1777 105 -504 144 O ATOM 838 NE2 GLN A 120 -7.587 18.832 73.348 1.00 17.06 N ANISOU 838 NE2 GLN A 120 3030 1977 1475 -170 -155 -149 N ATOM 839 N LEU A 121 -9.022 19.651 68.496 1.00 9.43 N ANISOU 839 N LEU A 121 1819 894 867 13 198 11 N ATOM 840 CA LEU A 121 -8.793 21.064 68.238 1.00 9.30 C ANISOU 840 CA LEU A 121 1809 919 804 -1 181 -23 C ATOM 841 C LEU A 121 -9.715 21.652 67.189 1.00 8.85 C ANISOU 841 C LEU A 121 1640 903 819 15 250 -33 C ATOM 842 O LEU A 121 -9.866 22.860 67.116 1.00 9.58 O ANISOU 842 O LEU A 121 1752 870 1018 -66 39 -17 O ATOM 843 CB LEU A 121 -7.354 21.287 67.780 1.00 9.54 C ANISOU 843 CB LEU A 121 1795 898 930 6 134 -83 C ATOM 844 CG LEU A 121 -6.247 21.040 68.797 1.00 11.21 C ANISOU 844 CG LEU A 121 1976 1049 1234 1 -110 -146 C ATOM 845 CD1 LEU A 121 -4.885 21.077 68.123 1.00 12.70 C ANISOU 845 CD1 LEU A 121 1988 1189 1645 6 -107 -40 C ATOM 846 CD2 LEU A 121 -6.313 22.035 69.945 1.00 13.83 C ANISOU 846 CD2 LEU A 121 2102 1585 1566 197 -230 -578 C ATOM 847 N ALA A 122 -10.308 20.816 66.352 1.00 9.69 N ANISOU 847 N ALA A 122 1790 816 1076 101 72 -103 N ATOM 848 CA ALA A 122 -11.027 21.312 65.183 1.00 10.07 C ANISOU 848 CA ALA A 122 1757 900 1167 77 -61 -150 C ATOM 849 C ALA A 122 -12.077 22.382 65.513 1.00 9.68 C ANISOU 849 C ALA A 122 1678 810 1187 -30 -3 -136 C ATOM 850 O ALA A 122 -12.052 23.454 64.931 1.00 9.67 O ANISOU 850 O ALA A 122 1660 816 1198 12 52 -117 O ATOM 851 CB ALA A 122 -11.638 20.147 64.401 1.00 11.08 C ANISOU 851 CB ALA A 122 1918 957 1336 93 -152 -224 C ATOM 852 N PRO A 123 -12.984 22.120 66.471 1.00 10.71 N ANISOU 852 N PRO A 123 1733 909 1425 -12 130 -35 N ATOM 853 CA PRO A 123 -14.020 23.127 66.697 1.00 11.45 C ANISOU 853 CA PRO A 123 1652 1079 1618 -14 257 -46 C ATOM 854 C PRO A 123 -13.457 24.504 67.060 1.00 10.76 C ANISOU 854 C PRO A 123 1859 1011 1219 32 414 -76 C ATOM 855 O PRO A 123 -13.890 25.511 66.500 1.00 12.20 O ANISOU 855 O PRO A 123 1935 1030 1670 92 293 -15 O ATOM 856 CB PRO A 123 -14.847 22.520 67.827 1.00 13.21 C ANISOU 856 CB PRO A 123 1743 1440 1834 -115 315 148 C ATOM 857 CG PRO A 123 -14.695 21.048 67.625 1.00 14.34 C ANISOU 857 CG PRO A 123 1982 1430 2035 -193 358 145 C ATOM 858 CD PRO A 123 -13.261 20.880 67.217 1.00 11.87 C ANISOU 858 CD PRO A 123 1901 1065 1542 -166 242 66 C ATOM 859 N GLN A 124 -12.484 24.557 67.965 1.00 10.91 N ANISOU 859 N GLN A 124 2016 919 1209 -25 356 -108 N ATOM 860 CA GLN A 124 -11.930 25.853 68.378 1.00 11.92 C ANISOU 860 CA GLN A 124 2310 972 1245 8 216 -215 C ATOM 861 C GLN A 124 -11.153 26.534 67.252 1.00 10.84 C ANISOU 861 C GLN A 124 2156 865 1095 67 49 -167 C ATOM 862 O GLN A 124 -11.055 27.759 67.215 1.00 11.84 O ANISOU 862 O GLN A 124 2485 887 1127 -88 160 -236 O ATOM 863 CB GLN A 124 -11.068 25.722 69.643 1.00 12.10 C ANISOU 863 CB GLN A 124 2379 1084 1133 -121 268 -284 C ATOM 864 CG GLN A 124 -9.695 25.081 69.440 1.00 12.18 C ANISOU 864 CG GLN A 124 2405 1272 948 1 239 -155 C ATOM 865 CD GLN A 124 -9.097 24.547 70.742 1.00 12.78 C ANISOU 865 CD GLN A 124 2535 1256 1065 15 147 -106 C ATOM 866 OE1 GLN A 124 -9.609 23.596 71.322 1.00 14.26 O ANISOU 866 OE1 GLN A 124 2958 1370 1090 7 214 61 O ATOM 867 NE2 GLN A 124 -8.006 25.137 71.195 1.00 13.37 N ANISOU 867 NE2 GLN A 124 2435 1334 1310 147 56 -27 N ATOM 868 N GLU A 125 -10.626 25.740 66.324 1.00 9.56 N ANISOU 868 N GLU A 125 1909 753 968 -82 41 -111 N ATOM 869 CA GLU A 125 -9.933 26.271 65.156 1.00 9.66 C ANISOU 869 CA GLU A 125 1813 857 1000 -130 -23 -39 C ATOM 870 C GLU A 125 -10.891 26.654 64.034 1.00 9.82 C ANISOU 870 C GLU A 125 1732 811 1186 -125 -90 1 C ATOM 871 O GLU A 125 -10.455 27.120 62.991 1.00 11.81 O ANISOU 871 O GLU A 125 1934 1255 1296 37 59 243 O ATOM 872 CB GLU A 125 -8.910 25.259 64.643 1.00 9.69 C ANISOU 872 CB GLU A 125 1832 903 944 -95 50 -28 C ATOM 873 CG GLU A 125 -7.813 24.928 65.636 1.00 10.40 C ANISOU 873 CG GLU A 125 1801 1069 1080 -15 94 30 C ATOM 874 CD GLU A 125 -6.989 26.137 66.013 1.00 13.09 C ANISOU 874 CD GLU A 125 1944 1317 1713 -91 -253 -110 C ATOM 875 OE1 GLU A 125 -6.762 26.993 65.132 1.00 14.05 O ANISOU 875 OE1 GLU A 125 2004 1273 2062 -84 -294 87 O ATOM 876 OE2 GLU A 125 -6.623 26.274 67.201 1.00 16.78 O ANISOU 876 OE2 GLU A 125 2392 2121 1859 -211 -399 -256 O ATOM 877 N GLY A 126 -12.187 26.446 64.230 1.00 9.93 N ANISOU 877 N GLY A 126 1743 850 1176 -107 -16 -50 N ATOM 878 CA GLY A 126 -13.179 26.771 63.217 1.00 10.33 C ANISOU 878 CA GLY A 126 1663 1038 1223 -105 -24 -53 C ATOM 879 C GLY A 126 -13.377 25.696 62.165 1.00 9.76 C ANISOU 879 C GLY A 126 1610 1026 1072 -95 189 -32 C ATOM 880 O GLY A 126 -13.969 25.974 61.127 1.00 11.56 O ANISOU 880 O GLY A 126 1852 1408 1129 26 34 -156 O ATOM 881 N MET A 127 -12.896 24.483 62.449 1.00 10.08 N ANISOU 881 N MET A 127 1706 927 1195 -131 114 -119 N ATOM 882 CA MET A 127 -12.972 23.341 61.550 1.00 10.58 C ANISOU 882 CA MET A 127 1844 972 1203 -172 252 -172 C ATOM 883 C MET A 127 -14.062 22.363 62.013 1.00 9.76 C ANISOU 883 C MET A 127 1707 915 1083 -127 20 -51 C ATOM 884 O MET A 127 -14.415 22.292 63.200 1.00 11.99 O ANISOU 884 O MET A 127 2141 1312 1103 -547 104 -71 O ATOM 885 CB MET A 127 -11.640 22.570 61.559 1.00 10.95 C ANISOU 885 CB MET A 127 1789 1202 1167 -96 358 -181 C ATOM 886 CG MET A 127 -10.414 23.373 61.179 1.00 11.29 C ANISOU 886 CG MET A 127 1791 1293 1205 -145 345 -109 C ATOM 887 SD MET A 127 -10.447 23.963 59.495 1.00 11.09 S ANISOU 887 SD MET A 127 1848 1041 1321 -5 398 -4 S ATOM 888 CE MET A 127 -10.736 25.658 59.757 1.00 11.86 C ANISOU 888 CE MET A 127 1582 1290 1633 -157 633 -594 C ATOM 889 N VAL A 128 -14.563 21.578 61.069 1.00 9.23 N ANISOU 889 N VAL A 128 1369 932 1205 13 -60 -84 N ATOM 890 CA VAL A 128 -15.352 20.383 61.351 1.00 9.50 C ANISOU 890 CA VAL A 128 1194 988 1425 21 24 -135 C ATOM 891 C VAL A 128 -14.371 19.224 61.577 1.00 8.79 C ANISOU 891 C VAL A 128 1179 937 1223 24 33 -219 C ATOM 892 O VAL A 128 -13.442 19.044 60.797 1.00 9.86 O ANISOU 892 O VAL A 128 1227 1148 1371 145 133 -68 O ATOM 893 CB VAL A 128 -16.330 20.125 60.186 1.00 10.39 C ANISOU 893 CB VAL A 128 1326 1181 1439 54 -26 -165 C ATOM 894 CG1 VAL A 128 -17.026 18.786 60.333 1.00 11.64 C ANISOU 894 CG1 VAL A 128 1572 1261 1589 -49 -169 -298 C ATOM 895 CG2 VAL A 128 -17.328 21.269 60.094 1.00 11.80 C ANISOU 895 CG2 VAL A 128 1373 1357 1752 128 -180 -213 C ATOM 896 N ALA A 129 -14.580 18.430 62.625 1.00 8.93 N ANISOU 896 N ALA A 129 1145 1016 1229 75 146 -214 N ATOM 897 CA ALA A 129 -13.722 17.280 62.900 1.00 8.67 C ANISOU 897 CA ALA A 129 1186 1006 1100 24 124 -114 C ATOM 898 C ALA A 129 -13.896 16.197 61.841 1.00 8.65 C ANISOU 898 C ALA A 129 1171 952 1163 19 107 -88 C ATOM 899 O ALA A 129 -14.970 16.043 61.243 1.00 8.94 O ANISOU 899 O ALA A 129 1196 960 1240 27 84 -112 O ATOM 900 CB ALA A 129 -14.033 16.693 64.256 1.00 10.06 C ANISOU 900 CB ALA A 129 1539 1163 1119 73 48 -39 C ATOM 901 N ALA A 130 -12.832 15.428 61.616 1.00 8.27 N ANISOU 901 N ALA A 130 1173 883 1086 -10 73 -102 N ATOM 902 CA ALA A 130 -12.963 14.185 60.876 1.00 8.12 C ANISOU 902 CA ALA A 130 1294 839 950 -9 128 -55 C ATOM 903 C ALA A 130 -13.795 13.177 61.670 1.00 8.48 C ANISOU 903 C ALA A 130 1328 837 1055 74 203 -40 C ATOM 904 O ALA A 130 -13.984 13.311 62.884 1.00 9.75 O ANISOU 904 O ALA A 130 1541 1063 1098 23 323 -91 O ATOM 905 CB ALA A 130 -11.602 13.601 60.576 1.00 8.24 C ANISOU 905 CB ALA A 130 1308 915 907 -64 226 -6 C ATOM 906 N GLN A 131 -14.296 12.166 60.970 1.00 8.56 N ANISOU 906 N GLN A 131 1204 906 1142 -58 263 -40 N ATOM 907 CA GLN A 131 -15.143 11.140 61.580 1.00 9.46 C ANISOU 907 CA GLN A 131 1190 1100 1305 -81 439 3 C ATOM 908 C GLN A 131 -14.375 10.166 62.453 1.00 9.80 C ANISOU 908 C GLN A 131 1285 1050 1389 -127 363 57 C ATOM 909 O GLN A 131 -14.959 9.592 63.373 1.00 12.69 O ANISOU 909 O GLN A 131 1491 1612 1718 53 602 468 O ATOM 910 CB GLN A 131 -15.814 10.339 60.477 1.00 10.26 C ANISOU 910 CB GLN A 131 1177 1228 1492 -224 432 -97 C ATOM 911 CG GLN A 131 -16.817 11.149 59.689 1.00 12.60 C ANISOU 911 CG GLN A 131 1468 1593 1725 -65 236 -72 C ATOM 912 CD GLN A 131 -17.199 10.502 58.378 1.00 13.62 C ANISOU 912 CD GLN A 131 1500 1884 1788 -147 252 -172 C ATOM 913 OE1 GLN A 131 -16.463 9.671 57.846 1.00 14.69 O ANISOU 913 OE1 GLN A 131 1515 2153 1914 -151 258 -353 O ATOM 914 NE2 GLN A 131 -18.337 10.905 57.834 1.00 15.83 N ANISOU 914 NE2 GLN A 131 1630 2297 2086 -41 140 -135 N ATOM 915 N HIS A 132 -13.094 9.965 62.169 1.00 8.49 N ANISOU 915 N HIS A 132 1308 868 1049 -113 322 92 N ATOM 916 CA HIS A 132 -12.278 8.969 62.827 1.00 9.13 C ANISOU 916 CA HIS A 132 1296 836 1336 -148 254 95 C ATOM 917 C HIS A 132 -10.990 9.600 63.305 1.00 8.29 C ANISOU 917 C HIS A 132 1251 793 1104 -63 259 64 C ATOM 918 O HIS A 132 -10.448 10.493 62.655 1.00 8.52 O ANISOU 918 O HIS A 132 1380 843 1014 -210 195 44 O ATOM 919 CB HIS A 132 -11.952 7.838 61.861 1.00 9.26 C ANISOU 919 CB HIS A 132 1336 829 1353 -111 243 74 C ATOM 920 CG HIS A 132 -13.159 7.181 61.281 1.00 11.12 C ANISOU 920 CG HIS A 132 1506 923 1794 -232 189 -126 C ATOM 921 ND1 HIS A 132 -13.944 6.301 61.994 1.00 13.73 N ANISOU 921 ND1 HIS A 132 1854 1344 2018 -547 173 30 N ATOM 922 CD2 HIS A 132 -13.727 7.292 60.060 1.00 12.10 C ANISOU 922 CD2 HIS A 132 1506 1212 1878 -297 51 -251 C ATOM 923 CE1 HIS A 132 -14.944 5.898 61.233 1.00 15.20 C ANISOU 923 CE1 HIS A 132 1832 1614 2327 -761 227 -179 C ATOM 924 NE2 HIS A 132 -14.829 6.475 60.051 1.00 13.94 N ANISOU 924 NE2 HIS A 132 1634 1527 2134 -488 18 -357 N ATOM 925 N SER A 133 -10.497 9.097 64.435 1.00 9.06 N ANISOU 925 N SER A 133 1418 854 1171 -95 236 191 N ATOM 926 CA SER A 133 -9.286 9.596 65.060 1.00 9.05 C ANISOU 926 CA SER A 133 1517 890 1030 -104 176 139 C ATOM 927 C SER A 133 -8.149 8.593 64.965 1.00 8.85 C ANISOU 927 C SER A 133 1494 842 1024 -106 105 158 C ATOM 928 O SER A 133 -8.290 7.428 65.328 1.00 10.72 O ANISOU 928 O SER A 133 1673 926 1473 -109 270 377 O ATOM 929 CB SER A 133 -9.535 9.928 66.527 1.00 10.39 C ANISOU 929 CB SER A 133 1897 1001 1046 -13 187 84 C ATOM 930 OG SER A 133 -10.373 11.054 66.648 1.00 11.69 O ANISOU 930 OG SER A 133 2155 1132 1153 128 358 106 O ATOM 931 N LEU A 134 -7.017 9.075 64.486 1.00 8.48 N ANISOU 931 N LEU A 134 1496 832 892 -38 151 128 N ATOM 932 CA LEU A 134 -5.772 8.342 64.475 1.00 8.77 C ANISOU 932 CA LEU A 134 1499 813 1016 -51 49 88 C ATOM 933 C LEU A 134 -5.073 8.534 65.808 1.00 8.94 C ANISOU 933 C LEU A 134 1708 812 875 -43 72 136 C ATOM 934 O LEU A 134 -5.023 9.642 66.343 1.00 9.81 O ANISOU 934 O LEU A 134 1827 878 1021 55 -66 -4 O ATOM 935 CB LEU A 134 -4.854 8.853 63.350 1.00 8.37 C ANISOU 935 CB LEU A 134 1341 830 1008 -86 40 54 C ATOM 936 CG LEU A 134 -5.456 8.845 61.938 1.00 9.17 C ANISOU 936 CG LEU A 134 1399 1094 991 -109 76 105 C ATOM 937 CD1 LEU A 134 -4.444 9.378 60.951 1.00 11.09 C ANISOU 937 CD1 LEU A 134 1642 1600 968 -261 128 172 C ATOM 938 CD2 LEU A 134 -5.884 7.435 61.554 1.00 10.17 C ANISOU 938 CD2 LEU A 134 1680 1123 1060 -48 3 -33 C ATOM 939 N THR A 135 -4.497 7.462 66.320 1.00 9.12 N ANISOU 939 N THR A 135 1754 847 863 -34 -18 136 N ATOM 940 CA THR A 135 -3.609 7.567 67.471 1.00 10.59 C ANISOU 940 CA THR A 135 2037 1042 942 -4 -161 204 C ATOM 941 C THR A 135 -2.257 6.984 67.089 1.00 10.58 C ANISOU 941 C THR A 135 1956 975 1089 -56 -244 275 C ATOM 942 O THR A 135 -2.144 6.255 66.098 1.00 10.53 O ANISOU 942 O THR A 135 1785 1031 1182 23 -125 183 O ATOM 943 CB THR A 135 -4.196 6.915 68.725 1.00 11.67 C ANISOU 943 CB THR A 135 2262 1164 1008 37 -31 223 C ATOM 944 OG1 THR A 135 -4.397 5.523 68.499 1.00 11.79 O ANISOU 944 OG1 THR A 135 2139 1123 1217 8 137 291 O ATOM 945 CG2 THR A 135 -5.532 7.551 69.102 1.00 13.46 C ANISOU 945 CG2 THR A 135 2424 1565 1124 180 132 250 C ATOM 946 N PHE A 136 -1.236 7.336 67.862 1.00 11.60 N ANISOU 946 N PHE A 136 1981 1291 1134 -106 -290 338 N ATOM 947 CA PHE A 136 0.149 7.088 67.486 1.00 12.15 C ANISOU 947 CA PHE A 136 1914 1413 1287 -119 -354 420 C ATOM 948 C PHE A 136 0.918 6.431 68.605 1.00 14.55 C ANISOU 948 C PHE A 136 2291 1682 1554 -76 -542 575 C ATOM 949 O PHE A 136 0.733 6.760 69.771 1.00 16.16 O ANISOU 949 O PHE A 136 2564 2077 1498 0 -656 563 O ATOM 950 CB PHE A 136 0.815 8.408 67.077 1.00 12.64 C ANISOU 950 CB PHE A 136 1844 1469 1489 -175 -403 427 C ATOM 951 CG PHE A 136 0.166 9.012 65.876 1.00 10.89 C ANISOU 951 CG PHE A 136 1706 1016 1414 -193 -358 255 C ATOM 952 CD1 PHE A 136 -0.942 9.832 66.008 1.00 11.57 C ANISOU 952 CD1 PHE A 136 1808 1157 1429 -111 -155 221 C ATOM 953 CD2 PHE A 136 0.601 8.684 64.606 1.00 10.48 C ANISOU 953 CD2 PHE A 136 1542 972 1467 -88 -284 263 C ATOM 954 CE1 PHE A 136 -1.587 10.334 64.890 1.00 10.89 C ANISOU 954 CE1 PHE A 136 1604 921 1611 -26 -173 232 C ATOM 955 CE2 PHE A 136 -0.046 9.173 63.486 1.00 10.27 C ANISOU 955 CE2 PHE A 136 1643 984 1273 -199 -195 284 C ATOM 956 CZ PHE A 136 -1.137 10.003 63.630 1.00 10.56 C ANISOU 956 CZ PHE A 136 1662 971 1379 -125 -366 291 C ATOM 957 N ALA A 137 1.780 5.498 68.228 1.00 14.74 N ANISOU 957 N ALA A 137 2379 1667 1554 -23 -579 592 N ATOM 958 CA ALA A 137 2.706 4.887 69.164 1.00 16.86 C ANISOU 958 CA ALA A 137 2639 1853 1914 179 -583 885 C ATOM 959 C ALA A 137 3.729 5.918 69.645 1.00 17.71 C ANISOU 959 C ALA A 137 2536 2316 1874 41 -698 876 C ATOM 960 O ALA A 137 3.883 6.979 69.045 1.00 17.15 O ANISOU 960 O ALA A 137 2335 2144 2033 -87 -929 755 O ATOM 961 CB ALA A 137 3.401 3.716 68.497 1.00 18.20 C ANISOU 961 CB ALA A 137 2572 1900 2439 196 -560 714 C ATOM 962 N ALA A 138 4.433 5.596 70.725 1.00 19.42 N ANISOU 962 N ALA A 138 2747 2642 1987 74 -839 898 N ATOM 963 CA ALA A 138 5.465 6.485 71.269 1.00 21.53 C ANISOU 963 CA ALA A 138 2748 3259 2172 125 -1015 415 C ATOM 964 C ALA A 138 6.525 6.868 70.235 1.00 20.27 C ANISOU 964 C ALA A 138 2654 2687 2357 175 -1074 590 C ATOM 965 O ALA A 138 7.066 7.974 70.277 1.00 22.82 O ANISOU 965 O ALA A 138 2666 3084 2918 -189 -1032 382 O ATOM 966 CB ALA A 138 6.129 5.844 72.478 1.00 23.81 C ANISOU 966 CB ALA A 138 3147 3717 2182 285 -1022 543 C ATOM 967 N ASN A 139 6.823 5.951 69.316 1.00 18.93 N ANISOU 967 N ASN A 139 2475 2318 2397 360 -1007 846 N ATOM 968 CA ASN A 139 7.806 6.208 68.261 1.00 18.51 C ANISOU 968 CA ASN A 139 2246 2231 2554 375 -954 697 C ATOM 969 C ASN A 139 7.284 7.012 67.069 1.00 16.76 C ANISOU 969 C ASN A 139 1936 1904 2526 243 -786 695 C ATOM 970 O ASN A 139 8.033 7.278 66.133 1.00 18.71 O ANISOU 970 O ASN A 139 1986 2573 2550 355 -760 860 O ATOM 971 CB ASN A 139 8.436 4.899 67.773 1.00 19.67 C ANISOU 971 CB ASN A 139 2292 2287 2893 401 -801 687 C ATOM 972 CG ASN A 139 7.452 3.972 67.071 1.00 19.12 C ANISOU 972 CG ASN A 139 2265 2142 2858 265 -742 1010 C ATOM 973 OD1 ASN A 139 6.341 4.361 66.704 1.00 20.03 O ANISOU 973 OD1 ASN A 139 2266 2358 2985 423 -691 953 O ATOM 974 ND2 ASN A 139 7.869 2.726 66.876 1.00 22.25 N ANISOU 974 ND2 ASN A 139 2863 2170 3420 353 -668 970 N ATOM 975 N GLY A 140 6.006 7.378 67.097 1.00 16.52 N ANISOU 975 N GLY A 140 1868 1976 2432 144 -828 818 N ATOM 976 CA GLY A 140 5.427 8.230 66.067 1.00 15.41 C ANISOU 976 CA GLY A 140 1826 1884 2144 -25 -662 817 C ATOM 977 C GLY A 140 4.595 7.529 65.008 1.00 13.65 C ANISOU 977 C GLY A 140 1505 1464 2215 14 -546 865 C ATOM 978 O GLY A 140 3.797 8.172 64.344 1.00 12.30 O ANISOU 978 O GLY A 140 1431 1337 1903 6 -466 721 O ATOM 979 N TRP A 141 4.758 6.223 64.819 1.00 14.11 N ANISOU 979 N TRP A 141 1472 1535 2352 140 -399 840 N ATOM 980 CA TRP A 141 3.970 5.537 63.787 1.00 13.44 C ANISOU 980 CA TRP A 141 1453 1330 2323 185 -213 722 C ATOM 981 C TRP A 141 2.517 5.408 64.208 1.00 11.62 C ANISOU 981 C TRP A 141 1510 1064 1841 117 -182 647 C ATOM 982 O TRP A 141 2.220 5.147 65.375 1.00 12.43 O ANISOU 982 O TRP A 141 1689 1303 1731 13 -375 642 O ATOM 983 CB TRP A 141 4.548 4.159 63.453 1.00 14.77 C ANISOU 983 CB TRP A 141 1687 1316 2607 261 -81 832 C ATOM 984 CG TRP A 141 5.810 4.269 62.677 1.00 15.71 C ANISOU 984 CG TRP A 141 1688 1440 2838 440 20 795 C ATOM 985 CD1 TRP A 141 7.065 3.968 63.105 1.00 17.94 C ANISOU 985 CD1 TRP A 141 1683 2128 3003 453 31 1030 C ATOM 986 CD2 TRP A 141 5.950 4.755 61.336 1.00 15.32 C ANISOU 986 CD2 TRP A 141 1584 1397 2839 337 180 738 C ATOM 987 NE1 TRP A 141 7.977 4.222 62.110 1.00 18.76 N ANISOU 987 NE1 TRP A 141 1640 2411 3077 581 83 1035 N ATOM 988 CE2 TRP A 141 7.319 4.716 61.016 1.00 16.98 C ANISOU 988 CE2 TRP A 141 1589 1872 2989 370 134 940 C ATOM 989 CE3 TRP A 141 5.047 5.227 60.377 1.00 15.25 C ANISOU 989 CE3 TRP A 141 1673 1422 2697 240 59 500 C ATOM 990 CZ2 TRP A 141 7.811 5.119 59.767 1.00 17.75 C ANISOU 990 CZ2 TRP A 141 1816 1967 2961 395 273 733 C ATOM 991 CZ3 TRP A 141 5.534 5.628 59.142 1.00 15.74 C ANISOU 991 CZ3 TRP A 141 2025 1512 2441 298 22 228 C ATOM 992 CH2 TRP A 141 6.903 5.578 58.850 1.00 16.71 C ANISOU 992 CH2 TRP A 141 2051 1717 2578 232 188 461 C ATOM 993 N VAL A 142 1.607 5.582 63.256 1.00 11.06 N ANISOU 993 N VAL A 142 1447 1080 1675 47 -81 480 N ATOM 994 CA VAL A 142 0.197 5.418 63.543 1.00 9.97 C ANISOU 994 CA VAL A 142 1463 954 1371 19 -68 357 C ATOM 995 C VAL A 142 -0.070 4.014 64.086 1.00 10.60 C ANISOU 995 C VAL A 142 1589 892 1547 39 -53 319 C ATOM 996 O VAL A 142 0.542 3.036 63.654 1.00 11.80 O ANISOU 996 O VAL A 142 1770 940 1771 143 65 356 O ATOM 997 CB VAL A 142 -0.674 5.714 62.299 1.00 9.58 C ANISOU 997 CB VAL A 142 1481 938 1220 32 -2 262 C ATOM 998 CG1 VAL A 142 -0.530 4.663 61.210 1.00 11.12 C ANISOU 998 CG1 VAL A 142 1711 1083 1432 7 4 89 C ATOM 999 CG2 VAL A 142 -2.133 5.914 62.681 1.00 9.89 C ANISOU 999 CG2 VAL A 142 1492 1164 1102 29 -29 308 C ATOM 1000 N GLU A 143 -0.985 3.934 65.046 1.00 10.56 N ANISOU 1000 N GLU A 143 1679 893 1440 -40 -86 416 N ATOM 1001 CA GLU A 143 -1.472 2.650 65.522 1.00 11.59 C ANISOU 1001 CA GLU A 143 1866 924 1611 -122 44 387 C ATOM 1002 C GLU A 143 -2.339 2.092 64.391 1.00 11.00 C ANISOU 1002 C GLU A 143 1809 792 1576 -135 161 321 C ATOM 1003 O GLU A 143 -3.332 2.700 64.012 1.00 11.15 O ANISOU 1003 O GLU A 143 1829 803 1602 -122 23 265 O ATOM 1004 CB GLU A 143 -2.184 2.840 66.863 1.00 13.58 C ANISOU 1004 CB GLU A 143 2371 1172 1613 -203 231 423 C ATOM 1005 CG GLU A 143 -1.160 3.284 67.919 1.00 17.65 C ANISOU 1005 CG GLU A 143 2897 2054 1752 -41 -282 582 C ATOM 1006 CD GLU A 143 -1.650 3.347 69.353 1.00 20.31 C ANISOU 1006 CD GLU A 143 3141 2561 2014 478 32 495 C ATOM 1007 OE1 GLU A 143 -2.662 4.017 69.643 1.00 21.92 O ANISOU 1007 OE1 GLU A 143 3289 2366 2674 719 -434 349 O ATOM 1008 OE2 GLU A 143 -0.965 2.758 70.214 1.00 25.96 O ANISOU 1008 OE2 GLU A 143 3956 3472 2434 777 -408 756 O ATOM 1009 N PRO A 144 -1.927 0.951 63.799 1.00 11.82 N ANISOU 1009 N PRO A 144 1889 942 1659 -71 141 173 N ATOM 1010 CA PRO A 144 -2.545 0.494 62.551 1.00 12.24 C ANISOU 1010 CA PRO A 144 1973 1276 1402 -97 406 80 C ATOM 1011 C PRO A 144 -4.062 0.292 62.606 1.00 10.96 C ANISOU 1011 C PRO A 144 1967 813 1382 -85 418 76 C ATOM 1012 O PRO A 144 -4.754 0.502 61.610 1.00 11.13 O ANISOU 1012 O PRO A 144 1867 1047 1315 -80 463 18 O ATOM 1013 CB PRO A 144 -1.843 -0.840 62.281 1.00 15.64 C ANISOU 1013 CB PRO A 144 2006 1609 2325 -7 450 -467 C ATOM 1014 CG PRO A 144 -0.540 -0.736 62.962 1.00 18.02 C ANISOU 1014 CG PRO A 144 2448 2020 2378 354 5 -215 C ATOM 1015 CD PRO A 144 -0.774 0.107 64.173 1.00 14.17 C ANISOU 1015 CD PRO A 144 2142 983 2257 89 -15 145 C ATOM 1016 N ALA A 145 -4.585 -0.119 63.754 1.00 10.51 N ANISOU 1016 N ALA A 145 1911 798 1285 -128 204 169 N ATOM 1017 CA ALA A 145 -6.025 -0.332 63.878 1.00 10.67 C ANISOU 1017 CA ALA A 145 1952 821 1280 -278 260 139 C ATOM 1018 C ALA A 145 -6.831 0.947 63.675 1.00 9.78 C ANISOU 1018 C ALA A 145 1770 856 1091 -224 409 -28 C ATOM 1019 O ALA A 145 -8.015 0.884 63.337 1.00 11.16 O ANISOU 1019 O ALA A 145 1829 933 1477 -287 346 -72 O ATOM 1020 CB ALA A 145 -6.356 -0.907 65.241 1.00 13.71 C ANISOU 1020 CB ALA A 145 2344 1192 1671 -329 564 460 C ATOM 1021 N THR A 146 -6.206 2.107 63.902 1.00 9.46 N ANISOU 1021 N THR A 146 1853 776 963 -159 233 21 N ATOM 1022 CA THR A 146 -6.893 3.390 63.741 1.00 9.40 C ANISOU 1022 CA THR A 146 1708 832 1032 -134 163 57 C ATOM 1023 C THR A 146 -6.858 3.909 62.313 1.00 9.41 C ANISOU 1023 C THR A 146 1718 854 1000 -104 123 40 C ATOM 1024 O THR A 146 -7.573 4.854 61.991 1.00 10.13 O ANISOU 1024 O THR A 146 1808 923 1117 19 226 48 O ATOM 1025 CB THR A 146 -6.386 4.467 64.725 1.00 9.66 C ANISOU 1025 CB THR A 146 1772 926 971 -107 181 -6 C ATOM 1026 OG1 THR A 146 -5.075 4.925 64.349 1.00 9.73 O ANISOU 1026 OG1 THR A 146 1759 806 1129 -172 107 54 O ATOM 1027 CG2 THR A 146 -6.424 3.962 66.156 1.00 10.82 C ANISOU 1027 CG2 THR A 146 2058 1070 980 -139 -13 13 C ATOM 1028 N ALA A 147 -6.081 3.254 61.445 1.00 9.10 N ANISOU 1028 N ALA A 147 1628 897 931 -96 75 52 N ATOM 1029 CA ALA A 147 -5.939 3.654 60.051 1.00 9.08 C ANISOU 1029 CA ALA A 147 1528 957 965 -83 88 114 C ATOM 1030 C ALA A 147 -6.252 2.457 59.146 1.00 8.75 C ANISOU 1030 C ALA A 147 1400 927 998 19 37 124 C ATOM 1031 O ALA A 147 -5.432 2.047 58.324 1.00 9.39 O ANISOU 1031 O ALA A 147 1487 974 1105 103 115 131 O ATOM 1032 CB ALA A 147 -4.529 4.177 59.800 1.00 10.48 C ANISOU 1032 CB ALA A 147 1647 1376 958 -268 99 64 C ATOM 1033 N PRO A 148 -7.457 1.890 59.285 1.00 8.91 N ANISOU 1033 N PRO A 148 1422 894 1068 -58 129 25 N ATOM 1034 CA PRO A 148 -7.777 0.728 58.464 1.00 9.13 C ANISOU 1034 CA PRO A 148 1580 891 996 -81 108 63 C ATOM 1035 C PRO A 148 -7.897 1.096 56.986 1.00 8.57 C ANISOU 1035 C PRO A 148 1510 765 980 -168 150 148 C ATOM 1036 O PRO A 148 -8.381 2.171 56.638 1.00 8.54 O ANISOU 1036 O PRO A 148 1354 839 1050 -31 171 40 O ATOM 1037 CB PRO A 148 -9.139 0.288 58.997 1.00 10.59 C ANISOU 1037 CB PRO A 148 1761 1152 1111 -349 225 63 C ATOM 1038 CG PRO A 148 -9.750 1.563 59.485 1.00 10.78 C ANISOU 1038 CG PRO A 148 1508 1362 1226 -226 211 28 C ATOM 1039 CD PRO A 148 -8.607 2.311 60.103 1.00 9.65 C ANISOU 1039 CD PRO A 148 1420 1049 1197 -110 248 58 C ATOM 1040 N ASN A 149 -7.485 0.167 56.137 1.00 8.98 N ANISOU 1040 N ASN A 149 1576 816 1017 -60 122 108 N ATOM 1041 CA ASN A 149 -7.623 0.304 54.694 1.00 9.11 C ANISOU 1041 CA ASN A 149 1506 989 967 -68 141 1 C ATOM 1042 C ASN A 149 -6.895 1.509 54.111 1.00 8.69 C ANISOU 1042 C ASN A 149 1522 825 954 35 119 -21 C ATOM 1043 O ASN A 149 -7.278 2.041 53.076 1.00 9.85 O ANISOU 1043 O ASN A 149 1809 890 1041 41 33 43 O ATOM 1044 CB ASN A 149 -9.105 0.260 54.298 1.00 10.62 C ANISOU 1044 CB ASN A 149 1561 1372 1102 -11 47 -188 C ATOM 1045 CG ASN A 149 -9.763 -1.047 54.709 1.00 12.50 C ANISOU 1045 CG ASN A 149 1666 1725 1359 -255 119 -128 C ATOM 1046 OD1 ASN A 149 -10.711 -1.081 55.505 1.00 17.15 O ANISOU 1046 OD1 ASN A 149 2169 2474 1873 -285 589 -47 O ATOM 1047 ND2 ASN A 149 -9.222 -2.124 54.232 1.00 11.89 N ANISOU 1047 ND2 ASN A 149 1759 1482 1273 -440 117 -111 N ATOM 1048 N PHE A 150 -5.804 1.904 54.755 1.00 8.99 N ANISOU 1048 N PHE A 150 1352 870 1193 58 90 186 N ATOM 1049 CA PHE A 150 -4.996 3.025 54.261 1.00 8.65 C ANISOU 1049 CA PHE A 150 1301 844 1141 74 143 130 C ATOM 1050 C PHE A 150 -4.087 2.656 53.080 1.00 9.39 C ANISOU 1050 C PHE A 150 1483 923 1160 91 215 116 C ATOM 1051 O PHE A 150 -3.486 3.538 52.469 1.00 9.05 O ANISOU 1051 O PHE A 150 1484 927 1026 1 234 33 O ATOM 1052 CB PHE A 150 -4.197 3.675 55.398 1.00 8.69 C ANISOU 1052 CB PHE A 150 1221 891 1189 67 132 138 C ATOM 1053 CG PHE A 150 -4.906 4.830 56.077 1.00 8.31 C ANISOU 1053 CG PHE A 150 1216 906 1033 38 130 146 C ATOM 1054 CD1 PHE A 150 -6.222 4.737 56.495 1.00 8.18 C ANISOU 1054 CD1 PHE A 150 1221 843 1041 -42 158 165 C ATOM 1055 CD2 PHE A 150 -4.228 6.018 56.307 1.00 8.92 C ANISOU 1055 CD2 PHE A 150 1177 1023 1189 0 128 67 C ATOM 1056 CE1 PHE A 150 -6.852 5.798 57.122 1.00 8.31 C ANISOU 1056 CE1 PHE A 150 1170 994 992 15 173 131 C ATOM 1057 CE2 PHE A 150 -4.856 7.089 56.932 1.00 9.26 C ANISOU 1057 CE2 PHE A 150 1296 920 1299 -53 108 66 C ATOM 1058 CZ PHE A 150 -6.167 6.974 57.352 1.00 8.88 C ANISOU 1058 CZ PHE A 150 1286 934 1151 68 172 -18 C ATOM 1059 N GLY A 151 -4.022 1.376 52.720 1.00 11.21 N ANISOU 1059 N GLY A 151 1682 1024 1552 84 468 -90 N ATOM 1060 CA GLY A 151 -3.251 0.978 51.549 1.00 12.01 C ANISOU 1060 CA GLY A 151 1847 1090 1626 30 552 -175 C ATOM 1061 C GLY A 151 -1.814 1.462 51.639 1.00 11.54 C ANISOU 1061 C GLY A 151 1796 1166 1421 142 406 -35 C ATOM 1062 O GLY A 151 -1.119 1.196 52.617 1.00 13.94 O ANISOU 1062 O GLY A 151 2044 1618 1634 363 326 343 O ATOM 1063 N PRO A 152 -1.350 2.191 50.622 1.00 10.92 N ANISOU 1063 N PRO A 152 1468 1291 1390 45 226 -6 N ATOM 1064 CA PRO A 152 0.041 2.638 50.616 1.00 11.62 C ANISOU 1064 CA PRO A 152 1451 1650 1312 46 286 -49 C ATOM 1065 C PRO A 152 0.341 3.825 51.533 1.00 10.81 C ANISOU 1065 C PRO A 152 1325 1546 1237 -46 238 91 C ATOM 1066 O PRO A 152 1.508 4.203 51.653 1.00 12.53 O ANISOU 1066 O PRO A 152 1364 1883 1513 -117 112 -71 O ATOM 1067 CB PRO A 152 0.255 3.040 49.157 1.00 13.10 C ANISOU 1067 CB PRO A 152 1777 1931 1266 -98 364 -183 C ATOM 1068 CG PRO A 152 -1.086 3.533 48.738 1.00 13.18 C ANISOU 1068 CG PRO A 152 1913 1887 1208 -155 247 109 C ATOM 1069 CD PRO A 152 -2.062 2.612 49.404 1.00 11.50 C ANISOU 1069 CD PRO A 152 1654 1498 1217 43 268 -32 C ATOM 1070 N LEU A 153 -0.671 4.421 52.162 1.00 10.09 N ANISOU 1070 N LEU A 153 1326 1433 1073 -125 159 21 N ATOM 1071 CA LEU A 153 -0.428 5.591 52.997 1.00 10.33 C ANISOU 1071 CA LEU A 153 1306 1360 1257 -249 10 88 C ATOM 1072 C LEU A 153 0.137 5.161 54.333 1.00 10.51 C ANISOU 1072 C LEU A 153 1362 1334 1295 -199 10 156 C ATOM 1073 O LEU A 153 -0.498 4.414 55.075 1.00 12.76 O ANISOU 1073 O LEU A 153 1726 1756 1364 -548 -96 358 O ATOM 1074 CB LEU A 153 -1.704 6.391 53.215 1.00 9.86 C ANISOU 1074 CB LEU A 153 1416 1219 1109 -288 143 43 C ATOM 1075 CG LEU A 153 -2.428 6.885 51.963 1.00 10.84 C ANISOU 1075 CG LEU A 153 1450 1401 1264 -187 -36 -36 C ATOM 1076 CD1 LEU A 153 -3.560 7.808 52.385 1.00 11.75 C ANISOU 1076 CD1 LEU A 153 1403 1532 1529 -99 -101 -56 C ATOM 1077 CD2 LEU A 153 -1.489 7.600 51.008 1.00 12.07 C ANISOU 1077 CD2 LEU A 153 1766 1628 1189 -204 -26 208 C ATOM 1078 N LYS A 154 1.319 5.667 54.642 1.00 9.64 N ANISOU 1078 N LYS A 154 1253 1115 1293 -42 61 131 N ATOM 1079 CA LYS A 154 2.033 5.367 55.871 1.00 9.88 C ANISOU 1079 CA LYS A 154 1430 932 1392 119 -35 102 C ATOM 1080 C LYS A 154 2.075 6.636 56.718 1.00 8.98 C ANISOU 1080 C LYS A 154 1282 863 1267 115 -80 236 C ATOM 1081 O LYS A 154 2.801 7.576 56.387 1.00 10.44 O ANISOU 1081 O LYS A 154 1442 983 1541 14 122 101 O ATOM 1082 CB LYS A 154 3.456 4.919 55.547 1.00 11.67 C ANISOU 1082 CB LYS A 154 1508 1165 1760 284 -28 51 C ATOM 1083 CG LYS A 154 3.562 3.559 54.886 1.00 15.61 C ANISOU 1083 CG LYS A 154 2345 1322 2263 125 160 -224 C ATOM 1084 CD LYS A 154 5.015 3.111 54.787 1.00 21.81 C ANISOU 1084 CD LYS A 154 2577 2469 3240 535 233 -144 C ATOM 1085 CE LYS A 154 5.693 2.870 56.128 1.00 25.66 C ANISOU 1085 CE LYS A 154 3004 3307 3438 -20 -79 -22 C ATOM 1086 NZ LYS A 154 7.075 2.343 55.942 1.00 30.51 N ANISOU 1086 NZ LYS A 154 3440 3713 4440 550 21 241 N ATOM 1087 N VAL A 155 1.312 6.664 57.811 1.00 9.56 N ANISOU 1087 N VAL A 155 1394 873 1365 -29 -5 149 N ATOM 1088 CA VAL A 155 1.097 7.891 58.575 1.00 8.72 C ANISOU 1088 CA VAL A 155 1140 883 1289 27 18 197 C ATOM 1089 C VAL A 155 2.019 7.936 59.790 1.00 8.39 C ANISOU 1089 C VAL A 155 1066 871 1249 104 62 251 C ATOM 1090 O VAL A 155 2.092 6.980 60.559 1.00 9.61 O ANISOU 1090 O VAL A 155 1322 960 1367 86 -90 363 O ATOM 1091 CB VAL A 155 -0.375 8.041 58.985 1.00 9.24 C ANISOU 1091 CB VAL A 155 1107 1014 1388 -20 25 339 C ATOM 1092 CG1 VAL A 155 -0.609 9.392 59.623 1.00 9.65 C ANISOU 1092 CG1 VAL A 155 1153 1134 1378 49 -16 265 C ATOM 1093 CG2 VAL A 155 -1.287 7.873 57.776 1.00 11.09 C ANISOU 1093 CG2 VAL A 155 1271 1368 1574 -110 -74 247 C ATOM 1094 N PHE A 156 2.687 9.074 59.963 1.00 8.67 N ANISOU 1094 N PHE A 156 1113 934 1247 61 -68 251 N ATOM 1095 CA PHE A 156 3.708 9.254 60.979 1.00 9.11 C ANISOU 1095 CA PHE A 156 1137 994 1329 129 -181 279 C ATOM 1096 C PHE A 156 3.516 10.600 61.678 1.00 8.63 C ANISOU 1096 C PHE A 156 1022 1024 1231 41 -281 249 C ATOM 1097 O PHE A 156 3.386 11.642 61.032 1.00 9.02 O ANISOU 1097 O PHE A 156 1225 1036 1163 22 -200 282 O ATOM 1098 CB PHE A 156 5.087 9.194 60.323 1.00 10.33 C ANISOU 1098 CB PHE A 156 1166 1157 1600 95 -112 281 C ATOM 1099 CG PHE A 156 6.229 9.352 61.288 1.00 11.29 C ANISOU 1099 CG PHE A 156 1171 1413 1704 165 -191 339 C ATOM 1100 CD1 PHE A 156 6.555 8.321 62.152 1.00 12.52 C ANISOU 1100 CD1 PHE A 156 1316 1524 1915 174 -213 487 C ATOM 1101 CD2 PHE A 156 6.985 10.516 61.329 1.00 11.37 C ANISOU 1101 CD2 PHE A 156 1234 1359 1725 208 -164 253 C ATOM 1102 CE1 PHE A 156 7.604 8.448 63.040 1.00 14.07 C ANISOU 1102 CE1 PHE A 156 1356 1965 2024 310 -312 550 C ATOM 1103 CE2 PHE A 156 8.036 10.649 62.219 1.00 12.81 C ANISOU 1103 CE2 PHE A 156 1187 1787 1890 206 -198 204 C ATOM 1104 CZ PHE A 156 8.343 9.614 63.078 1.00 14.16 C ANISOU 1104 CZ PHE A 156 1337 2084 1956 232 -371 350 C ATOM 1105 N TYR A 157 3.488 10.567 63.008 1.00 9.51 N ANISOU 1105 N TYR A 157 1277 1081 1252 26 -321 266 N ATOM 1106 CA TYR A 157 3.492 11.769 63.837 1.00 9.54 C ANISOU 1106 CA TYR A 157 1328 1138 1155 75 -306 266 C ATOM 1107 C TYR A 157 4.929 12.069 64.236 1.00 10.37 C ANISOU 1107 C TYR A 157 1340 1274 1325 16 -341 318 C ATOM 1108 O TYR A 157 5.512 11.310 64.994 1.00 11.40 O ANISOU 1108 O TYR A 157 1438 1352 1539 42 -505 368 O ATOM 1109 CB TYR A 157 2.641 11.577 65.097 1.00 10.01 C ANISOU 1109 CB TYR A 157 1395 1223 1185 18 -264 263 C ATOM 1110 CG TYR A 157 2.716 12.756 66.035 1.00 10.76 C ANISOU 1110 CG TYR A 157 1667 1353 1066 4 -202 243 C ATOM 1111 CD1 TYR A 157 2.254 14.006 65.643 1.00 10.83 C ANISOU 1111 CD1 TYR A 157 1703 1289 1123 -12 -319 142 C ATOM 1112 CD2 TYR A 157 3.271 12.636 67.301 1.00 12.71 C ANISOU 1112 CD2 TYR A 157 1989 1704 1135 92 -335 188 C ATOM 1113 CE1 TYR A 157 2.325 15.102 66.486 1.00 11.55 C ANISOU 1113 CE1 TYR A 157 1829 1333 1225 85 -283 52 C ATOM 1114 CE2 TYR A 157 3.348 13.730 68.155 1.00 13.32 C ANISOU 1114 CE2 TYR A 157 2063 1851 1145 174 -467 78 C ATOM 1115 CZ TYR A 157 2.869 14.956 67.745 1.00 12.97 C ANISOU 1115 CZ TYR A 157 1906 1631 1389 12 -495 1 C ATOM 1116 OH TYR A 157 2.946 16.034 68.595 1.00 14.29 O ANISOU 1116 OH TYR A 157 2171 1917 1340 46 -425 -217 O ATOM 1117 N PRO A 158 5.514 13.163 63.717 1.00 10.22 N ANISOU 1117 N PRO A 158 1247 1334 1301 -78 -383 274 N ATOM 1118 CA PRO A 158 6.949 13.400 63.921 1.00 11.26 C ANISOU 1118 CA PRO A 158 1239 1453 1584 -30 -371 178 C ATOM 1119 C PRO A 158 7.296 14.134 65.209 1.00 11.92 C ANISOU 1119 C PRO A 158 1411 1634 1485 -139 -493 249 C ATOM 1120 O PRO A 158 8.473 14.336 65.494 1.00 13.66 O ANISOU 1120 O PRO A 158 1415 2057 1715 -120 -563 194 O ATOM 1121 CB PRO A 158 7.322 14.271 62.719 1.00 11.35 C ANISOU 1121 CB PRO A 158 1282 1366 1661 -134 -278 147 C ATOM 1122 CG PRO A 158 6.084 15.067 62.468 1.00 10.72 C ANISOU 1122 CG PRO A 158 1351 1344 1375 -139 -407 190 C ATOM 1123 CD PRO A 158 4.936 14.127 62.759 1.00 10.11 C ANISOU 1123 CD PRO A 158 1279 1257 1304 -8 -350 205 C ATOM 1124 N GLY A 159 6.276 14.514 65.973 1.00 11.95 N ANISOU 1124 N GLY A 159 1471 1629 1439 -87 -509 147 N ATOM 1125 CA GLY A 159 6.421 15.390 67.112 1.00 13.19 C ANISOU 1125 CA GLY A 159 1834 1837 1339 0 -529 111 C ATOM 1126 C GLY A 159 5.860 16.759 66.784 1.00 12.42 C ANISOU 1126 C GLY A 159 1526 1756 1434 -78 -567 7 C ATOM 1127 O GLY A 159 5.617 17.092 65.622 1.00 12.22 O ANISOU 1127 O GLY A 159 1477 1726 1438 -2 -486 28 O ATOM 1128 N PRO A 160 5.679 17.586 67.814 1.00 13.59 N ANISOU 1128 N PRO A 160 1726 1987 1450 70 -618 -107 N ATOM 1129 CA PRO A 160 5.146 18.928 67.615 1.00 13.62 C ANISOU 1129 CA PRO A 160 1578 1983 1611 49 -508 -203 C ATOM 1130 C PRO A 160 6.132 19.817 66.859 1.00 12.79 C ANISOU 1130 C PRO A 160 1478 1795 1585 57 -520 -368 C ATOM 1131 O PRO A 160 7.344 19.734 67.073 1.00 13.77 O ANISOU 1131 O PRO A 160 1490 1920 1819 38 -618 -326 O ATOM 1132 CB PRO A 160 4.913 19.424 69.044 1.00 15.35 C ANISOU 1132 CB PRO A 160 1926 2219 1686 226 -316 -283 C ATOM 1133 CG PRO A 160 5.859 18.649 69.881 1.00 17.10 C ANISOU 1133 CG PRO A 160 2456 2402 1635 301 -513 -235 C ATOM 1134 CD PRO A 160 6.010 17.314 69.224 1.00 15.29 C ANISOU 1134 CD PRO A 160 2135 2194 1480 165 -643 -33 C ATOM 1135 N GLY A 161 5.618 20.670 65.983 1.00 12.28 N ANISOU 1135 N GLY A 161 1328 1708 1630 24 -500 -353 N ATOM 1136 CA GLY A 161 6.487 21.515 65.172 1.00 12.25 C ANISOU 1136 CA GLY A 161 1288 1675 1690 11 -366 -428 C ATOM 1137 C GLY A 161 5.727 22.703 64.647 1.00 11.61 C ANISOU 1137 C GLY A 161 1225 1532 1654 -54 -309 -441 C ATOM 1138 O GLY A 161 5.528 23.681 65.353 1.00 13.13 O ANISOU 1138 O GLY A 161 1538 1722 1726 120 -481 -585 O ATOM 1139 N HIS A 162 5.267 22.603 63.407 1.00 10.84 N ANISOU 1139 N HIS A 162 1151 1352 1614 -84 -250 -391 N ATOM 1140 CA HIS A 162 4.411 23.622 62.838 1.00 10.65 C ANISOU 1140 CA HIS A 162 1247 1194 1604 -202 -196 -266 C ATOM 1141 C HIS A 162 3.165 23.835 63.713 1.00 10.20 C ANISOU 1141 C HIS A 162 1288 1147 1441 -175 -245 -315 C ATOM 1142 O HIS A 162 2.736 24.963 63.959 1.00 10.78 O ANISOU 1142 O HIS A 162 1324 1206 1566 -131 -259 -350 O ATOM 1143 CB HIS A 162 4.039 23.229 61.417 1.00 10.18 C ANISOU 1143 CB HIS A 162 1187 1215 1464 -228 -45 -158 C ATOM 1144 CG HIS A 162 2.909 24.016 60.873 1.00 10.15 C ANISOU 1144 CG HIS A 162 1228 1208 1418 -295 -209 -103 C ATOM 1145 ND1 HIS A 162 3.049 25.311 60.432 1.00 11.17 N ANISOU 1145 ND1 HIS A 162 1161 1298 1782 -410 -229 40 N ATOM 1146 CD2 HIS A 162 1.598 23.713 60.762 1.00 9.72 C ANISOU 1146 CD2 HIS A 162 1211 1124 1357 -240 -215 -132 C ATOM 1147 CE1 HIS A 162 1.871 25.758 60.046 1.00 10.62 C ANISOU 1147 CE1 HIS A 162 1204 1246 1585 -322 -179 7 C ATOM 1148 NE2 HIS A 162 0.979 24.805 60.228 1.00 9.71 N ANISOU 1148 NE2 HIS A 162 1190 1194 1304 -274 -180 -79 N ATOM 1149 N THR A 163 2.578 22.723 64.150 1.00 10.22 N ANISOU 1149 N THR A 163 1346 1163 1373 -153 -198 -269 N ATOM 1150 CA THR A 163 1.560 22.714 65.190 1.00 10.13 C ANISOU 1150 CA THR A 163 1359 1205 1285 -122 -265 -347 C ATOM 1151 C THR A 163 1.817 21.503 66.087 1.00 10.58 C ANISOU 1151 C THR A 163 1375 1449 1193 -115 -315 -335 C ATOM 1152 O THR A 163 2.659 20.650 65.785 1.00 11.01 O ANISOU 1152 O THR A 163 1421 1398 1364 -27 -256 -111 O ATOM 1153 CB THR A 163 0.134 22.574 64.627 1.00 9.71 C ANISOU 1153 CB THR A 163 1338 1081 1269 -120 -249 -230 C ATOM 1154 OG1 THR A 163 0.078 21.373 63.853 1.00 9.48 O ANISOU 1154 OG1 THR A 163 1303 1058 1241 -50 -239 -197 O ATOM 1155 CG2 THR A 163 -0.280 23.765 63.782 1.00 9.72 C ANISOU 1155 CG2 THR A 163 1355 1086 1252 -136 -175 -168 C ATOM 1156 N SER A 164 1.073 21.434 67.186 1.00 11.06 N ANISOU 1156 N SER A 164 1576 1388 1235 -157 -269 -285 N ATOM 1157 CA ASER A 164 1.148 20.304 68.112 0.51 12.00 C ANISOU 1157 CA ASER A 164 1862 1565 1130 -120 -369 -227 C ATOM 1158 CA BSER A 164 1.188 20.289 68.088 0.49 11.97 C ANISOU 1158 CA BSER A 164 1903 1580 1062 -131 -361 -241 C ATOM 1159 C SER A 164 0.661 19.002 67.484 1.00 10.96 C ANISOU 1159 C SER A 164 1726 1413 1023 -65 -396 -69 C ATOM 1160 O SER A 164 1.104 17.918 67.858 1.00 12.16 O ANISOU 1160 O SER A 164 1885 1461 1271 -3 -538 9 O ATOM 1161 CB ASER A 164 0.297 20.588 69.350 0.51 13.04 C ANISOU 1161 CB ASER A 164 2017 1577 1360 -125 -180 -252 C ATOM 1162 CB BSER A 164 0.456 20.554 69.392 0.49 12.95 C ANISOU 1162 CB BSER A 164 2168 1580 1171 -163 -226 -304 C ATOM 1163 OG ASER A 164 -1.060 20.809 68.992 0.51 13.96 O ANISOU 1163 OG ASER A 164 2029 1817 1459 70 -71 -284 O ATOM 1164 OG BSER A 164 1.163 21.522 70.124 0.49 15.04 O ANISOU 1164 OG BSER A 164 2616 1876 1220 -283 -348 -479 O ATOM 1165 N ASP A 165 -0.269 19.128 66.540 1.00 9.60 N ANISOU 1165 N ASP A 165 1575 1197 874 -76 -252 -159 N ATOM 1166 CA ASP A 165 -0.987 17.985 65.974 1.00 9.21 C ANISOU 1166 CA ASP A 165 1484 1087 925 -59 -199 -45 C ATOM 1167 C ASP A 165 -0.529 17.564 64.588 1.00 8.58 C ANISOU 1167 C ASP A 165 1269 1047 942 -21 -224 -77 C ATOM 1168 O ASP A 165 -1.086 16.619 64.034 1.00 8.76 O ANISOU 1168 O ASP A 165 1338 1038 952 -141 -89 -72 O ATOM 1169 CB ASP A 165 -2.508 18.248 65.960 1.00 9.09 C ANISOU 1169 CB ASP A 165 1512 1061 881 -32 -41 -65 C ATOM 1170 CG ASP A 165 -2.925 19.427 65.087 1.00 8.56 C ANISOU 1170 CG ASP A 165 1370 932 949 -81 -99 -140 C ATOM 1171 OD1 ASP A 165 -2.215 20.459 65.088 1.00 9.50 O ANISOU 1171 OD1 ASP A 165 1446 979 1181 -123 -180 -60 O ATOM 1172 OD2 ASP A 165 -4.003 19.331 64.452 1.00 8.43 O ANISOU 1172 OD2 ASP A 165 1400 841 960 -83 -125 6 O ATOM 1173 N ASN A 166 0.464 18.242 64.017 1.00 8.69 N ANISOU 1173 N ASN A 166 1251 999 1053 -98 -287 -131 N ATOM 1174 CA ASN A 166 0.876 17.957 62.641 1.00 8.20 C ANISOU 1174 CA ASN A 166 1196 924 994 -68 -296 -36 C ATOM 1175 C ASN A 166 1.271 16.502 62.418 1.00 7.94 C ANISOU 1175 C ASN A 166 1075 978 961 -49 -261 4 C ATOM 1176 O ASN A 166 2.035 15.931 63.198 1.00 8.60 O ANISOU 1176 O ASN A 166 1179 1015 1072 -22 -338 23 O ATOM 1177 CB ASN A 166 1.950 18.955 62.113 1.00 8.49 C ANISOU 1177 CB ASN A 166 1124 938 1161 -44 -210 -72 C ATOM 1178 CG ASN A 166 3.210 19.126 62.976 1.00 9.47 C ANISOU 1178 CG ASN A 166 1150 1093 1354 -75 -282 -231 C ATOM 1179 OD1 ASN A 166 3.839 20.183 62.871 1.00 10.34 O ANISOU 1179 OD1 ASN A 166 1211 1274 1443 -215 -207 -138 O ATOM 1180 ND2 ASN A 166 3.625 18.129 63.743 1.00 10.23 N ANISOU 1180 ND2 ASN A 166 1178 1305 1404 -50 -380 -139 N ATOM 1181 N ILE A 167 0.751 15.914 61.344 1.00 7.09 N ANISOU 1181 N ILE A 167 937 866 889 -6 -173 28 N ATOM 1182 CA ILE A 167 1.133 14.566 60.944 1.00 7.51 C ANISOU 1182 CA ILE A 167 1037 833 982 3 -201 50 C ATOM 1183 C ILE A 167 1.643 14.584 59.493 1.00 7.14 C ANISOU 1183 C ILE A 167 960 786 966 -47 -195 52 C ATOM 1184 O ILE A 167 1.487 15.563 58.765 1.00 7.43 O ANISOU 1184 O ILE A 167 979 844 999 -1 -133 105 O ATOM 1185 CB ILE A 167 0.010 13.525 61.170 1.00 7.10 C ANISOU 1185 CB ILE A 167 1031 810 853 38 -71 91 C ATOM 1186 CG1 ILE A 167 -1.233 13.888 60.353 1.00 7.60 C ANISOU 1186 CG1 ILE A 167 995 834 1058 -29 -140 107 C ATOM 1187 CG2 ILE A 167 -0.299 13.418 62.649 1.00 7.96 C ANISOU 1187 CG2 ILE A 167 1156 948 920 -46 -9 146 C ATOM 1188 CD1 ILE A 167 -2.278 12.781 60.312 1.00 8.03 C ANISOU 1188 CD1 ILE A 167 989 876 1183 -36 -87 45 C ATOM 1189 N THR A 168 2.272 13.484 59.105 1.00 7.20 N ANISOU 1189 N THR A 168 919 859 956 40 -84 139 N ATOM 1190 CA THR A 168 2.959 13.362 57.826 1.00 7.34 C ANISOU 1190 CA THR A 168 920 860 1008 42 -28 144 C ATOM 1191 C THR A 168 2.604 12.010 57.205 1.00 7.26 C ANISOU 1191 C THR A 168 864 816 1076 84 -144 144 C ATOM 1192 O THR A 168 2.148 11.100 57.918 1.00 7.64 O ANISOU 1192 O THR A 168 1027 823 1052 47 -15 119 O ATOM 1193 CB THR A 168 4.486 13.507 57.979 1.00 8.11 C ANISOU 1193 CB THR A 168 942 930 1208 54 -155 159 C ATOM 1194 OG1 THR A 168 5.022 12.425 58.752 1.00 8.89 O ANISOU 1194 OG1 THR A 168 988 1044 1345 103 -173 231 O ATOM 1195 CG2 THR A 168 4.859 14.850 58.604 1.00 8.59 C ANISOU 1195 CG2 THR A 168 1000 1061 1203 10 -113 28 C ATOM 1196 N VAL A 169 2.796 11.883 55.892 1.00 7.56 N ANISOU 1196 N VAL A 169 968 796 1106 55 -68 89 N ATOM 1197 CA VAL A 169 2.320 10.697 55.176 1.00 7.97 C ANISOU 1197 CA VAL A 169 992 856 1180 47 -48 -7 C ATOM 1198 C VAL A 169 3.314 10.300 54.097 1.00 7.82 C ANISOU 1198 C VAL A 169 1003 822 1146 6 -2 23 C ATOM 1199 O VAL A 169 3.616 11.098 53.220 1.00 9.18 O ANISOU 1199 O VAL A 169 1276 1000 1211 51 146 98 O ATOM 1200 CB VAL A 169 0.943 10.962 54.510 1.00 8.42 C ANISOU 1200 CB VAL A 169 988 1009 1200 -17 -75 64 C ATOM 1201 CG1 VAL A 169 0.413 9.683 53.883 1.00 9.65 C ANISOU 1201 CG1 VAL A 169 1127 1094 1443 14 -47 -120 C ATOM 1202 CG2 VAL A 169 -0.072 11.542 55.500 1.00 8.89 C ANISOU 1202 CG2 VAL A 169 980 1117 1280 70 -43 143 C ATOM 1203 N GLY A 170 3.793 9.064 54.160 1.00 8.57 N ANISOU 1203 N GLY A 170 1093 948 1212 156 124 156 N ATOM 1204 CA GLY A 170 4.584 8.496 53.078 1.00 9.32 C ANISOU 1204 CA GLY A 170 1191 1040 1311 132 159 5 C ATOM 1205 C GLY A 170 3.709 7.676 52.159 1.00 9.18 C ANISOU 1205 C GLY A 170 1155 1008 1321 121 126 67 C ATOM 1206 O GLY A 170 2.684 7.152 52.597 1.00 9.88 O ANISOU 1206 O GLY A 170 1405 1211 1137 -140 186 -24 O ATOM 1207 N ILE A 171 4.089 7.569 50.889 1.00 10.17 N ANISOU 1207 N ILE A 171 1205 1328 1328 111 166 41 N ATOM 1208 CA ILE A 171 3.317 6.771 49.942 1.00 11.21 C ANISOU 1208 CA ILE A 171 1201 1666 1390 61 165 -122 C ATOM 1209 C ILE A 171 4.155 5.580 49.513 1.00 11.78 C ANISOU 1209 C ILE A 171 1178 1656 1640 2 255 -161 C ATOM 1210 O ILE A 171 5.087 5.692 48.703 1.00 12.27 O ANISOU 1210 O ILE A 171 1350 1613 1699 10 401 -239 O ATOM 1211 CB ILE A 171 2.855 7.573 48.715 1.00 12.46 C ANISOU 1211 CB ILE A 171 1423 1872 1438 167 124 -70 C ATOM 1212 CG1 ILE A 171 2.156 8.853 49.162 1.00 14.26 C ANISOU 1212 CG1 ILE A 171 1593 2148 1676 499 71 -146 C ATOM 1213 CG2 ILE A 171 1.931 6.719 47.854 1.00 14.12 C ANISOU 1213 CG2 ILE A 171 1633 2260 1469 115 17 -245 C ATOM 1214 CD1 ILE A 171 1.816 9.772 48.023 1.00 15.66 C ANISOU 1214 CD1 ILE A 171 1827 2180 1940 220 -104 16 C ATOM 1215 N ASP A 172 3.830 4.426 50.080 1.00 12.58 N ANISOU 1215 N ASP A 172 1384 1665 1729 52 287 -112 N ATOM 1216 CA ASP A 172 4.530 3.207 49.697 1.00 14.89 C ANISOU 1216 CA ASP A 172 1754 1596 2305 104 403 -97 C ATOM 1217 C ASP A 172 4.412 2.942 48.199 1.00 15.75 C ANISOU 1217 C ASP A 172 1988 1609 2387 -10 635 -328 C ATOM 1218 O ASP A 172 3.399 3.251 47.577 1.00 16.92 O ANISOU 1218 O ASP A 172 2204 2004 2220 -145 376 -526 O ATOM 1219 CB ASP A 172 4.006 2.013 50.493 1.00 17.86 C ANISOU 1219 CB ASP A 172 2303 1735 2747 202 554 196 C ATOM 1220 CG ASP A 172 4.792 1.775 51.757 1.00 24.37 C ANISOU 1220 CG ASP A 172 3182 3065 3012 -227 184 601 C ATOM 1221 OD1 ASP A 172 5.674 2.601 52.081 1.00 26.80 O ANISOU 1221 OD1 ASP A 172 3732 3089 3361 -390 99 436 O ATOM 1222 OD2 ASP A 172 4.533 0.753 52.425 1.00 30.78 O ANISOU 1222 OD2 ASP A 172 4409 3388 3895 -440 164 1102 O ATOM 1223 N GLY A 173 5.477 2.397 47.622 1.00 16.60 N ANISOU 1223 N GLY A 173 2244 1521 2542 90 758 -343 N ATOM 1224 CA GLY A 173 5.522 2.125 46.194 1.00 18.60 C ANISOU 1224 CA GLY A 173 2707 1703 2656 -57 901 -707 C ATOM 1225 C GLY A 173 5.951 3.318 45.366 1.00 17.42 C ANISOU 1225 C GLY A 173 2452 1747 2417 -163 991 -928 C ATOM 1226 O GLY A 173 5.988 3.233 44.141 1.00 21.29 O ANISOU 1226 O GLY A 173 3328 2289 2469 -647 1067 -1233 O ATOM 1227 N THR A 174 6.276 4.420 46.035 1.00 15.30 N ANISOU 1227 N THR A 174 1925 1575 2312 -128 773 -645 N ATOM 1228 CA THR A 174 6.719 5.628 45.367 1.00 14.59 C ANISOU 1228 CA THR A 174 1749 1688 2106 -168 548 -558 C ATOM 1229 C THR A 174 7.905 6.195 46.112 1.00 14.16 C ANISOU 1229 C THR A 174 1818 1652 1910 -44 554 -616 C ATOM 1230 O THR A 174 8.266 5.735 47.200 1.00 15.65 O ANISOU 1230 O THR A 174 1953 1848 2143 65 479 -409 O ATOM 1231 CB THR A 174 5.629 6.723 45.346 1.00 13.57 C ANISOU 1231 CB THR A 174 1728 1735 1693 -146 375 -565 C ATOM 1232 OG1 THR A 174 5.594 7.382 46.615 1.00 12.24 O ANISOU 1232 OG1 THR A 174 1624 1440 1586 -147 441 -360 O ATOM 1233 CG2 THR A 174 4.267 6.143 44.989 1.00 14.69 C ANISOU 1233 CG2 THR A 174 1720 2012 1850 -171 296 -469 C ATOM 1234 N ASP A 175 8.496 7.223 45.528 1.00 13.95 N ANISOU 1234 N ASP A 175 1510 1726 2061 -99 526 -614 N ATOM 1235 CA AASP A 175 9.604 7.940 46.141 0.53 14.21 C ANISOU 1235 CA AASP A 175 1510 1701 2187 -28 412 -615 C ATOM 1236 CA BASP A 175 9.602 7.910 46.187 0.47 13.94 C ANISOU 1236 CA BASP A 175 1476 1694 2124 -27 441 -583 C ATOM 1237 C ASP A 175 9.138 9.162 46.929 1.00 12.08 C ANISOU 1237 C ASP A 175 1287 1490 1813 -71 384 -358 C ATOM 1238 O ASP A 175 9.947 10.024 47.252 1.00 12.22 O ANISOU 1238 O ASP A 175 1198 1464 1979 33 86 -305 O ATOM 1239 CB AASP A 175 10.586 8.390 45.051 0.53 18.01 C ANISOU 1239 CB AASP A 175 2124 2411 2306 -246 630 -483 C ATOM 1240 CB BASP A 175 10.718 8.231 45.183 0.47 17.07 C ANISOU 1240 CB BASP A 175 1914 2360 2212 -100 688 -537 C ATOM 1241 CG AASP A 175 11.150 7.229 44.255 0.53 19.16 C ANISOU 1241 CG AASP A 175 2118 2526 2636 -257 715 -620 C ATOM 1242 CG BASP A 175 10.277 9.181 44.081 0.47 17.97 C ANISOU 1242 CG BASP A 175 2195 2436 2195 -172 751 -410 C ATOM 1243 OD1AASP A 175 11.495 6.202 44.871 0.53 22.66 O ANISOU 1243 OD1AASP A 175 2728 2767 3113 123 381 -588 O ATOM 1244 OD1BASP A 175 9.138 9.688 44.121 0.47 19.60 O ANISOU 1244 OD1BASP A 175 2456 2593 2398 122 426 -293 O ATOM 1245 OD2AASP A 175 11.255 7.348 43.016 0.53 23.97 O ANISOU 1245 OD2AASP A 175 2982 3449 2673 -28 698 -608 O ATOM 1246 OD2BASP A 175 11.086 9.415 43.159 0.47 20.55 O ANISOU 1246 OD2BASP A 175 2284 3190 2332 -57 892 -227 O ATOM 1247 N ILE A 176 7.843 9.234 47.235 1.00 10.63 N ANISOU 1247 N ILE A 176 1218 1305 1513 -41 231 -306 N ATOM 1248 CA ILE A 176 7.224 10.440 47.779 1.00 9.65 C ANISOU 1248 CA ILE A 176 1155 1155 1354 -9 159 -102 C ATOM 1249 C ILE A 176 6.922 10.349 49.278 1.00 8.73 C ANISOU 1249 C ILE A 176 915 1070 1331 104 136 -76 C ATOM 1250 O ILE A 176 6.363 9.364 49.768 1.00 9.70 O ANISOU 1250 O ILE A 176 1178 1050 1457 13 180 -115 O ATOM 1251 CB ILE A 176 5.910 10.731 47.018 1.00 10.47 C ANISOU 1251 CB ILE A 176 1220 1344 1411 -145 52 -31 C ATOM 1252 CG1 ILE A 176 6.201 11.021 45.545 1.00 12.34 C ANISOU 1252 CG1 ILE A 176 1600 1638 1451 -215 61 77 C ATOM 1253 CG2 ILE A 176 5.147 11.892 47.648 1.00 11.76 C ANISOU 1253 CG2 ILE A 176 1420 1292 1757 89 -136 49 C ATOM 1254 CD1 ILE A 176 4.975 11.018 44.661 1.00 13.69 C ANISOU 1254 CD1 ILE A 176 1759 1892 1550 -64 -50 -43 C ATOM 1255 N ALA A 177 7.253 11.422 49.993 1.00 8.99 N ANISOU 1255 N ALA A 177 911 1115 1387 103 145 -110 N ATOM 1256 CA ALA A 177 6.764 11.622 51.354 1.00 9.12 C ANISOU 1256 CA ALA A 177 1105 1005 1355 140 130 20 C ATOM 1257 C ALA A 177 6.219 13.050 51.475 1.00 8.52 C ANISOU 1257 C ALA A 177 872 974 1388 74 59 89 C ATOM 1258 O ALA A 177 6.789 13.992 50.924 1.00 9.72 O ANISOU 1258 O ALA A 177 1061 1049 1583 79 252 170 O ATOM 1259 CB ALA A 177 7.859 11.384 52.379 1.00 10.55 C ANISOU 1259 CB ALA A 177 1414 1131 1463 343 -21 -21 C ATOM 1260 N PHE A 178 5.115 13.175 52.210 1.00 8.09 N ANISOU 1260 N PHE A 178 855 878 1339 101 4 88 N ATOM 1261 CA PHE A 178 4.383 14.428 52.361 1.00 7.61 C ANISOU 1261 CA PHE A 178 824 885 1182 95 -2 114 C ATOM 1262 C PHE A 178 4.578 14.965 53.766 1.00 7.31 C ANISOU 1262 C PHE A 178 744 830 1202 79 32 145 C ATOM 1263 O PHE A 178 4.160 14.362 54.760 1.00 7.94 O ANISOU 1263 O PHE A 178 927 966 1122 5 -31 146 O ATOM 1264 CB PHE A 178 2.899 14.194 52.107 1.00 7.81 C ANISOU 1264 CB PHE A 178 886 955 1126 84 -82 103 C ATOM 1265 CG PHE A 178 2.056 15.443 52.182 1.00 7.70 C ANISOU 1265 CG PHE A 178 773 940 1212 38 -61 105 C ATOM 1266 CD1 PHE A 178 2.168 16.433 51.220 1.00 9.20 C ANISOU 1266 CD1 PHE A 178 965 1118 1410 192 100 239 C ATOM 1267 CD2 PHE A 178 1.114 15.609 53.205 1.00 7.81 C ANISOU 1267 CD2 PHE A 178 887 968 1111 18 -55 180 C ATOM 1268 CE1 PHE A 178 1.369 17.566 51.269 1.00 8.97 C ANISOU 1268 CE1 PHE A 178 1071 1000 1336 177 45 277 C ATOM 1269 CE2 PHE A 178 0.323 16.750 53.263 1.00 8.21 C ANISOU 1269 CE2 PHE A 178 704 1062 1353 34 26 106 C ATOM 1270 CZ PHE A 178 0.434 17.713 52.282 1.00 7.97 C ANISOU 1270 CZ PHE A 178 747 895 1385 78 -70 50 C ATOM 1271 N GLY A 179 5.200 16.138 53.841 1.00 7.54 N ANISOU 1271 N GLY A 179 839 921 1102 -22 -38 117 N ATOM 1272 CA GLY A 179 5.446 16.793 55.091 1.00 7.87 C ANISOU 1272 CA GLY A 179 853 944 1191 14 -60 78 C ATOM 1273 C GLY A 179 4.380 17.772 55.533 1.00 7.93 C ANISOU 1273 C GLY A 179 886 955 1170 9 -138 -10 C ATOM 1274 O GLY A 179 4.457 18.314 56.632 1.00 8.31 O ANISOU 1274 O GLY A 179 918 1046 1193 10 -107 -24 O ATOM 1275 N GLY A 180 3.381 18.027 54.694 1.00 8.08 N ANISOU 1275 N GLY A 180 923 977 1168 42 -156 -11 N ATOM 1276 CA GLY A 180 2.362 19.020 55.027 1.00 7.79 C ANISOU 1276 CA GLY A 180 822 974 1161 -41 -38 21 C ATOM 1277 C GLY A 180 2.998 20.359 55.316 1.00 7.86 C ANISOU 1277 C GLY A 180 840 935 1210 -36 -146 82 C ATOM 1278 O GLY A 180 3.930 20.775 54.640 1.00 8.89 O ANISOU 1278 O GLY A 180 900 1085 1391 -86 -69 157 O ATOM 1279 N CYS A 181 2.491 21.045 56.325 1.00 7.83 N ANISOU 1279 N CYS A 181 859 904 1212 -111 -168 61 N ATOM 1280 CA CYS A 181 2.964 22.392 56.625 1.00 8.58 C ANISOU 1280 CA CYS A 181 911 925 1422 -58 -160 -17 C ATOM 1281 C CYS A 181 4.192 22.391 57.526 1.00 8.37 C ANISOU 1281 C CYS A 181 856 1013 1310 -99 -60 -29 C ATOM 1282 O CYS A 181 4.749 23.445 57.810 1.00 10.14 O ANISOU 1282 O CYS A 181 1070 1062 1719 -172 -276 -64 O ATOM 1283 CB CYS A 181 1.860 23.261 57.210 1.00 8.57 C ANISOU 1283 CB CYS A 181 947 971 1337 -94 -185 -26 C ATOM 1284 SG CYS A 181 0.348 23.222 56.224 1.00 8.23 S ANISOU 1284 SG CYS A 181 884 1010 1231 -52 -114 36 S ATOM 1285 N LEU A 182 4.649 21.221 57.954 1.00 8.54 N ANISOU 1285 N LEU A 182 875 1042 1324 -100 -188 -17 N ATOM 1286 CA LEU A 182 5.863 21.123 58.753 1.00 8.97 C ANISOU 1286 CA LEU A 182 906 1156 1346 -154 -226 53 C ATOM 1287 C LEU A 182 7.104 21.509 57.947 1.00 9.02 C ANISOU 1287 C LEU A 182 846 1033 1549 -133 -139 -87 C ATOM 1288 O LEU A 182 8.037 22.110 58.490 1.00 9.76 O ANISOU 1288 O LEU A 182 931 1273 1501 -209 -180 -134 O ATOM 1289 CB LEU A 182 6.006 19.701 59.284 1.00 9.37 C ANISOU 1289 CB LEU A 182 1033 1156 1371 -89 -296 10 C ATOM 1290 CG LEU A 182 7.244 19.392 60.129 1.00 9.81 C ANISOU 1290 CG LEU A 182 968 1315 1442 -55 -243 87 C ATOM 1291 CD1 LEU A 182 7.195 20.130 61.454 1.00 10.97 C ANISOU 1291 CD1 LEU A 182 1244 1461 1463 -39 -417 22 C ATOM 1292 CD2 LEU A 182 7.344 17.896 60.350 1.00 10.97 C ANISOU 1292 CD2 LEU A 182 1147 1348 1671 -6 -355 198 C ATOM 1293 N ILE A 183 7.136 21.128 56.674 1.00 9.12 N ANISOU 1293 N ILE A 183 815 1113 1536 -161 -216 -82 N ATOM 1294 CA ILE A 183 8.327 21.248 55.830 1.00 9.66 C ANISOU 1294 CA ILE A 183 850 1223 1598 -99 -160 -105 C ATOM 1295 C ILE A 183 8.145 22.356 54.792 1.00 9.35 C ANISOU 1295 C ILE A 183 731 1235 1584 -91 -26 -101 C ATOM 1296 O ILE A 183 7.072 22.486 54.207 1.00 9.88 O ANISOU 1296 O ILE A 183 868 1301 1584 -188 -160 64 O ATOM 1297 CB ILE A 183 8.635 19.892 55.142 1.00 9.83 C ANISOU 1297 CB ILE A 183 943 1250 1542 -60 -5 -104 C ATOM 1298 CG1 ILE A 183 8.767 18.758 56.177 1.00 10.08 C ANISOU 1298 CG1 ILE A 183 1006 1175 1649 44 1 -90 C ATOM 1299 CG2 ILE A 183 9.874 19.989 54.270 1.00 10.78 C ANISOU 1299 CG2 ILE A 183 1156 1228 1711 -17 193 -138 C ATOM 1300 CD1 ILE A 183 9.898 18.904 57.173 1.00 10.78 C ANISOU 1300 CD1 ILE A 183 1079 1394 1622 73 -55 34 C ATOM 1301 N LYS A 184 9.194 23.172 54.643 1.00 10.37 N ANISOU 1301 N LYS A 184 868 1203 1869 -151 -107 -21 N ATOM 1302 CA BLYS A 184 9.307 24.212 53.616 0.33 11.31 C ANISOU 1302 CA BLYS A 184 981 1348 1966 -165 -53 80 C ATOM 1303 CA CLYS A 184 9.277 24.180 53.592 0.66 11.45 C ANISOU 1303 CA CLYS A 184 893 1393 2063 -161 -55 151 C ATOM 1304 C LYS A 184 10.420 23.824 52.652 1.00 11.13 C ANISOU 1304 C LYS A 184 872 1352 2004 -193 -79 81 C ATOM 1305 O LYS A 184 11.290 23.023 52.993 1.00 10.94 O ANISOU 1305 O LYS A 184 887 1416 1850 -80 58 -35 O ATOM 1306 CB BLYS A 184 9.665 25.563 54.239 0.33 12.41 C ANISOU 1306 CB BLYS A 184 1262 1332 2120 -169 81 6 C ATOM 1307 CB CLYS A 184 9.494 25.574 54.185 0.66 13.68 C ANISOU 1307 CB CLYS A 184 1522 1348 2327 -163 135 117 C ATOM 1308 CG BLYS A 184 8.746 26.013 55.357 0.33 13.76 C ANISOU 1308 CG BLYS A 184 1657 1390 2180 -87 147 -165 C ATOM 1309 CG CLYS A 184 8.244 26.171 54.816 0.66 15.04 C ANISOU 1309 CG CLYS A 184 1640 1719 2354 28 58 82 C ATOM 1310 CD BLYS A 184 7.293 26.065 54.907 0.33 15.26 C ANISOU 1310 CD BLYS A 184 1711 1731 2356 38 67 -100 C ATOM 1311 CD CLYS A 184 7.216 26.604 53.785 0.66 16.04 C ANISOU 1311 CD CLYS A 184 1623 1861 2607 -98 -47 150 C ATOM 1312 CE BLYS A 184 7.083 26.873 53.630 0.33 16.51 C ANISOU 1312 CE BLYS A 184 2058 1857 2356 15 30 -38 C ATOM 1313 CE CLYS A 184 7.666 27.839 53.018 0.66 16.97 C ANISOU 1313 CE CLYS A 184 2101 1926 2417 -240 1 87 C ATOM 1314 NZ BLYS A 184 6.923 26.037 52.404 0.33 14.80 N ANISOU 1314 NZ BLYS A 184 1797 1472 2351 278 -253 105 N ATOM 1315 NZ CLYS A 184 6.542 28.510 52.317 0.66 17.71 N ANISOU 1315 NZ CLYS A 184 2284 1855 2591 -77 9 23 N ATOM 1316 N ASP A 185 10.425 24.401 51.454 1.00 12.19 N ANISOU 1316 N ASP A 185 1012 1458 2161 -183 -112 299 N ATOM 1317 CA AASP A 185 11.401 24.011 50.432 0.42 12.97 C ANISOU 1317 CA AASP A 185 1114 1600 2213 -376 -9 215 C ATOM 1318 CA BASP A 185 11.415 23.943 50.474 0.58 12.74 C ANISOU 1318 CA BASP A 185 1100 1605 2135 -321 -48 233 C ATOM 1319 C ASP A 185 12.805 24.485 50.783 1.00 12.53 C ANISOU 1319 C ASP A 185 1105 1462 2192 -265 -40 54 C ATOM 1320 O ASP A 185 12.993 25.310 51.691 1.00 13.11 O ANISOU 1320 O ASP A 185 1142 1731 2106 -314 -7 -32 O ATOM 1321 CB AASP A 185 11.014 24.548 49.054 0.42 14.03 C ANISOU 1321 CB AASP A 185 1182 1815 2334 -482 -45 403 C ATOM 1322 CB BASP A 185 10.978 24.139 49.005 0.58 13.04 C ANISOU 1322 CB BASP A 185 1061 1739 2154 -314 -40 345 C ATOM 1323 CG AASP A 185 11.100 26.058 48.969 0.42 15.81 C ANISOU 1323 CG AASP A 185 1407 1838 2762 -589 -120 430 C ATOM 1324 CG BASP A 185 11.096 25.572 48.505 0.58 13.75 C ANISOU 1324 CG BASP A 185 1140 1859 2224 -268 46 519 C ATOM 1325 OD1AASP A 185 10.131 26.736 49.357 0.42 17.04 O ANISOU 1325 OD1AASP A 185 1704 1830 2941 -471 -149 261 O ATOM 1326 OD1BASP A 185 11.805 26.405 49.110 0.58 14.72 O ANISOU 1326 OD1BASP A 185 1585 1718 2287 -294 112 416 O ATOM 1327 OD2AASP A 185 12.139 26.562 48.502 0.42 16.13 O ANISOU 1327 OD2AASP A 185 1518 2046 2563 -431 128 514 O ATOM 1328 OD2BASP A 185 10.469 25.850 47.459 0.58 14.33 O ANISOU 1328 OD2BASP A 185 1443 1843 2157 -243 43 602 O ATOM 1329 N SER A 186 13.778 23.987 50.032 1.00 13.13 N ANISOU 1329 N SER A 186 1048 1671 2267 -160 8 166 N ATOM 1330 CA SER A 186 15.185 24.213 50.315 1.00 14.86 C ANISOU 1330 CA SER A 186 1034 2084 2528 -220 45 82 C ATOM 1331 C SER A 186 15.654 25.644 50.142 1.00 16.90 C ANISOU 1331 C SER A 186 1224 2212 2984 -390 292 109 C ATOM 1332 O SER A 186 16.754 25.978 50.573 1.00 19.93 O ANISOU 1332 O SER A 186 1355 2601 3615 -705 294 -244 O ATOM 1333 CB SER A 186 16.036 23.298 49.434 1.00 15.84 C ANISOU 1333 CB SER A 186 1140 2188 2688 -60 -6 42 C ATOM 1334 OG SER A 186 15.813 23.536 48.054 1.00 17.90 O ANISOU 1334 OG SER A 186 1814 2470 2516 -294 370 12 O ATOM 1335 N LYS A 187 14.832 26.473 49.507 1.00 17.21 N ANISOU 1335 N LYS A 187 1439 1965 3134 -517 368 322 N ATOM 1336 CA LYS A 187 15.144 27.879 49.317 1.00 19.53 C ANISOU 1336 CA LYS A 187 1891 2029 3499 -685 720 275 C ATOM 1337 C LYS A 187 14.253 28.812 50.142 1.00 18.60 C ANISOU 1337 C LYS A 187 1724 1748 3594 -518 338 230 C ATOM 1338 O LYS A 187 14.334 30.026 49.980 1.00 20.80 O ANISOU 1338 O LYS A 187 2205 1786 3912 -643 522 377 O ATOM 1339 CB LYS A 187 15.009 28.247 47.837 1.00 24.18 C ANISOU 1339 CB LYS A 187 3187 2358 3639 -636 663 600 C ATOM 1340 CG LYS A 187 15.988 27.551 46.908 1.00 28.82 C ANISOU 1340 CG LYS A 187 3727 3340 3881 -281 817 360 C ATOM 1341 CD LYS A 187 15.735 27.984 45.473 1.00 35.69 C ANISOU 1341 CD LYS A 187 4978 4594 3986 -137 569 485 C ATOM 1342 CE LYS A 187 16.739 27.388 44.502 1.00 39.23 C ANISOU 1342 CE LYS A 187 5326 5480 4100 29 631 131 C ATOM 1343 NZ LYS A 187 16.485 27.855 43.110 1.00 45.45 N ANISOU 1343 NZ LYS A 187 6549 6538 4180 64 52 112 N ATOM 1344 N ALA A 188 13.409 28.264 51.017 1.00 17.48 N ANISOU 1344 N ALA A 188 1576 1579 3482 -487 259 81 N ATOM 1345 CA ALA A 188 12.478 29.090 51.791 1.00 16.87 C ANISOU 1345 CA ALA A 188 1453 1643 3312 -405 38 31 C ATOM 1346 C ALA A 188 13.213 30.048 52.718 1.00 16.68 C ANISOU 1346 C ALA A 188 1415 1504 3417 -265 -205 137 C ATOM 1347 O ALA A 188 14.226 29.692 53.309 1.00 17.31 O ANISOU 1347 O ALA A 188 1573 1523 3480 -148 -317 101 O ATOM 1348 CB ALA A 188 11.532 28.218 52.600 1.00 17.02 C ANISOU 1348 CB ALA A 188 1507 1575 3384 -360 123 -7 C ATOM 1349 N LYS A 189 12.677 31.254 52.865 1.00 17.66 N ANISOU 1349 N LYS A 189 1506 1484 3719 -264 -354 6 N ATOM 1350 CA LYS A 189 13.273 32.252 53.742 1.00 18.30 C ANISOU 1350 CA LYS A 189 1683 1441 3827 -399 -98 -100 C ATOM 1351 C LYS A 189 12.840 32.107 55.191 1.00 19.50 C ANISOU 1351 C LYS A 189 2285 1517 3606 -521 -494 -30 C ATOM 1352 O LYS A 189 13.549 32.559 56.087 1.00 24.58 O ANISOU 1352 O LYS A 189 3136 2314 3888 -1114 -964 82 O ATOM 1353 CB LYS A 189 12.937 33.652 53.248 1.00 21.70 C ANISOU 1353 CB LYS A 189 2543 1575 4124 -112 153 15 C ATOM 1354 CG LYS A 189 13.830 34.098 52.108 1.00 25.63 C ANISOU 1354 CG LYS A 189 2966 2450 4322 -461 336 180 C ATOM 1355 CD LYS A 189 13.339 35.382 51.454 1.00 29.95 C ANISOU 1355 CD LYS A 189 4044 2653 4681 -360 215 464 C ATOM 1356 CE LYS A 189 13.053 36.483 52.465 1.00 33.43 C ANISOU 1356 CE LYS A 189 4371 3350 4980 -132 269 28 C ATOM 1357 NZ LYS A 189 13.237 37.839 51.877 1.00 37.09 N ANISOU 1357 NZ LYS A 189 4954 3596 5543 -119 254 400 N ATOM 1358 N SER A 190 11.688 31.496 55.436 1.00 20.00 N ANISOU 1358 N SER A 190 2457 1578 3563 -660 -340 -276 N ATOM 1359 CA SER A 190 11.231 31.317 56.807 1.00 21.74 C ANISOU 1359 CA SER A 190 2743 1914 3601 -670 -239 -163 C ATOM 1360 C SER A 190 10.306 30.122 56.930 1.00 20.48 C ANISOU 1360 C SER A 190 2814 1647 3320 -490 87 -187 C ATOM 1361 O SER A 190 9.934 29.494 55.932 1.00 20.65 O ANISOU 1361 O SER A 190 2761 1692 3389 -582 137 -173 O ATOM 1362 CB SER A 190 10.508 32.573 57.297 1.00 24.64 C ANISOU 1362 CB SER A 190 3189 2180 3989 -369 -117 -196 C ATOM 1363 OG SER A 190 9.192 32.635 56.776 1.00 26.48 O ANISOU 1363 OG SER A 190 3302 2157 4602 -320 -368 -19 O ATOM 1364 N LEU A 191 9.928 29.831 58.172 1.00 19.69 N ANISOU 1364 N LEU A 191 2435 1823 3223 -593 -34 -172 N ATOM 1365 CA LEU A 191 8.988 28.758 58.484 1.00 19.36 C ANISOU 1365 CA LEU A 191 2324 1706 3326 -502 -120 -125 C ATOM 1366 C LEU A 191 7.532 29.242 58.496 1.00 19.09 C ANISOU 1366 C LEU A 191 2360 1634 3259 -436 -140 61 C ATOM 1367 O LEU A 191 6.617 28.484 58.834 1.00 20.70 O ANISOU 1367 O LEU A 191 2370 1756 3739 -490 -219 269 O ATOM 1368 CB LEU A 191 9.352 28.135 59.836 1.00 19.17 C ANISOU 1368 CB LEU A 191 2017 2013 3251 -304 70 -108 C ATOM 1369 CG LEU A 191 10.744 27.497 59.893 1.00 19.75 C ANISOU 1369 CG LEU A 191 1982 2097 3425 -239 171 -224 C ATOM 1370 CD1 LEU A 191 11.129 27.169 61.325 1.00 21.91 C ANISOU 1370 CD1 LEU A 191 2444 2384 3495 -12 148 -142 C ATOM 1371 CD2 LEU A 191 10.800 26.250 59.028 1.00 19.41 C ANISOU 1371 CD2 LEU A 191 1869 1900 3602 -93 285 -133 C ATOM 1372 N GLY A 192 7.318 30.498 58.114 1.00 20.71 N ANISOU 1372 N GLY A 192 2468 1655 3743 -431 -381 101 N ATOM 1373 CA GLY A 192 5.986 31.081 58.092 1.00 21.98 C ANISOU 1373 CA GLY A 192 2588 1996 3764 -228 -233 39 C ATOM 1374 C GLY A 192 5.489 31.412 59.485 1.00 21.57 C ANISOU 1374 C GLY A 192 2787 1751 3654 -268 -163 364 C ATOM 1375 O GLY A 192 6.270 31.525 60.427 1.00 25.12 O ANISOU 1375 O GLY A 192 3009 2509 4025 -164 -418 -109 O ATOM 1376 N ASN A 193 4.177 31.570 59.607 1.00 25.01 N ANISOU 1376 N ASN A 193 2849 2650 4002 -46 -205 416 N ATOM 1377 CA ASN A 193 3.542 31.856 60.888 1.00 23.39 C ANISOU 1377 CA ASN A 193 2785 2305 3794 -344 -395 154 C ATOM 1378 C ASN A 193 3.779 30.712 61.878 1.00 21.91 C ANISOU 1378 C ASN A 193 2528 2112 3685 -44 -152 -23 C ATOM 1379 O ASN A 193 3.441 29.561 61.604 1.00 23.42 O ANISOU 1379 O ASN A 193 2740 2328 3831 -419 -475 70 O ATOM 1380 CB ASN A 193 2.040 32.096 60.687 1.00 27.64 C ANISOU 1380 CB ASN A 193 2926 3483 4091 78 -357 258 C ATOM 1381 CG ASN A 193 1.252 32.031 61.982 1.00 28.70 C ANISOU 1381 CG ASN A 193 2803 3974 4128 608 -268 -86 C ATOM 1382 OD1 ASN A 193 1.635 32.628 62.987 1.00 32.69 O ANISOU 1382 OD1 ASN A 193 3831 3914 4675 74 -271 -390 O ATOM 1383 ND2 ASN A 193 0.143 31.298 61.965 1.00 37.65 N ANISOU 1383 ND2 ASN A 193 3984 4784 5537 -425 -67 39 N ATOM 1384 N LEU A 194 4.364 31.053 63.021 1.00 22.51 N ANISOU 1384 N LEU A 194 2572 2418 3562 -116 82 -106 N ATOM 1385 CA LEU A 194 4.657 30.089 64.073 1.00 20.79 C ANISOU 1385 CA LEU A 194 2220 2220 3459 -33 279 -231 C ATOM 1386 C LEU A 194 3.728 30.283 65.273 1.00 18.62 C ANISOU 1386 C LEU A 194 2002 1616 3456 -67 121 -642 C ATOM 1387 O LEU A 194 4.020 29.826 66.374 1.00 20.23 O ANISOU 1387 O LEU A 194 2104 2148 3434 -390 -240 -740 O ATOM 1388 CB LEU A 194 6.122 30.223 64.492 1.00 21.05 C ANISOU 1388 CB LEU A 194 2222 2034 3741 -3 223 -454 C ATOM 1389 CG LEU A 194 7.134 29.859 63.401 1.00 22.51 C ANISOU 1389 CG LEU A 194 2148 2586 3819 -71 304 -364 C ATOM 1390 CD1 LEU A 194 8.535 30.269 63.821 1.00 23.71 C ANISOU 1390 CD1 LEU A 194 2120 2812 4075 -81 302 -347 C ATOM 1391 CD2 LEU A 194 7.084 28.374 63.072 1.00 22.63 C ANISOU 1391 CD2 LEU A 194 2226 2602 3769 156 312 -506 C ATOM 1392 N GLY A 195 2.582 30.920 65.049 1.00 20.27 N ANISOU 1392 N GLY A 195 2032 1880 3788 -5 182 -444 N ATOM 1393 CA GLY A 195 1.637 31.199 66.121 1.00 19.85 C ANISOU 1393 CA GLY A 195 2305 1760 3475 -40 109 -558 C ATOM 1394 C GLY A 195 1.197 29.974 66.905 1.00 17.70 C ANISOU 1394 C GLY A 195 2075 1653 2996 -45 -158 -744 C ATOM 1395 O GLY A 195 1.002 30.047 68.119 1.00 20.48 O ANISOU 1395 O GLY A 195 2824 1921 3034 -125 -130 -1203 O ATOM 1396 N ASP A 196 1.038 28.846 66.218 1.00 16.19 N ANISOU 1396 N ASP A 196 1832 1573 2745 13 -313 -602 N ATOM 1397 CA ASP A 196 0.618 27.605 66.867 1.00 14.19 C ANISOU 1397 CA ASP A 196 1611 1588 2192 -17 -341 -746 C ATOM 1398 C ASP A 196 1.766 26.606 66.965 1.00 14.67 C ANISOU 1398 C ASP A 196 1691 1754 2127 54 -540 -746 C ATOM 1399 O ASP A 196 1.547 25.446 67.306 1.00 14.85 O ANISOU 1399 O ASP A 196 1860 1716 2065 172 -487 -716 O ATOM 1400 CB ASP A 196 -0.554 26.989 66.098 1.00 13.31 C ANISOU 1400 CB ASP A 196 1701 1579 1777 2 -363 -657 C ATOM 1401 CG ASP A 196 -1.834 27.788 66.238 1.00 14.05 C ANISOU 1401 CG ASP A 196 1747 1698 1894 8 -328 -831 C ATOM 1402 OD1 ASP A 196 -2.014 28.485 67.246 1.00 17.38 O ANISOU 1402 OD1 ASP A 196 2115 2496 1992 427 -312 -1113 O ATOM 1403 OD2 ASP A 196 -2.688 27.698 65.340 1.00 15.59 O ANISOU 1403 OD2 ASP A 196 1819 2331 1771 253 -323 -984 O ATOM 1404 N ALA A 197 2.987 27.068 66.700 1.00 15.10 N ANISOU 1404 N ALA A 197 1690 1718 2329 67 -405 -950 N ATOM 1405 CA ALA A 197 4.147 26.196 66.625 1.00 15.12 C ANISOU 1405 CA ALA A 197 1662 1861 2219 123 -586 -860 C ATOM 1406 C ALA A 197 4.729 25.850 67.985 1.00 15.76 C ANISOU 1406 C ALA A 197 1846 2035 2105 171 -582 -981 C ATOM 1407 O ALA A 197 4.535 26.568 68.969 1.00 16.90 O ANISOU 1407 O ALA A 197 2199 2151 2069 335 -531 -954 O ATOM 1408 CB ALA A 197 5.222 26.824 65.750 1.00 15.77 C ANISOU 1408 CB ALA A 197 1784 1811 2397 96 -511 -759 C ATOM 1409 N ASP A 198 5.432 24.725 68.010 1.00 15.97 N ANISOU 1409 N ASP A 198 1940 2146 1979 285 -536 -860 N ATOM 1410 CA ASP A 198 6.271 24.331 69.132 1.00 16.53 C ANISOU 1410 CA ASP A 198 1963 2432 1885 239 -498 -830 C ATOM 1411 C ASP A 198 7.711 24.628 68.717 1.00 16.12 C ANISOU 1411 C ASP A 198 1870 2511 1741 356 -535 -905 C ATOM 1412 O ASP A 198 8.352 23.830 68.026 1.00 16.55 O ANISOU 1412 O ASP A 198 1943 2448 1897 360 -402 -833 O ATOM 1413 CB ASP A 198 6.065 22.848 69.437 1.00 18.17 C ANISOU 1413 CB ASP A 198 2453 2418 2030 313 -539 -797 C ATOM 1414 CG ASP A 198 6.782 22.402 70.691 1.00 19.52 C ANISOU 1414 CG ASP A 198 2701 2843 1873 224 -613 -943 C ATOM 1415 OD1 ASP A 198 7.904 22.886 70.951 1.00 20.15 O ANISOU 1415 OD1 ASP A 198 2441 3150 2064 382 -475 -751 O ATOM 1416 OD2 ASP A 198 6.228 21.550 71.418 1.00 24.30 O ANISOU 1416 OD2 ASP A 198 3454 3353 2425 -253 -790 -541 O ATOM 1417 N THR A 199 8.203 25.796 69.118 1.00 17.57 N ANISOU 1417 N THR A 199 2087 2496 2090 221 -357 -878 N ATOM 1418 CA THR A 199 9.499 26.290 68.655 1.00 20.06 C ANISOU 1418 CA THR A 199 2199 2728 2695 145 -222 -753 C ATOM 1419 C THR A 199 10.681 25.494 69.212 1.00 18.97 C ANISOU 1419 C THR A 199 2041 2761 2404 -30 -305 -838 C ATOM 1420 O THR A 199 11.724 25.384 68.566 1.00 22.07 O ANISOU 1420 O THR A 199 2289 3302 2795 467 -43 -801 O ATOM 1421 CB THR A 199 9.683 27.774 69.016 1.00 22.02 C ANISOU 1421 CB THR A 199 2617 2648 3098 130 -85 -593 C ATOM 1422 OG1 THR A 199 9.462 27.959 70.420 1.00 23.15 O ANISOU 1422 OG1 THR A 199 2805 2779 3212 161 -123 -1175 O ATOM 1423 CG2 THR A 199 8.706 28.637 68.227 1.00 25.08 C ANISOU 1423 CG2 THR A 199 3021 2892 3615 407 -158 -400 C ATOM 1424 N GLU A 200 10.507 24.932 70.401 1.00 18.82 N ANISOU 1424 N GLU A 200 2080 2903 2168 -68 -578 -1002 N ATOM 1425 CA GLU A 200 11.535 24.108 71.023 1.00 20.61 C ANISOU 1425 CA GLU A 200 2516 3229 2084 23 -882 -987 C ATOM 1426 C GLU A 200 11.755 22.815 70.241 1.00 18.54 C ANISOU 1426 C GLU A 200 1942 3042 2057 129 -736 -733 C ATOM 1427 O GLU A 200 12.895 22.383 70.060 1.00 19.75 O ANISOU 1427 O GLU A 200 1914 3246 2344 177 -855 -729 O ATOM 1428 CB GLU A 200 11.130 23.783 72.467 1.00 23.40 C ANISOU 1428 CB GLU A 200 2988 3681 2222 -10 -714 -802 C ATOM 1429 CG GLU A 200 12.096 22.892 73.236 1.00 28.28 C ANISOU 1429 CG GLU A 200 3516 4143 3085 242 -1045 -468 C ATOM 1430 CD GLU A 200 13.456 23.529 73.469 1.00 32.62 C ANISOU 1430 CD GLU A 200 3948 4194 4250 -170 -1291 -229 C ATOM 1431 OE1 GLU A 200 13.562 24.776 73.459 1.00 37.59 O ANISOU 1431 OE1 GLU A 200 4978 4244 5060 -133 -1304 157 O ATOM 1432 OE2 GLU A 200 14.429 22.770 73.665 1.00 38.52 O ANISOU 1432 OE2 GLU A 200 4343 4800 5492 397 -828 -67 O ATOM 1433 N HIS A 201 10.666 22.206 69.771 1.00 16.90 N ANISOU 1433 N HIS A 201 1896 2850 1673 258 -725 -637 N ATOM 1434 CA HIS A 201 10.736 20.853 69.226 1.00 16.46 C ANISOU 1434 CA HIS A 201 1896 2694 1662 247 -587 -409 C ATOM 1435 C HIS A 201 10.724 20.794 67.697 1.00 14.48 C ANISOU 1435 C HIS A 201 1669 2196 1636 196 -664 -442 C ATOM 1436 O HIS A 201 10.898 19.720 67.123 1.00 14.59 O ANISOU 1436 O HIS A 201 1611 2250 1681 157 -565 -526 O ATOM 1437 CB HIS A 201 9.589 20.007 69.786 1.00 18.18 C ANISOU 1437 CB HIS A 201 2200 2849 1857 192 -392 -249 C ATOM 1438 CG HIS A 201 9.692 19.760 71.260 1.00 21.80 C ANISOU 1438 CG HIS A 201 2966 3367 1949 382 -180 -20 C ATOM 1439 ND1 HIS A 201 8.847 20.346 72.178 1.00 22.43 N ANISOU 1439 ND1 HIS A 201 3001 3491 2030 589 -374 -242 N ATOM 1440 CD2 HIS A 201 10.554 19.002 71.979 1.00 24.34 C ANISOU 1440 CD2 HIS A 201 3274 3901 2073 602 -129 286 C ATOM 1441 CE1 HIS A 201 9.177 19.955 73.395 1.00 24.92 C ANISOU 1441 CE1 HIS A 201 3730 3832 1906 568 -4 -1 C ATOM 1442 NE2 HIS A 201 10.209 19.138 73.302 1.00 26.27 N ANISOU 1442 NE2 HIS A 201 3608 4202 2169 638 102 233 N ATOM 1443 N TYR A 202 10.537 21.935 67.035 1.00 13.41 N ANISOU 1443 N TYR A 202 1376 2105 1611 92 -453 -460 N ATOM 1444 CA TYR A 202 10.351 21.972 65.582 1.00 12.54 C ANISOU 1444 CA TYR A 202 1344 1858 1562 -19 -310 -448 C ATOM 1445 C TYR A 202 11.492 21.275 64.841 1.00 12.39 C ANISOU 1445 C TYR A 202 1295 1858 1553 -22 -367 -386 C ATOM 1446 O TYR A 202 11.244 20.400 64.006 1.00 12.38 O ANISOU 1446 O TYR A 202 1263 1871 1570 23 -455 -372 O ATOM 1447 CB TYR A 202 10.181 23.427 65.099 1.00 12.82 C ANISOU 1447 CB TYR A 202 1393 1826 1649 120 -267 -529 C ATOM 1448 CG TYR A 202 9.493 23.610 63.758 1.00 12.08 C ANISOU 1448 CG TYR A 202 1328 1559 1703 -26 -319 -359 C ATOM 1449 CD1 TYR A 202 9.903 22.920 62.625 1.00 12.61 C ANISOU 1449 CD1 TYR A 202 1329 1700 1761 142 -332 -354 C ATOM 1450 CD2 TYR A 202 8.467 24.526 63.615 1.00 11.81 C ANISOU 1450 CD2 TYR A 202 1295 1507 1684 -18 -211 -512 C ATOM 1451 CE1 TYR A 202 9.278 23.108 61.403 1.00 11.92 C ANISOU 1451 CE1 TYR A 202 1314 1515 1697 1 -298 -385 C ATOM 1452 CE2 TYR A 202 7.836 24.713 62.402 1.00 11.53 C ANISOU 1452 CE2 TYR A 202 1116 1462 1801 1 -299 -392 C ATOM 1453 CZ TYR A 202 8.245 24.006 61.296 1.00 11.11 C ANISOU 1453 CZ TYR A 202 1247 1354 1619 -124 -286 -296 C ATOM 1454 OH TYR A 202 7.579 24.202 60.103 1.00 11.21 O ANISOU 1454 OH TYR A 202 1243 1409 1606 -101 -289 -295 O ATOM 1455 N ALA A 203 12.734 21.633 65.155 1.00 12.95 N ANISOU 1455 N ALA A 203 1272 1857 1789 -37 -356 -442 N ATOM 1456 CA ALA A 203 13.858 21.074 64.414 1.00 12.79 C ANISOU 1456 CA ALA A 203 1214 1820 1823 0 -359 -321 C ATOM 1457 C ALA A 203 13.881 19.550 64.510 1.00 12.52 C ANISOU 1457 C ALA A 203 1305 1815 1637 0 -596 -241 C ATOM 1458 O ALA A 203 14.073 18.856 63.511 1.00 12.62 O ANISOU 1458 O ALA A 203 1206 1787 1802 37 -467 -279 O ATOM 1459 CB ALA A 203 15.172 21.656 64.912 1.00 14.74 C ANISOU 1459 CB ALA A 203 1327 2078 2195 -36 -545 -477 C ATOM 1460 N ALA A 204 13.732 19.030 65.722 1.00 13.19 N ANISOU 1460 N ALA A 204 1323 2043 1642 -77 -523 -251 N ATOM 1461 CA ALA A 204 13.739 17.586 65.930 1.00 13.91 C ANISOU 1461 CA ALA A 204 1423 2065 1796 60 -643 -185 C ATOM 1462 C ALA A 204 12.581 16.910 65.191 1.00 12.69 C ANISOU 1462 C ALA A 204 1285 2010 1526 90 -484 -184 C ATOM 1463 O ALA A 204 12.743 15.827 64.636 1.00 13.05 O ANISOU 1463 O ALA A 204 1461 1872 1625 168 -560 -89 O ATOM 1464 CB ALA A 204 13.685 17.262 67.415 1.00 15.75 C ANISOU 1464 CB ALA A 204 1824 2347 1811 44 -718 -105 C ATOM 1465 N SER A 205 11.419 17.557 65.168 1.00 12.24 N ANISOU 1465 N SER A 205 1257 1783 1609 -11 -478 -176 N ATOM 1466 CA SER A 205 10.260 16.996 64.489 1.00 11.95 C ANISOU 1466 CA SER A 205 1309 1734 1495 -129 -353 -152 C ATOM 1467 C SER A 205 10.487 16.941 62.974 1.00 11.01 C ANISOU 1467 C SER A 205 1172 1541 1469 63 -416 -80 C ATOM 1468 O SER A 205 10.178 15.932 62.338 1.00 10.79 O ANISOU 1468 O SER A 205 1061 1542 1497 -21 -368 -50 O ATOM 1469 CB SER A 205 9.009 17.774 64.877 1.00 12.47 C ANISOU 1469 CB SER A 205 1299 1857 1579 -102 -397 -140 C ATOM 1470 OG SER A 205 8.806 17.613 66.274 1.00 13.86 O ANISOU 1470 OG SER A 205 1683 2007 1575 -47 -502 -89 O ATOM 1471 N ALA A 206 11.062 18.002 62.402 1.00 10.85 N ANISOU 1471 N ALA A 206 1026 1554 1541 1 -284 -266 N ATOM 1472 CA ALA A 206 11.412 17.979 60.987 1.00 10.83 C ANISOU 1472 CA ALA A 206 1062 1525 1526 40 -272 -108 C ATOM 1473 C ALA A 206 12.386 16.836 60.674 1.00 10.33 C ANISOU 1473 C ALA A 206 995 1448 1482 -8 -211 -22 C ATOM 1474 O ALA A 206 12.217 16.116 59.690 1.00 10.78 O ANISOU 1474 O ALA A 206 1048 1532 1516 17 -245 -35 O ATOM 1475 CB ALA A 206 11.981 19.315 60.552 1.00 11.19 C ANISOU 1475 CB ALA A 206 1127 1573 1548 -37 -199 -115 C ATOM 1476 N ARG A 207 13.412 16.673 61.512 1.00 11.29 N ANISOU 1476 N ARG A 207 964 1716 1610 44 -261 -104 N ATOM 1477 CA ARG A 207 14.377 15.594 61.308 1.00 11.49 C ANISOU 1477 CA ARG A 207 975 1693 1696 29 -268 -20 C ATOM 1478 C ARG A 207 13.752 14.211 61.485 1.00 11.23 C ANISOU 1478 C ARG A 207 1009 1611 1647 65 -382 -68 C ATOM 1479 O ARG A 207 14.093 13.282 60.755 1.00 11.90 O ANISOU 1479 O ARG A 207 1116 1667 1739 64 -212 -46 O ATOM 1480 CB ARG A 207 15.603 15.789 62.201 1.00 12.20 C ANISOU 1480 CB ARG A 207 1084 1813 1738 74 -334 -156 C ATOM 1481 CG ARG A 207 16.405 17.012 61.788 1.00 13.17 C ANISOU 1481 CG ARG A 207 1045 1989 1968 -6 -310 -157 C ATOM 1482 CD ARG A 207 17.701 17.204 62.561 1.00 13.70 C ANISOU 1482 CD ARG A 207 1164 2138 1902 -103 -341 -199 C ATOM 1483 NE ARG A 207 18.442 18.330 61.986 1.00 13.42 N ANISOU 1483 NE ARG A 207 1142 2027 1928 -86 -299 -400 N ATOM 1484 CZ ARG A 207 18.617 19.524 62.548 1.00 13.04 C ANISOU 1484 CZ ARG A 207 950 2129 1876 -39 -239 -461 C ATOM 1485 NH1 ARG A 207 18.194 19.792 63.782 1.00 14.47 N ANISOU 1485 NH1 ARG A 207 1392 2323 1782 132 -352 -502 N ATOM 1486 NH2 ARG A 207 19.243 20.462 61.855 1.00 13.74 N ANISOU 1486 NH2 ARG A 207 1018 2171 2030 -162 -154 -484 N ATOM 1487 N ALA A 208 12.801 14.090 62.409 1.00 11.41 N ANISOU 1487 N ALA A 208 1127 1580 1628 116 -359 30 N ATOM 1488 CA ALA A 208 12.117 12.815 62.629 1.00 11.68 C ANISOU 1488 CA ALA A 208 1132 1664 1639 75 -277 162 C ATOM 1489 C ALA A 208 11.289 12.412 61.409 1.00 10.99 C ANISOU 1489 C ALA A 208 1069 1500 1605 116 -249 97 C ATOM 1490 O ALA A 208 11.242 11.240 61.047 1.00 11.46 O ANISOU 1490 O ALA A 208 1241 1461 1651 121 -347 132 O ATOM 1491 CB ALA A 208 11.252 12.879 63.874 1.00 12.63 C ANISOU 1491 CB ALA A 208 1445 1895 1457 172 -315 190 C ATOM 1492 N PHE A 209 10.631 13.383 60.778 1.00 10.81 N ANISOU 1492 N PHE A 209 1147 1461 1498 97 -322 37 N ATOM 1493 CA PHE A 209 9.950 13.135 59.505 1.00 10.10 C ANISOU 1493 CA PHE A 209 1009 1375 1452 86 -257 60 C ATOM 1494 C PHE A 209 10.917 12.542 58.476 1.00 10.15 C ANISOU 1494 C PHE A 209 944 1377 1536 160 -316 8 C ATOM 1495 O PHE A 209 10.626 11.534 57.834 1.00 10.51 O ANISOU 1495 O PHE A 209 1133 1276 1582 117 -251 43 O ATOM 1496 CB PHE A 209 9.316 14.431 58.984 1.00 10.04 C ANISOU 1496 CB PHE A 209 1112 1306 1397 75 -231 27 C ATOM 1497 CG PHE A 209 8.925 14.380 57.530 1.00 8.98 C ANISOU 1497 CG PHE A 209 883 1170 1359 80 -130 28 C ATOM 1498 CD1 PHE A 209 7.850 13.611 57.112 1.00 9.33 C ANISOU 1498 CD1 PHE A 209 878 1246 1418 31 -87 53 C ATOM 1499 CD2 PHE A 209 9.626 15.105 56.583 1.00 9.72 C ANISOU 1499 CD2 PHE A 209 941 1282 1469 -51 -72 -10 C ATOM 1500 CE1 PHE A 209 7.492 13.565 55.769 1.00 8.85 C ANISOU 1500 CE1 PHE A 209 803 1170 1390 77 -37 -62 C ATOM 1501 CE2 PHE A 209 9.286 15.058 55.241 1.00 9.55 C ANISOU 1501 CE2 PHE A 209 928 1266 1433 19 -22 20 C ATOM 1502 CZ PHE A 209 8.214 14.286 54.832 1.00 8.94 C ANISOU 1502 CZ PHE A 209 864 1183 1348 106 -18 -42 C ATOM 1503 N GLY A 210 12.086 13.157 58.325 1.00 10.59 N ANISOU 1503 N GLY A 210 1032 1358 1634 114 -211 24 N ATOM 1504 CA GLY A 210 13.073 12.638 57.387 1.00 11.25 C ANISOU 1504 CA GLY A 210 1082 1470 1721 86 -82 64 C ATOM 1505 C GLY A 210 13.503 11.219 57.716 1.00 11.40 C ANISOU 1505 C GLY A 210 1040 1462 1827 92 -110 21 C ATOM 1506 O GLY A 210 13.633 10.377 56.828 1.00 12.75 O ANISOU 1506 O GLY A 210 1320 1492 2030 211 -123 -37 O ATOM 1507 N ALA A 211 13.699 10.950 58.999 1.00 12.20 N ANISOU 1507 N ALA A 211 1177 1517 1939 279 -316 86 N ATOM 1508 CA ALA A 211 14.161 9.638 59.436 1.00 13.15 C ANISOU 1508 CA ALA A 211 1365 1590 2038 348 -256 193 C ATOM 1509 C ALA A 211 13.090 8.554 59.275 1.00 12.98 C ANISOU 1509 C ALA A 211 1380 1556 1994 356 -231 126 C ATOM 1510 O ALA A 211 13.413 7.375 59.137 1.00 14.41 O ANISOU 1510 O ALA A 211 1568 1610 2295 494 -188 200 O ATOM 1511 CB ALA A 211 14.640 9.701 60.877 1.00 14.93 C ANISOU 1511 CB ALA A 211 1620 1894 2160 470 -477 227 C ATOM 1512 N ALA A 212 11.821 8.951 59.315 1.00 12.45 N ANISOU 1512 N ALA A 212 1289 1488 1950 253 -322 164 N ATOM 1513 CA ALA A 212 10.713 8.016 59.144 1.00 12.15 C ANISOU 1513 CA ALA A 212 1423 1324 1868 188 -208 221 C ATOM 1514 C ALA A 212 10.588 7.535 57.708 1.00 11.46 C ANISOU 1514 C ALA A 212 1117 1359 1877 186 -72 141 C ATOM 1515 O ALA A 212 10.129 6.420 57.469 1.00 12.91 O ANISOU 1515 O ALA A 212 1555 1313 2035 108 -139 174 O ATOM 1516 CB ALA A 212 9.407 8.652 59.597 1.00 12.92 C ANISOU 1516 CB ALA A 212 1366 1598 1941 134 -199 168 C ATOM 1517 N PHE A 213 10.971 8.391 56.759 1.00 11.28 N ANISOU 1517 N PHE A 213 1082 1347 1855 197 -72 131 N ATOM 1518 CA PHE A 213 10.848 8.104 55.330 1.00 11.59 C ANISOU 1518 CA PHE A 213 1174 1385 1843 268 -22 124 C ATOM 1519 C PHE A 213 12.208 8.296 54.666 1.00 11.99 C ANISOU 1519 C PHE A 213 1138 1380 2035 267 -39 126 C ATOM 1520 O PHE A 213 12.377 9.159 53.810 1.00 12.28 O ANISOU 1520 O PHE A 213 1085 1499 2081 159 68 215 O ATOM 1521 CB PHE A 213 9.787 9.014 54.701 1.00 11.05 C ANISOU 1521 CB PHE A 213 1038 1338 1820 162 -31 134 C ATOM 1522 CG PHE A 213 8.452 8.938 55.397 1.00 10.63 C ANISOU 1522 CG PHE A 213 1062 1299 1678 120 -68 121 C ATOM 1523 CD1 PHE A 213 7.669 7.809 55.281 1.00 11.11 C ANISOU 1523 CD1 PHE A 213 1182 1308 1731 81 -23 59 C ATOM 1524 CD2 PHE A 213 8.000 9.983 56.184 1.00 10.58 C ANISOU 1524 CD2 PHE A 213 1138 1268 1614 83 -72 124 C ATOM 1525 CE1 PHE A 213 6.452 7.720 55.935 1.00 11.30 C ANISOU 1525 CE1 PHE A 213 1166 1350 1774 -68 -39 112 C ATOM 1526 CE2 PHE A 213 6.779 9.905 56.839 1.00 10.61 C ANISOU 1526 CE2 PHE A 213 1092 1332 1605 149 -106 188 C ATOM 1527 CZ PHE A 213 6.002 8.773 56.708 1.00 10.80 C ANISOU 1527 CZ PHE A 213 1084 1455 1564 79 -132 176 C ATOM 1528 N PRO A 214 13.197 7.483 55.066 1.00 13.82 N ANISOU 1528 N PRO A 214 1279 1593 2375 417 -71 178 N ATOM 1529 CA PRO A 214 14.581 7.762 54.680 1.00 16.28 C ANISOU 1529 CA PRO A 214 1305 1996 2884 484 15 295 C ATOM 1530 C PRO A 214 14.882 7.637 53.190 1.00 17.25 C ANISOU 1530 C PRO A 214 1593 1994 2964 658 145 457 C ATOM 1531 O PRO A 214 15.868 8.221 52.735 1.00 21.37 O ANISOU 1531 O PRO A 214 1841 2773 3503 618 788 514 O ATOM 1532 CB PRO A 214 15.380 6.725 55.477 1.00 17.72 C ANISOU 1532 CB PRO A 214 1546 2227 2958 582 -43 398 C ATOM 1533 CG PRO A 214 14.424 5.607 55.698 1.00 17.01 C ANISOU 1533 CG PRO A 214 1681 1982 2798 651 -118 472 C ATOM 1534 CD PRO A 214 13.090 6.264 55.887 1.00 15.03 C ANISOU 1534 CD PRO A 214 1621 1686 2402 519 -104 287 C ATOM 1535 N LYS A 215 14.070 6.880 52.445 1.00 17.01 N ANISOU 1535 N LYS A 215 1991 1922 2547 857 374 153 N ATOM 1536 CA ALYS A 215 14.313 6.641 51.017 0.48 18.32 C ANISOU 1536 CA ALYS A 215 2278 2150 2531 1064 451 167 C ATOM 1537 CA BLYS A 215 14.335 6.660 51.019 0.52 18.34 C ANISOU 1537 CA BLYS A 215 2297 2094 2575 981 430 124 C ATOM 1538 C LYS A 215 13.517 7.585 50.116 1.00 17.22 C ANISOU 1538 C LYS A 215 2247 1879 2416 817 380 63 C ATOM 1539 O LYS A 215 13.667 7.540 48.893 1.00 20.81 O ANISOU 1539 O LYS A 215 3199 2248 2460 910 537 -170 O ATOM 1540 CB ALYS A 215 13.954 5.202 50.631 0.48 13.30 C ANISOU 1540 CB ALYS A 215 2092 1840 1121 1454 66 668 C ATOM 1541 CB BLYS A 215 14.073 5.201 50.624 0.52 24.88 C ANISOU 1541 CB BLYS A 215 3292 2574 3586 267 469 -355 C ATOM 1542 CG ALYS A 215 14.594 4.100 51.482 0.48 19.53 C ANISOU 1542 CG ALYS A 215 3432 1805 2183 1490 -150 847 C ATOM 1543 CG BLYS A 215 14.680 4.133 51.531 0.52 26.33 C ANISOU 1543 CG BLYS A 215 3213 3223 3567 344 376 -218 C ATOM 1544 CD ALYS A 215 16.034 4.399 51.859 0.48 24.51 C ANISOU 1544 CD ALYS A 215 3273 2790 3248 712 226 309 C ATOM 1545 CD BLYS A 215 16.079 4.445 52.061 0.52 26.72 C ANISOU 1545 CD BLYS A 215 3162 3562 3427 431 355 -112 C ATOM 1546 CE ALYS A 215 16.721 3.157 52.407 0.48 25.77 C ANISOU 1546 CE ALYS A 215 3456 2602 3733 537 -14 284 C ATOM 1547 CE BLYS A 215 17.174 4.282 51.017 0.52 24.58 C ANISOU 1547 CE BLYS A 215 2702 3382 3252 938 3 28 C ATOM 1548 NZ ALYS A 215 15.812 2.318 53.240 0.48 26.72 N ANISOU 1548 NZ ALYS A 215 3251 2831 4070 513 -73 461 N ATOM 1549 NZ BLYS A 215 18.403 3.712 51.642 0.52 26.85 N ANISOU 1549 NZ BLYS A 215 2445 3840 3914 522 -267 4 N ATOM 1550 N ALA A 216 12.649 8.414 50.703 1.00 14.18 N ANISOU 1550 N ALA A 216 1706 1532 2150 400 212 -58 N ATOM 1551 CA ALA A 216 11.848 9.345 49.912 1.00 12.52 C ANISOU 1551 CA ALA A 216 1365 1554 1836 71 76 -118 C ATOM 1552 C ALA A 216 12.763 10.405 49.305 1.00 12.61 C ANISOU 1552 C ALA A 216 1188 1674 1928 43 106 -163 C ATOM 1553 O ALA A 216 13.475 11.106 50.016 1.00 16.62 O ANISOU 1553 O ALA A 216 2122 2144 2047 -659 -108 59 O ATOM 1554 CB ALA A 216 10.776 9.999 50.769 1.00 12.71 C ANISOU 1554 CB ALA A 216 1306 1555 1967 130 94 -34 C ATOM 1555 N SER A 217 12.750 10.505 47.982 1.00 12.27 N ANISOU 1555 N SER A 217 1126 1590 1946 1 205 -130 N ATOM 1556 CA SER A 217 13.538 11.507 47.282 1.00 13.20 C ANISOU 1556 CA SER A 217 1134 1727 2152 76 335 -12 C ATOM 1557 C SER A 217 12.736 12.713 46.815 1.00 12.46 C ANISOU 1557 C SER A 217 1098 1572 2062 39 312 -121 C ATOM 1558 O SER A 217 13.330 13.730 46.461 1.00 14.53 O ANISOU 1558 O SER A 217 1200 1855 2464 -41 491 157 O ATOM 1559 CB SER A 217 14.236 10.876 46.084 1.00 15.08 C ANISOU 1559 CB SER A 217 1499 1802 2428 204 516 -75 C ATOM 1560 OG SER A 217 13.301 10.302 45.194 1.00 17.21 O ANISOU 1560 OG SER A 217 1999 2161 2377 140 563 -424 O ATOM 1561 N MET A 218 11.405 12.596 46.798 1.00 11.80 N ANISOU 1561 N MET A 218 1088 1478 1918 63 305 -63 N ATOM 1562 CA MET A 218 10.522 13.702 46.467 1.00 11.14 C ANISOU 1562 CA MET A 218 1320 1310 1601 18 353 -59 C ATOM 1563 C MET A 218 9.722 14.047 47.711 1.00 10.31 C ANISOU 1563 C MET A 218 1087 1236 1591 13 302 -90 C ATOM 1564 O MET A 218 8.919 13.252 48.191 1.00 11.29 O ANISOU 1564 O MET A 218 1360 1279 1651 -146 416 -152 O ATOM 1565 CB MET A 218 9.574 13.347 45.327 1.00 11.55 C ANISOU 1565 CB MET A 218 1208 1614 1565 63 397 -20 C ATOM 1566 CG MET A 218 8.738 14.548 44.918 1.00 13.37 C ANISOU 1566 CG MET A 218 1574 1772 1734 189 342 184 C ATOM 1567 SD MET A 218 7.416 14.223 43.758 1.00 16.24 S ANISOU 1567 SD MET A 218 1690 2269 2212 100 -5 384 S ATOM 1568 CE MET A 218 8.293 13.399 42.435 1.00 20.88 C ANISOU 1568 CE MET A 218 2467 2934 2531 252 -223 -292 C ATOM 1569 N ILE A 219 9.983 15.234 48.233 1.00 9.60 N ANISOU 1569 N ILE A 219 888 1266 1491 14 155 -68 N ATOM 1570 CA ILE A 219 9.300 15.740 49.400 1.00 9.22 C ANISOU 1570 CA ILE A 219 995 1182 1324 8 68 13 C ATOM 1571 C ILE A 219 8.243 16.728 48.935 1.00 8.87 C ANISOU 1571 C ILE A 219 957 1124 1287 -55 71 75 C ATOM 1572 O ILE A 219 8.531 17.718 48.275 1.00 10.06 O ANISOU 1572 O ILE A 219 960 1301 1562 -2 91 333 O ATOM 1573 CB ILE A 219 10.298 16.388 50.383 1.00 9.93 C ANISOU 1573 CB ILE A 219 979 1246 1547 -37 -6 26 C ATOM 1574 CG1 ILE A 219 11.438 15.412 50.733 1.00 10.88 C ANISOU 1574 CG1 ILE A 219 998 1382 1751 17 -98 64 C ATOM 1575 CG2 ILE A 219 9.572 16.852 51.637 1.00 10.14 C ANISOU 1575 CG2 ILE A 219 1188 1251 1412 17 -139 -39 C ATOM 1576 CD1 ILE A 219 11.001 14.054 51.243 1.00 11.13 C ANISOU 1576 CD1 ILE A 219 1047 1317 1865 147 -257 140 C ATOM 1577 N VAL A 220 7.004 16.426 49.288 1.00 8.57 N ANISOU 1577 N VAL A 220 927 1016 1312 52 127 78 N ATOM 1578 CA VAL A 220 5.852 17.238 48.940 1.00 8.28 C ANISOU 1578 CA VAL A 220 960 972 1213 -2 55 124 C ATOM 1579 C VAL A 220 5.444 17.971 50.214 1.00 7.86 C ANISOU 1579 C VAL A 220 791 943 1250 -78 77 177 C ATOM 1580 O VAL A 220 5.523 17.422 51.328 1.00 8.51 O ANISOU 1580 O VAL A 220 1057 996 1179 -24 59 138 O ATOM 1581 CB VAL A 220 4.723 16.354 48.382 1.00 8.79 C ANISOU 1581 CB VAL A 220 1043 1047 1248 -75 35 150 C ATOM 1582 CG1 VAL A 220 3.505 17.182 47.995 1.00 9.48 C ANISOU 1582 CG1 VAL A 220 1082 1168 1351 -125 -64 281 C ATOM 1583 CG2 VAL A 220 5.235 15.578 47.179 1.00 9.99 C ANISOU 1583 CG2 VAL A 220 1410 1187 1199 -101 -1 82 C ATOM 1584 N MET A 221 4.987 19.212 50.066 1.00 7.80 N ANISOU 1584 N MET A 221 830 968 1166 -45 85 198 N ATOM 1585 CA AMET A 221 4.648 19.991 51.241 0.64 8.03 C ANISOU 1585 CA AMET A 221 865 933 1250 -54 -42 98 C ATOM 1586 CA BMET A 221 4.784 20.151 51.170 0.36 8.03 C ANISOU 1586 CA BMET A 221 794 1044 1213 -45 38 162 C ATOM 1587 C MET A 221 3.552 20.999 50.907 1.00 7.89 C ANISOU 1587 C MET A 221 799 971 1228 -63 87 214 C ATOM 1588 O MET A 221 3.186 21.186 49.752 1.00 8.73 O ANISOU 1588 O MET A 221 923 1157 1235 84 128 258 O ATOM 1589 CB AMET A 221 5.901 20.646 51.833 0.64 8.39 C ANISOU 1589 CB AMET A 221 748 1144 1295 -25 28 -9 C ATOM 1590 CB BMET A 221 5.979 21.100 51.247 0.36 9.15 C ANISOU 1590 CB BMET A 221 925 1092 1457 -143 48 162 C ATOM 1591 CG AMET A 221 6.482 21.733 50.941 0.64 9.21 C ANISOU 1591 CG AMET A 221 889 1180 1427 29 141 26 C ATOM 1592 CG BMET A 221 7.280 20.415 51.587 0.36 9.84 C ANISOU 1592 CG BMET A 221 944 1122 1671 -158 9 228 C ATOM 1593 SD AMET A 221 8.286 21.822 50.931 0.64 11.95 S ANISOU 1593 SD AMET A 221 926 1964 1651 -259 -10 -214 S ATOM 1594 SD BMET A 221 8.684 21.446 51.168 0.36 10.08 S ANISOU 1594 SD BMET A 221 855 1269 1703 -188 -10 174 S ATOM 1595 CE AMET A 221 8.662 20.444 49.855 0.64 12.16 C ANISOU 1595 CE AMET A 221 1213 1821 1585 37 71 -12 C ATOM 1596 CE BMET A 221 8.886 21.051 49.436 0.36 10.84 C ANISOU 1596 CE BMET A 221 1024 1339 1753 -68 143 121 C ATOM 1597 N SER A 222 2.979 21.610 51.942 1.00 7.75 N ANISOU 1597 N SER A 222 852 906 1184 -37 -34 180 N ATOM 1598 CA SER A 222 1.781 22.414 51.716 1.00 8.12 C ANISOU 1598 CA SER A 222 864 947 1274 36 -33 142 C ATOM 1599 C SER A 222 2.032 23.707 50.974 1.00 8.29 C ANISOU 1599 C SER A 222 787 951 1411 58 115 146 C ATOM 1600 O SER A 222 1.178 24.124 50.196 1.00 8.99 O ANISOU 1600 O SER A 222 980 1013 1421 23 50 302 O ATOM 1601 CB SER A 222 1.092 22.764 53.032 1.00 8.23 C ANISOU 1601 CB SER A 222 915 918 1291 -34 -26 150 C ATOM 1602 OG SER A 222 0.662 21.588 53.670 1.00 7.95 O ANISOU 1602 OG SER A 222 777 1030 1210 -9 66 231 O ATOM 1603 N HIS A 223 3.145 24.375 51.266 1.00 9.52 N ANISOU 1603 N HIS A 223 937 955 1723 -88 71 269 N ATOM 1604 CA HIS A 223 3.309 25.765 50.834 1.00 10.57 C ANISOU 1604 CA HIS A 223 1065 961 1989 -167 294 281 C ATOM 1605 C HIS A 223 4.570 25.986 50.015 1.00 12.54 C ANISOU 1605 C HIS A 223 1375 1127 2262 -129 612 264 C ATOM 1606 O HIS A 223 5.058 27.108 49.913 1.00 16.32 O ANISOU 1606 O HIS A 223 1949 1232 3017 -352 981 188 O ATOM 1607 CB HIS A 223 3.250 26.706 52.041 1.00 10.58 C ANISOU 1607 CB HIS A 223 1065 1046 1908 -141 231 262 C ATOM 1608 CG HIS A 223 1.996 26.568 52.835 1.00 9.17 C ANISOU 1608 CG HIS A 223 1022 913 1547 -92 95 142 C ATOM 1609 ND1 HIS A 223 0.745 26.745 52.280 1.00 9.51 N ANISOU 1609 ND1 HIS A 223 1071 1048 1493 -30 67 223 N ATOM 1610 CD2 HIS A 223 1.790 26.208 54.119 1.00 9.60 C ANISOU 1610 CD2 HIS A 223 1063 1054 1527 -63 36 248 C ATOM 1611 CE1 HIS A 223 -0.169 26.510 53.205 1.00 9.47 C ANISOU 1611 CE1 HIS A 223 1049 1150 1398 12 0 178 C ATOM 1612 NE2 HIS A 223 0.442 26.178 54.319 1.00 9.32 N ANISOU 1612 NE2 HIS A 223 1054 1157 1327 98 -9 18 N ATOM 1613 N SER A 224 5.077 24.907 49.431 1.00 11.78 N ANISOU 1613 N SER A 224 1015 1143 2315 -155 630 274 N ATOM 1614 CA SER A 224 6.119 24.965 48.429 1.00 12.71 C ANISOU 1614 CA SER A 224 1315 1322 2189 -40 663 185 C ATOM 1615 C SER A 224 5.868 23.863 47.401 1.00 12.06 C ANISOU 1615 C SER A 224 1288 1191 2100 -83 483 317 C ATOM 1616 O SER A 224 5.212 22.879 47.719 1.00 11.00 O ANISOU 1616 O SER A 224 1011 1221 1944 -52 325 360 O ATOM 1617 CB SER A 224 7.509 24.734 49.045 1.00 14.37 C ANISOU 1617 CB SER A 224 1324 1551 2583 -219 434 -114 C ATOM 1618 OG SER A 224 7.850 25.610 50.113 1.00 15.46 O ANISOU 1618 OG SER A 224 1464 1903 2507 -307 493 -152 O ATOM 1619 N ALA A 225 6.434 24.008 46.199 1.00 12.85 N ANISOU 1619 N ALA A 225 1443 1306 2130 -51 522 438 N ATOM 1620 CA ALA A 225 6.405 22.952 45.184 1.00 12.26 C ANISOU 1620 CA ALA A 225 1375 1500 1780 25 329 478 C ATOM 1621 C ALA A 225 7.270 21.780 45.647 1.00 11.13 C ANISOU 1621 C ALA A 225 1166 1453 1608 -37 380 350 C ATOM 1622 O ALA A 225 8.141 21.955 46.495 1.00 11.44 O ANISOU 1622 O ALA A 225 1216 1492 1636 -120 368 300 O ATOM 1623 CB ALA A 225 6.914 23.485 43.856 1.00 14.43 C ANISOU 1623 CB ALA A 225 1814 1715 1954 53 535 585 C ATOM 1624 N PRO A 226 7.072 20.584 45.072 1.00 10.67 N ANISOU 1624 N PRO A 226 1119 1485 1450 5 203 321 N ATOM 1625 CA PRO A 226 7.875 19.438 45.488 1.00 10.23 C ANISOU 1625 CA PRO A 226 983 1528 1373 15 206 238 C ATOM 1626 C PRO A 226 9.366 19.702 45.347 1.00 10.46 C ANISOU 1626 C PRO A 226 983 1527 1462 -10 256 222 C ATOM 1627 O PRO A 226 9.810 20.389 44.419 1.00 12.00 O ANISOU 1627 O PRO A 226 1174 1859 1523 -107 315 347 O ATOM 1628 CB PRO A 226 7.407 18.328 44.546 1.00 11.44 C ANISOU 1628 CB PRO A 226 1260 1530 1556 -32 256 115 C ATOM 1629 CG PRO A 226 5.993 18.689 44.241 1.00 11.41 C ANISOU 1629 CG PRO A 226 1275 1715 1344 -120 116 167 C ATOM 1630 CD PRO A 226 6.002 20.186 44.143 1.00 11.57 C ANISOU 1630 CD PRO A 226 1208 1767 1420 -38 165 276 C ATOM 1631 N ASP A 227 10.145 19.145 46.263 1.00 10.56 N ANISOU 1631 N ASP A 227 1009 1562 1442 -90 210 244 N ATOM 1632 CA ASP A 227 11.574 19.400 46.310 1.00 10.80 C ANISOU 1632 CA ASP A 227 1027 1475 1601 -125 234 104 C ATOM 1633 C ASP A 227 12.304 18.123 46.700 1.00 10.85 C ANISOU 1633 C ASP A 227 959 1543 1617 -64 215 102 C ATOM 1634 O ASP A 227 11.702 17.092 47.006 1.00 11.49 O ANISOU 1634 O ASP A 227 956 1506 1904 -40 165 103 O ATOM 1635 CB ASP A 227 11.840 20.515 47.336 1.00 12.37 C ANISOU 1635 CB ASP A 227 1151 1665 1883 -91 181 -87 C ATOM 1636 CG ASP A 227 13.180 21.243 47.130 1.00 13.97 C ANISOU 1636 CG ASP A 227 1332 1687 2288 -269 90 -64 C ATOM 1637 OD1 ASP A 227 13.928 20.946 46.175 1.00 14.88 O ANISOU 1637 OD1 ASP A 227 1357 1864 2432 -406 275 55 O ATOM 1638 OD2 ASP A 227 13.474 22.135 47.947 1.00 16.53 O ANISOU 1638 OD2 ASP A 227 1513 2097 2671 -369 158 -428 O ATOM 1639 N SER A 228 13.625 18.201 46.672 1.00 11.53 N ANISOU 1639 N SER A 228 942 1744 1694 -84 140 124 N ATOM 1640 CA SER A 228 14.467 17.129 47.168 1.00 11.60 C ANISOU 1640 CA SER A 228 959 1753 1694 -3 100 -107 C ATOM 1641 C SER A 228 14.464 17.122 48.696 1.00 10.93 C ANISOU 1641 C SER A 228 750 1695 1708 35 51 -81 C ATOM 1642 O SER A 228 13.823 17.956 49.351 1.00 11.24 O ANISOU 1642 O SER A 228 924 1624 1722 53 44 -76 O ATOM 1643 CB SER A 228 15.896 17.327 46.672 1.00 12.99 C ANISOU 1643 CB SER A 228 990 1953 1990 -42 166 6 C ATOM 1644 OG SER A 228 16.525 18.344 47.433 1.00 14.01 O ANISOU 1644 OG SER A 228 1109 2084 2131 -75 118 -109 O ATOM 1645 N ARG A 229 15.231 16.194 49.262 1.00 10.93 N ANISOU 1645 N ARG A 229 850 1663 1638 61 127 -57 N ATOM 1646 CA ARG A 229 15.367 16.111 50.710 1.00 10.72 C ANISOU 1646 CA ARG A 229 752 1637 1683 6 84 4 C ATOM 1647 C ARG A 229 16.061 17.323 51.316 1.00 11.08 C ANISOU 1647 C ARG A 229 882 1541 1784 107 129 -119 C ATOM 1648 O ARG A 229 16.015 17.499 52.537 1.00 10.66 O ANISOU 1648 O ARG A 229 756 1580 1712 100 118 21 O ATOM 1649 CB ARG A 229 16.096 14.842 51.130 1.00 11.30 C ANISOU 1649 CB ARG A 229 869 1585 1837 54 107 -10 C ATOM 1650 CG ARG A 229 15.377 13.566 50.752 1.00 11.76 C ANISOU 1650 CG ARG A 229 1016 1606 1845 26 108 -82 C ATOM 1651 CD ARG A 229 16.128 12.347 51.247 1.00 12.66 C ANISOU 1651 CD ARG A 229 1137 1604 2069 94 91 -136 C ATOM 1652 NE ARG A 229 16.088 12.201 52.703 1.00 12.30 N ANISOU 1652 NE ARG A 229 968 1574 2129 114 -47 -38 N ATOM 1653 CZ ARG A 229 15.092 11.644 53.388 1.00 12.04 C ANISOU 1653 CZ ARG A 229 1088 1465 2019 86 -39 -63 C ATOM 1654 NH1 ARG A 229 14.010 11.200 52.766 1.00 12.69 N ANISOU 1654 NH1 ARG A 229 1143 1693 1985 -149 -73 136 N ATOM 1655 NH2 ARG A 229 15.173 11.541 54.711 1.00 13.58 N ANISOU 1655 NH2 ARG A 229 1270 1853 2036 -102 -30 36 N ATOM 1656 N ALA A 230 16.653 18.189 50.497 1.00 11.20 N ANISOU 1656 N ALA A 230 925 1545 1786 32 28 -111 N ATOM 1657 CA ALA A 230 17.165 19.453 51.014 1.00 11.36 C ANISOU 1657 CA ALA A 230 930 1545 1838 6 48 -127 C ATOM 1658 C ALA A 230 16.053 20.297 51.661 1.00 10.99 C ANISOU 1658 C ALA A 230 838 1492 1843 22 -33 -62 C ATOM 1659 O ALA A 230 16.332 21.151 52.490 1.00 11.37 O ANISOU 1659 O ALA A 230 945 1506 1868 -9 -67 -77 O ATOM 1660 CB ALA A 230 17.878 20.244 49.931 1.00 12.70 C ANISOU 1660 CB ALA A 230 1045 1733 2046 -58 203 -88 C ATOM 1661 N ALA A 231 14.795 20.072 51.293 1.00 10.73 N ANISOU 1661 N ALA A 231 854 1477 1743 -25 -15 -103 N ATOM 1662 CA ALA A 231 13.704 20.734 51.999 1.00 10.50 C ANISOU 1662 CA ALA A 231 787 1474 1729 38 -11 5 C ATOM 1663 C ALA A 231 13.738 20.382 53.493 1.00 9.79 C ANISOU 1663 C ALA A 231 675 1364 1679 -46 -70 -133 C ATOM 1664 O ALA A 231 13.502 21.222 54.360 1.00 10.46 O ANISOU 1664 O ALA A 231 861 1379 1732 -16 -93 -176 O ATOM 1665 CB ALA A 231 12.381 20.326 51.385 1.00 10.55 C ANISOU 1665 CB ALA A 231 858 1533 1616 52 -51 -64 C ATOM 1666 N ILE A 232 14.006 19.114 53.792 1.00 9.52 N ANISOU 1666 N ILE A 232 743 1396 1479 -20 18 -82 N ATOM 1667 CA ILE A 232 14.019 18.652 55.176 1.00 9.70 C ANISOU 1667 CA ILE A 232 790 1407 1487 -57 -79 -72 C ATOM 1668 C ILE A 232 15.210 19.246 55.929 1.00 9.83 C ANISOU 1668 C ILE A 232 754 1351 1628 26 -87 -237 C ATOM 1669 O ILE A 232 15.052 19.800 57.025 1.00 10.16 O ANISOU 1669 O ILE A 232 797 1478 1586 -57 -64 -185 O ATOM 1670 CB ILE A 232 14.064 17.111 55.273 1.00 10.15 C ANISOU 1670 CB ILE A 232 910 1408 1536 -68 47 -149 C ATOM 1671 CG1 ILE A 232 12.866 16.490 54.544 1.00 10.55 C ANISOU 1671 CG1 ILE A 232 882 1493 1634 -82 55 -143 C ATOM 1672 CG2 ILE A 232 14.089 16.660 56.728 1.00 12.16 C ANISOU 1672 CG2 ILE A 232 1403 1621 1594 -192 -9 -51 C ATOM 1673 CD1 ILE A 232 13.012 15.002 54.311 1.00 12.29 C ANISOU 1673 CD1 ILE A 232 1455 1401 1811 -223 -240 -13 C ATOM 1674 N THR A 233 16.403 19.132 55.349 1.00 10.17 N ANISOU 1674 N THR A 233 772 1485 1607 -34 -53 -147 N ATOM 1675 CA THR A 233 17.587 19.651 56.013 1.00 10.77 C ANISOU 1675 CA THR A 233 798 1463 1831 -55 -108 -184 C ATOM 1676 C THR A 233 17.501 21.168 56.191 1.00 10.57 C ANISOU 1676 C THR A 233 807 1476 1732 -56 -102 -183 C ATOM 1677 O THR A 233 17.866 21.686 57.248 1.00 11.56 O ANISOU 1677 O THR A 233 968 1587 1836 -74 -155 -306 O ATOM 1678 CB THR A 233 18.877 19.263 55.266 1.00 11.07 C ANISOU 1678 CB THR A 233 780 1607 1816 -13 -115 -141 C ATOM 1679 OG1 THR A 233 18.777 19.626 53.889 1.00 12.11 O ANISOU 1679 OG1 THR A 233 885 1851 1863 58 -24 -39 O ATOM 1680 CG2 THR A 233 19.133 17.770 55.380 1.00 11.96 C ANISOU 1680 CG2 THR A 233 1025 1637 1881 91 -25 -207 C ATOM 1681 N HIS A 234 17.014 21.885 55.181 1.00 10.66 N ANISOU 1681 N HIS A 234 890 1409 1750 -89 -60 -144 N ATOM 1682 CA HIS A 234 16.917 23.333 55.277 1.00 11.44 C ANISOU 1682 CA HIS A 234 799 1456 2092 -120 -183 -192 C ATOM 1683 C HIS A 234 15.873 23.762 56.300 1.00 11.28 C ANISOU 1683 C HIS A 234 882 1343 2058 -32 -181 -218 C ATOM 1684 O HIS A 234 16.094 24.694 57.069 1.00 12.35 O ANISOU 1684 O HIS A 234 1033 1453 2205 -115 -200 -329 O ATOM 1685 CB HIS A 234 16.607 23.935 53.919 1.00 12.55 C ANISOU 1685 CB HIS A 234 1053 1554 2160 -125 -160 -57 C ATOM 1686 CG HIS A 234 16.437 25.421 53.939 1.00 13.10 C ANISOU 1686 CG HIS A 234 1173 1548 2254 -220 -112 -7 C ATOM 1687 ND1 HIS A 234 17.442 26.287 54.313 1.00 15.09 N ANISOU 1687 ND1 HIS A 234 1218 1669 2844 -254 -310 72 N ATOM 1688 CD2 HIS A 234 15.378 26.193 53.615 1.00 14.14 C ANISOU 1688 CD2 HIS A 234 1166 1588 2616 -194 -136 -71 C ATOM 1689 CE1 HIS A 234 17.005 27.529 54.220 1.00 15.74 C ANISOU 1689 CE1 HIS A 234 1303 1666 3009 -221 -212 79 C ATOM 1690 NE2 HIS A 234 15.755 27.499 53.798 1.00 15.16 N ANISOU 1690 NE2 HIS A 234 1291 1568 2899 -183 -132 14 N ATOM 1691 N THR A 235 14.724 23.093 56.300 1.00 10.95 N ANISOU 1691 N THR A 235 800 1443 1918 -17 -158 -244 N ATOM 1692 CA THR A 235 13.698 23.361 57.294 1.00 11.19 C ANISOU 1692 CA THR A 235 954 1395 1901 -9 -139 -298 C ATOM 1693 C THR A 235 14.239 23.169 58.708 1.00 11.05 C ANISOU 1693 C THR A 235 838 1463 1894 -5 -89 -352 C ATOM 1694 O THR A 235 14.049 24.018 59.581 1.00 11.59 O ANISOU 1694 O THR A 235 1008 1523 1872 -17 -223 -413 O ATOM 1695 CB THR A 235 12.452 22.477 57.070 1.00 10.69 C ANISOU 1695 CB THR A 235 831 1416 1813 9 -136 -236 C ATOM 1696 OG1 THR A 235 11.815 22.863 55.850 1.00 11.20 O ANISOU 1696 OG1 THR A 235 878 1444 1932 -11 -250 -208 O ATOM 1697 CG2 THR A 235 11.457 22.623 58.220 1.00 11.19 C ANISOU 1697 CG2 THR A 235 935 1534 1780 -35 -110 -340 C ATOM 1698 N ALA A 236 14.895 22.039 58.936 1.00 11.23 N ANISOU 1698 N ALA A 236 861 1489 1914 -2 -164 -372 N ATOM 1699 CA ALA A 236 15.424 21.738 60.259 1.00 11.65 C ANISOU 1699 CA ALA A 236 901 1638 1886 -27 -121 -378 C ATOM 1700 C ALA A 236 16.486 22.754 60.669 1.00 11.81 C ANISOU 1700 C ALA A 236 881 1749 1855 -47 -173 -386 C ATOM 1701 O ALA A 236 16.533 23.171 61.820 1.00 12.80 O ANISOU 1701 O ALA A 236 1108 1896 1857 -196 -171 -430 O ATOM 1702 CB ALA A 236 15.992 20.332 60.300 1.00 11.71 C ANISOU 1702 CB ALA A 236 980 1645 1822 -46 -138 -283 C ATOM 1703 N ARG A 237 17.327 23.163 59.723 1.00 12.39 N ANISOU 1703 N ARG A 237 812 1743 2152 -69 -137 -206 N ATOM 1704 CA ARG A 237 18.388 24.110 60.025 1.00 13.04 C ANISOU 1704 CA ARG A 237 1040 1942 1970 -271 -192 -247 C ATOM 1705 C ARG A 237 17.796 25.469 60.389 1.00 13.88 C ANISOU 1705 C ARG A 237 1227 1818 2226 -417 -272 -312 C ATOM 1706 O ARG A 237 18.278 26.121 61.306 1.00 15.86 O ANISOU 1706 O ARG A 237 1504 2093 2428 -412 -281 -617 O ATOM 1707 CB ARG A 237 19.379 24.220 58.860 1.00 13.72 C ANISOU 1707 CB ARG A 237 1189 1948 2074 -221 -87 -227 C ATOM 1708 CG ARG A 237 20.705 24.860 59.234 1.00 13.08 C ANISOU 1708 CG ARG A 237 1117 1784 2066 -48 -140 -316 C ATOM 1709 CD ARG A 237 21.553 23.920 60.068 1.00 14.62 C ANISOU 1709 CD ARG A 237 1224 2043 2286 53 -105 -46 C ATOM 1710 NE ARG A 237 22.818 24.543 60.449 1.00 14.35 N ANISOU 1710 NE ARG A 237 1437 1661 2353 -26 -226 -149 N ATOM 1711 CZ ARG A 237 23.229 24.780 61.697 1.00 15.90 C ANISOU 1711 CZ ARG A 237 1731 1863 2444 -310 -361 -221 C ATOM 1712 NH1 ARG A 237 22.485 24.443 62.751 1.00 19.12 N ANISOU 1712 NH1 ARG A 237 2146 2556 2559 -714 -198 -279 N ATOM 1713 NH2 ARG A 237 24.410 25.356 61.899 1.00 17.96 N ANISOU 1713 NH2 ARG A 237 1689 2224 2908 -466 -326 104 N ATOM 1714 N MET A 238 16.741 25.886 59.690 1.00 14.41 N ANISOU 1714 N MET A 238 1389 1712 2374 -264 -356 -435 N ATOM 1715 CA MET A 238 16.045 27.121 60.046 1.00 15.18 C ANISOU 1715 CA MET A 238 1771 1614 2380 -309 -297 -529 C ATOM 1716 C MET A 238 15.400 26.992 61.420 1.00 15.12 C ANISOU 1716 C MET A 238 1714 1708 2323 -244 -388 -502 C ATOM 1717 O MET A 238 15.416 27.936 62.206 1.00 17.54 O ANISOU 1717 O MET A 238 2181 1760 2723 -187 -476 -717 O ATOM 1718 CB MET A 238 14.991 27.504 59.001 1.00 15.94 C ANISOU 1718 CB MET A 238 1916 1680 2458 -12 -182 -353 C ATOM 1719 CG MET A 238 15.581 28.063 57.716 1.00 18.01 C ANISOU 1719 CG MET A 238 2419 1823 2598 34 -93 -127 C ATOM 1720 SD MET A 238 14.391 28.982 56.726 1.00 22.25 S ANISOU 1720 SD MET A 238 3269 2110 3074 568 -273 -60 S ATOM 1721 CE MET A 238 13.269 27.654 56.303 1.00 21.07 C ANISOU 1721 CE MET A 238 2471 2329 3203 568 215 18 C ATOM 1722 N ALA A 239 14.828 25.827 61.708 1.00 15.20 N ANISOU 1722 N ALA A 239 1604 1793 2375 -307 -229 -587 N ATOM 1723 CA ALA A 239 14.176 25.595 62.995 1.00 15.53 C ANISOU 1723 CA ALA A 239 1665 1964 2271 -208 -295 -705 C ATOM 1724 C ALA A 239 15.176 25.554 64.153 1.00 16.27 C ANISOU 1724 C ALA A 239 1735 2188 2258 -166 -295 -834 C ATOM 1725 O ALA A 239 14.807 25.844 65.284 1.00 17.93 O ANISOU 1725 O ALA A 239 1897 2588 2327 -148 -297 -1072 O ATOM 1726 CB ALA A 239 13.371 24.309 62.951 1.00 14.49 C ANISOU 1726 CB ALA A 239 1518 2018 1968 -204 -228 -654 C ATOM 1727 N ASP A 240 16.428 25.193 63.875 1.00 16.47 N ANISOU 1727 N ASP A 240 1656 2481 2119 -354 -269 -915 N ATOM 1728 CA ASP A 240 17.484 25.235 64.890 1.00 18.08 C ANISOU 1728 CA ASP A 240 1799 2774 2293 -377 -401 -1008 C ATOM 1729 C ASP A 240 17.571 26.631 65.511 1.00 20.13 C ANISOU 1729 C ASP A 240 2162 2899 2587 -516 -219 -1157 C ATOM 1730 O ASP A 240 17.874 26.766 66.690 1.00 23.46 O ANISOU 1730 O ASP A 240 2527 3579 2805 -529 -502 -1480 O ATOM 1731 CB ASP A 240 18.853 24.875 64.290 1.00 17.79 C ANISOU 1731 CB ASP A 240 1678 2718 2362 -467 -460 -972 C ATOM 1732 CG ASP A 240 19.027 23.387 64.021 1.00 16.48 C ANISOU 1732 CG ASP A 240 1334 2691 2235 -342 -392 -761 C ATOM 1733 OD1 ASP A 240 18.339 22.560 64.655 1.00 16.44 O ANISOU 1733 OD1 ASP A 240 1516 2636 2091 -222 -375 -667 O ATOM 1734 OD2 ASP A 240 19.880 23.044 63.170 1.00 16.32 O ANISOU 1734 OD2 ASP A 240 1416 2531 2254 -181 -415 -712 O ATOM 1735 N LYS A 241 17.287 27.658 64.710 1.00 21.09 N ANISOU 1735 N LYS A 241 2305 2721 2985 -643 -225 -1144 N ATOM 1736 CA LYS A 241 17.414 29.055 65.139 1.00 22.36 C ANISOU 1736 CA LYS A 241 2686 2838 2969 -625 -184 -1264 C ATOM 1737 C LYS A 241 16.300 29.513 66.076 1.00 23.66 C ANISOU 1737 C LYS A 241 2769 3006 3213 -381 -155 -1366 C ATOM 1738 O LYS A 241 16.441 30.525 66.755 1.00 27.09 O ANISOU 1738 O LYS A 241 3567 3156 3568 -283 205 -1656 O ATOM 1739 CB LYS A 241 17.440 29.972 63.920 1.00 23.46 C ANISOU 1739 CB LYS A 241 2824 2711 3379 -818 -188 -1060 C ATOM 1740 CG LYS A 241 18.524 29.606 62.927 1.00 25.79 C ANISOU 1740 CG LYS A 241 3126 3043 3629 -542 144 -565 C ATOM 1741 CD LYS A 241 18.755 30.717 61.928 1.00 29.54 C ANISOU 1741 CD LYS A 241 3670 3589 3965 -485 159 -89 C ATOM 1742 CE LYS A 241 19.565 30.214 60.750 1.00 30.95 C ANISOU 1742 CE LYS A 241 3193 4099 4465 -139 286 -66 C ATOM 1743 NZ LYS A 241 20.896 29.696 61.175 1.00 32.70 N ANISOU 1743 NZ LYS A 241 2920 4577 4926 -836 -265 86 N ATOM 1744 N LEU A 242 15.194 28.774 66.104 1.00 22.96 N ANISOU 1744 N LEU A 242 2686 2970 3065 -305 -23 -1468 N ATOM 1745 CA LEU A 242 14.076 29.085 66.997 1.00 25.10 C ANISOU 1745 CA LEU A 242 2787 3537 3210 -142 57 -1452 C ATOM 1746 C LEU A 242 14.401 28.769 68.450 1.00 27.16 C ANISOU 1746 C LEU A 242 3242 3774 3301 188 131 -1152 C ATOM 1747 O LEU A 242 13.698 29.212 69.357 1.00 30.69 O ANISOU 1747 O LEU A 242 3654 4575 3432 332 75 -1754 O ATOM 1748 CB LEU A 242 12.832 28.292 66.597 1.00 24.39 C ANISOU 1748 CB LEU A 242 2698 3353 3215 -87 138 -1444 C ATOM 1749 CG LEU A 242 12.280 28.518 65.191 1.00 24.33 C ANISOU 1749 CG LEU A 242 2797 3356 3092 -115 291 -1466 C ATOM 1750 CD1 LEU A 242 11.161 27.528 64.917 1.00 24.21 C ANISOU 1750 CD1 LEU A 242 2721 3313 3162 -75 277 -1405 C ATOM 1751 CD2 LEU A 242 11.791 29.950 65.028 1.00 28.43 C ANISOU 1751 CD2 LEU A 242 3266 3437 4100 -23 -8 -1127 C ATOM 1752 N ARG A 243 15.457 27.991 68.663 1.00 26.83 N ANISOU 1752 N ARG A 243 3455 3686 3051 61 -592 -1233 N ATOM 1753 CA ARG A 243 15.880 27.608 70.001 1.00 30.09 C ANISOU 1753 CA ARG A 243 4044 4001 3387 -190 -575 -423 C ATOM 1754 C ARG A 243 16.944 28.562 70.531 1.00 31.49 C ANISOU 1754 C ARG A 243 4443 4198 3323 -357 -730 -616 C ATOM 1755 O ARG A 243 17.092 28.723 71.740 1.00 35.19 O ANISOU 1755 O ARG A 243 5399 4695 3274 -568 -726 -270 O ATOM 1756 CB ARG A 243 16.413 26.179 69.976 1.00 31.55 C ANISOU 1756 CB ARG A 243 4182 3895 3909 -309 -566 -542 C ATOM 1757 CG ARG A 243 15.350 25.153 69.620 1.00 32.71 C ANISOU 1757 CG ARG A 243 3951 4127 4350 -443 -501 -279 C ATOM 1758 CD ARG A 243 15.967 23.870 69.093 1.00 32.27 C ANISOU 1758 CD ARG A 243 3645 4329 4287 -527 -379 -444 C ATOM 1759 NE ARG A 243 16.861 23.251 70.071 1.00 35.95 N ANISOU 1759 NE ARG A 243 4505 4819 4333 17 -203 -52 N ATOM 1760 CZ ARG A 243 16.463 22.552 71.133 1.00 35.96 C ANISOU 1760 CZ ARG A 243 3779 5200 4683 -274 -119 90 C ATOM 1761 NH1 ARG A 243 17.363 22.031 71.958 1.00 37.83 N ANISOU 1761 NH1 ARG A 243 4462 5544 4366 184 -193 7 N ATOM 1762 NH2 ARG A 243 15.173 22.365 71.383 1.00 37.22 N ANISOU 1762 NH2 ARG A 243 3563 5405 5173 -458 -588 -34 N TER 1763 ARG A 243 HETATM 1764 ZN ZN A 301 -1.016 24.943 59.633 1.00 8.93 ZN ANISOU 1764 ZN ZN A 301 1174 982 1236 -206 -84 -26 ZN HETATM 1765 ZN ZN A 302 -0.580 25.295 55.924 1.00 8.98 ZN ANISOU 1765 ZN ZN A 302 998 1082 1330 -28 -67 14 ZN HETATM 1766 O1 X8Z A 303 -0.201 29.652 58.568 1.00 22.61 O ANISOU 1766 O1 X8Z A 303 3432 1661 3495 -624 -583 340 O HETATM 1767 C4 X8Z A 303 -0.524 29.457 57.402 1.00 21.53 C ANISOU 1767 C4 X8Z A 303 3531 1331 3316 -463 -234 422 C HETATM 1768 C2 X8Z A 303 -1.849 28.805 57.114 1.00 17.35 C ANISOU 1768 C2 X8Z A 303 3045 1277 2268 66 -48 520 C HETATM 1769 C1 X8Z A 303 -2.043 27.589 58.000 1.00 12.27 C ANISOU 1769 C1 X8Z A 303 1926 927 1809 -11 -6 66 C HETATM 1770 S X8Z A 303 -0.623 26.467 57.932 1.00 10.32 S ANISOU 1770 S X8Z A 303 1497 1037 1384 -197 33 5 S HETATM 1771 C3 X8Z A 303 -2.981 29.787 57.363 1.00 21.32 C ANISOU 1771 C3 X8Z A 303 3432 1471 3197 391 -152 428 C HETATM 1772 N X8Z A 303 0.269 29.811 56.381 1.00 27.11 N ANISOU 1772 N X8Z A 303 4091 2161 4047 -1170 39 794 N HETATM 1773 C8 X8Z A 303 1.602 30.356 56.648 1.00 32.64 C ANISOU 1773 C8 X8Z A 303 4415 3231 4756 -1675 -67 483 C HETATM 1774 C9 X8Z A 303 1.536 31.805 57.052 1.00 35.19 C ANISOU 1774 C9 X8Z A 303 4813 3496 5059 -956 -479 164 C HETATM 1775 O3 X8Z A 303 0.490 32.460 56.837 1.00 32.96 O ANISOU 1775 O3 X8Z A 303 4937 2261 5325 -1265 -902 -133 O HETATM 1776 O2 X8Z A 303 2.538 32.312 57.599 1.00 38.17 O ANISOU 1776 O2 X8Z A 303 4985 4139 5377 -1384 -720 534 O HETATM 1777 C5 X8Z A 303 -0.010 29.735 54.948 1.00 28.31 C ANISOU 1777 C5 X8Z A 303 4766 2044 3945 -949 347 762 C HETATM 1778 C6 X8Z A 303 1.301 30.078 54.253 1.00 31.82 C ANISOU 1778 C6 X8Z A 303 4744 2800 4542 -1264 440 367 C HETATM 1779 C7 X8Z A 303 2.356 30.164 55.338 1.00 34.45 C ANISOU 1779 C7 X8Z A 303 4591 3334 5163 -1256 169 259 C HETATM 1780 O HOH A 401 8.137 28.244 49.593 1.00 22.86 O HETATM 1781 O HOH A 402 21.758 28.434 59.172 1.00 33.21 O HETATM 1782 O HOH A 403 -0.445 25.940 41.143 1.00 35.66 O HETATM 1783 O HOH A 404 -18.017 17.231 43.727 1.00 20.25 O HETATM 1784 O HOH A 405 -1.551 29.606 61.047 1.00 33.55 O HETATM 1785 O HOH A 406 0.824 33.920 46.878 1.00 19.31 O HETATM 1786 O HOH A 407 4.953 29.922 50.775 1.00 35.24 O HETATM 1787 O HOH A 408 10.818 29.165 48.618 1.00 31.02 O HETATM 1788 O HOH A 409 -5.059 28.955 65.578 1.00 13.41 O HETATM 1789 O HOH A 410 -2.832 -1.849 47.759 1.00 26.95 O HETATM 1790 O HOH A 411 -17.948 23.620 56.441 1.00 16.19 O HETATM 1791 O HOH A 412 -12.662 3.669 60.300 1.00 17.23 O HETATM 1792 O HOH A 413 19.825 21.941 53.147 1.00 17.50 O HETATM 1793 O HOH A 414 -12.922 10.440 66.267 1.00 25.86 O HETATM 1794 O HOH A 415 -9.634 5.763 63.387 1.00 14.26 O HETATM 1795 O HOH A 416 -10.507 35.309 52.286 1.00 21.21 O HETATM 1796 O HOH A 417 16.655 20.690 46.203 1.00 24.45 O HETATM 1797 O HOH A 418 -7.280 28.412 33.291 1.00 24.14 O HETATM 1798 O HOH A 419 -10.762 28.980 44.742 1.00 16.53 O HETATM 1799 O HOH A 420 2.325 23.889 69.724 1.00 32.39 O HETATM 1800 O HOH A 421 -15.546 6.186 52.428 1.00 18.45 O HETATM 1801 O HOH A 422 -16.467 6.641 49.785 1.00 19.18 O HETATM 1802 O HOH A 423 -14.325 25.068 58.626 1.00 14.51 O HETATM 1803 O HOH A 424 -18.192 14.875 40.976 1.00 30.65 O HETATM 1804 O HOH A 425 -10.905 3.131 56.090 1.00 12.41 O HETATM 1805 O HOH A 426 -20.253 23.540 55.046 1.00 21.17 O HETATM 1806 O HOH A 427 19.830 25.787 55.443 1.00 16.44 O HETATM 1807 O HOH A 428 -0.518 24.105 31.971 1.00 21.83 O HETATM 1808 O HOH A 429 -19.764 17.225 58.540 1.00 12.38 O HETATM 1809 O HOH A 430 -0.532 20.976 42.055 1.00 10.62 O HETATM 1810 O HOH A 431 0.075 2.188 38.022 1.00 19.28 O HETATM 1811 O HOH A 432 10.297 13.942 67.437 1.00 21.06 O HETATM 1812 O HOH A 433 4.484 25.445 56.023 1.00 15.84 O HETATM 1813 O HOH A 434 18.555 21.924 67.282 1.00 25.07 O HETATM 1814 O HOH A 435 -4.319 21.747 51.069 1.00 7.95 O HETATM 1815 O HOH A 436 -14.138 17.503 68.240 1.00 17.17 O HETATM 1816 O HOH A 437 -2.769 12.024 69.236 1.00 24.11 O HETATM 1817 O HOH A 438 -17.505 15.654 62.144 1.00 19.02 O HETATM 1818 O HOH A 439 -14.118 28.643 47.759 1.00 13.42 O HETATM 1819 O HOH A 440 3.309 20.896 71.679 1.00 34.50 O HETATM 1820 O HOH A 441 8.726 20.881 41.965 1.00 23.64 O HETATM 1821 O HOH A 442 10.318 10.978 41.059 1.00 40.95 O HETATM 1822 O HOH A 443 -11.746 22.526 70.002 1.00 12.18 O HETATM 1823 O HOH A 444 2.513 18.094 58.785 1.00 8.83 O HETATM 1824 O HOH A 445 -13.598 0.325 42.082 1.00 21.62 O HETATM 1825 O HOH A 446 -12.297 0.770 56.743 1.00 15.68 O HETATM 1826 O HOH A 447 -5.334 37.939 47.113 1.00 20.01 O HETATM 1827 O HOH A 448 -10.197 30.669 38.181 1.00 13.48 O HETATM 1828 O HOH A 449 -0.371 29.138 63.566 1.00 37.71 O HETATM 1829 O HOH A 450 14.645 14.068 65.521 1.00 15.65 O HETATM 1830 O HOH A 451 -4.277 15.140 61.697 1.00 7.44 O HETATM 1831 O HOH A 452 -10.634 23.958 73.840 1.00 24.14 O HETATM 1832 O HOH A 453 16.452 30.668 54.588 1.00 32.58 O HETATM 1833 O HOH A 454 -14.534 9.621 41.339 1.00 15.35 O HETATM 1834 O HOH A 455 -1.338 1.580 55.331 1.00 23.31 O HETATM 1835 O HOH A 456 -5.231 22.173 48.332 1.00 7.86 O HETATM 1836 O HOH A 457 16.436 13.224 59.311 1.00 27.84 O HETATM 1837 O HOH A 458 -9.352 -1.338 62.413 1.00 11.50 O HETATM 1838 O HOH A 459 5.624 26.240 60.133 1.00 13.46 O HETATM 1839 O HOH A 460 -16.749 6.943 58.130 1.00 24.58 O HETATM 1840 O HOH A 461 17.383 0.061 53.047 1.00 45.81 O HETATM 1841 O HOH A 462 -14.110 13.027 65.625 1.00 24.00 O HETATM 1842 O HOH A 463 -13.594 5.431 64.593 1.00 23.18 O HETATM 1843 O HOH A 464 1.990 2.129 61.476 1.00 25.04 O HETATM 1844 O HOH A 465 3.836 3.253 72.077 1.00 26.12 O HETATM 1845 O HOH A 466 10.071 16.564 68.505 1.00 23.39 O HETATM 1846 O HOH A 467 0.349 19.498 57.787 1.00 8.14 O HETATM 1847 O HOH A 468 -6.350 4.105 69.861 1.00 18.32 O HETATM 1848 O HOH A 469 18.419 9.099 52.097 1.00 38.57 O HETATM 1849 O HOH A 470 -7.702 -1.342 45.155 1.00 13.03 O HETATM 1850 O HOH A 471 10.226 23.663 45.764 1.00 19.45 O HETATM 1851 O HOH A 472 -0.641 4.336 57.848 1.00 15.47 O HETATM 1852 O HOH A 473 -6.608 27.880 59.989 1.00 11.98 O HETATM 1853 O HOH A 474 19.090 17.380 47.913 1.00 19.94 O HETATM 1854 O HOH A 475 1.123 28.853 43.170 1.00 22.69 O HETATM 1855 O HOH A 476 21.819 21.262 64.070 1.00 20.36 O HETATM 1856 O HOH A 477 -10.295 31.381 47.158 1.00 14.11 O HETATM 1857 O HOH A 478 -8.299 27.505 44.617 1.00 11.49 O HETATM 1858 O HOH A 479 4.765 23.953 53.670 1.00 12.54 O HETATM 1859 O HOH A 480 -23.495 12.357 48.206 1.00 25.14 O HETATM 1860 O HOH A 481 2.016 28.780 49.740 1.00 18.53 O HETATM 1861 O HOH A 482 -15.070 11.876 42.857 1.00 15.52 O HETATM 1862 O HOH A 483 24.418 25.375 58.313 1.00 22.09 O HETATM 1863 O HOH A 484 -13.982 22.319 58.352 1.00 10.04 O HETATM 1864 O HOH A 485 12.061 27.937 71.459 1.00 31.53 O HETATM 1865 O HOH A 486 -10.660 37.931 51.356 1.00 28.33 O HETATM 1866 O HOH A 487 4.957 20.119 47.324 1.00 9.00 O HETATM 1867 O HOH A 488 1.798 3.190 45.280 1.00 26.47 O HETATM 1868 O HOH A 489 8.815 32.691 60.550 1.00 34.15 O HETATM 1869 O HOH A 490 13.347 23.922 66.803 1.00 17.33 O HETATM 1870 O HOH A 491 -10.309 13.723 69.658 1.00 22.16 O HETATM 1871 O HOH A 492 16.128 6.657 59.265 1.00 23.51 O HETATM 1872 O HOH A 493 -9.675 6.247 67.472 1.00 19.01 O HETATM 1873 O HOH A 494 5.078 33.692 63.696 1.00 34.98 O HETATM 1874 O HOH A 495 -0.968 3.437 45.242 1.00 14.92 O HETATM 1875 O HOH A 496 -7.631 24.674 32.047 1.00 25.69 O HETATM 1876 O HOH A 497 -17.593 23.537 44.009 1.00 19.91 O HETATM 1877 O HOH A 498 -0.490 15.005 68.306 1.00 18.87 O HETATM 1878 O HOH A 499 -5.338 16.054 74.486 1.00 28.30 O HETATM 1879 O HOH A 500 -0.104 28.073 31.057 1.00 26.99 O HETATM 1880 O HOH A 501 18.102 13.239 54.390 1.00 18.00 O HETATM 1881 O HOH A 502 9.252 4.366 55.738 1.00 26.05 O HETATM 1882 O HOH A 503 -15.902 10.535 34.535 1.00 30.26 O HETATM 1883 O HOH A 504 1.979 27.657 63.524 1.00 22.47 O HETATM 1884 O HOH A 505 15.993 14.140 47.338 1.00 15.80 O HETATM 1885 O HOH A 506 19.675 20.317 58.947 1.00 12.38 O HETATM 1886 O HOH A 507 -0.646 23.567 67.920 1.00 18.42 O HETATM 1887 O HOH A 508 11.789 9.236 62.982 1.00 18.33 O HETATM 1888 O HOH A 509 -3.630 22.806 64.343 1.00 13.19 O HETATM 1889 O HOH A 510 -18.470 17.387 47.944 1.00 14.98 O HETATM 1890 O HOH A 511 -18.040 8.389 48.207 1.00 20.24 O HETATM 1891 O HOH A 512 -8.928 21.296 72.846 1.00 20.73 O HETATM 1892 O HOH A 513 -6.459 27.256 38.155 1.00 13.51 O HETATM 1893 O HOH A 514 14.106 20.508 68.288 1.00 17.44 O HETATM 1894 O HOH A 515 3.487 9.788 69.354 1.00 26.47 O HETATM 1895 O HOH A 516 17.435 18.093 65.947 1.00 18.89 O HETATM 1896 O HOH A 517 -9.901 33.851 48.212 1.00 16.22 O HETATM 1897 O HOH A 518 -20.007 11.174 46.275 1.00 19.51 O HETATM 1898 O HOH A 519 -1.742 9.375 69.805 1.00 16.43 O HETATM 1899 O HOH A 520 7.552 6.781 50.100 1.00 20.80 O HETATM 1900 O HOH A 521 -2.965 13.848 35.383 1.00 24.52 O HETATM 1901 O HOH A 522 3.463 16.406 35.727 1.00 32.28 O HETATM 1902 O HOH A 523 -16.886 21.739 64.543 1.00 15.96 O HETATM 1903 O HOH A 524 0.036 34.483 64.484 1.00 49.49 O HETATM 1904 O HOH A 525 2.507 28.279 70.067 1.00 34.96 O HETATM 1905 O HOH A 526 -7.855 10.057 32.650 1.00 27.82 O HETATM 1906 O HOH A 527 -18.804 10.528 55.002 1.00 18.71 O HETATM 1907 O HOH A 528 7.624 9.975 40.995 1.00 27.91 O HETATM 1908 O HOH A 529 -11.670 31.676 55.958 1.00 36.41 O HETATM 1909 O HOH A 530 1.450 22.374 40.654 1.00 17.64 O HETATM 1910 O HOH A 531 5.332 30.808 68.742 1.00 36.25 O HETATM 1911 O HOH A 532 -2.553 2.208 58.317 1.00 21.45 O HETATM 1912 O HOH A 533 -11.493 37.518 48.083 1.00 37.21 O HETATM 1913 O HOH A 534 -3.191 -0.677 66.223 1.00 16.55 O HETATM 1914 O HOH A 535 -12.992 26.226 41.001 1.00 18.48 O HETATM 1915 O HOH A 536 1.894 24.594 44.404 1.00 29.76 O HETATM 1916 O HOH A 537 -3.169 16.488 36.218 1.00 24.68 O HETATM 1917 O HOH A 538 1.587 1.744 71.154 1.00 36.87 O HETATM 1918 O HOH A 539 -8.523 20.984 33.120 1.00 36.75 O HETATM 1919 O HOH A 540 1.088 31.126 47.393 1.00 18.84 O HETATM 1920 O HOH A 541 -20.164 24.812 52.327 1.00 46.22 O HETATM 1921 O HOH A 542 -16.325 8.014 39.828 1.00 28.25 O HETATM 1922 O HOH A 543 -15.921 21.959 56.375 1.00 10.39 O HETATM 1923 O HOH A 544 7.637 11.036 66.966 1.00 30.60 O HETATM 1924 O HOH A 545 18.771 17.720 59.157 1.00 18.77 O HETATM 1925 O HOH A 546 13.390 15.218 43.957 1.00 36.17 O HETATM 1926 O HOH A 547 12.365 12.048 43.057 1.00 34.40 O HETATM 1927 O HOH A 548 7.544 7.657 42.761 1.00 24.36 O HETATM 1928 O HOH A 549 7.849 26.536 45.845 1.00 23.47 O HETATM 1929 O HOH A 550 -15.526 25.866 53.739 1.00 25.95 O HETATM 1930 O HOH A 551 -20.141 6.139 51.033 1.00 32.12 O HETATM 1931 O HOH A 552 -10.564 1.773 64.457 1.00 35.88 O HETATM 1932 O HOH A 553 11.652 5.362 47.669 1.00 42.25 O HETATM 1933 O HOH A 554 -2.602 31.277 66.599 1.00 40.24 O HETATM 1934 O HOH A 555 -16.271 8.833 45.928 1.00 16.09 O HETATM 1935 O HOH A 556 -2.355 20.989 71.616 1.00 32.03 O HETATM 1936 O HOH A 557 -17.103 26.758 50.332 1.00 14.24 O HETATM 1937 O HOH A 558 3.739 22.579 42.454 1.00 23.59 O HETATM 1938 O HOH A 559 -21.299 11.609 55.857 1.00 33.18 O HETATM 1939 O HOH A 560 8.534 25.592 72.491 1.00 35.10 O HETATM 1940 O HOH A 561 2.333 1.706 65.586 1.00 18.80 O HETATM 1941 O HOH A 562 -16.195 25.847 64.687 1.00 25.83 O HETATM 1942 O HOH A 563 1.266 35.223 49.352 1.00 25.20 O HETATM 1943 O HOH A 564 -12.060 7.273 66.153 1.00 18.52 O HETATM 1944 O HOH A 565 -0.392 16.909 35.539 1.00 17.74 O HETATM 1945 O HOH A 566 10.851 3.862 61.526 1.00 34.86 O HETATM 1946 O HOH A 567 10.624 6.346 65.057 1.00 41.54 O HETATM 1947 O HOH A 568 -8.002 31.973 56.693 1.00 27.49 O HETATM 1948 O HOH A 569 -12.811 30.669 53.518 1.00 23.43 O HETATM 1949 O HOH A 570 -16.853 18.932 64.455 1.00 12.77 O HETATM 1950 O HOH A 571 -1.819 5.463 72.090 1.00 41.26 O HETATM 1951 O HOH A 572 6.653 3.104 70.140 1.00 24.60 O HETATM 1952 O HOH A 573 2.708 5.901 41.654 1.00 17.93 O HETATM 1953 O HOH A 574 -5.277 12.462 34.449 1.00 44.91 O HETATM 1954 O HOH A 575 18.947 24.131 51.371 1.00 23.29 O HETATM 1955 O HOH A 576 -18.295 26.613 53.016 1.00 33.92 O HETATM 1956 O HOH A 577 2.999 23.551 34.058 1.00 33.91 O HETATM 1957 O HOH A 578 -16.169 3.932 38.637 1.00 37.78 O HETATM 1958 O HOH A 579 -20.198 12.840 59.137 1.00 27.30 O HETATM 1959 O HOH A 580 7.819 23.207 73.925 1.00 36.61 O HETATM 1960 O HOH A 581 7.573 13.738 38.883 1.00 38.09 O HETATM 1961 O HOH A 582 -4.176 -0.109 56.261 1.00 23.08 O HETATM 1962 O HOH A 583 -11.009 24.917 34.099 1.00 28.10 O HETATM 1963 O HOH A 584 -11.637 0.732 50.132 1.00 23.08 O HETATM 1964 O HOH A 585 3.504 28.137 47.534 1.00 24.78 O HETATM 1965 O HOH A 586 11.610 4.064 58.656 1.00 40.36 O HETATM 1966 O HOH A 587 6.430 27.107 71.275 1.00 25.56 O HETATM 1967 O HOH A 588 -4.872 -1.434 53.497 1.00 15.57 O HETATM 1968 O HOH A 589 10.317 6.501 50.135 1.00 33.11 O HETATM 1969 O HOH A 590 11.257 5.766 52.983 1.00 19.13 O HETATM 1970 O HOH A 591 6.438 5.543 52.539 1.00 24.61 O HETATM 1971 O HOH A 592 8.180 2.298 49.119 1.00 45.05 O HETATM 1972 O HOH A 593 15.100 30.596 60.638 1.00 31.52 O HETATM 1973 O HOH A 594 3.298 25.487 46.486 1.00 21.51 O HETATM 1974 O HOH A 595 9.552 31.470 52.988 1.00 35.02 O HETATM 1975 O HOH A 596 -7.113 16.274 30.700 1.00 34.54 O HETATM 1976 O HOH A 597 -16.574 29.217 49.017 1.00 28.30 O HETATM 1977 O HOH A 598 16.129 2.434 56.394 1.00 31.56 O HETATM 1978 O HOH A 599 4.118 25.206 71.807 1.00 38.21 O HETATM 1979 O HOH A 600 10.795 32.221 50.487 1.00 37.87 O HETATM 1980 O HOH A 601 11.329 31.111 60.749 1.00 32.83 O HETATM 1981 O HOH A 602 6.389 28.596 47.407 1.00 26.60 O HETATM 1982 O HOH A 603 18.028 9.392 54.846 1.00 41.02 O HETATM 1983 O HOH A 604 -12.054 3.090 53.496 1.00 21.89 O HETATM 1984 O HOH A 605 5.701 5.603 41.748 1.00 29.00 O HETATM 1985 O HOH A 606 -11.546 3.966 62.874 1.00 24.96 O HETATM 1986 O HOH A 607 6.011 11.168 69.432 1.00 35.68 O HETATM 1987 O HOH A 608 4.131 10.183 36.384 1.00 32.61 O HETATM 1988 O HOH A 609 -3.080 24.444 66.553 1.00 20.93 O HETATM 1989 O HOH A 610 -5.660 29.536 62.974 1.00 16.75 O HETATM 1990 O HOH A 611 -6.632 29.961 57.942 1.00 34.43 O HETATM 1991 O HOH A 612 15.302 12.046 63.878 1.00 22.29 O HETATM 1992 O HOH A 613 -1.464 -0.023 68.060 1.00 31.93 O HETATM 1993 O HOH A 614 -12.479 29.174 37.616 1.00 24.42 O HETATM 1994 O HOH A 615 -8.562 34.314 55.246 1.00 23.44 O HETATM 1995 O HOH A 616 13.752 18.924 70.577 1.00 24.96 O HETATM 1996 O HOH A 617 21.733 17.002 61.372 1.00 16.94 O HETATM 1997 O HOH A 618 -4.641 43.320 56.154 1.00 39.09 O HETATM 1998 O HOH A 619 21.907 18.616 63.612 1.00 16.40 O HETATM 1999 O HOH A 620 -23.088 9.927 49.624 1.00 40.10 O HETATM 2000 O HOH A 621 0.590 27.496 39.044 1.00 31.10 O HETATM 2001 O HOH A 622 -13.030 26.960 57.155 1.00 18.90 O HETATM 2002 O HOH A 623 -4.141 29.147 60.620 1.00 25.99 O HETATM 2003 O HOH A 624 11.642 6.488 62.304 1.00 34.23 O HETATM 2004 O HOH A 625 -13.714 26.091 43.738 1.00 21.71 O HETATM 2005 O HOH A 626 20.439 17.369 65.736 1.00 27.71 O HETATM 2006 O HOH A 627 11.188 17.015 43.175 1.00 39.50 O HETATM 2007 O HOH A 628 19.462 27.682 57.640 1.00 30.30 O HETATM 2008 O HOH A 629 -19.869 21.119 50.487 1.00 18.62 O HETATM 2009 O HOH A 630 -10.378 -1.490 45.581 1.00 24.81 O HETATM 2010 O HOH A 631 5.352 0.124 68.308 1.00 22.20 O HETATM 2011 O HOH A 632 16.783 19.961 67.977 1.00 19.74 O HETATM 2012 O HOH A 633 -14.253 28.248 39.663 1.00 31.11 O HETATM 2013 O HOH A 634 -17.753 12.644 42.494 1.00 20.28 O HETATM 2014 O HOH A 635 -12.691 30.874 48.542 1.00 15.46 O HETATM 2015 O HOH A 636 -17.851 12.800 63.412 1.00 45.11 O HETATM 2016 O HOH A 637 20.021 14.724 61.657 1.00 31.16 O HETATM 2017 O HOH A 638 2.134 23.138 31.307 1.00 39.61 O HETATM 2018 O HOH A 639 -14.100 23.156 71.316 1.00 25.15 O HETATM 2019 O HOH A 640 2.162 25.087 41.756 1.00 44.69 O HETATM 2020 O HOH A 641 12.911 12.987 67.504 1.00 25.94 O HETATM 2021 O HOH A 642 17.627 11.934 62.227 1.00 34.55 O HETATM 2022 O HOH A 643 -20.101 19.439 43.779 1.00 38.87 O HETATM 2023 O HOH A 644 -13.500 28.515 44.977 1.00 20.82 O HETATM 2024 O HOH A 645 2.305 18.139 72.118 1.00 43.83 O HETATM 2025 O HOH A 646 -10.617 4.099 65.820 1.00 44.91 O HETATM 2026 O HOH A 647 -16.749 26.139 43.056 1.00 33.21 O HETATM 2027 O HOH A 648 1.189 0.422 67.524 1.00 31.68 O HETATM 2028 O HOH A 649 -2.314 -1.277 70.523 1.00 35.97 O HETATM 2029 O HOH A 650 -16.057 3.757 56.907 1.00 35.18 O HETATM 2030 O HOH A 651 6.215 13.873 70.451 1.00 35.41 O HETATM 2031 O HOH A 652 -20.359 19.305 48.493 1.00 17.24 O HETATM 2032 O HOH A 653 12.171 16.498 70.425 1.00 25.40 O HETATM 2033 O HOH A 654 -17.790 7.592 43.839 1.00 28.00 O HETATM 2034 O HOH A 655 -16.743 3.935 48.704 1.00 40.38 O HETATM 2035 O HOH A 656 16.919 15.422 66.288 1.00 20.58 O HETATM 2036 O HOH A 657 19.751 15.519 46.012 1.00 25.36 O HETATM 2037 O HOH A 658 23.515 27.762 57.280 1.00 34.65 O HETATM 2038 O HOH A 659 -12.026 34.193 50.240 1.00 24.14 O HETATM 2039 O HOH A 660 -15.847 11.531 45.516 1.00 15.26 O HETATM 2040 O HOH A 661 -16.989 4.344 54.151 1.00 34.41 O HETATM 2041 O HOH A 662 -3.090 8.192 72.051 1.00 35.85 O HETATM 2042 O HOH A 663 -17.607 15.219 65.111 1.00 40.42 O HETATM 2043 O HOH A 664 -18.255 13.052 45.207 1.00 17.63 O HETATM 2044 O HOH A 665 -4.365 1.773 73.400 1.00 19.07 O HETATM 2045 O HOH A 666 2.462 29.869 45.377 1.00 23.26 O HETATM 2046 O HOH A 667 2.214 2.831 35.998 1.00 23.45 O HETATM 2047 O HOH A 668 13.885 9.805 64.687 1.00 25.55 O HETATM 2048 O HOH A 669 19.321 14.621 64.789 1.00 33.48 O HETATM 2049 O HOH A 670 -16.530 17.830 66.963 1.00 18.78 O HETATM 2050 O HOH A 671 -0.427 13.175 70.578 1.00 37.56 O HETATM 2051 O HOH A 672 17.608 7.595 61.632 1.00 40.93 O HETATM 2052 O HOH A 673 -18.957 15.711 45.772 1.00 17.23 O HETATM 2053 O HOH A 674 -20.886 21.146 46.250 1.00 34.96 O HETATM 2054 O HOH A 675 2.909 -0.206 69.689 1.00 31.97 O HETATM 2055 O HOH A 676 -16.155 1.270 41.184 1.00 33.83 O HETATM 2056 O HOH A 677 17.564 4.632 57.724 1.00 37.19 O HETATM 2057 O HOH A 678 -20.133 9.296 44.090 1.00 32.92 O HETATM 2058 O HOH A 679 -19.127 5.163 44.870 1.00 40.37 O HETATM 2059 O HOH A 680 13.999 14.349 69.800 1.00 38.31 O HETATM 2060 O HOH A 681 16.715 15.563 69.294 1.00 39.26 O CONECT 637 1764 CONECT 649 1764 CONECT 669 1765 CONECT 1148 1764 CONECT 1284 1765 CONECT 1612 1765 CONECT 1764 637 649 1148 1770 CONECT 1765 669 1284 1612 1770 CONECT 1766 1767 CONECT 1767 1766 1768 1772 CONECT 1768 1767 1769 1771 CONECT 1769 1768 1770 CONECT 1770 1764 1765 1769 CONECT 1771 1768 CONECT 1772 1767 1773 1777 CONECT 1773 1772 1774 1779 CONECT 1774 1773 1775 1776 CONECT 1775 1774 CONECT 1776 1774 CONECT 1777 1772 1778 CONECT 1778 1777 1779 CONECT 1779 1773 1778 MASTER 314 0 3 8 12 0 5 6 1994 1 22 19 END If you find results from this site helpful for your research, please cite one of our papers:
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