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*** MLR ***elNémo ID: 2402090300251998370Job options:ID = 2402090300251998370 JOBID = MLR USERID = MLR PRIVAT = 0 NMODES = 25 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER MLR HEADER HYDROLASE 27-APR-04 1T3R TITLE HIV PROTEASE WILD-TYPE IN COMPLEX WITH TMC114 INHIBITOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEASE RETROPEPSIN; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: HIV-1 PROTEASE; COMPND 5 EC: 3.4.23.16; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 OTHER_DETAILS: COMPLEXED WITH TMC114 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_TAXID: 11676; SOURCE 4 GENE: GAG-POL; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P566 KEYWDS HIV-1 PROTEASE; DRUG RESISTANCE; THERMODYNAMICS; SUBSTRATE ENVELOPE, KEYWDS 2 HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR N.M.KING,M.PRABU-JEYABALAN,E.A.NALIVAIKA,P.B.WIGERNICK,M.P.DE AUTHOR 2 BETHUNE,C.A.SCHIFFER REVDAT 4 27-OCT-21 1T3R 1 REMARK SEQADV HETSYN REVDAT 3 13-JUL-11 1T3R 1 VERSN REVDAT 2 24-FEB-09 1T3R 1 VERSN REVDAT 1 03-MAY-05 1T3R 0 JRNL AUTH D.L.SURLERAUX,A.TAHRI,W.G.VERSCHUEREN,G.M.PILLE,H.A.DE KOCK, JRNL AUTH 2 T.H.JONCKERS,A.PEETERS,S.DE MEYER,H.AZIJN,R.PAUWELS, JRNL AUTH 3 M.P.DE BETHUNE,N.M.KING,M.PRABU-JEYABALAN,C.A.SCHIFFER, JRNL AUTH 4 P.B.WIGERINCK JRNL TITL DISCOVERY AND SELECTION OF TMC114, A NEXT GENERATION HIV-1 JRNL TITL 2 PROTEASE INHIBITOR JRNL REF J.MED.CHEM. V. 48 1813 2005 JRNL REFN ISSN 0022-2623 JRNL PMID 15771427 JRNL DOI 10.1021/JM049560P REMARK 2 REMARK 2 RESOLUTION. 1.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.1.19 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.26 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5 REMARK 3 NUMBER OF REFLECTIONS : 52226 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) : 0.140 REMARK 3 R VALUE (WORKING SET) : 0.140 REMARK 3 FREE R VALUE : 0.179 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2775 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) : 1.20 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.23 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2913 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2040 REMARK 3 BIN FREE R VALUE SET COUNT : 146 REMARK 3 BIN FREE R VALUE : 0.2640 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1496 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 63 REMARK 3 SOLVENT ATOMS : 259 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.42 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.39000 REMARK 3 B22 (A**2) : -0.06000 REMARK 3 B33 (A**2) : 0.45000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.040 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.042 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.028 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.622 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.976 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.965 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1664 ; 0.039 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 1591 ; 0.007 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2284 ; 1.593 ; 2.018 REMARK 3 BOND ANGLES OTHERS (DEGREES): 3708 ; 0.722 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 215 ; 6.960 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 270 ; 0.149 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1822 ; 0.021 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 301 ; 0.028 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 285 ; 0.244 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1925 ; 0.274 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): 1088 ; 0.095 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 172 ; 0.254 ; 0.200 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): 18 ; 0.310 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 101 ; 0.312 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 49 ; 0.338 ; 0.200 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): 1033 ; 3.219 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1690 ; 4.242 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 631 ; 5.811 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 593 ; 8.132 ; 4.500 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): 1664 ; 2.590 ; 1.000 REMARK 3 SPHERICITY; FREE ATOMS (A**2): 267 ;16.645 ; 3.000 REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 1628 ; 9.511 ; 3.000 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 : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 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 REMARK 4 REMARK 4 1T3R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-APR-04. REMARK 100 THE DEPOSITION ID IS D_1000022274. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 190 REMARK 200 PH : 6.2 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 5.0.1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.900 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55056 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5 REMARK 200 DATA REDUNDANCY : 5.500 REMARK 200 R MERGE (I) : 0.03800 REMARK 200 R SYM (I) : 0.03800 REMARK 200 FOR THE DATA SET : 25.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.24 REMARK 200 COMPLETENESS FOR SHELL (%) : 76.2 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.31700 REMARK 200 R SYM FOR SHELL (I) : 0.31700 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: AMORE REMARK 200 STARTING MODEL: 1F7A REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 41.56 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1 MG/ML PROTEIN; 5:1 LIGAND:PROTEIN; REMARK 280 30% AMSOR; SODIUM CITRATE AND SODIUM PHOSPHATE, PH 6.2, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 300K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 25.37300 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 31.00300 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.90350 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 31.00300 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.37300 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.90350 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5530 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 9340 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 7 CG CD CE NZ REMARK 470 LYS A 41 CG CD CE NZ REMARK 470 LYS A 43 CG CD CE NZ REMARK 470 LYS B 41 CG CD CE NZ REMARK 470 LYS B 43 CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O GLY A 16 O HOH B 618 1655 1.94 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 ARG A 14 CB ARG A 14 CG -0.173 REMARK 500 GLU A 21 CD GLU A 21 OE2 0.083 REMARK 500 GLU A 34 CD GLU A 34 OE1 0.144 REMARK 500 GLU A 35 CD GLU A 35 OE2 0.069 REMARK 500 GLU A 65 CD GLU A 65 OE2 -0.130 REMARK 500 CYS A 67 CB CYS A 67 SG -0.188 REMARK 500 CYS A 95 CB CYS A 95 SG -0.139 REMARK 500 THR B 4 CA THR B 4 CB 0.248 REMARK 500 THR B 4 CB THR B 4 OG1 -0.215 REMARK 500 ARG B 8 NE ARG B 8 CZ 0.086 REMARK 500 ARG B 14 NE ARG B 14 CZ -0.098 REMARK 500 GLN B 18 CA GLN B 18 CB 0.132 REMARK 500 LYS B 45 CD LYS B 45 CE -0.176 REMARK 500 LYS B 45 CE LYS B 45 NZ -0.196 REMARK 500 MET B 46 CB MET B 46 CG 0.220 REMARK 500 TYR B 59 CD1 TYR B 59 CE1 -0.100 REMARK 500 CYS B 67 CB CYS B 67 SG -0.185 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ARG A 87 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 502 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 503 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 504 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 505 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 017 A 1200 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1F7A RELATED DB: PDB REMARK 900 USED AS STARTING MODEL FOR MOLECULAR REPLACEMENT REMARK 900 RELATED ID: 1T7I RELATED DB: PDB REMARK 900 RELATED ID: 1T7J RELATED DB: PDB DBREF 1T3R A 1 99 UNP P03369 POL_HV1A2 57 155 DBREF 1T3R B 1 99 UNP P03369 POL_HV1A2 57 155 SEQADV 1T3R LYS A 7 UNP P03369 GLN 63 ENGINEERED MUTATION SEQADV 1T3R LYS B 7 UNP P03369 GLN 63 ENGINEERED MUTATION SEQRES 1 A 99 PRO GLN ILE THR LEU TRP LYS ARG PRO LEU VAL THR ILE SEQRES 2 A 99 ARG ILE GLY GLY GLN LEU LYS GLU ALA LEU LEU ASP THR SEQRES 3 A 99 GLY ALA ASP ASP THR VAL LEU GLU GLU MET ASN LEU PRO SEQRES 4 A 99 GLY LYS TRP LYS PRO LYS MET ILE GLY GLY ILE GLY GLY SEQRES 5 A 99 PHE ILE LYS VAL ARG GLN TYR ASP GLN ILE PRO VAL GLU SEQRES 6 A 99 ILE CYS GLY HIS LYS ALA ILE GLY THR VAL LEU VAL GLY SEQRES 7 A 99 PRO THR PRO VAL ASN ILE ILE GLY ARG ASN LEU LEU THR SEQRES 8 A 99 GLN ILE GLY CYS THR LEU ASN PHE SEQRES 1 B 99 PRO GLN ILE THR LEU TRP LYS ARG PRO LEU VAL THR ILE SEQRES 2 B 99 ARG ILE GLY GLY GLN LEU LYS GLU ALA LEU LEU ASP THR SEQRES 3 B 99 GLY ALA ASP ASP THR VAL LEU GLU GLU MET ASN LEU PRO SEQRES 4 B 99 GLY LYS TRP LYS PRO LYS MET ILE GLY GLY ILE GLY GLY SEQRES 5 B 99 PHE ILE LYS VAL ARG GLN TYR ASP GLN ILE PRO VAL GLU SEQRES 6 B 99 ILE CYS GLY HIS LYS ALA ILE GLY THR VAL LEU VAL GLY SEQRES 7 B 99 PRO THR PRO VAL ASN ILE ILE GLY ARG ASN LEU LEU THR SEQRES 8 B 99 GLN ILE GLY CYS THR LEU ASN PHE HET PO4 A 502 5 HET PO4 A 504 5 HET PO4 A 505 5 HET 017 A1200 38 HET PO4 B 501 5 HET PO4 B 503 5 HETNAM PO4 PHOSPHATE ION HETNAM 017 (3R,3AS,6AR)-HEXAHYDROFURO[2,3-B]FURAN-3-YL(1S,2R)-3- HETNAM 2 017 [[(4-AMINOPHENYL)SULFONYL](ISOBUTYL)AMINO]-1-BENZYL-2- HETNAM 3 017 HYDROXYPROPYLCARBAMATE HETSYN 017 DARUNAVIR; TMC114; UIC-94017 FORMUL 3 PO4 5(O4 P 3-) FORMUL 6 017 C27 H37 N3 O7 S FORMUL 9 HOH *259(H2 O) HELIX 1 1 GLY A 86 THR A 91 1 6 HELIX 2 2 GLY B 86 THR B 91 1 6 SHEET 1 A 4 GLN A 2 ILE A 3 0 SHEET 2 A 4 THR B 96 ASN B 98 -1 O LEU B 97 N ILE A 3 SHEET 3 A 4 THR A 96 ASN A 98 -1 N ASN A 98 O THR B 96 SHEET 4 A 4 GLN B 2 THR B 4 -1 O ILE B 3 N LEU A 97 SHEET 1 B 8 LYS A 43 GLY A 49 0 SHEET 2 B 8 GLY A 52 ILE A 66 -1 O GLN A 58 N LYS A 43 SHEET 3 B 8 HIS A 69 VAL A 77 -1 O HIS A 69 N ILE A 66 SHEET 4 B 8 VAL A 32 LEU A 33 1 N LEU A 33 O LEU A 76 SHEET 5 B 8 ILE A 84 ILE A 85 -1 O ILE A 84 N VAL A 32 SHEET 6 B 8 GLN A 18 LEU A 24 1 N LEU A 23 O ILE A 85 SHEET 7 B 8 LEU A 10 ILE A 15 -1 N ILE A 15 O GLN A 18 SHEET 8 B 8 GLY A 52 ILE A 66 -1 O GLU A 65 N ARG A 14 SHEET 1 C 8 LYS B 43 GLY B 49 0 SHEET 2 C 8 GLY B 52 ILE B 66 -1 O GLN B 58 N LYS B 43 SHEET 3 C 8 HIS B 69 VAL B 77 -1 O VAL B 75 N TYR B 59 SHEET 4 C 8 VAL B 32 LEU B 33 1 N LEU B 33 O LEU B 76 SHEET 5 C 8 ILE B 84 ILE B 85 -1 O ILE B 84 N VAL B 32 SHEET 6 C 8 GLN B 18 LEU B 24 1 N LEU B 23 O ILE B 85 SHEET 7 C 8 LEU B 10 ILE B 15 -1 N ILE B 13 O LYS B 20 SHEET 8 C 8 GLY B 52 ILE B 66 -1 O GLU B 65 N ARG B 14 SITE 1 AC1 10 ARG A 14 GLY A 16 GLY A 17 HOH A1242 SITE 2 AC1 10 ARG B 14 GLY B 16 GLY B 17 HOH B 515 SITE 3 AC1 10 HOH B 525 HOH B 617 SITE 1 AC2 3 LYS A 7 ARG A 8 HOH A1225 SITE 1 AC3 7 GLY A 68 HIS A 69 LYS A 70 HOH A1210 SITE 2 AC3 7 HOH A1249 PRO B 1 LYS B 55 SITE 1 AC4 5 MET A 36 ASN A 37 PRO B 39 GLY B 40 SITE 2 AC4 5 HOH B 621 SITE 1 AC5 6 LYS A 20 GLU A 21 ASN A 83 HOH A1219 SITE 2 AC5 6 HOH A1226 HOH B 616 SITE 1 AC6 19 ASP A 25 GLY A 27 ALA A 28 ASP A 29 SITE 2 AC6 19 ASP A 30 GLY A 48 GLY A 49 ILE A 50 SITE 3 AC6 19 HOH A1203 HOH A1311 ASP B 25 GLY B 27 SITE 4 AC6 19 ALA B 28 ASP B 30 VAL B 32 GLY B 48 SITE 5 AC6 19 GLY B 49 VAL B 82 ILE B 84 CRYST1 50.746 57.807 62.006 90.00 90.00 90.00 P 21 21 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.019706 0.000000 0.000000 0.00000 SCALE2 0.000000 0.017299 0.000000 0.00000 SCALE3 0.000000 0.000000 0.016127 0.00000 ATOM 1 N PRO A 1 28.699 21.454 33.798 1.00 26.41 N ANISOU 1 N PRO A 1 3228 3823 2983 326 -22 -139 N ATOM 2 CA PRO A 1 27.719 22.265 34.525 1.00 24.79 C ANISOU 2 CA PRO A 1 2833 3634 2950 238 -116 -18 C ATOM 3 C PRO A 1 26.240 22.015 34.064 1.00 21.25 C ANISOU 3 C PRO A 1 2737 3064 2273 403 -170 13 C ATOM 4 O PRO A 1 26.033 21.403 33.071 1.00 22.75 O ANISOU 4 O PRO A 1 3013 3254 2374 732 -293 -487 O ATOM 5 CB PRO A 1 28.122 23.699 34.165 1.00 29.49 C ANISOU 5 CB PRO A 1 3630 3780 3795 173 0 -64 C ATOM 6 CG PRO A 1 28.733 23.595 32.866 1.00 29.10 C ANISOU 6 CG PRO A 1 3506 4035 3514 18 -74 20 C ATOM 7 CD PRO A 1 29.425 22.266 32.812 1.00 28.00 C ANISOU 7 CD PRO A 1 3406 3822 3410 -76 -264 54 C ATOM 8 N GLN A 2 25.279 22.419 34.914 1.00 21.01 N ANISOU 8 N GLN A 2 2911 3208 1862 453 -246 -92 N ATOM 9 CA GLN A 2 23.872 22.620 34.516 1.00 17.82 C ANISOU 9 CA GLN A 2 2575 2782 1411 284 -61 121 C ATOM 10 C GLN A 2 23.654 24.078 34.247 1.00 18.11 C ANISOU 10 C GLN A 2 2783 2713 1384 344 -136 -147 C ATOM 11 O GLN A 2 23.996 24.956 35.114 1.00 20.40 O ANISOU 11 O GLN A 2 3304 2912 1535 262 -202 8 O ATOM 12 CB GLN A 2 22.926 22.138 35.611 1.00 19.10 C ANISOU 12 CB GLN A 2 2921 2892 1444 430 159 273 C ATOM 13 CG GLN A 2 21.447 22.401 35.328 1.00 18.52 C ANISOU 13 CG GLN A 2 2848 2709 1478 305 289 290 C ATOM 14 CD GLN A 2 20.558 21.549 36.121 1.00 21.32 C ANISOU 14 CD GLN A 2 3536 2808 1755 122 192 302 C ATOM 15 OE1 GLN A 2 20.145 20.502 35.662 1.00 22.49 O ANISOU 15 OE1 GLN A 2 3459 3395 1691 -395 479 368 O ATOM 16 NE2 GLN A 2 20.336 21.926 37.380 1.00 21.05 N ANISOU 16 NE2 GLN A 2 2979 3111 1907 347 513 40 N ATOM 17 N ILE A 3 23.132 24.397 33.044 1.00 16.55 N ANISOU 17 N ILE A 3 2472 2473 1341 339 18 60 N ATOM 18 CA ILE A 3 22.953 25.808 32.633 1.00 16.67 C ANISOU 18 CA ILE A 3 2552 2337 1442 458 -7 -249 C ATOM 19 C ILE A 3 21.482 26.059 32.330 1.00 15.72 C ANISOU 19 C ILE A 3 2477 2010 1485 376 -5 21 C ATOM 20 O ILE A 3 20.868 25.364 31.520 1.00 15.91 O ANISOU 20 O ILE A 3 2515 2236 1291 504 -13 -201 O ATOM 21 CB ILE A 3 23.812 26.118 31.387 1.00 18.38 C ANISOU 21 CB ILE A 3 2784 2439 1761 342 103 77 C ATOM 22 CG1 ILE A 3 25.342 25.949 31.689 1.00 18.48 C ANISOU 22 CG1 ILE A 3 2985 2333 1701 251 137 376 C ATOM 23 CG2 ILE A 3 23.547 27.527 30.875 1.00 19.52 C ANISOU 23 CG2 ILE A 3 2860 2478 2078 630 178 48 C ATOM 24 CD1 ILE A 3 26.162 26.103 30.549 1.00 21.55 C ANISOU 24 CD1 ILE A 3 3126 3115 1943 317 107 306 C ATOM 25 N THR A 4 20.887 26.933 33.128 1.00 15.87 N ANISOU 25 N THR A 4 2589 2347 1091 456 -119 -143 N ATOM 26 CA THR A 4 19.503 27.351 32.833 1.00 15.75 C ANISOU 26 CA THR A 4 2575 2027 1382 491 29 -180 C ATOM 27 C THR A 4 19.446 28.398 31.741 1.00 15.51 C ANISOU 27 C THR A 4 2468 2054 1369 336 -99 -229 C ATOM 28 O THR A 4 20.430 28.870 31.310 1.00 16.38 O ANISOU 28 O THR A 4 2558 2118 1547 285 -229 -99 O ATOM 29 CB THR A 4 18.816 27.912 34.134 1.00 16.86 C ANISOU 29 CB THR A 4 2566 2562 1276 509 19 -53 C ATOM 30 OG1 THR A 4 19.563 29.057 34.578 1.00 19.32 O ANISOU 30 OG1 THR A 4 3214 2740 1385 449 -40 -46 O ATOM 31 CG2 THR A 4 18.833 26.841 35.249 1.00 18.60 C ANISOU 31 CG2 THR A 4 2823 2523 1719 531 307 -138 C ATOM 32 N LEU A 5 18.246 28.766 31.361 1.00 15.45 N ANISOU 32 N LEU A 5 2625 2165 1078 453 118 -333 N ATOM 33 CA LEU A 5 18.036 29.497 30.073 1.00 13.94 C ANISOU 33 CA LEU A 5 2308 1907 1082 331 97 -220 C ATOM 34 C LEU A 5 17.299 30.803 30.212 1.00 16.04 C ANISOU 34 C LEU A 5 2760 1992 1339 574 107 -446 C ATOM 35 O LEU A 5 16.815 31.385 29.209 1.00 15.73 O ANISOU 35 O LEU A 5 2583 2163 1228 669 82 -220 O ATOM 36 CB LEU A 5 17.384 28.590 29.088 1.00 13.41 C ANISOU 36 CB LEU A 5 2125 1980 991 348 64 -94 C ATOM 37 CG LEU A 5 18.226 27.325 28.692 1.00 13.46 C ANISOU 37 CG LEU A 5 2129 1848 1135 335 126 -138 C ATOM 38 CD1 LEU A 5 17.455 26.412 27.870 1.00 14.28 C ANISOU 38 CD1 LEU A 5 2127 2146 1150 187 366 -102 C ATOM 39 CD2 LEU A 5 19.482 27.737 27.925 1.00 14.09 C ANISOU 39 CD2 LEU A 5 2222 2037 1095 246 -83 -179 C ATOM 40 N TRP A 6 17.284 31.375 31.434 1.00 16.86 N ANISOU 40 N TRP A 6 3074 2169 1159 722 174 -326 N ATOM 41 CA TRP A 6 16.707 32.666 31.611 1.00 17.05 C ANISOU 41 CA TRP A 6 2845 2216 1417 514 101 -445 C ATOM 42 C TRP A 6 17.659 33.763 31.019 1.00 18.33 C ANISOU 42 C TRP A 6 2805 2206 1951 433 112 -820 C ATOM 43 O TRP A 6 17.204 34.845 30.676 1.00 20.73 O ANISOU 43 O TRP A 6 2979 2194 2704 541 114 -236 O ATOM 44 CB TRP A 6 16.356 32.919 33.157 1.00 20.30 C ANISOU 44 CB TRP A 6 3282 2674 1756 530 482 -924 C ATOM 45 CG TRP A 6 15.026 32.189 33.646 1.00 18.85 C ANISOU 45 CG TRP A 6 3162 2816 1183 236 264 -555 C ATOM 46 CD1 TRP A 6 13.705 32.558 33.336 1.00 19.94 C ANISOU 46 CD1 TRP A 6 2761 3126 1688 528 471 -492 C ATOM 47 CD2 TRP A 6 14.941 30.990 34.423 1.00 20.40 C ANISOU 47 CD2 TRP A 6 3070 2639 2041 489 34 -613 C ATOM 48 NE1 TRP A 6 12.820 31.577 33.761 1.00 21.82 N ANISOU 48 NE1 TRP A 6 3094 3240 1955 369 -165 -339 N ATOM 49 CE2 TRP A 6 13.542 30.616 34.493 1.00 20.77 C ANISOU 49 CE2 TRP A 6 3332 2861 1696 267 -221 -230 C ATOM 50 CE3 TRP A 6 15.875 30.123 34.920 1.00 20.29 C ANISOU 50 CE3 TRP A 6 3064 2957 1689 692 256 -660 C ATOM 51 CZ2 TRP A 6 13.127 29.428 35.041 1.00 21.27 C ANISOU 51 CZ2 TRP A 6 2917 3585 1580 512 253 -145 C ATOM 52 CZ3 TRP A 6 15.452 28.956 35.526 1.00 23.27 C ANISOU 52 CZ3 TRP A 6 3170 3374 2296 417 261 -242 C ATOM 53 CH2 TRP A 6 14.085 28.634 35.609 1.00 21.71 C ANISOU 53 CH2 TRP A 6 3005 3133 2110 364 135 264 C ATOM 54 N LYS A 7 18.943 33.460 30.863 1.00 18.01 N ANISOU 54 N LYS A 7 2737 2297 1807 457 51 -527 N ATOM 55 CA LYS A 7 19.868 34.291 30.152 1.00 18.47 C ANISOU 55 CA LYS A 7 2899 2250 1865 354 -194 -724 C ATOM 56 C LYS A 7 20.407 33.514 28.970 1.00 16.89 C ANISOU 56 C LYS A 7 2823 2173 1421 142 -172 -516 C ATOM 57 O LYS A 7 20.390 32.305 28.964 1.00 16.24 O ANISOU 57 O LYS A 7 2656 1968 1545 314 -46 -329 O ATOM 58 CB LYS A 7 21.039 34.694 31.043 1.00 22.07 C ANISOU 58 CB LYS A 7 3564 3071 1750 -210 -21 -1190 C ATOM 59 N ARG A 8 21.063 34.206 28.059 1.00 15.16 N ANISOU 59 N ARG A 8 2350 1673 1735 309 -198 -369 N ATOM 60 CA ARG A 8 21.751 33.512 26.958 1.00 14.08 C ANISOU 60 CA ARG A 8 2189 1788 1372 217 -258 -291 C ATOM 61 C ARG A 8 22.831 32.627 27.523 1.00 14.01 C ANISOU 61 C ARG A 8 2373 1656 1292 157 -309 -472 C ATOM 62 O ARG A 8 23.644 33.098 28.358 1.00 15.33 O ANISOU 62 O ARG A 8 2562 1734 1527 118 -562 -560 O ATOM 63 CB ARG A 8 22.393 34.533 25.995 1.00 15.05 C ANISOU 63 CB ARG A 8 2299 1934 1482 27 -365 -398 C ATOM 64 CG ARG A 8 21.388 35.299 25.145 1.00 16.10 C ANISOU 64 CG ARG A 8 2276 1738 2101 22 -371 -147 C ATOM 65 CD ARG A 8 21.981 36.283 24.289 1.00 18.66 C ANISOU 65 CD ARG A 8 2387 2236 2466 -331 -391 53 C ATOM 66 NE ARG A 8 20.974 36.967 23.478 1.00 26.58 N ANISOU 66 NE ARG A 8 3371 2557 4169 56 -417 425 N ATOM 67 CZ ARG A 8 21.155 38.127 22.865 1.00 28.39 C ANISOU 67 CZ ARG A 8 4006 3149 3631 -544 -785 471 C ATOM 68 NH1 ARG A 8 22.298 38.861 23.072 1.00 32.61 N ANISOU 68 NH1 ARG A 8 4183 3313 4894 -969 -276 320 N ATOM 69 NH2 ARG A 8 20.234 38.582 22.075 1.00 27.89 N ANISOU 69 NH2 ARG A 8 3546 2574 4477 -274 -492 1381 N ATOM 70 N PRO A 9 22.993 31.412 26.985 1.00 13.20 N ANISOU 70 N PRO A 9 1991 1450 1572 105 -140 -365 N ATOM 71 CA PRO A 9 24.058 30.507 27.473 1.00 12.81 C ANISOU 71 CA PRO A 9 2230 1621 1016 43 -352 -232 C ATOM 72 C PRO A 9 25.393 30.784 26.831 1.00 13.39 C ANISOU 72 C PRO A 9 2008 1794 1283 -7 -242 -359 C ATOM 73 O PRO A 9 25.886 30.054 25.979 1.00 13.14 O ANISOU 73 O PRO A 9 2044 1590 1358 80 -393 -228 O ATOM 74 CB PRO A 9 23.517 29.138 27.156 1.00 12.80 C ANISOU 74 CB PRO A 9 2105 1505 1251 155 -110 -250 C ATOM 75 CG PRO A 9 22.661 29.333 25.968 1.00 11.86 C ANISOU 75 CG PRO A 9 1717 1600 1188 -155 -120 -315 C ATOM 76 CD PRO A 9 21.995 30.679 26.191 1.00 12.06 C ANISOU 76 CD PRO A 9 1750 1561 1270 -70 -48 -387 C ATOM 77 N LEU A 10 25.975 31.915 27.261 1.00 15.80 N ANISOU 77 N LEU A 10 2387 1989 1625 -202 -321 -598 N ATOM 78 CA LEU A 10 27.264 32.344 26.801 1.00 14.99 C ANISOU 78 CA LEU A 10 2194 1917 1581 -90 -250 -271 C ATOM 79 C LEU A 10 28.381 31.764 27.624 1.00 17.09 C ANISOU 79 C LEU A 10 2367 2704 1421 -279 -383 -378 C ATOM 80 O LEU A 10 28.286 31.737 28.859 1.00 22.73 O ANISOU 80 O LEU A 10 3001 4247 1387 -311 -330 -468 O ATOM 81 CB LEU A 10 27.364 33.892 26.837 1.00 18.92 C ANISOU 81 CB LEU A 10 2699 2186 2301 -538 -251 -730 C ATOM 82 CG LEU A 10 26.444 34.574 25.905 1.00 20.44 C ANISOU 82 CG LEU A 10 2503 1908 3353 -266 88 -169 C ATOM 83 CD1 LEU A 10 26.254 36.027 26.276 1.00 23.88 C ANISOU 83 CD1 LEU A 10 3524 1978 3572 -280 192 -301 C ATOM 84 CD2 LEU A 10 26.983 34.490 24.453 1.00 21.23 C ANISOU 84 CD2 LEU A 10 2827 2231 3008 152 -813 -231 C ATOM 85 N VAL A 11 29.375 31.255 27.011 1.00 14.84 N ANISOU 85 N VAL A 11 2085 2000 1552 -168 -746 51 N ATOM 86 CA VAL A 11 30.473 30.664 27.715 1.00 16.59 C ANISOU 86 CA VAL A 11 2390 2079 1833 -215 -869 353 C ATOM 87 C VAL A 11 31.810 31.113 27.103 1.00 14.71 C ANISOU 87 C VAL A 11 2325 1865 1397 -54 -849 -29 C ATOM 88 O VAL A 11 31.877 31.590 25.971 1.00 15.58 O ANISOU 88 O VAL A 11 2106 2043 1770 -331 -977 250 O ATOM 89 CB VAL A 11 30.397 29.207 27.749 1.00 19.02 C ANISOU 89 CB VAL A 11 2734 2264 2230 -209 -935 556 C ATOM 90 CG1 VAL A 11 29.094 28.704 28.409 1.00 23.88 C ANISOU 90 CG1 VAL A 11 3030 3081 2961 -579 -953 960 C ATOM 91 CG2 VAL A 11 30.583 28.631 26.486 1.00 19.95 C ANISOU 91 CG2 VAL A 11 2707 1692 3179 -291 -345 76 C ATOM 92 N THR A 12 32.875 30.963 27.866 1.00 16.70 N ANISOU 92 N THR A 12 2106 2100 2138 -320 -1140 385 N ATOM 93 CA THR A 12 34.172 31.223 27.350 1.00 16.58 C ANISOU 93 CA THR A 12 2279 2090 1931 -287 -1005 193 C ATOM 94 C THR A 12 34.751 30.001 26.690 1.00 16.89 C ANISOU 94 C THR A 12 2239 1953 2222 4 -1024 167 C ATOM 95 O THR A 12 34.684 28.888 27.273 1.00 17.57 O ANISOU 95 O THR A 12 2615 1762 2298 -67 -1057 519 O ATOM 96 CB THR A 12 35.130 31.713 28.518 1.00 19.89 C ANISOU 96 CB THR A 12 2514 2456 2587 -480 -1332 51 C ATOM 97 OG1 THR A 12 34.586 32.859 29.079 1.00 20.17 O ANISOU 97 OG1 THR A 12 2804 2324 2536 -492 -1298 42 O ATOM 98 CG2 THR A 12 36.444 32.085 28.007 1.00 20.97 C ANISOU 98 CG2 THR A 12 2508 2528 2930 -360 -1382 28 C ATOM 99 N ILE A 13 35.321 30.172 25.494 1.00 15.74 N ANISOU 99 N ILE A 13 2121 1652 2205 -476 -902 290 N ATOM 100 CA ILE A 13 36.036 29.162 24.798 1.00 16.14 C ANISOU 100 CA ILE A 13 1954 1921 2258 -305 -830 425 C ATOM 101 C ILE A 13 37.486 29.576 24.558 1.00 18.01 C ANISOU 101 C ILE A 13 1850 1844 3148 -674 -782 564 C ATOM 102 O ILE A 13 37.809 30.785 24.600 1.00 18.55 O ANISOU 102 O ILE A 13 2051 1799 3196 -487 -1307 655 O ATOM 103 CB ILE A 13 35.326 28.822 23.452 1.00 15.76 C ANISOU 103 CB ILE A 13 1951 1727 2307 -336 -877 347 C ATOM 104 CG1 ILE A 13 35.489 29.988 22.407 1.00 16.94 C ANISOU 104 CG1 ILE A 13 1828 1911 2695 -404 -1006 513 C ATOM 105 CG2 ILE A 13 33.854 28.522 23.730 1.00 15.87 C ANISOU 105 CG2 ILE A 13 1798 1818 2411 -231 -1098 361 C ATOM 106 CD1 ILE A 13 35.054 29.629 20.995 1.00 15.73 C ANISOU 106 CD1 ILE A 13 1730 1899 2347 -124 -756 454 C ATOM 107 N ARG A 14 38.351 28.546 24.283 1.00 19.24 N ANISOU 107 N ARG A 14 1923 1889 3499 -466 -972 416 N ATOM 108 CA ARG A 14 39.740 28.714 23.796 1.00 19.48 C ANISOU 108 CA ARG A 14 1845 2023 3531 -149 -998 564 C ATOM 109 C ARG A 14 39.918 28.028 22.436 1.00 20.28 C ANISOU 109 C ARG A 14 1550 2488 3665 111 -746 405 C ATOM 110 O ARG A 14 39.637 26.872 22.330 1.00 21.28 O ANISOU 110 O ARG A 14 2017 1749 4316 -146 -720 1058 O ATOM 111 CB ARG A 14 40.748 27.997 24.860 1.00 25.11 C ANISOU 111 CB ARG A 14 2133 3121 4284 148 -1143 376 C ATOM 112 CG ARG A 14 41.974 28.524 25.047 1.00 26.05 C ANISOU 112 CG ARG A 14 1978 4063 3854 268 -745 323 C ATOM 113 CD ARG A 14 42.876 27.685 26.109 1.00 28.26 C ANISOU 113 CD ARG A 14 2717 4106 3912 545 -1009 51 C ATOM 114 NE ARG A 14 44.159 27.228 25.525 1.00 28.29 N ANISOU 114 NE ARG A 14 2799 3645 4306 347 -687 672 N ATOM 115 CZ ARG A 14 45.195 26.746 26.259 1.00 25.16 C ANISOU 115 CZ ARG A 14 2982 3757 2820 500 -413 435 C ATOM 116 NH1 ARG A 14 45.134 26.730 27.627 1.00 31.96 N ANISOU 116 NH1 ARG A 14 4540 4469 3132 401 214 785 N ATOM 117 NH2 ARG A 14 46.281 26.301 25.639 1.00 25.69 N ANISOU 117 NH2 ARG A 14 2276 4004 3480 -37 -8 772 N ATOM 118 N ILE A 15 40.496 28.785 21.374 1.00 17.55 N ANISOU 118 N ILE A 15 1534 1745 3385 -283 -771 402 N ATOM 119 CA ILE A 15 40.664 28.280 20.005 1.00 18.93 C ANISOU 119 CA ILE A 15 1883 2053 3253 -116 -482 584 C ATOM 120 C ILE A 15 41.849 29.017 19.370 1.00 22.09 C ANISOU 120 C ILE A 15 2236 2087 4071 -105 106 528 C ATOM 121 O ILE A 15 41.974 30.256 19.540 1.00 22.91 O ANISOU 121 O ILE A 15 1533 2186 4986 104 -529 656 O ATOM 122 CB ILE A 15 39.370 28.512 19.202 1.00 18.63 C ANISOU 122 CB ILE A 15 1863 2082 3134 -2 -897 700 C ATOM 123 CG1 ILE A 15 39.539 27.963 17.824 1.00 20.53 C ANISOU 123 CG1 ILE A 15 1745 2882 3173 460 186 759 C ATOM 124 CG2 ILE A 15 38.906 30.049 19.262 1.00 22.07 C ANISOU 124 CG2 ILE A 15 1856 2382 4145 413 -431 930 C ATOM 125 CD1 ILE A 15 38.335 28.008 16.992 1.00 21.04 C ANISOU 125 CD1 ILE A 15 2041 3004 2947 614 -101 1296 C ATOM 126 N GLY A 16 42.710 28.265 18.585 1.00 20.04 N ANISOU 126 N GLY A 16 2183 2166 3263 -240 -109 176 N ATOM 127 CA GLY A 16 43.870 28.844 17.943 1.00 21.12 C ANISOU 127 CA GLY A 16 2402 2552 3067 -217 -98 18 C ATOM 128 C GLY A 16 44.732 29.561 18.902 1.00 22.23 C ANISOU 128 C GLY A 16 2924 2375 3147 -208 -153 -110 C ATOM 129 O GLY A 16 45.498 30.522 18.511 1.00 23.46 O ANISOU 129 O GLY A 16 2607 2706 3601 -441 -365 113 O ATOM 130 N GLY A 17 44.609 29.232 20.109 1.00 20.72 N ANISOU 130 N GLY A 17 2207 2616 3046 -76 134 17 N ATOM 131 CA GLY A 17 45.383 29.828 21.189 1.00 25.17 C ANISOU 131 CA GLY A 17 3543 2677 3341 -8 -401 -247 C ATOM 132 C GLY A 17 44.727 30.930 21.930 1.00 23.89 C ANISOU 132 C GLY A 17 2286 3756 3034 346 -429 -409 C ATOM 133 O GLY A 17 45.299 31.459 22.831 1.00 26.29 O ANISOU 133 O GLY A 17 3050 3550 3387 469 -955 -592 O ATOM 134 N GLN A 18 43.639 31.479 21.343 1.00 21.91 N ANISOU 134 N GLN A 18 2217 2477 3629 75 -593 -171 N ATOM 135 CA GLN A 18 42.946 32.713 21.880 1.00 22.92 C ANISOU 135 CA GLN A 18 2392 2618 3697 -262 -558 -156 C ATOM 136 C GLN A 18 41.507 32.418 22.671 1.00 23.47 C ANISOU 136 C GLN A 18 2534 2591 3792 -137 -746 358 C ATOM 137 O GLN A 18 40.861 31.451 22.428 1.00 26.51 O ANISOU 137 O GLN A 18 2861 2188 5021 -809 -776 583 O ATOM 138 CB GLN A 18 42.656 33.686 20.670 1.00 23.78 C ANISOU 138 CB GLN A 18 2811 2588 3636 -76 -943 44 C ATOM 139 CG GLN A 18 43.872 34.050 19.911 1.00 31.20 C ANISOU 139 CG GLN A 18 3794 3332 4727 -125 -198 150 C ATOM 140 CD GLN A 18 44.718 34.960 20.660 1.00 30.20 C ANISOU 140 CD GLN A 18 3851 3143 4481 438 191 -702 C ATOM 141 OE1 GLN A 18 44.237 36.091 21.096 1.00 27.16 O ANISOU 141 OE1 GLN A 18 3459 2773 4085 0 1015 -492 O ATOM 142 NE2 GLN A 18 45.999 34.565 20.884 1.00 29.54 N ANISOU 142 NE2 GLN A 18 3720 3330 4171 533 -81 -181 N ATOM 143 N ALEU A 19 41.185 33.264 23.682 0.50 21.32 N ANISOU 143 N ALEU A 19 2547 2245 3309 -370 -1047 405 N ATOM 144 N BLEU A 19 41.153 33.288 23.569 0.50 19.10 N ANISOU 144 N BLEU A 19 2285 1908 3064 -426 -1268 391 N ATOM 145 CA ALEU A 19 39.800 33.235 24.388 0.50 24.41 C ANISOU 145 CA ALEU A 19 2879 2841 3553 -77 -788 560 C ATOM 146 CA BLEU A 19 39.837 33.221 24.286 0.50 21.98 C ANISOU 146 CA BLEU A 19 2692 2479 3181 -99 -904 521 C ATOM 147 C ALEU A 19 38.770 34.025 23.636 0.50 21.26 C ANISOU 147 C ALEU A 19 2436 2303 3337 -537 -903 678 C ATOM 148 C BLEU A 19 38.774 34.075 23.682 0.50 18.95 C ANISOU 148 C BLEU A 19 2306 2130 2763 -619 -1363 721 C ATOM 149 O ALEU A 19 39.058 35.123 23.132 0.50 26.30 O ANISOU 149 O ALEU A 19 3088 2498 4408 -720 -859 937 O ATOM 150 O BLEU A 19 38.981 35.286 23.492 0.50 23.09 O ANISOU 150 O BLEU A 19 2472 2490 3811 -1003 -1956 1190 O ATOM 151 CB ALEU A 19 39.862 33.793 25.850 0.50 23.07 C ANISOU 151 CB ALEU A 19 2847 2265 3652 -248 -603 593 C ATOM 152 CB BLEU A 19 39.984 33.634 25.654 0.50 20.78 C ANISOU 152 CB BLEU A 19 2883 1683 3330 -237 -692 117 C ATOM 153 CG ALEU A 19 40.627 32.946 26.937 0.50 25.76 C ANISOU 153 CG ALEU A 19 2565 3564 3658 184 -981 299 C ATOM 154 CG BLEU A 19 41.050 32.880 26.462 0.50 18.52 C ANISOU 154 CG BLEU A 19 2249 2007 2778 -220 -443 -163 C ATOM 155 CD1ALEU A 19 42.060 32.745 26.506 0.50 26.02 C ANISOU 155 CD1ALEU A 19 3180 3271 3433 23 -227 -209 C ATOM 156 CD1BLEU A 19 41.201 33.481 27.694 0.50 18.51 C ANISOU 156 CD1BLEU A 19 2773 1784 2474 -184 779 -587 C ATOM 157 CD2ALEU A 19 40.547 33.647 28.307 0.50 24.53 C ANISOU 157 CD2ALEU A 19 2414 3269 3635 221 -140 672 C ATOM 158 CD2BLEU A 19 40.668 31.509 26.641 0.50 15.71 C ANISOU 158 CD2BLEU A 19 1613 1869 2484 -58 -1027 473 C ATOM 159 N LYS A 20 37.513 33.520 23.671 1.00 20.23 N ANISOU 159 N LYS A 20 2308 1955 3421 -729 -1122 789 N ATOM 160 CA LYS A 20 36.328 34.205 23.109 1.00 17.88 C ANISOU 160 CA LYS A 20 2219 1964 2607 -365 -938 741 C ATOM 161 C LYS A 20 35.070 33.857 23.886 1.00 17.07 C ANISOU 161 C LYS A 20 2129 1797 2556 -604 -1120 295 C ATOM 162 O LYS A 20 35.007 32.812 24.512 1.00 19.34 O ANISOU 162 O LYS A 20 2735 1836 2778 -439 -1127 670 O ATOM 163 CB LYS A 20 36.137 33.795 21.686 1.00 20.70 C ANISOU 163 CB LYS A 20 2550 2667 2648 -349 -652 768 C ATOM 164 CG LYS A 20 37.224 34.141 20.858 1.00 22.91 C ANISOU 164 CG LYS A 20 2741 2886 3077 -375 -467 781 C ATOM 165 CD LYS A 20 37.058 33.621 19.526 1.00 20.63 C ANISOU 165 CD LYS A 20 2421 2431 2985 -167 195 316 C ATOM 166 CE LYS A 20 38.024 34.263 18.584 1.00 27.61 C ANISOU 166 CE LYS A 20 3121 3971 3397 -61 120 707 C ATOM 167 NZ LYS A 20 37.605 35.541 18.134 1.00 25.91 N ANISOU 167 NZ LYS A 20 3438 3268 3135 -778 -293 690 N ATOM 168 N AGLU A 21 34.054 34.645 23.757 0.50 16.90 N ANISOU 168 N AGLU A 21 2188 1763 2467 -549 -1011 522 N ATOM 169 N BGLU A 21 34.002 34.643 23.669 0.50 17.10 N ANISOU 169 N BGLU A 21 2181 1862 2452 -447 -1063 390 N ATOM 170 CA AGLU A 21 32.820 34.252 24.177 0.50 15.90 C ANISOU 170 CA AGLU A 21 2119 1922 2000 -385 -886 251 C ATOM 171 CA BGLU A 21 32.684 34.357 24.231 0.50 16.10 C ANISOU 171 CA BGLU A 21 2280 1912 1925 -331 -890 262 C ATOM 172 C AGLU A 21 32.056 33.618 23.043 0.50 13.94 C ANISOU 172 C AGLU A 21 2102 1497 1695 -325 -790 421 C ATOM 173 C BGLU A 21 31.778 33.810 23.163 0.50 12.52 C ANISOU 173 C BGLU A 21 1480 1558 1718 -297 -654 195 C ATOM 174 O AGLU A 21 32.174 34.070 21.815 0.50 11.55 O ANISOU 174 O AGLU A 21 1370 1380 1639 -50 -324 -62 O ATOM 175 O BGLU A 21 31.626 34.403 22.168 0.50 10.50 O ANISOU 175 O BGLU A 21 1359 1343 1287 129 -248 213 O ATOM 176 CB AGLU A 21 32.025 35.452 24.767 0.50 17.73 C ANISOU 176 CB AGLU A 21 2362 2116 2257 -495 -805 -216 C ATOM 177 CB BGLU A 21 32.057 35.626 24.776 0.50 18.52 C ANISOU 177 CB BGLU A 21 2587 2063 2386 -429 -719 -123 C ATOM 178 CG AGLU A 21 32.740 36.131 26.034 0.50 19.06 C ANISOU 178 CG AGLU A 21 2367 2094 2780 -626 -1168 -248 C ATOM 179 CG BGLU A 21 30.733 35.411 25.410 0.50 19.19 C ANISOU 179 CG BGLU A 21 2865 2331 2092 -376 -629 -52 C ATOM 180 CD AGLU A 21 32.849 35.201 27.181 0.50 19.91 C ANISOU 180 CD AGLU A 21 2482 2308 2771 -294 -808 -307 C ATOM 181 CD BGLU A 21 30.248 36.632 26.247 0.50 24.59 C ANISOU 181 CD BGLU A 21 3313 2867 3162 -56 -264 -417 C ATOM 182 OE1AGLU A 21 33.949 34.909 27.552 0.50 18.25 O ANISOU 182 OE1AGLU A 21 2810 2298 1823 -306 -1317 370 O ATOM 183 OE1BGLU A 21 29.889 37.722 25.612 0.50 31.64 O ANISOU 183 OE1BGLU A 21 4446 3688 3887 -441 -283 601 O ATOM 184 OE2AGLU A 21 31.773 34.835 27.782 0.50 22.31 O ANISOU 184 OE2AGLU A 21 3113 3417 1945 -632 -813 -125 O ATOM 185 OE2BGLU A 21 30.107 36.482 27.566 0.50 27.19 O ANISOU 185 OE2BGLU A 21 3935 3297 3098 -196 -228 -485 O ATOM 186 N ALA A 22 31.225 32.651 23.384 1.00 12.59 N ANISOU 186 N ALA A 22 1849 1401 1531 -194 -380 243 N ATOM 187 CA ALA A 22 30.334 31.986 22.363 1.00 11.08 C ANISOU 187 CA ALA A 22 1562 1226 1420 -198 -365 126 C ATOM 188 C ALA A 22 29.057 31.509 22.993 1.00 11.70 C ANISOU 188 C ALA A 22 1691 1474 1279 -292 -302 329 C ATOM 189 O ALA A 22 29.012 31.196 24.174 1.00 13.28 O ANISOU 189 O ALA A 22 1884 1884 1276 -164 -470 294 O ATOM 190 CB ALA A 22 31.084 30.851 21.700 1.00 11.90 C ANISOU 190 CB ALA A 22 1541 1456 1525 -149 -364 196 C ATOM 191 N LEU A 23 28.027 31.359 22.169 1.00 10.64 N ANISOU 191 N LEU A 23 1410 1418 1213 -129 -357 60 N ATOM 192 CA LEU A 23 26.747 30.934 22.555 1.00 10.58 C ANISOU 192 CA LEU A 23 1559 1343 1117 -160 -295 -55 C ATOM 193 C LEU A 23 26.536 29.464 22.322 1.00 9.27 C ANISOU 193 C LEU A 23 1244 1202 1073 -43 -102 -104 C ATOM 194 O LEU A 23 26.706 28.956 21.217 1.00 10.54 O ANISOU 194 O LEU A 23 1614 1292 1098 -151 -92 -106 O ATOM 195 CB LEU A 23 25.728 31.732 21.731 1.00 11.16 C ANISOU 195 CB LEU A 23 1475 1507 1258 53 -244 -1 C ATOM 196 CG LEU A 23 24.261 31.532 21.950 1.00 11.73 C ANISOU 196 CG LEU A 23 1647 1330 1476 -105 -117 -57 C ATOM 197 CD1 LEU A 23 23.847 32.113 23.292 1.00 14.01 C ANISOU 197 CD1 LEU A 23 1903 2093 1327 127 29 76 C ATOM 198 CD2 LEU A 23 23.448 32.173 20.820 1.00 12.25 C ANISOU 198 CD2 LEU A 23 1655 1627 1369 32 -177 178 C ATOM 199 N LEU A 24 26.167 28.747 23.370 1.00 9.83 N ANISOU 199 N LEU A 24 1546 1246 940 -66 -201 -147 N ATOM 200 CA LEU A 24 25.804 27.311 23.210 1.00 9.65 C ANISOU 200 CA LEU A 24 1327 1398 941 75 -60 -57 C ATOM 201 C LEU A 24 24.456 27.233 22.520 1.00 9.90 C ANISOU 201 C LEU A 24 1124 1422 1215 76 -40 -156 C ATOM 202 O LEU A 24 23.464 27.683 23.030 1.00 10.55 O ANISOU 202 O LEU A 24 1416 1555 1037 13 -73 -245 O ATOM 203 CB LEU A 24 25.761 26.606 24.556 1.00 10.38 C ANISOU 203 CB LEU A 24 1581 1321 1040 49 -72 12 C ATOM 204 CG LEU A 24 27.005 26.692 25.428 1.00 11.77 C ANISOU 204 CG LEU A 24 1878 1448 1144 127 -398 110 C ATOM 205 CD1 LEU A 24 26.786 25.947 26.736 1.00 15.11 C ANISOU 205 CD1 LEU A 24 2469 1869 1399 127 -622 189 C ATOM 206 CD2 LEU A 24 28.214 26.124 24.701 1.00 14.24 C ANISOU 206 CD2 LEU A 24 1626 2034 1748 136 -577 -389 C ATOM 207 N ASP A 25 24.465 26.647 21.304 1.00 9.16 N ANISOU 207 N ASP A 25 1210 1133 1137 77 -173 -30 N ATOM 208 CA ASP A 25 23.340 26.812 20.393 1.00 8.39 C ANISOU 208 CA ASP A 25 1218 1203 766 39 -19 -18 C ATOM 209 C ASP A 25 22.846 25.472 19.860 1.00 8.33 C ANISOU 209 C ASP A 25 1065 1061 1037 45 -17 -12 C ATOM 210 O ASP A 25 23.339 24.932 18.863 1.00 8.65 O ANISOU 210 O ASP A 25 1219 1033 1034 82 96 -67 O ATOM 211 CB ASP A 25 23.793 27.733 19.249 1.00 9.39 C ANISOU 211 CB ASP A 25 1235 1253 1078 21 82 14 C ATOM 212 CG ASP A 25 22.718 28.138 18.307 1.00 10.38 C ANISOU 212 CG ASP A 25 1468 1240 1232 175 -38 63 C ATOM 213 OD1 ASP A 25 21.606 27.554 18.423 1.00 10.49 O ANISOU 213 OD1 ASP A 25 1268 1279 1437 101 -103 -106 O ATOM 214 OD2 ASP A 25 22.950 28.989 17.433 1.00 11.81 O ANISOU 214 OD2 ASP A 25 1433 1598 1454 125 -55 142 O ATOM 215 N THR A 26 21.859 24.905 20.562 1.00 8.41 N ANISOU 215 N THR A 26 1162 1085 949 0 96 -101 N ATOM 216 CA THR A 26 21.386 23.566 20.190 1.00 8.04 C ANISOU 216 CA THR A 26 1083 1070 899 -36 35 -40 C ATOM 217 C THR A 26 20.648 23.556 18.880 1.00 8.17 C ANISOU 217 C THR A 26 1111 1081 912 4 150 -6 C ATOM 218 O THR A 26 20.489 22.492 18.288 1.00 8.68 O ANISOU 218 O THR A 26 1293 1046 956 95 -5 -56 O ATOM 219 CB THR A 26 20.495 22.967 21.267 1.00 8.00 C ANISOU 219 CB THR A 26 1085 970 984 44 1 -56 C ATOM 220 OG1 THR A 26 19.409 23.844 21.563 1.00 8.69 O ANISOU 220 OG1 THR A 26 1158 1089 1053 115 63 -38 O ATOM 221 CG2 THR A 26 21.295 22.709 22.560 1.00 9.09 C ANISOU 221 CG2 THR A 26 1250 1139 1065 174 37 15 C ATOM 222 N GLY A 27 20.199 24.723 18.372 1.00 7.84 N ANISOU 222 N GLY A 27 1093 944 940 -5 96 -7 N ATOM 223 CA GLY A 27 19.612 24.838 17.068 1.00 8.65 C ANISOU 223 CA GLY A 27 1189 1097 999 55 -18 109 C ATOM 224 C GLY A 27 20.580 24.986 15.932 1.00 8.31 C ANISOU 224 C GLY A 27 1145 1055 957 128 23 51 C ATOM 225 O GLY A 27 20.132 25.123 14.773 1.00 9.35 O ANISOU 225 O GLY A 27 1198 1349 1006 88 -65 115 O ATOM 226 N ALA A 28 21.856 24.973 16.210 1.00 8.21 N ANISOU 226 N ALA A 28 1022 1168 928 135 64 10 N ATOM 227 CA ALA A 28 22.892 25.033 15.169 1.00 8.59 C ANISOU 227 CA ALA A 28 1209 1028 1027 142 19 67 C ATOM 228 C ALA A 28 23.503 23.665 14.958 1.00 7.71 C ANISOU 228 C ALA A 28 907 1054 968 -17 157 1 C ATOM 229 O ALA A 28 23.988 23.034 15.918 1.00 8.48 O ANISOU 229 O ALA A 28 1175 1100 945 85 -1 45 O ATOM 230 CB ALA A 28 23.972 25.991 15.571 1.00 8.31 C ANISOU 230 CB ALA A 28 1092 1150 915 151 12 87 C ATOM 231 N ASP A 29 23.492 23.160 13.718 1.00 8.50 N ANISOU 231 N ASP A 29 1231 1161 837 130 -1 -96 N ATOM 232 CA ASP A 29 24.191 21.928 13.416 1.00 9.24 C ANISOU 232 CA ASP A 29 1275 1238 995 95 212 -179 C ATOM 233 C ASP A 29 25.682 22.139 13.572 1.00 9.82 C ANISOU 233 C ASP A 29 1317 1267 1145 228 155 -186 C ATOM 234 O ASP A 29 26.423 21.208 13.962 1.00 10.77 O ANISOU 234 O ASP A 29 1393 1344 1354 284 20 -123 O ATOM 235 CB ASP A 29 23.934 21.480 11.973 1.00 10.16 C ANISOU 235 CB ASP A 29 1392 1320 1145 88 213 -234 C ATOM 236 CG ASP A 29 22.488 21.270 11.630 1.00 11.43 C ANISOU 236 CG ASP A 29 1568 1684 1089 68 -6 -116 C ATOM 237 OD1 ASP A 29 21.602 21.095 12.505 1.00 11.34 O ANISOU 237 OD1 ASP A 29 1464 1378 1466 113 -85 -25 O ATOM 238 OD2 ASP A 29 22.200 21.166 10.403 1.00 13.84 O ANISOU 238 OD2 ASP A 29 1748 2101 1407 -124 -113 -178 O ATOM 239 N ASP A 30 26.121 23.313 13.168 1.00 9.92 N ANISOU 239 N ASP A 30 1222 1348 1199 145 126 -71 N ATOM 240 CA ASP A 30 27.545 23.670 12.985 1.00 10.48 C ANISOU 240 CA ASP A 30 1304 1484 1191 210 186 62 C ATOM 241 C ASP A 30 27.963 24.783 13.918 1.00 10.14 C ANISOU 241 C ASP A 30 1274 1301 1276 102 68 169 C ATOM 242 O ASP A 30 27.174 25.630 14.287 1.00 11.06 O ANISOU 242 O ASP A 30 1136 1408 1655 139 35 -38 O ATOM 243 CB ASP A 30 27.790 24.095 11.544 1.00 12.80 C ANISOU 243 CB ASP A 30 1383 1933 1548 46 268 178 C ATOM 244 CG ASP A 30 27.304 23.090 10.567 1.00 16.56 C ANISOU 244 CG ASP A 30 1789 2807 1695 129 -48 3 C ATOM 245 OD1 ASP A 30 27.611 21.936 10.719 1.00 20.66 O ANISOU 245 OD1 ASP A 30 2666 2843 2339 23 391 -554 O ATOM 246 OD2 ASP A 30 26.521 23.392 9.651 1.00 29.18 O ANISOU 246 OD2 ASP A 30 3268 5742 2075 1169 -580 -868 O ATOM 247 N THR A 31 29.260 24.806 14.222 1.00 10.81 N ANISOU 247 N THR A 31 1187 1462 1455 279 -14 -185 N ATOM 248 CA THR A 31 29.929 25.874 14.976 1.00 9.68 C ANISOU 248 CA THR A 31 1241 1267 1167 192 88 62 C ATOM 249 C THR A 31 30.409 26.961 14.006 1.00 10.39 C ANISOU 249 C THR A 31 1227 1409 1309 142 66 235 C ATOM 250 O THR A 31 31.077 26.652 13.017 1.00 11.54 O ANISOU 250 O THR A 31 1388 1600 1395 219 354 176 O ATOM 251 CB THR A 31 31.070 25.255 15.742 1.00 9.79 C ANISOU 251 CB THR A 31 1036 1314 1369 113 165 96 C ATOM 252 OG1 THR A 31 30.521 24.363 16.716 1.00 10.39 O ANISOU 252 OG1 THR A 31 1155 1290 1501 133 30 292 O ATOM 253 CG2 THR A 31 31.896 26.279 16.453 1.00 11.59 C ANISOU 253 CG2 THR A 31 1106 1569 1728 0 10 329 C ATOM 254 N VAL A 32 29.989 28.192 14.273 1.00 10.02 N ANISOU 254 N VAL A 32 1147 1289 1369 101 126 84 N ATOM 255 CA VAL A 32 30.273 29.340 13.384 1.00 9.86 C ANISOU 255 CA VAL A 32 1187 1260 1297 93 128 208 C ATOM 256 C VAL A 32 30.794 30.447 14.228 1.00 10.43 C ANISOU 256 C VAL A 32 1443 1124 1394 31 -20 204 C ATOM 257 O VAL A 32 30.123 30.918 15.153 1.00 10.70 O ANISOU 257 O VAL A 32 1323 1322 1419 -19 61 144 O ATOM 258 CB VAL A 32 29.035 29.788 12.591 1.00 9.96 C ANISOU 258 CB VAL A 32 1226 1391 1165 142 78 182 C ATOM 259 CG1 VAL A 32 29.472 30.685 11.457 1.00 11.45 C ANISOU 259 CG1 VAL A 32 1505 1679 1165 218 -24 188 C ATOM 260 CG2 VAL A 32 28.280 28.616 12.052 1.00 11.48 C ANISOU 260 CG2 VAL A 32 1199 1669 1493 289 51 93 C ATOM 261 N LEU A 33 32.020 30.890 13.917 1.00 10.63 N ANISOU 261 N LEU A 33 1283 1262 1493 -48 102 183 N ATOM 262 CA LEU A 33 32.664 31.982 14.629 1.00 10.43 C ANISOU 262 CA LEU A 33 1263 1393 1305 76 118 298 C ATOM 263 C LEU A 33 32.821 33.187 13.708 1.00 10.99 C ANISOU 263 C LEU A 33 1199 1540 1434 67 -61 137 C ATOM 264 O LEU A 33 32.975 33.045 12.513 1.00 11.39 O ANISOU 264 O LEU A 33 1364 1582 1380 -11 -35 346 O ATOM 265 CB LEU A 33 34.034 31.555 15.158 1.00 11.75 C ANISOU 265 CB LEU A 33 1272 1483 1710 51 -56 462 C ATOM 266 CG LEU A 33 34.038 30.342 16.075 1.00 13.47 C ANISOU 266 CG LEU A 33 1540 1817 1759 310 -77 383 C ATOM 267 CD1 LEU A 33 35.442 30.092 16.586 1.00 15.13 C ANISOU 267 CD1 LEU A 33 1855 1648 2242 192 -274 549 C ATOM 268 CD2 LEU A 33 33.078 30.477 17.215 1.00 14.00 C ANISOU 268 CD2 LEU A 33 2129 1790 1397 -26 -204 390 C ATOM 269 N GLU A 34 32.767 34.347 14.319 1.00 11.96 N ANISOU 269 N GLU A 34 1540 1314 1689 -101 -64 221 N ATOM 270 CA GLU A 34 33.059 35.623 13.638 1.00 13.57 C ANISOU 270 CA GLU A 34 1652 1630 1872 -22 -190 530 C ATOM 271 C GLU A 34 34.468 35.634 13.124 1.00 14.26 C ANISOU 271 C GLU A 34 1664 1672 2080 -334 -156 550 C ATOM 272 O GLU A 34 35.351 34.823 13.564 1.00 15.97 O ANISOU 272 O GLU A 34 1684 1923 2461 -260 -268 790 O ATOM 273 CB GLU A 34 32.847 36.786 14.626 1.00 16.99 C ANISOU 273 CB GLU A 34 2329 1791 2335 -516 -138 490 C ATOM 274 CG GLU A 34 31.411 36.889 15.194 1.00 19.71 C ANISOU 274 CG GLU A 34 2713 2115 2660 -218 49 232 C ATOM 275 CD GLU A 34 31.191 38.118 15.959 1.00 26.10 C ANISOU 275 CD GLU A 34 4464 2405 3046 -250 21 205 C ATOM 276 OE1 GLU A 34 30.475 39.176 15.395 1.00 26.28 O ANISOU 276 OE1 GLU A 34 4027 2351 3605 -599 -140 243 O ATOM 277 OE2 GLU A 34 31.700 38.176 17.047 1.00 29.34 O ANISOU 277 OE2 GLU A 34 5408 2603 3137 -561 -732 305 O ATOM 278 N GLU A 35 34.698 36.514 12.175 1.00 16.36 N ANISOU 278 N GLU A 35 1669 2015 2531 -324 -132 996 N ATOM 279 CA GLU A 35 35.990 36.650 11.528 1.00 17.77 C ANISOU 279 CA GLU A 35 2129 2233 2388 -136 -72 817 C ATOM 280 C GLU A 35 37.135 36.609 12.473 1.00 16.71 C ANISOU 280 C GLU A 35 1935 2005 2409 -341 -130 562 C ATOM 281 O GLU A 35 37.159 37.301 13.446 1.00 19.45 O ANISOU 281 O GLU A 35 2119 2216 3054 -492 -289 377 O ATOM 282 CB GLU A 35 36.047 37.946 10.703 1.00 19.52 C ANISOU 282 CB GLU A 35 2215 2276 2923 -295 -46 1122 C ATOM 283 CG GLU A 35 37.436 38.255 10.102 1.00 26.36 C ANISOU 283 CG GLU A 35 2908 3309 3797 -477 496 1166 C ATOM 284 CD GLU A 35 37.994 37.106 9.206 1.00 34.20 C ANISOU 284 CD GLU A 35 4782 4590 3621 -323 156 159 C ATOM 285 OE1 GLU A 35 37.193 36.358 8.636 1.00 37.42 O ANISOU 285 OE1 GLU A 35 5521 4992 3703 -713 161 229 O ATOM 286 OE2 GLU A 35 39.302 36.994 9.056 1.00 43.68 O ANISOU 286 OE2 GLU A 35 5125 5852 5618 -201 356 -146 O ATOM 287 N MET A 36 38.071 35.717 12.179 1.00 18.40 N ANISOU 287 N MET A 36 1903 2161 2925 -467 -76 494 N ATOM 288 CA MET A 36 39.325 35.509 12.967 1.00 19.59 C ANISOU 288 CA MET A 36 2029 2473 2941 -508 -356 319 C ATOM 289 C MET A 36 40.285 34.749 12.085 1.00 21.04 C ANISOU 289 C MET A 36 2186 2924 2884 -403 -316 346 C ATOM 290 O MET A 36 39.923 34.228 11.096 1.00 20.86 O ANISOU 290 O MET A 36 1756 3499 2669 -93 -90 247 O ATOM 291 CB MET A 36 39.040 34.723 14.206 1.00 18.89 C ANISOU 291 CB MET A 36 2321 2023 2831 -415 -355 284 C ATOM 292 CG MET A 36 38.683 33.296 13.972 1.00 17.19 C ANISOU 292 CG MET A 36 1765 2170 2597 -169 -157 625 C ATOM 293 SD MET A 36 38.555 32.305 15.425 1.00 20.88 S ANISOU 293 SD MET A 36 2177 2364 3392 -174 319 551 S ATOM 294 CE MET A 36 40.313 32.377 16.087 1.00 19.79 C ANISOU 294 CE MET A 36 2257 2640 2620 -129 286 651 C ATOM 295 N ASN A 37 41.582 34.807 12.419 1.00 21.74 N ANISOU 295 N ASN A 37 2096 2869 3295 -339 -211 411 N ATOM 296 CA ASN A 37 42.570 33.987 11.732 1.00 21.71 C ANISOU 296 CA ASN A 37 2469 2807 2972 -340 84 586 C ATOM 297 C ASN A 37 42.726 32.644 12.445 1.00 20.22 C ANISOU 297 C ASN A 37 2136 2806 2741 196 -41 481 C ATOM 298 O ASN A 37 42.709 32.595 13.651 1.00 20.97 O ANISOU 298 O ASN A 37 2061 3246 2658 164 407 536 O ATOM 299 CB ASN A 37 43.900 34.715 11.669 1.00 25.14 C ANISOU 299 CB ASN A 37 2422 3566 3564 -505 187 693 C ATOM 300 CG ASN A 37 43.805 36.057 10.895 1.00 27.66 C ANISOU 300 CG ASN A 37 3322 3403 3784 -632 159 595 C ATOM 301 OD1 ASN A 37 44.126 37.178 11.454 1.00 35.11 O ANISOU 301 OD1 ASN A 37 4821 3589 4929 -729 355 269 O ATOM 302 ND2 ASN A 37 43.404 35.980 9.690 1.00 30.91 N ANISOU 302 ND2 ASN A 37 3348 4619 3777 -540 123 937 N ATOM 303 N LEU A 38 42.770 31.587 11.682 1.00 19.08 N ANISOU 303 N LEU A 38 1769 3060 2417 -13 -240 514 N ATOM 304 CA LEU A 38 43.145 30.242 12.191 1.00 20.76 C ANISOU 304 CA LEU A 38 2193 2897 2795 112 -204 158 C ATOM 305 C LEU A 38 44.216 29.639 11.276 1.00 20.91 C ANISOU 305 C LEU A 38 2416 3394 2133 14 -386 -124 C ATOM 306 O LEU A 38 44.149 29.752 10.093 1.00 23.11 O ANISOU 306 O LEU A 38 1682 4568 2530 174 -314 5 O ATOM 307 CB LEU A 38 41.915 29.296 12.215 1.00 21.98 C ANISOU 307 CB LEU A 38 2484 3196 2669 52 55 -59 C ATOM 308 CG LEU A 38 40.893 29.505 13.284 1.00 21.42 C ANISOU 308 CG LEU A 38 2430 3434 2273 -149 -86 -78 C ATOM 309 CD1 LEU A 38 39.650 28.635 13.067 1.00 20.59 C ANISOU 309 CD1 LEU A 38 2965 2729 2128 -130 -306 592 C ATOM 310 CD2 LEU A 38 41.500 29.256 14.649 1.00 21.38 C ANISOU 310 CD2 LEU A 38 3179 2729 2215 -208 8 -343 C ATOM 311 N PRO A 39 45.081 28.825 11.834 1.00 25.42 N ANISOU 311 N PRO A 39 2598 3843 3215 347 -437 -318 N ATOM 312 CA PRO A 39 46.090 28.159 11.052 1.00 26.48 C ANISOU 312 CA PRO A 39 2840 3798 3422 238 -352 -351 C ATOM 313 C PRO A 39 45.562 27.031 10.171 1.00 25.01 C ANISOU 313 C PRO A 39 2645 3447 3410 261 -191 -316 C ATOM 314 O PRO A 39 44.673 26.312 10.562 1.00 27.21 O ANISOU 314 O PRO A 39 2537 4103 3698 203 -219 -258 O ATOM 315 CB PRO A 39 47.070 27.607 12.120 1.00 27.82 C ANISOU 315 CB PRO A 39 2915 3806 3847 131 -857 -435 C ATOM 316 CG PRO A 39 46.598 28.174 13.455 1.00 29.92 C ANISOU 316 CG PRO A 39 3283 3816 4267 564 -351 -214 C ATOM 317 CD PRO A 39 45.194 28.542 13.275 1.00 25.52 C ANISOU 317 CD PRO A 39 3003 3292 3399 442 -649 -117 C ATOM 318 N GLY A 40 46.273 26.771 9.080 1.00 26.67 N ANISOU 318 N GLY A 40 2544 3786 3802 -11 -131 -434 N ATOM 319 CA GLY A 40 46.069 25.598 8.306 1.00 27.90 C ANISOU 319 CA GLY A 40 3076 3764 3757 99 -9 -439 C ATOM 320 C GLY A 40 45.135 25.804 7.129 1.00 25.39 C ANISOU 320 C GLY A 40 2459 3638 3550 220 160 -477 C ATOM 321 O GLY A 40 44.690 26.967 6.791 1.00 26.01 O ANISOU 321 O GLY A 40 2498 3598 3785 -206 198 -458 O ATOM 322 N LYS A 41 44.866 24.735 6.474 1.00 25.54 N ANISOU 322 N LYS A 41 2300 3559 3843 444 -29 -379 N ATOM 323 CA LYS A 41 44.077 24.731 5.314 1.00 24.79 C ANISOU 323 CA LYS A 41 2387 3698 3332 438 162 -450 C ATOM 324 C LYS A 41 42.588 25.015 5.658 1.00 22.94 C ANISOU 324 C LYS A 41 2003 3402 3311 519 307 -88 C ATOM 325 O LYS A 41 42.093 24.657 6.796 1.00 24.65 O ANISOU 325 O LYS A 41 2789 3511 3063 344 -235 136 O ATOM 326 CB LYS A 41 44.194 23.364 4.616 1.00 27.25 C ANISOU 326 CB LYS A 41 2722 3694 3936 792 -57 -493 C ATOM 327 N TRP A 42 41.906 25.708 4.761 1.00 20.48 N ANISOU 327 N TRP A 42 1868 3528 2383 -113 299 -34 N ATOM 328 CA TRP A 42 40.471 25.831 4.864 1.00 17.40 C ANISOU 328 CA TRP A 42 1587 2739 2285 16 285 131 C ATOM 329 C TRP A 42 39.828 25.668 3.497 1.00 18.14 C ANISOU 329 C TRP A 42 1829 2975 2086 145 374 31 C ATOM 330 O TRP A 42 40.511 25.744 2.470 1.00 20.51 O ANISOU 330 O TRP A 42 2218 3467 2106 13 632 -142 O ATOM 331 CB TRP A 42 40.076 27.165 5.499 1.00 17.80 C ANISOU 331 CB TRP A 42 2176 2722 1862 -284 158 -6 C ATOM 332 CG TRP A 42 40.619 28.413 4.760 1.00 18.54 C ANISOU 332 CG TRP A 42 1923 3094 2025 -59 134 177 C ATOM 333 CD1 TRP A 42 41.801 28.989 4.950 1.00 22.42 C ANISOU 333 CD1 TRP A 42 2500 3955 2061 -603 -78 196 C ATOM 334 CD2 TRP A 42 39.995 29.117 3.696 1.00 17.55 C ANISOU 334 CD2 TRP A 42 2215 2862 1592 -53 833 138 C ATOM 335 NE1 TRP A 42 41.933 30.073 4.151 1.00 22.53 N ANISOU 335 NE1 TRP A 42 2606 3371 2583 -732 73 176 N ATOM 336 CE2 TRP A 42 40.848 30.138 3.322 1.00 19.64 C ANISOU 336 CE2 TRP A 42 2109 3119 2234 -19 687 268 C ATOM 337 CE3 TRP A 42 38.789 29.015 3.073 1.00 17.18 C ANISOU 337 CE3 TRP A 42 2207 2386 1931 123 570 -204 C ATOM 338 CZ2 TRP A 42 40.491 31.095 2.357 1.00 22.13 C ANISOU 338 CZ2 TRP A 42 3246 2732 2429 -605 216 273 C ATOM 339 CZ3 TRP A 42 38.447 29.930 2.088 1.00 20.03 C ANISOU 339 CZ3 TRP A 42 2776 2749 2082 -189 34 69 C ATOM 340 CH2 TRP A 42 39.281 30.946 1.756 1.00 21.14 C ANISOU 340 CH2 TRP A 42 3227 3110 1695 -255 563 178 C ATOM 341 N LYS A 43 38.530 25.368 3.481 1.00 16.57 N ANISOU 341 N LYS A 43 1730 2568 1995 295 272 -24 N ATOM 342 CA LYS A 43 37.784 25.272 2.263 1.00 18.91 C ANISOU 342 CA LYS A 43 2093 2902 2189 508 112 -57 C ATOM 343 C LYS A 43 36.677 26.281 2.281 1.00 16.98 C ANISOU 343 C LYS A 43 1793 2467 2191 435 304 -103 C ATOM 344 O LYS A 43 36.012 26.458 3.269 1.00 16.53 O ANISOU 344 O LYS A 43 1833 2607 1840 405 454 0 O ATOM 345 CB LYS A 43 37.225 23.898 2.129 1.00 24.19 C ANISOU 345 CB LYS A 43 2905 3140 3146 512 -233 -447 C ATOM 346 N PRO A 44 36.377 26.858 1.126 1.00 16.62 N ANISOU 346 N PRO A 44 1626 2822 1865 453 273 -160 N ATOM 347 CA PRO A 44 35.176 27.666 1.004 1.00 16.12 C ANISOU 347 CA PRO A 44 1659 2405 2059 325 84 -74 C ATOM 348 C PRO A 44 33.929 26.831 1.098 1.00 16.08 C ANISOU 348 C PRO A 44 1886 2076 2144 261 258 34 C ATOM 349 O PRO A 44 33.823 25.799 0.471 1.00 18.72 O ANISOU 349 O PRO A 44 1852 2612 2647 258 317 -464 O ATOM 350 CB PRO A 44 35.302 28.262 -0.399 1.00 17.89 C ANISOU 350 CB PRO A 44 2178 2450 2168 171 496 213 C ATOM 351 CG PRO A 44 36.699 28.037 -0.837 1.00 20.86 C ANISOU 351 CG PRO A 44 2591 3625 1709 405 524 -44 C ATOM 352 CD PRO A 44 37.216 26.876 -0.079 1.00 18.30 C ANISOU 352 CD PRO A 44 1844 3203 1903 343 181 -297 C ATOM 353 N LYS A 45 32.960 27.292 1.884 1.00 14.76 N ANISOU 353 N LYS A 45 1726 2039 1841 206 5 -377 N ATOM 354 CA LYS A 45 31.672 26.614 2.032 1.00 14.58 C ANISOU 354 CA LYS A 45 1824 2015 1700 215 -17 -386 C ATOM 355 C LYS A 45 30.576 27.697 2.122 1.00 13.40 C ANISOU 355 C LYS A 45 1749 1819 1521 170 -56 -409 C ATOM 356 O LYS A 45 30.877 28.890 2.350 1.00 14.14 O ANISOU 356 O LYS A 45 1559 1859 1952 220 22 -230 O ATOM 357 CB LYS A 45 31.665 25.726 3.266 1.00 18.03 C ANISOU 357 CB LYS A 45 2280 1997 2574 391 -186 -28 C ATOM 358 CG LYS A 45 32.634 24.460 3.145 1.00 24.24 C ANISOU 358 CG LYS A 45 2673 2825 3712 498 -366 77 C ATOM 359 CD LYS A 45 32.063 23.377 2.296 1.00 27.54 C ANISOU 359 CD LYS A 45 3181 3004 4277 508 -122 -207 C ATOM 360 CE LYS A 45 32.953 22.065 2.333 1.00 28.24 C ANISOU 360 CE LYS A 45 3775 2674 4279 450 53 -263 C ATOM 361 NZ LYS A 45 32.731 21.251 1.084 1.00 39.83 N ANISOU 361 NZ LYS A 45 5741 4177 5215 53 -558 -916 N ATOM 362 N MET A 46 29.358 27.260 1.998 1.00 13.14 N ANISOU 362 N MET A 46 1737 1829 1427 161 -31 -288 N ATOM 363 CA MET A 46 28.178 28.123 2.243 1.00 13.59 C ANISOU 363 CA MET A 46 1745 1681 1738 190 114 -146 C ATOM 364 C MET A 46 27.286 27.454 3.219 1.00 13.33 C ANISOU 364 C MET A 46 1737 1519 1808 141 172 -55 C ATOM 365 O MET A 46 27.165 26.243 3.223 1.00 15.98 O ANISOU 365 O MET A 46 2045 1608 2418 184 519 -220 O ATOM 366 CB MET A 46 27.428 28.373 0.937 1.00 13.92 C ANISOU 366 CB MET A 46 1650 1826 1810 325 -105 -249 C ATOM 367 CG MET A 46 28.192 29.272 0.003 1.00 15.83 C ANISOU 367 CG MET A 46 2240 2473 1300 144 -67 -224 C ATOM 368 SD MET A 46 27.339 29.508 -1.542 1.00 19.09 S ANISOU 368 SD MET A 46 2837 2662 1754 210 -396 -349 S ATOM 369 CE MET A 46 25.876 30.430 -0.989 1.00 20.19 C ANISOU 369 CE MET A 46 2870 2803 1999 797 -306 -124 C ATOM 370 N AILE A 47 26.614 28.259 4.045 0.50 11.47 N ANISOU 370 N AILE A 47 1322 1568 1466 119 37 -16 N ATOM 371 N BILE A 47 26.684 28.244 4.130 0.50 11.95 N ANISOU 371 N BILE A 47 1526 1581 1433 172 138 27 N ATOM 372 CA AILE A 47 25.721 27.757 5.045 0.50 12.92 C ANISOU 372 CA AILE A 47 1587 1489 1832 117 146 -136 C ATOM 373 CA BILE A 47 25.632 27.730 5.008 0.50 12.13 C ANISOU 373 CA BILE A 47 1575 1368 1666 160 110 -196 C ATOM 374 C AILE A 47 24.520 28.717 5.159 0.50 12.79 C ANISOU 374 C AILE A 47 1565 1636 1658 168 49 -15 C ATOM 375 C BILE A 47 24.480 28.684 5.063 0.50 12.05 C ANISOU 375 C BILE A 47 1450 1594 1531 185 -100 -57 C ATOM 376 O AILE A 47 24.661 29.907 4.948 0.50 12.70 O ANISOU 376 O AILE A 47 1515 1479 1829 209 149 27 O ATOM 377 O BILE A 47 24.657 29.887 4.910 0.50 12.53 O ANISOU 377 O BILE A 47 1510 1464 1785 249 187 15 O ATOM 378 CB AILE A 47 26.460 27.598 6.438 0.50 13.91 C ANISOU 378 CB AILE A 47 1762 1698 1825 259 231 -90 C ATOM 379 CB BILE A 47 26.165 27.442 6.474 0.50 11.48 C ANISOU 379 CB BILE A 47 1425 1295 1641 338 249 -167 C ATOM 380 CG1AILE A 47 25.631 26.829 7.391 0.50 16.03 C ANISOU 380 CG1AILE A 47 1554 2103 2430 -161 193 2 C ATOM 381 CG1BILE A 47 26.745 28.728 7.117 0.50 11.13 C ANISOU 381 CG1BILE A 47 1438 1467 1321 270 52 99 C ATOM 382 CG2AILE A 47 26.807 28.962 7.058 0.50 16.42 C ANISOU 382 CG2AILE A 47 2124 2055 2059 181 71 -45 C ATOM 383 CG2BILE A 47 27.195 26.398 6.444 0.50 12.59 C ANISOU 383 CG2BILE A 47 1260 1439 2085 219 -22 104 C ATOM 384 CD1AILE A 47 26.404 26.234 8.490 0.50 18.22 C ANISOU 384 CD1AILE A 47 2278 2312 2331 -155 276 248 C ATOM 385 CD1BILE A 47 26.915 28.692 8.641 0.50 11.62 C ANISOU 385 CD1BILE A 47 1507 1619 1286 194 0 63 C ATOM 386 N GLY A 48 23.357 28.156 5.461 1.00 12.00 N ANISOU 386 N GLY A 48 1530 1500 1530 123 57 -17 N ATOM 387 CA GLY A 48 22.140 28.930 5.627 1.00 12.49 C ANISOU 387 CA GLY A 48 1436 1594 1714 56 51 48 C ATOM 388 C GLY A 48 21.682 28.998 7.054 1.00 10.90 C ANISOU 388 C GLY A 48 1510 1446 1186 103 58 141 C ATOM 389 O GLY A 48 21.710 28.020 7.754 1.00 13.65 O ANISOU 389 O GLY A 48 2212 1465 1509 255 80 106 O ATOM 390 N GLY A 49 21.127 30.125 7.401 1.00 12.17 N ANISOU 390 N GLY A 49 1494 1649 1481 304 28 249 N ATOM 391 CA GLY A 49 20.531 30.386 8.694 1.00 11.10 C ANISOU 391 CA GLY A 49 1370 1496 1348 281 43 287 C ATOM 392 C GLY A 49 19.125 30.987 8.484 1.00 11.19 C ANISOU 392 C GLY A 49 1573 1586 1090 255 -25 257 C ATOM 393 O GLY A 49 18.503 30.806 7.401 1.00 12.43 O ANISOU 393 O GLY A 49 1507 1835 1378 308 -79 -5 O ATOM 394 N ILE A 50 18.607 31.602 9.501 1.00 10.19 N ANISOU 394 N ILE A 50 1296 1372 1204 225 -76 202 N ATOM 395 CA ILE A 50 17.245 32.068 9.435 1.00 10.92 C ANISOU 395 CA ILE A 50 1388 1290 1471 189 103 103 C ATOM 396 C ILE A 50 17.054 33.106 8.329 1.00 11.50 C ANISOU 396 C ILE A 50 1373 1480 1517 240 -90 118 C ATOM 397 O ILE A 50 15.949 33.258 7.803 1.00 12.89 O ANISOU 397 O ILE A 50 1286 2034 1576 315 -147 72 O ATOM 398 CB ILE A 50 16.762 32.604 10.811 1.00 12.62 C ANISOU 398 CB ILE A 50 1500 1744 1548 337 -7 158 C ATOM 399 CG1 ILE A 50 15.244 32.402 10.939 1.00 13.79 C ANISOU 399 CG1 ILE A 50 1463 2360 1417 355 43 359 C ATOM 400 CG2 ILE A 50 17.244 34.025 11.037 1.00 14.24 C ANISOU 400 CG2 ILE A 50 2009 1742 1656 538 -159 37 C ATOM 401 CD1 ILE A 50 14.670 32.795 12.264 1.00 16.34 C ANISOU 401 CD1 ILE A 50 1808 2733 1667 608 -40 449 C ATOM 402 N GLY A 51 18.093 33.877 8.024 1.00 12.09 N ANISOU 402 N GLY A 51 1369 1495 1728 193 -117 311 N ATOM 403 CA GLY A 51 17.999 35.016 7.146 1.00 12.75 C ANISOU 403 CA GLY A 51 1534 1597 1711 182 -62 192 C ATOM 404 C GLY A 51 18.533 34.794 5.785 1.00 13.69 C ANISOU 404 C GLY A 51 1570 1745 1887 188 -112 259 C ATOM 405 O GLY A 51 18.530 35.731 4.983 1.00 16.49 O ANISOU 405 O GLY A 51 2647 1787 1831 414 392 435 O ATOM 406 N GLY A 52 18.975 33.583 5.460 1.00 12.96 N ANISOU 406 N GLY A 52 1657 1673 1591 241 -147 113 N ATOM 407 CA GLY A 52 19.580 33.270 4.143 1.00 15.11 C ANISOU 407 CA GLY A 52 1764 2319 1656 119 -157 -11 C ATOM 408 C GLY A 52 20.961 32.649 4.313 1.00 11.45 C ANISOU 408 C GLY A 52 1378 1630 1340 72 -157 96 C ATOM 409 O GLY A 52 21.323 32.162 5.367 1.00 13.35 O ANISOU 409 O GLY A 52 1790 1917 1362 484 -105 274 O ATOM 410 N PHE A 53 21.719 32.715 3.235 1.00 11.37 N ANISOU 410 N PHE A 53 1501 1693 1125 73 -253 48 N ATOM 411 CA PHE A 53 22.973 32.032 3.102 1.00 10.60 C ANISOU 411 CA PHE A 53 1484 1388 1152 16 25 -43 C ATOM 412 C PHE A 53 24.141 32.987 3.193 1.00 10.82 C ANISOU 412 C PHE A 53 1625 1361 1123 144 111 0 C ATOM 413 O PHE A 53 24.081 34.093 2.717 1.00 12.42 O ANISOU 413 O PHE A 53 1673 1554 1492 32 -279 185 O ATOM 414 CB PHE A 53 23.017 31.226 1.805 1.00 13.29 C ANISOU 414 CB PHE A 53 2004 1620 1426 38 -264 -405 C ATOM 415 CG PHE A 53 22.251 29.989 1.874 1.00 14.51 C ANISOU 415 CG PHE A 53 2196 1904 1413 80 -434 -286 C ATOM 416 CD1 PHE A 53 20.855 29.994 1.857 1.00 15.65 C ANISOU 416 CD1 PHE A 53 2140 2096 1708 -295 -405 -103 C ATOM 417 CD2 PHE A 53 22.898 28.798 2.053 1.00 15.67 C ANISOU 417 CD2 PHE A 53 2390 1834 1729 186 -457 -374 C ATOM 418 CE1 PHE A 53 20.145 28.860 2.083 1.00 18.18 C ANISOU 418 CE1 PHE A 53 2438 2455 2012 -157 -942 -101 C ATOM 419 CE2 PHE A 53 22.157 27.587 2.147 1.00 18.77 C ANISOU 419 CE2 PHE A 53 2767 1829 2534 135 -385 -288 C ATOM 420 CZ PHE A 53 20.801 27.659 2.229 1.00 18.35 C ANISOU 420 CZ PHE A 53 2828 1837 2306 -412 -834 -298 C ATOM 421 N ILE A 54 25.249 32.475 3.756 1.00 10.69 N ANISOU 421 N ILE A 54 1450 1336 1273 99 -98 -50 N ATOM 422 CA ILE A 54 26.504 33.162 3.817 1.00 10.77 C ANISOU 422 CA ILE A 54 1300 1547 1244 95 -44 -57 C ATOM 423 C ILE A 54 27.643 32.272 3.359 1.00 10.93 C ANISOU 423 C ILE A 54 1431 1456 1265 136 -52 84 C ATOM 424 O ILE A 54 27.529 31.043 3.330 1.00 11.77 O ANISOU 424 O ILE A 54 1458 1511 1502 104 170 -160 O ATOM 425 CB ILE A 54 26.799 33.684 5.294 1.00 10.94 C ANISOU 425 CB ILE A 54 1440 1225 1489 43 -41 -52 C ATOM 426 CG1 ILE A 54 26.981 32.499 6.274 1.00 10.79 C ANISOU 426 CG1 ILE A 54 1374 1572 1154 -62 199 -71 C ATOM 427 CG2 ILE A 54 25.727 34.626 5.767 1.00 12.19 C ANISOU 427 CG2 ILE A 54 1735 1436 1460 188 189 11 C ATOM 428 CD1 ILE A 54 27.571 32.927 7.581 1.00 11.45 C ANISOU 428 CD1 ILE A 54 1328 1659 1361 -20 62 -29 C ATOM 429 N LYS A 55 28.744 32.912 2.999 1.00 10.89 N ANISOU 429 N LYS A 55 1455 1484 1197 111 141 167 N ATOM 430 CA LYS A 55 29.984 32.258 2.741 1.00 11.78 C ANISOU 430 CA LYS A 55 1477 1615 1381 113 -4 44 C ATOM 431 C LYS A 55 30.814 32.183 4.001 1.00 11.28 C ANISOU 431 C LYS A 55 1531 1563 1192 95 83 9 C ATOM 432 O LYS A 55 30.868 33.115 4.762 1.00 13.06 O ANISOU 432 O LYS A 55 1812 1717 1433 96 -205 -29 O ATOM 433 CB LYS A 55 30.781 32.994 1.660 1.00 12.60 C ANISOU 433 CB LYS A 55 1578 1748 1459 85 -27 118 C ATOM 434 CG LYS A 55 30.100 32.998 0.307 1.00 15.31 C ANISOU 434 CG LYS A 55 1854 2453 1509 131 -34 154 C ATOM 435 CD LYS A 55 30.691 34.017 -0.642 1.00 18.61 C ANISOU 435 CD LYS A 55 2581 2797 1693 273 446 180 C ATOM 436 CE LYS A 55 32.068 33.732 -0.973 1.00 21.97 C ANISOU 436 CE LYS A 55 2747 3413 2186 32 803 633 C ATOM 437 NZ LYS A 55 32.607 34.726 -1.947 1.00 28.59 N ANISOU 437 NZ LYS A 55 3868 4362 2630 -201 1414 732 N ATOM 438 N VAL A 56 31.389 31.022 4.250 1.00 11.48 N ANISOU 438 N VAL A 56 1476 1614 1270 101 45 -68 N ATOM 439 CA VAL A 56 32.262 30.783 5.368 1.00 11.33 C ANISOU 439 CA VAL A 56 1299 1617 1388 88 -148 110 C ATOM 440 C VAL A 56 33.556 30.087 4.887 1.00 13.60 C ANISOU 440 C VAL A 56 1661 1804 1700 11 -18 -138 C ATOM 441 O VAL A 56 33.617 29.495 3.807 1.00 14.57 O ANISOU 441 O VAL A 56 1550 2213 1771 238 73 -60 O ATOM 442 CB VAL A 56 31.565 29.890 6.474 1.00 12.18 C ANISOU 442 CB VAL A 56 1421 1879 1325 114 109 90 C ATOM 443 CG1 VAL A 56 30.416 30.614 7.050 1.00 13.28 C ANISOU 443 CG1 VAL A 56 1457 1976 1613 -127 208 298 C ATOM 444 CG2 VAL A 56 31.165 28.535 5.935 1.00 13.59 C ANISOU 444 CG2 VAL A 56 1665 1940 1556 -30 229 341 C ATOM 445 N ARG A 57 34.535 30.131 5.768 1.00 12.36 N ANISOU 445 N ARG A 57 1395 1856 1445 33 107 41 N ATOM 446 CA ARG A 57 35.747 29.317 5.648 1.00 12.54 C ANISOU 446 CA ARG A 57 1269 2070 1426 139 19 139 C ATOM 447 C ARG A 57 35.633 28.150 6.602 1.00 13.16 C ANISOU 447 C ARG A 57 1198 1999 1802 70 200 123 C ATOM 448 O ARG A 57 35.399 28.336 7.783 1.00 13.25 O ANISOU 448 O ARG A 57 1460 1904 1669 124 369 207 O ATOM 449 CB ARG A 57 37.002 30.155 6.009 1.00 14.02 C ANISOU 449 CB ARG A 57 1337 2270 1719 171 315 248 C ATOM 450 CG ARG A 57 37.164 31.460 5.161 1.00 16.21 C ANISOU 450 CG ARG A 57 1889 2382 1885 -102 195 240 C ATOM 451 CD ARG A 57 38.492 32.086 5.242 1.00 18.93 C ANISOU 451 CD ARG A 57 1991 2607 2594 -237 191 -27 C ATOM 452 NE ARG A 57 38.955 32.250 6.528 1.00 21.79 N ANISOU 452 NE ARG A 57 2435 3179 2663 -381 496 424 N ATOM 453 CZ ARG A 57 38.786 33.339 7.295 1.00 23.99 C ANISOU 453 CZ ARG A 57 2648 3669 2797 -268 143 246 C ATOM 454 NH1 ARG A 57 37.908 34.290 6.961 1.00 30.84 N ANISOU 454 NH1 ARG A 57 3640 3690 4385 44 28 393 N ATOM 455 NH2 ARG A 57 39.412 33.414 8.455 1.00 25.76 N ANISOU 455 NH2 ARG A 57 2678 4236 2872 -1085 8 12 N ATOM 456 N GLN A 58 35.774 26.931 6.062 1.00 13.70 N ANISOU 456 N GLN A 58 1525 1998 1682 227 361 211 N ATOM 457 CA GLN A 58 35.655 25.697 6.859 1.00 14.73 C ANISOU 457 CA GLN A 58 1477 2142 1976 342 399 307 C ATOM 458 C GLN A 58 36.992 25.206 7.228 1.00 16.12 C ANISOU 458 C GLN A 58 1545 2255 2324 383 564 313 C ATOM 459 O GLN A 58 37.813 24.852 6.333 1.00 16.24 O ANISOU 459 O GLN A 58 1737 2409 2022 513 534 318 O ATOM 460 CB GLN A 58 34.907 24.608 6.116 1.00 15.98 C ANISOU 460 CB GLN A 58 1680 2101 2287 316 532 -43 C ATOM 461 CG GLN A 58 34.880 23.308 6.844 1.00 19.05 C ANISOU 461 CG GLN A 58 2153 2334 2747 347 998 27 C ATOM 462 CD GLN A 58 34.080 22.227 6.132 1.00 22.51 C ANISOU 462 CD GLN A 58 2754 2293 3505 223 25 -1 C ATOM 463 OE1 GLN A 58 33.035 22.504 5.567 1.00 28.13 O ANISOU 463 OE1 GLN A 58 3481 2479 4726 131 -512 -123 O ATOM 464 NE2 GLN A 58 34.435 20.988 6.397 1.00 28.81 N ANISOU 464 NE2 GLN A 58 4402 2282 4262 216 572 76 N ATOM 465 N TYR A 59 37.280 25.189 8.537 1.00 14.95 N ANISOU 465 N TYR A 59 1315 1914 2452 416 588 277 N ATOM 466 CA TYR A 59 38.467 24.614 9.068 1.00 15.20 C ANISOU 466 CA TYR A 59 1497 2301 1978 181 537 525 C ATOM 467 C TYR A 59 38.098 23.298 9.756 1.00 16.18 C ANISOU 467 C TYR A 59 1473 2222 2450 505 482 363 C ATOM 468 O TYR A 59 37.283 23.275 10.684 1.00 17.45 O ANISOU 468 O TYR A 59 1592 2237 2801 587 704 756 O ATOM 469 CB TYR A 59 39.078 25.553 10.098 1.00 14.84 C ANISOU 469 CB TYR A 59 1145 2578 1916 626 259 514 C ATOM 470 CG TYR A 59 39.570 26.927 9.538 1.00 15.73 C ANISOU 470 CG TYR A 59 1569 2338 2069 246 328 513 C ATOM 471 CD1 TYR A 59 38.699 27.947 9.350 1.00 16.06 C ANISOU 471 CD1 TYR A 59 1718 2262 2122 238 230 223 C ATOM 472 CD2 TYR A 59 40.914 27.137 9.196 1.00 16.55 C ANISOU 472 CD2 TYR A 59 1641 2626 2020 -14 141 248 C ATOM 473 CE1 TYR A 59 39.098 29.125 8.881 1.00 16.82 C ANISOU 473 CE1 TYR A 59 2000 2106 2282 264 59 341 C ATOM 474 CE2 TYR A 59 41.315 28.370 8.723 1.00 17.81 C ANISOU 474 CE2 TYR A 59 1846 2654 2265 -422 166 60 C ATOM 475 CZ TYR A 59 40.414 29.343 8.573 1.00 18.86 C ANISOU 475 CZ TYR A 59 2628 2418 2118 -370 45 554 C ATOM 476 OH TYR A 59 40.808 30.628 8.062 1.00 23.73 O ANISOU 476 OH TYR A 59 3455 2541 3019 -1056 -307 716 O ATOM 477 N ASP A 60 38.837 22.240 9.444 1.00 19.24 N ANISOU 477 N ASP A 60 1948 2379 2982 552 701 464 N ATOM 478 CA ASP A 60 38.545 20.953 9.994 1.00 19.11 C ANISOU 478 CA ASP A 60 2053 2252 2955 407 473 164 C ATOM 479 C ASP A 60 39.469 20.595 11.129 1.00 18.20 C ANISOU 479 C ASP A 60 1810 2557 2546 388 786 309 C ATOM 480 O ASP A 60 40.642 21.038 11.191 1.00 20.89 O ANISOU 480 O ASP A 60 1959 2468 3510 556 732 842 O ATOM 481 CB ASP A 60 38.592 19.894 8.920 1.00 22.52 C ANISOU 481 CB ASP A 60 2777 2668 3110 436 436 -7 C ATOM 482 CG ASP A 60 37.455 20.030 7.920 1.00 27.11 C ANISOU 482 CG ASP A 60 3115 3389 3796 704 91 184 C ATOM 483 OD1 ASP A 60 36.234 20.343 8.361 1.00 27.27 O ANISOU 483 OD1 ASP A 60 3533 3325 3502 1389 248 -183 O ATOM 484 OD2 ASP A 60 37.599 19.725 6.745 1.00 34.21 O ANISOU 484 OD2 ASP A 60 4194 4553 4249 479 605 -242 O ATOM 485 N GLN A 61 38.999 19.716 12.002 1.00 18.26 N ANISOU 485 N GLN A 61 2050 2175 2711 696 691 319 N ATOM 486 CA GLN A 61 39.825 19.080 12.997 1.00 20.18 C ANISOU 486 CA GLN A 61 1986 2824 2858 401 289 124 C ATOM 487 C GLN A 61 40.547 20.079 13.806 1.00 15.81 C ANISOU 487 C GLN A 61 1415 2256 2334 532 353 219 C ATOM 488 O GLN A 61 41.768 19.969 14.076 1.00 21.66 O ANISOU 488 O GLN A 61 1910 2683 3635 503 309 552 O ATOM 489 CB GLN A 61 40.796 18.026 12.364 1.00 22.14 C ANISOU 489 CB GLN A 61 2260 2881 3269 814 238 264 C ATOM 490 CG GLN A 61 41.002 16.904 13.144 1.00 22.33 C ANISOU 490 CG GLN A 61 3298 2129 3056 402 -101 -391 C ATOM 491 CD GLN A 61 41.654 15.759 12.354 1.00 21.08 C ANISOU 491 CD GLN A 61 3254 2547 2208 664 -62 -31 C ATOM 492 OE1 GLN A 61 41.188 15.416 11.287 1.00 28.33 O ANISOU 492 OE1 GLN A 61 4576 3457 2728 497 -432 -362 O ATOM 493 NE2 GLN A 61 42.691 15.140 12.937 1.00 21.08 N ANISOU 493 NE2 GLN A 61 2893 2309 2805 51 98 221 N ATOM 494 N ILE A 62 39.801 21.134 14.225 1.00 16.87 N ANISOU 494 N ILE A 62 1804 2208 2397 287 338 515 N ATOM 495 CA ILE A 62 40.319 22.184 15.069 1.00 14.81 C ANISOU 495 CA ILE A 62 1095 2098 2431 417 120 412 C ATOM 496 C ILE A 62 40.049 21.974 16.602 1.00 16.43 C ANISOU 496 C ILE A 62 1376 2450 2414 358 81 540 C ATOM 497 O ILE A 62 38.912 21.892 17.018 1.00 15.43 O ANISOU 497 O ILE A 62 1089 1988 2783 151 150 689 O ATOM 498 CB ILE A 62 39.673 23.609 14.660 1.00 17.42 C ANISOU 498 CB ILE A 62 1866 1865 2886 379 104 470 C ATOM 499 CG1 ILE A 62 39.955 23.977 13.265 1.00 18.86 C ANISOU 499 CG1 ILE A 62 1732 2413 3019 293 374 551 C ATOM 500 CG2 ILE A 62 40.094 24.628 15.597 1.00 16.46 C ANISOU 500 CG2 ILE A 62 1450 2118 2685 367 54 782 C ATOM 501 CD1 ILE A 62 41.451 24.195 12.951 1.00 21.10 C ANISOU 501 CD1 ILE A 62 1538 3163 3316 395 384 1066 C ATOM 502 N PRO A 63 41.062 22.062 17.427 1.00 16.92 N ANISOU 502 N PRO A 63 1296 2299 2831 10 -28 677 N ATOM 503 CA PRO A 63 40.838 21.982 18.915 1.00 17.34 C ANISOU 503 CA PRO A 63 1263 2326 2999 385 -220 474 C ATOM 504 C PRO A 63 40.127 23.214 19.487 1.00 17.13 C ANISOU 504 C PRO A 63 1594 2219 2695 -249 -125 313 C ATOM 505 O PRO A 63 40.477 24.354 19.126 1.00 18.14 O ANISOU 505 O PRO A 63 1474 2041 3375 -19 -275 701 O ATOM 506 CB PRO A 63 42.315 21.773 19.488 1.00 18.47 C ANISOU 506 CB PRO A 63 1931 2264 2822 226 -493 732 C ATOM 507 CG PRO A 63 43.092 21.194 18.214 1.00 18.76 C ANISOU 507 CG PRO A 63 1910 2433 2781 -132 -267 552 C ATOM 508 CD PRO A 63 42.528 21.961 17.087 1.00 16.79 C ANISOU 508 CD PRO A 63 1505 2482 2392 276 283 657 C ATOM 509 N VAL A 64 39.067 22.981 20.261 1.00 16.71 N ANISOU 509 N VAL A 64 1407 2183 2757 120 -235 584 N ATOM 510 CA VAL A 64 38.362 24.033 20.905 1.00 14.86 C ANISOU 510 CA VAL A 64 1567 1881 2198 -361 -292 338 C ATOM 511 C VAL A 64 38.025 23.591 22.362 1.00 16.83 C ANISOU 511 C VAL A 64 1473 2305 2615 -53 -517 597 C ATOM 512 O VAL A 64 37.442 22.544 22.557 1.00 17.41 O ANISOU 512 O VAL A 64 2099 2069 2444 -501 -150 534 O ATOM 513 CB VAL A 64 36.982 24.368 20.192 1.00 15.91 C ANISOU 513 CB VAL A 64 1446 2058 2540 -28 -363 573 C ATOM 514 CG1 VAL A 64 36.329 25.524 20.906 1.00 16.34 C ANISOU 514 CG1 VAL A 64 1778 2264 2165 -400 -293 498 C ATOM 515 CG2 VAL A 64 37.164 24.679 18.795 1.00 15.94 C ANISOU 515 CG2 VAL A 64 1586 1806 2662 -122 -316 839 C ATOM 516 N GLU A 65 38.393 24.417 23.365 1.00 17.11 N ANISOU 516 N GLU A 65 1895 1810 2793 -53 -632 526 N ATOM 517 CA GLU A 65 38.066 24.113 24.779 1.00 17.76 C ANISOU 517 CA GLU A 65 1878 2032 2837 -455 -810 182 C ATOM 518 C GLU A 65 36.845 24.978 25.247 1.00 17.35 C ANISOU 518 C GLU A 65 2115 1897 2577 -228 -755 444 C ATOM 519 O GLU A 65 36.878 26.193 25.184 1.00 21.08 O ANISOU 519 O GLU A 65 2415 1790 3803 -366 -820 512 O ATOM 520 CB GLU A 65 39.279 24.358 25.725 1.00 21.09 C ANISOU 520 CB GLU A 65 2395 2306 3310 -221 -1071 437 C ATOM 521 CG GLU A 65 39.048 23.764 27.105 1.00 22.67 C ANISOU 521 CG GLU A 65 2579 3113 2921 -119 -542 -120 C ATOM 522 CD GLU A 65 40.335 23.784 28.021 1.00 32.00 C ANISOU 522 CD GLU A 65 3327 4856 3974 93 -945 165 C ATOM 523 OE1 GLU A 65 40.209 23.524 29.224 1.00 40.34 O ANISOU 523 OE1 GLU A 65 5567 5494 4264 571 -1078 352 O ATOM 524 OE2 GLU A 65 41.337 23.892 27.528 1.00 32.44 O ANISOU 524 OE2 GLU A 65 2792 5292 4239 -542 -1478 861 O ATOM 525 N ILE A 66 35.798 24.326 25.686 1.00 16.71 N ANISOU 525 N ILE A 66 2169 1459 2719 -259 -684 199 N ATOM 526 CA ILE A 66 34.543 24.984 25.984 1.00 17.69 C ANISOU 526 CA ILE A 66 2245 1623 2852 -251 -479 49 C ATOM 527 C ILE A 66 34.200 24.779 27.430 1.00 18.36 C ANISOU 527 C ILE A 66 2320 1958 2696 -223 -486 -146 C ATOM 528 O ILE A 66 33.973 23.670 27.865 1.00 18.90 O ANISOU 528 O ILE A 66 2651 2193 2336 -333 -582 207 O ATOM 529 CB ILE A 66 33.379 24.364 25.098 1.00 16.46 C ANISOU 529 CB ILE A 66 2029 1492 2733 -313 -447 15 C ATOM 530 CG1 ILE A 66 33.742 24.403 23.554 1.00 17.32 C ANISOU 530 CG1 ILE A 66 2250 1695 2635 -178 -359 149 C ATOM 531 CG2 ILE A 66 32.046 24.983 25.423 1.00 18.85 C ANISOU 531 CG2 ILE A 66 2045 1949 3168 -266 -514 173 C ATOM 532 CD1 ILE A 66 32.997 23.507 22.749 1.00 18.67 C ANISOU 532 CD1 ILE A 66 2275 2567 2252 -149 -882 255 C ATOM 533 N CYS A 67 34.258 25.849 28.232 1.00 21.23 N ANISOU 533 N CYS A 67 3108 1930 3027 -252 -356 -193 N ATOM 534 CA CYS A 67 34.069 25.709 29.704 1.00 24.95 C ANISOU 534 CA CYS A 67 3519 2883 3078 -146 -438 -372 C ATOM 535 C CYS A 67 34.967 24.641 30.264 1.00 25.34 C ANISOU 535 C CYS A 67 3678 2952 2995 -172 -596 -537 C ATOM 536 O CYS A 67 34.529 23.837 31.111 1.00 27.50 O ANISOU 536 O CYS A 67 4187 3157 3103 -378 -251 -786 O ATOM 537 CB CYS A 67 32.676 25.323 30.022 1.00 26.53 C ANISOU 537 CB CYS A 67 3852 3115 3111 9 38 -124 C ATOM 538 SG CYS A 67 31.562 26.480 29.783 1.00 34.91 S ANISOU 538 SG CYS A 67 5120 4201 3940 655 -766 399 S ATOM 539 N GLY A 68 36.157 24.533 29.747 1.00 21.55 N ANISOU 539 N GLY A 68 3283 2482 2421 -346 -1004 -379 N ATOM 540 CA GLY A 68 37.120 23.554 30.275 1.00 22.70 C ANISOU 540 CA GLY A 68 3441 2494 2687 63 -907 -326 C ATOM 541 C GLY A 68 37.041 22.134 29.657 1.00 22.05 C ANISOU 541 C GLY A 68 3047 2430 2899 -64 -1122 -228 C ATOM 542 O GLY A 68 37.810 21.293 30.016 1.00 25.26 O ANISOU 542 O GLY A 68 3501 3012 3082 399 -1440 -299 O ATOM 543 N HIS A 69 36.077 21.905 28.796 1.00 18.23 N ANISOU 543 N HIS A 69 2554 2196 2176 8 -820 -178 N ATOM 544 CA HIS A 69 35.898 20.596 28.135 1.00 16.56 C ANISOU 544 CA HIS A 69 2185 1818 2288 -71 -656 372 C ATOM 545 C HIS A 69 36.478 20.658 26.770 1.00 15.74 C ANISOU 545 C HIS A 69 2003 1702 2273 -194 -582 107 C ATOM 546 O HIS A 69 36.245 21.612 26.027 1.00 18.21 O ANISOU 546 O HIS A 69 2667 1637 2614 29 -458 378 O ATOM 547 CB HIS A 69 34.405 20.221 28.038 1.00 17.79 C ANISOU 547 CB HIS A 69 2104 2055 2599 -145 -651 221 C ATOM 548 CG HIS A 69 33.700 20.067 29.363 1.00 22.72 C ANISOU 548 CG HIS A 69 2297 3275 3059 -62 -446 287 C ATOM 549 ND1 HIS A 69 32.361 20.163 29.440 1.00 41.64 N ANISOU 549 ND1 HIS A 69 3699 6956 5166 -579 703 -654 N ATOM 550 CD2 HIS A 69 34.082 19.598 30.541 1.00 35.67 C ANISOU 550 CD2 HIS A 69 4403 5767 3380 85 162 252 C ATOM 551 CE1 HIS A 69 31.999 20.112 30.734 1.00 39.78 C ANISOU 551 CE1 HIS A 69 4429 6574 4108 154 -841 -26 C ATOM 552 NE2 HIS A 69 33.015 19.821 31.412 1.00 28.19 N ANISOU 552 NE2 HIS A 69 3132 4991 2587 577 -567 159 N ATOM 553 N LYS A 70 37.190 19.605 26.373 1.00 16.80 N ANISOU 553 N LYS A 70 2267 2011 2102 199 -327 386 N ATOM 554 CA LYS A 70 37.874 19.557 25.090 1.00 18.05 C ANISOU 554 CA LYS A 70 2256 1958 2643 324 -180 463 C ATOM 555 C LYS A 70 37.013 19.024 23.913 1.00 16.03 C ANISOU 555 C LYS A 70 1861 1901 2327 375 -13 372 C ATOM 556 O LYS A 70 36.346 17.976 24.020 1.00 17.43 O ANISOU 556 O LYS A 70 2348 1885 2387 -104 -87 477 O ATOM 557 CB LYS A 70 39.163 18.767 25.225 1.00 21.90 C ANISOU 557 CB LYS A 70 2357 2861 3100 505 -589 625 C ATOM 558 CG LYS A 70 40.224 19.486 26.169 1.00 27.91 C ANISOU 558 CG LYS A 70 2890 3848 3866 -55 -658 477 C ATOM 559 CD LYS A 70 41.442 18.586 26.499 1.00 35.63 C ANISOU 559 CD LYS A 70 3645 4860 5031 488 -263 419 C ATOM 560 CE LYS A 70 42.224 19.177 27.626 1.00 41.28 C ANISOU 560 CE LYS A 70 4883 5468 5334 -144 -380 -80 C ATOM 561 NZ LYS A 70 43.671 19.204 27.341 1.00 47.17 N ANISOU 561 NZ LYS A 70 5059 6602 6260 229 15 100 N ATOM 562 N ALA A 71 37.136 19.676 22.788 1.00 14.39 N ANISOU 562 N ALA A 71 1526 1816 2125 -25 -13 412 N ATOM 563 CA ALA A 71 36.590 19.188 21.546 1.00 13.87 C ANISOU 563 CA ALA A 71 1437 1644 2187 225 213 244 C ATOM 564 C ALA A 71 37.637 19.380 20.443 1.00 13.38 C ANISOU 564 C ALA A 71 1448 1589 2046 227 91 446 C ATOM 565 O ALA A 71 38.532 20.244 20.579 1.00 16.36 O ANISOU 565 O ALA A 71 1453 1754 3005 211 122 551 O ATOM 566 CB ALA A 71 35.306 19.952 21.209 1.00 13.51 C ANISOU 566 CB ALA A 71 1541 1511 2078 313 16 237 C ATOM 567 N ILE A 72 37.537 18.618 19.419 1.00 14.18 N ANISOU 567 N ILE A 72 1640 1463 2285 379 373 368 N ATOM 568 CA ILE A 72 38.308 18.847 18.169 1.00 14.64 C ANISOU 568 CA ILE A 72 1696 1547 2318 491 426 406 C ATOM 569 C ILE A 72 37.449 18.558 16.991 1.00 14.94 C ANISOU 569 C ILE A 72 1446 1945 2284 394 283 386 C ATOM 570 O ILE A 72 37.004 17.446 16.802 1.00 15.92 O ANISOU 570 O ILE A 72 1839 1647 2561 251 561 394 O ATOM 571 CB ILE A 72 39.591 17.876 18.107 1.00 15.63 C ANISOU 571 CB ILE A 72 1748 1757 2433 326 273 421 C ATOM 572 CG1 ILE A 72 40.406 17.934 19.373 1.00 14.90 C ANISOU 572 CG1 ILE A 72 1573 1803 2282 346 305 384 C ATOM 573 CG2 ILE A 72 40.386 18.197 16.872 1.00 16.56 C ANISOU 573 CG2 ILE A 72 1733 2014 2542 336 490 367 C ATOM 574 CD1 ILE A 72 41.605 16.965 19.408 1.00 17.18 C ANISOU 574 CD1 ILE A 72 1787 1740 2998 416 299 46 C ATOM 575 N GLY A 73 37.126 19.590 16.203 1.00 14.38 N ANISOU 575 N GLY A 73 1685 1570 2206 414 470 460 N ATOM 576 CA GLY A 73 36.213 19.418 15.104 1.00 15.04 C ANISOU 576 CA GLY A 73 1585 1593 2533 307 409 257 C ATOM 577 C GLY A 73 36.126 20.611 14.238 1.00 13.49 C ANISOU 577 C GLY A 73 1647 1592 1884 19 403 348 C ATOM 578 O GLY A 73 37.028 21.462 14.250 1.00 15.26 O ANISOU 578 O GLY A 73 1287 1821 2688 349 216 476 O ATOM 579 N THR A 74 35.109 20.634 13.415 1.00 14.48 N ANISOU 579 N THR A 74 1509 1708 2281 283 290 389 N ATOM 580 CA THR A 74 34.984 21.623 12.362 1.00 13.41 C ANISOU 580 CA THR A 74 1360 1669 2065 214 459 383 C ATOM 581 C THR A 74 34.521 22.943 12.904 1.00 13.32 C ANISOU 581 C THR A 74 1793 1506 1763 440 372 368 C ATOM 582 O THR A 74 33.567 23.029 13.711 1.00 13.10 O ANISOU 582 O THR A 74 1376 1587 2011 167 530 240 O ATOM 583 CB THR A 74 34.045 21.083 11.325 1.00 15.86 C ANISOU 583 CB THR A 74 1977 1815 2234 448 364 25 C ATOM 584 OG1 THR A 74 34.596 19.868 10.758 1.00 20.19 O ANISOU 584 OG1 THR A 74 2522 2034 3113 771 353 -153 O ATOM 585 CG2 THR A 74 33.856 22.000 10.238 1.00 16.58 C ANISOU 585 CG2 THR A 74 1761 2080 2457 340 269 45 C ATOM 586 N VAL A 75 35.204 24.013 12.511 1.00 12.43 N ANISOU 586 N VAL A 75 1249 1481 1992 387 452 435 N ATOM 587 CA VAL A 75 34.819 25.377 12.818 1.00 12.87 C ANISOU 587 CA VAL A 75 1333 1670 1885 106 438 341 C ATOM 588 C VAL A 75 34.663 26.137 11.521 1.00 11.91 C ANISOU 588 C VAL A 75 1213 1529 1780 228 412 397 C ATOM 589 O VAL A 75 35.532 26.126 10.656 1.00 13.58 O ANISOU 589 O VAL A 75 1276 1907 1976 416 447 454 O ATOM 590 CB VAL A 75 35.873 26.028 13.705 1.00 14.34 C ANISOU 590 CB VAL A 75 1753 1671 2022 36 167 337 C ATOM 591 CG1 VAL A 75 35.643 27.460 13.925 1.00 13.91 C ANISOU 591 CG1 VAL A 75 1519 2002 1763 96 81 207 C ATOM 592 CG2 VAL A 75 36.030 25.271 15.027 1.00 15.38 C ANISOU 592 CG2 VAL A 75 1713 1999 2128 238 -56 326 C ATOM 593 N LEU A 76 33.529 26.786 11.370 1.00 11.62 N ANISOU 593 N LEU A 76 1119 1636 1660 89 216 260 N ATOM 594 CA LEU A 76 33.255 27.664 10.242 1.00 11.68 C ANISOU 594 CA LEU A 76 1164 1543 1729 115 282 199 C ATOM 595 C LEU A 76 33.507 29.072 10.688 1.00 10.98 C ANISOU 595 C LEU A 76 1058 1565 1547 171 209 164 C ATOM 596 O LEU A 76 33.077 29.460 11.764 1.00 13.71 O ANISOU 596 O LEU A 76 1636 1708 1864 -185 610 35 O ATOM 597 CB LEU A 76 31.775 27.470 9.774 1.00 11.74 C ANISOU 597 CB LEU A 76 1392 1577 1491 205 124 217 C ATOM 598 CG LEU A 76 31.379 26.038 9.503 1.00 12.04 C ANISOU 598 CG LEU A 76 1385 1635 1554 242 317 113 C ATOM 599 CD1 LEU A 76 29.930 25.962 9.028 1.00 13.14 C ANISOU 599 CD1 LEU A 76 1378 1775 1839 114 406 31 C ATOM 600 CD2 LEU A 76 32.302 25.353 8.471 1.00 13.45 C ANISOU 600 CD2 LEU A 76 1533 1586 1990 134 249 -126 C ATOM 601 N VAL A 77 34.123 29.884 9.826 1.00 11.10 N ANISOU 601 N VAL A 77 1228 1522 1468 105 148 351 N ATOM 602 CA VAL A 77 34.415 31.270 10.144 1.00 11.76 C ANISOU 602 CA VAL A 77 1241 1609 1615 -66 -4 428 C ATOM 603 C VAL A 77 33.751 32.162 9.108 1.00 11.36 C ANISOU 603 C VAL A 77 1332 1490 1493 -237 51 353 C ATOM 604 O VAL A 77 33.965 31.989 7.912 1.00 12.22 O ANISOU 604 O VAL A 77 1484 1640 1518 -114 72 271 O ATOM 605 CB VAL A 77 35.952 31.530 10.155 1.00 13.68 C ANISOU 605 CB VAL A 77 1389 2286 1520 -175 -49 298 C ATOM 606 CG1 VAL A 77 36.265 33.011 10.403 1.00 15.32 C ANISOU 606 CG1 VAL A 77 1285 2498 2036 -311 -229 233 C ATOM 607 CG2 VAL A 77 36.622 30.679 11.213 1.00 16.07 C ANISOU 607 CG2 VAL A 77 1344 2584 2177 254 105 371 C ATOM 608 N GLY A 78 32.960 33.109 9.559 1.00 11.45 N ANISOU 608 N GLY A 78 1592 1415 1341 -105 -92 325 N ATOM 609 CA GLY A 78 32.274 34.021 8.626 1.00 13.32 C ANISOU 609 CA GLY A 78 1880 1633 1548 -174 -159 294 C ATOM 610 C GLY A 78 31.315 34.913 9.371 1.00 12.43 C ANISOU 610 C GLY A 78 1929 1322 1471 -131 -15 229 C ATOM 611 O GLY A 78 31.325 35.004 10.593 1.00 13.28 O ANISOU 611 O GLY A 78 1903 1571 1571 55 -180 182 O ATOM 612 N PRO A 79 30.449 35.606 8.611 1.00 13.00 N ANISOU 612 N PRO A 79 1864 1434 1639 1 -231 243 N ATOM 613 CA PRO A 79 29.646 36.704 9.175 1.00 13.49 C ANISOU 613 CA PRO A 79 2109 1251 1763 171 -574 66 C ATOM 614 C PRO A 79 28.442 36.186 9.885 1.00 13.71 C ANISOU 614 C PRO A 79 1896 1766 1545 267 -432 -183 C ATOM 615 O PRO A 79 27.342 36.499 9.535 1.00 18.42 O ANISOU 615 O PRO A 79 2303 2755 1940 287 -426 3 O ATOM 616 CB PRO A 79 29.257 37.538 7.952 1.00 14.97 C ANISOU 616 CB PRO A 79 2437 1349 1899 -54 -526 261 C ATOM 617 CG PRO A 79 29.242 36.562 6.826 1.00 14.79 C ANISOU 617 CG PRO A 79 2256 1494 1868 47 -306 321 C ATOM 618 CD PRO A 79 30.424 35.611 7.112 1.00 14.11 C ANISOU 618 CD PRO A 79 2003 1685 1670 -98 -294 188 C ATOM 619 N THR A 80 28.648 35.451 10.892 1.00 17.95 N ANISOU 619 N THR A 80 2189 2404 2224 -213 -710 613 N ATOM 620 CA THR A 80 27.599 35.138 11.841 1.00 16.10 C ANISOU 620 CA THR A 80 1967 1995 2153 -342 -623 542 C ATOM 621 C THR A 80 27.349 36.321 12.780 1.00 15.16 C ANISOU 621 C THR A 80 2033 1396 2330 -183 -475 740 C ATOM 622 O THR A 80 28.304 37.062 13.127 1.00 18.24 O ANISOU 622 O THR A 80 2331 1893 2704 -548 -769 768 O ATOM 623 CB THR A 80 27.957 33.895 12.659 1.00 14.80 C ANISOU 623 CB THR A 80 1815 1859 1949 -164 -440 323 C ATOM 624 OG1 THR A 80 26.930 33.665 13.645 1.00 15.00 O ANISOU 624 OG1 THR A 80 1843 1877 1978 -327 -349 306 O ATOM 625 CG2 THR A 80 29.318 34.039 13.414 1.00 13.19 C ANISOU 625 CG2 THR A 80 1687 1791 1534 -67 -377 383 C ATOM 626 N PRO A 81 26.105 36.536 13.276 1.00 16.32 N ANISOU 626 N PRO A 81 2219 1652 2326 -15 -642 417 N ATOM 627 CA PRO A 81 25.849 37.615 14.204 1.00 15.89 C ANISOU 627 CA PRO A 81 2202 1453 2381 -123 -486 541 C ATOM 628 C PRO A 81 26.561 37.488 15.582 1.00 14.60 C ANISOU 628 C PRO A 81 1867 1305 2373 -243 -474 535 C ATOM 629 O PRO A 81 26.748 38.497 16.309 1.00 17.40 O ANISOU 629 O PRO A 81 2260 1385 2965 -253 -654 229 O ATOM 630 CB PRO A 81 24.319 37.568 14.395 1.00 18.96 C ANISOU 630 CB PRO A 81 2353 1974 2876 -68 -634 550 C ATOM 631 CG PRO A 81 23.956 36.212 14.000 1.00 21.16 C ANISOU 631 CG PRO A 81 2097 2410 3533 -172 -593 -408 C ATOM 632 CD PRO A 81 24.843 35.838 12.878 1.00 18.23 C ANISOU 632 CD PRO A 81 2007 2004 2913 -202 -663 28 C ATOM 633 N AVAL A 82 26.899 36.280 15.945 0.50 14.33 N ANISOU 633 N AVAL A 82 1703 1284 2456 -209 -254 582 N ATOM 634 N BVAL A 82 26.749 36.295 16.038 0.50 13.89 N ANISOU 634 N BVAL A 82 1880 1219 2176 -281 -198 724 N ATOM 635 CA AVAL A 82 27.455 35.976 17.262 0.50 15.62 C ANISOU 635 CA AVAL A 82 2095 1661 2177 117 71 451 C ATOM 636 CA BVAL A 82 27.548 36.039 17.293 0.50 13.59 C ANISOU 636 CA BVAL A 82 1945 1246 1970 0 36 427 C ATOM 637 C AVAL A 82 28.215 34.637 17.101 0.50 12.57 C ANISOU 637 C AVAL A 82 1745 1365 1663 -132 -129 384 C ATOM 638 C BVAL A 82 28.200 34.677 17.118 0.50 11.42 C ANISOU 638 C BVAL A 82 1667 1158 1514 -158 -127 264 C ATOM 639 O AVAL A 82 27.873 33.829 16.251 0.50 13.64 O ANISOU 639 O AVAL A 82 2053 1455 1673 -130 -232 584 O ATOM 640 O BVAL A 82 27.713 33.831 16.341 0.50 11.84 O ANISOU 640 O BVAL A 82 1612 1286 1601 -185 -220 327 O ATOM 641 CB AVAL A 82 26.289 35.865 18.366 0.50 18.94 C ANISOU 641 CB AVAL A 82 2262 2204 2730 208 158 317 C ATOM 642 CB BVAL A 82 26.636 36.055 18.584 0.50 13.45 C ANISOU 642 CB BVAL A 82 1933 1087 2087 149 -154 258 C ATOM 643 CG1AVAL A 82 26.777 35.361 19.587 0.50 20.58 C ANISOU 643 CG1AVAL A 82 2427 2758 2631 609 153 177 C ATOM 644 CG1BVAL A 82 25.606 34.866 18.524 0.50 13.39 C ANISOU 644 CG1BVAL A 82 1863 865 2357 -21 130 18 C ATOM 645 CG2AVAL A 82 25.646 37.225 18.579 0.50 21.35 C ANISOU 645 CG2AVAL A 82 2749 2567 2795 597 456 393 C ATOM 646 CG2BVAL A 82 27.500 36.040 19.918 0.50 17.64 C ANISOU 646 CG2BVAL A 82 2644 1830 2228 212 -90 -447 C ATOM 647 N ASN A 83 29.262 34.454 17.843 1.00 12.23 N ANISOU 647 N ASN A 83 1625 1405 1616 -199 -222 202 N ATOM 648 CA ASN A 83 29.918 33.163 17.868 1.00 10.18 C ANISOU 648 CA ASN A 83 1259 1146 1462 14 -90 233 C ATOM 649 C ASN A 83 28.940 32.126 18.410 1.00 9.56 C ANISOU 649 C ASN A 83 1305 1189 1138 11 -80 229 C ATOM 650 O ASN A 83 28.401 32.316 19.499 1.00 10.88 O ANISOU 650 O ASN A 83 1615 1343 1175 -176 -70 10 O ATOM 651 CB ASN A 83 31.117 33.193 18.780 1.00 11.76 C ANISOU 651 CB ASN A 83 1470 1442 1553 -156 -112 157 C ATOM 652 CG ASN A 83 32.228 34.110 18.333 1.00 12.81 C ANISOU 652 CG ASN A 83 1621 1357 1887 -19 -20 34 C ATOM 653 OD1 ASN A 83 32.509 34.281 17.161 1.00 14.86 O ANISOU 653 OD1 ASN A 83 1963 1765 1917 -585 84 164 O ATOM 654 ND2 ASN A 83 32.948 34.643 19.332 1.00 14.53 N ANISOU 654 ND2 ASN A 83 1718 1601 2200 -232 -440 201 N ATOM 655 N ILE A 84 28.751 31.011 17.701 1.00 9.71 N ANISOU 655 N ILE A 84 1313 1148 1229 35 -74 109 N ATOM 656 CA ILE A 84 27.874 29.936 18.121 1.00 9.20 C ANISOU 656 CA ILE A 84 1207 1142 1144 32 100 77 C ATOM 657 C ILE A 84 28.601 28.631 18.142 1.00 9.26 C ANISOU 657 C ILE A 84 1156 1055 1306 28 -69 -12 C ATOM 658 O ILE A 84 29.316 28.267 17.216 1.00 10.16 O ANISOU 658 O ILE A 84 1407 1239 1212 113 51 164 O ATOM 659 CB ILE A 84 26.576 29.869 17.267 1.00 9.70 C ANISOU 659 CB ILE A 84 1234 1202 1246 -26 7 43 C ATOM 660 CG1 ILE A 84 26.827 29.553 15.830 1.00 11.46 C ANISOU 660 CG1 ILE A 84 1488 1501 1362 0 4 -53 C ATOM 661 CG2 ILE A 84 25.763 31.145 17.415 1.00 10.32 C ANISOU 661 CG2 ILE A 84 1258 1325 1337 67 -89 3 C ATOM 662 CD1 ILE A 84 25.551 29.561 14.956 1.00 11.38 C ANISOU 662 CD1 ILE A 84 1527 1651 1143 5 -38 198 C ATOM 663 N ILE A 85 28.365 27.876 19.221 1.00 9.14 N ANISOU 663 N ILE A 85 1197 1056 1219 -8 0 75 N ATOM 664 CA ILE A 85 28.828 26.486 19.351 1.00 9.36 C ANISOU 664 CA ILE A 85 1212 1079 1263 84 30 93 C ATOM 665 C ILE A 85 27.675 25.579 19.001 1.00 8.57 C ANISOU 665 C ILE A 85 1078 1029 1149 82 -7 31 C ATOM 666 O ILE A 85 26.640 25.590 19.683 1.00 9.80 O ANISOU 666 O ILE A 85 1228 1281 1211 87 -24 -41 O ATOM 667 CB ILE A 85 29.323 26.183 20.762 1.00 10.01 C ANISOU 667 CB ILE A 85 1178 1266 1359 -27 -198 66 C ATOM 668 CG1 ILE A 85 30.370 27.194 21.246 1.00 11.67 C ANISOU 668 CG1 ILE A 85 1551 1401 1481 -115 -225 297 C ATOM 669 CG2 ILE A 85 29.861 24.734 20.790 1.00 11.12 C ANISOU 669 CG2 ILE A 85 1504 1467 1254 58 -359 120 C ATOM 670 CD1 ILE A 85 31.564 27.345 20.370 1.00 13.23 C ANISOU 670 CD1 ILE A 85 1549 1694 1783 -172 -303 67 C ATOM 671 N GLY A 86 27.790 24.868 17.881 1.00 8.59 N ANISOU 671 N GLY A 86 1194 1061 1005 17 72 69 N ATOM 672 CA GLY A 86 26.758 23.991 17.406 1.00 8.51 C ANISOU 672 CA GLY A 86 1171 1046 1014 21 -25 73 C ATOM 673 C GLY A 86 26.921 22.578 17.831 1.00 8.53 C ANISOU 673 C GLY A 86 1154 1105 979 214 -33 70 C ATOM 674 O GLY A 86 27.866 22.214 18.537 1.00 8.90 O ANISOU 674 O GLY A 86 1129 1152 1099 74 -32 19 O ATOM 675 N ARG A 87 26.007 21.718 17.375 1.00 8.02 N ANISOU 675 N ARG A 87 1132 1004 909 41 -60 65 N ATOM 676 CA ARG A 87 25.947 20.365 17.846 1.00 8.66 C ANISOU 676 CA ARG A 87 1113 1003 1173 34 -27 -1 C ATOM 677 C ARG A 87 27.176 19.545 17.514 1.00 9.21 C ANISOU 677 C ARG A 87 1241 1088 1168 74 -22 105 C ATOM 678 O ARG A 87 27.501 18.630 18.264 1.00 9.73 O ANISOU 678 O ARG A 87 1349 1121 1226 88 -64 104 O ATOM 679 CB ARG A 87 24.700 19.647 17.320 1.00 8.89 C ANISOU 679 CB ARG A 87 1181 1085 1112 48 141 37 C ATOM 680 CG ARG A 87 23.394 20.197 17.875 1.00 8.86 C ANISOU 680 CG ARG A 87 1255 1003 1106 67 -8 68 C ATOM 681 CD ARG A 87 22.170 19.403 17.430 1.00 9.28 C ANISOU 681 CD ARG A 87 1134 1182 1208 72 -23 6 C ATOM 682 NE ARG A 87 21.968 19.409 15.990 1.00 9.49 N ANISOU 682 NE ARG A 87 1184 1174 1247 36 -27 37 N ATOM 683 CZ ARG A 87 22.388 18.449 15.166 1.00 10.06 C ANISOU 683 CZ ARG A 87 1270 1240 1312 -13 -7 115 C ATOM 684 NH1 ARG A 87 22.890 17.326 15.617 1.00 10.43 N ANISOU 684 NH1 ARG A 87 1464 1294 1205 99 52 -148 N ATOM 685 NH2 ARG A 87 22.216 18.648 13.886 1.00 10.97 N ANISOU 685 NH2 ARG A 87 1516 1376 1275 184 -30 13 N ATOM 686 N ASN A 88 27.887 19.896 16.470 1.00 9.32 N ANISOU 686 N ASN A 88 1122 1155 1262 131 99 1 N ATOM 687 CA ASN A 88 29.106 19.153 16.155 1.00 10.08 C ANISOU 687 CA ASN A 88 1207 1216 1407 34 94 51 C ATOM 688 C ASN A 88 30.087 19.154 17.303 1.00 9.96 C ANISOU 688 C ASN A 88 1232 1152 1401 144 44 158 C ATOM 689 O ASN A 88 30.781 18.162 17.501 1.00 12.07 O ANISOU 689 O ASN A 88 1296 1289 1999 209 -210 -25 O ATOM 690 CB ASN A 88 29.735 19.654 14.850 1.00 11.21 C ANISOU 690 CB ASN A 88 1172 1403 1683 144 295 26 C ATOM 691 CG ASN A 88 30.436 20.961 15.006 1.00 11.05 C ANISOU 691 CG ASN A 88 1366 1400 1429 91 136 74 C ATOM 692 OD1 ASN A 88 29.816 21.949 15.423 1.00 10.95 O ANISOU 692 OD1 ASN A 88 1284 1328 1546 125 112 -15 O ATOM 693 ND2 ASN A 88 31.706 21.004 14.621 1.00 11.46 N ANISOU 693 ND2 ASN A 88 1242 1409 1702 48 269 273 N ATOM 694 N LEU A 89 30.193 20.262 18.060 1.00 9.73 N ANISOU 694 N LEU A 89 1082 1230 1385 163 -17 6 N ATOM 695 CA LEU A 89 31.034 20.331 19.239 1.00 10.55 C ANISOU 695 CA LEU A 89 1178 1226 1604 43 1 148 C ATOM 696 C LEU A 89 30.293 20.075 20.534 1.00 9.81 C ANISOU 696 C LEU A 89 1207 1007 1513 139 -29 134 C ATOM 697 O LEU A 89 30.881 19.546 21.469 1.00 11.24 O ANISOU 697 O LEU A 89 1341 1194 1733 81 -194 319 O ATOM 698 CB LEU A 89 31.836 21.634 19.272 1.00 10.63 C ANISOU 698 CB LEU A 89 1206 1188 1644 -32 -174 121 C ATOM 699 CG LEU A 89 32.687 21.958 18.057 1.00 11.41 C ANISOU 699 CG LEU A 89 1186 1384 1762 19 212 203 C ATOM 700 CD1 LEU A 89 33.503 23.222 18.294 1.00 13.05 C ANISOU 700 CD1 LEU A 89 1316 1493 2148 20 -116 402 C ATOM 701 CD2 LEU A 89 33.615 20.800 17.673 1.00 12.99 C ANISOU 701 CD2 LEU A 89 1267 1666 1999 199 -60 258 C ATOM 702 N LEU A 90 29.012 20.439 20.626 1.00 9.75 N ANISOU 702 N LEU A 90 1155 1248 1299 240 -54 196 N ATOM 703 CA LEU A 90 28.258 20.161 21.849 1.00 9.36 C ANISOU 703 CA LEU A 90 1235 1093 1225 95 -43 9 C ATOM 704 C LEU A 90 28.221 18.668 22.129 1.00 9.28 C ANISOU 704 C LEU A 90 1141 1335 1048 161 90 139 C ATOM 705 O LEU A 90 28.290 18.263 23.285 1.00 10.52 O ANISOU 705 O LEU A 90 1365 1341 1289 93 -58 205 O ATOM 706 CB LEU A 90 26.836 20.707 21.745 1.00 9.47 C ANISOU 706 CB LEU A 90 1183 1121 1293 106 51 -3 C ATOM 707 CG LEU A 90 26.686 22.226 21.620 1.00 10.22 C ANISOU 707 CG LEU A 90 1465 1170 1248 117 -1 38 C ATOM 708 CD1 LEU A 90 25.228 22.610 21.379 1.00 11.95 C ANISOU 708 CD1 LEU A 90 1525 1223 1791 279 -176 -54 C ATOM 709 CD2 LEU A 90 27.219 22.988 22.825 1.00 12.09 C ANISOU 709 CD2 LEU A 90 1550 1402 1641 102 -113 -32 C ATOM 710 N THR A 91 28.118 17.837 21.093 1.00 9.64 N ANISOU 710 N THR A 91 1252 1109 1301 102 -28 20 N ATOM 711 CA THR A 91 28.120 16.392 21.315 1.00 10.34 C ANISOU 711 CA THR A 91 1214 1275 1439 89 125 143 C ATOM 712 C THR A 91 29.464 15.914 21.878 1.00 9.88 C ANISOU 712 C THR A 91 1375 1050 1327 108 89 51 C ATOM 713 O THR A 91 29.499 15.047 22.733 1.00 12.32 O ANISOU 713 O THR A 91 1482 1383 1815 133 -15 398 O ATOM 714 CB THR A 91 27.808 15.643 20.040 1.00 10.84 C ANISOU 714 CB THR A 91 1270 1190 1656 -21 -9 126 C ATOM 715 OG1 THR A 91 28.726 16.002 19.005 1.00 12.52 O ANISOU 715 OG1 THR A 91 1486 1518 1751 -1 148 -274 O ATOM 716 CG2 THR A 91 26.405 15.853 19.571 1.00 12.40 C ANISOU 716 CG2 THR A 91 1418 1500 1792 40 -15 -38 C ATOM 717 N GLN A 92 30.539 16.517 21.465 1.00 10.75 N ANISOU 717 N GLN A 92 1265 1281 1536 171 -21 144 N ATOM 718 CA GLN A 92 31.878 16.096 21.906 1.00 11.30 C ANISOU 718 CA GLN A 92 1264 1254 1773 244 -154 128 C ATOM 719 C GLN A 92 32.089 16.354 23.350 1.00 11.86 C ANISOU 719 C GLN A 92 1180 1527 1796 148 -276 78 C ATOM 720 O GLN A 92 32.775 15.580 24.018 1.00 14.53 O ANISOU 720 O GLN A 92 1701 1905 1913 500 -254 316 O ATOM 721 CB GLN A 92 32.983 16.797 21.104 1.00 12.37 C ANISOU 721 CB GLN A 92 1188 1368 2141 252 -154 207 C ATOM 722 CG GLN A 92 33.011 16.429 19.624 1.00 12.82 C ANISOU 722 CG GLN A 92 1644 1205 2021 146 43 77 C ATOM 723 CD GLN A 92 34.300 16.739 18.977 1.00 13.14 C ANISOU 723 CD GLN A 92 1784 1280 1927 362 78 180 C ATOM 724 OE1 GLN A 92 35.323 16.922 19.678 1.00 14.38 O ANISOU 724 OE1 GLN A 92 1431 1921 2109 186 92 436 O ATOM 725 NE2 GLN A 92 34.329 16.732 17.674 1.00 14.02 N ANISOU 725 NE2 GLN A 92 1641 1810 1874 424 191 222 N ATOM 726 N ILE A 93 31.497 17.425 23.911 1.00 11.35 N ANISOU 726 N ILE A 93 1319 1482 1510 73 -271 60 N ATOM 727 CA ILE A 93 31.625 17.763 25.302 1.00 12.60 C ANISOU 727 CA ILE A 93 1496 1662 1627 -2 -239 12 C ATOM 728 C ILE A 93 30.558 17.128 26.177 1.00 13.73 C ANISOU 728 C ILE A 93 1735 1664 1815 290 -419 76 C ATOM 729 O ILE A 93 30.514 17.394 27.407 1.00 15.32 O ANISOU 729 O ILE A 93 2039 1958 1821 207 -174 264 O ATOM 730 CB ILE A 93 31.745 19.306 25.539 1.00 14.20 C ANISOU 730 CB ILE A 93 1767 2026 1599 0 -491 -61 C ATOM 731 CG1 ILE A 93 30.416 20.029 25.238 1.00 12.80 C ANISOU 731 CG1 ILE A 93 1779 1581 1501 -48 -277 -46 C ATOM 732 CG2 ILE A 93 32.910 19.873 24.748 1.00 14.93 C ANISOU 732 CG2 ILE A 93 1829 1768 2076 -61 -205 -180 C ATOM 733 CD1 ILE A 93 30.451 21.460 25.580 1.00 14.98 C ANISOU 733 CD1 ILE A 93 2061 1721 1909 30 -252 -79 C ATOM 734 N GLY A 94 29.678 16.304 25.567 1.00 12.23 N ANISOU 734 N GLY A 94 1557 1596 1491 205 -94 319 N ATOM 735 CA GLY A 94 28.703 15.562 26.316 1.00 13.46 C ANISOU 735 CA GLY A 94 1855 1569 1690 153 -123 499 C ATOM 736 C GLY A 94 27.461 16.334 26.689 1.00 13.64 C ANISOU 736 C GLY A 94 2119 1598 1465 311 13 345 C ATOM 737 O GLY A 94 26.793 15.972 27.620 1.00 15.30 O ANISOU 737 O GLY A 94 2000 2035 1775 288 168 571 O ATOM 738 N ACYS A 95 27.101 17.327 25.899 0.50 13.18 N ANISOU 738 N ACYS A 95 1735 1682 1589 281 60 349 N ATOM 739 N BCYS A 95 27.155 17.364 25.954 0.50 12.75 N ANISOU 739 N BCYS A 95 1639 1591 1611 235 40 335 N ATOM 740 CA ACYS A 95 25.865 18.124 26.160 0.50 13.40 C ANISOU 740 CA ACYS A 95 1927 1922 1240 345 172 161 C ATOM 741 CA BCYS A 95 26.063 18.261 26.299 0.50 12.64 C ANISOU 741 CA BCYS A 95 1716 1820 1265 422 -59 373 C ATOM 742 C ACYS A 95 24.674 17.402 25.909 0.50 13.81 C ANISOU 742 C ACYS A 95 1885 1882 1479 665 -121 231 C ATOM 743 C BCYS A 95 24.701 17.680 25.814 0.50 13.90 C ANISOU 743 C BCYS A 95 1780 1958 1542 389 47 286 C ATOM 744 O ACYS A 95 24.485 16.789 24.794 0.50 15.63 O ANISOU 744 O ACYS A 95 1987 2486 1463 236 11 245 O ATOM 745 O BCYS A 95 24.589 17.165 24.708 0.50 15.65 O ANISOU 745 O BCYS A 95 1892 2599 1454 576 64 306 O ATOM 746 CB ACYS A 95 25.836 19.309 25.300 0.50 13.29 C ANISOU 746 CB ACYS A 95 1899 1537 1610 277 12 90 C ATOM 747 CB BCYS A 95 26.313 19.608 25.637 0.50 12.05 C ANISOU 747 CB BCYS A 95 1645 1635 1299 107 -84 167 C ATOM 748 SG ACYS A 95 26.822 20.561 25.810 0.50 19.46 S ANISOU 748 SG ACYS A 95 2687 2376 2329 -36 -336 159 S ATOM 749 SG BCYS A 95 25.189 20.907 26.088 0.50 11.53 S ANISOU 749 SG BCYS A 95 1549 1463 1365 392 -10 94 S ATOM 750 N THR A 96 23.713 17.650 26.759 1.00 13.94 N ANISOU 750 N THR A 96 1860 2022 1412 483 91 332 N ATOM 751 CA THR A 96 22.378 17.248 26.480 1.00 13.59 C ANISOU 751 CA THR A 96 1925 1811 1428 442 261 377 C ATOM 752 C THR A 96 21.397 18.301 26.950 1.00 12.68 C ANISOU 752 C THR A 96 1891 1456 1467 243 121 321 C ATOM 753 O THR A 96 21.734 19.172 27.712 1.00 13.65 O ANISOU 753 O THR A 96 1798 1931 1455 336 -82 301 O ATOM 754 CB THR A 96 21.987 15.914 27.176 1.00 16.90 C ANISOU 754 CB THR A 96 2142 2095 2180 677 130 570 C ATOM 755 OG1 THR A 96 22.143 16.053 28.602 1.00 17.81 O ANISOU 755 OG1 THR A 96 2394 2420 1951 731 368 943 O ATOM 756 CG2 THR A 96 22.879 14.735 26.688 1.00 18.35 C ANISOU 756 CG2 THR A 96 2613 1981 2378 707 473 553 C ATOM 757 N LEU A 97 20.177 18.221 26.421 1.00 12.57 N ANISOU 757 N LEU A 97 1868 1760 1146 266 184 183 N ATOM 758 CA LEU A 97 19.041 19.029 26.932 1.00 12.96 C ANISOU 758 CA LEU A 97 1845 1731 1346 368 47 369 C ATOM 759 C LEU A 97 18.255 18.178 27.906 1.00 13.77 C ANISOU 759 C LEU A 97 2023 1759 1449 425 164 193 C ATOM 760 O LEU A 97 18.061 17.025 27.669 1.00 15.41 O ANISOU 760 O LEU A 97 2433 1890 1529 83 533 376 O ATOM 761 CB LEU A 97 18.118 19.475 25.775 1.00 11.64 C ANISOU 761 CB LEU A 97 1612 1529 1280 146 104 105 C ATOM 762 CG LEU A 97 18.726 20.533 24.914 1.00 10.77 C ANISOU 762 CG LEU A 97 1400 1418 1274 139 64 158 C ATOM 763 CD1 LEU A 97 18.001 20.608 23.601 1.00 13.97 C ANISOU 763 CD1 LEU A 97 1517 2138 1650 19 -67 425 C ATOM 764 CD2 LEU A 97 18.709 21.813 25.589 1.00 14.48 C ANISOU 764 CD2 LEU A 97 2073 1879 1547 138 219 259 C ATOM 765 N ASN A 98 17.753 18.812 28.977 1.00 14.50 N ANISOU 765 N ASN A 98 2424 1754 1331 576 343 607 N ATOM 766 CA ASN A 98 17.076 18.128 30.058 1.00 15.60 C ANISOU 766 CA ASN A 98 2273 2117 1537 518 459 512 C ATOM 767 C ASN A 98 15.911 18.958 30.534 1.00 15.56 C ANISOU 767 C ASN A 98 2199 2006 1705 216 297 370 C ATOM 768 O ASN A 98 16.061 20.118 30.826 1.00 18.26 O ANISOU 768 O ASN A 98 2562 2420 1953 656 546 521 O ATOM 769 CB ASN A 98 18.055 17.798 31.230 1.00 16.66 C ANISOU 769 CB ASN A 98 2660 2227 1440 767 459 601 C ATOM 770 CG ASN A 98 19.140 16.852 30.800 1.00 19.48 C ANISOU 770 CG ASN A 98 2633 2512 2257 710 540 873 C ATOM 771 OD1 ASN A 98 18.924 15.608 30.827 1.00 22.18 O ANISOU 771 OD1 ASN A 98 3392 2600 2433 1024 650 890 O ATOM 772 ND2 ASN A 98 20.186 17.375 30.236 1.00 19.32 N ANISOU 772 ND2 ASN A 98 2621 3228 1492 809 317 462 N ATOM 773 N PHE A 99 14.824 18.328 30.719 1.00 18.27 N ANISOU 773 N PHE A 99 2293 2165 2483 479 599 431 N ATOM 774 CA PHE A 99 13.679 18.998 31.345 1.00 18.40 C ANISOU 774 CA PHE A 99 2316 2335 2339 405 542 390 C ATOM 775 C PHE A 99 12.735 17.947 32.006 1.00 22.44 C ANISOU 775 C PHE A 99 2771 2766 2988 365 879 564 C ATOM 776 O PHE A 99 13.146 16.777 32.048 1.00 23.51 O ANISOU 776 O PHE A 99 3011 2778 3141 -21 1157 429 O ATOM 777 CB PHE A 99 12.933 19.918 30.343 1.00 20.12 C ANISOU 777 CB PHE A 99 2349 2488 2805 458 472 451 C ATOM 778 CG PHE A 99 12.351 19.205 29.167 1.00 20.26 C ANISOU 778 CG PHE A 99 2620 2607 2467 389 529 658 C ATOM 779 CD1 PHE A 99 13.075 19.057 28.024 1.00 25.24 C ANISOU 779 CD1 PHE A 99 3367 3704 2518 37 702 350 C ATOM 780 CD2 PHE A 99 11.026 18.889 29.137 1.00 28.26 C ANISOU 780 CD2 PHE A 99 3101 3626 4008 -401 126 -219 C ATOM 781 CE1 PHE A 99 12.509 18.483 26.918 1.00 24.03 C ANISOU 781 CE1 PHE A 99 3344 3712 2072 243 608 619 C ATOM 782 CE2 PHE A 99 10.500 18.330 28.110 1.00 27.07 C ANISOU 782 CE2 PHE A 99 3058 4144 3080 -145 266 407 C ATOM 783 CZ PHE A 99 11.259 18.123 26.946 1.00 29.77 C ANISOU 783 CZ PHE A 99 3638 4195 3476 -4 361 250 C ATOM 784 OXT PHE A 99 11.671 18.362 32.563 1.00 25.87 O ANISOU 784 OXT PHE A 99 2967 3709 3152 515 1177 413 O TER 785 PHE A 99 ATOM 786 N PRO B 1 12.872 14.625 30.481 1.00 26.37 N ANISOU 786 N PRO B 1 3042 3350 3625 -477 652 252 N ATOM 787 CA PRO B 1 13.702 13.683 29.741 1.00 27.13 C ANISOU 787 CA PRO B 1 3384 3299 3624 -425 522 226 C ATOM 788 C PRO B 1 14.927 14.281 29.298 1.00 23.81 C ANISOU 788 C PRO B 1 3223 2955 2869 -414 900 326 C ATOM 789 O PRO B 1 15.187 15.454 29.666 1.00 25.05 O ANISOU 789 O PRO B 1 3459 2701 3356 -51 1089 790 O ATOM 790 CB PRO B 1 12.833 13.323 28.535 1.00 30.44 C ANISOU 790 CB PRO B 1 3716 3921 3927 -391 335 67 C ATOM 791 CG PRO B 1 11.907 14.442 28.388 1.00 32.22 C ANISOU 791 CG PRO B 1 4015 4166 4058 -198 -76 -175 C ATOM 792 CD PRO B 1 11.782 15.127 29.670 1.00 29.07 C ANISOU 792 CD PRO B 1 3300 4055 3690 -54 503 177 C ATOM 793 N GLN B 2 15.784 13.457 28.795 1.00 23.48 N ANISOU 793 N GLN B 2 3376 2730 2815 -292 965 911 N ATOM 794 CA GLN B 2 17.042 13.870 28.261 1.00 22.76 C ANISOU 794 CA GLN B 2 3099 2655 2893 33 833 489 C ATOM 795 C GLN B 2 17.085 13.741 26.716 1.00 22.86 C ANISOU 795 C GLN B 2 3311 2366 3007 -222 721 386 C ATOM 796 O GLN B 2 16.745 12.674 26.125 1.00 22.96 O ANISOU 796 O GLN B 2 3552 2280 2891 -216 1041 562 O ATOM 797 CB GLN B 2 18.163 13.040 28.867 1.00 24.33 C ANISOU 797 CB GLN B 2 3380 2907 2954 152 831 655 C ATOM 798 CG GLN B 2 19.454 13.476 28.448 1.00 23.12 C ANISOU 798 CG GLN B 2 3076 2295 3414 429 678 649 C ATOM 799 CD GLN B 2 20.528 12.781 29.156 1.00 26.04 C ANISOU 799 CD GLN B 2 3692 2381 3820 860 323 545 C ATOM 800 OE1 GLN B 2 21.120 11.784 28.599 1.00 28.07 O ANISOU 800 OE1 GLN B 2 3730 2670 4265 726 1007 751 O ATOM 801 NE2 GLN B 2 20.950 13.335 30.364 1.00 26.69 N ANISOU 801 NE2 GLN B 2 3960 2922 3256 988 268 1028 N ATOM 802 N ILE B 3 17.463 14.836 26.069 1.00 20.40 N ANISOU 802 N ILE B 3 3230 2038 2480 -290 1141 119 N ATOM 803 CA ILE B 3 17.585 14.885 24.634 1.00 20.06 C ANISOU 803 CA ILE B 3 2973 2275 2373 -274 668 -250 C ATOM 804 C ILE B 3 19.008 15.052 24.193 1.00 18.06 C ANISOU 804 C ILE B 3 2924 1857 2080 257 778 -143 C ATOM 805 O ILE B 3 19.716 15.949 24.638 1.00 16.86 O ANISOU 805 O ILE B 3 2756 2014 1634 234 657 189 O ATOM 806 CB ILE B 3 16.716 15.956 24.095 1.00 18.75 C ANISOU 806 CB ILE B 3 2620 2561 1940 -243 823 -243 C ATOM 807 CG1 ILE B 3 15.336 15.680 24.509 1.00 24.56 C ANISOU 807 CG1 ILE B 3 2935 3525 2871 -45 617 -32 C ATOM 808 CG2 ILE B 3 16.817 16.033 22.581 1.00 21.61 C ANISOU 808 CG2 ILE B 3 3628 2687 1894 -814 1009 39 C ATOM 809 CD1 ILE B 3 14.593 16.522 24.230 1.00 22.20 C ANISOU 809 CD1 ILE B 3 2452 3010 2970 135 532 330 C ATOM 810 N THR B 4 19.478 13.985 23.540 1.00 20.89 N ANISOU 810 N THR B 4 3890 1647 2398 68 1561 46 N ATOM 811 CA THR B 4 20.674 13.936 22.871 1.00 19.54 C ANISOU 811 CA THR B 4 3027 1726 2670 524 834 443 C ATOM 812 C THR B 4 20.847 14.999 21.796 1.00 14.64 C ANISOU 812 C THR B 4 2465 1479 1618 -123 545 -37 C ATOM 813 O THR B 4 19.897 15.354 21.179 1.00 16.96 O ANISOU 813 O THR B 4 2319 2372 1751 -669 417 -292 O ATOM 814 CB THR B 4 20.756 12.384 22.010 1.00 19.57 C ANISOU 814 CB THR B 4 2777 2358 2298 -434 243 -381 C ATOM 815 OG1 THR B 4 21.890 12.259 21.599 1.00 22.11 O ANISOU 815 OG1 THR B 4 3293 2181 2926 545 -417 -689 O ATOM 816 CG2 THR B 4 19.934 12.449 20.615 1.00 25.26 C ANISOU 816 CG2 THR B 4 3049 1874 4674 -354 -1219 -573 C ATOM 817 N LEU B 5 22.106 15.314 21.454 1.00 11.97 N ANISOU 817 N LEU B 5 1924 1174 1450 49 -120 -69 N ATOM 818 CA LEU B 5 22.356 16.291 20.383 1.00 9.93 C ANISOU 818 CA LEU B 5 1468 972 1331 28 79 98 C ATOM 819 C LEU B 5 23.064 15.662 19.173 1.00 10.10 C ANISOU 819 C LEU B 5 1166 1139 1531 -14 -1 -62 C ATOM 820 O LEU B 5 23.510 16.363 18.276 1.00 10.06 O ANISOU 820 O LEU B 5 1406 1156 1260 25 -2 -80 O ATOM 821 CB LEU B 5 23.104 17.470 20.914 1.00 10.43 C ANISOU 821 CB LEU B 5 1513 1157 1291 245 -110 -99 C ATOM 822 CG LEU B 5 22.317 18.306 21.955 1.00 10.63 C ANISOU 822 CG LEU B 5 1514 1052 1472 47 -4 -60 C ATOM 823 CD1 LEU B 5 23.196 19.343 22.547 1.00 11.55 C ANISOU 823 CD1 LEU B 5 1749 1282 1357 287 -122 -18 C ATOM 824 CD2 LEU B 5 21.099 18.935 21.357 1.00 11.34 C ANISOU 824 CD2 LEU B 5 1591 1387 1331 214 88 -74 C ATOM 825 N TRP B 6 23.052 14.325 19.078 1.00 10.96 N ANISOU 825 N TRP B 6 1397 1184 1582 132 87 0 N ATOM 826 CA TRP B 6 23.524 13.655 17.876 1.00 11.27 C ANISOU 826 CA TRP B 6 1414 1160 1708 261 80 -141 C ATOM 827 C TRP B 6 22.725 14.056 16.667 1.00 11.44 C ANISOU 827 C TRP B 6 1413 1413 1519 297 -7 -313 C ATOM 828 O TRP B 6 23.249 14.045 15.540 1.00 14.13 O ANISOU 828 O TRP B 6 1458 2165 1745 440 98 -389 O ATOM 829 CB TRP B 6 23.478 12.139 18.030 1.00 11.89 C ANISOU 829 CB TRP B 6 1304 1211 2000 144 -73 -218 C ATOM 830 CG TRP B 6 24.383 11.562 19.008 1.00 11.74 C ANISOU 830 CG TRP B 6 1629 1183 1649 147 85 -35 C ATOM 831 CD1 TRP B 6 24.028 10.776 20.065 1.00 16.18 C ANISOU 831 CD1 TRP B 6 2374 1880 1893 -319 -42 73 C ATOM 832 CD2 TRP B 6 25.766 11.520 18.949 1.00 12.39 C ANISOU 832 CD2 TRP B 6 1734 1152 1820 148 -130 131 C ATOM 833 NE1 TRP B 6 25.113 10.313 20.685 1.00 18.51 N ANISOU 833 NE1 TRP B 6 2824 1790 2418 -437 -429 799 N ATOM 834 CE2 TRP B 6 26.198 10.655 20.006 1.00 15.16 C ANISOU 834 CE2 TRP B 6 1913 1835 2009 28 -431 0 C ATOM 835 CE3 TRP B 6 26.711 12.015 18.081 1.00 14.34 C ANISOU 835 CE3 TRP B 6 1605 1487 2355 213 17 45 C ATOM 836 CZ2 TRP B 6 27.520 10.356 20.222 1.00 17.51 C ANISOU 836 CZ2 TRP B 6 2416 1974 2261 339 -410 88 C ATOM 837 CZ3 TRP B 6 28.083 11.737 18.360 1.00 17.74 C ANISOU 837 CZ3 TRP B 6 1956 2190 2595 -23 4 150 C ATOM 838 CH2 TRP B 6 28.438 10.909 19.395 1.00 18.15 C ANISOU 838 CH2 TRP B 6 1928 2060 2908 434 -205 273 C ATOM 839 N LYS B 7 21.454 14.304 16.845 1.00 11.00 N ANISOU 839 N LYS B 7 1392 1242 1542 120 48 -121 N ATOM 840 CA LYS B 7 20.574 14.755 15.767 1.00 10.96 C ANISOU 840 CA LYS B 7 1382 1343 1437 143 18 -323 C ATOM 841 C LYS B 7 19.888 16.049 16.244 1.00 9.99 C ANISOU 841 C LYS B 7 1204 1286 1303 50 42 -244 C ATOM 842 O LYS B 7 19.980 16.436 17.400 1.00 10.64 O ANISOU 842 O LYS B 7 1483 1216 1343 144 -45 -228 O ATOM 843 CB LYS B 7 19.508 13.669 15.406 1.00 13.34 C ANISOU 843 CB LYS B 7 1758 1355 1952 335 -207 -290 C ATOM 844 CG LYS B 7 18.559 13.314 16.346 1.00 18.18 C ANISOU 844 CG LYS B 7 2540 1868 2498 47 -147 -130 C ATOM 845 CD LYS B 7 17.454 12.215 15.713 1.00 24.02 C ANISOU 845 CD LYS B 7 2950 2432 3743 107 -112 -274 C ATOM 846 CE LYS B 7 16.544 11.634 16.772 1.00 26.45 C ANISOU 846 CE LYS B 7 3233 2397 4419 272 191 -138 C ATOM 847 NZ LYS B 7 15.347 10.832 16.155 1.00 36.56 N ANISOU 847 NZ LYS B 7 4389 4117 5385 -92 -799 -592 N ATOM 848 N ARG B 8 19.212 16.707 15.362 1.00 10.71 N ANISOU 848 N ARG B 8 1339 1407 1324 77 -128 -232 N ATOM 849 CA ARG B 8 18.504 17.931 15.739 1.00 10.03 C ANISOU 849 CA ARG B 8 1209 1321 1279 141 -48 -279 C ATOM 850 C ARG B 8 17.504 17.647 16.813 1.00 10.29 C ANISOU 850 C ARG B 8 1217 1205 1486 -114 70 -197 C ATOM 851 O ARG B 8 16.778 16.643 16.718 1.00 11.64 O ANISOU 851 O ARG B 8 1356 1204 1861 -25 62 -330 O ATOM 852 CB ARG B 8 17.799 18.508 14.549 1.00 11.87 C ANISOU 852 CB ARG B 8 1534 1404 1570 70 3 -29 C ATOM 853 CG ARG B 8 18.728 19.074 13.465 1.00 12.33 C ANISOU 853 CG ARG B 8 1602 1692 1391 -47 -228 -38 C ATOM 854 CD ARG B 8 17.984 19.805 12.366 1.00 16.65 C ANISOU 854 CD ARG B 8 2130 2944 1252 -206 -10 250 C ATOM 855 NE ARG B 8 18.893 20.425 11.448 1.00 20.33 N ANISOU 855 NE ARG B 8 2397 3729 1598 -444 -259 593 N ATOM 856 CZ ARG B 8 18.528 21.454 10.553 1.00 20.26 C ANISOU 856 CZ ARG B 8 2607 2716 2374 -15 69 86 C ATOM 857 NH1 ARG B 8 17.356 22.175 10.798 1.00 29.12 N ANISOU 857 NH1 ARG B 8 2366 3661 5035 621 8 2402 N ATOM 858 NH2 ARG B 8 19.452 21.980 9.735 1.00 19.66 N ANISOU 858 NH2 ARG B 8 2581 2763 2126 66 -282 92 N ATOM 859 N PRO B 9 17.392 18.489 17.828 1.00 9.33 N ANISOU 859 N PRO B 9 1172 1112 1261 25 86 -43 N ATOM 860 CA PRO B 9 16.482 18.214 18.959 1.00 10.43 C ANISOU 860 CA PRO B 9 1158 1132 1672 95 53 127 C ATOM 861 C PRO B 9 15.065 18.681 18.623 1.00 9.79 C ANISOU 861 C PRO B 9 1198 1151 1369 -13 171 -15 C ATOM 862 O PRO B 9 14.547 19.634 19.165 1.00 10.89 O ANISOU 862 O PRO B 9 1304 1241 1590 82 27 -90 O ATOM 863 CB PRO B 9 17.093 19.015 20.102 1.00 10.83 C ANISOU 863 CB PRO B 9 1321 1352 1439 194 85 11 C ATOM 864 CG PRO B 9 17.775 20.173 19.393 1.00 10.48 C ANISOU 864 CG PRO B 9 1266 1346 1367 48 10 -145 C ATOM 865 CD PRO B 9 18.340 19.575 18.137 1.00 9.92 C ANISOU 865 CD PRO B 9 1161 1267 1340 -54 -27 -352 C ATOM 866 N LEU B 10 14.429 17.958 17.701 1.00 11.79 N ANISOU 866 N LEU B 10 1264 1487 1726 -8 90 -250 N ATOM 867 CA LEU B 10 13.067 18.190 17.302 1.00 11.46 C ANISOU 867 CA LEU B 10 1145 1432 1774 -82 -96 -195 C ATOM 868 C LEU B 10 12.110 17.479 18.202 1.00 13.24 C ANISOU 868 C LEU B 10 1487 1206 2336 31 13 4 C ATOM 869 O LEU B 10 12.273 16.330 18.487 1.00 15.54 O ANISOU 869 O LEU B 10 1564 1395 2942 16 36 104 O ATOM 870 CB LEU B 10 12.893 17.698 15.904 1.00 15.18 C ANISOU 870 CB LEU B 10 1619 1890 2256 -22 -348 -391 C ATOM 871 CG LEU B 10 13.632 18.463 14.814 1.00 16.90 C ANISOU 871 CG LEU B 10 2048 2834 1538 147 -140 -465 C ATOM 872 CD1 LEU B 10 13.660 17.698 13.525 1.00 23.06 C ANISOU 872 CD1 LEU B 10 3357 3121 2283 240 105 -664 C ATOM 873 CD2 LEU B 10 12.973 19.930 14.586 1.00 18.90 C ANISOU 873 CD2 LEU B 10 2581 2319 2278 -269 -185 -177 C ATOM 874 N VAL B 11 11.109 18.190 18.637 1.00 12.06 N ANISOU 874 N VAL B 11 1235 1382 1961 81 70 159 N ATOM 875 CA VAL B 11 10.054 17.653 19.463 1.00 13.10 C ANISOU 875 CA VAL B 11 1309 1635 2032 80 152 194 C ATOM 876 C VAL B 11 8.702 18.109 18.995 1.00 13.85 C ANISOU 876 C VAL B 11 1341 1697 2224 -208 -62 177 C ATOM 877 O VAL B 11 8.596 19.022 18.162 1.00 14.46 O ANISOU 877 O VAL B 11 1386 1767 2340 -158 -64 361 O ATOM 878 CB VAL B 11 10.228 18.057 20.944 1.00 16.23 C ANISOU 878 CB VAL B 11 1727 2420 2018 20 273 220 C ATOM 879 CG1 VAL B 11 11.540 17.546 21.485 1.00 18.98 C ANISOU 879 CG1 VAL B 11 1866 2580 2762 28 -176 490 C ATOM 880 CG2 VAL B 11 10.081 19.562 21.093 1.00 18.48 C ANISOU 880 CG2 VAL B 11 1562 2843 2614 174 223 -510 C ATOM 881 N THR B 12 7.661 17.465 19.473 1.00 14.81 N ANISOU 881 N THR B 12 1281 1906 2438 -166 -14 456 N ATOM 882 CA THR B 12 6.309 17.838 19.125 1.00 16.16 C ANISOU 882 CA THR B 12 1377 2226 2537 -304 -124 105 C ATOM 883 C THR B 12 5.801 18.909 20.042 1.00 15.55 C ANISOU 883 C THR B 12 1251 2318 2339 -105 -25 135 C ATOM 884 O THR B 12 5.855 18.794 21.227 1.00 18.18 O ANISOU 884 O THR B 12 1837 2432 2637 91 232 397 O ATOM 885 CB THR B 12 5.378 16.583 19.163 1.00 17.76 C ANISOU 885 CB THR B 12 1584 2170 2994 -375 73 271 C ATOM 886 OG1 THR B 12 5.901 15.589 18.269 1.00 20.95 O ANISOU 886 OG1 THR B 12 2074 2646 3240 -886 -136 -75 O ATOM 887 CG2 THR B 12 3.970 16.907 18.603 1.00 20.74 C ANISOU 887 CG2 THR B 12 1747 2554 3577 -578 -285 131 C ATOM 888 N ILE B 13 5.216 19.915 19.435 1.00 17.31 N ANISOU 888 N ILE B 13 1454 2202 2918 -142 -5 148 N ATOM 889 CA ILE B 13 4.528 20.982 20.170 1.00 15.98 C ANISOU 889 CA ILE B 13 1315 2047 2708 -76 97 82 C ATOM 890 C ILE B 13 3.097 21.106 19.723 1.00 18.34 C ANISOU 890 C ILE B 13 1846 2132 2989 -377 131 374 C ATOM 891 O ILE B 13 2.746 20.644 18.660 1.00 20.02 O ANISOU 891 O ILE B 13 1554 2445 3606 34 -332 267 O ATOM 892 CB ILE B 13 5.271 22.334 19.947 1.00 16.98 C ANISOU 892 CB ILE B 13 1497 2199 2754 289 95 318 C ATOM 893 CG1 ILE B 13 5.179 22.803 18.552 1.00 16.60 C ANISOU 893 CG1 ILE B 13 1433 2145 2726 23 -78 127 C ATOM 894 CG2 ILE B 13 6.716 22.166 20.292 1.00 16.95 C ANISOU 894 CG2 ILE B 13 1611 2254 2575 -30 -141 410 C ATOM 895 CD1 ILE B 13 5.575 24.223 18.362 1.00 19.27 C ANISOU 895 CD1 ILE B 13 2007 2599 2716 -7 31 548 C ATOM 896 N ARG B 14 2.282 21.748 20.562 1.00 18.55 N ANISOU 896 N ARG B 14 1364 2230 3454 -36 136 235 N ATOM 897 CA ARG B 14 0.890 22.087 20.207 1.00 20.16 C ANISOU 897 CA ARG B 14 1511 2131 4017 -137 209 185 C ATOM 898 C ARG B 14 0.696 23.558 20.381 1.00 14.32 C ANISOU 898 C ARG B 14 1203 1720 2516 24 351 518 C ATOM 899 O ARG B 14 0.979 24.120 21.420 1.00 19.12 O ANISOU 899 O ARG B 14 1755 2112 3395 245 284 523 O ATOM 900 CB ARG B 14 -0.061 21.302 21.031 1.00 23.10 C ANISOU 900 CB ARG B 14 1667 2476 4631 -212 411 412 C ATOM 901 CG ARG B 14 -1.536 21.491 20.625 1.00 27.46 C ANISOU 901 CG ARG B 14 1557 2831 6043 -504 382 626 C ATOM 902 CD ARG B 14 -2.569 20.623 21.489 1.00 29.93 C ANISOU 902 CD ARG B 14 2115 3881 5376 -761 302 697 C ATOM 903 NE ARG B 14 -3.724 21.417 21.858 1.00 33.37 N ANISOU 903 NE ARG B 14 2579 4718 5380 -1075 539 -761 N ATOM 904 CZ ARG B 14 -4.769 21.431 21.213 1.00 41.32 C ANISOU 904 CZ ARG B 14 4391 6070 5237 448 -515 69 C ATOM 905 NH1 ARG B 14 -4.834 20.749 20.077 1.00 50.56 N ANISOU 905 NH1 ARG B 14 6314 6785 6110 -148 -357 -633 N ATOM 906 NH2 ARG B 14 -5.891 22.096 21.696 1.00 40.22 N ANISOU 906 NH2 ARG B 14 4309 5572 5399 -29 -117 226 N ATOM 907 N ILE B 15 0.175 24.179 19.340 1.00 19.64 N ANISOU 907 N ILE B 15 1643 2211 3605 3 495 855 N ATOM 908 CA ILE B 15 -0.056 25.637 19.395 1.00 19.19 C ANISOU 908 CA ILE B 15 2019 2188 3082 254 578 484 C ATOM 909 C ILE B 15 -1.175 25.998 18.496 1.00 20.95 C ANISOU 909 C ILE B 15 1807 2777 3376 -330 438 123 C ATOM 910 O ILE B 15 -1.312 25.453 17.417 1.00 27.04 O ANISOU 910 O ILE B 15 3630 2669 3972 956 -76 -38 O ATOM 911 CB ILE B 15 1.307 26.420 19.037 1.00 19.96 C ANISOU 911 CB ILE B 15 2309 2315 2957 -268 355 472 C ATOM 912 CG1 ILE B 15 1.114 27.923 19.222 1.00 24.87 C ANISOU 912 CG1 ILE B 15 3504 2668 3278 -307 -20 -7 C ATOM 913 CG2 ILE B 15 1.821 26.012 17.700 1.00 19.04 C ANISOU 913 CG2 ILE B 15 2071 2372 2790 -388 32 327 C ATOM 914 CD1 ILE B 15 0.899 28.597 18.094 1.00 27.07 C ANISOU 914 CD1 ILE B 15 3549 2915 3821 697 -5 448 C ATOM 915 N GLY B 16 -2.090 26.882 18.988 1.00 20.74 N ANISOU 915 N GLY B 16 2208 2538 3130 65 35 5 N ATOM 916 CA GLY B 16 -3.192 27.291 18.219 1.00 22.97 C ANISOU 916 CA GLY B 16 2553 2912 3261 145 -298 32 C ATOM 917 C GLY B 16 -4.059 26.119 17.739 1.00 23.82 C ANISOU 917 C GLY B 16 2682 2779 3588 -25 -273 242 C ATOM 918 O GLY B 16 -4.681 26.230 16.696 1.00 28.40 O ANISOU 918 O GLY B 16 3043 3398 4349 -95 -586 447 O ATOM 919 N GLY B 17 -4.102 24.987 18.551 1.00 21.83 N ANISOU 919 N GLY B 17 2252 2668 3371 -73 127 397 N ATOM 920 CA GLY B 17 -4.576 23.593 18.116 1.00 22.44 C ANISOU 920 CA GLY B 17 1566 3576 3385 -977 261 -33 C ATOM 921 C GLY B 17 -4.111 23.010 16.867 1.00 25.99 C ANISOU 921 C GLY B 17 2720 3254 3902 -897 282 -45 C ATOM 922 O GLY B 17 -4.809 22.110 16.302 1.00 29.71 O ANISOU 922 O GLY B 17 2627 3786 4876 -1193 234 -442 O ATOM 923 N GLN B 18 -2.832 23.264 16.528 1.00 24.80 N ANISOU 923 N GLN B 18 1968 2889 4565 -583 -76 0 N ATOM 924 CA GLN B 18 -2.092 22.379 15.603 1.00 24.41 C ANISOU 924 CA GLN B 18 2784 2803 3686 55 -169 87 C ATOM 925 C GLN B 18 -0.876 21.733 16.334 1.00 23.94 C ANISOU 925 C GLN B 18 2429 2751 3915 323 -387 -29 C ATOM 926 O GLN B 18 -0.324 22.311 17.244 1.00 24.70 O ANISOU 926 O GLN B 18 1981 2501 4903 245 -281 -163 O ATOM 927 CB GLN B 18 -1.464 23.176 14.280 1.00 21.11 C ANISOU 927 CB GLN B 18 1756 3078 3183 568 -21 -268 C ATOM 928 CG GLN B 18 -2.397 23.903 13.487 1.00 25.47 C ANISOU 928 CG GLN B 18 2685 3236 3754 427 -388 -3 C ATOM 929 CD GLN B 18 -1.772 24.583 12.336 1.00 26.79 C ANISOU 929 CD GLN B 18 2639 3803 3736 -231 -416 9 C ATOM 930 OE1 GLN B 18 -1.997 24.157 11.119 1.00 34.37 O ANISOU 930 OE1 GLN B 18 4604 4914 3538 -18 -528 -162 O ATOM 931 NE2 GLN B 18 -0.862 25.547 12.618 1.00 30.78 N ANISOU 931 NE2 GLN B 18 2631 4117 4944 -207 -892 51 N ATOM 932 N LEU B 19 -0.581 20.491 15.983 1.00 21.74 N ANISOU 932 N LEU B 19 1672 2418 4170 -264 -575 -117 N ATOM 933 CA LEU B 19 0.629 19.842 16.456 1.00 20.03 C ANISOU 933 CA LEU B 19 1905 2374 3330 -239 -306 146 C ATOM 934 C LEU B 19 1.677 20.061 15.416 1.00 21.22 C ANISOU 934 C LEU B 19 2138 2716 3206 -302 -276 375 C ATOM 935 O LEU B 19 1.401 20.021 14.256 1.00 25.14 O ANISOU 935 O LEU B 19 2573 3166 3812 -445 -1050 270 O ATOM 936 CB LEU B 19 0.407 18.324 16.705 1.00 20.87 C ANISOU 936 CB LEU B 19 2597 2064 3266 -361 -296 -388 C ATOM 937 CG LEU B 19 -0.395 17.872 17.837 1.00 21.62 C ANISOU 937 CG LEU B 19 2778 2578 2858 -492 -434 55 C ATOM 938 CD1 LEU B 19 -0.235 16.385 17.951 1.00 27.22 C ANISOU 938 CD1 LEU B 19 3283 2874 4183 -408 -444 -258 C ATOM 939 CD2 LEU B 19 -0.051 18.486 19.085 1.00 25.61 C ANISOU 939 CD2 LEU B 19 3166 3116 3447 -659 -38 -572 C ATOM 940 N LYS B 20 2.904 20.394 15.854 1.00 19.57 N ANISOU 940 N LYS B 20 1871 2378 3184 -61 -449 322 N ATOM 941 CA LYS B 20 3.968 20.718 14.943 1.00 19.04 C ANISOU 941 CA LYS B 20 2227 2344 2660 -130 -342 304 C ATOM 942 C LYS B 20 5.324 20.100 15.494 1.00 17.50 C ANISOU 942 C LYS B 20 1899 2325 2425 -31 -777 179 C ATOM 943 O LYS B 20 5.444 19.898 16.614 1.00 19.01 O ANISOU 943 O LYS B 20 2111 2651 2459 199 -715 17 O ATOM 944 CB LYS B 20 4.194 22.291 14.853 1.00 19.49 C ANISOU 944 CB LYS B 20 2364 2301 2738 166 -635 145 C ATOM 945 CG LYS B 20 2.958 23.031 14.535 1.00 19.62 C ANISOU 945 CG LYS B 20 2376 2153 2923 101 -217 327 C ATOM 946 CD LYS B 20 3.129 24.473 14.653 1.00 21.62 C ANISOU 946 CD LYS B 20 2498 2298 3417 270 120 558 C ATOM 947 CE LYS B 20 1.970 25.236 14.040 1.00 22.40 C ANISOU 947 CE LYS B 20 1985 3092 3434 -139 -189 530 C ATOM 948 NZ LYS B 20 2.058 25.347 12.538 1.00 23.87 N ANISOU 948 NZ LYS B 20 2435 3246 3386 -239 47 878 N ATOM 949 N GLU B 21 6.300 19.977 14.626 1.00 17.84 N ANISOU 949 N GLU B 21 2147 2013 2618 -496 -783 64 N ATOM 950 CA GLU B 21 7.724 19.613 15.052 1.00 16.17 C ANISOU 950 CA GLU B 21 1897 2006 2237 -336 -685 30 C ATOM 951 C GLU B 21 8.539 20.875 15.132 1.00 15.54 C ANISOU 951 C GLU B 21 1964 1732 2208 -175 -533 72 C ATOM 952 O GLU B 21 8.535 21.698 14.195 1.00 16.25 O ANISOU 952 O GLU B 21 2282 1877 2012 -410 -713 62 O ATOM 953 CB GLU B 21 8.378 18.644 14.034 1.00 18.44 C ANISOU 953 CB GLU B 21 2340 2188 2478 -612 -439 -75 C ATOM 954 CG GLU B 21 7.723 17.274 13.927 1.00 24.39 C ANISOU 954 CG GLU B 21 2643 2842 3780 -878 -397 -205 C ATOM 955 CD GLU B 21 7.663 16.559 15.253 1.00 25.99 C ANISOU 955 CD GLU B 21 3170 2813 3892 -586 -113 -119 C ATOM 956 OE1 GLU B 21 6.500 16.318 15.777 1.00 28.19 O ANISOU 956 OE1 GLU B 21 3035 2798 4876 -704 -11 -542 O ATOM 957 OE2 GLU B 21 8.754 16.121 15.764 1.00 30.07 O ANISOU 957 OE2 GLU B 21 3490 2993 4940 -347 -488 441 O ATOM 958 N ALA B 22 9.254 21.031 16.208 1.00 13.63 N ANISOU 958 N ALA B 22 1672 1496 2009 -132 -406 180 N ATOM 959 CA ALA B 22 10.031 22.247 16.434 1.00 12.58 C ANISOU 959 CA ALA B 22 1587 1293 1899 66 -437 8 C ATOM 960 C ALA B 22 11.360 21.897 17.139 1.00 10.83 C ANISOU 960 C ALA B 22 1399 1415 1299 33 -121 141 C ATOM 961 O ALA B 22 11.439 20.958 17.920 1.00 12.18 O ANISOU 961 O ALA B 22 1337 1371 1920 -14 -87 413 O ATOM 962 CB ALA B 22 9.247 23.191 17.292 1.00 12.98 C ANISOU 962 CB ALA B 22 1587 1549 1795 -44 -306 42 C ATOM 963 N LEU B 23 12.332 22.751 16.910 1.00 11.09 N ANISOU 963 N LEU B 23 1484 1228 1502 -57 -189 198 N ATOM 964 CA LEU B 23 13.662 22.627 17.505 1.00 9.96 C ANISOU 964 CA LEU B 23 1292 1040 1451 90 -79 140 C ATOM 965 C LEU B 23 13.684 23.189 18.884 1.00 9.75 C ANISOU 965 C LEU B 23 1018 1142 1543 68 -67 -184 C ATOM 966 O LEU B 23 13.306 24.369 19.080 1.00 12.57 O ANISOU 966 O LEU B 23 1747 1299 1729 423 -255 -124 O ATOM 967 CB LEU B 23 14.642 23.393 16.707 1.00 12.52 C ANISOU 967 CB LEU B 23 1708 1285 1761 120 252 152 C ATOM 968 CG LEU B 23 15.292 22.940 15.519 1.00 16.52 C ANISOU 968 CG LEU B 23 2020 1696 2560 90 454 80 C ATOM 969 CD1 LEU B 23 16.162 24.055 14.930 1.00 15.74 C ANISOU 969 CD1 LEU B 23 2114 1809 2057 228 700 649 C ATOM 970 CD2 LEU B 23 16.129 21.714 15.762 1.00 16.06 C ANISOU 970 CD2 LEU B 23 1890 1563 2648 349 484 265 C ATOM 971 N LEU B 24 14.219 22.458 19.838 1.00 9.78 N ANISOU 971 N LEU B 24 1240 989 1485 133 -37 -7 N ATOM 972 CA LEU B 24 14.536 23.029 21.136 1.00 10.42 C ANISOU 972 CA LEU B 24 1146 1145 1667 23 -38 -12 C ATOM 973 C LEU B 24 15.858 23.780 21.008 1.00 9.89 C ANISOU 973 C LEU B 24 1222 1123 1413 -9 -5 -71 C ATOM 974 O LEU B 24 16.891 23.139 20.880 1.00 10.79 O ANISOU 974 O LEU B 24 1114 1302 1681 146 -26 -135 O ATOM 975 CB LEU B 24 14.649 21.957 22.196 1.00 11.60 C ANISOU 975 CB LEU B 24 1538 1203 1664 11 51 130 C ATOM 976 CG LEU B 24 13.425 21.106 22.422 1.00 12.65 C ANISOU 976 CG LEU B 24 1579 1395 1829 13 261 86 C ATOM 977 CD1 LEU B 24 13.834 19.936 23.434 1.00 16.75 C ANISOU 977 CD1 LEU B 24 2337 2105 1921 -608 -213 521 C ATOM 978 CD2 LEU B 24 12.223 21.901 22.935 1.00 17.13 C ANISOU 978 CD2 LEU B 24 1703 2158 2648 -310 446 -511 C ATOM 979 N ASP B 25 15.794 25.119 20.987 1.00 9.19 N ANISOU 979 N ASP B 25 1287 1049 1154 62 -30 -12 N ATOM 980 CA ASP B 25 16.906 25.958 20.533 1.00 9.04 C ANISOU 980 CA ASP B 25 1140 1074 1219 166 -4 64 C ATOM 981 C ASP B 25 17.392 26.917 21.582 1.00 9.18 C ANISOU 981 C ASP B 25 1279 1049 1159 82 64 0 C ATOM 982 O ASP B 25 16.856 28.021 21.775 1.00 9.82 O ANISOU 982 O ASP B 25 1307 1152 1270 178 141 -46 O ATOM 983 CB ASP B 25 16.530 26.693 19.313 1.00 8.66 C ANISOU 983 CB ASP B 25 1143 1006 1140 98 148 -84 C ATOM 984 CG ASP B 25 17.674 27.300 18.619 1.00 9.06 C ANISOU 984 CG ASP B 25 1282 1124 1034 211 -17 17 C ATOM 985 OD1 ASP B 25 18.811 27.268 19.209 1.00 9.95 O ANISOU 985 OD1 ASP B 25 1341 1312 1128 18 40 -19 O ATOM 986 OD2 ASP B 25 17.548 27.810 17.484 1.00 10.37 O ANISOU 986 OD2 ASP B 25 1339 1392 1207 107 133 154 O ATOM 987 N THR B 26 18.468 26.541 22.265 1.00 9.25 N ANISOU 987 N THR B 26 1334 1055 1124 205 -30 -15 N ATOM 988 CA THR B 26 19.064 27.393 23.266 1.00 9.41 C ANISOU 988 CA THR B 26 1337 1249 989 247 73 -142 C ATOM 989 C THR B 26 19.709 28.658 22.685 1.00 9.20 C ANISOU 989 C THR B 26 1335 1131 1027 126 6 -169 C ATOM 990 O THR B 26 19.994 29.582 23.434 1.00 10.59 O ANISOU 990 O THR B 26 1698 1161 1162 115 2 -87 O ATOM 991 CB THR B 26 20.092 26.630 24.058 1.00 9.31 C ANISOU 991 CB THR B 26 1474 1322 741 194 186 -219 C ATOM 992 OG1 THR B 26 21.171 26.194 23.211 1.00 9.58 O ANISOU 992 OG1 THR B 26 1437 1189 1011 108 30 -12 O ATOM 993 CG2 THR B 26 19.509 25.427 24.714 1.00 9.94 C ANISOU 993 CG2 THR B 26 1549 1275 952 85 121 66 C ATOM 994 N GLY B 27 19.948 28.682 21.378 1.00 9.31 N ANISOU 994 N GLY B 27 1322 1076 1136 124 145 -161 N ATOM 995 CA GLY B 27 20.481 29.841 20.709 1.00 10.14 C ANISOU 995 CA GLY B 27 1266 1360 1224 -70 36 -56 C ATOM 996 C GLY B 27 19.470 30.904 20.315 1.00 9.76 C ANISOU 996 C GLY B 27 1426 1056 1223 73 75 30 C ATOM 997 O GLY B 27 19.845 31.926 19.780 1.00 11.36 O ANISOU 997 O GLY B 27 1526 1356 1431 -68 187 86 O ATOM 998 N ALA B 28 18.195 30.611 20.502 1.00 9.54 N ANISOU 998 N ALA B 28 1376 1077 1172 45 29 31 N ATOM 999 CA ALA B 28 17.115 31.482 20.082 1.00 10.67 C ANISOU 999 CA ALA B 28 1555 1182 1314 220 150 114 C ATOM 1000 C ALA B 28 16.526 32.175 21.333 1.00 10.65 C ANISOU 1000 C ALA B 28 1465 1201 1380 112 16 42 C ATOM 1001 O ALA B 28 16.056 31.518 22.252 1.00 10.66 O ANISOU 1001 O ALA B 28 1712 1229 1108 104 117 -3 O ATOM 1002 CB ALA B 28 16.023 30.684 19.434 1.00 10.57 C ANISOU 1002 CB ALA B 28 1515 1245 1254 320 76 42 C ATOM 1003 N ASP B 29 16.479 33.509 21.337 1.00 10.60 N ANISOU 1003 N ASP B 29 1726 1082 1217 166 13 54 N ATOM 1004 CA ASP B 29 15.920 34.212 22.459 1.00 11.21 C ANISOU 1004 CA ASP B 29 1847 1179 1232 250 134 -46 C ATOM 1005 C ASP B 29 14.441 33.954 22.545 1.00 12.25 C ANISOU 1005 C ASP B 29 1714 1419 1521 456 186 -198 C ATOM 1006 O ASP B 29 13.881 33.799 23.633 1.00 13.35 O ANISOU 1006 O ASP B 29 1830 1806 1434 382 162 -176 O ATOM 1007 CB ASP B 29 16.151 35.731 22.292 1.00 13.12 C ANISOU 1007 CB ASP B 29 1817 1261 1904 216 -4 -245 C ATOM 1008 CG ASP B 29 17.541 36.137 22.317 1.00 14.78 C ANISOU 1008 CG ASP B 29 2054 1185 2377 179 -142 1 C ATOM 1009 OD1 ASP B 29 18.433 35.462 22.913 1.00 14.23 O ANISOU 1009 OD1 ASP B 29 2074 1549 1783 126 -201 -148 O ATOM 1010 OD2 ASP B 29 17.799 37.300 21.955 1.00 19.65 O ANISOU 1010 OD2 ASP B 29 2570 1616 3279 -236 -379 601 O ATOM 1011 N ASP B 30 13.764 33.955 21.402 1.00 12.01 N ANISOU 1011 N ASP B 30 1678 1467 1415 115 79 41 N ATOM 1012 CA ASP B 30 12.337 33.876 21.321 1.00 12.45 C ANISOU 1012 CA ASP B 30 1756 1625 1348 373 46 89 C ATOM 1013 C ASP B 30 11.926 32.802 20.337 1.00 10.49 C ANISOU 1013 C ASP B 30 1236 1540 1207 364 55 -53 C ATOM 1014 O ASP B 30 12.525 32.664 19.311 1.00 16.23 O ANISOU 1014 O ASP B 30 1724 2651 1791 -226 580 -481 O ATOM 1015 CB ASP B 30 11.662 35.225 20.959 1.00 15.93 C ANISOU 1015 CB ASP B 30 2232 1561 2257 293 -311 -104 C ATOM 1016 CG ASP B 30 11.675 36.200 22.098 1.00 20.71 C ANISOU 1016 CG ASP B 30 3575 2250 2042 576 -42 -122 C ATOM 1017 OD1 ASP B 30 11.163 35.857 23.248 1.00 23.88 O ANISOU 1017 OD1 ASP B 30 4046 2439 2587 1059 506 -153 O ATOM 1018 OD2 ASP B 30 12.190 37.229 21.983 1.00 28.67 O ANISOU 1018 OD2 ASP B 30 5457 2828 2608 -648 309 23 O ATOM 1019 N THR B 31 10.812 32.211 20.597 1.00 11.55 N ANISOU 1019 N THR B 31 1320 1462 1606 224 158 13 N ATOM 1020 CA THR B 31 10.194 31.210 19.777 1.00 10.95 C ANISOU 1020 CA THR B 31 1411 1216 1534 428 131 388 C ATOM 1021 C THR B 31 9.725 31.796 18.437 1.00 10.47 C ANISOU 1021 C THR B 31 1345 1238 1392 321 242 315 C ATOM 1022 O THR B 31 9.052 32.857 18.417 1.00 11.63 O ANISOU 1022 O THR B 31 1476 1275 1665 314 124 328 O ATOM 1023 CB THR B 31 8.996 30.650 20.581 1.00 10.86 C ANISOU 1023 CB THR B 31 1387 1449 1289 241 119 198 C ATOM 1024 OG1 THR B 31 9.532 29.958 21.708 1.00 11.64 O ANISOU 1024 OG1 THR B 31 1514 1650 1256 437 306 428 O ATOM 1025 CG2 THR B 31 8.152 29.702 19.791 1.00 11.82 C ANISOU 1025 CG2 THR B 31 1522 1715 1252 434 347 237 C ATOM 1026 N AVAL B 32 9.986 31.087 17.371 0.50 9.67 N ANISOU 1026 N AVAL B 32 1076 1301 1294 110 64 187 N ATOM 1027 N BVAL B 32 10.038 31.124 17.363 0.50 9.96 N ANISOU 1027 N BVAL B 32 1148 1333 1301 183 -5 122 N ATOM 1028 CA AVAL B 32 9.677 31.536 15.998 0.50 10.27 C ANISOU 1028 CA AVAL B 32 1039 1455 1406 52 -196 185 C ATOM 1029 CA BVAL B 32 9.595 31.576 16.039 0.50 10.37 C ANISOU 1029 CA BVAL B 32 1182 1368 1390 18 -248 147 C ATOM 1030 C AVAL B 32 9.067 30.330 15.302 0.50 10.69 C ANISOU 1030 C AVAL B 32 1471 1443 1147 54 -48 310 C ATOM 1031 C BVAL B 32 9.131 30.396 15.213 0.50 11.58 C ANISOU 1031 C BVAL B 32 1452 1500 1448 188 -54 219 C ATOM 1032 O AVAL B 32 9.653 29.275 15.285 0.50 12.01 O ANISOU 1032 O AVAL B 32 1527 1442 1594 314 -156 144 O ATOM 1033 O BVAL B 32 9.883 29.415 14.984 0.50 10.76 O ANISOU 1033 O BVAL B 32 1355 1288 1444 232 106 336 O ATOM 1034 CB AVAL B 32 10.951 32.007 15.202 0.50 12.58 C ANISOU 1034 CB AVAL B 32 1628 1899 1253 -82 -77 383 C ATOM 1035 CB BVAL B 32 10.613 32.441 15.331 0.50 10.87 C ANISOU 1035 CB BVAL B 32 1396 1405 1327 171 -103 254 C ATOM 1036 CG1AVAL B 32 10.531 32.779 13.929 0.50 14.76 C ANISOU 1036 CG1AVAL B 32 1829 2135 1642 -86 -551 178 C ATOM 1037 CG1BVAL B 32 11.912 31.703 15.139 0.50 9.64 C ANISOU 1037 CG1BVAL B 32 1262 1401 1000 195 -236 91 C ATOM 1038 CG2AVAL B 32 11.851 32.854 16.060 0.50 12.18 C ANISOU 1038 CG2AVAL B 32 1550 1716 1359 262 30 80 C ATOM 1039 CG2BVAL B 32 10.039 32.913 13.931 0.50 12.58 C ANISOU 1039 CG2BVAL B 32 1592 1535 1651 -360 -1 246 C ATOM 1040 N LEU B 33 7.868 30.490 14.756 1.00 11.96 N ANISOU 1040 N LEU B 33 1245 1438 1858 172 -206 200 N ATOM 1041 CA LEU B 33 7.216 29.418 14.074 1.00 11.24 C ANISOU 1041 CA LEU B 33 1406 1489 1376 72 15 218 C ATOM 1042 C LEU B 33 7.002 29.790 12.642 1.00 11.12 C ANISOU 1042 C LEU B 33 1235 1443 1545 -178 -117 122 C ATOM 1043 O LEU B 33 6.810 30.994 12.262 1.00 12.51 O ANISOU 1043 O LEU B 33 1655 1492 1604 -49 -44 281 O ATOM 1044 CB LEU B 33 5.857 29.088 14.678 1.00 13.77 C ANISOU 1044 CB LEU B 33 1693 1802 1735 -245 -162 -53 C ATOM 1045 CG LEU B 33 5.931 28.738 16.215 1.00 16.72 C ANISOU 1045 CG LEU B 33 2294 2264 1791 -131 99 312 C ATOM 1046 CD1 LEU B 33 4.606 28.398 16.743 1.00 18.93 C ANISOU 1046 CD1 LEU B 33 2631 2673 1885 -637 101 323 C ATOM 1047 CD2 LEU B 33 6.875 27.635 16.489 1.00 19.01 C ANISOU 1047 CD2 LEU B 33 2948 2185 2089 85 -221 346 C ATOM 1048 N GLU B 34 6.947 28.752 11.801 1.00 12.53 N ANISOU 1048 N GLU B 34 1722 1536 1501 -115 -18 146 N ATOM 1049 CA GLU B 34 6.660 28.878 10.440 1.00 13.58 C ANISOU 1049 CA GLU B 34 1749 1808 1600 -196 16 156 C ATOM 1050 C GLU B 34 5.322 29.529 10.227 1.00 13.54 C ANISOU 1050 C GLU B 34 1950 1997 1197 -95 -97 60 C ATOM 1051 O GLU B 34 4.419 29.460 11.081 1.00 13.84 O ANISOU 1051 O GLU B 34 1782 1865 1608 -141 -16 418 O ATOM 1052 CB GLU B 34 6.665 27.499 9.785 1.00 14.53 C ANISOU 1052 CB GLU B 34 2040 1883 1596 72 116 -70 C ATOM 1053 CG GLU B 34 8.080 26.765 9.833 1.00 18.78 C ANISOU 1053 CG GLU B 34 2193 2432 2510 112 -225 -197 C ATOM 1054 CD GLU B 34 7.993 25.322 9.455 1.00 20.50 C ANISOU 1054 CD GLU B 34 2415 2349 3026 146 205 -54 C ATOM 1055 OE1 GLU B 34 6.962 24.904 8.970 1.00 28.89 O ANISOU 1055 OE1 GLU B 34 3766 3280 3931 115 -858 -1109 O ATOM 1056 OE2 GLU B 34 9.022 24.587 9.611 1.00 28.63 O ANISOU 1056 OE2 GLU B 34 2705 3342 4828 529 -693 -805 O ATOM 1057 N GLU B 35 5.186 30.158 9.070 1.00 14.04 N ANISOU 1057 N GLU B 35 2031 2214 1087 230 101 110 N ATOM 1058 CA GLU B 35 4.008 30.894 8.764 1.00 14.57 C ANISOU 1058 CA GLU B 35 1929 2190 1414 77 -230 238 C ATOM 1059 C GLU B 35 2.736 30.099 9.033 1.00 15.23 C ANISOU 1059 C GLU B 35 2069 2042 1674 36 -428 99 C ATOM 1060 O GLU B 35 2.618 28.985 8.623 1.00 17.36 O ANISOU 1060 O GLU B 35 2225 2126 2243 -319 -528 18 O ATOM 1061 CB GLU B 35 4.068 31.332 7.305 1.00 17.17 C ANISOU 1061 CB GLU B 35 2435 2465 1621 322 96 128 C ATOM 1062 CG GLU B 35 2.870 32.108 6.843 1.00 20.98 C ANISOU 1062 CG GLU B 35 2953 2773 2245 370 -196 644 C ATOM 1063 CD GLU B 35 2.585 33.345 7.670 1.00 22.72 C ANISOU 1063 CD GLU B 35 3224 2484 2921 740 -365 645 C ATOM 1064 OE1 GLU B 35 1.408 33.515 8.064 1.00 28.18 O ANISOU 1064 OE1 GLU B 35 3828 3495 3383 860 574 768 O ATOM 1065 OE2 GLU B 35 3.546 34.159 7.932 1.00 24.58 O ANISOU 1065 OE2 GLU B 35 4444 2433 2461 301 -225 634 O ATOM 1066 N MET B 36 1.805 30.723 9.840 1.00 14.73 N ANISOU 1066 N MET B 36 1734 2131 1730 -182 -359 256 N ATOM 1067 CA MET B 36 0.527 30.139 10.236 1.00 17.36 C ANISOU 1067 CA MET B 36 1988 2200 2408 -478 -279 146 C ATOM 1068 C MET B 36 -0.407 31.321 10.552 1.00 19.25 C ANISOU 1068 C MET B 36 1910 2701 2701 -293 -265 89 C ATOM 1069 O MET B 36 0.023 32.360 11.007 1.00 18.96 O ANISOU 1069 O MET B 36 1660 2221 3320 68 -108 456 O ATOM 1070 CB MET B 36 0.692 29.236 11.466 1.00 19.82 C ANISOU 1070 CB MET B 36 2259 2658 2613 -566 -95 350 C ATOM 1071 CG MET B 36 1.229 29.898 12.577 1.00 19.29 C ANISOU 1071 CG MET B 36 2509 2393 2425 -143 231 397 C ATOM 1072 SD MET B 36 1.356 28.807 14.099 1.00 22.97 S ANISOU 1072 SD MET B 36 2923 3116 2687 214 131 664 S ATOM 1073 CE MET B 36 -0.360 28.226 14.294 1.00 24.95 C ANISOU 1073 CE MET B 36 2668 3729 3080 274 556 596 C ATOM 1074 N ASN B 37 -1.709 31.132 10.332 1.00 20.26 N ANISOU 1074 N ASN B 37 1792 3083 2820 -475 -82 171 N ATOM 1075 CA ASN B 37 -2.638 32.231 10.517 1.00 21.01 C ANISOU 1075 CA ASN B 37 2125 3453 2404 -119 -174 367 C ATOM 1076 C ASN B 37 -3.266 32.173 11.886 1.00 21.41 C ANISOU 1076 C ASN B 37 2074 3548 2509 -741 253 672 C ATOM 1077 O ASN B 37 -4.454 31.833 12.014 1.00 24.76 O ANISOU 1077 O ASN B 37 1863 4532 3012 -644 22 285 O ATOM 1078 CB ASN B 37 -3.729 32.237 9.417 1.00 25.16 C ANISOU 1078 CB ASN B 37 2584 4030 2944 -116 -461 74 C ATOM 1079 CG ASN B 37 -4.495 33.615 9.318 1.00 28.86 C ANISOU 1079 CG ASN B 37 2634 4647 3681 249 -448 199 C ATOM 1080 OD1 ASN B 37 -5.650 33.678 8.768 1.00 41.63 O ANISOU 1080 OD1 ASN B 37 3805 6512 5500 858 -1657 166 O ATOM 1081 ND2 ASN B 37 -3.954 34.630 9.900 1.00 30.12 N ANISOU 1081 ND2 ASN B 37 3041 4164 4236 -79 140 419 N ATOM 1082 N LEU B 38 -2.522 32.587 12.908 1.00 21.91 N ANISOU 1082 N LEU B 38 1943 3411 2969 -270 -67 663 N ATOM 1083 CA LEU B 38 -3.034 32.656 14.287 1.00 19.95 C ANISOU 1083 CA LEU B 38 2009 2797 2771 -395 -92 571 C ATOM 1084 C LEU B 38 -4.029 33.750 14.449 1.00 21.78 C ANISOU 1084 C LEU B 38 2374 2696 3203 -370 14 686 C ATOM 1085 O LEU B 38 -3.793 34.868 14.014 1.00 21.95 O ANISOU 1085 O LEU B 38 2841 2389 3110 -496 -219 816 O ATOM 1086 CB LEU B 38 -1.936 32.923 15.259 1.00 22.74 C ANISOU 1086 CB LEU B 38 2604 2808 3224 -625 -396 729 C ATOM 1087 CG LEU B 38 -1.069 31.902 15.648 1.00 25.13 C ANISOU 1087 CG LEU B 38 2741 2572 4232 -529 -718 492 C ATOM 1088 CD1 LEU B 38 0.047 32.416 16.502 1.00 21.59 C ANISOU 1088 CD1 LEU B 38 2760 2575 2864 -467 -487 878 C ATOM 1089 CD2 LEU B 38 -1.812 30.783 16.428 1.00 24.06 C ANISOU 1089 CD2 LEU B 38 2393 2669 4081 -233 -599 627 C ATOM 1090 N PRO B 39 -4.979 33.534 15.305 1.00 21.55 N ANISOU 1090 N PRO B 39 2268 2625 3292 -369 -52 309 N ATOM 1091 CA PRO B 39 -5.876 34.619 15.681 1.00 22.44 C ANISOU 1091 CA PRO B 39 2471 2940 3113 -47 -201 266 C ATOM 1092 C PRO B 39 -5.241 35.554 16.642 1.00 21.52 C ANISOU 1092 C PRO B 39 2190 2997 2987 -444 186 343 C ATOM 1093 O PRO B 39 -4.319 35.148 17.343 1.00 23.61 O ANISOU 1093 O PRO B 39 2429 3611 2929 -812 54 736 O ATOM 1094 CB PRO B 39 -7.020 33.916 16.322 1.00 25.66 C ANISOU 1094 CB PRO B 39 2585 3301 3861 -248 -19 91 C ATOM 1095 CG PRO B 39 -6.481 32.552 16.730 1.00 24.43 C ANISOU 1095 CG PRO B 39 2648 2971 3660 -441 416 84 C ATOM 1096 CD PRO B 39 -5.407 32.216 15.866 1.00 24.15 C ANISOU 1096 CD PRO B 39 2434 2995 3743 -591 332 369 C ATOM 1097 N GLY B 40 -5.745 36.767 16.704 1.00 24.99 N ANISOU 1097 N GLY B 40 3225 3284 2984 -408 218 221 N ATOM 1098 CA GLY B 40 -5.375 37.721 17.748 1.00 25.65 C ANISOU 1098 CA GLY B 40 3273 3280 3192 -731 500 147 C ATOM 1099 C GLY B 40 -4.521 38.948 17.226 1.00 24.98 C ANISOU 1099 C GLY B 40 2781 3194 3516 -491 429 160 C ATOM 1100 O GLY B 40 -4.058 38.973 16.068 1.00 24.97 O ANISOU 1100 O GLY B 40 2638 3253 3597 210 410 323 O ATOM 1101 N LYS B 41 -4.249 39.859 18.112 1.00 22.61 N ANISOU 1101 N LYS B 41 2563 2772 3253 50 793 138 N ATOM 1102 CA LYS B 41 -3.396 41.006 17.797 1.00 22.18 C ANISOU 1102 CA LYS B 41 2118 2784 3526 164 377 97 C ATOM 1103 C LYS B 41 -1.942 40.606 17.690 1.00 19.98 C ANISOU 1103 C LYS B 41 2115 2402 3075 457 642 355 C ATOM 1104 O LYS B 41 -1.494 39.687 18.375 1.00 21.49 O ANISOU 1104 O LYS B 41 2325 2479 3361 343 927 908 O ATOM 1105 CB LYS B 41 -3.527 42.037 18.815 1.00 24.29 C ANISOU 1105 CB LYS B 41 2044 3459 3725 623 599 -115 C ATOM 1106 N TRP B 42 -1.191 41.380 16.943 1.00 17.83 N ANISOU 1106 N TRP B 42 1632 2520 2620 492 396 484 N ATOM 1107 CA TRP B 42 0.227 41.166 16.820 1.00 16.77 C ANISOU 1107 CA TRP B 42 1782 2153 2434 519 385 416 C ATOM 1108 C TRP B 42 0.923 42.476 16.515 1.00 19.20 C ANISOU 1108 C TRP B 42 1959 2160 3176 666 374 596 C ATOM 1109 O TRP B 42 0.256 43.504 16.205 1.00 19.32 O ANISOU 1109 O TRP B 42 2220 2130 2990 730 323 668 O ATOM 1110 CB TRP B 42 0.489 40.155 15.762 1.00 17.79 C ANISOU 1110 CB TRP B 42 1968 2287 2503 123 252 481 C ATOM 1111 CG TRP B 42 -0.066 40.502 14.375 1.00 20.38 C ANISOU 1111 CG TRP B 42 2091 3156 2494 667 233 228 C ATOM 1112 CD1 TRP B 42 -1.329 40.198 13.883 1.00 25.45 C ANISOU 1112 CD1 TRP B 42 2674 3744 3251 -27 39 562 C ATOM 1113 CD2 TRP B 42 0.618 41.195 13.312 1.00 21.83 C ANISOU 1113 CD2 TRP B 42 2300 2580 3413 686 128 757 C ATOM 1114 NE1 TRP B 42 -1.460 40.670 12.600 1.00 27.98 N ANISOU 1114 NE1 TRP B 42 2867 3873 3891 507 -435 1131 N ATOM 1115 CE2 TRP B 42 -0.312 41.351 12.247 1.00 25.46 C ANISOU 1115 CE2 TRP B 42 2263 3599 3812 944 -98 783 C ATOM 1116 CE3 TRP B 42 1.862 41.799 13.189 1.00 20.31 C ANISOU 1116 CE3 TRP B 42 2780 2318 2616 89 479 584 C ATOM 1117 CZ2 TRP B 42 0.025 41.973 11.050 1.00 29.34 C ANISOU 1117 CZ2 TRP B 42 3756 3539 3853 242 -268 654 C ATOM 1118 CZ3 TRP B 42 2.172 42.434 12.012 1.00 24.40 C ANISOU 1118 CZ3 TRP B 42 3727 3039 2504 -16 6 558 C ATOM 1119 CH2 TRP B 42 1.280 42.439 10.927 1.00 26.01 C ANISOU 1119 CH2 TRP B 42 3990 3299 2593 -263 -181 749 C ATOM 1120 N LYS B 43 2.250 42.460 16.608 1.00 17.48 N ANISOU 1120 N LYS B 43 1697 2112 2830 577 645 679 N ATOM 1121 CA LYS B 43 3.093 43.659 16.384 1.00 17.00 C ANISOU 1121 CA LYS B 43 1564 2182 2712 536 551 372 C ATOM 1122 C LYS B 43 4.218 43.209 15.433 1.00 15.16 C ANISOU 1122 C LYS B 43 1641 1932 2185 600 295 449 C ATOM 1123 O LYS B 43 4.762 42.138 15.617 1.00 15.41 O ANISOU 1123 O LYS B 43 1781 1572 2499 631 376 412 O ATOM 1124 CB LYS B 43 3.747 44.098 17.746 1.00 21.14 C ANISOU 1124 CB LYS B 43 2264 2652 3116 13 1159 -364 C ATOM 1125 N PRO B 44 4.634 44.042 14.449 1.00 14.87 N ANISOU 1125 N PRO B 44 1682 1627 2339 386 382 483 N ATOM 1126 CA PRO B 44 5.751 43.669 13.585 1.00 16.08 C ANISOU 1126 CA PRO B 44 1850 1879 2378 228 227 406 C ATOM 1127 C PRO B 44 7.053 43.707 14.292 1.00 14.07 C ANISOU 1127 C PRO B 44 1662 1714 1970 4 312 75 C ATOM 1128 O PRO B 44 7.311 44.549 15.161 1.00 15.46 O ANISOU 1128 O PRO B 44 1761 1810 2301 300 247 53 O ATOM 1129 CB PRO B 44 5.668 44.716 12.424 1.00 18.36 C ANISOU 1129 CB PRO B 44 2055 2539 2379 201 315 596 C ATOM 1130 CG PRO B 44 4.908 45.753 12.928 1.00 20.62 C ANISOU 1130 CG PRO B 44 3406 1914 2513 140 265 528 C ATOM 1131 CD PRO B 44 4.013 45.294 14.021 1.00 16.20 C ANISOU 1131 CD PRO B 44 1729 1651 2772 311 55 491 C ATOM 1132 N LYS B 45 7.976 42.792 13.856 1.00 12.76 N ANISOU 1132 N LYS B 45 1664 1462 1718 271 307 83 N ATOM 1133 CA LYS B 45 9.294 42.745 14.409 1.00 13.22 C ANISOU 1133 CA LYS B 45 1638 1631 1754 306 163 46 C ATOM 1134 C LYS B 45 10.238 42.236 13.336 1.00 11.33 C ANISOU 1134 C LYS B 45 1463 1311 1529 64 43 75 C ATOM 1135 O LYS B 45 9.804 41.550 12.424 1.00 12.84 O ANISOU 1135 O LYS B 45 1512 1558 1809 -229 148 -180 O ATOM 1136 CB LYS B 45 9.262 41.746 15.645 1.00 14.85 C ANISOU 1136 CB LYS B 45 1987 1807 1846 260 442 -2 C ATOM 1137 CG LYS B 45 10.453 41.652 16.442 1.00 16.26 C ANISOU 1137 CG LYS B 45 2183 1898 2096 12 353 177 C ATOM 1138 CD LYS B 45 10.251 40.656 17.625 1.00 18.57 C ANISOU 1138 CD LYS B 45 2892 2046 2116 85 201 394 C ATOM 1139 CE LYS B 45 11.388 40.350 18.247 1.00 24.01 C ANISOU 1139 CE LYS B 45 2694 3450 2976 31 341 97 C ATOM 1140 NZ LYS B 45 11.766 41.253 19.087 1.00 31.36 N ANISOU 1140 NZ LYS B 45 3961 3817 4136 -645 -183 -226 N ATOM 1141 N AMET B 46 11.526 42.568 13.486 0.50 10.65 N ANISOU 1141 N AMET B 46 1552 1320 1174 -55 85 -138 N ATOM 1142 N BMET B 46 11.506 42.525 13.476 0.50 10.79 N ANISOU 1142 N BMET B 46 1559 1343 1196 -32 117 -120 N ATOM 1143 CA AMET B 46 12.615 41.969 12.670 0.50 10.47 C ANISOU 1143 CA AMET B 46 1472 1202 1302 -16 83 -247 C ATOM 1144 CA BMET B 46 12.502 41.909 12.624 0.50 10.99 C ANISOU 1144 CA BMET B 46 1512 1341 1321 96 122 -176 C ATOM 1145 C AMET B 46 13.445 41.164 13.610 0.50 11.30 C ANISOU 1145 C AMET B 46 1539 1514 1239 -77 -19 -197 C ATOM 1146 C BMET B 46 13.537 41.236 13.513 0.50 11.55 C ANISOU 1146 C BMET B 46 1605 1611 1172 37 19 -176 C ATOM 1147 O AMET B 46 13.809 41.643 14.668 0.50 14.12 O ANISOU 1147 O AMET B 46 1911 2037 1417 312 -194 -420 O ATOM 1148 O BMET B 46 13.898 41.764 14.567 0.50 14.14 O ANISOU 1148 O BMET B 46 1842 1974 1554 243 -320 -424 O ATOM 1149 CB AMET B 46 13.466 43.059 12.058 0.50 11.76 C ANISOU 1149 CB AMET B 46 1245 1571 1652 -220 159 -184 C ATOM 1150 CB BMET B 46 13.111 42.949 11.663 0.50 12.91 C ANISOU 1150 CB BMET B 46 1541 1544 1818 -98 374 -173 C ATOM 1151 CG AMET B 46 12.789 43.857 11.007 0.50 13.09 C ANISOU 1151 CG AMET B 46 1808 1271 1893 -72 6 -82 C ATOM 1152 CG BMET B 46 12.029 43.400 10.392 0.50 11.70 C ANISOU 1152 CG BMET B 46 1123 1023 2298 294 853 245 C ATOM 1153 SD AMET B 46 12.639 42.926 9.468 0.50 17.21 S ANISOU 1153 SD AMET B 46 2911 1698 1929 -647 -352 31 S ATOM 1154 SD BMET B 46 12.735 44.629 9.414 0.50 13.86 S ANISOU 1154 SD BMET B 46 2042 1471 1751 -322 63 -16 S ATOM 1155 CE AMET B 46 14.151 43.490 8.578 0.50 19.01 C ANISOU 1155 CE AMET B 46 2954 2253 2014 -142 167 -188 C ATOM 1156 CE BMET B 46 14.231 43.876 8.903 0.50 12.74 C ANISOU 1156 CE BMET B 46 1683 1763 1392 -424 -170 129 C ATOM 1157 N ILE B 47 13.842 39.964 13.186 1.00 10.84 N ANISOU 1157 N ILE B 47 1302 1474 1343 42 47 -247 N ATOM 1158 CA ILE B 47 14.813 39.177 13.940 1.00 11.08 C ANISOU 1158 CA ILE B 47 1332 1584 1293 -57 89 -142 C ATOM 1159 C ILE B 47 15.931 38.753 13.009 1.00 10.70 C ANISOU 1159 C ILE B 47 1336 1432 1296 -30 71 -66 C ATOM 1160 O ILE B 47 15.724 38.518 11.826 1.00 11.02 O ANISOU 1160 O ILE B 47 1459 1480 1247 -130 137 -107 O ATOM 1161 CB ILE B 47 14.181 37.966 14.625 1.00 11.77 C ANISOU 1161 CB ILE B 47 1255 1855 1360 176 123 146 C ATOM 1162 CG1 ILE B 47 13.549 37.010 13.637 1.00 11.90 C ANISOU 1162 CG1 ILE B 47 1347 1691 1483 100 5 270 C ATOM 1163 CG2 ILE B 47 13.173 38.421 15.662 1.00 13.94 C ANISOU 1163 CG2 ILE B 47 1676 2061 1557 24 267 -111 C ATOM 1164 CD1 ILE B 47 13.022 35.724 14.291 1.00 13.69 C ANISOU 1164 CD1 ILE B 47 1674 1731 1794 -87 -54 376 C ATOM 1165 N GLY B 48 17.120 38.669 13.564 1.00 11.46 N ANISOU 1165 N GLY B 48 1403 1586 1364 99 135 -59 N ATOM 1166 CA GLY B 48 18.320 38.474 12.794 1.00 13.20 C ANISOU 1166 CA GLY B 48 1515 1521 1978 142 177 -70 C ATOM 1167 C GLY B 48 19.102 37.292 13.169 1.00 10.80 C ANISOU 1167 C GLY B 48 1325 1319 1458 0 74 43 C ATOM 1168 O GLY B 48 19.208 36.916 14.325 1.00 12.91 O ANISOU 1168 O GLY B 48 1568 1853 1484 190 49 -126 O ATOM 1169 N GLY B 49 19.683 36.657 12.171 1.00 10.19 N ANISOU 1169 N GLY B 49 1305 1355 1212 38 121 32 N ATOM 1170 CA GLY B 49 20.538 35.477 12.381 1.00 11.55 C ANISOU 1170 CA GLY B 49 1590 1385 1410 234 26 197 C ATOM 1171 C GLY B 49 21.561 35.370 11.272 1.00 10.81 C ANISOU 1171 C GLY B 49 1576 1466 1062 93 127 149 C ATOM 1172 O GLY B 49 21.815 36.339 10.553 1.00 10.84 O ANISOU 1172 O GLY B 49 1339 1374 1403 29 118 172 O ATOM 1173 N ILE B 50 22.071 34.177 11.061 1.00 11.10 N ANISOU 1173 N ILE B 50 1450 1391 1374 311 121 345 N ATOM 1174 CA ILE B 50 22.936 33.957 9.913 1.00 10.38 C ANISOU 1174 CA ILE B 50 1104 1567 1270 206 145 143 C ATOM 1175 C ILE B 50 22.138 34.215 8.636 1.00 10.65 C ANISOU 1175 C ILE B 50 1366 1419 1258 168 14 64 C ATOM 1176 O ILE B 50 21.036 33.724 8.470 1.00 11.98 O ANISOU 1176 O ILE B 50 1394 1614 1542 152 5 49 O ATOM 1177 CB ILE B 50 23.506 32.538 9.991 1.00 10.60 C ANISOU 1177 CB ILE B 50 1324 1481 1223 180 86 44 C ATOM 1178 CG1 ILE B 50 24.579 32.499 11.107 1.00 12.14 C ANISOU 1178 CG1 ILE B 50 1549 1625 1439 258 -114 103 C ATOM 1179 CG2 ILE B 50 24.076 32.097 8.657 1.00 11.67 C ANISOU 1179 CG2 ILE B 50 1470 1672 1289 225 117 90 C ATOM 1180 CD1 ILE B 50 25.054 31.129 11.469 1.00 12.48 C ANISOU 1180 CD1 ILE B 50 1511 1683 1548 309 -244 223 C ATOM 1181 N GLY B 51 22.724 35.054 7.768 1.00 11.06 N ANISOU 1181 N GLY B 51 1193 1622 1385 216 1 151 N ATOM 1182 CA GLY B 51 22.117 35.473 6.544 1.00 11.38 C ANISOU 1182 CA GLY B 51 1455 1657 1211 331 122 383 C ATOM 1183 C GLY B 51 21.413 36.789 6.607 1.00 12.55 C ANISOU 1183 C GLY B 51 1614 1608 1545 130 -205 225 C ATOM 1184 O GLY B 51 21.164 37.361 5.561 1.00 17.52 O ANISOU 1184 O GLY B 51 2565 2381 1710 686 -457 456 O ATOM 1185 N GLY B 52 21.137 37.318 7.779 1.00 11.23 N ANISOU 1185 N GLY B 52 1330 1448 1487 104 145 277 N ATOM 1186 CA GLY B 52 20.416 38.577 7.923 1.00 11.90 C ANISOU 1186 CA GLY B 52 1319 1420 1783 19 184 369 C ATOM 1187 C GLY B 52 19.111 38.420 8.657 1.00 10.49 C ANISOU 1187 C GLY B 52 1343 1381 1258 -60 -2 136 C ATOM 1188 O GLY B 52 18.942 37.539 9.473 1.00 11.27 O ANISOU 1188 O GLY B 52 1383 1487 1410 148 92 232 O ATOM 1189 N PHE B 53 18.185 39.321 8.346 1.00 12.20 N ANISOU 1189 N PHE B 53 1423 1809 1403 229 104 451 N ATOM 1190 CA PHE B 53 16.957 39.462 9.112 1.00 11.56 C ANISOU 1190 CA PHE B 53 1218 1684 1488 120 26 -9 C ATOM 1191 C PHE B 53 15.774 38.933 8.369 1.00 12.01 C ANISOU 1191 C PHE B 53 1608 1863 1089 267 0 -72 C ATOM 1192 O PHE B 53 15.726 38.936 7.123 1.00 14.24 O ANISOU 1192 O PHE B 53 1686 2510 1214 407 55 -61 O ATOM 1193 CB PHE B 53 16.725 40.951 9.501 1.00 12.89 C ANISOU 1193 CB PHE B 53 1667 1721 1508 358 266 338 C ATOM 1194 CG PHE B 53 17.579 41.421 10.634 1.00 12.18 C ANISOU 1194 CG PHE B 53 1432 1268 1926 149 60 258 C ATOM 1195 CD1 PHE B 53 18.942 41.726 10.437 1.00 14.55 C ANISOU 1195 CD1 PHE B 53 1681 1390 2457 371 59 319 C ATOM 1196 CD2 PHE B 53 17.064 41.636 11.845 1.00 12.87 C ANISOU 1196 CD2 PHE B 53 1628 1350 1909 -134 -116 -82 C ATOM 1197 CE1 PHE B 53 19.705 42.160 11.508 1.00 14.95 C ANISOU 1197 CE1 PHE B 53 1518 1551 2609 -159 -33 159 C ATOM 1198 CE2 PHE B 53 17.868 42.077 12.876 1.00 14.30 C ANISOU 1198 CE2 PHE B 53 1956 1226 2248 -30 -272 36 C ATOM 1199 CZ PHE B 53 19.203 42.267 12.664 1.00 16.23 C ANISOU 1199 CZ PHE B 53 1918 2006 2241 -152 -580 3 C ATOM 1200 N ILE B 54 14.734 38.522 9.114 1.00 11.86 N ANISOU 1200 N ILE B 54 1240 1815 1451 152 -82 -94 N ATOM 1201 CA ILE B 54 13.400 38.256 8.561 1.00 12.23 C ANISOU 1201 CA ILE B 54 1475 1658 1513 288 -275 -370 C ATOM 1202 C ILE B 54 12.393 39.047 9.341 1.00 10.99 C ANISOU 1202 C ILE B 54 1390 1282 1502 100 -32 -221 C ATOM 1203 O ILE B 54 12.606 39.407 10.497 1.00 11.96 O ANISOU 1203 O ILE B 54 1371 1648 1525 14 -35 -327 O ATOM 1204 CB ILE B 54 13.024 36.761 8.529 1.00 13.71 C ANISOU 1204 CB ILE B 54 1714 1794 1698 334 -407 -513 C ATOM 1205 CG1 ILE B 54 12.995 36.149 9.924 1.00 14.03 C ANISOU 1205 CG1 ILE B 54 1871 1385 2074 389 -433 -398 C ATOM 1206 CG2 ILE B 54 13.908 36.034 7.589 1.00 15.57 C ANISOU 1206 CG2 ILE B 54 2228 2019 1666 649 -428 -456 C ATOM 1207 CD1 ILE B 54 12.236 34.848 10.004 1.00 15.87 C ANISOU 1207 CD1 ILE B 54 2111 1653 2264 315 -620 -256 C ATOM 1208 N LYS B 55 11.280 39.342 8.666 1.00 11.17 N ANISOU 1208 N LYS B 55 1381 1332 1529 144 -77 -94 N ATOM 1209 CA LYS B 55 10.174 39.996 9.260 1.00 11.43 C ANISOU 1209 CA LYS B 55 1470 1319 1553 139 -3 180 C ATOM 1210 C LYS B 55 9.198 38.981 9.859 1.00 10.36 C ANISOU 1210 C LYS B 55 1203 1289 1444 66 -189 30 C ATOM 1211 O LYS B 55 8.862 38.018 9.201 1.00 12.33 O ANISOU 1211 O LYS B 55 1534 1575 1575 -123 -129 -30 O ATOM 1212 CB LYS B 55 9.432 40.791 8.181 1.00 13.42 C ANISOU 1212 CB LYS B 55 1649 1536 1911 338 141 156 C ATOM 1213 CG LYS B 55 10.264 41.756 7.342 1.00 20.94 C ANISOU 1213 CG LYS B 55 2872 2013 3068 2 165 145 C ATOM 1214 CD LYS B 55 9.439 42.429 6.150 1.00 24.72 C ANISOU 1214 CD LYS B 55 4481 2386 2523 65 73 129 C ATOM 1215 CE LYS B 55 10.298 43.532 5.433 1.00 27.31 C ANISOU 1215 CE LYS B 55 4643 1903 3831 -365 -131 8 C ATOM 1216 NZ LYS B 55 11.712 43.053 5.257 1.00 36.64 N ANISOU 1216 NZ LYS B 55 4960 4001 4958 24 719 -235 N ATOM 1217 N VAL B 56 8.757 39.233 11.072 1.00 11.07 N ANISOU 1217 N VAL B 56 1357 1225 1623 -8 -139 81 N ATOM 1218 CA VAL B 56 7.844 38.344 11.760 1.00 12.25 C ANISOU 1218 CA VAL B 56 1484 1255 1914 72 111 388 C ATOM 1219 C VAL B 56 6.728 39.131 12.437 1.00 13.12 C ANISOU 1219 C VAL B 56 1525 1434 2026 -41 25 181 C ATOM 1220 O VAL B 56 6.803 40.363 12.608 1.00 13.57 O ANISOU 1220 O VAL B 56 1495 1633 2025 -26 195 146 O ATOM 1221 CB VAL B 56 8.611 37.467 12.831 1.00 11.73 C ANISOU 1221 CB VAL B 56 1420 1343 1693 -123 -60 249 C ATOM 1222 CG1 VAL B 56 9.655 36.610 12.170 1.00 13.60 C ANISOU 1222 CG1 VAL B 56 1340 1547 2277 145 -181 259 C ATOM 1223 CG2 VAL B 56 9.237 38.330 13.896 1.00 13.51 C ANISOU 1223 CG2 VAL B 56 1648 1524 1959 15 -166 398 C ATOM 1224 N ARG B 57 5.696 38.403 12.787 1.00 12.50 N ANISOU 1224 N ARG B 57 1481 1350 1918 180 117 302 N ATOM 1225 CA ARG B 57 4.560 38.942 13.570 1.00 13.08 C ANISOU 1225 CA ARG B 57 1257 1556 2156 194 146 351 C ATOM 1226 C ARG B 57 4.664 38.433 14.984 1.00 12.16 C ANISOU 1226 C ARG B 57 1170 1510 1940 90 82 289 C ATOM 1227 O ARG B 57 4.804 37.195 15.199 1.00 13.63 O ANISOU 1227 O ARG B 57 1602 1325 2251 322 142 376 O ATOM 1228 CB ARG B 57 3.225 38.471 12.966 1.00 13.94 C ANISOU 1228 CB ARG B 57 1563 1731 2000 280 -41 604 C ATOM 1229 CG ARG B 57 3.043 38.872 11.615 1.00 16.79 C ANISOU 1229 CG ARG B 57 1818 2370 2191 118 -153 119 C ATOM 1230 CD ARG B 57 1.632 38.607 11.044 1.00 21.28 C ANISOU 1230 CD ARG B 57 2074 2924 3087 345 -626 162 C ATOM 1231 NE ARG B 57 1.161 37.191 11.178 1.00 22.37 N ANISOU 1231 NE ARG B 57 2055 3053 3392 88 -465 191 N ATOM 1232 CZ ARG B 57 1.465 36.189 10.335 1.00 21.77 C ANISOU 1232 CZ ARG B 57 2646 2666 2959 -47 -366 668 C ATOM 1233 NH1 ARG B 57 2.387 36.360 9.365 1.00 27.38 N ANISOU 1233 NH1 ARG B 57 3324 2778 4298 223 578 346 N ATOM 1234 NH2 ARG B 57 0.865 35.026 10.476 1.00 26.50 N ANISOU 1234 NH2 ARG B 57 3222 2360 4485 158 -218 1227 N ATOM 1235 N GLN B 58 4.697 39.355 15.955 1.00 13.39 N ANISOU 1235 N GLN B 58 1610 1568 1906 403 199 250 N ATOM 1236 CA GLN B 58 4.841 39.000 17.350 1.00 13.81 C ANISOU 1236 CA GLN B 58 1578 1698 1968 561 430 173 C ATOM 1237 C GLN B 58 3.486 38.871 18.028 1.00 13.68 C ANISOU 1237 C GLN B 58 1603 1407 2188 389 396 361 C ATOM 1238 O GLN B 58 2.746 39.890 18.138 1.00 15.93 O ANISOU 1238 O GLN B 58 1938 1713 2400 746 525 522 O ATOM 1239 CB GLN B 58 5.690 40.064 18.100 1.00 14.31 C ANISOU 1239 CB GLN B 58 1849 1770 1816 572 208 252 C ATOM 1240 CG GLN B 58 5.791 39.794 19.548 1.00 17.30 C ANISOU 1240 CG GLN B 58 2249 2067 2256 663 407 274 C ATOM 1241 CD GLN B 58 6.558 40.800 20.306 1.00 21.37 C ANISOU 1241 CD GLN B 58 2895 2342 2883 153 338 180 C ATOM 1242 OE1 GLN B 58 7.463 41.445 19.772 1.00 23.86 O ANISOU 1242 OE1 GLN B 58 2941 2812 3312 -235 691 -200 O ATOM 1243 NE2 GLN B 58 6.225 40.944 21.634 1.00 29.58 N ANISOU 1243 NE2 GLN B 58 3956 3913 3370 -139 937 -274 N ATOM 1244 N TYR B 59 3.128 37.677 18.463 1.00 14.84 N ANISOU 1244 N TYR B 59 1577 1530 2530 458 527 581 N ATOM 1245 CA TYR B 59 1.911 37.412 19.242 1.00 15.48 C ANISOU 1245 CA TYR B 59 1634 2017 2231 622 517 535 C ATOM 1246 C TYR B 59 2.275 37.193 20.712 1.00 18.41 C ANISOU 1246 C TYR B 59 2246 2253 2494 693 431 586 C ATOM 1247 O TYR B 59 3.236 36.515 21.014 1.00 22.25 O ANISOU 1247 O TYR B 59 2291 3329 2833 1272 640 1244 O ATOM 1248 CB TYR B 59 1.206 36.183 18.708 1.00 17.04 C ANISOU 1248 CB TYR B 59 1826 1958 2690 611 714 578 C ATOM 1249 CG TYR B 59 0.683 36.268 17.298 1.00 16.53 C ANISOU 1249 CG TYR B 59 1367 1944 2967 14 460 564 C ATOM 1250 CD1 TYR B 59 1.502 36.057 16.219 1.00 18.28 C ANISOU 1250 CD1 TYR B 59 2119 2254 2572 188 442 826 C ATOM 1251 CD2 TYR B 59 -0.659 36.587 17.040 1.00 19.02 C ANISOU 1251 CD2 TYR B 59 1425 2428 3373 284 351 571 C ATOM 1252 CE1 TYR B 59 1.067 36.099 15.006 1.00 18.51 C ANISOU 1252 CE1 TYR B 59 1601 2575 2855 -235 325 546 C ATOM 1253 CE2 TYR B 59 -1.119 36.650 15.765 1.00 22.07 C ANISOU 1253 CE2 TYR B 59 1903 2540 3943 160 -422 359 C ATOM 1254 CZ TYR B 59 -0.258 36.397 14.736 1.00 24.91 C ANISOU 1254 CZ TYR B 59 2468 3065 3929 86 -73 493 C ATOM 1255 OH TYR B 59 -0.661 36.458 13.375 1.00 29.61 O ANISOU 1255 OH TYR B 59 2798 3849 4603 -472 -325 942 O ATOM 1256 N ASP B 60 1.455 37.666 21.594 1.00 17.87 N ANISOU 1256 N ASP B 60 2111 2011 2666 429 364 436 N ATOM 1257 CA ASP B 60 1.731 37.530 22.961 1.00 19.83 C ANISOU 1257 CA ASP B 60 2552 2332 2648 238 529 337 C ATOM 1258 C ASP B 60 0.758 36.627 23.689 1.00 17.14 C ANISOU 1258 C ASP B 60 2093 2121 2298 404 340 348 C ATOM 1259 O ASP B 60 -0.392 36.374 23.190 1.00 18.65 O ANISOU 1259 O ASP B 60 1929 2181 2974 458 378 443 O ATOM 1260 CB ASP B 60 1.781 38.819 23.570 1.00 23.44 C ANISOU 1260 CB ASP B 60 3853 2666 2384 -180 326 385 C ATOM 1261 CG ASP B 60 2.976 39.730 22.992 1.00 26.11 C ANISOU 1261 CG ASP B 60 3314 2965 3639 -41 566 141 C ATOM 1262 OD1 ASP B 60 4.110 39.185 22.656 1.00 27.61 O ANISOU 1262 OD1 ASP B 60 3634 3028 3829 -14 830 278 O ATOM 1263 OD2 ASP B 60 2.854 40.919 22.869 1.00 31.72 O ANISOU 1263 OD2 ASP B 60 4927 2884 4240 431 -270 183 O ATOM 1264 N GLN B 61 1.269 35.955 24.712 1.00 17.98 N ANISOU 1264 N GLN B 61 2279 2035 2516 332 518 416 N ATOM 1265 CA GLN B 61 0.439 35.145 25.614 1.00 19.30 C ANISOU 1265 CA GLN B 61 2504 2451 2375 430 784 418 C ATOM 1266 C GLN B 61 -0.295 34.047 24.808 1.00 18.65 C ANISOU 1266 C GLN B 61 2168 2230 2686 480 514 687 C ATOM 1267 O GLN B 61 -1.468 33.750 25.031 1.00 20.35 O ANISOU 1267 O GLN B 61 2144 2487 3099 475 1012 175 O ATOM 1268 CB GLN B 61 -0.484 36.051 26.455 1.00 22.41 C ANISOU 1268 CB GLN B 61 2911 2708 2895 443 745 366 C ATOM 1269 CG GLN B 61 0.288 36.873 27.501 1.00 27.29 C ANISOU 1269 CG GLN B 61 3209 3333 3826 353 689 -387 C ATOM 1270 CD GLN B 61 0.981 35.947 28.615 1.00 34.82 C ANISOU 1270 CD GLN B 61 4434 4535 4260 216 -93 -139 C ATOM 1271 OE1 GLN B 61 2.207 35.795 28.623 1.00 37.57 O ANISOU 1271 OE1 GLN B 61 4738 4963 4572 860 -82 -331 O ATOM 1272 NE2 GLN B 61 0.125 35.273 29.500 1.00 33.81 N ANISOU 1272 NE2 GLN B 61 5047 3624 4172 626 77 -150 N ATOM 1273 N ILE B 62 0.471 33.333 23.970 1.00 15.71 N ANISOU 1273 N ILE B 62 1823 1762 2385 364 372 441 N ATOM 1274 CA ILE B 62 -0.064 32.232 23.229 1.00 14.75 C ANISOU 1274 CA ILE B 62 1560 1903 2141 311 270 539 C ATOM 1275 C ILE B 62 0.257 30.949 23.995 1.00 15.32 C ANISOU 1275 C ILE B 62 1712 1786 2320 433 321 464 C ATOM 1276 O ILE B 62 1.419 30.668 24.255 1.00 14.88 O ANISOU 1276 O ILE B 62 1480 1916 2256 368 463 583 O ATOM 1277 CB ILE B 62 0.561 32.163 21.805 1.00 15.35 C ANISOU 1277 CB ILE B 62 1762 2013 2057 174 193 327 C ATOM 1278 CG1 ILE B 62 0.320 33.510 21.039 1.00 16.21 C ANISOU 1278 CG1 ILE B 62 2062 1954 2143 539 231 664 C ATOM 1279 CG2 ILE B 62 0.053 30.959 21.050 1.00 17.95 C ANISOU 1279 CG2 ILE B 62 2297 2108 2412 139 1 530 C ATOM 1280 CD1 ILE B 62 -1.134 33.857 20.839 1.00 21.41 C ANISOU 1280 CD1 ILE B 62 2100 2864 3170 774 284 1054 C ATOM 1281 N PRO B 63 -0.757 30.078 24.249 1.00 15.79 N ANISOU 1281 N PRO B 63 1725 2002 2271 221 245 539 N ATOM 1282 CA PRO B 63 -0.478 28.785 24.834 1.00 15.81 C ANISOU 1282 CA PRO B 63 1830 2048 2128 266 179 641 C ATOM 1283 C PRO B 63 0.180 27.854 23.840 1.00 17.90 C ANISOU 1283 C PRO B 63 2122 2034 2642 285 -77 423 C ATOM 1284 O PRO B 63 -0.332 27.656 22.761 1.00 20.19 O ANISOU 1284 O PRO B 63 3083 2191 2395 684 320 500 O ATOM 1285 CB PRO B 63 -1.858 28.294 25.296 1.00 16.62 C ANISOU 1285 CB PRO B 63 1997 2226 2090 -158 68 739 C ATOM 1286 CG PRO B 63 -2.847 29.158 24.687 1.00 21.46 C ANISOU 1286 CG PRO B 63 1928 2420 3804 172 508 836 C ATOM 1287 CD PRO B 63 -2.213 30.354 24.122 1.00 16.28 C ANISOU 1287 CD PRO B 63 1569 2093 2522 91 517 494 C ATOM 1288 N VAL B 64 1.273 27.233 24.291 1.00 18.73 N ANISOU 1288 N VAL B 64 2311 2251 2553 567 463 819 N ATOM 1289 CA VAL B 64 2.082 26.260 23.472 1.00 20.00 C ANISOU 1289 CA VAL B 64 2943 1840 2815 427 482 684 C ATOM 1290 C VAL B 64 2.442 25.064 24.412 1.00 20.52 C ANISOU 1290 C VAL B 64 2495 2361 2939 530 679 760 C ATOM 1291 O VAL B 64 2.982 25.272 25.472 1.00 25.35 O ANISOU 1291 O VAL B 64 3748 2796 3088 1033 719 964 O ATOM 1292 CB VAL B 64 3.390 26.862 22.972 1.00 21.59 C ANISOU 1292 CB VAL B 64 2717 2374 3109 539 738 670 C ATOM 1293 CG1 VAL B 64 4.155 25.811 22.022 1.00 21.11 C ANISOU 1293 CG1 VAL B 64 2568 2346 3105 111 1020 754 C ATOM 1294 CG2 VAL B 64 3.151 28.103 22.222 1.00 21.40 C ANISOU 1294 CG2 VAL B 64 2577 2584 2967 513 709 840 C ATOM 1295 N AGLU B 65 2.089 23.875 24.045 0.50 19.18 N ANISOU 1295 N AGLU B 65 2318 2293 2674 501 908 738 N ATOM 1296 N BGLU B 65 2.003 23.810 23.945 0.50 18.67 N ANISOU 1296 N BGLU B 65 2082 2207 2802 550 789 827 N ATOM 1297 CA AGLU B 65 2.536 22.729 24.809 0.50 19.38 C ANISOU 1297 CA AGLU B 65 2293 2306 2762 555 804 562 C ATOM 1298 CA BGLU B 65 2.279 22.520 24.628 0.50 18.85 C ANISOU 1298 CA BGLU B 65 2211 1999 2952 436 704 597 C ATOM 1299 C AGLU B 65 3.643 22.060 24.072 0.50 18.94 C ANISOU 1299 C AGLU B 65 2256 2195 2743 599 762 563 C ATOM 1300 C BGLU B 65 3.483 21.853 23.982 0.50 19.15 C ANISOU 1300 C BGLU B 65 2297 2015 2961 350 812 699 C ATOM 1301 O AGLU B 65 3.696 22.094 22.897 0.50 19.26 O ANISOU 1301 O AGLU B 65 2481 2054 2780 790 628 389 O ATOM 1302 O BGLU B 65 3.447 21.543 22.794 0.50 18.55 O ANISOU 1302 O BGLU B 65 1734 1800 3512 323 470 404 O ATOM 1303 CB AGLU B 65 1.381 21.757 25.077 0.50 19.40 C ANISOU 1303 CB AGLU B 65 2505 2023 2840 439 384 315 C ATOM 1304 CB BGLU B 65 1.002 21.559 24.537 0.50 19.51 C ANISOU 1304 CB BGLU B 65 2333 1933 3148 510 599 455 C ATOM 1305 CG AGLU B 65 1.582 20.823 26.243 0.50 20.44 C ANISOU 1305 CG AGLU B 65 2780 2563 2423 301 454 197 C ATOM 1306 CG BGLU B 65 -0.283 22.188 25.096 0.50 18.26 C ANISOU 1306 CG BGLU B 65 2302 2496 2137 302 567 457 C ATOM 1307 CD AGLU B 65 0.334 19.866 26.468 0.50 25.76 C ANISOU 1307 CD AGLU B 65 3298 3459 3027 -293 319 378 C ATOM 1308 CD BGLU B 65 -0.863 23.316 24.172 0.50 16.66 C ANISOU 1308 CD BGLU B 65 1755 2168 2405 454 -188 -181 C ATOM 1309 OE1AGLU B 65 0.139 18.890 25.646 0.50 32.72 O ANISOU 1309 OE1AGLU B 65 4465 4043 3923 98 244 -243 O ATOM 1310 OE1BGLU B 65 -1.206 23.027 22.991 0.50 16.36 O ANISOU 1310 OE1BGLU B 65 1691 2146 2379 -281 130 -71 O ATOM 1311 OE2AGLU B 65 -0.479 20.165 27.338 0.50 30.56 O ANISOU 1311 OE2AGLU B 65 3579 4162 3868 -26 555 -457 O ATOM 1312 OE2BGLU B 65 -0.977 24.486 24.629 0.50 17.64 O ANISOU 1312 OE2BGLU B 65 2313 2101 2288 778 -440 -412 O ATOM 1313 N ILE B 66 4.571 21.627 24.800 1.00 18.41 N ANISOU 1313 N ILE B 66 2349 2099 2545 718 961 600 N ATOM 1314 CA ILE B 66 5.835 21.110 24.258 1.00 18.93 C ANISOU 1314 CA ILE B 66 2336 2447 2406 640 877 476 C ATOM 1315 C ILE B 66 6.100 19.787 24.970 1.00 19.74 C ANISOU 1315 C ILE B 66 2426 2352 2722 759 402 493 C ATOM 1316 O ILE B 66 6.411 19.753 26.180 1.00 20.51 O ANISOU 1316 O ILE B 66 2563 2503 2728 961 895 624 O ATOM 1317 CB ILE B 66 6.950 22.062 24.510 1.00 17.44 C ANISOU 1317 CB ILE B 66 2295 2209 2122 726 723 460 C ATOM 1318 CG1 ILE B 66 6.659 23.423 23.842 1.00 19.85 C ANISOU 1318 CG1 ILE B 66 2427 2436 2678 638 1017 353 C ATOM 1319 CG2 ILE B 66 8.303 21.483 24.002 1.00 19.65 C ANISOU 1319 CG2 ILE B 66 2461 2752 2253 710 1104 506 C ATOM 1320 CD1 ILE B 66 7.307 24.492 24.460 1.00 23.26 C ANISOU 1320 CD1 ILE B 66 2881 2827 3127 380 247 774 C ATOM 1321 N CYS B 67 6.008 18.742 24.250 1.00 21.88 N ANISOU 1321 N CYS B 67 2637 2627 3049 806 517 385 N ATOM 1322 CA CYS B 67 6.182 17.375 24.873 1.00 24.28 C ANISOU 1322 CA CYS B 67 3267 2554 3403 799 405 313 C ATOM 1323 C CYS B 67 5.366 17.172 26.108 1.00 25.79 C ANISOU 1323 C CYS B 67 3571 3104 3125 759 249 521 C ATOM 1324 O CYS B 67 5.855 16.673 27.101 1.00 27.22 O ANISOU 1324 O CYS B 67 4135 2659 3546 1135 414 884 O ATOM 1325 CB CYS B 67 7.633 17.111 25.199 1.00 24.09 C ANISOU 1325 CB CYS B 67 3423 2549 3180 1320 563 306 C ATOM 1326 SG CYS B 67 8.604 17.099 23.894 1.00 31.16 S ANISOU 1326 SG CYS B 67 4058 3508 4272 1244 1242 1027 S ATOM 1327 N GLY B 68 4.180 17.713 26.107 1.00 25.90 N ANISOU 1327 N GLY B 68 3414 2873 3554 499 689 530 N ATOM 1328 CA GLY B 68 3.290 17.572 27.238 1.00 27.05 C ANISOU 1328 CA GLY B 68 3637 3121 3517 -175 659 604 C ATOM 1329 C GLY B 68 3.498 18.534 28.363 1.00 26.45 C ANISOU 1329 C GLY B 68 3095 3319 3635 157 831 495 C ATOM 1330 O GLY B 68 2.704 18.531 29.315 1.00 33.24 O ANISOU 1330 O GLY B 68 4132 4253 4242 -508 1551 923 O ATOM 1331 N HIS B 69 4.375 19.493 28.190 1.00 21.02 N ANISOU 1331 N HIS B 69 3154 2228 2605 604 738 1037 N ATOM 1332 CA HIS B 69 4.559 20.500 29.180 1.00 21.59 C ANISOU 1332 CA HIS B 69 3153 2228 2823 631 653 734 C ATOM 1333 C HIS B 69 3.892 21.775 28.685 1.00 19.88 C ANISOU 1333 C HIS B 69 3163 2137 2252 782 1145 819 C ATOM 1334 O HIS B 69 4.115 22.197 27.529 1.00 22.83 O ANISOU 1334 O HIS B 69 3681 2466 2524 1339 1604 1093 O ATOM 1335 CB HIS B 69 6.070 20.777 29.452 1.00 21.94 C ANISOU 1335 CB HIS B 69 3408 2112 2814 404 597 647 C ATOM 1336 CG HIS B 69 6.802 19.631 30.091 1.00 22.26 C ANISOU 1336 CG HIS B 69 2968 2657 2829 460 620 569 C ATOM 1337 ND1 HIS B 69 7.445 19.750 31.308 1.00 22.01 N ANISOU 1337 ND1 HIS B 69 3247 2421 2694 658 779 576 N ATOM 1338 CD2 HIS B 69 7.171 18.455 29.592 1.00 23.64 C ANISOU 1338 CD2 HIS B 69 3111 2729 3143 295 723 602 C ATOM 1339 CE1 HIS B 69 7.989 18.572 31.621 1.00 26.97 C ANISOU 1339 CE1 HIS B 69 4315 2599 3331 493 43 306 C ATOM 1340 NE2 HIS B 69 7.787 17.756 30.613 1.00 22.01 N ANISOU 1340 NE2 HIS B 69 2731 2421 3208 280 225 424 N ATOM 1341 N LYS B 70 3.107 22.421 29.529 1.00 17.34 N ANISOU 1341 N LYS B 70 2458 1999 2131 568 997 675 N ATOM 1342 CA LYS B 70 2.416 23.604 29.142 1.00 17.00 C ANISOU 1342 CA LYS B 70 2124 2080 2253 448 730 424 C ATOM 1343 C LYS B 70 3.288 24.807 29.246 1.00 17.01 C ANISOU 1343 C LYS B 70 2076 2343 2044 493 728 492 C ATOM 1344 O LYS B 70 4.014 24.943 30.108 1.00 17.75 O ANISOU 1344 O LYS B 70 2310 2265 2168 410 612 686 O ATOM 1345 CB LYS B 70 1.237 23.779 30.027 1.00 16.10 C ANISOU 1345 CB LYS B 70 2020 2156 1940 420 592 421 C ATOM 1346 CG LYS B 70 0.160 22.712 29.840 1.00 16.98 C ANISOU 1346 CG LYS B 70 2521 1859 2071 296 496 207 C ATOM 1347 CD LYS B 70 -1.005 22.918 30.816 1.00 17.86 C ANISOU 1347 CD LYS B 70 1976 2408 2399 152 715 215 C ATOM 1348 CE LYS B 70 -2.078 21.899 30.621 1.00 20.28 C ANISOU 1348 CE LYS B 70 2317 2725 2663 160 246 -2 C ATOM 1349 NZ LYS B 70 -1.640 20.530 30.988 1.00 26.13 N ANISOU 1349 NZ LYS B 70 2916 2746 4263 -6 389 409 N ATOM 1350 N ALA B 71 3.130 25.731 28.289 1.00 18.17 N ANISOU 1350 N ALA B 71 2192 2133 2578 408 525 841 N ATOM 1351 CA ALA B 71 3.816 26.993 28.324 1.00 17.47 C ANISOU 1351 CA ALA B 71 1820 2147 2670 477 427 558 C ATOM 1352 C ALA B 71 2.837 28.074 27.783 1.00 14.22 C ANISOU 1352 C ALA B 71 1688 1606 2107 386 489 300 C ATOM 1353 O ALA B 71 1.858 27.725 27.133 1.00 16.13 O ANISOU 1353 O ALA B 71 1899 1981 2246 281 564 616 O ATOM 1354 CB ALA B 71 5.095 26.925 27.444 1.00 19.26 C ANISOU 1354 CB ALA B 71 1924 2348 3045 636 645 850 C ATOM 1355 N ILE B 72 3.179 29.298 27.996 1.00 15.20 N ANISOU 1355 N ILE B 72 1637 1837 2301 337 457 543 N ATOM 1356 CA ILE B 72 2.384 30.403 27.471 1.00 14.64 C ANISOU 1356 CA ILE B 72 1661 1733 2167 410 516 341 C ATOM 1357 C ILE B 72 3.219 31.617 27.364 1.00 13.60 C ANISOU 1357 C ILE B 72 1697 1787 1684 313 354 385 C ATOM 1358 O ILE B 72 3.908 32.002 28.282 1.00 15.90 O ANISOU 1358 O ILE B 72 1809 2162 2069 440 256 417 O ATOM 1359 CB ILE B 72 1.077 30.651 28.311 1.00 15.67 C ANISOU 1359 CB ILE B 72 1727 2039 2187 392 454 459 C ATOM 1360 CG1 ILE B 72 0.319 31.794 27.716 1.00 16.78 C ANISOU 1360 CG1 ILE B 72 1666 2208 2499 474 614 326 C ATOM 1361 CG2 ILE B 72 1.381 30.863 29.746 1.00 18.77 C ANISOU 1361 CG2 ILE B 72 2168 2509 2454 372 325 431 C ATOM 1362 CD1 ILE B 72 -1.007 32.000 28.331 1.00 18.13 C ANISOU 1362 CD1 ILE B 72 1978 2266 2644 426 567 361 C ATOM 1363 N GLY B 73 3.288 32.165 26.187 1.00 14.86 N ANISOU 1363 N GLY B 73 1769 2042 1834 418 410 543 N ATOM 1364 CA GLY B 73 4.132 33.324 25.987 1.00 15.71 C ANISOU 1364 CA GLY B 73 1714 1946 2308 540 443 265 C ATOM 1365 C GLY B 73 4.194 33.816 24.562 1.00 13.54 C ANISOU 1365 C GLY B 73 1448 1914 1780 333 367 135 C ATOM 1366 O GLY B 73 3.365 33.521 23.769 1.00 15.33 O ANISOU 1366 O GLY B 73 1806 1987 2030 205 334 646 O ATOM 1367 N THR B 74 5.247 34.518 24.277 1.00 15.55 N ANISOU 1367 N THR B 74 1826 1878 2203 604 243 372 N ATOM 1368 CA THR B 74 5.407 35.125 22.969 1.00 15.05 C ANISOU 1368 CA THR B 74 1914 1773 2030 335 324 387 C ATOM 1369 C THR B 74 5.758 34.136 21.922 1.00 13.14 C ANISOU 1369 C THR B 74 1626 1565 1801 141 366 282 C ATOM 1370 O THR B 74 6.640 33.290 22.110 1.00 14.41 O ANISOU 1370 O THR B 74 1620 1909 1944 425 338 351 O ATOM 1371 CB THR B 74 6.474 36.220 23.037 1.00 17.25 C ANISOU 1371 CB THR B 74 2493 1966 2093 -37 337 241 C ATOM 1372 OG1 THR B 74 6.019 37.276 23.883 1.00 21.90 O ANISOU 1372 OG1 THR B 74 3665 2022 2632 54 471 97 O ATOM 1373 CG2 THR B 74 6.756 36.909 21.628 1.00 20.88 C ANISOU 1373 CG2 THR B 74 3095 2198 2637 -15 574 773 C ATOM 1374 N VAL B 75 5.102 34.253 20.773 1.00 13.79 N ANISOU 1374 N VAL B 75 1583 1751 1903 296 338 503 N ATOM 1375 CA VAL B 75 5.382 33.457 19.636 1.00 13.36 C ANISOU 1375 CA VAL B 75 1530 1596 1950 315 6 532 C ATOM 1376 C VAL B 75 5.531 34.384 18.431 1.00 13.07 C ANISOU 1376 C VAL B 75 1421 1562 1981 485 92 218 C ATOM 1377 O VAL B 75 4.672 35.251 18.206 1.00 15.35 O ANISOU 1377 O VAL B 75 1642 1777 2412 602 356 761 O ATOM 1378 CB VAL B 75 4.250 32.408 19.366 1.00 17.14 C ANISOU 1378 CB VAL B 75 2094 1751 2665 241 11 607 C ATOM 1379 CG1 VAL B 75 4.410 31.732 18.096 1.00 19.65 C ANISOU 1379 CG1 VAL B 75 2526 2072 2868 13 237 690 C ATOM 1380 CG2 VAL B 75 4.189 31.381 20.486 1.00 16.16 C ANISOU 1380 CG2 VAL B 75 2293 1626 2220 -48 69 423 C ATOM 1381 N LEU B 76 6.645 34.278 17.764 1.00 11.62 N ANISOU 1381 N LEU B 76 1221 1326 1865 374 -28 407 N ATOM 1382 CA LEU B 76 6.872 35.022 16.525 1.00 11.76 C ANISOU 1382 CA LEU B 76 1270 1314 1884 314 -55 269 C ATOM 1383 C LEU B 76 6.490 34.153 15.367 1.00 13.28 C ANISOU 1383 C LEU B 76 1745 1533 1765 304 -80 114 C ATOM 1384 O LEU B 76 6.704 32.905 15.449 1.00 16.04 O ANISOU 1384 O LEU B 76 2092 1521 2480 507 -540 -27 O ATOM 1385 CB LEU B 76 8.343 35.439 16.439 1.00 11.19 C ANISOU 1385 CB LEU B 76 1421 1239 1592 161 125 253 C ATOM 1386 CG LEU B 76 8.894 36.181 17.689 1.00 11.60 C ANISOU 1386 CG LEU B 76 1300 1588 1520 212 164 175 C ATOM 1387 CD1 LEU B 76 10.385 36.463 17.491 1.00 11.91 C ANISOU 1387 CD1 LEU B 76 1443 1532 1549 92 38 233 C ATOM 1388 CD2 LEU B 76 8.142 37.409 17.977 1.00 12.22 C ANISOU 1388 CD2 LEU B 76 1317 1879 1445 367 7 30 C ATOM 1389 N VAL B 77 5.874 34.716 14.342 1.00 11.99 N ANISOU 1389 N VAL B 77 1453 1319 1782 -13 -266 252 N ATOM 1390 CA VAL B 77 5.465 33.952 13.192 1.00 11.32 C ANISOU 1390 CA VAL B 77 1211 1438 1652 108 -110 165 C ATOM 1391 C VAL B 77 5.982 34.613 11.937 1.00 12.45 C ANISOU 1391 C VAL B 77 1400 1588 1738 -123 -165 194 C ATOM 1392 O VAL B 77 5.785 35.814 11.728 1.00 12.71 O ANISOU 1392 O VAL B 77 1517 1318 1992 75 -179 286 O ATOM 1393 CB VAL B 77 3.874 33.835 13.112 1.00 13.96 C ANISOU 1393 CB VAL B 77 1418 1631 2255 137 -185 329 C ATOM 1394 CG1 VAL B 77 3.486 33.081 11.873 1.00 14.29 C ANISOU 1394 CG1 VAL B 77 1432 2036 1961 -152 -194 376 C ATOM 1395 CG2 VAL B 77 3.351 33.147 14.348 1.00 13.90 C ANISOU 1395 CG2 VAL B 77 1462 1873 1946 -172 -167 118 C ATOM 1396 N GLY B 78 6.629 33.837 11.086 1.00 11.83 N ANISOU 1396 N GLY B 78 1449 1297 1748 -17 49 327 N ATOM 1397 CA GLY B 78 7.126 34.368 9.834 1.00 12.40 C ANISOU 1397 CA GLY B 78 1401 1653 1655 7 -121 232 C ATOM 1398 C GLY B 78 7.859 33.346 9.076 1.00 12.37 C ANISOU 1398 C GLY B 78 1458 1676 1566 32 -181 218 C ATOM 1399 O GLY B 78 7.770 32.138 9.404 1.00 13.09 O ANISOU 1399 O GLY B 78 1452 1649 1873 90 -85 247 O ATOM 1400 N PRO B 79 8.585 33.749 8.054 1.00 12.67 N ANISOU 1400 N PRO B 79 1657 1753 1404 196 -215 346 N ATOM 1401 CA PRO B 79 9.089 32.809 7.052 1.00 12.58 C ANISOU 1401 CA PRO B 79 1713 1617 1449 187 -251 150 C ATOM 1402 C PRO B 79 10.408 32.208 7.529 1.00 12.83 C ANISOU 1402 C PRO B 79 1846 1598 1431 266 40 18 C ATOM 1403 O PRO B 79 11.400 32.231 6.795 1.00 14.93 O ANISOU 1403 O PRO B 79 1903 2275 1494 433 54 374 O ATOM 1404 CB PRO B 79 9.232 33.690 5.770 1.00 14.43 C ANISOU 1404 CB PRO B 79 1775 2111 1596 72 -134 370 C ATOM 1405 CG PRO B 79 9.540 35.090 6.346 1.00 13.68 C ANISOU 1405 CG PRO B 79 1963 1698 1537 61 -110 230 C ATOM 1406 CD PRO B 79 8.711 35.187 7.588 1.00 14.05 C ANISOU 1406 CD PRO B 79 1775 1752 1810 46 -20 359 C ATOM 1407 N THR B 80 10.398 31.573 8.699 1.00 13.07 N ANISOU 1407 N THR B 80 1513 1830 1620 208 -13 442 N ATOM 1408 CA THR B 80 11.514 30.801 9.145 1.00 12.42 C ANISOU 1408 CA THR B 80 1455 1854 1410 109 -41 246 C ATOM 1409 C THR B 80 11.468 29.475 8.428 1.00 13.63 C ANISOU 1409 C THR B 80 1641 1838 1697 335 -159 429 C ATOM 1410 O THR B 80 10.434 28.892 8.229 1.00 15.02 O ANISOU 1410 O THR B 80 2119 1959 1629 182 -394 163 O ATOM 1411 CB THR B 80 11.483 30.622 10.657 1.00 12.39 C ANISOU 1411 CB THR B 80 1578 1791 1336 66 102 292 C ATOM 1412 OG1 THR B 80 12.580 29.738 11.040 1.00 13.35 O ANISOU 1412 OG1 THR B 80 1504 2002 1567 295 -131 371 O ATOM 1413 CG2 THR B 80 10.198 30.032 11.164 1.00 12.94 C ANISOU 1413 CG2 THR B 80 1535 1529 1850 123 -60 221 C ATOM 1414 N PRO B 81 12.647 28.897 8.141 1.00 15.73 N ANISOU 1414 N PRO B 81 2170 2475 1332 361 -296 49 N ATOM 1415 CA PRO B 81 12.663 27.593 7.545 1.00 16.83 C ANISOU 1415 CA PRO B 81 2549 2327 1516 624 -283 13 C ATOM 1416 C PRO B 81 12.360 26.420 8.501 1.00 17.68 C ANISOU 1416 C PRO B 81 2688 2395 1633 574 -513 41 C ATOM 1417 O PRO B 81 12.108 25.302 8.037 1.00 19.76 O ANISOU 1417 O PRO B 81 3076 2776 1654 547 -722 -132 O ATOM 1418 CB PRO B 81 14.067 27.457 7.000 1.00 17.95 C ANISOU 1418 CB PRO B 81 2578 2437 1803 342 -135 227 C ATOM 1419 CG PRO B 81 14.882 28.338 7.692 1.00 20.48 C ANISOU 1419 CG PRO B 81 2240 3284 2255 678 -334 -196 C ATOM 1420 CD PRO B 81 13.949 29.488 8.173 1.00 16.07 C ANISOU 1420 CD PRO B 81 1758 2754 1594 652 318 359 C ATOM 1421 N AVAL B 82 12.402 26.670 9.785 0.50 15.90 N ANISOU 1421 N AVAL B 82 2543 2141 1358 410 -664 -18 N ATOM 1422 N BVAL B 82 12.388 26.681 9.783 0.50 15.81 N ANISOU 1422 N BVAL B 82 2549 2110 1347 411 -699 26 N ATOM 1423 CA AVAL B 82 12.115 25.636 10.800 0.50 15.75 C ANISOU 1423 CA AVAL B 82 2267 2012 1703 438 -396 23 C ATOM 1424 CA BVAL B 82 12.203 25.650 10.810 0.50 15.48 C ANISOU 1424 CA BVAL B 82 2321 1891 1669 405 -477 49 C ATOM 1425 C AVAL B 82 11.376 26.263 11.944 0.50 12.80 C ANISOU 1425 C AVAL B 82 1815 1684 1362 134 -509 -65 C ATOM 1426 C BVAL B 82 11.410 26.271 11.959 0.50 13.04 C ANISOU 1426 C BVAL B 82 1891 1629 1433 172 -510 -14 C ATOM 1427 O AVAL B 82 11.625 27.433 12.292 0.50 14.53 O ANISOU 1427 O AVAL B 82 2410 1425 1686 42 -199 45 O ATOM 1428 O BVAL B 82 11.630 27.439 12.303 0.50 14.55 O ANISOU 1428 O BVAL B 82 2405 1419 1702 38 -214 46 O ATOM 1429 CB AVAL B 82 13.410 24.982 11.312 0.50 15.71 C ANISOU 1429 CB AVAL B 82 2388 1913 1666 446 -469 84 C ATOM 1430 CB BVAL B 82 13.597 25.119 11.328 0.50 15.79 C ANISOU 1430 CB BVAL B 82 2503 1671 1823 381 -536 297 C ATOM 1431 CG1AVAL B 82 14.046 24.150 10.247 0.50 19.47 C ANISOU 1431 CG1AVAL B 82 2506 2406 2485 392 -121 109 C ATOM 1432 CG1BVAL B 82 13.409 24.045 12.348 0.50 15.59 C ANISOU 1432 CG1BVAL B 82 2562 1878 1483 608 -122 295 C ATOM 1433 CG2AVAL B 82 14.360 26.018 11.802 0.50 15.45 C ANISOU 1433 CG2AVAL B 82 1689 2596 1584 -75 -166 685 C ATOM 1434 CG2BVAL B 82 14.444 24.615 10.180 0.50 17.10 C ANISOU 1434 CG2BVAL B 82 2035 1723 2737 -93 -408 231 C ATOM 1435 N ASN B 83 10.552 25.493 12.623 1.00 13.45 N ANISOU 1435 N ASN B 83 1975 1565 1568 -15 -590 -100 N ATOM 1436 CA ASN B 83 9.913 25.948 13.859 1.00 13.03 C ANISOU 1436 CA ASN B 83 1851 1439 1659 116 -438 -29 C ATOM 1437 C ASN B 83 10.962 25.876 14.980 1.00 11.00 C ANISOU 1437 C ASN B 83 1485 1257 1435 103 -311 72 C ATOM 1438 O ASN B 83 11.658 24.863 15.113 1.00 12.32 O ANISOU 1438 O ASN B 83 1941 1171 1567 91 -254 32 O ATOM 1439 CB ASN B 83 8.729 25.043 14.268 1.00 14.23 C ANISOU 1439 CB ASN B 83 1674 1673 2057 118 -501 149 C ATOM 1440 CG ASN B 83 7.555 25.068 13.300 1.00 14.00 C ANISOU 1440 CG ASN B 83 2031 1591 1695 179 -482 175 C ATOM 1441 OD1 ASN B 83 7.032 26.125 12.951 1.00 15.78 O ANISOU 1441 OD1 ASN B 83 1966 1724 2304 66 -643 209 O ATOM 1442 ND2 ASN B 83 7.094 23.906 12.930 1.00 17.67 N ANISOU 1442 ND2 ASN B 83 2127 1966 2621 -174 -869 -54 N ATOM 1443 N ILE B 84 11.069 26.933 15.716 1.00 10.55 N ANISOU 1443 N ILE B 84 1544 1204 1259 159 -275 88 N ATOM 1444 CA ILE B 84 12.066 27.097 16.740 1.00 10.30 C ANISOU 1444 CA ILE B 84 1441 1185 1286 132 -238 35 C ATOM 1445 C ILE B 84 11.422 27.415 18.089 1.00 10.72 C ANISOU 1445 C ILE B 84 1486 1138 1447 133 -28 -15 C ATOM 1446 O ILE B 84 10.715 28.444 18.205 1.00 11.44 O ANISOU 1446 O ILE B 84 1621 1368 1355 457 62 246 O ATOM 1447 CB ILE B 84 13.018 28.257 16.333 1.00 10.72 C ANISOU 1447 CB ILE B 84 1324 1383 1366 291 -147 92 C ATOM 1448 CG1 ILE B 84 13.836 27.841 15.107 1.00 12.61 C ANISOU 1448 CG1 ILE B 84 1434 1760 1597 37 -208 -20 C ATOM 1449 CG2 ILE B 84 13.962 28.701 17.485 1.00 12.47 C ANISOU 1449 CG2 ILE B 84 1527 1621 1590 182 -98 -192 C ATOM 1450 CD1 ILE B 84 14.544 28.997 14.424 1.00 13.63 C ANISOU 1450 CD1 ILE B 84 1462 1902 1814 70 180 -159 C ATOM 1451 N ILE B 85 11.675 26.581 19.108 1.00 10.21 N ANISOU 1451 N ILE B 85 1367 1098 1412 270 14 2 N ATOM 1452 CA ILE B 85 11.297 26.930 20.476 1.00 10.72 C ANISOU 1452 CA ILE B 85 1419 1255 1398 246 186 73 C ATOM 1453 C ILE B 85 12.493 27.592 21.121 1.00 9.85 C ANISOU 1453 C ILE B 85 1314 1379 1050 198 294 61 C ATOM 1454 O ILE B 85 13.560 26.972 21.266 1.00 10.94 O ANISOU 1454 O ILE B 85 1266 1395 1494 326 132 -60 O ATOM 1455 CB ILE B 85 10.880 25.654 21.304 1.00 12.09 C ANISOU 1455 CB ILE B 85 1633 1474 1484 95 137 168 C ATOM 1456 CG1 ILE B 85 9.754 24.932 20.582 1.00 15.23 C ANISOU 1456 CG1 ILE B 85 2090 1412 2284 -120 -47 322 C ATOM 1457 CG2 ILE B 85 10.524 26.063 22.665 1.00 12.69 C ANISOU 1457 CG2 ILE B 85 1481 1689 1649 120 474 429 C ATOM 1458 CD1 ILE B 85 8.467 25.766 20.430 1.00 18.65 C ANISOU 1458 CD1 ILE B 85 2246 1857 2980 -188 -631 190 C ATOM 1459 N GLY B 86 12.333 28.857 21.483 1.00 10.06 N ANISOU 1459 N GLY B 86 1415 1159 1248 315 104 26 N ATOM 1460 CA GLY B 86 13.383 29.610 22.055 1.00 9.99 C ANISOU 1460 CA GLY B 86 1661 1230 901 271 169 92 C ATOM 1461 C GLY B 86 13.328 29.669 23.553 1.00 9.83 C ANISOU 1461 C GLY B 86 1304 1351 1076 316 192 60 C ATOM 1462 O GLY B 86 12.439 29.093 24.212 1.00 11.00 O ANISOU 1462 O GLY B 86 1517 1370 1290 313 162 185 O ATOM 1463 N ARG B 87 14.278 30.351 24.130 1.00 10.61 N ANISOU 1463 N ARG B 87 1500 1486 1045 276 144 152 N ATOM 1464 CA ARG B 87 14.458 30.370 25.564 1.00 10.61 C ANISOU 1464 CA ARG B 87 1486 1670 872 412 78 -27 C ATOM 1465 C ARG B 87 13.252 30.891 26.323 1.00 12.37 C ANISOU 1465 C ARG B 87 1803 1745 1153 471 62 154 C ATOM 1466 O ARG B 87 12.985 30.426 27.462 1.00 13.84 O ANISOU 1466 O ARG B 87 1862 2188 1209 632 313 364 O ATOM 1467 CB ARG B 87 15.676 31.153 25.942 1.00 10.62 C ANISOU 1467 CB ARG B 87 1856 1374 801 382 133 -40 C ATOM 1468 CG ARG B 87 16.983 30.575 25.492 1.00 11.63 C ANISOU 1468 CG ARG B 87 1563 1597 1257 285 28 -99 C ATOM 1469 CD ARG B 87 18.210 31.314 26.036 1.00 12.31 C ANISOU 1469 CD ARG B 87 1754 1732 1189 493 3 67 C ATOM 1470 NE ARG B 87 18.308 32.667 25.573 1.00 12.98 N ANISOU 1470 NE ARG B 87 1897 1676 1358 249 -150 -309 N ATOM 1471 CZ ARG B 87 17.923 33.750 26.266 1.00 14.06 C ANISOU 1471 CZ ARG B 87 2167 1799 1374 377 -48 -54 C ATOM 1472 NH1 ARG B 87 17.482 33.674 27.521 1.00 14.54 N ANISOU 1472 NH1 ARG B 87 2423 1653 1449 477 -104 -390 N ATOM 1473 NH2 ARG B 87 17.988 34.931 25.701 1.00 15.22 N ANISOU 1473 NH2 ARG B 87 2707 1662 1411 152 -81 -344 N ATOM 1474 N ASN B 88 12.454 31.772 25.714 1.00 11.17 N ANISOU 1474 N ASN B 88 1733 1612 898 497 240 34 N ATOM 1475 CA ASN B 88 11.272 32.266 26.405 1.00 12.83 C ANISOU 1475 CA ASN B 88 1802 1709 1362 426 377 -222 C ATOM 1476 C ASN B 88 10.330 31.186 26.827 1.00 13.19 C ANISOU 1476 C ASN B 88 2034 1895 1082 587 358 294 C ATOM 1477 O ASN B 88 9.654 31.352 27.847 1.00 15.57 O ANISOU 1477 O ASN B 88 2168 2298 1448 667 793 250 O ATOM 1478 CB ASN B 88 10.568 33.349 25.527 1.00 12.79 C ANISOU 1478 CB ASN B 88 1684 1461 1712 476 432 -24 C ATOM 1479 CG ASN B 88 9.803 32.782 24.387 1.00 13.49 C ANISOU 1479 CG ASN B 88 1753 1619 1752 299 338 443 C ATOM 1480 OD1 ASN B 88 10.351 32.034 23.533 1.00 12.59 O ANISOU 1480 OD1 ASN B 88 1780 1641 1361 413 330 158 O ATOM 1481 ND2 ASN B 88 8.531 33.181 24.274 1.00 13.57 N ANISOU 1481 ND2 ASN B 88 1591 1843 1720 516 315 389 N ATOM 1482 N LEU B 89 10.210 30.103 26.056 1.00 13.00 N ANISOU 1482 N LEU B 89 1677 1803 1457 518 506 166 N ATOM 1483 CA LEU B 89 9.413 28.958 26.411 1.00 13.92 C ANISOU 1483 CA LEU B 89 1803 2000 1484 535 568 385 C ATOM 1484 C LEU B 89 10.193 27.791 26.992 1.00 13.78 C ANISOU 1484 C LEU B 89 1945 1956 1333 665 623 311 C ATOM 1485 O LEU B 89 9.644 27.042 27.818 1.00 15.18 O ANISOU 1485 O LEU B 89 1965 2276 1525 548 746 612 O ATOM 1486 CB LEU B 89 8.590 28.506 25.270 1.00 13.59 C ANISOU 1486 CB LEU B 89 1615 1784 1765 482 664 423 C ATOM 1487 CG LEU B 89 7.658 29.568 24.600 1.00 13.46 C ANISOU 1487 CG LEU B 89 1501 1825 1787 360 386 289 C ATOM 1488 CD1 LEU B 89 6.853 28.923 23.541 1.00 15.36 C ANISOU 1488 CD1 LEU B 89 1678 1960 2199 145 507 763 C ATOM 1489 CD2 LEU B 89 6.752 30.269 25.656 1.00 15.01 C ANISOU 1489 CD2 LEU B 89 1678 2036 1988 452 588 520 C ATOM 1490 N LEU B 90 11.475 27.643 26.634 1.00 12.29 N ANISOU 1490 N LEU B 90 1742 1651 1274 459 438 380 N ATOM 1491 CA LEU B 90 12.274 26.603 27.228 1.00 12.48 C ANISOU 1491 CA LEU B 90 1770 1769 1200 355 328 375 C ATOM 1492 C LEU B 90 12.338 26.726 28.715 1.00 13.48 C ANISOU 1492 C LEU B 90 1879 1987 1254 491 548 487 C ATOM 1493 O LEU B 90 12.306 25.707 29.410 1.00 16.04 O ANISOU 1493 O LEU B 90 2232 2357 1503 902 749 663 O ATOM 1494 CB LEU B 90 13.692 26.573 26.629 1.00 11.51 C ANISOU 1494 CB LEU B 90 1476 1638 1256 394 316 295 C ATOM 1495 CG LEU B 90 13.788 26.238 25.125 1.00 11.34 C ANISOU 1495 CG LEU B 90 1586 1428 1294 344 303 196 C ATOM 1496 CD1 LEU B 90 15.226 26.468 24.633 1.00 11.34 C ANISOU 1496 CD1 LEU B 90 1728 1777 801 364 218 12 C ATOM 1497 CD2 LEU B 90 13.358 24.827 24.881 1.00 12.38 C ANISOU 1497 CD2 LEU B 90 1530 1746 1425 306 294 124 C ATOM 1498 N THR B 91 12.497 27.923 29.225 1.00 14.65 N ANISOU 1498 N THR B 91 2234 2117 1214 715 276 423 N ATOM 1499 CA THR B 91 12.514 28.086 30.712 1.00 16.50 C ANISOU 1499 CA THR B 91 2097 3000 1169 869 320 220 C ATOM 1500 C THR B 91 11.186 27.602 31.324 1.00 17.17 C ANISOU 1500 C THR B 91 1983 3310 1231 955 416 170 C ATOM 1501 O THR B 91 11.203 27.023 32.450 1.00 18.29 O ANISOU 1501 O THR B 91 2387 3357 1202 944 474 416 O ATOM 1502 CB THR B 91 12.764 29.538 31.103 1.00 18.89 C ANISOU 1502 CB THR B 91 2453 3314 1408 818 52 -7 C ATOM 1503 OG1 THR B 91 11.819 30.395 30.494 1.00 19.93 O ANISOU 1503 OG1 THR B 91 2913 2927 1732 1323 135 -282 O ATOM 1504 CG2 THR B 91 14.145 30.047 30.670 1.00 18.42 C ANISOU 1504 CG2 THR B 91 2958 2824 1217 709 61 -112 C ATOM 1505 N GLN B 92 10.071 27.832 30.653 1.00 16.73 N ANISOU 1505 N GLN B 92 2180 2773 1403 1175 545 511 N ATOM 1506 CA GLN B 92 8.791 27.545 31.232 1.00 18.14 C ANISOU 1506 CA GLN B 92 2286 2876 1729 894 674 310 C ATOM 1507 C GLN B 92 8.529 26.039 31.369 1.00 19.54 C ANISOU 1507 C GLN B 92 2299 3023 2100 857 860 736 C ATOM 1508 O GLN B 92 7.802 25.598 32.277 1.00 21.58 O ANISOU 1508 O GLN B 92 2789 3456 1951 1024 1129 1072 O ATOM 1509 CB GLN B 92 7.732 28.144 30.405 1.00 17.22 C ANISOU 1509 CB GLN B 92 2097 2720 1722 740 709 735 C ATOM 1510 CG GLN B 92 7.712 29.654 30.394 1.00 17.95 C ANISOU 1510 CG GLN B 92 2104 2700 2014 590 709 652 C ATOM 1511 CD GLN B 92 6.454 30.223 29.783 1.00 17.33 C ANISOU 1511 CD GLN B 92 2444 2535 1606 342 191 509 C ATOM 1512 OE1 GLN B 92 5.679 29.511 29.362 1.00 23.32 O ANISOU 1512 OE1 GLN B 92 2379 2625 3855 347 -73 1046 O ATOM 1513 NE2 GLN B 92 6.483 31.502 29.461 1.00 24.09 N ANISOU 1513 NE2 GLN B 92 3164 2507 3479 619 -722 -76 N ATOM 1514 N ILE B 93 9.182 25.254 30.533 1.00 19.08 N ANISOU 1514 N ILE B 93 2357 2688 2201 1143 1103 788 N ATOM 1515 CA ILE B 93 9.050 23.771 30.601 1.00 20.74 C ANISOU 1515 CA ILE B 93 2331 2779 2770 675 841 740 C ATOM 1516 C ILE B 93 10.219 23.103 31.326 1.00 20.47 C ANISOU 1516 C ILE B 93 2569 3049 2159 732 1071 692 C ATOM 1517 O ILE B 93 10.264 21.866 31.441 1.00 24.52 O ANISOU 1517 O ILE B 93 3630 3150 2534 1295 1299 1095 O ATOM 1518 CB ILE B 93 8.900 23.129 29.231 1.00 19.73 C ANISOU 1518 CB ILE B 93 2458 2172 2863 607 990 763 C ATOM 1519 CG1 ILE B 93 10.196 23.290 28.417 1.00 19.59 C ANISOU 1519 CG1 ILE B 93 2528 2707 2207 561 983 649 C ATOM 1520 CG2 ILE B 93 7.757 23.755 28.458 1.00 20.63 C ANISOU 1520 CG2 ILE B 93 2574 2782 2479 584 884 579 C ATOM 1521 CD1 ILE B 93 10.176 22.541 27.111 1.00 21.14 C ANISOU 1521 CD1 ILE B 93 2588 2252 3191 84 1058 312 C ATOM 1522 N GLY B 94 11.050 23.876 31.922 1.00 19.19 N ANISOU 1522 N GLY B 94 2380 3020 1889 1028 984 809 N ATOM 1523 CA GLY B 94 12.074 23.324 32.808 1.00 21.76 C ANISOU 1523 CA GLY B 94 2784 3149 2335 1338 723 983 C ATOM 1524 C GLY B 94 13.375 22.893 32.148 1.00 19.87 C ANISOU 1524 C GLY B 94 2687 3063 1797 1249 867 866 C ATOM 1525 O GLY B 94 14.147 22.175 32.749 1.00 21.90 O ANISOU 1525 O GLY B 94 2818 3326 2177 1516 1095 1426 O ATOM 1526 N CYS B 95 13.631 23.370 30.943 1.00 18.57 N ANISOU 1526 N CYS B 95 2678 2794 1582 1278 623 687 N ATOM 1527 CA CYS B 95 14.751 22.865 30.121 1.00 17.40 C ANISOU 1527 CA CYS B 95 2586 2300 1725 914 679 421 C ATOM 1528 C CYS B 95 16.098 23.520 30.542 1.00 16.89 C ANISOU 1528 C CYS B 95 2527 2284 1606 763 732 515 C ATOM 1529 O CYS B 95 16.240 24.742 30.594 1.00 20.06 O ANISOU 1529 O CYS B 95 3119 2412 2091 998 1096 531 O ATOM 1530 CB CYS B 95 14.445 23.138 28.633 1.00 17.32 C ANISOU 1530 CB CYS B 95 2704 2173 1704 681 439 767 C ATOM 1531 SG CYS B 95 15.519 22.343 27.529 1.00 18.62 S ANISOU 1531 SG CYS B 95 2267 2733 2071 934 704 656 S ATOM 1532 N THR B 96 17.141 22.650 30.687 1.00 16.03 N ANISOU 1532 N THR B 96 2564 2249 1277 883 528 477 N ATOM 1533 CA THR B 96 18.489 23.082 30.938 1.00 16.44 C ANISOU 1533 CA THR B 96 2701 2136 1407 669 157 266 C ATOM 1534 C THR B 96 19.433 22.409 29.949 1.00 13.17 C ANISOU 1534 C THR B 96 2223 1846 933 505 133 199 C ATOM 1535 O THR B 96 19.087 21.390 29.353 1.00 14.87 O ANISOU 1535 O THR B 96 2240 2149 1259 489 214 172 O ATOM 1536 CB THR B 96 18.970 22.705 32.364 1.00 18.50 C ANISOU 1536 CB THR B 96 3047 2788 1192 682 400 271 C ATOM 1537 OG1 THR B 96 18.750 21.317 32.595 1.00 18.58 O ANISOU 1537 OG1 THR B 96 2795 2664 1600 692 367 568 O ATOM 1538 CG2 THR B 96 18.209 23.472 33.445 1.00 21.13 C ANISOU 1538 CG2 THR B 96 3503 2904 1619 687 459 -63 C ATOM 1539 N LEU B 97 20.609 22.972 29.837 1.00 14.65 N ANISOU 1539 N LEU B 97 2391 1775 1399 515 209 148 N ATOM 1540 CA LEU B 97 21.738 22.344 29.161 1.00 13.67 C ANISOU 1540 CA LEU B 97 2119 1810 1264 401 163 44 C ATOM 1541 C LEU B 97 22.591 21.705 30.215 1.00 14.83 C ANISOU 1541 C LEU B 97 2285 1831 1519 417 108 72 C ATOM 1542 O LEU B 97 22.842 22.322 31.254 1.00 17.70 O ANISOU 1542 O LEU B 97 2741 1926 2056 545 -328 -211 O ATOM 1543 CB LEU B 97 22.591 23.388 28.477 1.00 16.03 C ANISOU 1543 CB LEU B 97 2300 1929 1861 270 80 178 C ATOM 1544 CG LEU B 97 22.060 23.965 27.249 1.00 16.05 C ANISOU 1544 CG LEU B 97 1976 2223 1900 284 -99 -98 C ATOM 1545 CD1 LEU B 97 22.789 25.296 26.813 1.00 19.24 C ANISOU 1545 CD1 LEU B 97 2533 2486 2291 109 63 515 C ATOM 1546 CD2 LEU B 97 22.135 22.934 26.122 1.00 17.64 C ANISOU 1546 CD2 LEU B 97 2559 2702 1442 409 45 166 C ATOM 1547 N ASN B 98 23.163 20.574 29.936 1.00 15.03 N ANISOU 1547 N ASN B 98 2589 1870 1250 528 153 208 N ATOM 1548 CA ASN B 98 23.929 19.848 30.932 1.00 16.84 C ANISOU 1548 CA ASN B 98 2654 2145 1598 619 143 359 C ATOM 1549 C ASN B 98 25.108 19.170 30.258 1.00 16.26 C ANISOU 1549 C ASN B 98 2352 2055 1770 545 111 151 C ATOM 1550 O ASN B 98 24.949 18.437 29.320 1.00 17.04 O ANISOU 1550 O ASN B 98 2494 2205 1773 639 -5 223 O ATOM 1551 CB ASN B 98 23.076 18.787 31.618 1.00 16.41 C ANISOU 1551 CB ASN B 98 2131 2400 1703 612 57 223 C ATOM 1552 CG ASN B 98 21.897 19.359 32.314 1.00 17.32 C ANISOU 1552 CG ASN B 98 2763 2354 1463 672 244 260 C ATOM 1553 OD1 ASN B 98 20.861 19.696 31.696 1.00 21.19 O ANISOU 1553 OD1 ASN B 98 2948 3043 2057 974 164 467 O ATOM 1554 ND2 ASN B 98 21.968 19.398 33.597 1.00 21.01 N ANISOU 1554 ND2 ASN B 98 3211 3259 1510 316 363 506 N ATOM 1555 N PHE B 99 26.308 19.340 30.868 1.00 19.05 N ANISOU 1555 N PHE B 99 2538 2503 2195 610 -42 184 N ATOM 1556 CA PHE B 99 27.477 18.594 30.495 1.00 19.26 C ANISOU 1556 CA PHE B 99 2428 2636 2254 497 51 213 C ATOM 1557 C PHE B 99 28.480 18.540 31.605 1.00 23.60 C ANISOU 1557 C PHE B 99 2755 3459 2750 389 -84 119 C ATOM 1558 O PHE B 99 29.553 17.923 31.408 1.00 26.36 O ANISOU 1558 O PHE B 99 3025 3880 3110 792 -180 725 O ATOM 1559 CB PHE B 99 28.125 19.197 29.195 1.00 18.95 C ANISOU 1559 CB PHE B 99 2170 2672 2357 587 -100 132 C ATOM 1560 CG PHE B 99 28.559 20.660 29.319 1.00 20.10 C ANISOU 1560 CG PHE B 99 2544 2764 2326 458 -215 229 C ATOM 1561 CD1 PHE B 99 27.689 21.660 29.066 1.00 19.53 C ANISOU 1561 CD1 PHE B 99 2842 2443 2135 467 -389 200 C ATOM 1562 CD2 PHE B 99 29.904 20.980 29.389 1.00 22.05 C ANISOU 1562 CD2 PHE B 99 2672 2564 3139 206 -244 400 C ATOM 1563 CE1 PHE B 99 28.111 22.973 29.105 1.00 21.02 C ANISOU 1563 CE1 PHE B 99 2856 2490 2639 510 -248 507 C ATOM 1564 CE2 PHE B 99 30.313 22.255 29.420 1.00 22.95 C ANISOU 1564 CE2 PHE B 99 2734 2704 3280 29 -455 147 C ATOM 1565 CZ PHE B 99 29.422 23.262 29.175 1.00 23.61 C ANISOU 1565 CZ PHE B 99 3176 2409 3382 184 -69 -154 C ATOM 1566 OXT PHE B 99 28.224 19.068 32.704 1.00 24.03 O ANISOU 1566 OXT PHE B 99 3057 3529 2544 526 -310 201 O TER 1567 PHE B 99 HETATM 1568 P PO4 A 502 21.885 38.055 28.472 1.00 48.18 P ANISOU 1568 P PO4 A 502 7425 4338 6542 -728 -211 -475 P HETATM 1569 O1 PO4 A 502 20.858 37.017 28.170 1.00 29.71 O ANISOU 1569 O1 PO4 A 502 5708 2636 2942 169 -226 -847 O HETATM 1570 O2 PO4 A 502 22.214 37.997 29.948 1.00 51.15 O ANISOU 1570 O2 PO4 A 502 7216 5665 6553 -804 -686 -322 O HETATM 1571 O3 PO4 A 502 21.307 39.440 28.149 1.00 53.51 O ANISOU 1571 O3 PO4 A 502 7234 5416 7680 228 -110 241 O HETATM 1572 O4 PO4 A 502 23.219 37.809 27.658 1.00 51.63 O ANISOU 1572 O4 PO4 A 502 7180 5767 6669 -170 -184 195 O HETATM 1573 P PO4 A 504 42.373 37.711 14.743 1.00 40.32 P ANISOU 1573 P PO4 A 504 5222 3664 6432 -743 -338 1127 P HETATM 1574 O1 PO4 A 504 41.820 36.448 15.184 1.00 27.77 O ANISOU 1574 O1 PO4 A 504 3264 2652 4633 -286 -505 472 O HETATM 1575 O2 PO4 A 504 43.098 38.349 15.925 1.00 48.29 O ANISOU 1575 O2 PO4 A 504 5823 6185 6338 -52 -481 -28 O HETATM 1576 O3 PO4 A 504 41.277 38.652 14.226 1.00 44.12 O ANISOU 1576 O3 PO4 A 504 5603 4123 7036 370 26 345 O HETATM 1577 O4 PO4 A 504 43.377 37.445 13.606 1.00 50.93 O ANISOU 1577 O4 PO4 A 504 6722 6316 6311 -268 83 360 O HETATM 1578 P PO4 A 505 34.643 38.029 22.219 1.00 49.35 P ANISOU 1578 P PO4 A 505 4814 5880 8055 -96 -819 401 P HETATM 1579 O1 PO4 A 505 34.551 36.694 21.697 1.00 35.99 O ANISOU 1579 O1 PO4 A 505 2836 5070 5767 113 -781 1030 O HETATM 1580 O2 PO4 A 505 34.964 37.984 23.733 1.00 51.20 O ANISOU 1580 O2 PO4 A 505 6372 5473 7607 -361 -122 -185 O HETATM 1581 O3 PO4 A 505 33.267 38.781 21.998 1.00 49.54 O ANISOU 1581 O3 PO4 A 505 5555 5214 8054 303 -639 -7 O HETATM 1582 O4 PO4 A 505 35.779 38.755 21.456 1.00 55.19 O ANISOU 1582 O4 PO4 A 505 6207 7035 7727 -288 310 416 O HETATM 1583 N1 017 A1200 14.279 34.925 18.220 1.00 14.67 N ANISOU 1583 N1 017 A1200 1726 1789 2057 346 395 12 N HETATM 1584 C2 017 A1200 15.195 34.330 17.380 1.00 12.94 C ANISOU 1584 C2 017 A1200 1584 1675 1658 405 179 5 C HETATM 1585 C3 017 A1200 16.193 35.169 16.760 1.00 12.63 C ANISOU 1585 C3 017 A1200 1719 1582 1495 369 -308 -10 C HETATM 1586 C4 017 A1200 17.180 34.513 15.867 1.00 11.85 C ANISOU 1586 C4 017 A1200 1408 1448 1645 416 -79 9 C HETATM 1587 C5 017 A1200 17.012 33.220 15.616 1.00 10.81 C ANISOU 1587 C5 017 A1200 1451 1355 1300 269 -33 -5 C HETATM 1588 C6 017 A1200 15.919 32.472 16.187 1.00 13.71 C ANISOU 1588 C6 017 A1200 1658 1686 1863 473 126 250 C HETATM 1589 C7 017 A1200 14.979 33.107 17.003 1.00 14.04 C ANISOU 1589 C7 017 A1200 1909 1699 1726 543 239 297 C HETATM 1590 S8 017 A1200 18.136 32.331 14.660 1.00 10.16 S ANISOU 1590 S8 017 A1200 1418 1164 1278 192 106 157 S HETATM 1591 O9 017 A1200 18.756 33.247 13.785 1.00 11.32 O ANISOU 1591 O9 017 A1200 1718 1349 1233 111 239 206 O HETATM 1592 O10 017 A1200 17.453 31.221 14.098 1.00 11.42 O ANISOU 1592 O10 017 A1200 1475 1384 1478 321 -121 141 O HETATM 1593 N11 017 A1200 19.316 31.708 15.598 1.00 10.03 N ANISOU 1593 N11 017 A1200 1446 1137 1227 134 29 15 N HETATM 1594 C12 017 A1200 20.128 32.699 16.353 1.00 11.72 C ANISOU 1594 C12 017 A1200 1507 1407 1538 167 -46 61 C HETATM 1595 C13 017 A1200 21.628 32.355 16.432 1.00 11.02 C ANISOU 1595 C13 017 A1200 1317 1365 1505 56 -113 167 C HETATM 1596 C14 017 A1200 22.279 32.317 15.034 1.00 12.13 C ANISOU 1596 C14 017 A1200 1555 1426 1627 -39 102 230 C HETATM 1597 C15 017 A1200 22.282 33.401 17.329 1.00 12.08 C ANISOU 1597 C15 017 A1200 1486 1458 1645 2 -205 83 C HETATM 1598 C16 017 A1200 19.063 30.433 16.294 1.00 9.17 C ANISOU 1598 C16 017 A1200 1280 1120 1082 86 53 135 C HETATM 1599 C17 017 A1200 19.962 29.337 15.738 1.00 8.55 C ANISOU 1599 C17 017 A1200 1240 1147 861 126 11 147 C HETATM 1600 O18 017 A1200 19.895 28.206 16.604 1.00 9.54 O ANISOU 1600 O18 017 A1200 1295 1260 1068 195 -97 98 O HETATM 1601 C19 017 A1200 19.599 28.895 14.297 1.00 8.43 C ANISOU 1601 C19 017 A1200 1096 1073 1034 180 -16 70 C HETATM 1602 N20 017 A1200 20.709 28.031 13.805 1.00 8.78 N ANISOU 1602 N20 017 A1200 1143 1204 989 58 0 148 N HETATM 1603 C21 017 A1200 21.566 28.405 12.887 1.00 9.33 C ANISOU 1603 C21 017 A1200 1315 1111 1118 90 42 188 C HETATM 1604 O22 017 A1200 21.634 29.442 12.299 1.00 9.69 O ANISOU 1604 O22 017 A1200 1302 1143 1235 184 186 227 O HETATM 1605 O23 017 A1200 22.469 27.402 12.655 1.00 9.66 O ANISOU 1605 O23 017 A1200 1196 1329 1145 242 168 154 O HETATM 1606 C24 017 A1200 23.321 27.511 11.496 1.00 10.12 C ANISOU 1606 C24 017 A1200 1240 1372 1232 144 261 278 C HETATM 1607 C25 017 A1200 24.640 26.896 11.912 1.00 10.46 C ANISOU 1607 C25 017 A1200 1165 1457 1352 90 147 165 C HETATM 1608 O26 017 A1200 24.413 25.475 11.833 1.00 10.09 O ANISOU 1608 O26 017 A1200 1188 1459 1185 130 -49 122 O HETATM 1609 C27 017 A1200 23.493 25.227 10.779 1.00 10.21 C ANISOU 1609 C27 017 A1200 1408 1362 1110 288 163 49 C HETATM 1610 O28 017 A1200 22.483 24.363 11.236 1.00 10.86 O ANISOU 1610 O28 017 A1200 1465 1407 1254 45 -125 71 O HETATM 1611 C29 017 A1200 21.193 25.063 11.296 1.00 10.64 C ANISOU 1611 C29 017 A1200 1203 1440 1400 120 -93 88 C HETATM 1612 C30 017 A1200 21.363 26.256 10.383 1.00 10.81 C ANISOU 1612 C30 017 A1200 1355 1548 1202 -4 -129 210 C HETATM 1613 C31 017 A1200 22.839 26.537 10.396 1.00 10.71 C ANISOU 1613 C31 017 A1200 1364 1558 1144 157 27 206 C HETATM 1614 C32 017 A1200 18.307 28.149 14.166 1.00 9.08 C ANISOU 1614 C32 017 A1200 1009 1231 1208 103 -58 105 C HETATM 1615 C33 017 A1200 18.054 26.400 12.363 1.00 10.63 C ANISOU 1615 C33 017 A1200 1348 1355 1333 159 -153 -98 C HETATM 1616 C34 017 A1200 17.831 26.025 11.051 1.00 11.17 C ANISOU 1616 C34 017 A1200 1531 1274 1438 154 -274 -223 C HETATM 1617 C35 017 A1200 17.597 26.981 10.098 1.00 11.51 C ANISOU 1617 C35 017 A1200 1431 1533 1408 157 -58 11 C HETATM 1618 C36 017 A1200 17.550 28.293 10.460 1.00 11.00 C ANISOU 1618 C36 017 A1200 1533 1506 1138 130 -141 45 C HETATM 1619 C37 017 A1200 17.765 28.674 11.767 1.00 10.26 C ANISOU 1619 C37 017 A1200 1570 1360 968 29 -78 70 C HETATM 1620 C38 017 A1200 18.024 27.733 12.757 1.00 9.32 C ANISOU 1620 C38 017 A1200 1201 1244 1096 40 -21 23 C HETATM 1621 P PO4 B 501 -5.626 26.300 22.085 1.00 23.36 P ANISOU 1621 P PO4 B 501 2912 2992 2969 -349 -343 492 P HETATM 1622 O1 PO4 B 501 -4.465 25.632 22.864 1.00 24.90 O ANISOU 1622 O1 PO4 B 501 3245 3580 2633 -792 -1169 638 O HETATM 1623 O2 PO4 B 501 -4.920 27.015 21.053 1.00 26.37 O ANISOU 1623 O2 PO4 B 501 3311 2701 4008 -926 1056 -313 O HETATM 1624 O3 PO4 B 501 -6.680 25.278 21.514 1.00 31.16 O ANISOU 1624 O3 PO4 B 501 3220 4608 4010 -1522 423 -1016 O HETATM 1625 O4 PO4 B 501 -6.552 27.339 22.925 1.00 28.48 O ANISOU 1625 O4 PO4 B 501 2629 3651 4540 447 625 336 O HETATM 1626 P PO4 B 503 12.482 12.194 33.278 1.00 38.88 P ANISOU 1626 P PO4 B 503 6369 4805 3597 -929 774 992 P HETATM 1627 O1 PO4 B 503 12.623 10.721 33.366 1.00 39.20 O ANISOU 1627 O1 PO4 B 503 5784 4309 4799 -1573 383 1435 O HETATM 1628 O2 PO4 B 503 13.862 12.883 33.347 1.00 49.22 O ANISOU 1628 O2 PO4 B 503 5744 6389 6568 -583 94 124 O HETATM 1629 O3 PO4 B 503 11.756 12.585 32.008 1.00 43.18 O ANISOU 1629 O3 PO4 B 503 5696 6200 4508 113 220 684 O HETATM 1630 O4 PO4 B 503 11.649 12.645 34.454 1.00 51.01 O ANISOU 1630 O4 PO4 B 503 7301 7162 4918 59 1055 -122 O HETATM 1631 O HOH A1201 20.056 21.395 15.795 1.00 9.72 O ANISOU 1631 O HOH A1201 1375 1126 1189 88 -87 -142 O HETATM 1632 O HOH A1202 19.502 22.761 13.407 1.00 11.00 O ANISOU 1632 O HOH A1202 1590 1367 1221 61 -42 218 O HETATM 1633 O HOH A1203 20.376 31.870 11.841 1.00 11.01 O ANISOU 1633 O HOH A1203 1577 1310 1293 166 87 226 O HETATM 1634 O HOH A1204 24.470 14.948 23.041 1.00 18.99 O ANISOU 1634 O HOH A1204 2570 2506 2139 941 -33 277 O HETATM 1635 O HOH A1205 32.126 16.598 15.801 1.00 20.67 O ANISOU 1635 O HOH A1205 2331 2679 2841 845 337 46 O HETATM 1636 O HOH A1206 31.152 23.564 12.349 1.00 14.98 O ANISOU 1636 O HOH A1206 1647 2270 1773 693 514 273 O HETATM 1637 O HOH A1207 19.773 31.510 33.212 1.00 23.07 O ANISOU 1637 O HOH A1207 4176 2651 1938 803 -645 -498 O HETATM 1638 O HOH A1208 38.527 15.568 15.489 1.00 16.16 O ANISOU 1638 O HOH A1208 2405 1867 1866 392 391 357 O HETATM 1639 O HOH A1209 30.242 38.855 12.622 1.00 19.27 O ANISOU 1639 O HOH A1209 2149 1880 3291 76 -131 659 O HETATM 1640 O HOH A1210 37.509 18.927 30.928 1.00 66.30 O ANISOU 1640 O HOH A1210 8978 8382 7828 -19 -219 -412 O HETATM 1641 O HOH A1211 22.554 36.018 1.390 1.00 22.79 O ANISOU 1641 O HOH A1211 2783 3019 2854 198 -398 -1102 O HETATM 1642 O HOH A1212 15.214 33.413 5.158 1.00 23.27 O ANISOU 1642 O HOH A1212 2278 4460 2101 -258 -84 -41 O HETATM 1643 O HOH A1213 32.655 38.325 11.281 1.00 18.19 O ANISOU 1643 O HOH A1213 2230 1700 2979 66 -393 643 O HETATM 1644 O HOH A1214 36.725 18.360 11.936 1.00 23.65 O ANISOU 1644 O HOH A1214 2453 2693 3839 880 958 164 O HETATM 1645 O HOH A1215 30.244 36.892 19.101 1.00 19.55 O ANISOU 1645 O HOH A1215 3088 1953 2386 220 -860 -189 O HETATM 1646 O HOH A1216 22.211 30.573 30.150 1.00 20.39 O ANISOU 1646 O HOH A1216 2890 2568 2288 509 181 193 O HETATM 1647 O HOH A1217 26.106 18.484 13.537 1.00 24.44 O ANISOU 1647 O HOH A1217 3413 1901 3972 -8 -663 -464 O HETATM 1648 O HOH A1218 40.990 22.357 7.513 1.00 26.41 O ANISOU 1648 O HOH A1218 2412 3857 3763 478 846 246 O HETATM 1649 O HOH A1219 35.011 36.725 19.441 1.00 27.60 O ANISOU 1649 O HOH A1219 3016 2766 4702 -976 -109 749 O HETATM 1650 O HOH A1220 28.937 24.711 0.721 1.00 26.97 O ANISOU 1650 O HOH A1220 3138 2632 4478 219 -146 -1635 O HETATM 1651 O HOH A1221 32.743 37.872 8.649 1.00 27.12 O ANISOU 1651 O HOH A1221 3094 4525 2684 -604 -72 230 O HETATM 1652 O HOH A1222 30.254 21.326 11.163 1.00 27.66 O ANISOU 1652 O HOH A1222 2607 4229 3673 729 -536 -928 O HETATM 1653 O HOH A1223 24.667 15.436 29.507 1.00 21.39 O ANISOU 1653 O HOH A1223 2577 2492 3055 821 233 746 O HETATM 1654 O HOH A1224 35.448 34.771 16.380 1.00 21.81 O ANISOU 1654 O HOH A1224 2696 2786 2803 -658 -771 845 O HETATM 1655 O HOH A1225 24.419 35.603 29.375 1.00 26.71 O ANISOU 1655 O HOH A1225 3973 2778 3397 -332 -209 -1372 O HETATM 1656 O HOH A1226 31.153 37.034 21.547 1.00 24.76 O ANISOU 1656 O HOH A1226 3566 2877 2965 164 -890 265 O HETATM 1657 O HOH A1227 23.183 25.239 5.038 1.00 25.08 O ANISOU 1657 O HOH A1227 2607 2497 4423 119 386 193 O HETATM 1658 O HOH A1228 40.557 20.352 22.611 1.00 25.67 O ANISOU 1658 O HOH A1228 2459 3479 3813 -359 -341 1070 O HETATM 1659 O HOH A1229 34.909 34.098 6.281 1.00 27.77 O ANISOU 1659 O HOH A1229 3899 3374 3277 -680 1030 679 O HETATM 1660 O HOH A1230 26.947 37.818 4.115 1.00 34.01 O ANISOU 1660 O HOH A1230 4955 3701 4266 918 474 1212 O HETATM 1661 O HOH A1231 19.571 33.367 35.118 1.00 30.22 O ANISOU 1661 O HOH A1231 5115 3454 2912 -298 26 -871 O HETATM 1662 O HOH A1232 14.317 35.443 30.347 1.00 41.94 O ANISOU 1662 O HOH A1232 4360 6363 5210 637 775 -169 O HETATM 1663 O HOH A1233 24.076 21.260 8.457 1.00 32.39 O ANISOU 1663 O HOH A1233 4193 5959 2155 -574 562 -17 O HETATM 1664 O HOH A1234 32.796 30.455 0.789 1.00 28.13 O ANISOU 1664 O HOH A1234 3757 3722 3207 577 1230 604 O HETATM 1665 O HOH A1235 16.879 37.933 4.787 1.00 28.00 O ANISOU 1665 O HOH A1235 4775 3244 2618 1317 871 530 O HETATM 1666 O HOH A1236 24.953 40.472 16.765 1.00 34.00 O ANISOU 1666 O HOH A1236 5190 3691 4035 1705 -689 -1214 O HETATM 1667 O HOH A1237 34.545 31.412 1.720 1.00 30.01 O ANISOU 1667 O HOH A1237 4551 3782 3070 474 1018 1060 O HETATM 1668 O HOH A1238 35.938 33.777 31.163 1.00 29.47 O ANISOU 1668 O HOH A1238 4540 3366 3289 611 -1556 -212 O HETATM 1669 O HOH A1239 14.337 33.445 28.692 1.00 30.90 O ANISOU 1669 O HOH A1239 4148 4326 3266 780 -194 287 O HETATM 1670 O HOH A1240 22.650 28.564 34.792 1.00 26.66 O ANISOU 1670 O HOH A1240 3904 3793 2430 -204 -494 -843 O HETATM 1671 O HOH A1241 25.499 12.874 24.637 1.00 29.83 O ANISOU 1671 O HOH A1241 3296 3301 4735 1147 -813 -506 O HETATM 1672 O HOH A1242 41.746 25.134 22.803 1.00 24.60 O ANISOU 1672 O HOH A1242 2203 2906 4235 137 -11 1156 O HETATM 1673 O HOH A1243 42.773 18.912 22.293 1.00 35.51 O ANISOU 1673 O HOH A1243 3873 4602 5017 550 -554 1170 O HETATM 1674 O HOH A1244 28.371 14.951 16.383 1.00 27.22 O ANISOU 1674 O HOH A1244 3819 4042 2482 -623 -114 -284 O HETATM 1675 O HOH A1245 46.003 28.741 16.572 1.00 29.53 O ANISOU 1675 O HOH A1245 3841 4245 3133 -623 29 -25 O HETATM 1676 O HOH A1246 37.435 40.536 13.076 1.00 41.26 O ANISOU 1676 O HOH A1246 4436 5395 5844 761 -350 692 O HETATM 1677 O HOH A1247 25.053 23.610 7.494 1.00 31.32 O ANISOU 1677 O HOH A1247 3884 4875 3141 -850 -530 -233 O HETATM 1678 O HOH A1248 33.742 16.688 28.022 1.00 26.46 O ANISOU 1678 O HOH A1248 3868 2978 3206 170 -462 539 O HETATM 1679 O HOH A1249 35.443 16.383 25.881 1.00 31.26 O ANISOU 1679 O HOH A1249 4264 4481 3130 -565 721 1030 O HETATM 1680 O HOH A1250 15.513 16.399 33.653 1.00 28.44 O ANISOU 1680 O HOH A1250 4050 4163 2590 -82 499 831 O HETATM 1681 O HOH A1251 25.338 27.070 35.519 1.00 35.80 O ANISOU 1681 O HOH A1251 5802 4431 3369 -860 -398 -773 O HETATM 1682 O HOH A1252 36.111 28.461 29.662 1.00 28.85 O ANISOU 1682 O HOH A1252 4595 2921 3443 -8 -1378 585 O HETATM 1683 O AHOH A1253 31.177 12.878 24.119 0.50 24.08 O ANISOU 1683 O AHOH A1253 4439 2318 2389 -395 -42 -82 O HETATM 1684 O BHOH A1253 18.188 40.860 6.058 0.50 35.73 O ANISOU 1684 O BHOH A1253 4555 5185 3833 105 57 1635 O HETATM 1685 O HOH A1254 10.764 20.315 33.810 1.00 30.38 O ANISOU 1685 O HOH A1254 5087 3512 2942 647 1096 863 O HETATM 1686 O HOH A1255 27.995 14.575 29.793 1.00 30.38 O ANISOU 1686 O HOH A1255 3766 4299 3475 501 -259 1274 O HETATM 1687 O HOH A1256 37.545 26.813 28.286 1.00 30.35 O ANISOU 1687 O HOH A1256 3518 3012 5002 -493 -397 -375 O HETATM 1688 O HOH A1257 43.767 18.571 15.523 1.00 26.15 O ANISOU 1688 O HOH A1257 2598 2867 4469 272 157 732 O HETATM 1689 O HOH A1258 25.719 12.974 27.397 1.00 32.15 O ANISOU 1689 O HOH A1258 5055 3078 4080 551 -353 -102 O HETATM 1690 O HOH A1259 32.635 35.021 4.224 1.00 30.91 O ANISOU 1690 O HOH A1259 4455 3489 3800 -1433 926 -445 O HETATM 1691 O HOH A1260 44.792 24.695 12.710 1.00 30.61 O ANISOU 1691 O HOH A1260 2414 3839 5377 -73 -579 -471 O HETATM 1692 O HOH A1261 32.684 28.589 30.555 1.00 41.52 O ANISOU 1692 O HOH A1261 6500 5633 3643 1384 -1889 56 O HETATM 1693 O HOH A1262 24.455 31.227 31.391 1.00 32.24 O ANISOU 1693 O HOH A1262 4609 4550 3090 -532 -233 -472 O HETATM 1694 O HOH A1263 18.720 18.456 36.423 1.00 28.00 O ANISOU 1694 O HOH A1263 3599 3822 3215 -361 231 404 O HETATM 1695 O HOH A1264 27.912 12.399 23.952 1.00 38.97 O ANISOU 1695 O HOH A1264 6223 1620 6962 1327 1449 -839 O HETATM 1696 O HOH A1265 29.009 37.657 23.043 1.00 39.75 O ANISOU 1696 O HOH A1265 4725 5789 4589 11 -541 313 O HETATM 1697 O HOH A1266 41.992 22.457 23.047 1.00 30.43 O ANISOU 1697 O HOH A1266 3585 3606 4368 291 -701 220 O HETATM 1698 O HOH A1267 46.896 32.717 19.184 1.00 29.90 O ANISOU 1698 O HOH A1267 3133 4208 4017 -763 262 -803 O HETATM 1699 O HOH A1268 44.655 29.609 7.419 1.00 30.54 O ANISOU 1699 O HOH A1268 4032 5151 2418 -1248 386 -212 O HETATM 1700 O HOH A1269 28.110 32.805 -3.098 1.00 29.00 O ANISOU 1700 O HOH A1269 3636 4827 2554 -830 123 -357 O HETATM 1701 O HOH A1270 20.387 24.569 4.514 1.00 41.39 O ANISOU 1701 O HOH A1270 5563 4342 5818 -293 -13 344 O HETATM 1702 O HOH A1271 17.306 14.511 32.564 1.00 27.93 O ANISOU 1702 O HOH A1271 3812 3323 3475 449 683 851 O HETATM 1703 O HOH A1272 26.089 16.318 15.993 1.00 31.89 O ANISOU 1703 O HOH A1272 3091 4141 4886 -68 -167 809 O HETATM 1704 O HOH A1273 25.310 36.597 2.688 1.00 28.48 O ANISOU 1704 O HOH A1273 4392 3081 3347 -553 -181 22 O HETATM 1705 O HOH A1274 32.223 30.978 30.868 1.00 35.13 O ANISOU 1705 O HOH A1274 5173 4798 3377 -176 -1281 -46 O HETATM 1706 O HOH A1275 25.031 16.305 13.856 1.00 33.56 O ANISOU 1706 O HOH A1275 4413 4571 3764 1187 1078 -534 O HETATM 1707 O HOH A1276 30.501 21.624 8.159 1.00 34.20 O ANISOU 1707 O HOH A1276 4910 4627 3456 246 -139 -699 O HETATM 1708 O HOH A1277 24.712 17.765 11.324 1.00 34.86 O ANISOU 1708 O HOH A1277 5012 5053 3178 866 -133 -996 O HETATM 1709 O HOH A1278 42.106 37.123 19.766 1.00 33.83 O ANISOU 1709 O HOH A1278 4176 3767 4910 -262 -986 767 O HETATM 1710 O HOH A1279 19.937 26.074 6.365 1.00 38.55 O ANISOU 1710 O HOH A1279 5898 3256 5493 -1400 32 -288 O HETATM 1711 O HOH A1280 22.643 31.133 33.338 1.00 35.62 O ANISOU 1711 O HOH A1280 4976 4258 4299 -267 -226 -418 O HETATM 1712 O HOH A1281 25.340 23.312 5.051 1.00 42.71 O ANISOU 1712 O HOH A1281 6433 5477 4317 -537 -102 -541 O HETATM 1713 O HOH A1282 38.841 22.407 5.563 1.00 35.94 O ANISOU 1713 O HOH A1282 5656 3304 4692 575 1814 198 O HETATM 1714 O HOH A1283 44.781 18.255 11.861 1.00 40.96 O ANISOU 1714 O HOH A1283 3882 5394 6287 -1323 -331 -297 O HETATM 1715 O HOH A1284 18.218 36.012 34.680 1.00 38.51 O ANISOU 1715 O HOH A1284 5701 5100 3830 48 58 -783 O HETATM 1716 O HOH A1285 43.783 28.111 29.364 1.00 44.82 O ANISOU 1716 O HOH A1285 5344 4814 6869 621 1439 -214 O HETATM 1717 O HOH A1286 38.353 37.628 16.353 1.00 36.63 O ANISOU 1717 O HOH A1286 5419 4003 4494 403 205 427 O HETATM 1718 O HOH A1287 28.388 39.092 19.490 1.00 37.49 O ANISOU 1718 O HOH A1287 5082 3711 5452 -51 593 -454 O HETATM 1719 O HOH A1288 32.279 20.461 34.588 1.00 39.70 O ANISOU 1719 O HOH A1288 4630 5344 5109 603 -792 -231 O HETATM 1720 O HOH A1289 27.637 16.777 14.422 1.00 36.29 O ANISOU 1720 O HOH A1289 5179 3745 4863 -639 -787 -1028 O HETATM 1721 O HOH A1290 34.831 36.424 7.793 1.00 32.74 O ANISOU 1721 O HOH A1290 4505 3325 4607 -690 -220 211 O HETATM 1722 O HOH A1291 18.420 28.713 5.642 1.00 32.44 O ANISOU 1722 O HOH A1291 3231 4835 4258 953 -622 -1846 O HETATM 1723 O HOH A1292 44.539 21.832 12.952 1.00 40.72 O ANISOU 1723 O HOH A1292 4806 4662 6000 1432 583 -342 O HETATM 1724 O HOH A1293 28.710 40.292 17.167 1.00 32.26 O ANISOU 1724 O HOH A1293 3265 4536 4454 -1210 -364 -120 O HETATM 1725 O HOH A1294 31.089 18.696 11.526 1.00 32.98 O ANISOU 1725 O HOH A1294 4166 4527 3836 -74 339 -399 O HETATM 1726 O HOH A1295 22.138 25.318 7.205 1.00 36.48 O ANISOU 1726 O HOH A1295 6915 3234 3708 155 598 -935 O HETATM 1727 O HOH A1296 43.165 35.376 24.302 1.00 34.46 O ANISOU 1727 O HOH A1296 3710 4141 5242 -1698 -710 -297 O HETATM 1728 O HOH A1297 9.950 16.601 33.231 1.00 42.27 O ANISOU 1728 O HOH A1297 4559 6389 5109 29 1494 287 O HETATM 1729 O HOH A1298 47.676 26.803 15.174 1.00 32.51 O ANISOU 1729 O HOH A1298 3158 5693 3501 -660 422 44 O HETATM 1730 O HOH A1299 24.497 38.712 24.884 1.00 35.29 O ANISOU 1730 O HOH A1299 3929 4092 5388 -193 -312 -231 O HETATM 1731 O HOH A1300 26.077 23.475 37.496 1.00 39.84 O ANISOU 1731 O HOH A1300 4840 7383 2914 172 -836 -1032 O HETATM 1732 O HOH A1301 45.583 39.291 21.124 1.00 42.18 O ANISOU 1732 O HOH A1301 4339 5985 5702 -446 183 -202 O HETATM 1733 O HOH A1302 36.208 35.773 26.365 1.00 39.14 O ANISOU 1733 O HOH A1302 4346 4878 5646 -328 -1089 -314 O HETATM 1734 O HOH A1303 41.931 23.159 1.641 1.00 40.61 O ANISOU 1734 O HOH A1303 4660 4994 5776 92 845 439 O HETATM 1735 O HOH A1304 40.929 38.006 10.984 1.00 42.83 O ANISOU 1735 O HOH A1304 3860 6268 6144 -947 272 1001 O HETATM 1736 O HOH A1305 21.309 15.342 33.578 1.00 45.22 O ANISOU 1736 O HOH A1305 5988 5651 5541 361 -1157 843 O HETATM 1737 O HOH A1306 46.579 37.296 24.570 1.00 42.72 O ANISOU 1737 O HOH A1306 5358 4744 6127 -779 129 776 O HETATM 1738 O HOH A1307 36.639 33.881 2.663 1.00 43.37 O ANISOU 1738 O HOH A1307 6399 4186 5893 43 -186 966 O HETATM 1739 O HOH A1308 24.975 36.848 8.418 1.00 15.39 O ANISOU 1739 O HOH A1308 2102 2177 1568 221 -38 -356 O HETATM 1740 O HOH A1309 45.923 21.928 7.589 1.00 42.77 O ANISOU 1740 O HOH A1309 5852 5104 5293 -202 -570 -899 O HETATM 1741 O HOH A1310 34.878 23.303 -0.051 1.00 32.26 O ANISOU 1741 O HOH A1310 4519 3025 4713 524 724 234 O HETATM 1742 O HOH A1311 13.769 37.610 19.371 1.00 31.62 O ANISOU 1742 O HOH A1311 4348 3054 4611 1299 -825 -942 O HETATM 1743 O HOH A1312 22.704 16.012 12.662 1.00 37.90 O ANISOU 1743 O HOH A1312 7779 3030 3590 290 1264 -1233 O HETATM 1744 O HOH A1313 44.642 32.978 24.326 1.00 34.43 O ANISOU 1744 O HOH A1313 2991 5138 4951 841 647 48 O HETATM 1745 O HOH A1314 43.119 24.270 9.372 1.00 28.78 O ANISOU 1745 O HOH A1314 3499 3775 3658 -64 -509 -462 O HETATM 1746 O HOH A1315 22.451 36.019 20.668 1.00 22.40 O ANISOU 1746 O HOH A1315 2973 2949 2588 -618 754 -250 O HETATM 1747 O HOH A1316 28.600 35.812 2.964 1.00 17.57 O ANISOU 1747 O HOH A1316 2534 1887 2252 -123 138 444 O HETATM 1748 O HOH A1317 33.107 18.564 13.765 1.00 17.56 O ANISOU 1748 O HOH A1317 1421 2326 2925 370 669 21 O HETATM 1749 O HOH A1318 26.425 19.750 9.549 1.00 39.08 O ANISOU 1749 O HOH A1318 4618 5214 5014 56 834 -2297 O HETATM 1750 O HOH A1319 33.522 18.357 4.079 1.00 44.77 O ANISOU 1750 O HOH A1319 6330 4799 5881 991 168 1 O HETATM 1751 O HOH A1320 22.063 41.553 21.585 1.00 47.19 O ANISOU 1751 O HOH A1320 6058 4796 7072 -137 402 299 O HETATM 1752 O HOH A1321 19.608 40.813 19.710 1.00 39.21 O ANISOU 1752 O HOH A1321 5887 4626 4385 -641 2 -359 O HETATM 1753 O HOH A1322 30.733 20.588 36.755 1.00 47.94 O ANISOU 1753 O HOH A1322 5188 6224 6802 184 206 47 O HETATM 1754 O HOH A1323 32.724 23.497 33.263 1.00 40.20 O ANISOU 1754 O HOH A1323 5334 4929 5008 -208 -189 -143 O HETATM 1755 O HOH A1324 20.727 21.038 40.272 1.00 36.61 O ANISOU 1755 O HOH A1324 4855 4269 4785 755 725 -450 O HETATM 1756 O HOH A1325 32.029 25.530 35.172 1.00 39.36 O ANISOU 1756 O HOH A1325 4394 4484 6076 -332 -674 -747 O HETATM 1757 O HOH A1326 40.751 22.044 4.169 1.00 43.23 O ANISOU 1757 O HOH A1326 6176 5901 4347 -410 -577 137 O HETATM 1758 O HOH A1327 35.055 30.170 31.704 1.00 38.05 O ANISOU 1758 O HOH A1327 5614 5239 3603 1297 -1587 499 O HETATM 1759 O HOH A1328 26.870 35.574 30.263 1.00 43.47 O ANISOU 1759 O HOH A1328 5210 5791 5515 64 -389 -456 O HETATM 1760 O HOH A1329 31.101 33.574 30.326 1.00 48.08 O ANISOU 1760 O HOH A1329 7009 5814 5442 286 -127 -286 O HETATM 1761 O HOH A1330 39.572 37.150 21.646 1.00 42.30 O ANISOU 1761 O HOH A1330 6553 3087 6431 -318 118 469 O HETATM 1762 O HOH A1331 46.762 22.551 10.702 1.00 40.74 O ANISOU 1762 O HOH A1331 4384 5898 5194 13 884 845 O HETATM 1763 O HOH A1332 35.775 17.843 5.329 1.00 44.19 O ANISOU 1763 O HOH A1332 6412 5111 5266 132 34 53 O HETATM 1764 O HOH A1333 22.630 37.426 18.479 1.00 44.32 O ANISOU 1764 O HOH A1333 6025 4330 6482 120 216 456 O HETATM 1765 O HOH B 504 20.059 32.352 23.522 1.00 13.80 O ANISOU 1765 O HOH B 504 2205 1382 1654 97 215 -199 O HETATM 1766 O HOH B 505 20.507 34.197 21.507 1.00 15.58 O ANISOU 1766 O HOH B 505 2051 2003 1863 64 12 272 O HETATM 1767 O HOH B 506 16.430 20.696 33.775 1.00 23.03 O ANISOU 1767 O HOH B 506 2894 3631 2226 1097 912 1031 O HETATM 1768 O HOH B 507 4.274 26.896 12.385 1.00 19.03 O ANISOU 1768 O HOH B 507 2115 2300 2813 -105 -241 506 O HETATM 1769 O HOH B 508 7.331 35.119 26.449 1.00 27.78 O ANISOU 1769 O HOH B 508 1916 3439 5200 564 599 2096 O HETATM 1770 O HOH B 509 18.250 34.775 19.403 1.00 19.66 O ANISOU 1770 O HOH B 509 3078 2854 1537 -987 -147 459 O HETATM 1771 O HOH B 510 11.226 38.582 5.803 1.00 16.85 O ANISOU 1771 O HOH B 510 2428 2169 1805 427 -501 -352 O HETATM 1772 O HOH B 511 7.083 21.848 32.909 1.00 21.68 O ANISOU 1772 O HOH B 511 3430 3033 1772 680 652 353 O HETATM 1773 O HOH B 512 18.309 15.699 19.458 1.00 22.14 O ANISOU 1773 O HOH B 512 2786 3613 2012 1029 152 557 O HETATM 1774 O HOH B 513 13.268 21.368 35.290 1.00 16.39 O ANISOU 1774 O HOH B 513 2248 2271 1707 5 221 335 O HETATM 1775 O HOH B 514 12.879 24.151 35.808 1.00 18.35 O ANISOU 1775 O HOH B 514 2318 2532 2119 269 -233 -159 O HETATM 1776 O HOH B 515 -2.282 25.216 21.978 1.00 21.48 O ANISOU 1776 O HOH B 515 2665 2895 2598 502 469 248 O HETATM 1777 O HOH B 516 14.238 34.890 26.221 1.00 24.98 O ANISOU 1777 O HOH B 516 3612 3458 2418 103 -86 -857 O HETATM 1778 O HOH B 517 5.459 23.896 32.088 1.00 21.41 O ANISOU 1778 O HOH B 517 3376 3312 1445 1316 425 -74 O HETATM 1779 O HOH B 518 7.728 29.685 7.373 1.00 16.96 O ANISOU 1779 O HOH B 518 2202 2301 1937 90 56 491 O HETATM 1780 O HOH B 519 9.015 29.148 34.883 1.00 43.32 O ANISOU 1780 O HOH B 519 5159 6251 5049 22 -653 190 O HETATM 1781 O HOH B 520 13.623 26.044 33.466 1.00 24.43 O ANISOU 1781 O HOH B 520 2829 4366 2084 938 500 862 O HETATM 1782 O HOH B 521 25.112 9.620 24.647 1.00 24.58 O ANISOU 1782 O HOH B 521 3315 2355 3668 250 -82 -848 O HETATM 1783 O HOH B 522 -0.061 25.407 27.096 1.00 22.33 O ANISOU 1783 O HOH B 522 3494 2715 2275 11 71 305 O HETATM 1784 O HOH B 523 10.236 22.555 12.067 1.00 21.91 O ANISOU 1784 O HOH B 523 2677 2242 3403 -20 -329 -577 O HETATM 1785 O HOH B 524 3.775 36.921 25.815 1.00 24.11 O ANISOU 1785 O HOH B 524 3201 2669 3290 595 -69 130 O HETATM 1786 O HOH B 525 -2.442 28.288 21.282 1.00 24.81 O ANISOU 1786 O HOH B 525 2446 2824 4154 -142 1464 -501 O HETATM 1787 O HOH B 526 8.878 34.461 21.070 1.00 26.92 O ANISOU 1787 O HOH B 526 3729 3369 3130 236 759 -237 O HETATM 1788 O HOH B 527 2.194 26.368 9.454 1.00 28.97 O ANISOU 1788 O HOH B 527 4441 3240 3325 -18 -254 512 O HETATM 1789 O HOH B 528 20.476 37.082 2.968 1.00 26.68 O ANISOU 1789 O HOH B 528 3695 3941 2500 324 408 750 O HETATM 1790 O HOH B 529 16.194 13.952 19.322 1.00 26.95 O ANISOU 1790 O HOH B 529 3007 3901 3331 625 -472 -85 O HETATM 1791 O HOH B 530 -7.964 25.545 18.326 1.00 23.85 O ANISOU 1791 O HOH B 530 1852 2040 5167 187 181 722 O HETATM 1792 O HOH B 531 20.049 15.903 12.263 1.00 23.87 O ANISOU 1792 O HOH B 531 4650 2462 1956 93 -561 -664 O HETATM 1793 O HOH B 532 12.163 20.807 10.967 1.00 26.82 O ANISOU 1793 O HOH B 532 2793 3698 3698 358 -1144 -432 O HETATM 1794 O HOH B 533 9.143 39.275 4.185 1.00 20.88 O ANISOU 1794 O HOH B 533 2601 2708 2624 330 -607 -448 O HETATM 1795 O HOH B 534 20.093 8.373 28.681 1.00 32.60 O ANISOU 1795 O HOH B 534 3790 3875 4721 520 1145 750 O HETATM 1796 O HOH B 535 6.030 20.723 11.805 1.00 30.51 O ANISOU 1796 O HOH B 535 3332 4437 3822 -207 -1155 1504 O HETATM 1797 O HOH B 536 15.739 14.859 14.844 1.00 22.41 O ANISOU 1797 O HOH B 536 3274 2593 2645 -383 -540 -872 O HETATM 1798 O HOH B 537 9.565 36.985 25.150 1.00 39.25 O ANISOU 1798 O HOH B 537 5575 4020 5317 947 386 -560 O HETATM 1799 O HOH B 538 9.010 23.208 34.209 1.00 35.10 O ANISOU 1799 O HOH B 538 3560 5872 3902 -51 1652 -357 O HETATM 1800 O HOH B 539 -2.501 43.372 15.143 1.00 27.05 O ANISOU 1800 O HOH B 539 2521 3119 4635 768 -770 658 O HETATM 1801 O HOH B 540 -0.804 39.254 20.807 1.00 30.39 O ANISOU 1801 O HOH B 540 3340 4511 3693 2147 86 -457 O HETATM 1802 O HOH B 541 2.375 18.404 22.966 1.00 34.98 O ANISOU 1802 O HOH B 541 3201 2788 7300 640 71 611 O HETATM 1803 O HOH B 542 14.905 20.464 11.029 1.00 32.13 O ANISOU 1803 O HOH B 542 2431 4163 5613 560 -39 981 O HETATM 1804 O HOH B 543 6.448 27.696 5.934 1.00 19.77 O ANISOU 1804 O HOH B 543 3544 2230 1735 -11 -33 221 O HETATM 1805 O HOH B 544 8.935 33.449 29.391 1.00 25.53 O ANISOU 1805 O HOH B 544 3264 2747 3688 248 1075 -453 O HETATM 1806 O HOH B 545 6.544 38.062 7.813 1.00 25.33 O ANISOU 1806 O HOH B 545 3052 3176 3393 273 -1185 -305 O HETATM 1807 O HOH B 546 16.565 12.122 21.874 1.00 29.60 O ANISOU 1807 O HOH B 546 2969 2812 5462 -175 -181 604 O HETATM 1808 O HOH B 547 4.396 13.392 17.438 1.00 37.27 O ANISOU 1808 O HOH B 547 4239 3734 6186 -1381 -948 405 O HETATM 1809 O HOH B 548 0.308 21.158 12.000 1.00 39.57 O ANISOU 1809 O HOH B 548 5833 3704 5495 606 -618 568 O HETATM 1810 O HOH B 549 -0.393 45.321 18.257 1.00 32.29 O ANISOU 1810 O HOH B 549 4718 3652 3898 1594 196 -323 O HETATM 1811 O HOH B 550 17.386 39.870 16.168 1.00 26.60 O ANISOU 1811 O HOH B 550 3264 4994 1849 710 -779 -1094 O HETATM 1812 O HOH B 551 -2.683 35.785 11.621 1.00 37.04 O ANISOU 1812 O HOH B 551 4445 5690 3939 -1327 -441 1761 O HETATM 1813 O HOH B 552 12.086 32.851 29.741 1.00 27.50 O ANISOU 1813 O HOH B 552 4155 3559 2734 849 313 478 O HETATM 1814 O HOH B 553 25.957 14.039 15.127 1.00 31.32 O ANISOU 1814 O HOH B 553 3931 3865 4103 328 69 411 O HETATM 1815 O HOH B 554 10.396 24.580 5.830 1.00 32.31 O ANISOU 1815 O HOH B 554 5231 4091 2954 -252 -1555 539 O HETATM 1816 O HOH B 555 -2.925 37.102 19.155 1.00 33.59 O ANISOU 1816 O HOH B 555 4263 3511 4988 -185 1265 1023 O HETATM 1817 O HOH B 556 4.351 24.868 8.774 1.00 28.02 O ANISOU 1817 O HOH B 556 3617 3137 3892 75 -251 319 O HETATM 1818 O HOH B 557 3.954 16.798 14.667 1.00 33.46 O ANISOU 1818 O HOH B 557 3716 3692 5303 -1114 -225 -235 O HETATM 1819 O HOH B 558 30.464 16.088 29.801 1.00 28.82 O ANISOU 1819 O HOH B 558 4479 3861 2609 283 -166 714 O HETATM 1820 O HOH B 559 20.575 10.240 27.056 1.00 33.54 O ANISOU 1820 O HOH B 559 5838 3285 3618 982 377 506 O HETATM 1821 O HOH B 560 9.556 41.810 21.114 1.00 38.40 O ANISOU 1821 O HOH B 560 5335 5825 3429 141 558 -413 O HETATM 1822 O HOH B 561 15.411 18.004 10.490 1.00 29.83 O ANISOU 1822 O HOH B 561 3495 4219 3619 -530 19 -62 O HETATM 1823 O HOH B 562 5.893 47.878 10.061 1.00 35.92 O ANISOU 1823 O HOH B 562 4482 5504 3660 -247 12 -910 O HETATM 1824 O HOH B 563 -2.201 28.661 8.649 1.00 29.85 O ANISOU 1824 O HOH B 563 2088 5250 4004 -527 -306 -1032 O HETATM 1825 O HOH B 564 -0.992 17.924 23.164 1.00 46.28 O ANISOU 1825 O HOH B 564 4652 6199 6730 906 -1493 745 O HETATM 1826 O HOH B 565 7.688 25.319 6.067 1.00 31.58 O ANISOU 1826 O HOH B 565 3873 3629 4495 98 -553 844 O HETATM 1827 O HOH B 566 13.615 43.441 17.686 1.00 42.24 O ANISOU 1827 O HOH B 566 5342 6448 4259 229 -1367 918 O HETATM 1828 O HOH B 567 21.217 36.675 16.069 1.00 29.55 O ANISOU 1828 O HOH B 567 3379 4224 3624 241 -514 628 O HETATM 1829 O HOH B 568 15.299 37.397 25.335 1.00 39.49 O ANISOU 1829 O HOH B 568 5895 4269 4841 847 801 -306 O HETATM 1830 O HOH B 569 9.672 39.413 21.198 1.00 34.96 O ANISOU 1830 O HOH B 569 3726 4371 5186 -176 121 -637 O HETATM 1831 O HOH B 570 13.360 13.966 14.676 1.00 40.67 O ANISOU 1831 O HOH B 570 5473 3842 6135 -487 -96 -106 O HETATM 1832 O HOH B 571 -2.420 19.334 14.090 1.00 32.17 O ANISOU 1832 O HOH B 571 2791 3447 5985 -673 -1320 -617 O HETATM 1833 O HOH B 572 18.414 10.500 25.086 1.00 28.06 O ANISOU 1833 O HOH B 572 3579 2524 4556 361 -1 195 O HETATM 1834 O HOH B 573 8.336 15.094 29.931 1.00 36.46 O ANISOU 1834 O HOH B 573 4152 3893 5806 1305 727 -424 O HETATM 1835 O HOH B 574 15.859 43.115 16.268 1.00 36.67 O ANISOU 1835 O HOH B 574 3175 5961 4797 -488 -463 319 O HETATM 1836 O HOH B 575 -3.998 33.357 26.145 1.00 40.72 O ANISOU 1836 O HOH B 575 4712 5064 5694 558 1119 -242 O HETATM 1837 O HOH B 576 -4.768 19.887 15.201 1.00 30.33 O ANISOU 1837 O HOH B 576 3418 4355 3748 -1190 55 17 O HETATM 1838 O HOH B 577 4.627 23.440 11.393 1.00 30.89 O ANISOU 1838 O HOH B 577 3224 4353 4157 -53 -1529 -177 O HETATM 1839 O HOH B 578 -0.745 18.321 12.691 1.00 43.86 O ANISOU 1839 O HOH B 578 5823 6338 4504 -962 69 -417 O HETATM 1840 O HOH B 579 13.539 38.539 23.395 1.00 38.02 O ANISOU 1840 O HOH B 579 5086 4717 4641 113 565 -575 O HETATM 1841 O HOH B 580 2.196 41.646 20.232 1.00 28.67 O ANISOU 1841 O HOH B 580 4634 3081 3176 589 400 41 O HETATM 1842 O HOH B 581 19.277 36.583 17.288 1.00 31.14 O ANISOU 1842 O HOH B 581 4561 3572 3696 -442 -499 662 O HETATM 1843 O HOH B 582 5.480 41.755 10.332 1.00 36.06 O ANISOU 1843 O HOH B 582 4819 4098 4782 729 61 1129 O HETATM 1844 O AHOH B 583 -6.758 25.612 15.632 0.50 35.22 O ANISOU 1844 O AHOH B 583 4940 4199 4242 18 -796 -158 O HETATM 1845 O BHOH B 583 43.882 26.857 16.886 0.50 27.44 O ANISOU 1845 O BHOH B 583 3203 3375 3848 -591 -426 159 O HETATM 1846 O HOH B 584 23.632 11.006 28.594 1.00 35.39 O ANISOU 1846 O HOH B 584 5406 3736 4303 819 206 -760 O HETATM 1847 O HOH B 585 3.731 27.861 6.408 1.00 31.19 O ANISOU 1847 O HOH B 585 3431 4043 4373 -396 557 -1371 O HETATM 1848 O HOH B 586 10.145 27.141 35.000 1.00 32.58 O ANISOU 1848 O HOH B 586 3978 5681 2716 910 929 -157 O HETATM 1849 O HOH B 587 16.466 38.778 20.376 1.00 39.28 O ANISOU 1849 O HOH B 587 5254 5308 4361 470 -842 1218 O HETATM 1850 O HOH B 588 24.244 18.394 35.194 1.00 36.68 O ANISOU 1850 O HOH B 588 5152 5584 3198 409 -939 839 O HETATM 1851 O HOH B 589 1.876 34.177 31.837 1.00 39.05 O ANISOU 1851 O HOH B 589 5691 4368 4779 41 929 -252 O HETATM 1852 O HOH B 590 14.237 15.403 20.359 1.00 31.39 O ANISOU 1852 O HOH B 590 3039 3737 5148 -10 -711 804 O HETATM 1853 O HOH B 591 -3.904 37.568 13.766 1.00 37.01 O ANISOU 1853 O HOH B 591 6016 4724 3320 -310 -459 878 O HETATM 1854 O HOH B 592 11.467 12.816 24.176 1.00 53.16 O ANISOU 1854 O HOH B 592 6875 6280 7043 -252 247 360 O HETATM 1855 O HOH B 593 30.886 18.101 33.805 1.00 41.22 O ANISOU 1855 O HOH B 593 4524 6591 4545 497 -979 578 O HETATM 1856 O HOH B 594 8.305 18.925 10.000 1.00 40.55 O ANISOU 1856 O HOH B 594 4855 6205 4347 -470 -606 -770 O HETATM 1857 O HOH B 595 0.608 42.091 23.682 1.00 41.95 O ANISOU 1857 O HOH B 595 6257 4317 5364 437 169 368 O HETATM 1858 O HOH B 596 -2.835 37.043 21.662 1.00 38.49 O ANISOU 1858 O HOH B 596 4161 5365 5097 466 108 -423 O HETATM 1859 O HOH B 597 31.877 14.104 28.088 1.00 42.77 O ANISOU 1859 O HOH B 597 5466 4601 6184 1003 -900 -522 O HETATM 1860 O HOH B 598 11.726 22.221 8.513 1.00 37.15 O ANISOU 1860 O HOH B 598 5349 5190 3574 -264 -521 -222 O HETATM 1861 O HOH B 599 4.009 38.970 8.409 1.00 36.03 O ANISOU 1861 O HOH B 599 4655 5122 3913 152 385 -237 O HETATM 1862 O HOH B 600 22.873 13.384 12.622 1.00 40.97 O ANISOU 1862 O HOH B 600 7104 5648 2814 267 -711 -1293 O HETATM 1863 O HOH B 601 8.981 14.232 17.795 1.00 44.16 O ANISOU 1863 O HOH B 601 6358 4024 6395 721 -239 188 O HETATM 1864 O HOH B 602 10.472 15.549 13.972 1.00 34.62 O ANISOU 1864 O HOH B 602 4601 4959 3593 -586 83 -961 O HETATM 1865 O HOH B 603 1.667 22.963 11.160 1.00 33.58 O ANISOU 1865 O HOH B 603 4330 4668 3760 933 -390 -212 O HETATM 1866 O HOH B 604 8.483 32.492 32.082 1.00 35.98 O ANISOU 1866 O HOH B 604 5920 3923 3828 388 1780 -142 O HETATM 1867 O HOH B 605 17.528 15.097 11.965 1.00 27.88 O ANISOU 1867 O HOH B 605 4305 3876 2410 -431 -914 -667 O HETATM 1868 O HOH B 606 13.150 44.978 20.881 1.00 40.24 O ANISOU 1868 O HOH B 606 5280 4683 5324 -1207 -21 432 O HETATM 1869 O HOH B 607 8.214 38.896 24.913 1.00 44.14 O ANISOU 1869 O HOH B 607 5501 4960 6309 -21 -653 -411 O HETATM 1870 O HOH B 608 16.031 27.056 32.040 1.00 19.14 O ANISOU 1870 O HOH B 608 2437 3120 1716 691 430 18 O HETATM 1871 O HOH B 609 10.056 30.638 32.854 1.00 28.43 O ANISOU 1871 O HOH B 609 3406 4263 3130 440 1140 -332 O HETATM 1872 O HOH B 610 18.547 11.703 22.884 1.00 31.79 O ANISOU 1872 O HOH B 610 5336 2397 4342 48 133 -196 O HETATM 1873 O HOH B 611 5.592 21.384 9.577 1.00 47.06 O ANISOU 1873 O HOH B 611 5970 6075 5836 -223 -577 -450 O HETATM 1874 O HOH B 612 -5.144 43.897 19.917 1.00 44.74 O ANISOU 1874 O HOH B 612 5254 5646 6099 46 -10 212 O HETATM 1875 O HOH B 613 19.313 8.939 32.071 1.00 41.91 O ANISOU 1875 O HOH B 613 4338 5731 5853 1452 1344 -168 O HETATM 1876 O HOH B 614 22.632 11.763 24.215 1.00 26.98 O ANISOU 1876 O HOH B 614 5643 2113 2492 -930 -1142 670 O HETATM 1877 O HOH B 615 11.544 12.328 9.955 1.00 41.90 O ANISOU 1877 O HOH B 615 6118 3938 5862 -108 66 -107 O HETATM 1878 O HOH B 616 12.874 8.983 11.202 1.00 38.70 O ANISOU 1878 O HOH B 616 5156 4108 5439 -178 170 -396 O HETATM 1879 O HOH B 617 -5.262 23.446 24.464 1.00 39.61 O ANISOU 1879 O HOH B 617 4794 5790 4463 -407 411 -806 O HETATM 1880 O HOH B 618 -3.348 30.127 18.634 1.00 25.99 O ANISOU 1880 O HOH B 618 2940 3436 3497 -304 50 185 O HETATM 1881 O HOH B 619 13.304 14.435 11.295 1.00 37.67 O ANISOU 1881 O HOH B 619 4783 4676 4851 501 -278 -1021 O HETATM 1882 O HOH B 620 9.200 22.233 8.943 1.00 39.37 O ANISOU 1882 O HOH B 620 5001 3369 6587 112 -93 -651 O HETATM 1883 O HOH B 621 -9.978 36.285 17.171 1.00 39.62 O ANISOU 1883 O HOH B 621 5501 3915 5638 -572 611 -111 O HETATM 1884 O HOH B 622 3.425 39.605 26.787 1.00 42.29 O ANISOU 1884 O HOH B 622 6190 3995 5881 265 -402 -1043 O HETATM 1885 O HOH B 623 6.931 43.326 23.857 1.00 46.08 O ANISOU 1885 O HOH B 623 6081 4712 6714 9 -226 -328 O HETATM 1886 O HOH B 624 19.394 23.793 7.557 1.00 36.05 O ANISOU 1886 O HOH B 624 5358 4321 4015 7 -1187 1434 O HETATM 1887 O HOH B 625 16.818 22.966 7.539 1.00 43.73 O ANISOU 1887 O HOH B 625 5706 5875 5034 129 -232 564 O HETATM 1888 O HOH B 626 1.926 16.063 21.899 1.00 49.70 O ANISOU 1888 O HOH B 626 6715 6529 5638 -328 256 -269 O HETATM 1889 O HOH B 627 13.147 40.781 5.590 1.00 37.44 O ANISOU 1889 O HOH B 627 4743 5073 4409 -1260 344 1079 O HETATM 1890 O HOH B 628 17.482 36.806 27.827 1.00 40.89 O ANISOU 1890 O HOH B 628 8112 3503 3921 1512 -323 -1429 O HETATM 1891 O HOH B 629 7.528 15.609 22.388 1.00 27.69 O ANISOU 1891 O HOH B 629 3750 2732 4036 -102 1098 502 O CONECT 1568 1569 1570 1571 1572 CONECT 1569 1568 CONECT 1570 1568 CONECT 1571 1568 CONECT 1572 1568 CONECT 1573 1574 1575 1576 1577 CONECT 1574 1573 CONECT 1575 1573 CONECT 1576 1573 CONECT 1577 1573 CONECT 1578 1579 1580 1581 1582 CONECT 1579 1578 CONECT 1580 1578 CONECT 1581 1578 CONECT 1582 1578 CONECT 1583 1584 CONECT 1584 1583 1585 1589 CONECT 1585 1584 1586 CONECT 1586 1585 1587 CONECT 1587 1586 1588 1590 CONECT 1588 1587 1589 CONECT 1589 1584 1588 CONECT 1590 1587 1591 1592 1593 CONECT 1591 1590 CONECT 1592 1590 CONECT 1593 1590 1594 1598 CONECT 1594 1593 1595 CONECT 1595 1594 1596 1597 CONECT 1596 1595 CONECT 1597 1595 CONECT 1598 1593 1599 CONECT 1599 1598 1600 1601 CONECT 1600 1599 CONECT 1601 1599 1602 1614 CONECT 1602 1601 1603 CONECT 1603 1602 1604 1605 CONECT 1604 1603 CONECT 1605 1603 1606 CONECT 1606 1605 1607 1613 CONECT 1607 1606 1608 CONECT 1608 1607 1609 CONECT 1609 1608 1610 1613 CONECT 1610 1609 1611 CONECT 1611 1610 1612 CONECT 1612 1611 1613 CONECT 1613 1606 1609 1612 CONECT 1614 1601 1620 CONECT 1615 1616 1620 CONECT 1616 1615 1617 CONECT 1617 1616 1618 CONECT 1618 1617 1619 CONECT 1619 1618 1620 CONECT 1620 1614 1615 1619 CONECT 1621 1622 1623 1624 1625 CONECT 1622 1621 CONECT 1623 1621 CONECT 1624 1621 CONECT 1625 1621 CONECT 1626 1627 1628 1629 1630 CONECT 1627 1626 CONECT 1628 1626 CONECT 1629 1626 CONECT 1630 1626 MASTER 355 0 6 2 20 0 15 6 1818 2 63 16 END If you find results from this site helpful for your research, please cite one of our papers:
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