Browse entries in the PDBbind-CN Database
HEADER APOPTOSIS 31-AUG-10 2XPX TITLE CRYSTAL STRUCTURE OF BHRF1:BAK BH3 COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: APOPTOSIS REGULATOR BHRF1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: BCL-2, RESIDUES 1-160; COMPND 5 SYNONYM: BHRF1, EARLY ANTIGEN PROTEIN R, EA-R, NUCLEAR ANTIGEN; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: BCL-2 HOMOLOGOUS ANTAGONIST/KILLER; COMPND 9 CHAIN: B; COMPND 10 FRAGMENT: RESIDUES 67-92; COMPND 11 SYNONYM: BAK, APOPTOSIS REGULATOR BAK, BCL-2-LIKE PROTEIN 7, COMPND 12 BCL2-L-7; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN HERPESVIRUS 4; SOURCE 3 ORGANISM_TAXID: 10376; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_VARIANT: PLYZS; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PDUET; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 17 EXPRESSION_SYSTEM_VARIANT: PLYZS; SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PDUET KEYWDS APOPTOSIS, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR M.KVANSAKUL,D.C.S.HUANG,P.M.COLMAN REVDAT 2 28-DEC-11 2XPX 1 JRNL REMARK VERSN REVDAT 1 26-JAN-11 2XPX 0 JRNL AUTH M.KVANSAKUL,A.H.WEI,J.I.FLETCHER,S.N.WILLIS,L.CHEN, JRNL AUTH 2 A.W.ROBERTS,D.C.S.HUANG,P.M.COLMAN JRNL TITL STRUCTURAL BASIS FOR APOPTOSIS INHIBITION BY EPSTEIN-BARR JRNL TITL 2 VIRUS BHRF1. JRNL REF PLOS PATHOG. V. 6 1236 2010 JRNL REFN ISSN 1553-7366 JRNL PMID 21203485 JRNL DOI 10.1371/JOURNAL.PPAT.1001236 REMARK 2 REMARK 2 RESOLUTION. 2.05 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0109 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.95 REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE REMARK 3 COMPLETENESS FOR RANGE (%) : 99.56 REMARK 3 NUMBER OF REFLECTIONS : 12943 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) : 0.18505 REMARK 3 R VALUE (WORKING SET) : 0.18352 REMARK 3 FREE R VALUE : 0.21696 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.9 REMARK 3 FREE R VALUE TEST SET COUNT : 668 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.053 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.106 REMARK 3 REFLECTION IN BIN (WORKING SET) : 889 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.41 REMARK 3 BIN R VALUE (WORKING SET) : 0.248 REMARK 3 BIN FREE R VALUE SET COUNT : 56 REMARK 3 BIN FREE R VALUE : 0.332 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1437 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 24 REMARK 3 SOLVENT ATOMS : 73 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.774 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.00 REMARK 3 B22 (A**2) : 0.00 REMARK 3 B33 (A**2) : 0.00 REMARK 3 B12 (A**2) : 0.00 REMARK 3 B13 (A**2) : 0.00 REMARK 3 B23 (A**2) : 0.00 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.179 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.155 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.102 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.364 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1457 ; 0.021 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1972 ; 1.843 ; 1.941 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 179 ; 7.646 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 68 ;33.010 ;22.206 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 236 ;17.682 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;19.759 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 223 ; 0.138 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1098 ; 0.011 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 891 ; 1.138 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1417 ; 1.948 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 566 ; 3.074 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 552 ; 4.548 ; 4.500 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL 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 : 3 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 3 A 157 REMARK 3 ORIGIN FOR THE GROUP (A): -31.4998 10.6644 -20.8262 REMARK 3 T TENSOR REMARK 3 T11: 0.1751 T22: 0.1840 REMARK 3 T33: 0.1773 T12: 0.0190 REMARK 3 T13: 0.0016 T23: -0.0245 REMARK 3 L TENSOR REMARK 3 L11: 1.3537 L22: 2.2797 REMARK 3 L33: 2.6404 L12: -0.2667 REMARK 3 L13: 0.0206 L23: 0.8398 REMARK 3 S TENSOR REMARK 3 S11: -0.0089 S12: 0.0209 S13: 0.0096 REMARK 3 S21: 0.0427 S22: 0.1326 S23: -0.1468 REMARK 3 S31: -0.1170 S32: 0.1694 S33: -0.1237 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 69 B 91 REMARK 3 ORIGIN FOR THE GROUP (A): -32.9072 26.1778 -22.1560 REMARK 3 T TENSOR REMARK 3 T11: 0.4049 T22: 0.0183 REMARK 3 T33: 0.2372 T12: 0.0023 REMARK 3 T13: 0.0653 T23: 0.0286 REMARK 3 L TENSOR REMARK 3 L11: 14.9108 L22: 8.3738 REMARK 3 L33: 25.0160 L12: 4.9471 REMARK 3 L13: 17.6067 L23: 7.6261 REMARK 3 S TENSOR REMARK 3 S11: -0.9382 S12: 0.2801 S13: 1.3377 REMARK 3 S21: -1.0029 S22: -0.0777 S23: -0.0629 REMARK 3 S31: -1.5368 S32: 0.2840 S33: 1.0159 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 3 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 1158 A 1163 REMARK 3 RESIDUE RANGE : A 2001 A 2065 REMARK 3 RESIDUE RANGE : B 2001 B 2008 REMARK 3 ORIGIN FOR THE GROUP (A): -32.4956 10.3165 -19.9510 REMARK 3 T TENSOR REMARK 3 T11: 0.4116 T22: 0.4376 REMARK 3 T33: 0.4279 T12: 0.0418 REMARK 3 T13: 0.0346 T23: -0.0224 REMARK 3 L TENSOR REMARK 3 L11: 2.0152 L22: 2.2506 REMARK 3 L33: 2.4111 L12: 0.6379 REMARK 3 L13: 0.3609 L23: 0.5560 REMARK 3 S TENSOR REMARK 3 S11: -0.0872 S12: -0.0872 S13: -0.0405 REMARK 3 S21: 0.1007 S22: 0.1273 S23: -0.0991 REMARK 3 S31: -0.0666 S32: 0.1512 S33: -0.0400 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : 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. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B REMARK 3 FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. REMARK 4 REMARK 4 2XPX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-AUG-10. REMARK 100 THE PDBE ID CODE IS EBI-45224. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.4 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X06SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12945 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.05 REMARK 200 RESOLUTION RANGE LOW (A) : 50.00 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : 10 REMARK 200 R MERGE (I) : 0.06 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 33.90 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12 REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8 REMARK 200 DATA REDUNDANCY IN SHELL : 5.1 REMARK 200 R MERGE FOR SHELL (I) : 0.50 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.20 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 2V6Q REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M NANO3, 50 MM MALIC ACID REMARK 280 PH 4.4 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+1/3 REMARK 290 6555 -X,-X+Y,-Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 62.48600 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 31.24300 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 31.24300 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 62.48600 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: 2910 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 8660 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.9 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A -12 REMARK 465 GLY A -11 REMARK 465 SER A -10 REMARK 465 HIS A -9 REMARK 465 HIS A -8 REMARK 465 HIS A -7 REMARK 465 HIS A -6 REMARK 465 HIS A -5 REMARK 465 HIS A -4 REMARK 465 SER A -3 REMARK 465 GLN A -2 REMARK 465 ASP A -1 REMARK 465 PRO A 0 REMARK 465 MET A 1 REMARK 465 ALA A 2 REMARK 465 GLY A 94 REMARK 465 ASP A 95 REMARK 465 ILE A 158 REMARK 465 PRO A 159 REMARK 465 GLY A 160 REMARK 465 PRO B 67 REMARK 465 SER B 68 REMARK 465 GLU B 92 REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 TYR A 3 CB CG CD1 CD2 CE1 CE2 CZ OH REMARK 480 ARG A 39 CG CD NE CZ NH1 NH2 REMARK 480 GLU A 43 OE2 REMARK 480 ASN A 70 OD1 REMARK 480 GLU A 77 OE1 OE2 REMARK 480 GLN A 119 CG CD OE1 NE2 REMARK 480 GLN A 146 CG CD OE1 NE2 REMARK 480 ASN A 157 CG OD1 ND2 REMARK 480 GLN B 73 OE1 NE2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 NE ARG A 39 O HOH A 2020 1.06 REMARK 500 CD1 TYR A 3 O HOH A 2002 1.22 REMARK 500 CG TYR A 3 O HOH A 2002 1.50 REMARK 500 CD ARG A 39 O HOH A 2020 1.59 REMARK 500 CG ARG A 39 O HOH A 2020 1.83 REMARK 500 CB TYR A 3 O HOH A 2002 1.86 REMARK 500 NE2 GLN B 77 O HOH B 2004 1.92 REMARK 500 O HOH A 2008 O HOH A 2054 1.95 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 TYR A 3 CA TYR A 3 CB 0.207 REMARK 500 ARG A 39 CB ARG A 39 CG -0.168 REMARK 500 GLU A 77 CD GLU A 77 OE1 -0.397 REMARK 500 GLU A 77 CD GLU A 77 OE2 0.219 REMARK 500 ASN A 84 CB ASN A 84 CG 0.149 REMARK 500 GLN A 119 CB GLN A 119 CG -0.369 REMARK 500 GLN A 146 CB GLN A 146 CG -0.217 REMARK 500 ASN A 157 CB ASN A 157 CG -0.138 REMARK 500 GLN B 73 CD GLN B 73 OE1 0.291 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 TYR A 3 N - CA - CB ANGL. DEV. = -21.3 DEGREES REMARK 500 PRO A 37 C - N - CA ANGL. DEV. = 20.0 DEGREES REMARK 500 PRO A 37 C - N - CD ANGL. DEV. = -27.0 DEGREES REMARK 500 GLU A 77 OE1 - CD - OE2 ANGL. DEV. = 22.9 DEGREES REMARK 500 GLU A 77 CG - CD - OE2 ANGL. DEV. = -14.2 DEGREES REMARK 500 GLN A 119 CA - CB - CG ANGL. DEV. = 16.9 DEGREES REMARK 500 ARG A 131 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 GLN A 146 CA - CB - CG ANGL. DEV. = 18.3 DEGREES REMARK 500 GLN B 73 CG - CD - OE1 ANGL. DEV. = -15.9 DEGREES REMARK 500 GLN B 73 CG - CD - NE2 ANGL. DEV. = 15.5 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 PRO A 37 83.36 34.91 REMARK 500 HIS A 78 83.66 -155.86 REMARK 500 HIS A 92 -73.16 19.06 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 THR A 36 PRO A 37 -123.60 REMARK 500 GLU A 155 ASP A 156 -146.27 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 GLU A 43 0.11 SIDE CHAIN REMARK 500 GLN B 73 0.12 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 TYR A 3 45.6 L L OUTSIDE RANGE REMARK 500 VAL A 86 24.2 L L OUTSIDE RANGE 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 NO3 A1158 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A1159 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A1160 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A1161 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1162 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1163 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1BXL RELATED DB: PDB REMARK 900 STRUCTURE OF BCL-XL/BAK PEPTIDE COMPLEX, REMARK 900 NMR, MINIMIZED AVERAGE STRUCTURE REMARK 900 RELATED ID: 2JCN RELATED DB: PDB REMARK 900 THE CRYSTAL STRUCTURE OF BAK1 - A REMARK 900 MITOCHONDRIAL APOPTOSIS REGULATOR REMARK 900 RELATED ID: 2JBY RELATED DB: PDB REMARK 900 A VIRAL PROTEIN UNEXPECTEDLY MIMICS THE REMARK 900 STRUCTURE AND FUNCTION OF PRO-SURVIVAL BCL-2 REMARK 900 RELATED ID: 1Q59 RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF THE BHRF1 PROTEIN FROM REMARK 900 EPSTEIN-BARRVIRUS, A HOMOLOG OF HUMAN BCL-2 DBREF 2XPX A 1 160 UNP P03182 EAR_EBVB9 1 160 DBREF 2XPX B 67 92 UNP Q16611 BAK_HUMAN 67 92 SEQADV 2XPX MET A -12 UNP P03182 EXPRESSION TAG SEQADV 2XPX GLY A -11 UNP P03182 EXPRESSION TAG SEQADV 2XPX SER A -10 UNP P03182 EXPRESSION TAG SEQADV 2XPX HIS A -9 UNP P03182 EXPRESSION TAG SEQADV 2XPX HIS A -8 UNP P03182 EXPRESSION TAG SEQADV 2XPX HIS A -7 UNP P03182 EXPRESSION TAG SEQADV 2XPX HIS A -6 UNP P03182 EXPRESSION TAG SEQADV 2XPX HIS A -5 UNP P03182 EXPRESSION TAG SEQADV 2XPX HIS A -4 UNP P03182 EXPRESSION TAG SEQADV 2XPX SER A -3 UNP P03182 EXPRESSION TAG SEQADV 2XPX GLN A -2 UNP P03182 EXPRESSION TAG SEQADV 2XPX ASP A -1 UNP P03182 EXPRESSION TAG SEQADV 2XPX PRO A 0 UNP P03182 EXPRESSION TAG SEQRES 1 A 173 MET GLY SER HIS HIS HIS HIS HIS HIS SER GLN ASP PRO SEQRES 2 A 173 MET ALA TYR SER THR ARG GLU ILE LEU LEU ALA LEU CYS SEQRES 3 A 173 ILE ARG ASP SER ARG VAL HIS GLY ASN GLY THR LEU HIS SEQRES 4 A 173 PRO VAL LEU GLU LEU ALA ALA ARG GLU THR PRO LEU ARG SEQRES 5 A 173 LEU SER PRO GLU ASP THR VAL VAL LEU ARG TYR HIS VAL SEQRES 6 A 173 LEU LEU GLU GLU ILE ILE GLU ARG ASN SER GLU THR PHE SEQRES 7 A 173 THR GLU THR TRP ASN ARG PHE ILE THR HIS THR GLU HIS SEQRES 8 A 173 VAL ASP LEU ASP PHE ASN SER VAL PHE LEU GLU ILE PHE SEQRES 9 A 173 HIS ARG GLY ASP PRO SER LEU GLY ARG ALA LEU ALA TRP SEQRES 10 A 173 MET ALA TRP CYS MET HIS ALA CYS ARG THR LEU CYS CYS SEQRES 11 A 173 ASN GLN SER THR PRO TYR TYR VAL VAL ASP LEU SER VAL SEQRES 12 A 173 ARG GLY MET LEU GLU ALA SER GLU GLY LEU ASP GLY TRP SEQRES 13 A 173 ILE HIS GLN GLN GLY GLY TRP SER THR LEU ILE GLU ASP SEQRES 14 A 173 ASN ILE PRO GLY SEQRES 1 B 26 PRO SER SER THR MET GLY GLN VAL GLY ARG GLN LEU ALA SEQRES 2 B 26 ILE ILE GLY ASP ASP ILE ASN ARG ARG TYR ASP SER GLU HET NO3 A1158 4 HET NO3 A1159 4 HET NO3 A1160 4 HET NO3 A1161 4 HET EDO A1162 4 HET EDO A1163 4 HETNAM NO3 NITRATE ION HETNAM EDO 1,2-ETHANEDIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 3 NO3 4(N O3 1-) FORMUL 4 EDO 2(C2 H6 O2) FORMUL 5 HOH *73(H2 O) HELIX 1 1 SER A 4 GLY A 21 1 18 HELIX 2 2 HIS A 26 THR A 36 1 11 HELIX 3 3 ASP A 44 ASN A 61 1 18 HELIX 4 4 ASN A 61 THR A 76 1 16 HELIX 5 5 HIS A 78 HIS A 92 1 15 HELIX 6 6 SER A 97 ASN A 118 1 22 HELIX 7 7 PRO A 122 GLU A 138 1 17 HELIX 8 8 LEU A 140 GLN A 147 1 8 HELIX 9 9 GLY A 149 ASP A 156 1 8 HELIX 10 10 SER B 69 ASP B 90 1 22 SITE 1 AC1 8 SER A 17 ARG A 18 GLY A 21 ASN A 22 SITE 2 AC1 8 GLY A 23 THR A 24 LEU A 25 HOH A2065 SITE 1 AC2 5 ILE A 57 ARG A 60 ASN A 61 ILE B 85 SITE 2 AC2 5 ARG B 88 SITE 1 AC3 5 ARG A 15 ARG A 18 PRO A 42 GLU A 43 SITE 2 AC3 5 GLU A 67 SITE 1 AC4 5 ASP A 16 SER A 17 GLY A 21 ARG A 113 SITE 2 AC4 5 CYS A 117 SITE 1 AC5 4 HIS A 26 HIS A 78 THR A 121 TYR A 123 SITE 1 AC6 5 GLU A 77 HIS A 78 VAL A 79 TYR A 123 SITE 2 AC6 5 TYR A 124 CRYST1 62.387 62.387 93.729 90.00 90.00 120.00 P 32 2 1 6 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 0.016029 0.009254 0.000000 0.00000 SCALE2 0.000000 0.018509 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010669 0.00000 ATOM 1 N TYR A 3 -15.945 6.841 -20.180 1.00 55.95 N ANISOU 1 N TYR A 3 5277 8242 7741 506 -414 -1577 N ATOM 2 CA TYR A 3 -17.416 6.625 -20.399 1.00 52.72 C ANISOU 2 CA TYR A 3 5133 7664 7233 505 -368 -1399 C ATOM 3 C TYR A 3 -17.905 7.545 -21.543 1.00 51.03 C ANISOU 3 C TYR A 3 4967 7423 6998 304 -173 -1340 C ATOM 4 O TYR A 3 -17.648 8.771 -21.528 1.00 51.64 O ANISOU 4 O TYR A 3 5002 7524 7094 132 -108 -1360 O ATOM 5 CB TYR A 3 -17.736 7.402 -18.873 0.00 54.59 C ANISOU 5 CB TYR A 3 5464 7849 7427 486 -499 -1359 C ATOM 6 CG TYR A 3 -17.480 6.423 -17.749 0.00 55.27 C ANISOU 6 CG TYR A 3 5574 7934 7493 701 -695 -1381 C ATOM 7 CD1 TYR A 3 -16.394 6.582 -16.898 0.00 57.03 C ANISOU 7 CD1 TYR A 3 5639 8269 7759 759 -837 -1512 C ATOM 8 CD2 TYR A 3 -18.324 5.341 -17.541 0.00 54.38 C ANISOU 8 CD2 TYR A 3 5648 7703 7312 842 -741 -1271 C ATOM 9 CE1 TYR A 3 -16.156 5.690 -15.870 0.00 57.87 C ANISOU 9 CE1 TYR A 3 5790 8369 7828 973 -1030 -1525 C ATOM 10 CE2 TYR A 3 -18.094 4.443 -16.515 0.00 55.23 C ANISOU 10 CE2 TYR A 3 5812 7789 7384 1039 -914 -1276 C ATOM 11 CZ TYR A 3 -17.010 4.623 -15.683 0.00 56.97 C ANISOU 11 CZ TYR A 3 5890 8121 7634 1114 -1063 -1399 C ATOM 12 OH TYR A 3 -16.775 3.732 -14.661 0.00 58.02 O ANISOU 12 OH TYR A 3 6102 8228 7715 1328 -1250 -1398 O ATOM 13 N SER A 4 -18.622 6.962 -22.509 1.00 46.85 N ANISOU 13 N SER A 4 4544 6833 6422 326 -88 -1267 N ATOM 14 CA SER A 4 -19.324 7.725 -23.532 1.00 43.30 C ANISOU 14 CA SER A 4 4197 6333 5921 171 66 -1183 C ATOM 15 C SER A 4 -20.612 8.360 -22.935 1.00 41.01 C ANISOU 15 C SER A 4 4110 5909 5563 131 34 -1043 C ATOM 16 O SER A 4 -21.054 7.975 -21.842 1.00 39.62 O ANISOU 16 O SER A 4 4007 5677 5370 231 -91 -1004 O ATOM 17 CB SER A 4 -19.681 6.794 -24.674 1.00 42.97 C ANISOU 17 CB SER A 4 4204 6279 5845 233 135 -1166 C ATOM 18 OG SER A 4 -20.732 5.874 -24.331 1.00 41.09 O ANISOU 18 OG SER A 4 4124 5927 5562 355 45 -1077 O ATOM 19 N THR A 5 -21.176 9.344 -23.628 1.00 39.34 N ANISOU 19 N THR A 5 3990 5649 5308 -9 147 -972 N ATOM 20 CA THR A 5 -22.446 9.937 -23.244 1.00 39.60 C ANISOU 20 CA THR A 5 4205 5563 5279 -31 130 -848 C ATOM 21 C THR A 5 -23.585 8.871 -23.151 1.00 38.03 C ANISOU 21 C THR A 5 4123 5292 5036 96 69 -765 C ATOM 22 O THR A 5 -24.422 8.855 -22.215 1.00 37.10 O ANISOU 22 O THR A 5 4104 5101 4891 144 -4 -697 O ATOM 23 CB THR A 5 -22.857 11.055 -24.218 1.00 40.09 C ANISOU 23 CB THR A 5 4358 5581 5295 -175 260 -786 C ATOM 24 OG1 THR A 5 -21.756 11.967 -24.399 1.00 42.11 O ANISOU 24 OG1 THR A 5 4509 5895 5595 -317 339 -865 O ATOM 25 CG2 THR A 5 -24.029 11.790 -23.655 1.00 36.79 C ANISOU 25 CG2 THR A 5 4100 5050 4829 -181 226 -682 C ATOM 26 N ARG A 6 -23.594 7.975 -24.104 1.00 38.05 N ANISOU 26 N ARG A 6 4113 5315 5031 141 105 -779 N ATOM 27 CA ARG A 6 -24.621 6.954 -24.115 1.00 39.06 C ANISOU 27 CA ARG A 6 4345 5370 5128 235 56 -715 C ATOM 28 C ARG A 6 -24.519 6.145 -22.793 1.00 38.34 C ANISOU 28 C ARG A 6 4256 5250 5061 355 -70 -723 C ATOM 29 O ARG A 6 -25.536 5.938 -22.137 1.00 36.64 O ANISOU 29 O ARG A 6 4155 4953 4813 384 -114 -639 O ATOM 30 CB ARG A 6 -24.469 6.101 -25.401 1.00 38.59 C ANISOU 30 CB ARG A 6 4265 5339 5057 262 112 -757 C ATOM 31 CG ARG A 6 -25.141 4.781 -25.366 1.00 43.21 C ANISOU 31 CG ARG A 6 4923 5858 5637 367 48 -736 C ATOM 32 CD ARG A 6 -24.583 3.919 -26.505 1.00 52.33 C ANISOU 32 CD ARG A 6 6030 7059 6794 411 94 -821 C ATOM 33 NE ARG A 6 -25.520 3.919 -27.604 1.00 63.08 N ANISOU 33 NE ARG A 6 7488 8388 8090 361 148 -775 N ATOM 34 CZ ARG A 6 -25.530 3.022 -28.609 1.00 71.70 C ANISOU 34 CZ ARG A 6 8600 9483 9159 403 172 -828 C ATOM 35 NH1 ARG A 6 -24.620 2.018 -28.689 1.00 67.67 N ANISOU 35 NH1 ARG A 6 8019 9002 8692 505 157 -932 N ATOM 36 NH2 ARG A 6 -26.479 3.143 -29.555 1.00 74.50 N ANISOU 36 NH2 ARG A 6 9052 9813 9442 352 202 -784 N ATOM 37 N GLU A 7 -23.298 5.759 -22.388 1.00 39.45 N ANISOU 37 N GLU A 7 4273 5464 5253 422 -125 -823 N ATOM 38 CA GLU A 7 -23.098 5.025 -21.117 1.00 40.34 C ANISOU 38 CA GLU A 7 4406 5549 5371 553 -260 -829 C ATOM 39 C GLU A 7 -23.542 5.815 -19.890 1.00 39.30 C ANISOU 39 C GLU A 7 4350 5380 5203 524 -313 -772 C ATOM 40 O GLU A 7 -24.121 5.235 -18.970 1.00 38.19 O ANISOU 40 O GLU A 7 4323 5166 5021 605 -387 -709 O ATOM 41 CB GLU A 7 -21.648 4.581 -20.914 1.00 42.31 C ANISOU 41 CB GLU A 7 4493 5900 5683 646 -327 -961 C ATOM 42 CG GLU A 7 -21.297 3.219 -21.595 1.00 47.14 C ANISOU 42 CG GLU A 7 5078 6512 6321 775 -337 -1016 C ATOM 43 CD GLU A 7 -19.810 2.889 -21.466 1.00 54.43 C ANISOU 43 CD GLU A 7 5807 7558 7316 878 -399 -1165 C ATOM 44 OE1 GLU A 7 -18.954 3.819 -21.553 1.00 58.92 O ANISOU 44 OE1 GLU A 7 6208 8249 7932 786 -359 -1251 O ATOM 45 OE2 GLU A 7 -19.486 1.690 -21.243 1.00 63.36 O ANISOU 45 OE2 GLU A 7 6953 8660 8462 1054 -492 -1202 O ATOM 46 N ILE A 8 -23.196 7.106 -19.838 1.00 37.18 N ANISOU 46 N ILE A 8 4023 5157 4946 409 -273 -802 N ATOM 47 CA ILE A 8 -23.531 7.866 -18.660 1.00 38.17 C ANISOU 47 CA ILE A 8 4221 5249 5034 390 -327 -768 C ATOM 48 C ILE A 8 -25.058 8.118 -18.620 1.00 34.59 C ANISOU 48 C ILE A 8 3931 4694 4519 360 -276 -642 C ATOM 49 O ILE A 8 -25.676 8.000 -17.571 1.00 34.13 O ANISOU 49 O ILE A 8 3974 4584 4411 412 -329 -588 O ATOM 50 CB ILE A 8 -22.687 9.159 -18.436 1.00 39.83 C ANISOU 50 CB ILE A 8 4333 5521 5278 279 -318 -851 C ATOM 51 CG1 ILE A 8 -23.105 9.825 -17.099 1.00 43.60 C ANISOU 51 CG1 ILE A 8 4912 5951 5703 283 -392 -823 C ATOM 52 CG2 ILE A 8 -22.941 10.223 -19.492 1.00 41.50 C ANISOU 52 CG2 ILE A 8 4555 5717 5499 122 -179 -826 C ATOM 53 CD1 ILE A 8 -21.897 10.279 -16.270 1.00 50.69 C ANISOU 53 CD1 ILE A 8 5694 6933 6635 276 -492 -948 C ATOM 54 N LEU A 9 -25.654 8.414 -19.769 1.00 33.39 N ANISOU 54 N LEU A 9 3800 4521 4366 286 -175 -600 N ATOM 55 CA LEU A 9 -27.089 8.601 -19.813 1.00 31.37 C ANISOU 55 CA LEU A 9 3668 4188 4064 271 -137 -497 C ATOM 56 C LEU A 9 -27.810 7.321 -19.382 1.00 29.84 C ANISOU 56 C LEU A 9 3543 3943 3850 363 -181 -445 C ATOM 57 O LEU A 9 -28.770 7.373 -18.599 1.00 29.24 O ANISOU 57 O LEU A 9 3559 3815 3734 378 -187 -377 O ATOM 58 CB LEU A 9 -27.615 9.083 -21.188 1.00 29.53 C ANISOU 58 CB LEU A 9 3451 3946 3824 194 -42 -464 C ATOM 59 CG LEU A 9 -29.126 9.380 -21.218 1.00 28.61 C ANISOU 59 CG LEU A 9 3440 3764 3666 192 -19 -371 C ATOM 60 CD1 LEU A 9 -29.539 10.429 -20.098 1.00 27.75 C ANISOU 60 CD1 LEU A 9 3392 3619 3534 183 -33 -345 C ATOM 61 CD2 LEU A 9 -29.645 9.828 -22.586 1.00 27.84 C ANISOU 61 CD2 LEU A 9 3368 3661 3547 140 48 -340 C ATOM 62 N LEU A 10 -27.392 6.197 -19.924 1.00 30.01 N ANISOU 62 N LEU A 10 3529 3975 3899 418 -198 -477 N ATOM 63 CA LEU A 10 -28.053 4.928 -19.588 1.00 30.99 C ANISOU 63 CA LEU A 10 3739 4028 4009 491 -233 -428 C ATOM 64 C LEU A 10 -27.842 4.656 -18.098 1.00 30.85 C ANISOU 64 C LEU A 10 3782 3983 3956 568 -316 -411 C ATOM 65 O LEU A 10 -28.791 4.311 -17.401 1.00 30.31 O ANISOU 65 O LEU A 10 3826 3847 3845 577 -313 -333 O ATOM 66 CB LEU A 10 -27.535 3.755 -20.466 1.00 31.39 C ANISOU 66 CB LEU A 10 3753 4079 4095 546 -242 -481 C ATOM 67 CG LEU A 10 -28.040 2.328 -20.099 1.00 32.48 C ANISOU 67 CG LEU A 10 3996 4118 4226 622 -286 -441 C ATOM 68 CD1 LEU A 10 -29.602 2.234 -20.059 1.00 28.73 C ANISOU 68 CD1 LEU A 10 3619 3570 3726 552 -237 -347 C ATOM 69 CD2 LEU A 10 -27.505 1.362 -21.106 1.00 33.68 C ANISOU 69 CD2 LEU A 10 4112 4269 4416 673 -288 -510 C ATOM 70 N ALA A 11 -26.627 4.864 -17.571 1.00 32.00 N ANISOU 70 N ALA A 11 3856 4190 4114 618 -389 -487 N ATOM 71 CA ALA A 11 -26.423 4.638 -16.112 1.00 33.01 C ANISOU 71 CA ALA A 11 4060 4295 4185 704 -487 -472 C ATOM 72 C ALA A 11 -27.305 5.547 -15.231 1.00 32.41 C ANISOU 72 C ALA A 11 4078 4193 4044 650 -457 -408 C ATOM 73 O ALA A 11 -27.802 5.120 -14.196 1.00 32.00 O ANISOU 73 O ALA A 11 4152 4087 3921 703 -487 -346 O ATOM 74 CB ALA A 11 -24.930 4.744 -15.689 1.00 32.57 C ANISOU 74 CB ALA A 11 3891 4327 4155 776 -595 -584 C ATOM 75 N LEU A 12 -27.522 6.801 -15.678 1.00 32.30 N ANISOU 75 N LEU A 12 4014 4209 4048 546 -389 -422 N ATOM 76 CA LEU A 12 -28.367 7.778 -14.959 1.00 31.35 C ANISOU 76 CA LEU A 12 3975 4063 3873 503 -353 -376 C ATOM 77 C LEU A 12 -29.809 7.327 -14.978 1.00 30.26 C ANISOU 77 C LEU A 12 3930 3861 3706 496 -281 -278 C ATOM 78 O LEU A 12 -30.523 7.443 -13.967 1.00 29.05 O ANISOU 78 O LEU A 12 3874 3677 3485 514 -269 -229 O ATOM 79 CB LEU A 12 -28.263 9.147 -15.668 1.00 31.26 C ANISOU 79 CB LEU A 12 3900 4077 3899 399 -293 -412 C ATOM 80 CG LEU A 12 -27.008 9.912 -15.264 1.00 35.00 C ANISOU 80 CG LEU A 12 4298 4606 4392 374 -354 -513 C ATOM 81 CD1 LEU A 12 -26.779 11.023 -16.268 1.00 37.54 C ANISOU 81 CD1 LEU A 12 4561 4938 4764 254 -275 -544 C ATOM 82 CD2 LEU A 12 -27.056 10.434 -13.781 1.00 30.72 C ANISOU 82 CD2 LEU A 12 3841 4052 3777 409 -421 -526 C ATOM 83 N CYS A 13 -30.276 6.857 -16.140 1.00 28.48 N ANISOU 83 N CYS A 13 3668 3623 3528 462 -228 -257 N ATOM 84 CA CYS A 13 -31.632 6.301 -16.235 1.00 28.18 C ANISOU 84 CA CYS A 13 3692 3535 3480 445 -167 -180 C ATOM 85 C CYS A 13 -31.817 5.061 -15.351 1.00 28.74 C ANISOU 85 C CYS A 13 3862 3546 3511 501 -195 -133 C ATOM 86 O CYS A 13 -32.853 4.920 -14.734 1.00 29.23 O ANISOU 86 O CYS A 13 3998 3573 3534 482 -142 -69 O ATOM 87 CB CYS A 13 -32.007 5.969 -17.709 1.00 28.27 C ANISOU 87 CB CYS A 13 3645 3550 3548 400 -127 -184 C ATOM 88 SG CYS A 13 -32.172 7.487 -18.793 1.00 28.59 S ANISOU 88 SG CYS A 13 3623 3635 3605 330 -75 -203 S ATOM 89 N ILE A 14 -30.849 4.146 -15.354 1.00 30.20 N ANISOU 89 N ILE A 14 4050 3717 3707 570 -269 -164 N ATOM 90 CA ILE A 14 -30.921 2.986 -14.473 1.00 31.86 C ANISOU 90 CA ILE A 14 4389 3849 3868 637 -306 -113 C ATOM 91 C ILE A 14 -30.972 3.419 -13.015 1.00 31.94 C ANISOU 91 C ILE A 14 4498 3858 3779 674 -329 -79 C ATOM 92 O ILE A 14 -31.838 2.985 -12.267 1.00 33.41 O ANISOU 92 O ILE A 14 4808 3985 3902 662 -278 1 O ATOM 93 CB ILE A 14 -29.775 1.985 -14.737 1.00 32.14 C ANISOU 93 CB ILE A 14 4414 3866 3933 736 -400 -163 C ATOM 94 CG1 ILE A 14 -29.999 1.350 -16.121 1.00 32.33 C ANISOU 94 CG1 ILE A 14 4382 3869 4035 697 -357 -186 C ATOM 95 CG2 ILE A 14 -29.712 0.885 -13.599 1.00 32.87 C ANISOU 95 CG2 ILE A 14 4680 3860 3948 833 -461 -101 C ATOM 96 CD1 ILE A 14 -28.665 0.895 -16.789 1.00 29.88 C ANISOU 96 CD1 ILE A 14 3982 3595 3777 783 -429 -283 C ATOM 97 N ARG A 15 -30.038 4.248 -12.605 1.00 32.60 N ANISOU 97 N ARG A 15 4531 4010 3845 711 -401 -146 N ATOM 98 CA ARG A 15 -30.023 4.772 -11.256 1.00 35.20 C ANISOU 98 CA ARG A 15 4954 4348 4070 747 -435 -134 C ATOM 99 C ARG A 15 -31.343 5.447 -10.850 1.00 36.06 C ANISOU 99 C ARG A 15 5122 4446 4134 676 -318 -75 C ATOM 100 O ARG A 15 -31.905 5.140 -9.762 1.00 37.48 O ANISOU 100 O ARG A 15 5444 4588 4210 701 -291 -10 O ATOM 101 CB ARG A 15 -28.855 5.742 -11.091 1.00 36.15 C ANISOU 101 CB ARG A 15 4978 4554 4204 766 -526 -240 C ATOM 102 CG ARG A 15 -29.019 6.747 -9.903 1.00 41.14 C ANISOU 102 CG ARG A 15 5686 5206 4738 767 -540 -251 C ATOM 103 CD ARG A 15 -28.262 6.435 -8.665 1.00 53.21 C ANISOU 103 CD ARG A 15 7307 6746 6163 877 -672 -273 C ATOM 104 NE ARG A 15 -28.746 5.277 -7.938 1.00 59.18 N ANISOU 104 NE ARG A 15 8240 7425 6819 952 -673 -172 N ATOM 105 CZ ARG A 15 -28.760 5.167 -6.596 1.00 64.96 C ANISOU 105 CZ ARG A 15 9140 8141 7400 1028 -727 -141 C ATOM 106 NH1 ARG A 15 -28.382 6.178 -5.817 1.00 65.22 N ANISOU 106 NH1 ARG A 15 9182 8235 7365 1041 -789 -212 N ATOM 107 NH2 ARG A 15 -29.187 4.038 -6.020 1.00 60.13 N ANISOU 107 NH2 ARG A 15 8710 7443 6694 1087 -713 -35 N ATOM 108 N ASP A 16 -31.849 6.330 -11.717 1.00 33.94 N ANISOU 108 N ASP A 16 4752 4209 3934 595 -245 -95 N ATOM 109 CA ASP A 16 -33.137 6.994 -11.486 1.00 34.39 C ANISOU 109 CA ASP A 16 4836 4265 3967 544 -136 -54 C ATOM 110 C ASP A 16 -34.301 6.020 -11.336 1.00 36.21 C ANISOU 110 C ASP A 16 5130 4446 4181 517 -47 32 C ATOM 111 O ASP A 16 -35.234 6.246 -10.494 1.00 33.41 O ANISOU 111 O ASP A 16 4845 4089 3759 505 37 74 O ATOM 112 CB ASP A 16 -33.427 7.924 -12.662 1.00 32.91 C ANISOU 112 CB ASP A 16 4533 4107 3864 482 -93 -87 C ATOM 113 CG ASP A 16 -34.496 8.977 -12.320 1.00 34.44 C ANISOU 113 CG ASP A 16 4743 4310 4032 463 -12 -74 C ATOM 114 OD1 ASP A 16 -34.267 9.817 -11.413 1.00 30.77 O ANISOU 114 OD1 ASP A 16 4333 3853 3503 490 -28 -105 O ATOM 115 OD2 ASP A 16 -35.529 8.981 -13.005 1.00 33.51 O ANISOU 115 OD2 ASP A 16 4577 4195 3960 429 59 -45 O ATOM 116 N SER A 17 -34.316 4.948 -12.165 1.00 36.81 N ANISOU 116 N SER A 17 5180 4483 4322 496 -51 50 N ATOM 117 CA SER A 17 -35.323 3.876 -11.978 1.00 39.75 C ANISOU 117 CA SER A 17 5625 4792 4686 452 29 126 C ATOM 118 C SER A 17 -35.226 3.211 -10.590 1.00 41.59 C ANISOU 118 C SER A 17 6036 4966 4800 499 27 189 C ATOM 119 O SER A 17 -36.258 2.830 -10.004 1.00 42.46 O ANISOU 119 O SER A 17 6224 5043 4865 444 135 257 O ATOM 120 CB SER A 17 -35.225 2.771 -13.049 1.00 39.98 C ANISOU 120 CB SER A 17 5622 4770 4799 426 9 123 C ATOM 121 OG SER A 17 -35.893 3.194 -14.230 1.00 43.61 O ANISOU 121 OG SER A 17 5952 5275 5345 358 52 93 O ATOM 122 N ARG A 18 -34.011 3.001 -10.096 1.00 43.13 N ANISOU 122 N ARG A 18 6297 5149 4943 598 -94 167 N ATOM 123 CA ARG A 18 -33.856 2.389 -8.755 1.00 46.63 C ANISOU 123 CA ARG A 18 6937 5532 5247 663 -117 232 C ATOM 124 C ARG A 18 -34.437 3.336 -7.677 1.00 48.55 C ANISOU 124 C ARG A 18 7241 5825 5382 654 -48 246 C ATOM 125 O ARG A 18 -35.018 2.864 -6.699 1.00 50.49 O ANISOU 125 O ARG A 18 7647 6023 5513 649 25 325 O ATOM 126 CB ARG A 18 -32.400 2.019 -8.420 1.00 46.71 C ANISOU 126 CB ARG A 18 6996 5533 5219 798 -288 193 C ATOM 127 CG ARG A 18 -31.657 1.097 -9.406 1.00 48.75 C ANISOU 127 CG ARG A 18 7195 5750 5577 841 -368 160 C ATOM 128 CD ARG A 18 -32.543 0.035 -9.938 1.00 49.95 C ANISOU 128 CD ARG A 18 7404 5799 5776 765 -274 229 C ATOM 129 NE ARG A 18 -31.823 -1.105 -10.497 1.00 52.95 N ANISOU 129 NE ARG A 18 7813 6099 6207 840 -359 213 N ATOM 130 CZ ARG A 18 -32.354 -2.325 -10.579 1.00 53.18 C ANISOU 130 CZ ARG A 18 7975 5990 6240 810 -314 283 C ATOM 131 NH1 ARG A 18 -33.593 -2.538 -10.128 1.00 53.05 N ANISOU 131 NH1 ARG A 18 8058 5916 6183 692 -177 374 N ATOM 132 NH2 ARG A 18 -31.645 -3.331 -11.089 1.00 54.76 N ANISOU 132 NH2 ARG A 18 8212 6108 6486 896 -399 257 N ATOM 133 N VAL A 19 -34.332 4.649 -7.868 1.00 47.77 N ANISOU 133 N VAL A 19 7026 5811 5312 646 -56 170 N ATOM 134 CA VAL A 19 -34.855 5.622 -6.864 1.00 49.77 C ANISOU 134 CA VAL A 19 7339 6108 5462 650 6 164 C ATOM 135 C VAL A 19 -36.402 5.809 -6.915 1.00 50.76 C ANISOU 135 C VAL A 19 7436 6245 5605 564 187 207 C ATOM 136 O VAL A 19 -37.033 6.031 -5.908 1.00 52.36 O ANISOU 136 O VAL A 19 7736 6459 5697 568 276 236 O ATOM 137 CB VAL A 19 -34.140 7.006 -7.055 1.00 48.90 C ANISOU 137 CB VAL A 19 7129 6066 5385 672 -73 57 C ATOM 138 CG1 VAL A 19 -34.795 8.132 -6.231 1.00 50.34 C ANISOU 138 CG1 VAL A 19 7358 6283 5484 673 1 33 C ATOM 139 CG2 VAL A 19 -32.661 6.887 -6.736 1.00 48.87 C ANISOU 139 CG2 VAL A 19 7145 6073 5349 754 -245 -1 C ATOM 140 N HIS A 20 -36.996 5.736 -8.098 1.00 50.50 N ANISOU 140 N HIS A 20 7260 6221 5708 493 237 201 N ATOM 141 CA HIS A 20 -38.360 6.151 -8.301 1.00 51.74 C ANISOU 141 CA HIS A 20 7335 6418 5906 428 376 209 C ATOM 142 C HIS A 20 -39.291 4.984 -8.514 1.00 53.30 C ANISOU 142 C HIS A 20 7533 6575 6142 339 479 276 C ATOM 143 O HIS A 20 -40.487 5.141 -8.384 1.00 54.49 O ANISOU 143 O HIS A 20 7629 6766 6308 280 611 287 O ATOM 144 CB HIS A 20 -38.491 7.083 -9.517 1.00 51.17 C ANISOU 144 CB HIS A 20 7092 6394 5956 416 352 143 C ATOM 145 CG HIS A 20 -38.075 8.485 -9.232 1.00 52.17 C ANISOU 145 CG HIS A 20 7214 6556 6050 472 311 78 C ATOM 146 ND1 HIS A 20 -36.762 8.909 -9.342 1.00 49.97 N ANISOU 146 ND1 HIS A 20 6946 6271 5769 510 185 27 N ATOM 147 CD2 HIS A 20 -38.780 9.544 -8.764 1.00 51.75 C ANISOU 147 CD2 HIS A 20 7157 6541 5965 497 380 48 C ATOM 148 CE1 HIS A 20 -36.687 10.182 -8.994 1.00 50.72 C ANISOU 148 CE1 HIS A 20 7049 6386 5835 539 179 -30 C ATOM 149 NE2 HIS A 20 -37.898 10.592 -8.649 1.00 53.68 N ANISOU 149 NE2 HIS A 20 7423 6783 6189 541 293 -17 N ATOM 150 N GLY A 21 -38.769 3.815 -8.824 1.00 52.99 N ANISOU 150 N GLY A 21 7553 6457 6124 326 422 313 N ATOM 151 CA GLY A 21 -39.636 2.802 -9.364 1.00 55.01 C ANISOU 151 CA GLY A 21 7779 6669 6456 220 506 353 C ATOM 152 C GLY A 21 -40.110 1.732 -8.401 1.00 58.09 C ANISOU 152 C GLY A 21 8340 6974 6758 163 608 446 C ATOM 153 O GLY A 21 -40.028 1.862 -7.166 1.00 59.14 O ANISOU 153 O GLY A 21 8624 7100 6748 204 647 491 O ATOM 154 N ASN A 22 -40.613 0.651 -8.976 1.00 58.74 N ANISOU 154 N ASN A 22 8416 6984 6920 61 653 477 N ATOM 155 CA ASN A 22 -41.287 -0.377 -8.158 1.00 61.45 C ANISOU 155 CA ASN A 22 8917 7234 7196 -36 787 571 C ATOM 156 C ASN A 22 -40.357 -1.558 -7.742 1.00 61.75 C ANISOU 156 C ASN A 22 9196 7113 7155 17 704 644 C ATOM 157 O ASN A 22 -40.809 -2.538 -7.150 1.00 63.65 O ANISOU 157 O ASN A 22 9606 7240 7338 -65 805 734 O ATOM 158 CB ASN A 22 -42.549 -0.887 -8.909 1.00 61.67 C ANISOU 158 CB ASN A 22 8805 7269 7358 -205 906 557 C ATOM 159 CG ASN A 22 -42.205 -1.694 -10.196 1.00 60.99 C ANISOU 159 CG ASN A 22 8666 7107 7399 -235 802 520 C ATOM 160 OD1 ASN A 22 -43.016 -2.503 -10.660 1.00 61.95 O ANISOU 160 OD1 ASN A 22 8749 7180 7608 -378 876 522 O ATOM 161 ND2 ASN A 22 -41.008 -1.493 -10.747 1.00 59.09 N ANISOU 161 ND2 ASN A 22 8423 6860 7167 -108 636 478 N ATOM 162 N GLY A 23 -39.063 -1.446 -8.055 1.00 60.15 N ANISOU 162 N GLY A 23 9005 6899 6950 157 524 603 N ATOM 163 CA GLY A 23 -38.101 -2.538 -7.799 1.00 59.67 C ANISOU 163 CA GLY A 23 9145 6694 6832 243 416 653 C ATOM 164 C GLY A 23 -37.790 -3.448 -9.009 1.00 57.87 C ANISOU 164 C GLY A 23 8870 6380 6738 226 344 617 C ATOM 165 O GLY A 23 -36.919 -4.308 -8.924 1.00 58.59 O ANISOU 165 O GLY A 23 9109 6355 6799 324 238 640 O ATOM 166 N THR A 24 -38.504 -3.286 -10.125 1.00 55.61 N ANISOU 166 N THR A 24 8389 6148 6593 116 394 557 N ATOM 167 CA THR A 24 -38.198 -4.013 -11.332 1.00 53.98 C ANISOU 167 CA THR A 24 8127 5878 6503 106 321 503 C ATOM 168 C THR A 24 -37.676 -3.023 -12.411 1.00 50.73 C ANISOU 168 C THR A 24 7493 5607 6173 166 231 392 C ATOM 169 O THR A 24 -38.396 -2.111 -12.847 1.00 50.24 O ANISOU 169 O THR A 24 7263 5665 6162 102 287 352 O ATOM 170 CB THR A 24 -39.427 -4.861 -11.848 1.00 56.46 C ANISOU 170 CB THR A 24 8426 6117 6909 -83 441 517 C ATOM 171 OG1 THR A 24 -39.938 -5.690 -10.791 1.00 58.85 O ANISOU 171 OG1 THR A 24 8944 6288 7129 -161 552 628 O ATOM 172 CG2 THR A 24 -39.058 -5.747 -13.054 1.00 53.88 C ANISOU 172 CG2 THR A 24 8084 5701 6688 -85 356 456 C ATOM 173 N LEU A 25 -36.415 -3.190 -12.821 1.00 46.88 N ANISOU 173 N LEU A 25 7012 5106 5696 294 95 343 N ATOM 174 CA LEU A 25 -35.879 -2.396 -13.903 1.00 42.71 C ANISOU 174 CA LEU A 25 6295 4693 5241 332 29 244 C ATOM 175 C LEU A 25 -36.707 -2.697 -15.136 1.00 40.33 C ANISOU 175 C LEU A 25 5887 4393 5046 218 76 202 C ATOM 176 O LEU A 25 -36.946 -3.871 -15.444 1.00 39.83 O ANISOU 176 O LEU A 25 5907 4209 5019 171 84 212 O ATOM 177 CB LEU A 25 -34.408 -2.773 -14.173 1.00 43.25 C ANISOU 177 CB LEU A 25 6384 4739 5312 478 -106 190 C ATOM 178 CG LEU A 25 -33.526 -1.755 -14.876 1.00 42.82 C ANISOU 178 CG LEU A 25 6158 4818 5294 536 -172 96 C ATOM 179 CD1 LEU A 25 -33.501 -0.380 -14.070 1.00 38.61 C ANISOU 179 CD1 LEU A 25 5579 4393 4699 544 -160 103 C ATOM 180 CD2 LEU A 25 -32.108 -2.274 -15.053 1.00 38.46 C ANISOU 180 CD2 LEU A 25 5614 4248 4750 678 -292 36 C ATOM 181 N HIS A 26 -37.102 -1.666 -15.872 1.00 36.69 N ANISOU 181 N HIS A 26 5255 4057 4629 181 93 151 N ATOM 182 CA HIS A 26 -37.803 -1.921 -17.137 1.00 36.63 C ANISOU 182 CA HIS A 26 5143 4064 4711 93 108 99 C ATOM 183 C HIS A 26 -36.987 -2.862 -18.050 1.00 35.89 C ANISOU 183 C HIS A 26 5084 3898 4657 139 29 41 C ATOM 184 O HIS A 26 -35.786 -2.654 -18.186 1.00 35.35 O ANISOU 184 O HIS A 26 5010 3854 4569 252 -45 4 O ATOM 185 CB HIS A 26 -38.103 -0.601 -17.907 1.00 35.72 C ANISOU 185 CB HIS A 26 4858 4092 4620 87 108 49 C ATOM 186 CG HIS A 26 -39.146 -0.808 -18.961 1.00 34.48 C ANISOU 186 CG HIS A 26 4604 3962 4535 -9 128 8 C ATOM 187 ND1 HIS A 26 -40.489 -0.550 -18.732 1.00 37.08 N ANISOU 187 ND1 HIS A 26 4860 4337 4892 -100 204 24 N ATOM 188 CD2 HIS A 26 -39.078 -1.429 -20.155 1.00 31.18 C ANISOU 188 CD2 HIS A 26 4159 3522 4165 -31 80 -55 C ATOM 189 CE1 HIS A 26 -41.186 -0.901 -19.800 1.00 32.70 C ANISOU 189 CE1 HIS A 26 4218 3801 4404 -171 187 -32 C ATOM 190 NE2 HIS A 26 -40.350 -1.442 -20.678 1.00 37.08 N ANISOU 190 NE2 HIS A 26 4811 4310 4966 -133 111 -79 N ATOM 191 N PRO A 27 -37.636 -3.839 -18.720 1.00 36.48 N ANISOU 191 N PRO A 27 5176 3892 4791 49 46 19 N ATOM 192 CA PRO A 27 -36.910 -4.737 -19.651 1.00 36.02 C ANISOU 192 CA PRO A 27 5157 3761 4768 98 -25 -51 C ATOM 193 C PRO A 27 -36.131 -3.950 -20.688 1.00 34.48 C ANISOU 193 C PRO A 27 4835 3688 4577 174 -80 -133 C ATOM 194 O PRO A 27 -35.082 -4.385 -21.169 1.00 33.88 O ANISOU 194 O PRO A 27 4781 3588 4504 270 -139 -191 O ATOM 195 CB PRO A 27 -38.044 -5.563 -20.316 1.00 36.96 C ANISOU 195 CB PRO A 27 5275 3813 4957 -47 12 -78 C ATOM 196 CG PRO A 27 -39.136 -5.556 -19.269 1.00 39.66 C ANISOU 196 CG PRO A 27 5647 4131 5292 -162 111 7 C ATOM 197 CD PRO A 27 -39.079 -4.180 -18.656 1.00 36.91 C ANISOU 197 CD PRO A 27 5211 3924 4890 -108 134 43 C ATOM 198 N VAL A 28 -36.621 -2.760 -21.030 1.00 33.59 N ANISOU 198 N VAL A 28 4593 3708 4461 136 -55 -139 N ATOM 199 CA VAL A 28 -35.946 -1.959 -22.082 1.00 31.97 C ANISOU 199 CA VAL A 28 4287 3610 4248 188 -90 -207 C ATOM 200 C VAL A 28 -34.534 -1.487 -21.576 1.00 32.94 C ANISOU 200 C VAL A 28 4414 3767 4335 303 -124 -213 C ATOM 201 O VAL A 28 -33.558 -1.491 -22.331 1.00 31.43 O ANISOU 201 O VAL A 28 4183 3613 4146 364 -155 -282 O ATOM 202 CB VAL A 28 -36.835 -0.709 -22.453 1.00 32.73 C ANISOU 202 CB VAL A 28 4274 3823 4339 133 -59 -197 C ATOM 203 CG1 VAL A 28 -35.978 0.386 -23.102 1.00 28.11 C ANISOU 203 CG1 VAL A 28 3625 3335 3720 191 -77 -232 C ATOM 204 CG2 VAL A 28 -38.069 -1.160 -23.327 1.00 29.76 C ANISOU 204 CG2 VAL A 28 3855 3448 4006 36 -56 -231 C ATOM 205 N LEU A 29 -34.464 -1.105 -20.286 1.00 31.12 N ANISOU 205 N LEU A 29 4225 3531 4069 327 -115 -149 N ATOM 206 CA LEU A 29 -33.205 -0.716 -19.686 1.00 32.00 C ANISOU 206 CA LEU A 29 4335 3675 4148 429 -163 -163 C ATOM 207 C LEU A 29 -32.239 -1.920 -19.534 1.00 32.33 C ANISOU 207 C LEU A 29 4456 3630 4196 532 -230 -193 C ATOM 208 O LEU A 29 -31.014 -1.778 -19.713 1.00 32.05 O ANISOU 208 O LEU A 29 4363 3647 4166 626 -283 -258 O ATOM 209 CB LEU A 29 -33.475 -0.019 -18.291 1.00 30.36 C ANISOU 209 CB LEU A 29 4171 3481 3885 430 -145 -93 C ATOM 210 CG LEU A 29 -34.229 1.306 -18.412 1.00 33.68 C ANISOU 210 CG LEU A 29 4508 3989 4299 363 -89 -80 C ATOM 211 CD1 LEU A 29 -34.385 2.014 -17.063 1.00 30.89 C ANISOU 211 CD1 LEU A 29 4203 3651 3885 379 -71 -30 C ATOM 212 CD2 LEU A 29 -33.464 2.235 -19.380 1.00 32.17 C ANISOU 212 CD2 LEU A 29 4211 3887 4125 376 -108 -147 C ATOM 213 N GLU A 30 -32.779 -3.094 -19.202 1.00 33.06 N ANISOU 213 N GLU A 30 4679 3588 4293 517 -226 -150 N ATOM 214 CA GLU A 30 -31.974 -4.304 -19.170 1.00 33.04 C ANISOU 214 CA GLU A 30 4776 3477 4300 625 -293 -178 C ATOM 215 C GLU A 30 -31.380 -4.558 -20.554 1.00 33.92 C ANISOU 215 C GLU A 30 4799 3626 4461 659 -313 -289 C ATOM 216 O GLU A 30 -30.168 -4.900 -20.700 1.00 34.27 O ANISOU 216 O GLU A 30 4825 3681 4516 793 -377 -359 O ATOM 217 CB GLU A 30 -32.812 -5.556 -18.720 1.00 34.85 C ANISOU 217 CB GLU A 30 5187 3525 4528 572 -268 -109 C ATOM 218 CG GLU A 30 -33.498 -5.444 -17.357 1.00 36.61 C ANISOU 218 CG GLU A 30 5523 3700 4688 522 -221 8 C ATOM 219 CD GLU A 30 -32.629 -5.793 -16.123 1.00 41.15 C ANISOU 219 CD GLU A 30 6244 4208 5183 666 -296 59 C ATOM 220 OE1 GLU A 30 -31.388 -5.863 -16.193 1.00 41.13 O ANISOU 220 OE1 GLU A 30 6214 4233 5178 820 -398 -3 O ATOM 221 OE2 GLU A 30 -33.228 -5.994 -15.045 1.00 47.19 O ANISOU 221 OE2 GLU A 30 7153 4898 5880 625 -249 161 O ATOM 222 N LEU A 31 -32.241 -4.495 -21.552 1.00 34.21 N ANISOU 222 N LEU A 31 4790 3681 4527 548 -262 -312 N ATOM 223 CA LEU A 31 -31.811 -4.695 -22.936 1.00 35.97 C ANISOU 223 CA LEU A 31 4944 3946 4777 567 -269 -418 C ATOM 224 C LEU A 31 -30.751 -3.683 -23.338 1.00 35.02 C ANISOU 224 C LEU A 31 4687 3978 4643 626 -269 -476 C ATOM 225 O LEU A 31 -29.742 -4.058 -23.885 1.00 37.00 O ANISOU 225 O LEU A 31 4902 4251 4907 719 -293 -563 O ATOM 226 CB LEU A 31 -33.020 -4.637 -23.868 1.00 35.26 C ANISOU 226 CB LEU A 31 4829 3868 4702 434 -226 -428 C ATOM 227 CG LEU A 31 -32.761 -4.748 -25.387 1.00 39.38 C ANISOU 227 CG LEU A 31 5295 4442 5225 438 -229 -535 C ATOM 228 CD1 LEU A 31 -31.970 -6.041 -25.672 1.00 43.45 C ANISOU 228 CD1 LEU A 31 5895 4851 5763 541 -270 -613 C ATOM 229 CD2 LEU A 31 -34.073 -4.842 -26.144 1.00 38.16 C ANISOU 229 CD2 LEU A 31 5135 4283 5080 312 -214 -543 C ATOM 230 N ALA A 32 -30.956 -2.388 -23.072 1.00 35.40 N ANISOU 230 N ALA A 32 4656 4128 4667 569 -236 -434 N ATOM 231 CA ALA A 32 -29.930 -1.408 -23.520 1.00 35.26 C ANISOU 231 CA ALA A 32 4514 4243 4641 598 -223 -493 C ATOM 232 C ALA A 32 -28.620 -1.657 -22.775 1.00 35.71 C ANISOU 232 C ALA A 32 4547 4311 4709 723 -283 -533 C ATOM 233 O ALA A 32 -27.561 -1.485 -23.346 1.00 37.46 O ANISOU 233 O ALA A 32 4667 4618 4947 773 -280 -622 O ATOM 234 CB ALA A 32 -30.410 0.068 -23.333 1.00 32.45 C ANISOU 234 CB ALA A 32 4103 3970 4257 512 -179 -439 C ATOM 235 N ALA A 33 -28.681 -2.063 -21.504 1.00 35.37 N ANISOU 235 N ALA A 33 4596 4190 4652 777 -338 -473 N ATOM 236 CA ALA A 33 -27.450 -2.437 -20.754 1.00 35.99 C ANISOU 236 CA ALA A 33 4666 4274 4735 924 -426 -516 C ATOM 237 C ALA A 33 -26.713 -3.603 -21.453 1.00 37.82 C ANISOU 237 C ALA A 33 4901 4462 5006 1041 -463 -607 C ATOM 238 O ALA A 33 -25.505 -3.537 -21.640 1.00 36.22 O ANISOU 238 O ALA A 33 4582 4348 4831 1141 -498 -705 O ATOM 239 CB ALA A 33 -27.774 -2.805 -19.281 1.00 34.19 C ANISOU 239 CB ALA A 33 4584 3948 4460 969 -484 -421 C ATOM 240 N ARG A 34 -27.449 -4.659 -21.820 1.00 40.43 N ANISOU 240 N ARG A 34 5361 4656 5344 1026 -454 -586 N ATOM 241 C ARG A 34 -26.250 -5.366 -23.882 1.00 44.26 C ANISOU 241 C ARG A 34 5714 5217 5885 1128 -426 -798 C ATOM 242 O ARG A 34 -25.126 -5.743 -24.220 1.00 46.00 O ANISOU 242 O ARG A 34 5858 5486 6134 1260 -453 -907 O ATOM 243 CA AARG A 34 -26.914 -5.825 -22.556 0.50 43.69 C ANISOU 243 CA AARG A 34 5807 5000 5791 1133 -483 -677 C ATOM 244 CB AARG A 34 -28.103 -6.765 -22.824 0.50 43.45 C ANISOU 244 CB AARG A 34 5940 4804 5763 1051 -459 -629 C ATOM 245 CG AARG A 34 -27.784 -8.206 -23.061 0.50 47.47 C ANISOU 245 CG AARG A 34 6580 5158 6300 1166 -511 -683 C ATOM 246 CD AARG A 34 -29.014 -8.960 -23.474 0.50 47.27 C ANISOU 246 CD AARG A 34 6689 4985 6285 1039 -473 -651 C ATOM 247 NE AARG A 34 -29.285 -8.835 -24.894 0.50 53.33 N ANISOU 247 NE AARG A 34 7375 5823 7066 964 -423 -743 N ATOM 248 CZ AARG A 34 -30.491 -8.948 -25.456 0.50 54.26 C ANISOU 248 CZ AARG A 34 7528 5900 7189 805 -382 -728 C ATOM 249 NH1AARG A 34 -31.586 -9.178 -24.733 0.50 52.33 N ANISOU 249 NH1AARG A 34 7382 5550 6952 686 -366 -627 N ATOM 250 NH2AARG A 34 -30.600 -8.843 -26.770 0.50 56.00 N ANISOU 250 NH2AARG A 34 7682 6193 7403 765 -355 -823 N ATOM 251 CA BARG A 34 -26.807 -5.807 -22.518 0.50 43.59 C ANISOU 251 CA BARG A 34 5787 4995 5779 1145 -488 -682 C ATOM 252 CB BARG A 34 -27.721 -7.051 -22.640 0.50 43.59 C ANISOU 252 CB BARG A 34 5977 4800 5786 1117 -490 -643 C ATOM 253 CG BARG A 34 -27.004 -8.254 -23.328 0.50 47.77 C ANISOU 253 CG BARG A 34 6553 5246 6350 1259 -533 -754 C ATOM 254 CD BARG A 34 -27.762 -9.577 -23.195 0.50 46.16 C ANISOU 254 CD BARG A 34 6573 4810 6155 1247 -553 -713 C ATOM 255 NE BARG A 34 -26.879 -10.753 -23.017 0.50 50.04 N ANISOU 255 NE BARG A 34 7176 5172 6667 1452 -641 -772 N ATOM 256 CZ BARG A 34 -26.163 -11.055 -21.920 0.50 49.29 C ANISOU 256 CZ BARG A 34 7153 5023 6553 1616 -736 -735 C ATOM 257 NH1BARG A 34 -25.415 -12.177 -21.879 0.50 52.79 N ANISOU 257 NH1BARG A 34 7708 5335 7015 1819 -823 -796 N ATOM 258 NH2BARG A 34 -26.166 -10.257 -20.877 0.50 43.74 N ANISOU 258 NH2BARG A 34 6419 4393 5806 1595 -754 -644 N ATOM 259 N GLU A 35 -26.966 -4.496 -24.611 1.00 44.66 N ANISOU 259 N GLU A 35 5711 5344 5915 976 -342 -776 N ATOM 260 CA GLU A 35 -26.564 -4.122 -25.987 1.00 48.96 C ANISOU 260 CA GLU A 35 6148 6003 6453 947 -270 -872 C ATOM 261 C GLU A 35 -25.536 -3.044 -26.128 1.00 51.65 C ANISOU 261 C GLU A 35 6320 6510 6795 947 -228 -923 C ATOM 262 O GLU A 35 -24.886 -2.946 -27.155 1.00 52.62 O ANISOU 262 O GLU A 35 6354 6726 6914 956 -165 -1019 O ATOM 263 CB GLU A 35 -27.758 -3.771 -26.874 1.00 48.06 C ANISOU 263 CB GLU A 35 6070 5888 6301 803 -211 -836 C ATOM 264 CG GLU A 35 -28.738 -4.892 -27.075 1.00 51.94 C ANISOU 264 CG GLU A 35 6701 6231 6801 778 -240 -824 C ATOM 265 CD GLU A 35 -28.219 -6.083 -27.863 1.00 58.69 C ANISOU 265 CD GLU A 35 7603 7023 7671 875 -257 -939 C ATOM 266 OE1 GLU A 35 -28.890 -7.145 -27.748 1.00 63.18 O ANISOU 266 OE1 GLU A 35 8309 7435 8262 867 -296 -929 O ATOM 267 OE2 GLU A 35 -27.178 -5.998 -28.586 1.00 59.08 O ANISOU 267 OE2 GLU A 35 7562 7173 7714 953 -225 -1044 O ATOM 268 N THR A 36 -25.364 -2.245 -25.077 1.00 54.18 N ANISOU 268 N THR A 36 6600 6869 7118 930 -256 -866 N ATOM 269 CA THR A 36 -24.432 -1.111 -25.097 1.00 55.98 C ANISOU 269 CA THR A 36 6668 7247 7356 898 -216 -913 C ATOM 270 C THR A 36 -22.991 -1.556 -24.928 1.00 58.82 C ANISOU 270 C THR A 36 6902 7679 7767 1040 -261 -1033 C ATOM 271 O THR A 36 -22.128 -1.108 -25.707 1.00 60.98 O ANISOU 271 O THR A 36 7027 8083 8059 1019 -185 -1130 O ATOM 272 CB THR A 36 -24.852 0.005 -24.032 1.00 53.84 C ANISOU 272 CB THR A 36 6406 6985 7066 816 -233 -817 C ATOM 273 OG1 THR A 36 -25.992 0.732 -24.540 1.00 54.79 O ANISOU 273 OG1 THR A 36 6584 7090 7144 681 -163 -738 O ATOM 274 CG2 THR A 36 -23.691 1.002 -23.754 1.00 58.20 C ANISOU 274 CG2 THR A 36 6797 7671 7646 801 -224 -883 C ATOM 275 N PRO A 37 -22.764 -2.624 -24.149 1.00 60.67 N ANISOU 275 N PRO A 37 7207 7821 8023 1194 -373 -1040 N ATOM 276 CA PRO A 37 -22.003 -2.980 -22.992 1.00 62.27 C ANISOU 276 CA PRO A 37 7392 8017 8249 1341 -497 -1060 C ATOM 277 C PRO A 37 -21.915 -1.837 -22.027 1.00 61.39 C ANISOU 277 C PRO A 37 7227 7976 8124 1271 -524 -1012 C ATOM 278 O PRO A 37 -20.905 -1.112 -22.009 1.00 62.26 O ANISOU 278 O PRO A 37 7153 8232 8272 1266 -521 -1102 O ATOM 279 CB PRO A 37 -20.604 -3.329 -23.574 1.00 64.24 C ANISOU 279 CB PRO A 37 7462 8387 8561 1472 -501 -1226 C ATOM 280 CG PRO A 37 -20.894 -3.771 -24.996 1.00 64.13 C ANISOU 280 CG PRO A 37 7468 8359 8540 1433 -392 -1275 C ATOM 281 CD PRO A 37 -22.419 -3.651 -25.155 1.00 64.01 C ANISOU 281 CD PRO A 37 7632 8223 8465 1285 -350 -1139 C ATOM 282 N LEU A 38 -22.942 -1.682 -21.197 1.00 59.34 N ANISOU 282 N LEU A 38 7121 7615 7812 1213 -547 -883 N ATOM 283 CA LEU A 38 -22.780 -0.709 -20.098 1.00 57.57 C ANISOU 283 CA LEU A 38 6866 7445 7564 1180 -595 -850 C ATOM 284 C LEU A 38 -21.621 -1.160 -19.165 1.00 58.63 C ANISOU 284 C LEU A 38 6947 7616 7714 1361 -743 -922 C ATOM 285 O LEU A 38 -21.724 -2.199 -18.493 1.00 58.69 O ANISOU 285 O LEU A 38 7101 7508 7691 1501 -840 -880 O ATOM 286 CB LEU A 38 -24.083 -0.469 -19.329 1.00 54.31 C ANISOU 286 CB LEU A 38 6625 6927 7083 1098 -583 -706 C ATOM 287 CG LEU A 38 -24.009 0.540 -18.167 1.00 54.60 C ANISOU 287 CG LEU A 38 6657 7010 7080 1067 -628 -675 C ATOM 288 CD1 LEU A 38 -23.848 2.021 -18.628 1.00 46.64 C ANISOU 288 CD1 LEU A 38 5512 6115 6093 921 -546 -712 C ATOM 289 CD2 LEU A 38 -25.276 0.408 -17.348 1.00 52.77 C ANISOU 289 CD2 LEU A 38 6615 6660 6775 1028 -616 -540 C ATOM 290 N ARG A 39 -20.547 -0.364 -19.107 1.00 58.20 N ANISOU 290 N ARG A 39 6690 7718 7704 1356 -763 -1030 N ATOM 291 CA ARG A 39 -19.460 -0.708 -18.209 1.00 60.24 C ANISOU 291 CA ARG A 39 6875 8033 7979 1531 -922 -1112 C ATOM 292 C ARG A 39 -19.534 0.093 -16.908 1.00 59.20 C ANISOU 292 C ARG A 39 6785 7918 7790 1502 -1008 -1067 C ATOM 293 O ARG A 39 -18.974 -0.324 -15.881 1.00 61.59 O ANISOU 293 O ARG A 39 7116 8221 8063 1663 -1170 -1090 O ATOM 294 CB ARG A 39 -18.066 -0.625 -18.924 1.00 62.26 C ANISOU 294 CB ARG A 39 6858 8463 8336 1583 -915 -1294 C ATOM 295 CG ARG A 39 -17.824 -1.041 -20.189 0.00 47.93 C ANISOU 295 CG ARG A 39 4958 6682 6571 1582 -809 -1365 C ATOM 296 CD ARG A 39 -16.543 -0.635 -20.899 0.00 49.33 C ANISOU 296 CD ARG A 39 4844 7057 6840 1573 -753 -1541 C ATOM 297 NE ARG A 39 -16.265 -1.483 -22.055 0.00 50.04 N ANISOU 297 NE ARG A 39 4890 7158 6966 1650 -674 -1620 N ATOM 298 CZ ARG A 39 -15.250 -1.300 -22.887 0.00 51.38 C ANISOU 298 CZ ARG A 39 4819 7495 7207 1644 -586 -1774 C ATOM 299 NH1 ARG A 39 -14.405 -0.295 -22.695 0.00 52.18 N ANISOU 299 NH1 ARG A 39 4694 7766 7366 1548 -565 -1864 N ATOM 300 NH2 ARG A 39 -15.073 -2.121 -23.913 0.00 52.08 N ANISOU 300 NH2 ARG A 39 4895 7583 7312 1726 -511 -1846 N ATOM 301 N LEU A 40 -20.281 1.202 -16.931 1.00 56.75 N ANISOU 301 N LEU A 40 6501 7609 7451 1312 -908 -1000 N ATOM 302 CA LEU A 40 -20.334 2.139 -15.807 1.00 54.24 C ANISOU 302 CA LEU A 40 6210 7317 7081 1265 -969 -978 C ATOM 303 C LEU A 40 -21.445 1.709 -14.852 1.00 52.52 C ANISOU 303 C LEU A 40 6249 6952 6753 1300 -1000 -830 C ATOM 304 O LEU A 40 -22.586 1.508 -15.286 1.00 51.21 O ANISOU 304 O LEU A 40 6207 6687 6565 1220 -892 -726 O ATOM 305 CB LEU A 40 -20.581 3.563 -16.357 1.00 53.44 C ANISOU 305 CB LEU A 40 6022 7276 7007 1050 -837 -985 C ATOM 306 CG LEU A 40 -20.717 4.773 -15.415 1.00 54.39 C ANISOU 306 CG LEU A 40 6167 7417 7083 960 -865 -975 C ATOM 307 CD1 LEU A 40 -19.452 4.991 -14.543 1.00 54.60 C ANISOU 307 CD1 LEU A 40 6058 7557 7131 1040 -1022 -1105 C ATOM 308 CD2 LEU A 40 -21.050 6.033 -16.210 1.00 50.38 C ANISOU 308 CD2 LEU A 40 5605 6929 6606 756 -716 -971 C ATOM 309 N SER A 41 -21.132 1.589 -13.559 1.00 50.73 N ANISOU 309 N SER A 41 6101 6719 6453 1414 -1145 -824 N ATOM 310 CA SER A 41 -22.138 1.308 -12.530 1.00 48.82 C ANISOU 310 CA SER A 41 6110 6350 6087 1435 -1160 -685 C ATOM 311 C SER A 41 -23.097 2.494 -12.255 1.00 46.99 C ANISOU 311 C SER A 41 5929 6115 5809 1263 -1053 -620 C ATOM 312 O SER A 41 -22.666 3.626 -12.174 1.00 45.75 O ANISOU 312 O SER A 41 5652 6055 5677 1184 -1056 -695 O ATOM 313 CB SER A 41 -21.471 0.919 -11.213 1.00 50.64 C ANISOU 313 CB SER A 41 6426 6586 6230 1613 -1350 -701 C ATOM 314 OG SER A 41 -22.471 0.740 -10.230 1.00 49.48 O ANISOU 314 OG SER A 41 6532 6321 5947 1611 -1336 -561 O ATOM 315 N PRO A 42 -24.412 2.223 -12.133 1.00 46.35 N ANISOU 315 N PRO A 42 6023 5918 5668 1205 -954 -487 N ATOM 316 CA PRO A 42 -25.327 3.298 -11.763 1.00 45.73 C ANISOU 316 CA PRO A 42 5996 5840 5542 1077 -864 -434 C ATOM 317 C PRO A 42 -25.075 3.787 -10.345 1.00 47.22 C ANISOU 317 C PRO A 42 6269 6051 5620 1133 -963 -441 C ATOM 318 O PRO A 42 -25.650 4.820 -9.926 1.00 46.06 O ANISOU 318 O PRO A 42 6154 5917 5430 1043 -905 -425 O ATOM 319 CB PRO A 42 -26.695 2.641 -11.824 1.00 44.83 C ANISOU 319 CB PRO A 42 6040 5605 5387 1033 -756 -303 C ATOM 320 CG PRO A 42 -26.490 1.448 -12.751 1.00 46.09 C ANISOU 320 CG PRO A 42 6182 5713 5618 1083 -757 -309 C ATOM 321 CD PRO A 42 -25.122 0.966 -12.450 1.00 45.87 C ANISOU 321 CD PRO A 42 6101 5728 5600 1239 -910 -396 C ATOM 322 N GLU A 43 -24.281 3.031 -9.582 1.00 49.93 N ANISOU 322 N GLU A 43 6670 6393 5908 1294 -1117 -463 N ATOM 323 CA GLU A 43 -23.850 3.502 -8.234 1.00 52.27 C ANISOU 323 CA GLU A 43 7040 6731 6088 1367 -1246 -494 C ATOM 324 C GLU A 43 -22.452 4.146 -8.196 1.00 53.63 C ANISOU 324 C GLU A 43 7005 7046 6324 1401 -1386 -661 C ATOM 325 O GLU A 43 -21.953 4.528 -7.132 1.00 55.46 O ANISOU 325 O GLU A 43 7274 7329 6470 1467 -1521 -714 O ATOM 326 CB GLU A 43 -23.947 2.392 -7.191 1.00 55.32 C ANISOU 326 CB GLU A 43 7660 7024 6334 1527 -1343 -404 C ATOM 327 CG GLU A 43 -25.382 1.995 -6.937 1.00 60.24 C ANISOU 327 CG GLU A 43 8497 7519 6874 1458 -1192 -245 C ATOM 328 CD GLU A 43 -25.650 1.503 -5.524 1.00 68.75 C ANISOU 328 CD GLU A 43 9843 8523 7758 1561 -1253 -151 C ATOM 329 OE1 GLU A 43 -26.509 2.168 -4.849 1.00 72.40 O ANISOU 329 OE1 GLU A 43 10408 8980 8120 1478 -1157 -97 O ATOM 330 OE2 GLU A 43 -24.641 1.036 -4.984 0.00 88.71 O ANISOU 330 OE2 GLU A 43 12402 11069 10233 1729 -1439 -197 O ATOM 331 N ASP A 44 -21.824 4.276 -9.347 1.00 52.10 N ANISOU 331 N ASP A 44 6593 6924 6279 1349 -1351 -752 N ATOM 332 CA ASP A 44 -20.578 4.995 -9.454 1.00 53.12 C ANISOU 332 CA ASP A 44 6494 7198 6492 1332 -1441 -917 C ATOM 333 C ASP A 44 -20.800 6.444 -9.012 1.00 51.92 C ANISOU 333 C ASP A 44 6334 7079 6314 1185 -1405 -952 C ATOM 334 O ASP A 44 -21.814 7.049 -9.341 1.00 48.60 O ANISOU 334 O ASP A 44 5988 6594 5886 1053 -1252 -872 O ATOM 335 CB ASP A 44 -20.129 4.984 -10.911 1.00 53.82 C ANISOU 335 CB ASP A 44 6370 7344 6735 1255 -1341 -985 C ATOM 336 CG ASP A 44 -18.680 5.259 -11.055 1.00 58.43 C ANISOU 336 CG ASP A 44 6701 8083 7418 1281 -1444 -1163 C ATOM 337 OD1 ASP A 44 -18.291 6.445 -10.963 1.00 62.93 O ANISOU 337 OD1 ASP A 44 7152 8732 8025 1147 -1434 -1252 O ATOM 338 OD2 ASP A 44 -17.912 4.279 -11.243 1.00 64.74 O ANISOU 338 OD2 ASP A 44 7414 8923 8260 1440 -1538 -1223 O ATOM 339 N THR A 45 -19.840 7.003 -8.278 1.00 52.12 N ANISOU 339 N THR A 45 6267 7205 6330 1213 -1554 -1081 N ATOM 340 CA THR A 45 -19.991 8.353 -7.727 1.00 52.00 C ANISOU 340 CA THR A 45 6269 7207 6282 1084 -1542 -1128 C ATOM 341 C THR A 45 -20.223 9.469 -8.777 1.00 49.56 C ANISOU 341 C THR A 45 5848 6896 6086 866 -1367 -1151 C ATOM 342 O THR A 45 -20.922 10.423 -8.471 1.00 48.67 O ANISOU 342 O THR A 45 5839 6727 5926 765 -1296 -1120 O ATOM 343 CB THR A 45 -18.813 8.731 -6.739 1.00 54.42 C ANISOU 343 CB THR A 45 6483 7631 6564 1150 -1760 -1289 C ATOM 344 OG1 THR A 45 -17.583 8.463 -7.400 1.00 60.19 O ANISOU 344 OG1 THR A 45 6947 8486 7438 1171 -1828 -1425 O ATOM 345 CG2 THR A 45 -18.870 7.849 -5.492 1.00 54.23 C ANISOU 345 CG2 THR A 45 6657 7578 6368 1364 -1929 -1236 C ATOM 346 N VAL A 46 -19.632 9.367 -9.972 1.00 48.04 N ANISOU 346 N VAL A 46 5460 6762 6033 802 -1299 -1207 N ATOM 347 CA VAL A 46 -19.888 10.347 -11.034 1.00 47.18 C ANISOU 347 CA VAL A 46 5281 6635 6012 602 -1124 -1207 C ATOM 348 C VAL A 46 -21.392 10.323 -11.520 1.00 43.45 C ANISOU 348 C VAL A 46 4989 6032 5489 562 -964 -1039 C ATOM 349 O VAL A 46 -21.965 11.361 -11.878 1.00 41.04 O ANISOU 349 O VAL A 46 4726 5674 5193 426 -851 -1011 O ATOM 350 CB VAL A 46 -18.900 10.170 -12.236 1.00 47.56 C ANISOU 350 CB VAL A 46 5086 6781 6202 546 -1072 -1302 C ATOM 351 CG1 VAL A 46 -19.129 8.859 -12.926 1.00 50.28 C ANISOU 351 CG1 VAL A 46 5443 7106 6556 665 -1039 -1232 C ATOM 352 CG2 VAL A 46 -19.126 11.243 -13.249 1.00 48.44 C ANISOU 352 CG2 VAL A 46 5161 6867 6379 336 -895 -1295 C ATOM 353 N VAL A 47 -21.995 9.134 -11.485 1.00 41.32 N ANISOU 353 N VAL A 47 4824 5708 5167 686 -967 -937 N ATOM 354 CA VAL A 47 -23.407 8.941 -11.809 1.00 39.14 C ANISOU 354 CA VAL A 47 4702 5325 4845 662 -840 -792 C ATOM 355 C VAL A 47 -24.288 9.501 -10.673 1.00 39.74 C ANISOU 355 C VAL A 47 4955 5339 4804 666 -842 -733 C ATOM 356 O VAL A 47 -25.258 10.210 -10.938 1.00 38.81 O ANISOU 356 O VAL A 47 4902 5165 4677 580 -725 -674 O ATOM 357 CB VAL A 47 -23.726 7.464 -12.109 1.00 39.65 C ANISOU 357 CB VAL A 47 4821 5345 4900 775 -842 -715 C ATOM 358 CG1 VAL A 47 -25.249 7.285 -12.498 1.00 35.07 C ANISOU 358 CG1 VAL A 47 4375 4663 4286 726 -705 -578 C ATOM 359 CG2 VAL A 47 -22.842 6.968 -13.271 1.00 38.64 C ANISOU 359 CG2 VAL A 47 4516 5281 4884 778 -830 -790 C ATOM 360 N LEU A 48 -23.920 9.262 -9.410 1.00 40.17 N ANISOU 360 N LEU A 48 5086 5413 4765 770 -976 -760 N ATOM 361 CA LEU A 48 -24.712 9.830 -8.328 1.00 40.53 C ANISOU 361 CA LEU A 48 5303 5410 4687 774 -967 -717 C ATOM 362 C LEU A 48 -24.649 11.353 -8.371 1.00 41.47 C ANISOU 362 C LEU A 48 5379 5538 4839 644 -928 -794 C ATOM 363 O LEU A 48 -25.678 12.027 -8.112 1.00 39.59 O ANISOU 363 O LEU A 48 5260 5237 4547 603 -834 -740 O ATOM 364 CB LEU A 48 -24.313 9.289 -6.940 1.00 42.70 C ANISOU 364 CB LEU A 48 5694 5702 4828 917 -1124 -730 C ATOM 365 CG LEU A 48 -24.296 7.752 -6.717 1.00 42.05 C ANISOU 365 CG LEU A 48 5701 5586 4691 1065 -1184 -649 C ATOM 366 CD1 LEU A 48 -23.759 7.474 -5.259 1.00 47.43 C ANISOU 366 CD1 LEU A 48 6512 6291 5218 1211 -1365 -677 C ATOM 367 CD2 LEU A 48 -25.641 7.058 -6.940 1.00 40.69 C ANISOU 367 CD2 LEU A 48 5672 5308 4481 1051 -1035 -492 C ATOM 368 N ARG A 49 -23.470 11.896 -8.690 1.00 41.31 N ANISOU 368 N ARG A 49 5193 5592 4911 580 -994 -925 N ATOM 369 CA ARG A 49 -23.307 13.363 -8.744 1.00 42.20 C ANISOU 369 CA ARG A 49 5276 5695 5063 437 -958 -1007 C ATOM 370 C ARG A 49 -24.056 13.971 -9.898 1.00 40.06 C ANISOU 370 C ARG A 49 5007 5354 4861 319 -785 -940 C ATOM 371 O ARG A 49 -24.731 14.995 -9.729 1.00 39.70 O ANISOU 371 O ARG A 49 5062 5235 4786 257 -719 -925 O ATOM 372 CB ARG A 49 -21.842 13.779 -8.775 1.00 43.71 C ANISOU 372 CB ARG A 49 5280 5986 5343 374 -1065 -1172 C ATOM 373 CG ARG A 49 -21.107 13.381 -7.508 1.00 48.21 C ANISOU 373 CG ARG A 49 5857 6630 5831 500 -1267 -1259 C ATOM 374 CD ARG A 49 -19.579 13.383 -7.726 1.00 55.34 C ANISOU 374 CD ARG A 49 6512 7666 6848 470 -1385 -1426 C ATOM 375 NE ARG A 49 -19.075 14.734 -7.515 1.00 57.88 N ANISOU 375 NE ARG A 49 6774 8001 7217 308 -1400 -1558 N ATOM 376 CZ ARG A 49 -17.796 15.075 -7.454 1.00 64.70 C ANISOU 376 CZ ARG A 49 7429 8980 8175 242 -1507 -1733 C ATOM 377 NH1 ARG A 49 -16.843 14.144 -7.593 1.00 66.32 N ANISOU 377 NH1 ARG A 49 7446 9314 8439 346 -1617 -1804 N ATOM 378 NH2 ARG A 49 -17.480 16.356 -7.240 1.00 66.22 N ANISOU 378 NH2 ARG A 49 7600 9155 8406 71 -1506 -1846 N ATOM 379 N TYR A 50 -23.957 13.370 -11.081 1.00 37.94 N ANISOU 379 N TYR A 50 4638 5103 4675 299 -716 -902 N ATOM 380 CA TYR A 50 -24.799 13.852 -12.176 1.00 36.59 C ANISOU 380 CA TYR A 50 4497 4862 4542 212 -563 -822 C ATOM 381 C TYR A 50 -26.281 13.687 -11.887 1.00 34.08 C ANISOU 381 C TYR A 50 4338 4466 4143 274 -497 -700 C ATOM 382 O TYR A 50 -27.048 14.524 -12.265 1.00 34.26 O ANISOU 382 O TYR A 50 4424 4425 4169 217 -408 -661 O ATOM 383 CB TYR A 50 -24.481 13.187 -13.518 1.00 35.70 C ANISOU 383 CB TYR A 50 4265 4786 4513 186 -499 -805 C ATOM 384 CG TYR A 50 -23.336 13.894 -14.159 1.00 36.27 C ANISOU 384 CG TYR A 50 4191 4913 4677 57 -480 -911 C ATOM 385 CD1 TYR A 50 -22.055 13.374 -14.087 1.00 39.65 C ANISOU 385 CD1 TYR A 50 4449 5452 5164 78 -565 -1023 C ATOM 386 CD2 TYR A 50 -23.530 15.081 -14.823 1.00 37.38 C ANISOU 386 CD2 TYR A 50 4364 4993 4847 -85 -374 -904 C ATOM 387 CE1 TYR A 50 -21.007 14.030 -14.642 1.00 41.96 C ANISOU 387 CE1 TYR A 50 4588 5807 5548 -57 -531 -1130 C ATOM 388 CE2 TYR A 50 -22.490 15.747 -15.390 1.00 39.20 C ANISOU 388 CE2 TYR A 50 4473 5264 5158 -227 -336 -997 C ATOM 389 CZ TYR A 50 -21.236 15.226 -15.285 1.00 42.36 C ANISOU 389 CZ TYR A 50 4685 5787 5622 -222 -408 -1114 C ATOM 390 OH TYR A 50 -20.192 15.883 -15.876 1.00 44.77 O ANISOU 390 OH TYR A 50 4847 6147 6018 -383 -351 -1216 O ATOM 391 N HIS A 51 -26.650 12.605 -11.241 1.00 33.64 N ANISOU 391 N HIS A 51 4345 4418 4021 389 -541 -645 N ATOM 392 CA HIS A 51 -28.065 12.396 -10.926 1.00 35.02 C ANISOU 392 CA HIS A 51 4652 4531 4124 433 -464 -537 C ATOM 393 C HIS A 51 -28.631 13.527 -10.043 1.00 35.06 C ANISOU 393 C HIS A 51 4768 4497 4058 423 -444 -554 C ATOM 394 O HIS A 51 -29.703 14.061 -10.342 1.00 34.38 O ANISOU 394 O HIS A 51 4734 4360 3970 402 -343 -501 O ATOM 395 CB HIS A 51 -28.293 11.028 -10.282 1.00 34.21 C ANISOU 395 CB HIS A 51 4617 4430 3953 542 -506 -474 C ATOM 396 CG HIS A 51 -29.726 10.771 -10.020 1.00 34.81 C ANISOU 396 CG HIS A 51 4804 4453 3969 560 -406 -370 C ATOM 397 ND1 HIS A 51 -30.596 10.355 -11.006 1.00 35.64 N ANISOU 397 ND1 HIS A 51 4878 4533 4131 526 -308 -300 N ATOM 398 CD2 HIS A 51 -30.468 10.941 -8.908 1.00 32.83 C ANISOU 398 CD2 HIS A 51 4684 4181 3609 600 -379 -336 C ATOM 399 CE1 HIS A 51 -31.819 10.246 -10.499 1.00 30.43 C ANISOU 399 CE1 HIS A 51 4307 3842 3412 541 -228 -229 C ATOM 400 NE2 HIS A 51 -31.769 10.616 -9.239 1.00 39.41 N ANISOU 400 NE2 HIS A 51 5544 4982 4447 584 -258 -248 N ATOM 401 N VAL A 52 -27.883 13.942 -9.014 1.00 36.23 N ANISOU 401 N VAL A 52 4945 4669 4150 441 -546 -642 N ATOM 402 CA VAL A 52 -28.234 15.175 -8.273 1.00 37.44 C ANISOU 402 CA VAL A 52 5199 4781 4246 418 -534 -689 C ATOM 403 C VAL A 52 -28.432 16.419 -9.148 1.00 37.14 C ANISOU 403 C VAL A 52 5140 4680 4290 310 -451 -710 C ATOM 404 O VAL A 52 -29.437 17.117 -8.996 1.00 36.28 O ANISOU 404 O VAL A 52 5131 4508 4147 323 -373 -678 O ATOM 405 CB VAL A 52 -27.234 15.500 -7.097 1.00 38.83 C ANISOU 405 CB VAL A 52 5400 4998 4354 440 -680 -808 C ATOM 406 CG1 VAL A 52 -27.753 16.671 -6.245 1.00 39.29 C ANISOU 406 CG1 VAL A 52 5595 5001 4331 433 -660 -855 C ATOM 407 CG2 VAL A 52 -27.102 14.290 -6.201 1.00 40.92 C ANISOU 407 CG2 VAL A 52 5724 5310 4512 568 -769 -772 C ATOM 408 N LEU A 53 -27.483 16.706 -10.036 1.00 37.39 N ANISOU 408 N LEU A 53 5052 4728 4426 210 -463 -765 N ATOM 409 CA LEU A 53 -27.557 17.913 -10.881 1.00 38.36 C ANISOU 409 CA LEU A 53 5183 4775 4617 96 -384 -779 C ATOM 410 C LEU A 53 -28.740 17.840 -11.807 1.00 36.93 C ANISOU 410 C LEU A 53 5039 4544 4449 119 -270 -663 C ATOM 411 O LEU A 53 -29.417 18.838 -12.031 1.00 37.09 O ANISOU 411 O LEU A 53 5149 4477 4467 100 -207 -644 O ATOM 412 CB LEU A 53 -26.324 18.014 -11.779 1.00 39.49 C ANISOU 412 CB LEU A 53 5180 4959 4865 -25 -392 -843 C ATOM 413 CG LEU A 53 -25.217 19.051 -11.536 1.00 46.49 C ANISOU 413 CG LEU A 53 6027 5838 5801 -156 -439 -977 C ATOM 414 CD1 LEU A 53 -24.984 19.573 -10.086 1.00 45.50 C ANISOU 414 CD1 LEU A 53 5977 5707 5605 -129 -549 -1078 C ATOM 415 CD2 LEU A 53 -23.944 18.526 -12.218 1.00 47.14 C ANISOU 415 CD2 LEU A 53 5909 6024 5978 -231 -462 -1043 C ATOM 416 N LEU A 54 -28.974 16.668 -12.384 1.00 35.97 N ANISOU 416 N LEU A 54 4850 4473 4343 163 -252 -592 N ATOM 417 CA LEU A 54 -30.083 16.531 -13.344 1.00 35.11 C ANISOU 417 CA LEU A 54 4760 4331 4251 181 -159 -494 C ATOM 418 C LEU A 54 -31.414 16.600 -12.601 1.00 34.39 C ANISOU 418 C LEU A 54 4766 4211 4090 272 -122 -443 C ATOM 419 O LEU A 54 -32.349 17.223 -13.099 1.00 34.94 O ANISOU 419 O LEU A 54 4878 4229 4168 284 -57 -402 O ATOM 420 CB LEU A 54 -29.976 15.227 -14.135 1.00 34.36 C ANISOU 420 CB LEU A 54 4571 4295 4191 198 -154 -447 C ATOM 421 CG LEU A 54 -28.750 15.194 -15.070 1.00 34.22 C ANISOU 421 CG LEU A 54 4442 4314 4245 111 -162 -500 C ATOM 422 CD1 LEU A 54 -28.906 14.043 -15.981 1.00 32.09 C ANISOU 422 CD1 LEU A 54 4108 4083 4001 139 -139 -451 C ATOM 423 CD2 LEU A 54 -28.547 16.518 -15.870 1.00 31.84 C ANISOU 423 CD2 LEU A 54 4166 3953 3979 -1 -99 -517 C ATOM 424 N GLU A 55 -31.498 15.976 -11.420 1.00 33.76 N ANISOU 424 N GLU A 55 4724 4167 3938 340 -161 -448 N ATOM 425 CA GLU A 55 -32.710 16.126 -10.574 1.00 34.22 C ANISOU 425 CA GLU A 55 4877 4207 3919 417 -106 -413 C ATOM 426 C GLU A 55 -33.032 17.574 -10.198 1.00 35.23 C ANISOU 426 C GLU A 55 5094 4269 4024 419 -83 -465 C ATOM 427 O GLU A 55 -34.196 17.968 -10.284 1.00 34.90 O ANISOU 427 O GLU A 55 5088 4199 3972 470 -7 -430 O ATOM 428 CB GLU A 55 -32.758 15.136 -9.381 1.00 33.66 C ANISOU 428 CB GLU A 55 4857 4181 3752 484 -136 -395 C ATOM 429 CG GLU A 55 -33.965 15.288 -8.380 1.00 35.25 C ANISOU 429 CG GLU A 55 5161 4377 3856 554 -56 -367 C ATOM 430 CD GLU A 55 -35.392 15.047 -8.969 1.00 40.14 C ANISOU 430 CD GLU A 55 5740 4999 4514 569 62 -291 C ATOM 431 OE1 GLU A 55 -35.498 14.487 -10.061 1.00 38.69 O ANISOU 431 OE1 GLU A 55 5464 4822 4412 534 72 -247 O ATOM 432 OE2 GLU A 55 -36.404 15.448 -8.313 1.00 42.64 O ANISOU 432 OE2 GLU A 55 6110 5317 4773 620 144 -289 O ATOM 433 N GLU A 56 -32.025 18.374 -9.828 1.00 35.76 N ANISOU 433 N GLU A 56 5191 4308 4089 366 -150 -558 N ATOM 434 CA GLU A 56 -32.261 19.802 -9.587 1.00 38.34 C ANISOU 434 CA GLU A 56 5619 4543 4405 356 -130 -615 C ATOM 435 C GLU A 56 -32.827 20.515 -10.818 1.00 36.75 C ANISOU 435 C GLU A 56 5422 4265 4277 332 -61 -568 C ATOM 436 O GLU A 56 -33.759 21.307 -10.704 1.00 37.36 O ANISOU 436 O GLU A 56 5585 4276 4334 396 -11 -562 O ATOM 437 CB GLU A 56 -31.003 20.523 -9.071 1.00 39.16 C ANISOU 437 CB GLU A 56 5746 4623 4510 274 -220 -734 C ATOM 438 CG GLU A 56 -30.515 19.834 -7.806 1.00 47.86 C ANISOU 438 CG GLU A 56 6859 5805 5519 326 -309 -782 C ATOM 439 CD GLU A 56 -29.231 20.406 -7.226 1.00 56.55 C ANISOU 439 CD GLU A 56 7957 6910 6620 251 -426 -917 C ATOM 440 OE1 GLU A 56 -28.243 20.657 -7.994 1.00 61.53 O ANISOU 440 OE1 GLU A 56 8484 7541 7355 132 -454 -964 O ATOM 441 OE2 GLU A 56 -29.191 20.552 -5.991 1.00 60.20 O ANISOU 441 OE2 GLU A 56 8512 7387 6974 309 -488 -982 O ATOM 442 N ILE A 57 -32.274 20.218 -11.998 1.00 34.58 N ANISOU 442 N ILE A 57 5061 4001 4078 252 -59 -535 N ATOM 443 CA ILE A 57 -32.796 20.830 -13.243 1.00 33.20 C ANISOU 443 CA ILE A 57 4910 3755 3952 236 0 -478 C ATOM 444 C ILE A 57 -34.258 20.425 -13.486 1.00 32.53 C ANISOU 444 C ILE A 57 4816 3693 3850 352 52 -398 C ATOM 445 O ILE A 57 -35.107 21.255 -13.769 1.00 32.57 O ANISOU 445 O ILE A 57 4893 3627 3853 412 86 -380 O ATOM 446 CB ILE A 57 -31.917 20.410 -14.475 1.00 33.96 C ANISOU 446 CB ILE A 57 4913 3879 4112 130 3 -455 C ATOM 447 CG1 ILE A 57 -30.526 21.106 -14.396 1.00 33.44 C ANISOU 447 CG1 ILE A 57 4845 3780 4082 -8 -26 -545 C ATOM 448 CG2 ILE A 57 -32.698 20.620 -15.785 1.00 31.37 C ANISOU 448 CG2 ILE A 57 4609 3509 3803 149 60 -370 C ATOM 449 CD1 ILE A 57 -29.386 20.277 -15.170 1.00 33.75 C ANISOU 449 CD1 ILE A 57 4735 3910 4179 -101 -33 -558 C ATOM 450 N ILE A 58 -34.556 19.138 -13.384 1.00 31.79 N ANISOU 450 N ILE A 58 4633 3697 3749 385 54 -357 N ATOM 451 CA ILE A 58 -35.939 18.658 -13.480 1.00 32.45 C ANISOU 451 CA ILE A 58 4685 3819 3825 475 105 -298 C ATOM 452 C ILE A 58 -36.882 19.418 -12.507 1.00 34.06 C ANISOU 452 C ILE A 58 4968 3996 3978 572 145 -327 C ATOM 453 O ILE A 58 -37.948 19.862 -12.903 1.00 33.95 O ANISOU 453 O ILE A 58 4954 3966 3980 647 184 -305 O ATOM 454 CB ILE A 58 -36.003 17.110 -13.195 1.00 30.94 C ANISOU 454 CB ILE A 58 4411 3722 3625 476 105 -261 C ATOM 455 CG1 ILE A 58 -35.399 16.372 -14.378 1.00 31.67 C ANISOU 455 CG1 ILE A 58 4421 3838 3774 411 80 -232 C ATOM 456 CG2 ILE A 58 -37.454 16.614 -12.962 1.00 32.48 C ANISOU 456 CG2 ILE A 58 4572 3962 3808 548 172 -218 C ATOM 457 CD1 ILE A 58 -35.194 14.918 -14.138 1.00 29.44 C ANISOU 457 CD1 ILE A 58 4082 3617 3488 406 65 -209 C ATOM 458 N GLU A 59 -36.503 19.505 -11.222 1.00 35.93 N ANISOU 458 N GLU A 59 5266 4238 4146 581 131 -383 N ATOM 459 CA GLU A 59 -37.357 20.120 -10.203 1.00 39.13 C ANISOU 459 CA GLU A 59 5750 4631 4487 677 180 -421 C ATOM 460 C GLU A 59 -37.617 21.572 -10.571 1.00 39.89 C ANISOU 460 C GLU A 59 5934 4616 4608 714 184 -459 C ATOM 461 O GLU A 59 -38.750 22.069 -10.387 1.00 41.27 O ANISOU 461 O GLU A 59 6130 4780 4770 826 240 -466 O ATOM 462 CB GLU A 59 -36.693 20.097 -8.814 1.00 39.73 C ANISOU 462 CB GLU A 59 5908 4720 4468 673 146 -487 C ATOM 463 CG GLU A 59 -36.570 18.690 -8.234 1.00 45.17 C ANISOU 463 CG GLU A 59 6555 5503 5105 666 145 -443 C ATOM 464 CD GLU A 59 -36.079 18.707 -6.797 1.00 50.22 C ANISOU 464 CD GLU A 59 7302 6158 5621 691 108 -503 C ATOM 465 OE1 GLU A 59 -35.547 19.761 -6.302 1.00 56.97 O ANISOU 465 OE1 GLU A 59 8247 6957 6444 688 58 -596 O ATOM 466 OE2 GLU A 59 -36.298 17.668 -6.115 1.00 60.46 O ANISOU 466 OE2 GLU A 59 8610 7519 6842 716 133 -458 O ATOM 467 N ARG A 60 -36.575 22.226 -11.077 1.00 38.79 N ANISOU 467 N ARG A 60 5843 4391 4503 622 129 -486 N ATOM 468 CA ARG A 60 -36.632 23.647 -11.434 1.00 41.26 C ANISOU 468 CA ARG A 60 6278 4562 4836 635 128 -519 C ATOM 469 C ARG A 60 -37.404 23.893 -12.711 1.00 40.28 C ANISOU 469 C ARG A 60 6139 4401 4763 686 152 -444 C ATOM 470 O ARG A 60 -37.918 24.975 -12.902 1.00 40.45 O ANISOU 470 O ARG A 60 6269 4312 4786 760 161 -456 O ATOM 471 CB ARG A 60 -35.222 24.262 -11.508 1.00 41.58 C ANISOU 471 CB ARG A 60 6381 4520 4898 491 74 -577 C ATOM 472 CG ARG A 60 -34.656 24.384 -10.076 1.00 46.55 C ANISOU 472 CG ARG A 60 7062 5164 5461 479 32 -681 C ATOM 473 CD ARG A 60 -33.196 24.660 -10.041 1.00 55.32 C ANISOU 473 CD ARG A 60 8174 6246 6602 325 -36 -753 C ATOM 474 NE ARG A 60 -32.992 26.060 -9.725 1.00 64.86 N ANISOU 474 NE ARG A 60 9536 7302 7807 293 -46 -839 N ATOM 475 CZ ARG A 60 -32.781 26.555 -8.510 1.00 61.87 C ANISOU 475 CZ ARG A 60 9249 6897 7362 309 -89 -950 C ATOM 476 NH1 ARG A 60 -32.696 25.780 -7.439 1.00 60.76 N ANISOU 476 NH1 ARG A 60 9069 6878 7139 361 -129 -985 N ATOM 477 NH2 ARG A 60 -32.622 27.843 -8.405 1.00 65.23 N ANISOU 477 NH2 ARG A 60 9823 7163 7799 270 -94 -1026 N ATOM 478 N ASN A 61 -37.486 22.862 -13.566 1.00 37.72 N ANISOU 478 N ASN A 61 5690 4167 4474 655 153 -371 N ATOM 479 CA ASN A 61 -38.199 22.955 -14.844 1.00 38.40 C ANISOU 479 CA ASN A 61 5755 4239 4597 705 157 -301 C ATOM 480 C ASN A 61 -39.343 21.973 -14.971 1.00 37.26 C ANISOU 480 C ASN A 61 5472 4220 4464 788 181 -261 C ATOM 481 O ASN A 61 -39.696 21.552 -16.071 1.00 36.53 O ANISOU 481 O ASN A 61 5315 4162 4402 793 166 -206 O ATOM 482 CB ASN A 61 -37.189 22.760 -15.981 1.00 37.39 C ANISOU 482 CB ASN A 61 5618 4090 4499 574 135 -261 C ATOM 483 CG ASN A 61 -36.079 23.808 -15.942 1.00 38.25 C ANISOU 483 CG ASN A 61 5854 4070 4610 466 127 -304 C ATOM 484 OD1 ASN A 61 -34.966 23.587 -15.399 1.00 38.39 O ANISOU 484 OD1 ASN A 61 5844 4111 4633 353 110 -359 O ATOM 485 ND2 ASN A 61 -36.395 24.953 -16.422 1.00 36.96 N ANISOU 485 ND2 ASN A 61 5832 3771 4442 503 133 -289 N ATOM 486 N SER A 62 -39.943 21.635 -13.826 1.00 38.77 N ANISOU 486 N SER A 62 5626 4480 4626 849 223 -296 N ATOM 487 CA SER A 62 -40.803 20.431 -13.756 1.00 38.30 C ANISOU 487 CA SER A 62 5420 4553 4580 873 262 -263 C ATOM 488 C SER A 62 -42.001 20.501 -14.750 1.00 36.76 C ANISOU 488 C SER A 62 5142 4391 4434 965 260 -233 C ATOM 489 O SER A 62 -42.269 19.571 -15.496 1.00 35.87 O ANISOU 489 O SER A 62 4918 4353 4359 929 248 -192 O ATOM 490 CB SER A 62 -41.273 20.238 -12.299 1.00 39.17 C ANISOU 490 CB SER A 62 5533 4718 4633 921 329 -306 C ATOM 491 OG SER A 62 -42.331 19.317 -12.223 1.00 42.35 O ANISOU 491 OG SER A 62 5804 5233 5054 948 392 -281 O ATOM 492 N GLU A 63 -42.737 21.610 -14.711 1.00 36.48 N ANISOU 492 N GLU A 63 5162 4302 4397 1095 263 -264 N ATOM 493 CA GLU A 63 -43.857 21.789 -15.618 1.00 36.42 C ANISOU 493 CA GLU A 63 5078 4327 4432 1209 238 -246 C ATOM 494 C GLU A 63 -43.423 21.826 -17.107 1.00 34.24 C ANISOU 494 C GLU A 63 4836 4002 4172 1166 159 -184 C ATOM 495 O GLU A 63 -43.997 21.134 -17.945 1.00 33.87 O ANISOU 495 O GLU A 63 4672 4040 4157 1176 129 -155 O ATOM 496 CB GLU A 63 -44.623 23.038 -15.250 1.00 37.35 C ANISOU 496 CB GLU A 63 5269 4381 4541 1378 246 -298 C ATOM 497 CG GLU A 63 -45.803 23.270 -16.112 1.00 42.08 C ANISOU 497 CG GLU A 63 5782 5023 5183 1525 203 -292 C ATOM 498 CD GLU A 63 -46.797 22.105 -16.053 1.00 48.21 C ANISOU 498 CD GLU A 63 6321 5986 6008 1525 244 -302 C ATOM 499 OE1 GLU A 63 -46.766 21.266 -15.095 1.00 49.57 O ANISOU 499 OE1 GLU A 63 6418 6243 6172 1438 332 -319 O ATOM 500 OE2 GLU A 63 -47.583 22.026 -17.006 1.00 45.82 O ANISOU 500 OE2 GLU A 63 5920 5740 5749 1604 181 -293 O ATOM 501 N THR A 64 -42.389 22.587 -17.431 1.00 32.91 N ANISOU 501 N THR A 64 4827 3700 3976 1105 132 -168 N ATOM 502 CA THR A 64 -41.991 22.706 -18.829 1.00 33.36 C ANISOU 502 CA THR A 64 4941 3706 4030 1065 78 -107 C ATOM 503 C THR A 64 -41.505 21.303 -19.355 1.00 32.44 C ANISOU 503 C THR A 64 4698 3699 3930 937 76 -76 C ATOM 504 O THR A 64 -41.811 20.909 -20.482 1.00 31.09 O ANISOU 504 O THR A 64 4485 3567 3762 947 34 -37 O ATOM 505 CB THR A 64 -40.893 23.796 -18.982 1.00 34.07 C ANISOU 505 CB THR A 64 5230 3626 4088 991 76 -99 C ATOM 506 OG1 THR A 64 -41.423 25.071 -18.593 1.00 34.61 O ANISOU 506 OG1 THR A 64 5434 3575 4143 1121 70 -128 O ATOM 507 CG2 THR A 64 -40.405 23.886 -20.470 1.00 34.59 C ANISOU 507 CG2 THR A 64 5370 3640 4132 929 44 -26 C ATOM 508 N PHE A 65 -40.800 20.557 -18.492 1.00 32.07 N ANISOU 508 N PHE A 65 4600 3697 3888 835 114 -101 N ATOM 509 CA PHE A 65 -40.397 19.155 -18.845 1.00 32.60 C ANISOU 509 CA PHE A 65 4553 3859 3975 736 113 -82 C ATOM 510 C PHE A 65 -41.589 18.262 -19.101 1.00 32.69 C ANISOU 510 C PHE A 65 4421 3980 4018 789 110 -74 C ATOM 511 O PHE A 65 -41.570 17.521 -20.074 1.00 32.09 O ANISOU 511 O PHE A 65 4289 3949 3957 748 78 -50 O ATOM 512 CB PHE A 65 -39.452 18.532 -17.786 1.00 31.19 C ANISOU 512 CB PHE A 65 4361 3701 3788 645 140 -110 C ATOM 513 CG PHE A 65 -38.011 18.893 -17.982 1.00 32.15 C ANISOU 513 CG PHE A 65 4557 3758 3900 542 125 -122 C ATOM 514 CD1 PHE A 65 -37.637 19.990 -18.784 1.00 35.87 C ANISOU 514 CD1 PHE A 65 5138 4128 4361 523 116 -108 C ATOM 515 CD2 PHE A 65 -37.018 18.163 -17.344 1.00 31.11 C ANISOU 515 CD2 PHE A 65 4389 3663 3768 462 121 -149 C ATOM 516 CE1 PHE A 65 -36.285 20.332 -18.977 1.00 37.14 C ANISOU 516 CE1 PHE A 65 5351 4237 4523 401 121 -127 C ATOM 517 CE2 PHE A 65 -35.657 18.488 -17.539 1.00 35.04 C ANISOU 517 CE2 PHE A 65 4921 4121 4272 362 106 -177 C ATOM 518 CZ PHE A 65 -35.284 19.599 -18.338 1.00 35.46 C ANISOU 518 CZ PHE A 65 5066 4082 4325 319 115 -170 C ATOM 519 N THR A 66 -42.615 18.354 -18.246 1.00 34.01 N ANISOU 519 N THR A 66 4530 4195 4198 874 147 -104 N ATOM 520 CA THR A 66 -43.864 17.593 -18.438 1.00 35.00 C ANISOU 520 CA THR A 66 4497 4434 4369 916 155 -111 C ATOM 521 C THR A 66 -44.594 17.964 -19.719 1.00 36.55 C ANISOU 521 C THR A 66 4661 4643 4581 1002 78 -101 C ATOM 522 O THR A 66 -44.967 17.051 -20.498 1.00 33.94 O ANISOU 522 O THR A 66 4225 4391 4282 965 42 -94 O ATOM 523 CB THR A 66 -44.817 17.750 -17.220 1.00 38.13 C ANISOU 523 CB THR A 66 4830 4884 4772 990 233 -155 C ATOM 524 OG1 THR A 66 -44.120 17.365 -16.043 1.00 37.39 O ANISOU 524 OG1 THR A 66 4789 4778 4639 914 296 -160 O ATOM 525 CG2 THR A 66 -46.163 16.964 -17.357 1.00 38.22 C ANISOU 525 CG2 THR A 66 4647 5029 4846 1013 259 -177 C ATOM 526 N GLU A 67 -44.781 19.282 -19.975 1.00 36.02 N ANISOU 526 N GLU A 67 4703 4494 4489 1120 41 -100 N ATOM 527 CA GLU A 67 -45.474 19.739 -21.188 1.00 38.25 C ANISOU 527 CA GLU A 67 4987 4778 4768 1231 -51 -84 C ATOM 528 C GLU A 67 -44.704 19.379 -22.449 1.00 36.76 C ANISOU 528 C GLU A 67 4864 4561 4542 1144 -106 -32 C ATOM 529 O GLU A 67 -45.302 18.924 -23.421 1.00 37.67 O ANISOU 529 O GLU A 67 4904 4748 4662 1176 -176 -28 O ATOM 530 CB GLU A 67 -45.705 21.287 -21.209 1.00 39.26 C ANISOU 530 CB GLU A 67 5269 4786 4863 1384 -83 -83 C ATOM 531 CG GLU A 67 -46.565 21.829 -20.043 1.00 46.13 C ANISOU 531 CG GLU A 67 6087 5680 5762 1511 -31 -149 C ATOM 532 CD GLU A 67 -46.795 23.367 -20.174 1.00 48.97 C ANISOU 532 CD GLU A 67 6621 5898 6089 1681 -77 -152 C ATOM 533 OE1 GLU A 67 -47.507 23.803 -21.116 1.00 58.03 O ANISOU 533 OE1 GLU A 67 7776 7041 7231 1825 -172 -137 O ATOM 534 OE2 GLU A 67 -46.240 24.117 -19.370 1.00 49.52 O ANISOU 534 OE2 GLU A 67 6829 5854 6133 1672 -27 -171 O ATOM 535 N THR A 68 -43.409 19.661 -22.480 1.00 35.72 N ANISOU 535 N THR A 68 4873 4330 4370 1040 -76 -1 N ATOM 536 CA THR A 68 -42.624 19.333 -23.702 1.00 35.63 C ANISOU 536 CA THR A 68 4922 4299 4315 952 -107 43 C ATOM 537 C THR A 68 -42.644 17.822 -23.978 1.00 34.26 C ANISOU 537 C THR A 68 4598 4244 4175 866 -110 27 C ATOM 538 O THR A 68 -42.819 17.428 -25.109 1.00 31.33 O ANISOU 538 O THR A 68 4215 3910 3778 868 -166 41 O ATOM 539 CB THR A 68 -41.161 19.827 -23.654 1.00 33.79 C ANISOU 539 CB THR A 68 4835 3958 4048 833 -56 66 C ATOM 540 OG1 THR A 68 -40.594 19.458 -22.417 1.00 34.98 O ANISOU 540 OG1 THR A 68 4933 4123 4235 758 2 26 O ATOM 541 CG2 THR A 68 -41.105 21.411 -23.810 1.00 36.12 C ANISOU 541 CG2 THR A 68 5329 4098 4295 903 -65 95 C ATOM 542 N TRP A 69 -42.459 16.992 -22.907 1.00 32.49 N ANISOU 542 N TRP A 69 4277 4068 3999 794 -50 -4 N ATOM 543 CA TRP A 69 -42.502 15.522 -23.056 1.00 31.84 C ANISOU 543 CA TRP A 69 4072 4072 3952 712 -47 -20 C ATOM 544 C TRP A 69 -43.895 15.097 -23.590 1.00 33.65 C ANISOU 544 C TRP A 69 4171 4396 4218 779 -102 -44 C ATOM 545 O TRP A 69 -44.014 14.359 -24.603 1.00 34.50 O ANISOU 545 O TRP A 69 4236 4550 4323 747 -156 -50 O ATOM 546 CB TRP A 69 -42.109 14.780 -21.727 1.00 30.75 C ANISOU 546 CB TRP A 69 3889 3949 3846 639 24 -37 C ATOM 547 CG TRP A 69 -42.272 13.322 -21.928 1.00 33.65 C ANISOU 547 CG TRP A 69 4155 4379 4250 566 24 -48 C ATOM 548 CD1 TRP A 69 -43.250 12.504 -21.363 1.00 35.32 C ANISOU 548 CD1 TRP A 69 4250 4657 4512 552 56 -67 C ATOM 549 CD2 TRP A 69 -41.590 12.510 -22.919 1.00 33.23 C ANISOU 549 CD2 TRP A 69 4108 4328 4188 497 -10 -46 C ATOM 550 NE1 TRP A 69 -43.136 11.208 -21.898 1.00 35.49 N ANISOU 550 NE1 TRP A 69 4221 4703 4560 469 39 -75 N ATOM 551 CE2 TRP A 69 -42.146 11.194 -22.847 1.00 35.74 C ANISOU 551 CE2 TRP A 69 4326 4698 4555 445 -5 -67 C ATOM 552 CE3 TRP A 69 -40.527 12.767 -23.848 1.00 31.12 C ANISOU 552 CE3 TRP A 69 3927 4022 3874 467 -30 -34 C ATOM 553 CZ2 TRP A 69 -41.683 10.136 -23.660 1.00 34.21 C ANISOU 553 CZ2 TRP A 69 4124 4508 4366 381 -34 -81 C ATOM 554 CZ3 TRP A 69 -40.079 11.756 -24.654 1.00 31.93 C ANISOU 554 CZ3 TRP A 69 4009 4147 3976 409 -49 -49 C ATOM 555 CH2 TRP A 69 -40.662 10.431 -24.567 1.00 30.87 C ANISOU 555 CH2 TRP A 69 3781 4056 3892 374 -58 -76 C ATOM 556 N ASN A 70 -44.959 15.569 -22.931 1.00 34.86 N ANISOU 556 N ASN A 70 4253 4587 4405 874 -90 -70 N ATOM 557 CA ASN A 70 -46.317 15.303 -23.374 1.00 38.69 C ANISOU 557 CA ASN A 70 4588 5177 4937 946 -145 -109 C ATOM 558 C ASN A 70 -46.585 15.708 -24.826 1.00 38.66 C ANISOU 558 C ASN A 70 4625 5175 4887 1028 -267 -98 C ATOM 559 O ASN A 70 -47.148 14.928 -25.561 1.00 39.51 O ANISOU 559 O ASN A 70 4626 5368 5018 1010 -331 -129 O ATOM 560 CB ASN A 70 -47.363 15.949 -22.435 1.00 40.39 C ANISOU 560 CB ASN A 70 4718 5434 5193 1059 -105 -148 C ATOM 561 CG ASN A 70 -47.426 15.218 -21.062 1.00 46.77 C ANISOU 561 CG ASN A 70 5447 6281 6042 968 20 -168 C ATOM 562 OD1 ASN A 70 -46.585 14.507 -20.606 0.00 60.91 O ANISOU 562 OD1 ASN A 70 7286 8037 7820 848 73 -143 O ATOM 563 ND2 ASN A 70 -48.334 15.724 -20.160 1.00 53.53 N ANISOU 563 ND2 ASN A 70 6225 7188 6928 1058 81 -210 N ATOM 564 N ARG A 71 -46.197 16.895 -25.268 1.00 39.92 N ANISOU 564 N ARG A 71 4954 5238 4976 1114 -303 -55 N ATOM 565 CA ARG A 71 -46.436 17.179 -26.690 1.00 41.89 C ANISOU 565 CA ARG A 71 5269 5488 5159 1190 -421 -34 C ATOM 566 C ARG A 71 -45.594 16.338 -27.653 1.00 40.84 C ANISOU 566 C ARG A 71 5185 5357 4975 1066 -434 -14 C ATOM 567 O ARG A 71 -46.091 15.898 -28.707 1.00 40.62 O ANISOU 567 O ARG A 71 5119 5398 4919 1095 -531 -33 O ATOM 568 CB ARG A 71 -46.367 18.649 -27.030 1.00 44.05 C ANISOU 568 CB ARG A 71 5734 5646 5358 1323 -462 16 C ATOM 569 CG ARG A 71 -45.049 19.274 -26.953 1.00 49.83 C ANISOU 569 CG ARG A 71 6669 6235 6030 1239 -390 76 C ATOM 570 CD ARG A 71 -44.982 20.385 -28.050 1.00 57.80 C ANISOU 570 CD ARG A 71 7897 7135 6928 1341 -464 143 C ATOM 571 NE ARG A 71 -45.510 21.702 -27.671 1.00 61.96 N ANISOU 571 NE ARG A 71 8532 7562 7447 1503 -491 155 N ATOM 572 CZ ARG A 71 -44.897 22.597 -26.874 1.00 66.11 C ANISOU 572 CZ ARG A 71 9192 7951 7975 1480 -412 171 C ATOM 573 NH1 ARG A 71 -43.715 22.352 -26.292 1.00 64.46 N ANISOU 573 NH1 ARG A 71 9008 7701 7782 1298 -304 172 N ATOM 574 NH2 ARG A 71 -45.482 23.775 -26.669 1.00 67.41 N ANISOU 574 NH2 ARG A 71 9470 8017 8128 1650 -452 176 N ATOM 575 N PHE A 72 -44.323 16.128 -27.293 1.00 38.40 N ANISOU 575 N PHE A 72 4956 4981 4652 938 -342 13 N ATOM 576 CA PHE A 72 -43.413 15.288 -28.112 1.00 37.39 C ANISOU 576 CA PHE A 72 4864 4858 4482 823 -334 19 C ATOM 577 C PHE A 72 -44.072 13.910 -28.341 1.00 37.40 C ANISOU 577 C PHE A 72 4700 4970 4541 779 -374 -41 C ATOM 578 O PHE A 72 -44.195 13.450 -29.475 1.00 38.04 O ANISOU 578 O PHE A 72 4789 5091 4574 778 -446 -57 O ATOM 579 CB PHE A 72 -42.061 15.102 -27.365 1.00 35.33 C ANISOU 579 CB PHE A 72 4649 4538 4236 700 -226 30 C ATOM 580 CG PHE A 72 -41.113 14.138 -28.064 1.00 34.81 C ANISOU 580 CG PHE A 72 4591 4491 4146 592 -206 18 C ATOM 581 CD1 PHE A 72 -41.149 12.784 -27.772 1.00 32.42 C ANISOU 581 CD1 PHE A 72 4168 4247 3905 527 -198 -27 C ATOM 582 CD2 PHE A 72 -40.257 14.606 -29.067 1.00 35.14 C ANISOU 582 CD2 PHE A 72 4770 4488 4096 564 -193 52 C ATOM 583 CE1 PHE A 72 -40.254 11.885 -28.419 1.00 37.12 C ANISOU 583 CE1 PHE A 72 4776 4852 4477 447 -181 -49 C ATOM 584 CE2 PHE A 72 -39.341 13.747 -29.706 1.00 35.97 C ANISOU 584 CE2 PHE A 72 4875 4618 4174 475 -160 29 C ATOM 585 CZ PHE A 72 -39.340 12.392 -29.411 1.00 35.91 C ANISOU 585 CZ PHE A 72 4743 4667 4232 427 -161 -25 C ATOM 586 N ILE A 73 -44.474 13.270 -27.240 1.00 36.81 N ANISOU 586 N ILE A 73 4490 4935 4561 737 -322 -76 N ATOM 587 CA ILE A 73 -44.791 11.871 -27.243 1.00 37.45 C ANISOU 587 CA ILE A 73 4443 5082 4704 647 -323 -126 C ATOM 588 C ILE A 73 -46.169 11.669 -27.857 1.00 40.28 C ANISOU 588 C ILE A 73 4670 5541 5094 708 -423 -179 C ATOM 589 O ILE A 73 -46.398 10.654 -28.499 1.00 41.03 O ANISOU 589 O ILE A 73 4699 5683 5206 644 -470 -227 O ATOM 590 CB ILE A 73 -44.608 11.161 -25.852 1.00 36.00 C ANISOU 590 CB ILE A 73 4195 4888 4595 560 -220 -132 C ATOM 591 CG1 ILE A 73 -44.530 9.623 -25.995 1.00 35.34 C ANISOU 591 CG1 ILE A 73 4047 4824 4557 444 -213 -168 C ATOM 592 CG2 ILE A 73 -45.852 11.460 -24.873 1.00 37.04 C ANISOU 592 CG2 ILE A 73 4199 5078 4795 613 -187 -155 C ATOM 593 CD1 ILE A 73 -43.328 9.034 -26.843 1.00 32.74 C ANISOU 593 CD1 ILE A 73 3816 4449 4174 388 -227 -167 C ATOM 594 N THR A 74 -47.047 12.665 -27.741 1.00 42.00 N ANISOU 594 N THR A 74 4854 5788 5316 841 -466 -181 N ATOM 595 CA THR A 74 -48.368 12.580 -28.326 1.00 45.60 C ANISOU 595 CA THR A 74 5165 6355 5807 921 -578 -244 C ATOM 596 C THR A 74 -48.395 12.980 -29.778 1.00 47.64 C ANISOU 596 C THR A 74 5522 6618 5960 1011 -716 -236 C ATOM 597 O THR A 74 -49.379 12.712 -30.454 1.00 51.37 O ANISOU 597 O THR A 74 5878 7193 6450 1066 -836 -300 O ATOM 598 CB THR A 74 -49.446 13.436 -27.571 1.00 46.50 C ANISOU 598 CB THR A 74 5167 6520 5979 1053 -575 -269 C ATOM 599 OG1 THR A 74 -49.042 14.804 -27.531 1.00 47.41 O ANISOU 599 OG1 THR A 74 5454 6539 6020 1180 -580 -207 O ATOM 600 CG2 THR A 74 -49.638 12.912 -26.158 1.00 46.36 C ANISOU 600 CG2 THR A 74 5030 6525 6058 960 -434 -290 C ATOM 601 N HIS A 75 -47.350 13.637 -30.262 1.00 46.36 N ANISOU 601 N HIS A 75 5576 6352 5687 1025 -701 -161 N ATOM 602 CA HIS A 75 -47.319 14.052 -31.640 1.00 47.84 C ANISOU 602 CA HIS A 75 5896 6533 5748 1107 -817 -138 C ATOM 603 C HIS A 75 -46.352 13.226 -32.540 1.00 47.84 C ANISOU 603 C HIS A 75 5991 6516 5669 989 -803 -136 C ATOM 604 O HIS A 75 -46.398 13.365 -33.749 1.00 50.61 O ANISOU 604 O HIS A 75 6445 6882 5904 1045 -900 -130 O ATOM 605 CB HIS A 75 -47.031 15.555 -31.765 1.00 48.11 C ANISOU 605 CB HIS A 75 6131 6460 5690 1232 -822 -53 C ATOM 606 CG HIS A 75 -48.137 16.432 -31.217 1.00 53.07 C ANISOU 606 CG HIS A 75 6683 7109 6370 1401 -878 -70 C ATOM 607 ND1 HIS A 75 -48.938 17.224 -32.022 1.00 59.39 N ANISOU 607 ND1 HIS A 75 7540 7925 7101 1592 -1027 -63 N ATOM 608 CD2 HIS A 75 -48.602 16.602 -29.952 1.00 54.18 C ANISOU 608 CD2 HIS A 75 6694 7269 6625 1419 -806 -101 C ATOM 609 CE1 HIS A 75 -49.823 17.862 -31.280 1.00 56.65 C ANISOU 609 CE1 HIS A 75 7092 7602 6831 1728 -1045 -94 C ATOM 610 NE2 HIS A 75 -49.651 17.492 -30.023 1.00 58.79 N ANISOU 610 NE2 HIS A 75 7244 7880 7213 1620 -904 -120 N ATOM 611 N THR A 76 -45.475 12.412 -31.965 1.00 45.83 N ANISOU 611 N THR A 76 5716 6232 5466 843 -687 -142 N ATOM 612 CA THR A 76 -44.529 11.626 -32.780 1.00 44.22 C ANISOU 612 CA THR A 76 5594 6015 5194 747 -666 -153 C ATOM 613 C THR A 76 -45.179 10.405 -33.403 1.00 45.16 C ANISOU 613 C THR A 76 5598 6221 5339 707 -753 -245 C ATOM 614 O THR A 76 -45.958 9.688 -32.747 1.00 43.96 O ANISOU 614 O THR A 76 5271 6120 5310 663 -761 -304 O ATOM 615 CB THR A 76 -43.229 11.257 -31.993 1.00 42.75 C ANISOU 615 CB THR A 76 5438 5759 5046 628 -521 -131 C ATOM 616 OG1 THR A 76 -42.322 10.621 -32.876 1.00 41.81 O ANISOU 616 OG1 THR A 76 5397 5634 4854 563 -500 -149 O ATOM 617 CG2 THR A 76 -43.474 10.348 -30.809 1.00 38.42 C ANISOU 617 CG2 THR A 76 4738 5226 4633 554 -468 -170 C ATOM 618 N GLU A 77 -44.866 10.181 -34.678 1.00 45.30 N ANISOU 618 N GLU A 77 5723 6253 5236 713 -814 -260 N ATOM 619 CA GLU A 77 -45.172 8.865 -35.330 1.00 47.08 C ANISOU 619 CA GLU A 77 5872 6541 5475 646 -882 -361 C ATOM 620 C GLU A 77 -43.954 7.911 -35.452 1.00 43.88 C ANISOU 620 C GLU A 77 5530 6086 5058 531 -782 -382 C ATOM 621 O GLU A 77 -44.064 6.762 -35.917 1.00 44.09 O ANISOU 621 O GLU A 77 5515 6138 5101 469 -822 -470 O ATOM 622 CB GLU A 77 -45.805 9.095 -36.711 1.00 49.41 C ANISOU 622 CB GLU A 77 6231 6904 5638 744 -1043 -394 C ATOM 623 CG GLU A 77 -46.895 10.239 -36.732 1.00 54.03 C ANISOU 623 CG GLU A 77 6788 7532 6208 904 -1160 -364 C ATOM 624 CD GLU A 77 -47.774 10.210 -37.980 1.00 54.69 C ANISOU 624 CD GLU A 77 6881 7711 6189 1006 -1358 -426 C ATOM 625 OE1 GLU A 77 -48.289 9.529 -37.943 0.00 82.71 O ANISOU 625 OE1 GLU A 77 10300 11316 9808 965 -1406 -503 O ATOM 626 OE2 GLU A 77 -47.244 11.297 -38.817 0.00 84.50 O ANISOU 626 OE2 GLU A 77 10912 11427 9769 1115 -1376 -326 O ATOM 627 N HIS A 78 -42.799 8.400 -35.015 1.00 40.63 N ANISOU 627 N HIS A 78 5211 5601 4624 507 -656 -312 N ATOM 628 C HIS A 78 -40.625 8.180 -34.044 1.00 36.28 C ANISOU 628 C HIS A 78 4723 4948 4113 394 -434 -269 C ATOM 629 O HIS A 78 -39.748 9.073 -34.270 1.00 34.26 O ANISOU 629 O HIS A 78 4581 4658 3778 400 -364 -211 O ATOM 630 CA AHIS A 78 -41.548 7.648 -35.108 0.50 38.45 C ANISOU 630 CA AHIS A 78 4985 5286 4337 423 -558 -333 C ATOM 631 CB AHIS A 78 -40.919 7.752 -36.502 0.50 40.36 C ANISOU 631 CB AHIS A 78 5378 5544 4414 441 -563 -341 C ATOM 632 CG AHIS A 78 -41.090 9.085 -37.156 0.50 41.10 C ANISOU 632 CG AHIS A 78 5607 5636 4374 526 -596 -262 C ATOM 633 ND1AHIS A 78 -41.813 9.254 -38.316 0.50 44.86 N ANISOU 633 ND1AHIS A 78 6158 6164 4722 605 -723 -279 N ATOM 634 CD2AHIS A 78 -40.589 10.306 -36.849 0.50 43.72 C ANISOU 634 CD2AHIS A 78 6036 5908 4669 546 -521 -166 C ATOM 635 CE1AHIS A 78 -41.766 10.521 -38.688 0.50 44.15 C ANISOU 635 CE1AHIS A 78 6218 6040 4518 679 -724 -185 C ATOM 636 NE2AHIS A 78 -41.028 11.184 -37.814 0.50 43.28 N ANISOU 636 NE2AHIS A 78 6125 5855 4465 637 -597 -116 N ATOM 637 CA BHIS A 78 -41.510 7.728 -35.200 0.50 38.27 C ANISOU 637 CA BHIS A 78 4976 5264 4300 428 -559 -329 C ATOM 638 CB BHIS A 78 -40.826 8.215 -36.507 0.50 39.70 C ANISOU 638 CB BHIS A 78 5329 5450 4305 458 -550 -309 C ATOM 639 CG BHIS A 78 -41.660 8.109 -37.752 0.50 39.92 C ANISOU 639 CG BHIS A 78 5405 5543 4220 522 -689 -352 C ATOM 640 ND1BHIS A 78 -41.536 7.071 -38.652 0.50 44.04 N ANISOU 640 ND1BHIS A 78 5948 6101 4685 491 -727 -444 N ATOM 641 CD2BHIS A 78 -42.580 8.951 -38.286 0.50 44.77 C ANISOU 641 CD2BHIS A 78 6067 6191 4753 627 -808 -320 C ATOM 642 CE1BHIS A 78 -42.370 7.249 -39.663 0.50 41.05 C ANISOU 642 CE1BHIS A 78 5620 5783 4194 565 -869 -471 C ATOM 643 NE2BHIS A 78 -43.021 8.383 -39.463 0.50 44.82 N ANISOU 643 NE2BHIS A 78 6111 6263 4656 655 -925 -394 N ATOM 644 N VAL A 79 -40.842 7.626 -32.851 1.00 33.56 N ANISOU 644 N VAL A 79 4266 4586 3901 352 -405 -281 N ATOM 645 CA VAL A 79 -40.243 8.163 -31.655 1.00 32.59 C ANISOU 645 CA VAL A 79 4137 4412 3833 338 -315 -228 C ATOM 646 C VAL A 79 -38.709 8.310 -31.743 1.00 31.26 C ANISOU 646 C VAL A 79 4048 4208 3622 300 -222 -215 C ATOM 647 O VAL A 79 -38.148 9.345 -31.378 1.00 29.28 O ANISOU 647 O VAL A 79 3850 3924 3351 304 -167 -162 O ATOM 648 CB VAL A 79 -40.584 7.346 -30.392 1.00 34.04 C ANISOU 648 CB VAL A 79 4212 4580 4141 294 -291 -245 C ATOM 649 CG1 VAL A 79 -40.062 8.139 -29.163 1.00 34.41 C ANISOU 649 CG1 VAL A 79 4271 4583 4218 300 -215 -188 C ATOM 650 CG2 VAL A 79 -42.092 7.243 -30.268 1.00 39.69 C ANISOU 650 CG2 VAL A 79 4824 5345 4910 313 -360 -267 C ATOM 651 N ASP A 80 -38.036 7.249 -32.166 1.00 31.01 N ANISOU 651 N ASP A 80 4012 4182 3588 261 -203 -274 N ATOM 652 CA ASP A 80 -36.559 7.242 -32.128 1.00 29.90 C ANISOU 652 CA ASP A 80 3903 4026 3433 229 -110 -283 C ATOM 653 C ASP A 80 -36.015 8.268 -33.140 1.00 30.99 C ANISOU 653 C ASP A 80 4149 4176 3448 229 -66 -249 C ATOM 654 O ASP A 80 -35.099 9.000 -32.797 1.00 32.40 O ANISOU 654 O ASP A 80 4350 4334 3624 197 16 -220 O ATOM 655 CB ASP A 80 -35.965 5.823 -32.322 1.00 28.34 C ANISOU 655 CB ASP A 80 3673 3828 3267 209 -101 -364 C ATOM 656 CG ASP A 80 -36.497 5.091 -33.568 1.00 32.22 C ANISOU 656 CG ASP A 80 4198 4350 3695 217 -163 -427 C ATOM 657 OD1 ASP A 80 -37.404 5.588 -34.306 1.00 31.70 O ANISOU 657 OD1 ASP A 80 4169 4316 3558 242 -230 -411 O ATOM 658 OD2 ASP A 80 -35.948 4.012 -33.843 1.00 34.15 O ANISOU 658 OD2 ASP A 80 4437 4584 3953 209 -150 -501 O ATOM 659 N LEU A 81 -36.593 8.362 -34.331 1.00 31.83 N ANISOU 659 N LEU A 81 4331 4314 3450 260 -119 -253 N ATOM 660 CA LEU A 81 -36.190 9.405 -35.286 1.00 33.89 C ANISOU 660 CA LEU A 81 4730 4573 3572 263 -75 -202 C ATOM 661 C LEU A 81 -36.396 10.836 -34.720 1.00 34.52 C ANISOU 661 C LEU A 81 4868 4597 3652 279 -61 -109 C ATOM 662 O LEU A 81 -35.567 11.713 -34.911 1.00 33.90 O ANISOU 662 O LEU A 81 4882 4483 3517 235 31 -64 O ATOM 663 CB LEU A 81 -36.921 9.304 -36.659 1.00 35.30 C ANISOU 663 CB LEU A 81 5005 4794 3614 315 -160 -214 C ATOM 664 CG LEU A 81 -36.674 8.048 -37.519 1.00 40.64 C ANISOU 664 CG LEU A 81 5674 5521 4247 302 -171 -313 C ATOM 665 CD1 LEU A 81 -37.617 7.871 -38.809 1.00 38.94 C ANISOU 665 CD1 LEU A 81 5546 5355 3895 363 -295 -343 C ATOM 666 CD2 LEU A 81 -35.146 7.974 -37.928 1.00 43.82 C ANISOU 666 CD2 LEU A 81 6120 5934 4595 243 -18 -337 C ATOM 667 N ASP A 82 -37.523 11.072 -34.080 1.00 34.40 N ANISOU 667 N ASP A 82 4802 4570 3698 340 -148 -87 N ATOM 668 CA ASP A 82 -37.817 12.418 -33.568 1.00 35.89 C ANISOU 668 CA ASP A 82 5056 4697 3884 378 -145 -11 C ATOM 669 C ASP A 82 -36.891 12.836 -32.389 1.00 34.09 C ANISOU 669 C ASP A 82 4796 4417 3740 311 -47 1 C ATOM 670 O ASP A 82 -36.616 14.033 -32.234 1.00 34.86 O ANISOU 670 O ASP A 82 4994 4444 3806 304 -5 58 O ATOM 671 CB ASP A 82 -39.289 12.543 -33.226 1.00 34.68 C ANISOU 671 CB ASP A 82 4840 4562 3774 476 -260 -7 C ATOM 672 CG ASP A 82 -40.155 12.525 -34.473 1.00 40.02 C ANISOU 672 CG ASP A 82 5576 5285 4345 556 -374 -12 C ATOM 673 OD1 ASP A 82 -39.630 12.776 -35.563 1.00 43.34 O ANISOU 673 OD1 ASP A 82 6139 5697 4631 549 -354 12 O ATOM 674 OD2 ASP A 82 -41.356 12.243 -34.382 1.00 41.13 O ANISOU 674 OD2 ASP A 82 5618 5477 4532 625 -482 -45 O ATOM 675 N PHE A 83 -36.445 11.882 -31.561 1.00 32.89 N ANISOU 675 N PHE A 83 4518 4290 3688 267 -21 -54 N ATOM 676 CA PHE A 83 -35.396 12.162 -30.550 1.00 31.80 C ANISOU 676 CA PHE A 83 4348 4119 3615 205 58 -59 C ATOM 677 C PHE A 83 -34.174 12.766 -31.230 1.00 33.97 C ANISOU 677 C PHE A 83 4704 4381 3824 128 155 -51 C ATOM 678 O PHE A 83 -33.670 13.788 -30.782 1.00 31.77 O ANISOU 678 O PHE A 83 4474 4046 3552 84 207 -22 O ATOM 679 CB PHE A 83 -34.947 10.931 -29.740 1.00 30.68 C ANISOU 679 CB PHE A 83 4082 4009 3567 183 62 -120 C ATOM 680 CG PHE A 83 -35.664 10.792 -28.437 1.00 28.58 C ANISOU 680 CG PHE A 83 3752 3726 3382 216 24 -112 C ATOM 681 CD1 PHE A 83 -36.788 9.984 -28.312 1.00 27.52 C ANISOU 681 CD1 PHE A 83 3559 3614 3282 251 -36 -123 C ATOM 682 CD2 PHE A 83 -35.230 11.513 -27.333 1.00 33.44 C ANISOU 682 CD2 PHE A 83 4370 4304 4032 202 55 -97 C ATOM 683 CE1 PHE A 83 -37.460 9.914 -27.092 1.00 29.26 C ANISOU 683 CE1 PHE A 83 3727 3823 3568 271 -46 -111 C ATOM 684 CE2 PHE A 83 -35.898 11.432 -26.097 1.00 31.49 C ANISOU 684 CE2 PHE A 83 4080 4044 3840 236 33 -88 C ATOM 685 CZ PHE A 83 -37.011 10.623 -26.007 1.00 29.79 C ANISOU 685 CZ PHE A 83 3809 3855 3653 269 -9 -92 C ATOM 686 N ASN A 84 -33.712 12.117 -32.320 1.00 34.68 N ANISOU 686 N ASN A 84 4806 4521 3849 106 185 -86 N ATOM 687 CA ASN A 84 -32.584 12.637 -33.091 1.00 37.77 C ANISOU 687 CA ASN A 84 5270 4915 4166 23 299 -83 C ATOM 688 C ASN A 84 -32.858 14.034 -33.671 1.00 37.14 C ANISOU 688 C ASN A 84 5370 4760 3981 14 324 9 C ATOM 689 O ASN A 84 -32.000 14.941 -33.582 1.00 35.62 O ANISOU 689 O ASN A 84 5236 4520 3780 -79 426 33 O ATOM 690 CB ASN A 84 -32.039 11.548 -34.123 1.00 38.01 C ANISOU 690 CB ASN A 84 5273 5026 4143 12 337 -154 C ATOM 691 CG ASN A 84 -31.296 10.286 -33.351 1.00 45.86 C ANISOU 691 CG ASN A 84 6094 6070 5262 10 342 -252 C ATOM 692 OD1 ASN A 84 -30.051 10.102 -33.508 1.00 51.86 O ANISOU 692 OD1 ASN A 84 6796 6875 6034 -46 439 -311 O ATOM 693 ND2 ASN A 84 -32.068 9.459 -32.489 1.00 42.15 N ANISOU 693 ND2 ASN A 84 5546 5588 4883 72 239 -269 N ATOM 694 N SER A 85 -34.084 14.274 -34.166 1.00 37.68 N ANISOU 694 N SER A 85 5528 4809 3979 111 224 59 N ATOM 695 CA SER A 85 -34.479 15.668 -34.561 1.00 39.44 C ANISOU 695 CA SER A 85 5943 4937 4107 137 222 156 C ATOM 696 C SER A 85 -34.461 16.748 -33.478 1.00 39.66 C ANISOU 696 C SER A 85 5996 4865 4208 124 238 194 C ATOM 697 O SER A 85 -33.985 17.874 -33.738 1.00 40.70 O ANISOU 697 O SER A 85 6285 4900 4278 64 314 255 O ATOM 698 CB SER A 85 -35.825 15.759 -35.295 1.00 39.45 C ANISOU 698 CB SER A 85 6030 4942 4016 273 88 195 C ATOM 699 OG SER A 85 -35.740 15.013 -36.518 1.00 44.77 O ANISOU 699 OG SER A 85 6742 5691 4579 275 82 167 O ATOM 700 N VAL A 86 -35.027 16.490 -32.299 1.00 38.06 N ANISOU 700 N VAL A 86 5666 4672 4124 178 172 163 N ATOM 701 CA VAL A 86 -34.880 17.507 -31.276 1.00 38.05 C ANISOU 701 CA VAL A 86 5698 4577 4180 159 197 184 C ATOM 702 C VAL A 86 -33.423 17.731 -30.825 1.00 37.23 C ANISOU 702 C VAL A 86 5565 4455 4124 9 314 149 C ATOM 703 O VAL A 86 -33.022 18.876 -30.568 1.00 36.85 O ANISOU 703 O VAL A 86 5627 4304 4071 -52 367 180 O ATOM 704 CB VAL A 86 -35.918 17.485 -30.078 1.00 39.46 C ANISOU 704 CB VAL A 86 5787 4755 4452 263 110 168 C ATOM 705 CG1 VAL A 86 -36.937 16.482 -30.217 1.00 39.14 C ANISOU 705 CG1 VAL A 86 5636 4805 4430 350 20 141 C ATOM 706 CG2 VAL A 86 -35.239 17.573 -28.668 1.00 39.69 C ANISOU 706 CG2 VAL A 86 5731 4765 4583 198 155 123 C ATOM 707 N PHE A 87 -32.637 16.644 -30.768 1.00 35.03 N ANISOU 707 N PHE A 87 5139 4276 3894 -49 349 77 N ATOM 708 CA PHE A 87 -31.223 16.786 -30.465 1.00 34.55 C ANISOU 708 CA PHE A 87 5021 4226 3881 -183 452 27 C ATOM 709 C PHE A 87 -30.501 17.802 -31.410 1.00 36.66 C ANISOU 709 C PHE A 87 5441 4430 4059 -301 573 72 C ATOM 710 O PHE A 87 -29.770 18.713 -30.950 1.00 36.37 O ANISOU 710 O PHE A 87 5438 4324 4058 -412 643 67 O ATOM 711 CB PHE A 87 -30.526 15.422 -30.387 1.00 33.49 C ANISOU 711 CB PHE A 87 4710 4211 3804 -196 461 -62 C ATOM 712 CG PHE A 87 -29.078 15.532 -30.041 1.00 35.20 C ANISOU 712 CG PHE A 87 4832 4461 4081 -317 552 -131 C ATOM 713 CD1 PHE A 87 -28.659 15.357 -28.710 1.00 34.43 C ANISOU 713 CD1 PHE A 87 4612 4378 4091 -318 509 -191 C ATOM 714 CD2 PHE A 87 -28.133 15.848 -31.026 1.00 34.44 C ANISOU 714 CD2 PHE A 87 4769 4387 3930 -431 681 -142 C ATOM 715 CE1 PHE A 87 -27.288 15.494 -28.381 1.00 38.18 C ANISOU 715 CE1 PHE A 87 4979 4898 4630 -426 576 -271 C ATOM 716 CE2 PHE A 87 -26.768 15.991 -30.711 1.00 40.64 C ANISOU 716 CE2 PHE A 87 5437 5220 4786 -555 771 -221 C ATOM 717 CZ PHE A 87 -26.342 15.812 -29.362 1.00 39.71 C ANISOU 717 CZ PHE A 87 5176 5125 4789 -548 707 -292 C ATOM 718 N LEU A 88 -30.733 17.674 -32.716 1.00 37.49 N ANISOU 718 N LEU A 88 5653 4551 4041 -284 597 116 N ATOM 719 CA LEU A 88 -30.179 18.586 -33.707 1.00 40.99 C ANISOU 719 CA LEU A 88 6277 4928 4370 -389 719 177 C ATOM 720 C LEU A 88 -30.571 20.023 -33.533 1.00 41.53 C ANISOU 720 C LEU A 88 6546 4830 4402 -396 718 267 C ATOM 721 O LEU A 88 -29.739 20.891 -33.669 1.00 41.17 O ANISOU 721 O LEU A 88 6596 4706 4340 -542 840 288 O ATOM 722 CB LEU A 88 -30.570 18.173 -35.125 1.00 42.52 C ANISOU 722 CB LEU A 88 6581 5165 4410 -335 720 217 C ATOM 723 CG LEU A 88 -30.010 16.865 -35.564 1.00 44.97 C ANISOU 723 CG LEU A 88 6738 5620 4728 -348 755 125 C ATOM 724 CD1 LEU A 88 -30.404 16.679 -37.071 1.00 48.44 C ANISOU 724 CD1 LEU A 88 7340 6086 4980 -302 762 170 C ATOM 725 CD2 LEU A 88 -28.516 17.047 -35.406 1.00 50.39 C ANISOU 725 CD2 LEU A 88 7337 6339 5471 -517 919 67 C ATOM 726 N GLU A 89 -31.860 20.244 -33.270 1.00 42.28 N ANISOU 726 N GLU A 89 6706 4874 4486 -236 581 314 N ATOM 727 CA GLU A 89 -32.440 21.547 -32.944 1.00 45.50 C ANISOU 727 CA GLU A 89 7296 5118 4874 -189 546 389 C ATOM 728 C GLU A 89 -31.717 22.269 -31.811 1.00 45.59 C ANISOU 728 C GLU A 89 7278 5048 4996 -304 604 349 C ATOM 729 O GLU A 89 -31.544 23.468 -31.864 1.00 45.32 O ANISOU 729 O GLU A 89 7435 4858 4927 -364 655 405 O ATOM 730 CB GLU A 89 -33.947 21.426 -32.614 1.00 44.48 C ANISOU 730 CB GLU A 89 7154 4993 4754 21 380 406 C ATOM 731 CG GLU A 89 -34.768 21.060 -33.848 1.00 52.90 C ANISOU 731 CG GLU A 89 8305 6106 5689 139 303 455 C ATOM 732 CD GLU A 89 -34.843 22.224 -34.905 1.00 60.36 C ANISOU 732 CD GLU A 89 9559 6908 6468 151 331 572 C ATOM 733 OE1 GLU A 89 -34.277 23.352 -34.712 1.00 64.55 O ANISOU 733 OE1 GLU A 89 10253 7285 6989 56 422 622 O ATOM 734 OE2 GLU A 89 -35.534 22.027 -35.929 1.00 67.45 O ANISOU 734 OE2 GLU A 89 10553 7838 7238 263 252 616 O ATOM 735 N ILE A 90 -31.319 21.510 -30.787 1.00 46.05 N ANISOU 735 N ILE A 90 7108 5208 5182 -327 585 250 N ATOM 736 CA ILE A 90 -30.577 22.046 -29.635 1.00 46.71 C ANISOU 736 CA ILE A 90 7134 5243 5372 -431 620 189 C ATOM 737 C ILE A 90 -29.089 22.226 -29.937 1.00 48.73 C ANISOU 737 C ILE A 90 7353 5516 5647 -646 764 144 C ATOM 738 O ILE A 90 -28.502 23.229 -29.531 1.00 50.06 O ANISOU 738 O ILE A 90 7596 5574 5849 -773 825 133 O ATOM 739 CB ILE A 90 -30.747 21.136 -28.368 1.00 44.14 C ANISOU 739 CB ILE A 90 6591 5023 5159 -358 530 101 C ATOM 740 CG1 ILE A 90 -32.228 20.940 -28.081 1.00 44.86 C ANISOU 740 CG1 ILE A 90 6698 5110 5237 -166 411 139 C ATOM 741 CG2 ILE A 90 -30.007 21.770 -27.136 1.00 45.25 C ANISOU 741 CG2 ILE A 90 6691 5111 5391 -454 546 31 C ATOM 742 CD1 ILE A 90 -32.575 19.747 -27.150 1.00 43.67 C ANISOU 742 CD1 ILE A 90 6347 5080 5165 -88 337 75 C ATOM 743 N PHE A 91 -28.486 21.251 -30.606 1.00 50.18 N ANISOU 743 N PHE A 91 7411 5838 5818 -687 820 105 N ATOM 744 CA PHE A 91 -27.035 21.211 -30.766 1.00 53.81 C ANISOU 744 CA PHE A 91 7762 6361 6322 -877 956 31 C ATOM 745 C PHE A 91 -26.411 21.566 -32.123 1.00 58.98 C ANISOU 745 C PHE A 91 8538 7003 6868 -1013 1120 78 C ATOM 746 O PHE A 91 -25.191 21.460 -32.271 1.00 62.18 O ANISOU 746 O PHE A 91 8821 7486 7320 -1175 1247 2 O ATOM 747 CB PHE A 91 -26.469 19.916 -30.202 1.00 51.78 C ANISOU 747 CB PHE A 91 7231 6277 6166 -847 916 -86 C ATOM 748 CG PHE A 91 -26.776 19.734 -28.716 1.00 48.84 C ANISOU 748 CG PHE A 91 6753 5907 5898 -763 786 -139 C ATOM 749 CD1 PHE A 91 -26.086 20.485 -27.747 1.00 49.51 C ANISOU 749 CD1 PHE A 91 6801 5944 6066 -871 795 -201 C ATOM 750 CD2 PHE A 91 -27.769 18.826 -28.302 1.00 43.00 C ANISOU 750 CD2 PHE A 91 5961 5213 5165 -587 660 -129 C ATOM 751 CE1 PHE A 91 -26.372 20.311 -26.356 1.00 47.84 C ANISOU 751 CE1 PHE A 91 6510 5738 5928 -785 674 -251 C ATOM 752 CE2 PHE A 91 -28.066 18.629 -26.935 1.00 45.86 C ANISOU 752 CE2 PHE A 91 6243 5579 5603 -513 558 -170 C ATOM 753 CZ PHE A 91 -27.344 19.392 -25.939 1.00 45.65 C ANISOU 753 CZ PHE A 91 6191 5510 5645 -607 563 -231 C ATOM 754 N HIS A 92 -27.216 21.962 -33.109 1.00 62.26 N ANISOU 754 N HIS A 92 9187 7333 7136 -945 1119 196 N ATOM 755 CA HIS A 92 -26.761 22.825 -34.232 1.00 68.24 C ANISOU 755 CA HIS A 92 10168 7996 7764 -1088 1280 280 C ATOM 756 C HIS A 92 -25.232 22.930 -34.532 1.00 70.90 C ANISOU 756 C HIS A 92 10406 8396 8137 -1335 1487 210 C ATOM 757 O HIS A 92 -24.703 22.443 -35.569 1.00 71.24 O ANISOU 757 O HIS A 92 10435 8539 8093 -1396 1612 203 O ATOM 758 CB HIS A 92 -27.082 24.280 -33.807 1.00 70.07 C ANISOU 758 CB HIS A 92 10628 8003 7991 -1128 1273 358 C ATOM 759 CG HIS A 92 -28.393 24.817 -34.269 1.00 72.63 C ANISOU 759 CG HIS A 92 11213 8195 8189 -950 1165 487 C ATOM 760 ND1 HIS A 92 -29.604 24.368 -33.775 1.00 70.87 N ANISOU 760 ND1 HIS A 92 10934 8003 7991 -720 978 486 N ATOM 761 CD2 HIS A 92 -28.680 25.826 -35.130 1.00 75.01 C ANISOU 761 CD2 HIS A 92 11836 8323 8340 -964 1217 618 C ATOM 762 CE1 HIS A 92 -30.586 25.062 -34.329 1.00 73.37 C ANISOU 762 CE1 HIS A 92 11502 8189 8186 -589 908 600 C ATOM 763 NE2 HIS A 92 -30.052 25.945 -35.162 1.00 77.71 N ANISOU 763 NE2 HIS A 92 12297 8607 8621 -723 1043 686 N ATOM 764 N ARG A 93 -24.559 23.662 -33.623 1.00 72.35 N ANISOU 764 N ARG A 93 10533 8513 8445 -1482 1525 154 N ATOM 765 CA ARG A 93 -23.201 24.212 -33.827 1.00 75.55 C ANISOU 765 CA ARG A 93 10892 8921 8892 -1755 1727 100 C ATOM 766 C ARG A 93 -22.078 23.249 -33.389 1.00 75.67 C ANISOU 766 C ARG A 93 10546 9157 9049 -1823 1764 -71 C ATOM 767 O ARG A 93 -22.346 22.206 -32.748 1.00 73.60 O ANISOU 767 O ARG A 93 10085 9020 8861 -1655 1616 -144 O ATOM 768 CB ARG A 93 -23.088 25.550 -33.090 1.00 76.70 C ANISOU 768 CB ARG A 93 11175 8868 9101 -1885 1737 117 C ATOM 769 CG ARG A 93 -23.929 26.701 -33.689 1.00 79.90 C ANISOU 769 CG ARG A 93 11975 9025 9358 -1861 1749 287 C ATOM 770 CD ARG A 93 -25.318 26.910 -33.067 1.00 81.37 C ANISOU 770 CD ARG A 93 12284 9101 9533 -1611 1537 348 C ATOM 771 NE ARG A 93 -25.382 27.986 -32.049 1.00 85.47 N ANISOU 771 NE ARG A 93 12899 9438 10139 -1662 1492 332 N ATOM 772 CZ ARG A 93 -25.677 27.813 -30.747 1.00 85.86 C ANISOU 772 CZ ARG A 93 12796 9516 10312 -1563 1347 242 C ATOM 773 NH1 ARG A 93 -25.930 26.608 -30.251 1.00 84.74 N ANISOU 773 NH1 ARG A 93 12401 9569 10229 -1414 1233 168 N ATOM 774 NH2 ARG A 93 -25.714 28.851 -29.910 1.00 86.71 N ANISOU 774 NH2 ARG A 93 13019 9447 10480 -1614 1318 223 N ATOM 775 N PRO A 96 -21.517 24.613 -28.284 1.00 74.11 N ANISOU 775 N PRO A 96 9990 8822 9349 -1882 1358 -385 N ATOM 776 CA PRO A 96 -22.222 23.618 -27.480 1.00 72.20 C ANISOU 776 CA PRO A 96 9631 8672 9129 -1641 1173 -409 C ATOM 777 C PRO A 96 -22.051 23.880 -25.960 1.00 71.81 C ANISOU 777 C PRO A 96 9490 8610 9186 -1632 1042 -512 C ATOM 778 O PRO A 96 -21.007 23.533 -25.344 1.00 73.66 O ANISOU 778 O PRO A 96 9486 8975 9526 -1711 1023 -655 O ATOM 779 CB PRO A 96 -21.592 22.286 -27.934 1.00 72.00 C ANISOU 779 CB PRO A 96 9362 8867 9128 -1602 1199 -480 C ATOM 780 CG PRO A 96 -21.163 22.562 -29.377 1.00 74.26 C ANISOU 780 CG PRO A 96 9738 9147 9329 -1746 1399 -424 C ATOM 781 CD PRO A 96 -20.976 24.063 -29.545 1.00 75.21 C ANISOU 781 CD PRO A 96 10071 9075 9429 -1951 1511 -370 C ATOM 782 N SER A 97 -23.052 24.514 -25.362 1.00 68.71 N ANISOU 782 N SER A 97 9284 8064 8757 -1530 951 -450 N ATOM 783 CA SER A 97 -22.944 25.016 -23.994 1.00 66.34 C ANISOU 783 CA SER A 97 8962 7715 8529 -1539 847 -540 C ATOM 784 C SER A 97 -23.135 23.879 -22.921 1.00 63.01 C ANISOU 784 C SER A 97 8350 7447 8145 -1355 688 -611 C ATOM 785 O SER A 97 -23.840 22.890 -23.167 1.00 60.69 O ANISOU 785 O SER A 97 8025 7229 7805 -1182 642 -551 O ATOM 786 CB SER A 97 -23.977 26.142 -23.870 1.00 66.84 C ANISOU 786 CB SER A 97 9317 7550 8527 -1487 828 -445 C ATOM 787 OG SER A 97 -24.428 26.331 -22.556 1.00 67.16 O ANISOU 787 OG SER A 97 9367 7555 8596 -1382 697 -501 O ATOM 788 N LEU A 98 -22.485 24.005 -21.760 1.00 60.31 N ANISOU 788 N LEU A 98 7891 7146 7881 -1401 605 -740 N ATOM 789 CA LEU A 98 -22.710 23.064 -20.660 1.00 57.36 C ANISOU 789 CA LEU A 98 7391 6885 7517 -1225 452 -794 C ATOM 790 C LEU A 98 -24.200 22.974 -20.189 1.00 52.97 C ANISOU 790 C LEU A 98 6996 6248 6881 -1017 374 -695 C ATOM 791 O LEU A 98 -24.688 21.918 -19.851 1.00 50.81 O ANISOU 791 O LEU A 98 6651 6068 6585 -856 299 -675 O ATOM 792 CB LEU A 98 -21.830 23.414 -19.466 1.00 58.31 C ANISOU 792 CB LEU A 98 7404 7041 7712 -1306 364 -947 C ATOM 793 CG LEU A 98 -22.166 22.555 -18.228 1.00 60.34 C ANISOU 793 CG LEU A 98 7590 7387 7948 -1111 200 -987 C ATOM 794 CD1 LEU A 98 -21.765 21.065 -18.412 1.00 63.08 C ANISOU 794 CD1 LEU A 98 7733 7921 8315 -1005 159 -1005 C ATOM 795 CD2 LEU A 98 -21.609 23.115 -16.945 1.00 62.04 C ANISOU 795 CD2 LEU A 98 7778 7598 8197 -1161 92 -1122 C ATOM 796 N GLY A 99 -24.869 24.115 -20.163 1.00 52.35 N ANISOU 796 N GLY A 99 7134 5993 6765 -1032 398 -641 N ATOM 797 CA GLY A 99 -26.270 24.225 -19.757 1.00 49.67 C ANISOU 797 CA GLY A 99 6942 5574 6358 -846 341 -561 C ATOM 798 C GLY A 99 -27.179 23.470 -20.714 1.00 46.34 C ANISOU 798 C GLY A 99 6535 5192 5880 -718 364 -442 C ATOM 799 O GLY A 99 -28.103 22.797 -20.271 1.00 43.29 O ANISOU 799 O GLY A 99 6130 4854 5465 -550 297 -410 O ATOM 800 N ARG A 100 -26.880 23.577 -22.012 1.00 45.43 N ANISOU 800 N ARG A 100 6452 5062 5748 -809 463 -386 N ATOM 801 CA ARG A 100 -27.639 22.921 -23.041 1.00 44.76 C ANISOU 801 CA ARG A 100 6390 5016 5602 -706 483 -286 C ATOM 802 C ARG A 100 -27.464 21.435 -22.975 1.00 42.17 C ANISOU 802 C ARG A 100 5862 4865 5297 -633 440 -319 C ATOM 803 O ARG A 100 -28.443 20.717 -23.137 1.00 39.51 O ANISOU 803 O ARG A 100 5524 4564 4923 -489 394 -262 O ATOM 804 CB ARG A 100 -27.290 23.372 -24.468 1.00 46.10 C ANISOU 804 CB ARG A 100 6660 5131 5724 -823 603 -220 C ATOM 805 CG ARG A 100 -27.716 24.786 -24.781 1.00 51.08 C ANISOU 805 CG ARG A 100 7549 5556 6304 -861 646 -147 C ATOM 806 CD ARG A 100 -27.963 24.955 -26.239 1.00 49.78 C ANISOU 806 CD ARG A 100 7527 5343 6044 -875 727 -36 C ATOM 807 NE ARG A 100 -28.421 26.309 -26.479 1.00 55.55 N ANISOU 807 NE ARG A 100 8532 5856 6720 -887 752 41 N ATOM 808 CZ ARG A 100 -29.039 26.705 -27.591 1.00 56.51 C ANISOU 808 CZ ARG A 100 8857 5884 6730 -831 781 163 C ATOM 809 NH1 ARG A 100 -29.337 25.821 -28.548 1.00 55.65 N ANISOU 809 NH1 ARG A 100 8700 5894 6552 -758 782 213 N ATOM 810 NH2 ARG A 100 -29.395 27.976 -27.732 1.00 55.60 N ANISOU 810 NH2 ARG A 100 9009 5550 6565 -834 797 231 N ATOM 811 N ALA A 101 -26.221 21.002 -22.747 1.00 41.62 N ANISOU 811 N ALA A 101 5623 4898 5292 -734 452 -418 N ATOM 812 CA ALA A 101 -25.941 19.581 -22.602 1.00 40.88 C ANISOU 812 CA ALA A 101 5346 4960 5226 -653 402 -461 C ATOM 813 C ALA A 101 -26.752 18.970 -21.425 1.00 38.73 C ANISOU 813 C ALA A 101 5062 4706 4947 -492 283 -458 C ATOM 814 O ALA A 101 -27.363 17.920 -21.570 1.00 38.32 O ANISOU 814 O ALA A 101 4972 4711 4875 -377 249 -419 O ATOM 815 CB ALA A 101 -24.450 19.345 -22.454 1.00 41.08 C ANISOU 815 CB ALA A 101 5188 5091 5329 -771 422 -582 C ATOM 816 N LEU A 102 -26.765 19.652 -20.284 1.00 38.11 N ANISOU 816 N LEU A 102 5029 4573 4880 -494 229 -502 N ATOM 817 CA LEU A 102 -27.434 19.181 -19.114 1.00 35.87 C ANISOU 817 CA LEU A 102 4748 4307 4575 -360 136 -505 C ATOM 818 C LEU A 102 -28.944 19.266 -19.271 1.00 34.63 C ANISOU 818 C LEU A 102 4712 4085 4362 -242 143 -404 C ATOM 819 O LEU A 102 -29.622 18.416 -18.768 1.00 31.70 O ANISOU 819 O LEU A 102 4310 3762 3972 -129 98 -381 O ATOM 820 CB LEU A 102 -27.010 19.973 -17.854 1.00 36.77 C ANISOU 820 CB LEU A 102 4892 4381 4699 -397 79 -591 C ATOM 821 CG LEU A 102 -25.518 19.784 -17.483 1.00 41.17 C ANISOU 821 CG LEU A 102 5293 5030 5319 -496 39 -715 C ATOM 822 CD1 LEU A 102 -25.157 20.673 -16.359 1.00 47.00 C ANISOU 822 CD1 LEU A 102 6077 5719 6062 -544 -22 -806 C ATOM 823 CD2 LEU A 102 -25.215 18.317 -17.140 1.00 39.89 C ANISOU 823 CD2 LEU A 102 4989 5005 5164 -388 -36 -738 C ATOM 824 N ALA A 103 -29.453 20.335 -19.888 1.00 35.45 N ANISOU 824 N ALA A 103 4955 4075 4441 -268 195 -351 N ATOM 825 CA ALA A 103 -30.888 20.455 -20.162 1.00 34.16 C ANISOU 825 CA ALA A 103 4888 3862 4231 -142 192 -265 C ATOM 826 C ALA A 103 -31.338 19.227 -20.976 1.00 32.53 C ANISOU 826 C ALA A 103 4595 3751 4015 -81 190 -215 C ATOM 827 O ALA A 103 -32.324 18.584 -20.628 1.00 30.58 O ANISOU 827 O ALA A 103 4321 3542 3757 30 155 -188 O ATOM 828 CB ALA A 103 -31.178 21.777 -20.937 1.00 34.92 C ANISOU 828 CB ALA A 103 5157 3815 4297 -177 242 -214 C ATOM 829 N TRP A 104 -30.573 18.849 -22.002 1.00 32.44 N ANISOU 829 N TRP A 104 4532 3783 4009 -163 234 -216 N ATOM 830 CA TRP A 104 -30.928 17.695 -22.800 1.00 32.20 C ANISOU 830 CA TRP A 104 4432 3835 3966 -111 229 -184 C ATOM 831 C TRP A 104 -30.826 16.417 -21.954 1.00 32.00 C ANISOU 831 C TRP A 104 4281 3901 3976 -54 174 -226 C ATOM 832 O TRP A 104 -31.702 15.600 -22.019 1.00 30.63 O ANISOU 832 O TRP A 104 4086 3758 3793 28 146 -192 O ATOM 833 CB TRP A 104 -29.991 17.580 -23.992 1.00 35.00 C ANISOU 833 CB TRP A 104 4763 4223 4314 -213 299 -193 C ATOM 834 CG TRP A 104 -29.976 16.246 -24.653 1.00 32.88 C ANISOU 834 CG TRP A 104 4399 4053 4043 -173 292 -199 C ATOM 835 CD1 TRP A 104 -29.051 15.257 -24.474 1.00 33.07 C ANISOU 835 CD1 TRP A 104 4284 4167 4113 -189 286 -270 C ATOM 836 CD2 TRP A 104 -30.956 15.716 -25.570 1.00 33.92 C ANISOU 836 CD2 TRP A 104 4566 4197 4124 -100 278 -143 C ATOM 837 NE1 TRP A 104 -29.378 14.162 -25.243 1.00 32.80 N ANISOU 837 NE1 TRP A 104 4214 4189 4061 -135 279 -259 N ATOM 838 CE2 TRP A 104 -30.528 14.427 -25.932 1.00 30.55 C ANISOU 838 CE2 TRP A 104 4032 3860 3716 -89 274 -185 C ATOM 839 CE3 TRP A 104 -32.154 16.221 -26.117 1.00 35.99 C ANISOU 839 CE3 TRP A 104 4939 4405 4329 -33 256 -69 C ATOM 840 CZ2 TRP A 104 -31.245 13.610 -26.827 1.00 36.35 C ANISOU 840 CZ2 TRP A 104 4771 4627 4412 -32 253 -162 C ATOM 841 CZ3 TRP A 104 -32.877 15.408 -27.014 1.00 35.96 C ANISOU 841 CZ3 TRP A 104 4924 4451 4288 29 226 -47 C ATOM 842 CH2 TRP A 104 -32.419 14.128 -27.347 1.00 34.62 C ANISOU 842 CH2 TRP A 104 4652 4364 4137 19 227 -94 C ATOM 843 N MET A 105 -29.766 16.265 -21.149 1.00 31.62 N ANISOU 843 N MET A 105 4157 3890 3967 -99 152 -301 N ATOM 844 CA MET A 105 -29.628 15.012 -20.388 1.00 31.88 C ANISOU 844 CA MET A 105 4099 3996 4019 -29 90 -331 C ATOM 845 C MET A 105 -30.734 14.905 -19.343 1.00 28.73 C ANISOU 845 C MET A 105 3756 3570 3592 65 51 -294 C ATOM 846 O MET A 105 -31.267 13.817 -19.097 1.00 29.29 O ANISOU 846 O MET A 105 3798 3674 3658 133 27 -270 O ATOM 847 CB MET A 105 -28.233 14.929 -19.702 1.00 31.93 C ANISOU 847 CB MET A 105 4012 4055 4066 -76 53 -427 C ATOM 848 CG MET A 105 -27.002 14.953 -20.707 1.00 37.42 C ANISOU 848 CG MET A 105 4610 4805 4802 -179 109 -484 C ATOM 849 SD MET A 105 -26.860 13.364 -21.500 1.00 38.00 S ANISOU 849 SD MET A 105 4590 4962 4887 -110 108 -486 S ATOM 850 CE MET A 105 -25.904 12.531 -20.194 1.00 36.73 C ANISOU 850 CE MET A 105 4315 4873 4768 -38 -3 -577 C ATOM 851 N ALA A 106 -31.068 16.020 -18.719 1.00 27.79 N ANISOU 851 N ALA A 106 3721 3386 3452 63 55 -296 N ATOM 852 CA ALA A 106 -32.172 16.005 -17.701 1.00 27.75 C ANISOU 852 CA ALA A 106 3769 3363 3413 155 38 -269 C ATOM 853 C ALA A 106 -33.513 15.714 -18.365 1.00 27.56 C ANISOU 853 C ALA A 106 3754 3338 3380 217 66 -199 C ATOM 854 O ALA A 106 -34.326 14.916 -17.829 1.00 27.58 O ANISOU 854 O ALA A 106 3732 3373 3373 279 62 -175 O ATOM 855 CB ALA A 106 -32.218 17.318 -16.943 1.00 27.20 C ANISOU 855 CB ALA A 106 3794 3220 3321 149 39 -301 C ATOM 856 N TRP A 107 -33.710 16.262 -19.570 1.00 26.27 N ANISOU 856 N TRP A 107 3621 3142 3217 195 92 -168 N ATOM 857 CA TRP A 107 -34.971 16.009 -20.273 1.00 26.93 C ANISOU 857 CA TRP A 107 3703 3238 3293 261 96 -114 C ATOM 858 C TRP A 107 -35.124 14.547 -20.626 1.00 25.83 C ANISOU 858 C TRP A 107 3471 3171 3172 266 83 -106 C ATOM 859 O TRP A 107 -36.214 13.972 -20.428 1.00 28.05 O ANISOU 859 O TRP A 107 3717 3481 3459 319 79 -84 O ATOM 860 CB TRP A 107 -35.078 16.916 -21.505 1.00 27.37 C ANISOU 860 CB TRP A 107 3836 3239 3325 248 112 -80 C ATOM 861 CG TRP A 107 -36.407 16.919 -22.115 1.00 28.42 C ANISOU 861 CG TRP A 107 3976 3380 3442 337 93 -36 C ATOM 862 CD1 TRP A 107 -37.556 17.606 -21.665 1.00 30.38 C ANISOU 862 CD1 TRP A 107 4258 3599 3685 439 81 -24 C ATOM 863 CD2 TRP A 107 -36.783 16.239 -23.292 1.00 29.49 C ANISOU 863 CD2 TRP A 107 4075 3564 3566 346 74 -11 C ATOM 864 NE1 TRP A 107 -38.604 17.358 -22.520 1.00 29.02 N ANISOU 864 NE1 TRP A 107 4055 3466 3507 510 48 5 N ATOM 865 CE2 TRP A 107 -38.156 16.541 -23.537 1.00 29.15 C ANISOU 865 CE2 TRP A 107 4037 3526 3514 451 38 14 C ATOM 866 CE3 TRP A 107 -36.082 15.409 -24.212 1.00 29.72 C ANISOU 866 CE3 TRP A 107 4067 3638 3588 283 80 -18 C ATOM 867 CZ2 TRP A 107 -38.849 16.046 -24.671 1.00 27.78 C ANISOU 867 CZ2 TRP A 107 3832 3402 3321 487 -5 32 C ATOM 868 CZ3 TRP A 107 -36.758 14.948 -25.334 1.00 29.45 C ANISOU 868 CZ3 TRP A 107 4023 3642 3526 316 49 2 C ATOM 869 CH2 TRP A 107 -38.147 15.248 -25.552 1.00 27.38 C ANISOU 869 CH2 TRP A 107 3764 3387 3253 416 -1 26 C ATOM 870 N CYS A 108 -34.037 13.921 -21.096 1.00 26.32 N ANISOU 870 N CYS A 108 3489 3262 3247 207 81 -133 N ATOM 871 CA CYS A 108 -34.048 12.476 -21.370 1.00 26.25 C ANISOU 871 CA CYS A 108 3409 3306 3259 216 64 -137 C ATOM 872 C CYS A 108 -34.270 11.630 -20.152 1.00 25.19 C ANISOU 872 C CYS A 108 3255 3183 3135 252 44 -140 C ATOM 873 O CYS A 108 -35.088 10.692 -20.158 1.00 26.07 O ANISOU 873 O CYS A 108 3343 3307 3257 274 43 -117 O ATOM 874 CB CYS A 108 -32.727 12.087 -22.042 1.00 25.36 C ANISOU 874 CB CYS A 108 3255 3223 3159 162 71 -181 C ATOM 875 SG CYS A 108 -32.591 12.756 -23.764 1.00 29.76 S ANISOU 875 SG CYS A 108 3852 3774 3679 111 118 -164 S ATOM 876 N MET A 109 -33.510 11.895 -19.087 1.00 27.43 N ANISOU 876 N MET A 109 3554 3459 3409 251 27 -170 N ATOM 877 CA MET A 109 -33.736 11.149 -17.862 1.00 28.15 C ANISOU 877 CA MET A 109 3660 3553 3484 294 9 -162 C ATOM 878 C MET A 109 -35.198 11.339 -17.378 1.00 27.87 C ANISOU 878 C MET A 109 3655 3507 3429 328 49 -117 C ATOM 879 O MET A 109 -35.870 10.377 -16.957 1.00 28.99 O ANISOU 879 O MET A 109 3792 3655 3568 342 65 -88 O ATOM 880 CB MET A 109 -32.713 11.566 -16.797 1.00 27.92 C ANISOU 880 CB MET A 109 3653 3523 3430 297 -32 -209 C ATOM 881 CG MET A 109 -32.816 10.681 -15.536 1.00 30.07 C ANISOU 881 CG MET A 109 3967 3797 3660 352 -61 -194 C ATOM 882 SD MET A 109 -31.578 11.141 -14.298 1.00 31.90 S ANISOU 882 SD MET A 109 4228 4042 3850 373 -140 -263 S ATOM 883 CE MET A 109 -32.475 12.465 -13.422 1.00 30.76 C ANISOU 883 CE MET A 109 4174 3864 3647 381 -96 -259 C ATOM 884 N HIS A 110 -35.718 12.555 -17.477 1.00 28.82 N ANISOU 884 N HIS A 110 3803 3608 3539 340 72 -116 N ATOM 885 CA HIS A 110 -37.120 12.810 -17.061 1.00 28.42 C ANISOU 885 CA HIS A 110 3757 3563 3479 389 114 -90 C ATOM 886 C HIS A 110 -38.137 12.013 -17.918 1.00 28.87 C ANISOU 886 C HIS A 110 3740 3656 3574 387 126 -62 C ATOM 887 O HIS A 110 -39.139 11.458 -17.387 1.00 28.62 O ANISOU 887 O HIS A 110 3675 3651 3549 399 165 -46 O ATOM 888 CB HIS A 110 -37.452 14.316 -17.109 1.00 29.64 C ANISOU 888 CB HIS A 110 3962 3679 3619 426 124 -102 C ATOM 889 CG HIS A 110 -38.915 14.587 -17.086 1.00 31.29 C ANISOU 889 CG HIS A 110 4144 3909 3836 493 159 -86 C ATOM 890 ND1 HIS A 110 -39.635 14.715 -15.907 1.00 39.38 N ANISOU 890 ND1 HIS A 110 5178 4950 4834 541 208 -96 N ATOM 891 CD2 HIS A 110 -39.815 14.643 -18.092 1.00 29.53 C ANISOU 891 CD2 HIS A 110 3869 3709 3643 524 151 -68 C ATOM 892 CE1 HIS A 110 -40.908 14.895 -16.199 1.00 33.61 C ANISOU 892 CE1 HIS A 110 4385 4256 4129 599 236 -91 C ATOM 893 NE2 HIS A 110 -41.041 14.832 -17.516 1.00 38.82 N ANISOU 893 NE2 HIS A 110 5003 4921 4825 592 191 -75 N ATOM 894 N ALA A 111 -37.863 11.941 -19.234 1.00 27.19 N ANISOU 894 N ALA A 111 3504 3446 3383 363 96 -63 N ATOM 895 CA ALA A 111 -38.722 11.202 -20.161 1.00 26.20 C ANISOU 895 CA ALA A 111 3311 3355 3287 357 87 -52 C ATOM 896 C ALA A 111 -38.675 9.696 -19.814 1.00 26.24 C ANISOU 896 C ALA A 111 3286 3368 3315 316 93 -51 C ATOM 897 O ALA A 111 -39.718 9.035 -19.794 1.00 26.02 O ANISOU 897 O ALA A 111 3206 3364 3317 303 113 -43 O ATOM 898 CB ALA A 111 -38.264 11.423 -21.623 1.00 24.19 C ANISOU 898 CB ALA A 111 3067 3100 3025 342 52 -58 C ATOM 899 N CYS A 112 -37.462 9.169 -19.605 1.00 26.77 N ANISOU 899 N CYS A 112 3386 3412 3373 297 74 -63 N ATOM 900 CA CYS A 112 -37.332 7.766 -19.193 1.00 28.45 C ANISOU 900 CA CYS A 112 3604 3605 3599 277 72 -56 C ATOM 901 C CYS A 112 -38.092 7.456 -17.888 1.00 26.80 C ANISOU 901 C CYS A 112 3424 3386 3372 279 121 -22 C ATOM 902 O CYS A 112 -38.774 6.426 -17.783 1.00 27.73 O ANISOU 902 O CYS A 112 3533 3489 3513 241 149 -2 O ATOM 903 CB CYS A 112 -35.820 7.337 -19.111 1.00 26.87 C ANISOU 903 CB CYS A 112 3431 3387 3391 286 30 -84 C ATOM 904 SG CYS A 112 -35.649 5.549 -18.890 1.00 29.93 S ANISOU 904 SG CYS A 112 3849 3726 3796 285 11 -77 S ATOM 905 N ARG A 113 -37.952 8.329 -16.881 1.00 28.96 N ANISOU 905 N ARG A 113 3742 3661 3599 314 139 -18 N ATOM 906 CA ARG A 113 -38.672 8.152 -15.627 1.00 28.90 C ANISOU 906 CA ARG A 113 3775 3652 3554 320 201 12 C ATOM 907 C ARG A 113 -40.210 8.087 -15.868 1.00 29.76 C ANISOU 907 C ARG A 113 3804 3800 3703 295 270 22 C ATOM 908 O ARG A 113 -40.904 7.209 -15.342 1.00 29.29 O ANISOU 908 O ARG A 113 3745 3737 3647 250 332 50 O ATOM 909 CB ARG A 113 -38.350 9.270 -14.679 1.00 29.62 C ANISOU 909 CB ARG A 113 3925 3746 3584 369 205 -4 C ATOM 910 CG ARG A 113 -39.192 9.317 -13.314 1.00 32.29 C ANISOU 910 CG ARG A 113 4315 4095 3859 386 290 20 C ATOM 911 CD ARG A 113 -38.992 10.693 -12.614 1.00 32.78 C ANISOU 911 CD ARG A 113 4429 4162 3866 444 289 -18 C ATOM 912 NE ARG A 113 -37.561 10.905 -12.283 1.00 34.72 N ANISOU 912 NE ARG A 113 4741 4378 4072 456 201 -48 N ATOM 913 CZ ARG A 113 -37.078 11.998 -11.702 1.00 37.11 C ANISOU 913 CZ ARG A 113 5098 4670 4330 488 175 -95 C ATOM 914 NH1 ARG A 113 -35.768 12.090 -11.403 1.00 31.23 N ANISOU 914 NH1 ARG A 113 4391 3914 3561 487 88 -134 N ATOM 915 NH2 ARG A 113 -37.922 12.978 -11.375 1.00 36.65 N ANISOU 915 NH2 ARG A 113 5056 4617 4254 524 233 -112 N ATOM 916 N THR A 114 -40.720 9.023 -16.637 1.00 29.39 N ANISOU 916 N THR A 114 3691 3791 3687 324 257 -2 N ATOM 917 CA THR A 114 -42.162 9.077 -16.976 1.00 32.77 C ANISOU 917 CA THR A 114 4012 4276 4162 320 298 -12 C ATOM 918 C THR A 114 -42.665 7.824 -17.688 1.00 32.71 C ANISOU 918 C THR A 114 3934 4278 4215 242 293 -13 C ATOM 919 O THR A 114 -43.655 7.231 -17.283 1.00 34.87 O ANISOU 919 O THR A 114 4147 4580 4520 191 362 -10 O ATOM 920 CB THR A 114 -42.488 10.291 -17.846 1.00 32.31 C ANISOU 920 CB THR A 114 3913 4245 4119 389 253 -37 C ATOM 921 OG1 THR A 114 -41.967 11.468 -17.209 1.00 35.85 O ANISOU 921 OG1 THR A 114 4446 4661 4516 451 256 -42 O ATOM 922 CG2 THR A 114 -44.043 10.469 -18.057 1.00 36.02 C ANISOU 922 CG2 THR A 114 4253 4792 4639 418 283 -61 C ATOM 923 N LEU A 115 -41.941 7.396 -18.705 1.00 31.46 N ANISOU 923 N LEU A 115 3789 4092 4071 224 220 -24 N ATOM 924 CA LEU A 115 -42.237 6.151 -19.445 1.00 32.91 C ANISOU 924 CA LEU A 115 3932 4267 4306 150 201 -38 C ATOM 925 C LEU A 115 -42.190 4.911 -18.548 1.00 34.56 C ANISOU 925 C LEU A 115 4200 4416 4517 81 257 -6 C ATOM 926 O LEU A 115 -43.033 4.069 -18.662 1.00 35.55 O ANISOU 926 O LEU A 115 4276 4541 4693 1 291 -13 O ATOM 927 CB LEU A 115 -41.167 5.973 -20.560 1.00 30.58 C ANISOU 927 CB LEU A 115 3674 3945 4002 161 121 -59 C ATOM 928 CG LEU A 115 -41.292 6.932 -21.770 1.00 33.63 C ANISOU 928 CG LEU A 115 4021 4378 4378 208 64 -84 C ATOM 929 CD1 LEU A 115 -40.041 6.913 -22.612 1.00 33.25 C ANISOU 929 CD1 LEU A 115 4030 4304 4298 216 20 -98 C ATOM 930 CD2 LEU A 115 -42.549 6.645 -22.631 1.00 34.88 C ANISOU 930 CD2 LEU A 115 4077 4594 4581 187 32 -118 C ATOM 931 N CYS A 116 -41.171 4.802 -17.683 1.00 35.81 N ANISOU 931 N CYS A 116 4472 4517 4616 112 259 26 N ATOM 932 CA CYS A 116 -40.949 3.579 -16.907 1.00 40.06 C ANISOU 932 CA CYS A 116 5108 4975 5137 67 292 66 C ATOM 933 C CYS A 116 -41.850 3.440 -15.642 1.00 44.80 C ANISOU 933 C CYS A 116 5738 5576 5706 24 407 112 C ATOM 934 O CYS A 116 -42.026 2.303 -15.137 1.00 46.53 O ANISOU 934 O CYS A 116 6038 5722 5920 -45 456 153 O ATOM 935 CB CYS A 116 -39.465 3.408 -16.545 1.00 37.95 C ANISOU 935 CB CYS A 116 4952 4652 4816 134 227 75 C ATOM 936 SG CYS A 116 -38.410 3.074 -17.945 1.00 38.42 S ANISOU 936 SG CYS A 116 4984 4699 4915 159 128 19 S ATOM 937 N CYS A 117 -42.417 4.563 -15.150 1.00 47.21 N ANISOU 937 N CYS A 117 5993 5958 5988 63 456 104 N ATOM 938 C CYS A 117 -44.770 4.377 -14.367 1.00 52.27 C ANISOU 938 C CYS A 117 6490 6692 6678 -53 663 107 C ATOM 939 O CYS A 117 -45.586 4.088 -13.543 1.00 53.65 O ANISOU 939 O CYS A 117 6657 6886 6841 -115 788 128 O ATOM 940 CA ACYS A 117 -43.317 4.514 -13.973 0.50 50.95 C ANISOU 940 CA ACYS A 117 6482 6452 6424 26 585 137 C ATOM 941 CB ACYS A 117 -43.191 5.770 -13.124 0.50 51.12 C ANISOU 941 CB ACYS A 117 6535 6520 6370 119 609 130 C ATOM 942 SG ACYS A 117 -44.213 7.132 -13.713 0.50 54.59 S ANISOU 942 SG ACYS A 117 6806 7069 6869 177 620 65 S ATOM 943 CA BCYS A 117 -43.325 4.593 -13.975 0.50 50.49 C ANISOU 943 CA BCYS A 117 6420 6399 6366 31 585 134 C ATOM 944 CB BCYS A 117 -43.260 5.952 -13.273 0.50 50.42 C ANISOU 944 CB BCYS A 117 6423 6443 6291 127 602 120 C ATOM 945 SG BCYS A 117 -41.803 6.249 -12.220 0.50 50.76 S ANISOU 945 SG BCYS A 117 6652 6425 6209 209 546 145 S ATOM 946 N ASN A 118 -45.086 4.598 -15.644 1.00 53.31 N ANISOU 946 N ASN A 118 6492 6871 6892 -48 586 52 N ATOM 947 CA ASN A 118 -46.443 4.407 -16.125 1.00 54.59 C ANISOU 947 CA ASN A 118 6480 7114 7146 -119 630 6 C ATOM 948 C ASN A 118 -46.625 2.986 -16.628 1.00 54.29 C ANISOU 948 C ASN A 118 6441 7015 7172 -255 628 3 C ATOM 949 O ASN A 118 -46.309 2.714 -17.772 1.00 53.23 O ANISOU 949 O ASN A 118 6284 6865 7077 -254 520 -33 O ATOM 950 CB ASN A 118 -46.777 5.400 -17.246 1.00 54.32 C ANISOU 950 CB ASN A 118 6316 7166 7157 -31 532 -57 C ATOM 951 CG ASN A 118 -48.267 5.443 -17.558 1.00 59.43 C ANISOU 951 CG ASN A 118 6758 7928 7894 -69 569 -118 C ATOM 952 OD1 ASN A 118 -48.736 6.329 -18.271 1.00 64.04 O ANISOU 952 OD1 ASN A 118 7234 8593 8506 24 497 -168 O ATOM 953 ND2 ASN A 118 -49.022 4.477 -17.029 1.00 63.79 N ANISOU 953 ND2 ASN A 118 7257 8487 8494 -207 681 -118 N ATOM 954 N GLN A 119 -47.174 2.100 -15.783 1.00 55.37 N ANISOU 954 N GLN A 119 6610 7114 7314 -376 755 39 N ATOM 955 CA GLN A 119 -47.377 0.678 -16.156 1.00 55.71 C ANISOU 955 CA GLN A 119 6679 7068 7420 -525 767 39 C ATOM 956 C GLN A 119 -48.300 0.508 -17.389 1.00 55.42 C ANISOU 956 C GLN A 119 6442 7112 7505 -594 709 -57 C ATOM 957 O GLN A 119 -48.252 -0.536 -18.020 1.00 56.62 O ANISOU 957 O GLN A 119 6620 7185 7708 -692 669 -80 O ATOM 958 CB GLN A 119 -47.829 -0.202 -14.959 1.00 56.83 C ANISOU 958 CB GLN A 119 6918 7139 7535 -659 933 106 C ATOM 959 CG GLN A 119 -47.426 -1.214 -14.585 0.00 45.73 C ANISOU 959 CG GLN A 119 5676 5599 6101 -728 962 163 C ATOM 960 CD GLN A 119 -48.420 -2.255 -14.071 0.00 47.95 C ANISOU 960 CD GLN A 119 5963 5828 6427 -935 1123 187 C ATOM 961 OE1 GLN A 119 -49.266 -2.753 -14.808 0.00 48.93 O ANISOU 961 OE1 GLN A 119 5938 5980 6672 -1068 1132 118 O ATOM 962 NE2 GLN A 119 -48.304 -2.591 -12.803 0.00 48.92 N ANISOU 962 NE2 GLN A 119 6267 5874 6448 -968 1251 285 N ATOM 963 N SER A 120 -49.090 1.529 -17.751 1.00 54.64 N ANISOU 963 N SER A 120 6155 7162 7445 -530 690 -118 N ATOM 964 CA SER A 120 -49.876 1.468 -19.001 1.00 55.19 C ANISOU 964 CA SER A 120 6037 7319 7614 -561 595 -216 C ATOM 965 C SER A 120 -49.082 1.792 -20.328 1.00 52.13 C ANISOU 965 C SER A 120 5687 6919 7201 -453 415 -247 C ATOM 966 O SER A 120 -49.584 1.584 -21.463 1.00 52.71 O ANISOU 966 O SER A 120 5647 7046 7334 -479 315 -328 O ATOM 967 CB SER A 120 -51.202 2.239 -18.886 1.00 57.30 C ANISOU 967 CB SER A 120 6069 7756 7946 -541 643 -282 C ATOM 968 OG SER A 120 -51.112 3.589 -19.322 1.00 60.36 O ANISOU 968 OG SER A 120 6409 8228 8299 -354 547 -303 O ATOM 969 N THR A 121 -47.842 2.252 -20.200 1.00 47.46 N ANISOU 969 N THR A 121 5255 6260 6517 -344 376 -190 N ATOM 970 CA THR A 121 -47.099 2.611 -21.399 1.00 44.59 C ANISOU 970 CA THR A 121 4928 5893 6122 -254 237 -217 C ATOM 971 C THR A 121 -46.772 1.374 -22.237 1.00 40.39 C ANISOU 971 C THR A 121 4445 5282 5619 -342 177 -253 C ATOM 972 O THR A 121 -46.196 0.441 -21.713 1.00 40.27 O ANISOU 972 O THR A 121 4554 5150 5595 -403 223 -214 O ATOM 973 CB THR A 121 -45.764 3.374 -21.056 1.00 43.57 C ANISOU 973 CB THR A 121 4947 5712 5896 -137 221 -157 C ATOM 974 OG1 THR A 121 -46.077 4.425 -20.149 1.00 48.11 O ANISOU 974 OG1 THR A 121 5498 6339 6443 -68 284 -129 O ATOM 975 CG2 THR A 121 -45.154 3.979 -22.327 1.00 39.43 C ANISOU 975 CG2 THR A 121 4438 5208 5337 -50 102 -185 C ATOM 976 N PRO A 122 -47.127 1.377 -23.532 1.00 39.53 N ANISOU 976 N PRO A 122 4254 5231 5535 -335 67 -329 N ATOM 977 CA PRO A 122 -46.754 0.195 -24.369 1.00 38.92 C ANISOU 977 CA PRO A 122 4241 5071 5475 -410 7 -377 C ATOM 978 C PRO A 122 -45.219 0.051 -24.432 1.00 36.68 C ANISOU 978 C PRO A 122 4135 4687 5113 -337 -11 -334 C ATOM 979 O PRO A 122 -44.459 1.043 -24.449 1.00 33.00 O ANISOU 979 O PRO A 122 3712 4249 4578 -220 -29 -298 O ATOM 980 CB PRO A 122 -47.339 0.497 -25.768 1.00 39.79 C ANISOU 980 CB PRO A 122 4241 5284 5593 -380 -122 -468 C ATOM 981 CG PRO A 122 -48.326 1.599 -25.505 1.00 40.23 C ANISOU 981 CG PRO A 122 4144 5473 5670 -319 -116 -471 C ATOM 982 CD PRO A 122 -47.833 2.402 -24.328 1.00 39.77 C ANISOU 982 CD PRO A 122 4151 5393 5565 -246 -18 -378 C ATOM 983 N TYR A 123 -44.803 -1.206 -24.401 1.00 35.52 N ANISOU 983 N TYR A 123 4088 4420 4989 -411 -1 -344 N ATOM 984 CA TYR A 123 -43.402 -1.599 -24.499 1.00 34.18 C ANISOU 984 CA TYR A 123 4069 4154 4764 -343 -23 -326 C ATOM 985 C TYR A 123 -42.670 -0.870 -25.624 1.00 32.50 C ANISOU 985 C TYR A 123 3855 4006 4486 -236 -105 -362 C ATOM 986 O TYR A 123 -41.586 -0.357 -25.418 1.00 30.92 O ANISOU 986 O TYR A 123 3719 3799 4230 -147 -98 -326 O ATOM 987 CB TYR A 123 -43.350 -3.126 -24.758 1.00 35.41 C ANISOU 987 CB TYR A 123 4311 4178 4967 -437 -33 -369 C ATOM 988 CG TYR A 123 -41.908 -3.600 -24.993 1.00 36.69 C ANISOU 988 CG TYR A 123 4614 4247 5079 -344 -68 -373 C ATOM 989 CD1 TYR A 123 -41.031 -3.796 -23.889 1.00 33.11 C ANISOU 989 CD1 TYR A 123 4278 3707 4596 -287 -23 -296 C ATOM 990 CD2 TYR A 123 -41.440 -3.847 -26.283 1.00 33.25 C ANISOU 990 CD2 TYR A 123 4191 3821 4622 -305 -146 -458 C ATOM 991 CE1 TYR A 123 -39.728 -4.225 -24.093 1.00 33.63 C ANISOU 991 CE1 TYR A 123 4445 3705 4628 -187 -64 -314 C ATOM 992 CE2 TYR A 123 -40.116 -4.283 -26.497 1.00 34.06 C ANISOU 992 CE2 TYR A 123 4402 3855 4687 -212 -167 -476 C ATOM 993 CZ TYR A 123 -39.279 -4.472 -25.409 1.00 32.73 C ANISOU 993 CZ TYR A 123 4323 3607 4505 -151 -129 -407 C ATOM 994 OH TYR A 123 -37.990 -4.895 -25.611 1.00 30.82 O ANISOU 994 OH TYR A 123 4161 3312 4235 -45 -158 -437 O ATOM 995 N TYR A 124 -43.251 -0.873 -26.831 1.00 31.80 N ANISOU 995 N TYR A 124 3699 3982 4403 -253 -182 -439 N ATOM 996 CA TYR A 124 -42.560 -0.257 -27.988 1.00 31.62 C ANISOU 996 CA TYR A 124 3703 4013 4297 -160 -249 -470 C ATOM 997 C TYR A 124 -42.290 1.221 -27.826 1.00 30.16 C ANISOU 997 C TYR A 124 3503 3904 4053 -66 -237 -410 C ATOM 998 O TYR A 124 -41.268 1.749 -28.329 1.00 28.42 O ANISOU 998 O TYR A 124 3347 3692 3759 5 -243 -402 O ATOM 999 CB TYR A 124 -43.351 -0.517 -29.284 1.00 32.09 C ANISOU 999 CB TYR A 124 3707 4133 4354 -192 -345 -564 C ATOM 1000 CG TYR A 124 -44.525 0.435 -29.555 1.00 34.46 C ANISOU 1000 CG TYR A 124 3877 4558 4658 -170 -396 -571 C ATOM 1001 CD1 TYR A 124 -45.846 0.042 -29.278 1.00 35.72 C ANISOU 1001 CD1 TYR A 124 3903 4756 4912 -264 -406 -613 C ATOM 1002 CD2 TYR A 124 -44.311 1.686 -30.158 1.00 35.56 C ANISOU 1002 CD2 TYR A 124 4030 4775 4706 -57 -438 -544 C ATOM 1003 CE1 TYR A 124 -46.940 0.864 -29.572 1.00 42.48 C ANISOU 1003 CE1 TYR A 124 4620 5741 5781 -225 -468 -639 C ATOM 1004 CE2 TYR A 124 -45.412 2.571 -30.453 1.00 37.34 C ANISOU 1004 CE2 TYR A 124 4149 5110 4930 -7 -505 -554 C ATOM 1005 CZ TYR A 124 -46.697 2.131 -30.171 1.00 41.41 C ANISOU 1005 CZ TYR A 124 4513 5675 5546 -82 -526 -608 C ATOM 1006 OH TYR A 124 -47.768 2.958 -30.445 1.00 44.83 O ANISOU 1006 OH TYR A 124 4821 6226 5988 -16 -601 -631 O ATOM 1007 N VAL A 125 -43.163 1.909 -27.103 1.00 28.49 N ANISOU 1007 N VAL A 125 3208 3743 3872 -67 -208 -372 N ATOM 1008 CA VAL A 125 -42.911 3.302 -26.822 1.00 29.21 C ANISOU 1008 CA VAL A 125 3305 3880 3912 24 -192 -317 C ATOM 1009 C VAL A 125 -41.742 3.503 -25.870 1.00 28.92 C ANISOU 1009 C VAL A 125 3356 3781 3851 51 -126 -259 C ATOM 1010 O VAL A 125 -40.858 4.359 -26.095 1.00 28.74 O ANISOU 1010 O VAL A 125 3386 3766 3769 114 -127 -238 O ATOM 1011 CB VAL A 125 -44.248 3.991 -26.266 1.00 30.30 C ANISOU 1011 CB VAL A 125 3323 4094 4095 33 -180 -306 C ATOM 1012 CG1 VAL A 125 -44.020 5.465 -25.932 1.00 28.20 C ANISOU 1012 CG1 VAL A 125 3083 3855 3777 136 -165 -254 C ATOM 1013 CG2 VAL A 125 -45.349 3.893 -27.391 1.00 31.61 C ANISOU 1013 CG2 VAL A 125 3384 4345 4281 27 -279 -381 C ATOM 1014 N VAL A 126 -41.739 2.761 -24.765 1.00 28.30 N ANISOU 1014 N VAL A 126 3296 3641 3814 2 -67 -233 N ATOM 1015 CA VAL A 126 -40.567 2.804 -23.898 1.00 27.05 C ANISOU 1015 CA VAL A 126 3226 3426 3627 39 -30 -191 C ATOM 1016 C VAL A 126 -39.284 2.435 -24.649 1.00 26.72 C ANISOU 1016 C VAL A 126 3245 3354 3553 73 -66 -225 C ATOM 1017 O VAL A 126 -38.275 3.115 -24.506 1.00 26.17 O ANISOU 1017 O VAL A 126 3205 3295 3444 126 -59 -212 O ATOM 1018 CB VAL A 126 -40.742 1.885 -22.661 1.00 27.49 C ANISOU 1018 CB VAL A 126 3327 3406 3714 -12 28 -154 C ATOM 1019 CG1 VAL A 126 -39.567 2.142 -21.667 1.00 27.01 C ANISOU 1019 CG1 VAL A 126 3354 3306 3605 51 45 -111 C ATOM 1020 CG2 VAL A 126 -42.058 2.142 -21.999 1.00 25.61 C ANISOU 1020 CG2 VAL A 126 3013 3210 3509 -62 85 -133 C ATOM 1021 N ASP A 127 -39.336 1.340 -25.426 1.00 27.36 N ANISOU 1021 N ASP A 127 3341 3399 3656 37 -98 -279 N ATOM 1022 CA ASP A 127 -38.192 0.803 -26.151 1.00 26.63 C ANISOU 1022 CA ASP A 127 3302 3278 3538 73 -123 -329 C ATOM 1023 C ASP A 127 -37.595 1.851 -27.133 1.00 27.40 C ANISOU 1023 C ASP A 127 3385 3455 3568 121 -133 -346 C ATOM 1024 O ASP A 127 -36.424 2.188 -27.049 1.00 26.61 O ANISOU 1024 O ASP A 127 3306 3362 3442 165 -111 -347 O ATOM 1025 CB ASP A 127 -38.658 -0.489 -26.903 1.00 28.29 C ANISOU 1025 CB ASP A 127 3531 3436 3783 19 -159 -396 C ATOM 1026 CG ASP A 127 -37.495 -1.344 -27.390 1.00 30.46 C ANISOU 1026 CG ASP A 127 3876 3653 4045 67 -174 -454 C ATOM 1027 OD1 ASP A 127 -36.399 -0.836 -27.694 1.00 31.35 O ANISOU 1027 OD1 ASP A 127 3991 3809 4112 137 -164 -467 O ATOM 1028 OD2 ASP A 127 -37.668 -2.553 -27.488 1.00 33.10 O ANISOU 1028 OD2 ASP A 127 4263 3896 4418 33 -191 -495 O ATOM 1029 N LEU A 128 -38.416 2.327 -28.077 1.00 27.00 N ANISOU 1029 N LEU A 128 3304 3466 3490 110 -168 -363 N ATOM 1030 CA LEU A 128 -37.961 3.305 -29.085 1.00 28.69 C ANISOU 1030 CA LEU A 128 3539 3742 3621 149 -173 -367 C ATOM 1031 C LEU A 128 -37.493 4.630 -28.453 1.00 27.09 C ANISOU 1031 C LEU A 128 3343 3555 3395 179 -129 -303 C ATOM 1032 O LEU A 128 -36.554 5.242 -28.927 1.00 28.18 O ANISOU 1032 O LEU A 128 3516 3711 3479 194 -99 -303 O ATOM 1033 CB LEU A 128 -39.076 3.547 -30.148 1.00 27.59 C ANISOU 1033 CB LEU A 128 3381 3659 3444 147 -241 -391 C ATOM 1034 CG LEU A 128 -39.354 2.270 -30.955 1.00 30.92 C ANISOU 1034 CG LEU A 128 3807 4065 3874 110 -291 -476 C ATOM 1035 CD1 LEU A 128 -40.335 2.552 -32.052 1.00 36.07 C ANISOU 1035 CD1 LEU A 128 4443 4786 4475 118 -377 -512 C ATOM 1036 CD2 LEU A 128 -38.059 1.688 -31.544 1.00 36.89 C ANISOU 1036 CD2 LEU A 128 4633 4796 4588 130 -261 -527 C ATOM 1037 N SER A 129 -38.107 5.032 -27.361 1.00 26.90 N ANISOU 1037 N SER A 129 3289 3521 3412 178 -117 -255 N ATOM 1038 CA SER A 129 -37.677 6.282 -26.670 1.00 27.57 C ANISOU 1038 CA SER A 129 3392 3607 3476 205 -79 -206 C ATOM 1039 C SER A 129 -36.313 6.147 -26.060 1.00 26.94 C ANISOU 1039 C SER A 129 3333 3501 3403 206 -44 -213 C ATOM 1040 O SER A 129 -35.468 7.070 -26.205 1.00 27.49 O ANISOU 1040 O SER A 129 3425 3582 3438 209 -17 -208 O ATOM 1041 CB SER A 129 -38.676 6.678 -25.585 1.00 26.44 C ANISOU 1041 CB SER A 129 3214 3462 3370 214 -69 -166 C ATOM 1042 OG SER A 129 -39.932 7.041 -26.156 1.00 30.97 O ANISOU 1042 OG SER A 129 3744 4080 3943 231 -108 -168 O ATOM 1043 N VAL A 130 -36.067 5.018 -25.377 1.00 25.59 N ANISOU 1043 N VAL A 130 3158 3290 3274 202 -48 -228 N ATOM 1044 CA VAL A 130 -34.797 4.834 -24.702 1.00 26.96 C ANISOU 1044 CA VAL A 130 3342 3446 3456 226 -37 -242 C ATOM 1045 C VAL A 130 -33.730 4.638 -25.808 1.00 28.09 C ANISOU 1045 C VAL A 130 3475 3619 3579 233 -30 -304 C ATOM 1046 O VAL A 130 -32.668 5.233 -25.756 1.00 27.61 O ANISOU 1046 O VAL A 130 3395 3588 3507 238 -5 -322 O ATOM 1047 CB VAL A 130 -34.845 3.644 -23.673 1.00 26.60 C ANISOU 1047 CB VAL A 130 3322 3335 3447 239 -52 -234 C ATOM 1048 CG1 VAL A 130 -33.394 3.167 -23.287 1.00 28.74 C ANISOU 1048 CG1 VAL A 130 3603 3594 3725 293 -72 -272 C ATOM 1049 CG2 VAL A 130 -35.625 4.054 -22.452 1.00 29.13 C ANISOU 1049 CG2 VAL A 130 3659 3642 3769 230 -32 -173 C ATOM 1050 N ARG A 131 -34.053 3.899 -26.861 1.00 28.12 N ANISOU 1050 N ARG A 131 3488 3625 3572 226 -45 -342 N ATOM 1051 CA ARG A 131 -33.084 3.778 -27.937 1.00 28.80 C ANISOU 1051 CA ARG A 131 3570 3749 3623 236 -21 -404 C ATOM 1052 C ARG A 131 -32.820 5.154 -28.574 1.00 29.00 C ANISOU 1052 C ARG A 131 3603 3829 3586 208 25 -381 C ATOM 1053 O ARG A 131 -31.657 5.500 -28.835 1.00 28.61 O ANISOU 1053 O ARG A 131 3532 3817 3522 199 77 -415 O ATOM 1054 CB ARG A 131 -33.553 2.740 -28.995 1.00 28.93 C ANISOU 1054 CB ARG A 131 3612 3754 3625 235 -50 -459 C ATOM 1055 CG ARG A 131 -33.532 1.295 -28.437 1.00 28.57 C ANISOU 1055 CG ARG A 131 3583 3630 3643 259 -84 -492 C ATOM 1056 CD ARG A 131 -34.172 0.434 -29.449 1.00 28.53 C ANISOU 1056 CD ARG A 131 3610 3604 3626 239 -116 -547 C ATOM 1057 NE ARG A 131 -34.131 -1.020 -29.200 1.00 30.09 N ANISOU 1057 NE ARG A 131 3851 3705 3877 255 -146 -593 N ATOM 1058 CZ ARG A 131 -33.098 -1.853 -29.429 1.00 32.72 C ANISOU 1058 CZ ARG A 131 4208 4005 4219 321 -144 -665 C ATOM 1059 NH1 ARG A 131 -31.886 -1.442 -29.854 1.00 32.70 N ANISOU 1059 NH1 ARG A 131 4164 4077 4182 377 -103 -710 N ATOM 1060 NH2 ARG A 131 -33.273 -3.141 -29.228 1.00 33.81 N ANISOU 1060 NH2 ARG A 131 4412 4031 4403 333 -179 -699 N ATOM 1061 N GLY A 132 -33.887 5.913 -28.862 1.00 27.70 N ANISOU 1061 N GLY A 132 3471 3667 3385 193 8 -329 N ATOM 1062 CA GLY A 132 -33.741 7.242 -29.494 1.00 28.77 C ANISOU 1062 CA GLY A 132 3655 3827 3451 174 46 -293 C ATOM 1063 C GLY A 132 -32.893 8.201 -28.667 1.00 28.42 C ANISOU 1063 C GLY A 132 3600 3772 3427 149 95 -272 C ATOM 1064 O GLY A 132 -32.000 8.879 -29.201 1.00 29.61 O ANISOU 1064 O GLY A 132 3770 3943 3538 108 159 -281 O ATOM 1065 N MET A 133 -33.177 8.316 -27.391 1.00 27.28 N ANISOU 1065 N MET A 133 3432 3597 3338 164 70 -247 N ATOM 1066 CA MET A 133 -32.376 9.217 -26.530 1.00 30.38 C ANISOU 1066 CA MET A 133 3816 3978 3748 139 101 -242 C ATOM 1067 C MET A 133 -30.922 8.780 -26.430 1.00 30.66 C ANISOU 1067 C MET A 133 3786 4050 3814 122 128 -310 C ATOM 1068 O MET A 133 -30.008 9.628 -26.442 1.00 30.45 O ANISOU 1068 O MET A 133 3744 4040 3785 68 177 -329 O ATOM 1069 CB MET A 133 -32.988 9.396 -25.118 1.00 29.55 C ANISOU 1069 CB MET A 133 3710 3838 3679 168 68 -209 C ATOM 1070 CG MET A 133 -32.859 8.143 -24.156 1.00 31.62 C ANISOU 1070 CG MET A 133 3933 4093 3989 204 31 -231 C ATOM 1071 SD MET A 133 -33.704 8.461 -22.568 1.00 32.40 S ANISOU 1071 SD MET A 133 4058 4156 4097 231 15 -183 S ATOM 1072 CE MET A 133 -35.389 8.846 -23.075 1.00 30.15 C ANISOU 1072 CE MET A 133 3786 3870 3800 237 20 -136 C ATOM 1073 N LEU A 134 -30.683 7.472 -26.326 1.00 29.58 N ANISOU 1073 N LEU A 134 3605 3923 3711 167 97 -355 N ATOM 1074 CA LEU A 134 -29.284 6.985 -26.204 1.00 30.60 C ANISOU 1074 CA LEU A 134 3654 4096 3876 181 109 -434 C ATOM 1075 C LEU A 134 -28.483 7.255 -27.461 1.00 31.93 C ANISOU 1075 C LEU A 134 3796 4324 4010 134 189 -482 C ATOM 1076 O LEU A 134 -27.354 7.734 -27.374 1.00 33.63 O ANISOU 1076 O LEU A 134 3940 4589 4249 95 235 -532 O ATOM 1077 CB LEU A 134 -29.185 5.488 -25.776 1.00 28.59 C ANISOU 1077 CB LEU A 134 3381 3819 3663 262 48 -470 C ATOM 1078 CG LEU A 134 -29.772 5.173 -24.369 1.00 28.35 C ANISOU 1078 CG LEU A 134 3387 3728 3656 302 -16 -420 C ATOM 1079 CD1 LEU A 134 -29.733 3.607 -24.054 1.00 29.44 C ANISOU 1079 CD1 LEU A 134 3548 3814 3824 378 -70 -442 C ATOM 1080 CD2 LEU A 134 -29.023 5.907 -23.268 1.00 25.49 C ANISOU 1080 CD2 LEU A 134 2991 3386 3308 305 -34 -428 C ATOM 1081 N GLU A 135 -29.090 7.003 -28.631 1.00 32.62 N ANISOU 1081 N GLU A 135 3943 4413 4039 130 209 -471 N ATOM 1082 CA GLU A 135 -28.448 7.183 -29.927 1.00 33.82 C ANISOU 1082 CA GLU A 135 4099 4622 4130 90 296 -512 C ATOM 1083 C GLU A 135 -28.225 8.668 -30.231 1.00 33.26 C ANISOU 1083 C GLU A 135 4074 4552 4009 -3 374 -463 C ATOM 1084 O GLU A 135 -27.150 9.035 -30.638 1.00 33.33 O ANISOU 1084 O GLU A 135 4037 4614 4012 -66 467 -509 O ATOM 1085 CB GLU A 135 -29.310 6.529 -31.038 1.00 33.21 C ANISOU 1085 CB GLU A 135 4098 4538 3983 118 275 -510 C ATOM 1086 CG GLU A 135 -29.204 5.029 -30.901 1.00 39.27 C ANISOU 1086 CG GLU A 135 4823 5296 4801 192 224 -581 C ATOM 1087 CD GLU A 135 -30.128 4.220 -31.868 1.00 40.31 C ANISOU 1087 CD GLU A 135 5028 5409 4879 216 182 -598 C ATOM 1088 OE1 GLU A 135 -31.060 4.768 -32.502 1.00 36.73 O ANISOU 1088 OE1 GLU A 135 4648 4954 4354 190 165 -547 O ATOM 1089 OE2 GLU A 135 -29.848 2.998 -31.989 1.00 51.22 O ANISOU 1089 OE2 GLU A 135 6392 6777 6293 269 159 -674 O ATOM 1090 N ALA A 136 -29.255 9.516 -30.008 1.00 31.20 N ANISOU 1090 N ALA A 136 3908 4229 3719 -12 339 -374 N ATOM 1091 CA ALA A 136 -29.124 10.966 -30.218 1.00 31.45 C ANISOU 1091 CA ALA A 136 4018 4228 3703 -91 404 -319 C ATOM 1092 C ALA A 136 -27.973 11.558 -29.369 1.00 32.39 C ANISOU 1092 C ALA A 136 4055 4358 3894 -163 450 -361 C ATOM 1093 O ALA A 136 -27.235 12.401 -29.850 1.00 32.97 O ANISOU 1093 O ALA A 136 4150 4437 3940 -264 549 -364 O ATOM 1094 CB ALA A 136 -30.399 11.676 -29.926 1.00 29.48 C ANISOU 1094 CB ALA A 136 3868 3905 3428 -55 341 -232 C ATOM 1095 N SER A 137 -27.851 11.072 -28.126 1.00 32.59 N ANISOU 1095 N SER A 137 3992 4386 4004 -114 375 -395 N ATOM 1096 CA SER A 137 -26.917 11.594 -27.128 1.00 32.74 C ANISOU 1096 CA SER A 137 3932 4417 4091 -163 378 -442 C ATOM 1097 C SER A 137 -25.453 11.399 -27.495 1.00 34.36 C ANISOU 1097 C SER A 137 4006 4715 4335 -223 452 -542 C ATOM 1098 O SER A 137 -24.594 12.101 -26.995 1.00 33.53 O ANISOU 1098 O SER A 137 3834 4629 4277 -304 480 -589 O ATOM 1099 CB SER A 137 -27.223 10.933 -25.768 1.00 31.17 C ANISOU 1099 CB SER A 137 3690 4205 3947 -71 267 -451 C ATOM 1100 OG SER A 137 -28.437 11.467 -25.266 1.00 31.79 O ANISOU 1100 OG SER A 137 3873 4207 3999 -45 227 -370 O ATOM 1101 N GLU A 138 -25.188 10.430 -28.364 1.00 34.50 N ANISOU 1101 N GLU A 138 3979 4793 4335 -182 483 -586 N ATOM 1102 CA GLU A 138 -23.881 10.169 -28.874 1.00 37.50 C ANISOU 1102 CA GLU A 138 4227 5276 4744 -223 568 -689 C ATOM 1103 C GLU A 138 -23.295 11.406 -29.570 1.00 38.21 C ANISOU 1103 C GLU A 138 4342 5377 4798 -386 713 -681 C ATOM 1104 O GLU A 138 -22.093 11.526 -29.565 1.00 38.99 O ANISOU 1104 O GLU A 138 4296 5563 4954 -457 785 -776 O ATOM 1105 CB GLU A 138 -23.861 8.994 -29.910 1.00 39.47 C ANISOU 1105 CB GLU A 138 4465 5576 4955 -148 595 -734 C ATOM 1106 CG GLU A 138 -24.321 7.648 -29.308 1.00 41.24 C ANISOU 1106 CG GLU A 138 4673 5775 5220 2 466 -752 C ATOM 1107 CD GLU A 138 -24.530 6.575 -30.370 1.00 42.12 C ANISOU 1107 CD GLU A 138 4816 5903 5283 68 483 -789 C ATOM 1108 OE1 GLU A 138 -24.166 6.775 -31.545 1.00 48.14 O ANISOU 1108 OE1 GLU A 138 5591 6721 5978 15 596 -817 O ATOM 1109 OE2 GLU A 138 -25.127 5.554 -30.031 1.00 46.24 O ANISOU 1109 OE2 GLU A 138 5370 6374 5826 167 386 -786 O ATOM 1110 N GLY A 139 -24.142 12.259 -30.149 1.00 37.80 N ANISOU 1110 N GLY A 139 4470 5238 4653 -438 750 -573 N ATOM 1111 CA GLY A 139 -23.738 13.545 -30.748 1.00 39.29 C ANISOU 1111 CA GLY A 139 4741 5396 4793 -597 885 -537 C ATOM 1112 C GLY A 139 -23.004 14.481 -29.780 1.00 41.51 C ANISOU 1112 C GLY A 139 4951 5658 5164 -710 897 -576 C ATOM 1113 O GLY A 139 -22.404 15.461 -30.202 1.00 43.87 O ANISOU 1113 O GLY A 139 5285 5937 5447 -870 1024 -573 O ATOM 1114 N LEU A 140 -23.049 14.197 -28.481 1.00 40.99 N ANISOU 1114 N LEU A 140 4798 5591 5185 -636 767 -614 N ATOM 1115 CA LEU A 140 -22.329 15.017 -27.481 1.00 42.22 C ANISOU 1115 CA LEU A 140 4878 5738 5425 -733 754 -672 C ATOM 1116 C LEU A 140 -20.896 14.537 -27.213 1.00 44.10 C ANISOU 1116 C LEU A 140 4870 6120 5764 -771 773 -823 C ATOM 1117 O LEU A 140 -20.150 15.201 -26.467 1.00 45.42 O ANISOU 1117 O LEU A 140 4946 6304 6009 -869 763 -895 O ATOM 1118 CB LEU A 140 -23.072 15.073 -26.143 1.00 40.03 C ANISOU 1118 CB LEU A 140 4645 5391 5174 -636 602 -643 C ATOM 1119 CG LEU A 140 -24.408 15.802 -26.126 1.00 40.01 C ANISOU 1119 CG LEU A 140 4855 5250 5098 -606 577 -518 C ATOM 1120 CD1 LEU A 140 -25.087 15.614 -24.813 1.00 36.51 C ANISOU 1120 CD1 LEU A 140 4424 4769 4678 -495 443 -508 C ATOM 1121 CD2 LEU A 140 -24.173 17.264 -26.472 1.00 35.71 C ANISOU 1121 CD2 LEU A 140 4428 4612 4530 -765 677 -486 C ATOM 1122 N ASP A 141 -20.509 13.400 -27.776 1.00 44.67 N ANISOU 1122 N ASP A 141 4831 6300 5843 -686 789 -882 N ATOM 1123 CA ASP A 141 -19.210 12.779 -27.430 1.00 47.30 C ANISOU 1123 CA ASP A 141 4910 6781 6280 -669 777 -1037 C ATOM 1124 C ASP A 141 -17.980 13.579 -27.831 1.00 50.86 C ANISOU 1124 C ASP A 141 5221 7317 6786 -866 928 -1131 C ATOM 1125 O ASP A 141 -17.003 13.633 -27.077 1.00 52.08 O ANISOU 1125 O ASP A 141 5175 7564 7050 -896 882 -1257 O ATOM 1126 CB ASP A 141 -19.082 11.366 -28.002 1.00 47.48 C ANISOU 1126 CB ASP A 141 4857 6887 6295 -518 767 -1087 C ATOM 1127 CG ASP A 141 -19.926 10.340 -27.250 1.00 47.74 C ANISOU 1127 CG ASP A 141 4953 6863 6324 -322 593 -1044 C ATOM 1128 OD1 ASP A 141 -20.285 10.577 -26.090 1.00 45.58 O ANISOU 1128 OD1 ASP A 141 4714 6530 6074 -287 473 -1014 O ATOM 1129 OD2 ASP A 141 -20.151 9.256 -27.811 1.00 49.98 O ANISOU 1129 OD2 ASP A 141 5248 7163 6580 -207 584 -1053 O ATOM 1130 N GLY A 142 -18.040 14.176 -29.012 1.00 52.40 N ANISOU 1130 N GLY A 142 5525 7484 6901 -1000 1104 -1073 N ATOM 1131 CA GLY A 142 -16.980 15.027 -29.530 1.00 56.81 C ANISOU 1131 CA GLY A 142 5989 8102 7493 -1224 1288 -1140 C ATOM 1132 C GLY A 142 -16.748 16.207 -28.606 1.00 58.78 C ANISOU 1132 C GLY A 142 6244 8278 7813 -1372 1256 -1152 C ATOM 1133 O GLY A 142 -15.605 16.498 -28.252 1.00 61.39 O ANISOU 1133 O GLY A 142 6359 8710 8255 -1496 1295 -1288 O ATOM 1134 N TRP A 143 -17.820 16.890 -28.216 1.00 57.58 N ANISOU 1134 N TRP A 143 6327 7952 7598 -1358 1183 -1023 N ATOM 1135 CA TRP A 143 -17.718 18.049 -27.356 1.00 58.86 C ANISOU 1135 CA TRP A 143 6536 8017 7813 -1488 1150 -1031 C ATOM 1136 C TRP A 143 -17.242 17.692 -25.945 1.00 59.65 C ANISOU 1136 C TRP A 143 6445 8193 8025 -1409 971 -1155 C ATOM 1137 O TRP A 143 -16.311 18.336 -25.422 1.00 61.83 O ANISOU 1137 O TRP A 143 6583 8510 8398 -1561 982 -1270 O ATOM 1138 CB TRP A 143 -19.074 18.735 -27.234 1.00 58.66 C ANISOU 1138 CB TRP A 143 6808 7792 7689 -1441 1097 -871 C ATOM 1139 CG TRP A 143 -19.091 19.847 -26.247 1.00 59.42 C ANISOU 1139 CG TRP A 143 6973 7772 7833 -1537 1040 -884 C ATOM 1140 CD1 TRP A 143 -18.545 21.083 -26.412 1.00 64.05 C ANISOU 1140 CD1 TRP A 143 7620 8273 8443 -1770 1160 -899 C ATOM 1141 CD2 TRP A 143 -19.658 19.830 -24.932 1.00 58.24 C ANISOU 1141 CD2 TRP A 143 6849 7573 7707 -1410 857 -892 C ATOM 1142 NE1 TRP A 143 -18.759 21.851 -25.293 1.00 63.80 N ANISOU 1142 NE1 TRP A 143 7656 8135 8452 -1790 1052 -921 N ATOM 1143 CE2 TRP A 143 -19.450 21.103 -24.374 1.00 61.39 C ANISOU 1143 CE2 TRP A 143 7329 7855 8139 -1566 868 -916 C ATOM 1144 CE3 TRP A 143 -20.339 18.867 -24.181 1.00 59.38 C ANISOU 1144 CE3 TRP A 143 6971 7752 7838 -1188 696 -878 C ATOM 1145 CZ2 TRP A 143 -19.882 21.436 -23.087 1.00 60.04 C ANISOU 1145 CZ2 TRP A 143 7212 7615 7985 -1493 718 -937 C ATOM 1146 CZ3 TRP A 143 -20.771 19.186 -22.917 1.00 58.51 C ANISOU 1146 CZ3 TRP A 143 6914 7577 7739 -1123 560 -887 C ATOM 1147 CH2 TRP A 143 -20.537 20.465 -22.374 1.00 59.66 C ANISOU 1147 CH2 TRP A 143 7135 7618 7913 -1269 569 -921 C ATOM 1148 N ILE A 144 -17.890 16.716 -25.304 1.00 56.89 N ANISOU 1148 N ILE A 144 6101 7855 7659 -1181 804 -1132 N ATOM 1149 CA ILE A 144 -17.454 16.317 -23.979 1.00 57.51 C ANISOU 1149 CA ILE A 144 6029 8004 7819 -1087 629 -1238 C ATOM 1150 C ILE A 144 -15.999 15.820 -23.946 1.00 59.41 C ANISOU 1150 C ILE A 144 5961 8440 8174 -1116 635 -1418 C ATOM 1151 O ILE A 144 -15.290 16.042 -22.954 1.00 60.39 O ANISOU 1151 O ILE A 144 5937 8626 8383 -1139 528 -1538 O ATOM 1152 CB ILE A 144 -18.445 15.379 -23.218 1.00 54.20 C ANISOU 1152 CB ILE A 144 5700 7544 7349 -846 457 -1168 C ATOM 1153 CG1 ILE A 144 -18.318 13.931 -23.630 1.00 55.95 C ANISOU 1153 CG1 ILE A 144 5821 7865 7571 -680 429 -1192 C ATOM 1154 CG2 ILE A 144 -19.863 15.859 -23.405 1.00 55.54 C ANISOU 1154 CG2 ILE A 144 6137 7548 7417 -823 472 -1005 C ATOM 1155 CD1 ILE A 144 -17.493 13.136 -22.650 1.00 63.02 C ANISOU 1155 CD1 ILE A 144 6521 8878 8544 -556 277 -1320 C ATOM 1156 N HIS A 145 -15.573 15.140 -25.008 1.00 60.17 N ANISOU 1156 N HIS A 145 5954 8638 8269 -1102 753 -1447 N ATOM 1157 CA HIS A 145 -14.166 14.711 -25.116 1.00 63.43 C ANISOU 1157 CA HIS A 145 6053 9251 8796 -1130 787 -1631 C ATOM 1158 C HIS A 145 -13.163 15.908 -25.042 1.00 65.26 C ANISOU 1158 C HIS A 145 6146 9528 9120 -1402 892 -1739 C ATOM 1159 O HIS A 145 -12.193 15.836 -24.288 1.00 66.06 O ANISOU 1159 O HIS A 145 5999 9761 9339 -1408 797 -1903 O ATOM 1160 CB HIS A 145 -13.892 13.820 -26.340 1.00 63.48 C ANISOU 1160 CB HIS A 145 5984 9359 8776 -1071 919 -1651 C ATOM 1161 CG HIS A 145 -12.469 13.349 -26.403 1.00 68.40 C ANISOU 1161 CG HIS A 145 6267 10200 9524 -1074 950 -1853 C ATOM 1162 ND1 HIS A 145 -11.978 12.357 -25.579 1.00 70.26 N ANISOU 1162 ND1 HIS A 145 6316 10545 9837 -861 761 -1968 N ATOM 1163 CD2 HIS A 145 -11.414 13.781 -27.138 1.00 72.73 C ANISOU 1163 CD2 HIS A 145 6619 10879 10136 -1265 1146 -1966 C ATOM 1164 CE1 HIS A 145 -10.691 12.169 -25.831 1.00 72.10 C ANISOU 1164 CE1 HIS A 145 6238 10976 10181 -901 829 -2152 C ATOM 1165 NE2 HIS A 145 -10.325 13.020 -26.773 1.00 74.19 N ANISOU 1165 NE2 HIS A 145 6481 11264 10444 -1154 1071 -2157 N ATOM 1166 N GLN A 146 -13.458 16.991 -25.776 1.00 66.02 N ANISOU 1166 N GLN A 146 6419 9505 9161 -1616 1070 -1645 N ATOM 1167 CA GLN A 146 -12.695 18.256 -25.729 1.00 68.50 C ANISOU 1167 CA GLN A 146 6672 9806 9550 -1907 1186 -1718 C ATOM 1168 C GLN A 146 -12.719 18.926 -24.341 1.00 69.08 C ANISOU 1168 C GLN A 146 6756 9809 9682 -1933 1006 -1768 C ATOM 1169 O GLN A 146 -11.884 19.810 -24.050 1.00 72.33 O ANISOU 1169 O GLN A 146 7047 10244 10192 -2159 1053 -1884 O ATOM 1170 CB GLN A 146 -13.192 19.222 -26.811 1.00 68.66 C ANISOU 1170 CB GLN A 146 6954 9666 9467 -2099 1403 -1570 C ATOM 1171 CG GLN A 146 -13.073 19.206 -28.109 0.00 95.16 C ANISOU 1171 CG GLN A 146 10359 13043 12754 -2189 1617 -1519 C ATOM 1172 CD GLN A 146 -13.674 20.312 -28.989 0.00 96.15 C ANISOU 1172 CD GLN A 146 10806 12971 12757 -2367 1794 -1353 C ATOM 1173 OE1 GLN A 146 -14.843 20.700 -28.824 0.00 97.49 O ANISOU 1173 OE1 GLN A 146 11261 12950 12829 -2283 1710 -1200 O ATOM 1174 NE2 GLN A 146 -12.873 20.820 -29.936 0.00100.56 N ANISOU 1174 NE2 GLN A 146 11321 13574 13315 -2610 2045 -1382 N ATOM 1175 N GLN A 147 -13.667 18.524 -23.490 1.00 66.66 N ANISOU 1175 N GLN A 147 6595 9417 9314 -1717 810 -1689 N ATOM 1176 CA GLN A 147 -13.691 18.951 -22.069 1.00 66.73 C ANISOU 1176 CA GLN A 147 6609 9385 9361 -1692 616 -1751 C ATOM 1177 C GLN A 147 -13.025 17.917 -21.151 1.00 66.11 C ANISOU 1177 C GLN A 147 6282 9485 9352 -1503 415 -1895 C ATOM 1178 O GLN A 147 -13.122 18.023 -19.932 1.00 66.42 O ANISOU 1178 O GLN A 147 6339 9505 9395 -1425 227 -1938 O ATOM 1179 CB GLN A 147 -15.131 19.204 -21.529 1.00 64.05 C ANISOU 1179 CB GLN A 147 6586 8847 8905 -1568 521 -1587 C ATOM 1180 CG GLN A 147 -16.145 19.807 -22.473 1.00 63.80 C ANISOU 1180 CG GLN A 147 6835 8637 8767 -1627 669 -1407 C ATOM 1181 CD GLN A 147 -15.727 21.126 -23.025 1.00 69.73 C ANISOU 1181 CD GLN A 147 7657 9294 9543 -1909 839 -1412 C ATOM 1182 OE1 GLN A 147 -15.182 21.963 -22.307 1.00 73.50 O ANISOU 1182 OE1 GLN A 147 8090 9742 10094 -2058 804 -1512 O ATOM 1183 NE2 GLN A 147 -15.967 21.328 -24.323 1.00 72.69 N ANISOU 1183 NE2 GLN A 147 8157 9614 9850 -1992 1028 -1304 N ATOM 1184 N GLY A 148 -12.412 16.897 -21.725 1.00 65.90 N ANISOU 1184 N GLY A 148 6050 9622 9367 -1407 447 -1962 N ATOM 1185 CA GLY A 148 -11.775 15.875 -20.923 1.00 65.84 C ANISOU 1185 CA GLY A 148 5821 9774 9420 -1201 251 -2093 C ATOM 1186 C GLY A 148 -12.713 14.894 -20.260 1.00 63.56 C ANISOU 1186 C GLY A 148 5697 9417 9035 -916 73 -1987 C ATOM 1187 O GLY A 148 -12.302 14.211 -19.332 1.00 64.89 O ANISOU 1187 O GLY A 148 5749 9676 9232 -742 -124 -2077 O ATOM 1188 N GLY A 149 -13.965 14.789 -20.718 1.00 60.48 N ANISOU 1188 N GLY A 149 5578 8871 8530 -864 136 -1800 N ATOM 1189 CA GLY A 149 -14.872 13.754 -20.193 1.00 57.50 C ANISOU 1189 CA GLY A 149 5347 8433 8069 -611 -6 -1699 C ATOM 1190 C GLY A 149 -15.892 14.208 -19.136 1.00 55.55 C ANISOU 1190 C GLY A 149 5331 8038 7738 -566 -120 -1599 C ATOM 1191 O GLY A 149 -15.717 15.244 -18.500 1.00 54.56 O ANISOU 1191 O GLY A 149 5224 7877 7630 -693 -149 -1645 O ATOM 1192 N TRP A 150 -16.948 13.405 -18.942 1.00 53.41 N ANISOU 1192 N TRP A 150 5232 7684 7377 -389 -179 -1472 N ATOM 1193 CA TRP A 150 -17.985 13.690 -17.944 1.00 52.35 C ANISOU 1193 CA TRP A 150 5311 7423 7155 -326 -271 -1376 C ATOM 1194 C TRP A 150 -17.464 13.723 -16.495 1.00 54.46 C ANISOU 1194 C TRP A 150 5526 7740 7426 -254 -462 -1474 C ATOM 1195 O TRP A 150 -17.895 14.558 -15.683 1.00 52.39 O ANISOU 1195 O TRP A 150 5390 7396 7118 -300 -507 -1458 O ATOM 1196 CB TRP A 150 -19.134 12.682 -18.074 1.00 50.71 C ANISOU 1196 CB TRP A 150 5264 7140 6865 -161 -283 -1236 C ATOM 1197 CG TRP A 150 -19.914 12.822 -19.365 1.00 49.04 C ANISOU 1197 CG TRP A 150 5153 6857 6622 -230 -121 -1126 C ATOM 1198 CD1 TRP A 150 -19.792 12.050 -20.507 1.00 49.50 C ANISOU 1198 CD1 TRP A 150 5155 6961 6692 -203 -37 -1119 C ATOM 1199 CD2 TRP A 150 -20.930 13.795 -19.650 1.00 48.53 C ANISOU 1199 CD2 TRP A 150 5273 6666 6502 -322 -35 -1017 C ATOM 1200 NE1 TRP A 150 -20.671 12.490 -21.481 1.00 47.53 N ANISOU 1200 NE1 TRP A 150 5046 6625 6388 -278 89 -1010 N ATOM 1201 CE2 TRP A 150 -21.389 13.552 -20.976 1.00 48.96 C ANISOU 1201 CE2 TRP A 150 5373 6699 6530 -344 87 -943 C ATOM 1202 CE3 TRP A 150 -21.518 14.825 -18.912 1.00 48.50 C ANISOU 1202 CE3 TRP A 150 5404 6561 6460 -371 -58 -980 C ATOM 1203 CZ2 TRP A 150 -22.387 14.333 -21.575 1.00 46.59 C ANISOU 1203 CZ2 TRP A 150 5247 6286 6170 -409 175 -831 C ATOM 1204 CZ3 TRP A 150 -22.510 15.606 -19.507 1.00 47.18 C ANISOU 1204 CZ3 TRP A 150 5406 6276 6243 -432 39 -872 C ATOM 1205 CH2 TRP A 150 -22.938 15.348 -20.826 1.00 47.22 C ANISOU 1205 CH2 TRP A 150 5450 6267 6223 -446 147 -796 C ATOM 1206 N SER A 151 -16.542 12.810 -16.173 1.00 56.94 N ANISOU 1206 N SER A 151 5660 8187 7787 -126 -581 -1582 N ATOM 1207 CA SER A 151 -16.002 12.743 -14.824 1.00 60.64 C ANISOU 1207 CA SER A 151 6080 8715 8246 -31 -786 -1680 C ATOM 1208 C SER A 151 -15.259 14.032 -14.524 1.00 63.07 C ANISOU 1208 C SER A 151 6279 9064 8622 -230 -788 -1812 C ATOM 1209 O SER A 151 -15.437 14.631 -13.430 1.00 63.38 O ANISOU 1209 O SER A 151 6416 9058 8606 -235 -901 -1835 O ATOM 1210 CB SER A 151 -15.066 11.557 -14.606 1.00 61.84 C ANISOU 1210 CB SER A 151 6048 9006 8442 157 -925 -1783 C ATOM 1211 OG SER A 151 -15.613 10.405 -15.176 1.00 64.52 O ANISOU 1211 OG SER A 151 6467 9301 8745 301 -885 -1679 O ATOM 1212 N THR A 152 -14.455 14.468 -15.493 1.00 65.15 N ANISOU 1212 N THR A 152 6351 9407 8997 -403 -654 -1899 N ATOM 1213 CA THR A 152 -13.687 15.694 -15.309 1.00 68.29 C ANISOU 1213 CA THR A 152 6632 9838 9476 -629 -635 -2033 C ATOM 1214 C THR A 152 -14.581 16.924 -15.189 1.00 68.56 C ANISOU 1214 C THR A 152 6913 9688 9449 -781 -552 -1937 C ATOM 1215 O THR A 152 -14.324 17.787 -14.344 1.00 69.55 O ANISOU 1215 O THR A 152 7051 9790 9583 -873 -636 -2026 O ATOM 1216 CB THR A 152 -12.603 15.905 -16.411 1.00 69.97 C ANISOU 1216 CB THR A 152 6581 10180 9825 -808 -479 -2149 C ATOM 1217 OG1 THR A 152 -11.621 14.874 -16.314 1.00 68.53 O ANISOU 1217 OG1 THR A 152 6134 10190 9716 -655 -589 -2283 O ATOM 1218 CG2 THR A 152 -11.929 17.240 -16.225 1.00 70.65 C ANISOU 1218 CG2 THR A 152 6579 10271 9996 -1076 -439 -2274 C ATOM 1219 N LEU A 153 -15.612 16.999 -16.024 1.00 68.04 N ANISOU 1219 N LEU A 153 7039 9491 9321 -797 -398 -1768 N ATOM 1220 CA LEU A 153 -16.598 18.079 -15.953 1.00 69.94 C ANISOU 1220 CA LEU A 153 7534 9546 9495 -895 -326 -1662 C ATOM 1221 C LEU A 153 -17.259 18.220 -14.569 1.00 70.69 C ANISOU 1221 C LEU A 153 7793 9569 9498 -772 -485 -1644 C ATOM 1222 O LEU A 153 -17.472 19.346 -14.101 1.00 71.94 O ANISOU 1222 O LEU A 153 8072 9622 9641 -885 -483 -1665 O ATOM 1223 CB LEU A 153 -17.691 17.915 -17.010 1.00 67.92 C ANISOU 1223 CB LEU A 153 7451 9181 9173 -869 -175 -1481 C ATOM 1224 CG LEU A 153 -17.656 18.745 -18.300 1.00 70.33 C ANISOU 1224 CG LEU A 153 7798 9418 9506 -1073 33 -1435 C ATOM 1225 CD1 LEU A 153 -18.722 18.239 -19.283 1.00 67.84 C ANISOU 1225 CD1 LEU A 153 7631 9034 9110 -982 131 -1267 C ATOM 1226 CD2 LEU A 153 -17.827 20.257 -18.069 1.00 69.97 C ANISOU 1226 CD2 LEU A 153 7904 9221 9459 -1255 82 -1436 C ATOM 1227 N ILE A 154 -17.569 17.099 -13.914 1.00 70.80 N ANISOU 1227 N ILE A 154 7825 9630 9444 -547 -614 -1609 N ATOM 1228 CA ILE A 154 -18.212 17.186 -12.605 1.00 72.02 C ANISOU 1228 CA ILE A 154 8150 9724 9491 -430 -746 -1586 C ATOM 1229 C ILE A 154 -17.264 17.341 -11.397 1.00 75.49 C ANISOU 1229 C ILE A 154 8486 10260 9938 -410 -941 -1754 C ATOM 1230 O ILE A 154 -17.513 18.208 -10.546 1.00 76.26 O ANISOU 1230 O ILE A 154 8709 10285 9982 -455 -996 -1791 O ATOM 1231 CB ILE A 154 -19.222 16.046 -12.362 1.00 70.16 C ANISOU 1231 CB ILE A 154 8051 9455 9150 -215 -776 -1443 C ATOM 1232 CG1 ILE A 154 -20.266 16.503 -11.346 1.00 67.97 C ANISOU 1232 CG1 ILE A 154 8006 9067 8752 -157 -812 -1376 C ATOM 1233 CG2 ILE A 154 -18.521 14.749 -11.926 1.00 69.68 C ANISOU 1233 CG2 ILE A 154 7862 9523 9090 -40 -924 -1497 C ATOM 1234 CD1 ILE A 154 -21.603 16.030 -11.648 1.00 68.16 C ANISOU 1234 CD1 ILE A 154 8192 9003 8704 -67 -722 -1208 C ATOM 1235 N GLU A 155 -16.209 16.505 -11.333 1.00 78.49 N ANISOU 1235 N GLU A 155 8641 10802 10379 -331 -1051 -1863 N ATOM 1236 CA GLU A 155 -15.218 16.464 -10.224 1.00 82.33 C ANISOU 1236 CA GLU A 155 8996 11413 10873 -275 -1270 -2036 C ATOM 1237 C GLU A 155 -14.496 17.805 -10.033 1.00 85.11 C ANISOU 1237 C GLU A 155 9253 11775 11309 -509 -1274 -2197 C ATOM 1238 O GLU A 155 -13.865 18.078 -9.002 1.00 86.97 O ANISOU 1238 O GLU A 155 9428 12082 11534 -496 -1458 -2345 O ATOM 1239 CB GLU A 155 -14.175 15.360 -10.473 1.00 83.20 C ANISOU 1239 CB GLU A 155 8848 11701 11062 -152 -1363 -2129 C ATOM 1240 CG GLU A 155 -14.677 13.933 -10.234 1.00 83.12 C ANISOU 1240 CG GLU A 155 8941 11685 10956 118 -1441 -2011 C ATOM 1241 CD GLU A 155 -13.673 12.856 -10.667 1.00 85.84 C ANISOU 1241 CD GLU A 155 9039 12185 11390 246 -1509 -2101 C ATOM 1242 OE1 GLU A 155 -12.477 12.983 -10.335 1.00 87.93 O ANISOU 1242 OE1 GLU A 155 9063 12606 11741 239 -1641 -2290 O ATOM 1243 OE2 GLU A 155 -14.080 11.878 -11.342 1.00 85.64 O ANISOU 1243 OE2 GLU A 155 9056 12128 11354 359 -1435 -1992 O ATOM 1244 N ASP A 156 -14.708 18.670 -11.013 1.00 86.12 N ANISOU 1244 N ASP A 156 9409 11808 11503 -724 -1068 -2154 N ATOM 1245 CA ASP A 156 -13.726 19.620 -11.472 1.00 89.12 C ANISOU 1245 CA ASP A 156 9607 12230 12023 -985 -997 -2302 C ATOM 1246 C ASP A 156 -14.501 20.776 -12.099 1.00 88.96 C ANISOU 1246 C ASP A 156 9800 12007 11992 -1176 -800 -2196 C ATOM 1247 O ASP A 156 -15.735 20.771 -12.099 1.00 87.85 O ANISOU 1247 O ASP A 156 9913 11724 11741 -1077 -748 -2029 O ATOM 1248 CB ASP A 156 -13.002 18.867 -12.586 1.00 89.41 C ANISOU 1248 CB ASP A 156 9396 12407 12169 -998 -898 -2325 C ATOM 1249 CG ASP A 156 -11.563 18.669 -12.327 1.00 91.16 C ANISOU 1249 CG ASP A 156 9282 12839 12514 -1031 -1018 -2547 C ATOM 1250 OD1 ASP A 156 -11.139 17.534 -11.962 1.00 87.44 O ANISOU 1250 OD1 ASP A 156 8674 12512 12037 -806 -1173 -2595 O ATOM 1251 OD2 ASP A 156 -10.862 19.675 -12.544 1.00 96.42 O ANISOU 1251 OD2 ASP A 156 9824 13521 13290 -1291 -946 -2674 O ATOM 1252 N ASN A 157 -13.796 21.743 -12.679 1.00 91.30 N ANISOU 1252 N ASN A 157 9996 12289 12403 -1447 -684 -2289 N ATOM 1253 CA ASN A 157 -14.426 22.725 -13.590 1.00 91.29 C ANISOU 1253 CA ASN A 157 10192 12095 12400 -1629 -466 -2170 C ATOM 1254 C ASN A 157 -15.697 23.391 -13.035 1.00 89.70 C ANISOU 1254 C ASN A 157 10325 11683 12076 -1564 -478 -2054 C ATOM 1255 O ASN A 157 -16.814 22.971 -13.352 1.00 87.15 O ANISOU 1255 O ASN A 157 10175 11280 11657 -1411 -422 -1878 O ATOM 1256 CB ASN A 157 -14.715 22.079 -14.975 1.00 90.08 C ANISOU 1256 CB ASN A 157 10021 11957 12249 -1604 -285 -2028 C ATOM 1257 CG ASN A 157 -15.341 23.053 -15.703 0.00 56.31 C ANISOU 1257 CG ASN A 157 5958 7489 7947 -1753 -111 -1916 C ATOM 1258 OD1 ASN A 157 -15.145 24.261 -15.681 0.00 57.78 O ANISOU 1258 OD1 ASN A 157 6229 7553 8171 -1966 -49 -1963 O ATOM 1259 ND2 ASN A 157 -16.276 22.505 -16.456 0.00 54.25 N ANISOU 1259 ND2 ASN A 157 5828 7176 7606 -1624 -24 -1739 N TER 1260 ASN A 157 ATOM 1261 N SER B 69 -44.021 21.284 -36.765 1.00 82.42 N ANISOU 1261 N SER B 69 15882 7597 7839 1298 -2548 583 N ATOM 1262 CA SER B 69 -42.807 21.457 -35.909 1.00 78.73 C ANISOU 1262 CA SER B 69 15178 7342 7395 1080 -1923 709 C ATOM 1263 C SER B 69 -43.145 21.494 -34.432 1.00 74.70 C ANISOU 1263 C SER B 69 13944 6985 7451 1236 -1809 388 C ATOM 1264 O SER B 69 -42.951 22.530 -33.767 1.00 74.55 O ANISOU 1264 O SER B 69 13822 6804 7702 1311 -1932 357 O ATOM 1265 CB SER B 69 -42.024 22.715 -36.297 1.00 82.71 C ANISOU 1265 CB SER B 69 16223 7592 7610 718 -2067 1159 C ATOM 1266 OG SER B 69 -42.641 23.899 -35.794 1.00 87.78 O ANISOU 1266 OG SER B 69 16962 7645 8743 956 -2805 1078 O ATOM 1267 N THR B 70 -43.653 20.379 -33.890 1.00 71.89 N ANISOU 1267 N THR B 70 13139 6973 7203 1186 -1668 160 N ATOM 1268 CA THR B 70 -43.636 20.297 -32.428 1.00 69.16 C ANISOU 1268 CA THR B 70 12145 7001 7130 1051 -1397 -24 C ATOM 1269 C THR B 70 -42.186 20.046 -32.001 1.00 64.86 C ANISOU 1269 C THR B 70 11745 6397 6501 901 -887 200 C ATOM 1270 O THR B 70 -41.783 20.539 -30.943 1.00 63.39 O ANISOU 1270 O THR B 70 11224 6340 6523 855 -666 147 O ATOM 1271 CB THR B 70 -44.678 19.331 -31.722 1.00 70.41 C ANISOU 1271 CB THR B 70 11730 7730 7293 691 -1494 -236 C ATOM 1272 OG1 THR B 70 -44.002 18.318 -30.936 1.00 71.65 O ANISOU 1272 OG1 THR B 70 11940 7941 7342 227 -1244 -15 O ATOM 1273 CG2 THR B 70 -45.665 18.740 -32.656 1.00 72.42 C ANISOU 1273 CG2 THR B 70 12124 7977 7413 645 -1931 -282 C ATOM 1274 N MET B 71 -41.419 19.320 -32.838 1.00 63.70 N ANISOU 1274 N MET B 71 12021 6155 6028 915 -762 311 N ATOM 1275 CA MET B 71 -39.986 19.036 -32.592 1.00 62.32 C ANISOU 1275 CA MET B 71 11843 6112 5723 928 -358 298 C ATOM 1276 C MET B 71 -39.139 20.344 -32.544 1.00 61.70 C ANISOU 1276 C MET B 71 11722 6133 5587 781 -53 507 C ATOM 1277 O MET B 71 -38.202 20.464 -31.738 1.00 59.81 O ANISOU 1277 O MET B 71 11213 6048 5462 713 263 482 O ATOM 1278 CB MET B 71 -39.403 18.056 -33.624 1.00 65.78 C ANISOU 1278 CB MET B 71 12579 6676 5737 1169 -397 68 C ATOM 1279 CG MET B 71 -40.112 16.667 -33.758 1.00 68.34 C ANISOU 1279 CG MET B 71 13178 6676 6110 1294 -966 -128 C ATOM 1280 SD MET B 71 -40.666 16.075 -32.147 1.00 70.85 S ANISOU 1280 SD MET B 71 13318 6753 6849 841 -1259 33 S ATOM 1281 CE MET B 71 -42.166 15.153 -32.574 1.00 69.76 C ANISOU 1281 CE MET B 71 13469 6392 6644 475 -1971 132 C ATOM 1282 N GLY B 72 -39.469 21.283 -33.440 1.00 64.03 N ANISOU 1282 N GLY B 72 12391 6268 5671 647 -298 758 N ATOM 1283 CA GLY B 72 -38.907 22.643 -33.440 1.00 64.49 C ANISOU 1283 CA GLY B 72 12670 6176 5656 290 -371 1112 C ATOM 1284 C GLY B 72 -39.117 23.320 -32.105 1.00 60.94 C ANISOU 1284 C GLY B 72 11912 5434 5808 452 -523 979 C ATOM 1285 O GLY B 72 -38.173 23.851 -31.533 1.00 59.93 O ANISOU 1285 O GLY B 72 11693 5356 5722 201 -309 1122 O ATOM 1286 N GLN B 73 -40.351 23.261 -31.605 1.00 59.30 N ANISOU 1286 N GLN B 73 11437 5102 5992 857 -882 614 N ATOM 1287 CA GLN B 73 -40.740 23.990 -30.408 1.00 59.65 C ANISOU 1287 CA GLN B 73 11075 5096 6492 1131 -1117 258 C ATOM 1288 C GLN B 73 -40.187 23.368 -29.137 1.00 54.79 C ANISOU 1288 C GLN B 73 9906 4932 5981 1006 -535 130 C ATOM 1289 O GLN B 73 -39.834 24.086 -28.201 1.00 56.83 O ANISOU 1289 O GLN B 73 9965 5156 6473 1073 -555 -8 O ATOM 1290 CB GLN B 73 -42.270 24.163 -30.337 1.00 62.84 C ANISOU 1290 CB GLN B 73 11136 5611 7130 1623 -1694 -309 C ATOM 1291 CG GLN B 73 -42.826 24.799 -29.013 1.00 66.80 C ANISOU 1291 CG GLN B 73 10903 6496 7982 2058 -1914 -1030 C ATOM 1292 CD GLN B 73 -42.398 26.255 -28.756 1.00 70.96 C ANISOU 1292 CD GLN B 73 11835 6310 8818 2401 -2585 -1146 C ATOM 1293 OE1 GLN B 73 -43.296 27.112 -29.644 0.00102.90 O ANISOU 1293 OE1 GLN B 73 16369 9688 13041 2965 -3764 -1441 O ATOM 1294 NE2 GLN B 73 -41.338 26.760 -28.632 0.00 90.06 N ANISOU 1294 NE2 GLN B 73 14712 8258 11248 2091 -2532 -703 N ATOM 1295 N VAL B 74 -40.134 22.040 -29.088 1.00 51.72 N ANISOU 1295 N VAL B 74 9379 4858 5415 825 -194 165 N ATOM 1296 CA VAL B 74 -39.574 21.330 -27.968 1.00 46.97 C ANISOU 1296 CA VAL B 74 8485 4514 4848 618 130 138 C ATOM 1297 C VAL B 74 -38.096 21.690 -27.893 1.00 46.33 C ANISOU 1297 C VAL B 74 8538 4293 4772 578 428 318 C ATOM 1298 O VAL B 74 -37.583 22.046 -26.815 1.00 44.73 O ANISOU 1298 O VAL B 74 8088 4154 4755 521 562 261 O ATOM 1299 CB VAL B 74 -39.792 19.804 -28.103 1.00 47.53 C ANISOU 1299 CB VAL B 74 8690 4650 4718 400 54 197 C ATOM 1300 CG1 VAL B 74 -38.959 19.012 -27.090 1.00 43.83 C ANISOU 1300 CG1 VAL B 74 8229 4165 4258 179 116 252 C ATOM 1301 CG2 VAL B 74 -41.266 19.502 -27.940 1.00 49.84 C ANISOU 1301 CG2 VAL B 74 8687 5317 4935 165 -215 59 C ATOM 1302 N GLY B 75 -37.425 21.619 -29.050 1.00 47.86 N ANISOU 1302 N GLY B 75 9040 4469 4675 549 536 483 N ATOM 1303 CA GLY B 75 -36.028 22.008 -29.189 1.00 49.15 C ANISOU 1303 CA GLY B 75 9157 4855 4661 356 858 599 C ATOM 1304 C GLY B 75 -35.748 23.396 -28.628 1.00 50.72 C ANISOU 1304 C GLY B 75 9383 4818 5069 110 746 814 C ATOM 1305 O GLY B 75 -34.759 23.592 -27.924 1.00 50.66 O ANISOU 1305 O GLY B 75 9127 4971 5151 -37 979 813 O ATOM 1306 N ARG B 76 -36.620 24.352 -28.921 1.00 52.51 N ANISOU 1306 N ARG B 76 9958 4584 5409 133 224 928 N ATOM 1307 CA ARG B 76 -36.356 25.752 -28.574 1.00 56.96 C ANISOU 1307 CA ARG B 76 10806 4672 6166 -67 -234 1117 C ATOM 1308 C ARG B 76 -36.580 25.986 -27.095 1.00 53.30 C ANISOU 1308 C ARG B 76 9915 4151 6185 327 -304 683 C ATOM 1309 O ARG B 76 -35.829 26.693 -26.422 1.00 54.09 O ANISOU 1309 O ARG B 76 10030 4075 6448 153 -388 758 O ATOM 1310 CB ARG B 76 -37.195 26.701 -29.432 1.00 62.46 C ANISOU 1310 CB ARG B 76 12194 4698 6840 -52 -1116 1287 C ATOM 1311 CG ARG B 76 -36.536 26.928 -30.828 1.00 72.17 C ANISOU 1311 CG ARG B 76 14040 6004 7376 -887 -1137 1972 C ATOM 1312 CD ARG B 76 -37.314 27.907 -31.837 1.00 84.24 C ANISOU 1312 CD ARG B 76 16578 6670 8760 -1073 -2280 2333 C ATOM 1313 NE ARG B 76 -38.025 27.139 -32.891 1.00 89.69 N ANISOU 1313 NE ARG B 76 17358 7608 9113 -903 -2173 2287 N ATOM 1314 CZ ARG B 76 -39.349 26.930 -32.953 1.00 90.51 C ANISOU 1314 CZ ARG B 76 17412 7382 9597 -115 -2652 1807 C ATOM 1315 NH1 ARG B 76 -40.186 27.484 -32.059 1.00 91.18 N ANISOU 1315 NH1 ARG B 76 17272 7013 10361 651 -3304 1206 N ATOM 1316 NH2 ARG B 76 -39.841 26.169 -33.931 1.00 90.99 N ANISOU 1316 NH2 ARG B 76 17560 7712 9302 -77 -2508 1823 N ATOM 1317 N GLN B 77 -37.619 25.343 -26.591 1.00 51.23 N ANISOU 1317 N GLN B 77 9228 4185 6050 750 -262 223 N ATOM 1318 CA GLN B 77 -37.941 25.370 -25.186 1.00 50.17 C ANISOU 1318 CA GLN B 77 8542 4388 6133 996 -212 -259 C ATOM 1319 C GLN B 77 -36.761 24.779 -24.368 1.00 46.45 C ANISOU 1319 C GLN B 77 7886 4140 5622 673 329 -70 C ATOM 1320 O GLN B 77 -36.368 25.329 -23.323 1.00 47.28 O ANISOU 1320 O GLN B 77 7803 4253 5907 721 291 -248 O ATOM 1321 CB GLN B 77 -39.279 24.645 -25.017 1.00 50.33 C ANISOU 1321 CB GLN B 77 8080 5009 6032 1169 -206 -681 C ATOM 1322 CG GLN B 77 -40.105 25.000 -23.844 1.00 57.82 C ANISOU 1322 CG GLN B 77 8318 6633 7017 1458 -344 -1407 C ATOM 1323 CD GLN B 77 -40.321 26.506 -23.659 1.00 65.48 C ANISOU 1323 CD GLN B 77 9342 7193 8345 2153 -1094 -1979 C ATOM 1324 OE1 GLN B 77 -41.211 27.108 -24.274 1.00 75.94 O ANISOU 1324 OE1 GLN B 77 10727 8305 9821 2710 -1799 -2421 O ATOM 1325 NE2 GLN B 77 -39.511 27.108 -22.795 1.00 63.59 N ANISOU 1325 NE2 GLN B 77 9145 6750 8268 2180 -1119 -2032 N ATOM 1326 N LEU B 78 -36.138 23.717 -24.873 1.00 43.01 N ANISOU 1326 N LEU B 78 7536 3835 4971 449 693 196 N ATOM 1327 CA LEU B 78 -35.018 23.084 -24.131 1.00 41.64 C ANISOU 1327 CA LEU B 78 7201 3812 4808 314 984 225 C ATOM 1328 C LEU B 78 -33.758 23.916 -24.212 1.00 42.63 C ANISOU 1328 C LEU B 78 7340 3862 4993 134 1094 395 C ATOM 1329 O LEU B 78 -32.965 24.008 -23.263 1.00 43.30 O ANISOU 1329 O LEU B 78 7217 4001 5234 82 1180 326 O ATOM 1330 CB LEU B 78 -34.759 21.610 -24.575 1.00 40.67 C ANISOU 1330 CB LEU B 78 7178 3789 4486 347 1043 214 C ATOM 1331 CG LEU B 78 -35.777 20.538 -24.195 1.00 42.04 C ANISOU 1331 CG LEU B 78 7436 3990 4546 223 791 181 C ATOM 1332 CD1 LEU B 78 -35.471 19.140 -24.818 1.00 44.46 C ANISOU 1332 CD1 LEU B 78 8097 4087 4710 341 505 141 C ATOM 1333 CD2 LEU B 78 -35.799 20.450 -22.690 1.00 44.26 C ANISOU 1333 CD2 LEU B 78 7535 4439 4844 -64 738 157 C ATOM 1334 N ALA B 79 -33.576 24.548 -25.355 1.00 45.47 N ANISOU 1334 N ALA B 79 7971 4154 5150 -105 1034 669 N ATOM 1335 CA ALA B 79 -32.507 25.486 -25.567 1.00 49.14 C ANISOU 1335 CA ALA B 79 8509 4656 5505 -622 1035 979 C ATOM 1336 C ALA B 79 -32.588 26.679 -24.589 1.00 49.85 C ANISOU 1336 C ALA B 79 8766 4183 5992 -638 556 989 C ATOM 1337 O ALA B 79 -31.573 27.118 -24.045 1.00 51.00 O ANISOU 1337 O ALA B 79 8777 4390 6210 -968 606 1096 O ATOM 1338 CB ALA B 79 -32.565 26.023 -27.028 1.00 54.28 C ANISOU 1338 CB ALA B 79 9613 5328 5682 -1145 871 1416 C ATOM 1339 N ILE B 80 -33.790 27.212 -24.407 1.00 50.13 N ANISOU 1339 N ILE B 80 9048 3729 6269 -215 6 762 N ATOM 1340 CA ILE B 80 -33.998 28.318 -23.451 1.00 53.16 C ANISOU 1340 CA ILE B 80 9556 3602 7041 52 -631 479 C ATOM 1341 C ILE B 80 -33.555 27.873 -22.045 1.00 48.19 C ANISOU 1341 C ILE B 80 8366 3384 6559 221 -215 141 C ATOM 1342 O ILE B 80 -32.842 28.582 -21.336 1.00 48.94 O ANISOU 1342 O ILE B 80 8514 3231 6850 94 -443 144 O ATOM 1343 CB ILE B 80 -35.459 28.834 -23.503 1.00 55.68 C ANISOU 1343 CB ILE B 80 10010 3586 7561 751 -1362 -57 C ATOM 1344 CG1 ILE B 80 -35.674 29.619 -24.813 1.00 63.57 C ANISOU 1344 CG1 ILE B 80 11866 3818 8472 495 -2157 384 C ATOM 1345 CG2 ILE B 80 -35.751 29.739 -22.311 1.00 60.75 C ANISOU 1345 CG2 ILE B 80 10516 3996 8569 1338 -1993 -746 C ATOM 1346 CD1 ILE B 80 -37.135 30.032 -25.113 1.00 68.12 C ANISOU 1346 CD1 ILE B 80 12594 4029 9258 1311 -3035 -225 C ATOM 1347 N ILE B 81 -33.966 26.664 -21.677 1.00 43.51 N ANISOU 1347 N ILE B 81 7343 3369 5818 391 288 -76 N ATOM 1348 CA ILE B 81 -33.631 26.126 -20.372 1.00 41.23 C ANISOU 1348 CA ILE B 81 6675 3453 5537 402 557 -297 C ATOM 1349 C ILE B 81 -32.107 25.965 -20.271 1.00 41.87 C ANISOU 1349 C ILE B 81 6748 3486 5674 75 794 5 C ATOM 1350 O ILE B 81 -31.549 26.348 -19.254 1.00 41.16 O ANISOU 1350 O ILE B 81 6539 3355 5743 60 712 -118 O ATOM 1351 CB ILE B 81 -34.386 24.786 -20.109 1.00 39.78 C ANISOU 1351 CB ILE B 81 6257 3802 5055 353 825 -399 C ATOM 1352 CG1 ILE B 81 -35.871 25.115 -19.896 1.00 41.56 C ANISOU 1352 CG1 ILE B 81 6181 4453 5156 609 619 -886 C ATOM 1353 CG2 ILE B 81 -33.761 23.976 -18.918 1.00 35.36 C ANISOU 1353 CG2 ILE B 81 5574 3481 4378 100 966 -375 C ATOM 1354 CD1 ILE B 81 -36.737 23.882 -19.850 1.00 45.07 C ANISOU 1354 CD1 ILE B 81 6421 5512 5192 271 807 -857 C ATOM 1355 N GLY B 82 -31.460 25.387 -21.302 1.00 41.83 N ANISOU 1355 N GLY B 82 6762 3642 5489 -129 1065 263 N ATOM 1356 CA GLY B 82 -29.990 25.327 -21.361 1.00 44.78 C ANISOU 1356 CA GLY B 82 6887 4293 5834 -401 1279 350 C ATOM 1357 C GLY B 82 -29.339 26.685 -21.048 1.00 49.51 C ANISOU 1357 C GLY B 82 7576 4649 6587 -827 1028 568 C ATOM 1358 O GLY B 82 -28.406 26.756 -20.253 1.00 49.77 O ANISOU 1358 O GLY B 82 7334 4807 6768 -922 1063 477 O ATOM 1359 N ASP B 83 -29.860 27.758 -21.649 1.00 53.38 N ANISOU 1359 N ASP B 83 8557 4667 7060 -1088 593 856 N ATOM 1360 CA ASP B 83 -29.324 29.093 -21.405 1.00 61.48 C ANISOU 1360 CA ASP B 83 9930 5200 8230 -1594 29 1140 C ATOM 1361 C ASP B 83 -29.534 29.499 -19.959 1.00 60.09 C ANISOU 1361 C ASP B 83 9720 4628 8484 -1079 -324 696 C ATOM 1362 O ASP B 83 -28.610 30.044 -19.357 1.00 62.27 O ANISOU 1362 O ASP B 83 9964 4793 8905 -1425 -504 793 O ATOM 1363 CB ASP B 83 -29.900 30.160 -22.370 1.00 67.24 C ANISOU 1363 CB ASP B 83 11472 5225 8850 -1987 -745 1566 C ATOM 1364 CG ASP B 83 -29.509 29.909 -23.824 1.00 74.34 C ANISOU 1364 CG ASP B 83 12442 6684 9121 -2797 -408 2115 C ATOM 1365 OD1 ASP B 83 -28.516 29.145 -24.049 1.00 75.66 O ANISOU 1365 OD1 ASP B 83 11906 7907 8933 -3127 388 2092 O ATOM 1366 OD2 ASP B 83 -30.200 30.458 -24.736 1.00 77.12 O ANISOU 1366 OD2 ASP B 83 13514 6501 9287 -3040 -1006 2462 O ATOM 1367 N ASP B 84 -30.722 29.212 -19.401 1.00 57.98 N ANISOU 1367 N ASP B 84 9365 4340 8323 -331 -397 164 N ATOM 1368 CA ASP B 84 -31.026 29.540 -17.991 1.00 59.05 C ANISOU 1368 CA ASP B 84 9318 4450 8667 167 -658 -424 C ATOM 1369 C ASP B 84 -30.067 28.839 -17.043 1.00 56.78 C ANISOU 1369 C ASP B 84 8637 4585 8352 -6 -183 -417 C ATOM 1370 O ASP B 84 -29.660 29.431 -16.053 1.00 59.14 O ANISOU 1370 O ASP B 84 8927 4713 8829 66 -484 -642 O ATOM 1371 CB ASP B 84 -32.435 29.111 -17.595 1.00 57.87 C ANISOU 1371 CB ASP B 84 8850 4774 8366 785 -597 -1051 C ATOM 1372 CG ASP B 84 -33.531 29.880 -18.338 1.00 63.73 C ANISOU 1372 CG ASP B 84 9882 5119 9213 1239 -1276 -1354 C ATOM 1373 OD1 ASP B 84 -33.271 31.016 -18.824 1.00 67.01 O ANISOU 1373 OD1 ASP B 84 10947 4617 9894 1185 -2120 -1173 O ATOM 1374 OD2 ASP B 84 -34.663 29.325 -18.441 1.00 63.09 O ANISOU 1374 OD2 ASP B 84 9422 5629 8919 1585 -1085 -1760 O ATOM 1375 N ILE B 85 -29.755 27.564 -17.322 1.00 53.25 N ANISOU 1375 N ILE B 85 7930 4606 7696 -137 390 -244 N ATOM 1376 CA ILE B 85 -28.847 26.742 -16.503 1.00 51.46 C ANISOU 1376 CA ILE B 85 7437 4652 7464 -197 608 -290 C ATOM 1377 C ILE B 85 -27.434 27.408 -16.434 1.00 55.69 C ANISOU 1377 C ILE B 85 7848 5096 8215 -548 511 -128 C ATOM 1378 O ILE B 85 -26.860 27.578 -15.347 1.00 56.74 O ANISOU 1378 O ILE B 85 7884 5171 8504 -522 344 -289 O ATOM 1379 CB ILE B 85 -28.757 25.274 -17.016 1.00 48.47 C ANISOU 1379 CB ILE B 85 6967 4567 6881 -139 886 -235 C ATOM 1380 CG1 ILE B 85 -30.081 24.510 -16.768 1.00 47.93 C ANISOU 1380 CG1 ILE B 85 7043 4635 6532 -50 875 -315 C ATOM 1381 CG2 ILE B 85 -27.628 24.528 -16.340 1.00 48.43 C ANISOU 1381 CG2 ILE B 85 6791 4651 6961 -85 800 -361 C ATOM 1382 CD1 ILE B 85 -30.206 23.178 -17.558 1.00 44.86 C ANISOU 1382 CD1 ILE B 85 6794 4284 5968 -15 903 -209 C ATOM 1383 N ASN B 86 -26.894 27.791 -17.583 1.00 59.43 N ANISOU 1383 N ASN B 86 8297 5682 8600 -1003 601 204 N ATOM 1384 CA ASN B 86 -25.607 28.480 -17.631 1.00 65.58 C ANISOU 1384 CA ASN B 86 8864 6633 9422 -1633 517 423 C ATOM 1385 C ASN B 86 -25.514 29.687 -16.691 1.00 68.97 C ANISOU 1385 C ASN B 86 9649 6391 10166 -1773 -109 452 C ATOM 1386 O ASN B 86 -24.542 29.825 -15.917 1.00 71.29 O ANISOU 1386 O ASN B 86 9666 6799 10623 -1943 -188 368 O ATOM 1387 CB ASN B 86 -25.307 28.948 -19.054 1.00 70.48 C ANISOU 1387 CB ASN B 86 9526 7588 9665 -2428 610 900 C ATOM 1388 CG ASN B 86 -25.000 27.813 -19.989 1.00 68.60 C ANISOU 1388 CG ASN B 86 8729 8297 9038 -2321 1229 707 C ATOM 1389 OD1 ASN B 86 -24.357 26.832 -19.627 1.00 65.18 O ANISOU 1389 OD1 ASN B 86 7709 8401 8656 -1854 1479 212 O ATOM 1390 ND2 ASN B 86 -25.440 27.955 -21.219 1.00 70.22 N ANISOU 1390 ND2 ASN B 86 9166 8676 8838 -2700 1329 1026 N ATOM 1391 N ARG B 87 -26.521 30.553 -16.755 1.00 71.15 N ANISOU 1391 N ARG B 87 10537 5948 10549 -1596 -682 455 N ATOM 1392 CA ARG B 87 -26.537 31.760 -15.915 1.00 76.05 C ANISOU 1392 CA ARG B 87 11604 5798 11493 -1530 -1538 299 C ATOM 1393 C ARG B 87 -26.667 31.337 -14.462 1.00 72.70 C ANISOU 1393 C ARG B 87 10850 5589 11183 -852 -1405 -324 C ATOM 1394 O ARG B 87 -25.997 31.904 -13.570 1.00 74.45 O ANISOU 1394 O ARG B 87 11115 5557 11617 -936 -1796 -446 O ATOM 1395 CB ARG B 87 -27.686 32.688 -16.309 1.00 80.00 C ANISOU 1395 CB ARG B 87 12815 5472 12110 -1177 -2406 156 C ATOM 1396 CG ARG B 87 -27.542 33.287 -17.689 1.00 87.14 C ANISOU 1396 CG ARG B 87 14327 5950 12833 -2045 -2839 910 C ATOM 1397 CD ARG B 87 -28.678 34.281 -17.988 1.00 95.53 C ANISOU 1397 CD ARG B 87 16271 5913 14112 -1539 -4082 670 C ATOM 1398 NE ARG B 87 -29.880 33.603 -18.472 1.00 93.14 N ANISOU 1398 NE ARG B 87 15740 5962 13687 -795 -3697 285 N ATOM 1399 CZ ARG B 87 -30.279 33.578 -19.746 1.00 95.36 C ANISOU 1399 CZ ARG B 87 16429 6080 13724 -1153 -3815 755 C ATOM 1400 NH1 ARG B 87 -31.376 32.914 -20.075 1.00 91.42 N ANISOU 1400 NH1 ARG B 87 15637 5952 13148 -434 -3463 332 N ATOM 1401 NH2 ARG B 87 -29.589 34.200 -20.697 1.00100.82 N ANISOU 1401 NH2 ARG B 87 17813 6343 14150 -2366 -4298 1684 N ATOM 1402 N ARG B 88 -27.510 30.321 -14.238 1.00 67.24 N ANISOU 1402 N ARG B 88 9870 5415 10261 -337 -899 -653 N ATOM 1403 CA ARG B 88 -27.749 29.802 -12.896 1.00 66.24 C ANISOU 1403 CA ARG B 88 9484 5692 9993 43 -765 -1134 C ATOM 1404 C ARG B 88 -26.441 29.354 -12.272 1.00 66.55 C ANISOU 1404 C ARG B 88 9315 5846 10123 -253 -628 -965 C ATOM 1405 O ARG B 88 -26.108 29.828 -11.197 1.00 69.02 O ANISOU 1405 O ARG B 88 9658 6038 10529 -160 -958 -1233 O ATOM 1406 CB ARG B 88 -28.798 28.699 -12.881 1.00 62.35 C ANISOU 1406 CB ARG B 88 8782 5825 9082 243 -309 -1296 C ATOM 1407 CG ARG B 88 -29.714 28.702 -11.655 1.00 63.38 C ANISOU 1407 CG ARG B 88 8694 6562 8827 543 -375 -1936 C ATOM 1408 CD ARG B 88 -29.594 27.458 -10.789 1.00 61.40 C ANISOU 1408 CD ARG B 88 8333 6897 8101 163 -59 -1794 C ATOM 1409 NE ARG B 88 -29.924 26.198 -11.528 1.00 58.89 N ANISOU 1409 NE ARG B 88 8093 6730 7554 -141 248 -1360 N ATOM 1410 CZ ARG B 88 -29.418 24.996 -11.228 1.00 57.26 C ANISOU 1410 CZ ARG B 88 8108 6488 7161 -505 209 -1000 C ATOM 1411 NH1 ARG B 88 -28.550 24.886 -10.217 1.00 55.68 N ANISOU 1411 NH1 ARG B 88 8028 6161 6966 -627 -54 -991 N ATOM 1412 NH2 ARG B 88 -29.764 23.905 -11.920 1.00 53.26 N ANISOU 1412 NH2 ARG B 88 7796 5957 6484 -705 252 -686 N ATOM 1413 N TYR B 89 -25.677 28.516 -12.973 1.00 66.52 N ANISOU 1413 N TYR B 89 9068 6103 10104 -518 -250 -646 N ATOM 1414 CA TYR B 89 -24.344 28.075 -12.520 1.00 69.06 C ANISOU 1414 CA TYR B 89 9059 6617 10563 -661 -246 -656 C ATOM 1415 C TYR B 89 -23.301 29.180 -12.317 1.00 75.37 C ANISOU 1415 C TYR B 89 9764 7229 11644 -1101 -577 -545 C ATOM 1416 O TYR B 89 -22.393 29.038 -11.495 1.00 77.43 O ANISOU 1416 O TYR B 89 9788 7577 12054 -1103 -739 -707 O ATOM 1417 CB TYR B 89 -23.770 27.052 -13.464 1.00 69.02 C ANISOU 1417 CB TYR B 89 8674 7080 10471 -660 92 -616 C ATOM 1418 CG TYR B 89 -24.446 25.701 -13.435 1.00 65.11 C ANISOU 1418 CG TYR B 89 8354 6628 9757 -261 150 -737 C ATOM 1419 CD1 TYR B 89 -25.449 25.392 -12.505 1.00 61.66 C ANISOU 1419 CD1 TYR B 89 8319 6022 9088 -181 1 -759 C ATOM 1420 CD2 TYR B 89 -24.055 24.726 -14.323 1.00 64.70 C ANISOU 1420 CD2 TYR B 89 8055 6888 9643 -47 260 -872 C ATOM 1421 CE1 TYR B 89 -26.046 24.138 -12.482 1.00 59.92 C ANISOU 1421 CE1 TYR B 89 8376 5822 8568 -124 -95 -710 C ATOM 1422 CE2 TYR B 89 -24.644 23.495 -14.323 1.00 65.09 C ANISOU 1422 CE2 TYR B 89 8442 6767 9521 257 60 -942 C ATOM 1423 CZ TYR B 89 -25.645 23.191 -13.404 1.00 62.51 C ANISOU 1423 CZ TYR B 89 8648 6144 8958 111 -151 -761 C ATOM 1424 OH TYR B 89 -26.203 21.914 -13.437 1.00 63.40 O ANISOU 1424 OH TYR B 89 9216 6058 8817 142 -505 -686 O ATOM 1425 N ASP B 90 -23.434 30.285 -13.043 1.00 80.39 N ANISOU 1425 N ASP B 90 10679 7534 12333 -1556 -828 -230 N ATOM 1426 CA ASP B 90 -22.566 31.465 -12.831 1.00 88.14 C ANISOU 1426 CA ASP B 90 11793 8166 13532 -2205 -1388 3 C ATOM 1427 C ASP B 90 -22.798 32.221 -11.501 1.00 89.92 C ANISOU 1427 C ASP B 90 12430 7715 14022 -1798 -2072 -376 C ATOM 1428 O ASP B 90 -22.071 33.164 -11.182 1.00 95.48 O ANISOU 1428 O ASP B 90 13333 7995 14951 -2291 -2690 -224 O ATOM 1429 CB ASP B 90 -22.654 32.420 -14.030 1.00 94.35 C ANISOU 1429 CB ASP B 90 13012 8641 14197 -3032 -1734 593 C ATOM 1430 CG ASP B 90 -21.864 31.922 -15.223 1.00 97.86 C ANISOU 1430 CG ASP B 90 12837 10107 14238 -3826 -1098 970 C ATOM 1431 OD1 ASP B 90 -20.623 32.097 -15.223 1.00104.90 O ANISOU 1431 OD1 ASP B 90 13168 11652 15037 -4610 -1036 1115 O ATOM 1432 OD2 ASP B 90 -22.480 31.360 -16.157 1.00 95.71 O ANISOU 1432 OD2 ASP B 90 12546 10137 13682 -3669 -667 1032 O ATOM 1433 N SER B 91 -23.796 31.775 -10.734 1.00 86.40 N ANISOU 1433 N SER B 91 12059 7320 13451 -989 -1973 -897 N ATOM 1434 CA SER B 91 -24.114 32.316 -9.414 1.00 88.89 C ANISOU 1434 CA SER B 91 12583 7381 13812 -488 -2487 -1476 C ATOM 1435 C SER B 91 -24.271 31.161 -8.400 1.00 85.53 C ANISOU 1435 C SER B 91 11843 7632 13024 -169 -2015 -1781 C ATOM 1436 O SER B 91 -23.311 30.446 -8.062 1.00 84.73 O ANISOU 1436 O SER B 91 11506 7730 12959 -392 -1847 -1601 O ATOM 1437 CB SER B 91 -25.423 33.100 -9.504 1.00 91.87 C ANISOU 1437 CB SER B 91 13340 7411 14154 109 -2999 -1975 C ATOM 1438 OG SER B 91 -25.601 33.652 -10.810 1.00 93.34 O ANISOU 1438 OG SER B 91 13914 7048 14503 -230 -3306 -1517 O TER 1439 SER B 91 HETATM 1440 N NO3 A1158 -36.763 -0.157 -10.374 1.00 52.63 N ANISOU 1440 N NO3 A1158 7277 6522 6197 417 382 682 N HETATM 1441 O1 NO3 A1158 -36.117 -0.079 -11.610 1.00 50.92 O1- ANISOU 1441 O1 NO3 A1158 6958 6255 6134 489 335 592 O1- HETATM 1442 O2 NO3 A1158 -38.045 0.409 -10.303 1.00 53.06 O ANISOU 1442 O2 NO3 A1158 7286 6670 6205 325 525 648 O HETATM 1443 O3 NO3 A1158 -36.127 -0.790 -9.275 1.00 55.14 O ANISOU 1443 O3 NO3 A1158 7734 6803 6414 439 285 801 O HETATM 1444 N NO3 A1159 -32.261 25.123 -14.096 1.00 63.54 N ANISOU 1444 N NO3 A1159 8797 7354 7990 249 43 -941 N HETATM 1445 O1 NO3 A1159 -31.276 24.253 -13.694 1.00 64.89 O1- ANISOU 1445 O1 NO3 A1159 8882 7688 8084 178 34 -932 O1- HETATM 1446 O2 NO3 A1159 -32.043 26.361 -14.662 1.00 61.60 O ANISOU 1446 O2 NO3 A1159 8665 6924 7816 177 -8 -953 O HETATM 1447 O3 NO3 A1159 -33.508 24.640 -13.870 1.00 67.42 O ANISOU 1447 O3 NO3 A1159 9251 7879 8487 399 102 -934 O HETATM 1448 N NO3 A1160 -28.468 1.287 -7.960 1.00 77.21 N ANISOU 1448 N NO3 A1160 10248 9818 9268 1009 -551 572 N HETATM 1449 O1 NO3 A1160 -27.424 0.351 -8.166 1.00 79.05 O1- ANISOU 1449 O1 NO3 A1160 10433 9968 9633 1137 -698 601 O1- HETATM 1450 O2 NO3 A1160 -28.510 2.441 -8.706 1.00 74.61 O ANISOU 1450 O2 NO3 A1160 9796 9568 8985 964 -454 428 O HETATM 1451 O3 NO3 A1160 -29.478 1.103 -6.995 1.00 78.38 O ANISOU 1451 O3 NO3 A1160 10568 9974 9238 924 -496 682 O HETATM 1452 N NO3 A1161 -38.871 5.016 -12.871 1.00 58.48 N ANISOU 1452 N NO3 A1161 7548 7590 7082 434 642 204 N HETATM 1453 O1 NO3 A1161 -38.952 3.635 -12.665 1.00 59.82 O1- ANISOU 1453 O1 NO3 A1161 7780 7699 7249 389 640 302 O1- HETATM 1454 O2 NO3 A1161 -40.114 5.576 -12.931 1.00 59.30 O ANISOU 1454 O2 NO3 A1161 7585 7751 7195 406 736 162 O HETATM 1455 O3 NO3 A1161 -37.664 5.821 -13.045 1.00 59.01 O ANISOU 1455 O3 NO3 A1161 7610 7656 7156 497 556 146 O HETATM 1456 C1 EDO A1162 -44.020 -3.283 -20.518 1.00 55.38 C ANISOU 1456 C1 EDO A1162 7015 6615 7410 -243 703 228 C HETATM 1457 O1 EDO A1162 -42.966 -4.295 -20.680 1.00 57.60 O ANISOU 1457 O1 EDO A1162 7424 6731 7729 -202 656 231 O HETATM 1458 C2 EDO A1162 -43.663 -1.966 -21.248 1.00 50.86 C ANISOU 1458 C2 EDO A1162 6356 6147 6820 -145 664 150 C HETATM 1459 O2 EDO A1162 -44.034 -0.726 -20.565 1.00 51.45 O ANISOU 1459 O2 EDO A1162 6353 6353 6842 -97 697 163 O HETATM 1460 C1 EDO A1163 -44.540 -5.080 -28.981 1.00 51.96 C ANISOU 1460 C1 EDO A1163 6560 6083 7100 -557 419 -386 C HETATM 1461 O1 EDO A1163 -43.298 -5.632 -29.552 1.00 51.41 O ANISOU 1461 O1 EDO A1163 6594 5913 7027 -495 432 -480 O HETATM 1462 C2 EDO A1163 -44.444 -3.576 -28.691 1.00 47.75 C ANISOU 1462 C2 EDO A1163 5942 5693 6506 -461 411 -327 C HETATM 1463 O2 EDO A1163 -45.371 -3.078 -27.679 1.00 45.37 O ANISOU 1463 O2 EDO A1163 5547 5464 6228 -469 430 -232 O HETATM 1464 O HOH A2001 -16.422 10.630 -20.527 1.00 57.28 O ANISOU 1464 O HOH A2001 5423 8443 7899 148 142 -1151 O HETATM 1465 O HOH A2002 -16.774 7.664 -17.304 1.00 66.46 O ANISOU 1465 O HOH A2002 6660 9442 9149 760 -332 -965 O HETATM 1466 O HOH A2003 -14.826 11.609 -23.119 1.00 77.07 O ANISOU 1466 O HOH A2003 7639 11200 10444 -227 492 -1369 O HETATM 1467 O HOH A2004 -21.131 3.563 -25.550 1.00 53.36 O ANISOU 1467 O HOH A2004 5442 7344 7489 691 628 -1152 O HETATM 1468 O HOH A2005 -21.622 5.164 -28.083 1.00 54.17 O ANISOU 1468 O HOH A2005 5642 7596 7344 302 902 -1212 O HETATM 1469 O HOH A2006 -29.638 0.100 -26.902 1.00 67.92 O ANISOU 1469 O HOH A2006 8247 8471 9088 559 610 -722 O HETATM 1470 O HOH A2007 -27.469 1.894 -27.033 1.00 51.58 O ANISOU 1470 O HOH A2007 5974 6638 6985 536 660 -817 O HETATM 1471 O HOH A2008 -29.661 2.266 -28.389 1.00 65.36 O ANISOU 1471 O HOH A2008 7905 8356 8571 345 695 -746 O HETATM 1472 O HOH A2009 -35.006 7.979 -15.462 1.00 41.04 O ANISOU 1472 O HOH A2009 5202 5344 5048 564 393 -45 O HETATM 1473 O HOH A2010 -35.654 5.493 -15.461 1.00 41.82 O ANISOU 1473 O HOH A2010 5338 5368 5184 551 419 79 O HETATM 1474 O HOH A2011 -29.888 -3.884 -8.116 1.00 67.06 O ANISOU 1474 O HOH A2011 9397 7901 8183 1073 -610 1039 O HETATM 1475 O HOH A2012 -34.700 11.994 -7.404 1.00 57.13 O ANISOU 1475 O HOH A2012 7669 7749 6288 567 375 -292 O HETATM 1476 O HOH A2013 -40.929 -3.460 -15.047 1.00 63.18 O ANISOU 1476 O HOH A2013 8431 7516 8058 19 663 608 O HETATM 1477 O HOH A2014 -41.646 -7.100 -10.781 1.00 61.48 O ANISOU 1477 O HOH A2014 9479 5473 8405 312 -461 -493 O HETATM 1478 O HOH A2015 -37.401 0.888 -14.832 1.00 46.90 O ANISOU 1478 O HOH A2015 6176 5769 5877 429 480 357 O HETATM 1479 O HOH A2016 -34.833 -7.612 -13.690 1.00 60.99 O ANISOU 1479 O HOH A2016 8475 6561 8135 853 4 -705 O HETATM 1480 O HOH A2017 -32.552 -8.144 -22.559 1.00 46.59 O ANISOU 1480 O HOH A2017 6235 4588 6879 841 264 -254 O HETATM 1481 O HOH A2018 -23.800 -6.556 -27.139 1.00 63.45 O ANISOU 1481 O HOH A2018 7280 7401 9429 1498 559 -1427 O HETATM 1482 O HOH A2019 -18.933 -0.068 -22.909 1.00 70.30 O ANISOU 1482 O HOH A2019 7296 9272 10143 1407 222 -1216 O HETATM 1483 O HOH A2020 -17.229 -1.796 -21.750 1.00 89.08 O ANISOU 1483 O HOH A2020 9441 11563 12840 1822 -35 -1283 O HETATM 1484 O HOH A2021 -23.304 -1.895 -9.854 1.00 62.44 O ANISOU 1484 O HOH A2021 7871 7683 8172 1659 -1120 436 O HETATM 1485 O HOH A2022 -20.396 0.891 -7.775 1.00 59.12 O ANISOU 1485 O HOH A2022 7120 7784 7560 1655 -1524 270 O HETATM 1486 O HOH A2023 -26.483 4.316 -3.370 1.00 76.58 O ANISOU 1486 O HOH A2023 11164 9212 8722 -3212 772 465 O HETATM 1487 O HOH A2024 -17.410 5.429 -7.343 1.00 60.78 O ANISOU 1487 O HOH A2024 6762 8627 7706 1331 -1672 -220 O HETATM 1488 O HOH A2025 -16.778 11.635 -9.275 1.00 74.82 O ANISOU 1488 O HOH A2025 8287 10694 9446 526 -1216 -784 O HETATM 1489 O HOH A2026 -34.115 21.918 -6.283 1.00 63.11 O ANISOU 1489 O HOH A2026 8759 8082 7137 554 323 -1298 O HETATM 1490 O HOH A2027 -37.262 27.453 -12.332 1.00 49.38 O ANISOU 1490 O HOH A2027 7148 5213 6401 875 198 -1292 O HETATM 1491 O HOH A2028 -35.332 27.996 -11.212 1.00 57.85 O ANISOU 1491 O HOH A2028 8356 6301 7326 659 141 -1414 O HETATM 1492 O HOH A2029 -45.223 19.012 -12.923 1.00 60.25 O ANISOU 1492 O HOH A2029 7356 7711 7824 1232 838 -880 O HETATM 1493 O HOH A2030 -48.632 19.581 -17.741 1.00 59.23 O ANISOU 1493 O HOH A2030 6806 7415 8285 1494 452 -679 O HETATM 1494 O HOH A2031 -40.687 27.341 -19.778 1.00 48.37 O ANISOU 1494 O HOH A2031 6890 4698 6789 1095 -193 -530 O HETATM 1495 O HOH A2032 -45.146 9.013 -21.487 1.00 48.85 O ANISOU 1495 O HOH A2032 5652 6407 6502 451 502 -73 O HETATM 1496 O HOH A2033 -49.739 16.262 -24.313 1.00 72.37 O ANISOU 1496 O HOH A2033 8311 9201 9985 1113 -103 -153 O HETATM 1497 O HOH A2034 -47.620 9.648 -30.748 1.00 53.14 O ANISOU 1497 O HOH A2034 6202 6989 7000 191 -285 48 O HETATM 1498 O HOH A2035 -42.605 12.835 -40.239 1.00 73.99 O ANISOU 1498 O HOH A2035 10111 9660 8340 -612 -702 401 O HETATM 1499 O HOH A2036 -29.275 13.641 -34.227 1.00 66.41 O ANISOU 1499 O HOH A2036 8637 8847 7748 -846 738 -273 O HETATM 1500 O HOH A2037 -25.998 18.164 -33.452 1.00 62.59 O ANISOU 1500 O HOH A2037 8253 8298 7231 -1364 815 -164 O HETATM 1501 O HOH A2038 -24.208 22.997 -29.714 1.00 67.96 O ANISOU 1501 O HOH A2038 9081 8544 8196 -1609 580 -126 O HETATM 1502 O HOH A2039 -25.932 24.565 -37.826 1.00 52.02 O ANISOU 1502 O HOH A2039 6904 7210 5653 625 -364 -162 O HETATM 1503 O HOH A2040 -26.479 24.453 -31.275 1.00 61.05 O ANISOU 1503 O HOH A2040 8695 7311 7191 -1614 400 188 O HETATM 1504 O HOH A2041 -25.428 24.607 -28.837 1.00 60.37 O ANISOU 1504 O HOH A2041 8387 7248 7304 -1515 388 -27 O HETATM 1505 O HOH A2042 -18.445 25.063 -27.806 1.00 81.37 O ANISOU 1505 O HOH A2042 10239 10594 10083 -2384 757 -524 O HETATM 1506 O HOH A2043 -22.881 26.687 -29.634 1.00 90.92 O ANISOU 1506 O HOH A2043 12352 11096 11096 -2158 512 -14 O HETATM 1507 O HOH A2044 -19.445 24.939 -21.050 1.00 63.43 O ANISOU 1507 O HOH A2044 7873 8144 8085 -1607 170 -843 O HETATM 1508 O HOH A2045 -38.850 14.902 -20.572 1.00 36.72 O ANISOU 1508 O HOH A2045 4621 4565 4767 564 326 -188 O HETATM 1509 O HOH A2046 -43.810 14.011 -18.125 1.00 50.99 O ANISOU 1509 O HOH A2046 6103 6577 6696 793 552 -281 O HETATM 1510 O HOH A2047 -40.566 13.748 -12.560 1.00 50.17 O ANISOU 1510 O HOH A2047 6342 6631 6089 722 730 -401 O HETATM 1511 O HOH A2048 -42.176 11.789 -14.376 1.00 52.11 O ANISOU 1511 O HOH A2048 6409 6894 6496 662 767 -254 O HETATM 1512 O HOH A2049 -43.547 1.398 -18.270 1.00 39.86 O ANISOU 1512 O HOH A2049 4875 5052 5219 67 762 204 O HETATM 1513 O HOH A2050 -41.941 1.438 -11.972 1.00 57.78 O ANISOU 1513 O HOH A2050 7556 7442 6957 116 881 473 O HETATM 1514 O HOH A2051 -49.318 4.443 -13.929 1.00 60.44 O ANISOU 1514 O HOH A2051 6950 8332 7685 -13 1341 49 O HETATM 1515 O HOH A2052 -49.185 2.176 -13.644 1.00 63.29 O ANISOU 1515 O HOH A2052 7465 8592 7989 -247 1376 220 O HETATM 1516 O HOH A2053 -46.809 -3.419 -24.043 1.00 43.36 O ANISOU 1516 O HOH A2053 5216 5228 6030 -522 615 12 O HETATM 1517 O HOH A2054 -30.497 1.163 -29.758 1.00 40.07 O ANISOU 1517 O HOH A2054 4782 5099 5344 282 742 -828 O HETATM 1518 O HOH A2055 -32.292 6.623 -32.992 1.00 49.83 O ANISOU 1518 O HOH A2055 6273 6638 6024 -252 694 -568 O HETATM 1519 O HOH A2056 -26.537 8.914 -32.927 1.00 56.23 O ANISOU 1519 O HOH A2056 6761 7786 6819 -477 1026 -800 O HETATM 1520 O HOH A2057 -26.982 12.850 -32.393 1.00 41.99 O ANISOU 1520 O HOH A2057 5206 5866 4881 -733 869 -487 O HETATM 1521 O HOH A2058 -20.262 16.966 -30.048 1.00 47.97 O ANISOU 1521 O HOH A2058 5420 6964 5843 -1356 1056 -746 O HETATM 1522 O HOH A2059 -22.236 8.058 -26.639 1.00 42.91 O ANISOU 1522 O HOH A2059 4375 6166 5762 92 755 -966 O HETATM 1523 O HOH A2060 -17.802 7.407 -27.461 1.00 57.25 O ANISOU 1523 O HOH A2060 5483 8421 7850 84 959 -1423 O HETATM 1524 O HOH A2061 -19.951 13.211 -31.325 1.00 62.21 O ANISOU 1524 O HOH A2061 6903 9015 7721 -1026 1265 -1017 O HETATM 1525 O HOH A2062 -18.030 22.442 -28.708 1.00 94.90 O ANISOU 1525 O HOH A2062 11582 12686 11791 -2167 941 -649 O HETATM 1526 O HOH A2063 -11.675 12.341 -22.508 1.00 83.10 O ANISOU 1526 O HOH A2063 7788 12361 11426 -391 429 -1640 O HETATM 1527 O HOH A2064 -15.189 10.381 -17.864 1.00 57.04 O ANISOU 1527 O HOH A2064 5228 8508 7934 338 -240 -1152 O HETATM 1528 O HOH A2065 -36.865 0.446 -7.082 1.00 63.26 O ANISOU 1528 O HOH A2065 8877 8075 7086 338 386 830 O HETATM 1529 O HOH B2001 -42.426 18.132 -35.839 1.00 63.60 O ANISOU 1529 O HOH B2001 8790 7746 7628 -57 -791 651 O HETATM 1530 O HOH B2002 -44.575 17.864 -35.196 1.00 61.73 O ANISOU 1530 O HOH B2002 8314 7525 7616 192 -943 623 O HETATM 1531 O HOH B2003 -39.733 21.022 -36.071 1.00 71.47 O ANISOU 1531 O HOH B2003 10233 8454 8468 -312 -728 823 O HETATM 1532 O HOH B2004 -38.013 27.182 -21.596 1.00 60.89 O ANISOU 1532 O HOH B2004 8673 6276 8187 638 -254 -297 O HETATM 1533 O HOH B2005 -34.997 27.600 -16.510 1.00 61.87 O ANISOU 1533 O HOH B2005 8817 6591 8098 465 -39 -830 O HETATM 1534 O HOH B2006 -27.344 27.054 -8.497 1.00 61.49 O ANISOU 1534 O HOH B2006 8713 7365 7285 -232 -275 -1561 O HETATM 1535 O HOH B2007 -28.180 21.445 -11.756 1.00 44.16 O ANISOU 1535 O HOH B2007 5977 5578 5226 58 -83 -931 O HETATM 1536 O HOH B2008 -21.051 30.407 -9.523 1.00 78.07 O ANISOU 1536 O HOH B2008 10675 9390 9598 -1322 -666 -1813 O CONECT 1440 1441 1442 1443 CONECT 1441 1440 CONECT 1442 1440 CONECT 1443 1440 CONECT 1444 1445 1446 1447 CONECT 1445 1444 CONECT 1446 1444 CONECT 1447 1444 CONECT 1448 1449 1450 1451 CONECT 1449 1448 CONECT 1450 1448 CONECT 1451 1448 CONECT 1452 1453 1454 1455 CONECT 1453 1452 CONECT 1454 1452 CONECT 1455 1452 CONECT 1456 1457 1458 CONECT 1457 1456 CONECT 1458 1456 1459 CONECT 1459 1458 CONECT 1460 1461 1462 CONECT 1461 1460 CONECT 1462 1460 1463 CONECT 1463 1462 MASTER 524 0 6 10 0 0 11 6 1534 2 24 16 END
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Related entries of code: 2xpx
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
Check Database
Protein Sequence Similarity
1bxl
RCSB PDB
PDBbind
16aa, >1BXL_2|Chain... at 100%
3qbr
RCSB PDB
PDBbind
34aa, >3QBR_2|Chains... at 100%
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
2xpx
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
APOPTOSIS REGULATOR BHRF1
Ligand Name
Bak BH3 peptide
EC.Number
E.C.-.-.-.-
Resolution
2.05(Å)
Affinity (Kd/Ki/IC50)
Kd=150nM
Release Year
2011
Protein/NA Sequence
Check fasta file
Primary Reference
(2010) Plos Pathog. Vol. 6: pp. 1236
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
P03182
Q16611
Entrez Gene ID
NCBI Entrez Gene ID:
3783706
578
ASD
Information of known allosteric effects of PDB entries
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