Browse entries in the PDBbind-CN Database
HEADER BETA-LACTAMASE 23-JUN-00 1E3U TITLE MAD STRUCTURE OF OXA10 CLASS D BETA-LACTAMASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: BETA-LACTAMASE OXA-10; COMPND 3 CHAIN: A, B, C; COMPND 4 EC: 3.5.2.6; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: BETA-LACTAMASE OXA-10; COMPND 8 CHAIN: D; COMPND 9 EC: 3.5.2.6; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA; SOURCE 3 ORGANISM_TAXID: 287; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_CELLULAR_LOCATION: EXCRETED; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET24A; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA; SOURCE 11 ORGANISM_TAXID: 287; SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 14 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 15 EXPRESSION_SYSTEM_CELLULAR_LOCATION: EXCRETED; SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: PET24A KEYWDS BETA-LACTAMASE, ANTIOBITIC RESISTANCE EXPDTA X-RAY DIFFRACTION AUTHOR L.MAVEYRAUD,D.GOLEMI,L.P.KOTRA,S.TRANIER,S.VAKULENKO,S.MOBASHERY, AUTHOR 2 J.P.SAMAMA REVDAT 4 24-JUL-19 1E3U 1 REMARK REVDAT 3 12-JUL-17 1E3U 1 REVDAT 2 24-FEB-09 1E3U 1 VERSN REVDAT 1 12-JAN-01 1E3U 0 JRNL AUTH L.MAVEYRAUD,D.GOLEMI,L.P.KOTRA,S.TRANIER,S.VAKULENKO, JRNL AUTH 2 S.MOBASHERY,J.P.SAMAMA JRNL TITL INSIGHTS INTO CLASS D BETA-LACTAMASES ARE REVEALED BY THE JRNL TITL 2 CRYSTAL STRUCTURE OF THE OXA10 ENZYME FROM PSEUDOMONAS JRNL TITL 3 AERUGINOSA JRNL REF STRUCTURE V. 8 1289 2000 JRNL REFN ISSN 0969-2126 JRNL PMID 11188693 JRNL DOI 10.1016/S0969-2126(00)00534-7 REMARK 2 REMARK 2 RESOLUTION. 1.66 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.66 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 121338 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) : NULL REMARK 3 R VALUE (WORKING SET) : 0.181 REMARK 3 FREE R VALUE : 0.210 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 6428 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 7643 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 163 REMARK 3 SOLVENT ATOMS : 949 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 19.32 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.74 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.140 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.095 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.035 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.021 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : 0.004 ; 0.020 REMARK 3 ANGLE DISTANCE (A) : 0.016 ; 0.040 REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.017 ; 0.050 REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : 0.007 ; 0.030 REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.067 ; 0.150 REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : 0.171 ; 0.300 REMARK 3 MULTIPLE TORSION (A) : 0.223 ; 0.300 REMARK 3 H-BOND (X...Y) (A) : 0.125 ; 0.300 REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : 5.600 ; 7.000 REMARK 3 STAGGERED (DEGREES) : 11.700; 15.000 REMARK 3 TRANSVERSE (DEGREES) : 31.900; 20.000 REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 0.796 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.128 ; 5.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 2.349 ; 10.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; 15.000 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: INDIVIDUAL ANISOTROPIC B FACTORS WERE REMARK 3 REFINED REMARK 4 REMARK 4 1E3U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-JUN-00. REMARK 100 THE DEPOSITION ID IS D_1290005045. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-APR-00 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 8.20 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG REMARK 200 BEAMLINE : X31 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.95375, 1.0376 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : COLLIMATOR REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 127968 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.653 REMARK 200 RESOLUTION RANGE LOW (A) : 43.100 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9 REMARK 200 DATA REDUNDANCY : 4.700 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.06400 REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.75 REMARK 200 COMPLETENESS FOR SHELL (%) : 93.4 REMARK 200 DATA REDUNDANCY IN SHELL : 3.40 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.32200 REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: MAD REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD REMARK 200 SOFTWARE USED: SHARP, SOLVE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 0.56 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUMS SULFATE 2.0 M, TRIS HCL 100 REMARK 280 MM, PH 8.2-8.5, PH 8.20 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 41.47000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PQS REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PQS REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 SER A 21 REMARK 465 GLY A 265 REMARK 465 GLY A 266 REMARK 465 SER B 21 REMARK 465 GLY B 265 REMARK 465 GLY B 266 REMARK 465 SER C 21 REMARK 465 GLY C 94 REMARK 465 LYS C 95 REMARK 465 PRO C 96 REMARK 465 SER D 21 REMARK 465 GLY D 94 REMARK 465 LYS D 95 REMARK 465 PRO D 96 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLU A 214 CG CD OE1 OE2 REMARK 470 LYS C 100 CG CD CE NZ REMARK 470 GLN C 101 CG CD OE1 NE2 REMARK 470 GLU C 129 CG CD OE1 OE2 REMARK 470 GLU C 214 CG CD OE1 OE2 REMARK 470 LYS D 84 CG CD CE NZ REMARK 470 PRO D 93 CG CD REMARK 470 LYS D 100 CG CD CE NZ REMARK 470 GLN D 101 CG CD OE1 NE2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ARG C 250 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES REMARK 500 ARG C 250 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES REMARK 500 ARG D 109 NE - CZ - NH2 ANGL. DEV. = -4.4 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 SER A 46 -46.79 78.61 REMARK 500 SER A 50 74.24 -116.66 REMARK 500 ALA A 66 -139.56 45.42 REMARK 500 ASN A 85 -169.75 -163.37 REMARK 500 LYS A 152 8.69 -153.24 REMARK 500 GLU A 229 -119.52 52.74 REMARK 500 SER B 46 -50.80 78.92 REMARK 500 ALA B 66 -134.30 48.61 REMARK 500 ASN B 85 -168.55 -160.81 REMARK 500 LYS B 152 6.29 -151.13 REMARK 500 GLU B 229 -121.10 53.05 REMARK 500 SER C 46 -52.04 78.58 REMARK 500 ALA C 66 -134.42 47.61 REMARK 500 ASN C 85 -168.23 -166.80 REMARK 500 ALA C 116 51.71 -149.72 REMARK 500 LYS C 152 8.24 -156.77 REMARK 500 GLU C 229 -118.90 54.65 REMARK 500 SER D 46 -52.65 82.00 REMARK 500 ALA D 66 -132.95 48.58 REMARK 500 ASN D 85 -167.60 -163.05 REMARK 500 ALA D 116 56.55 -146.91 REMARK 500 LYS D 152 11.97 -155.11 REMARK 500 GLU D 229 -122.90 50.59 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH C 630 DISTANCE = 5.97 ANGSTROMS REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 AUC A 301 AU REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH A 401 O REMARK 620 2 AUC A 301 C1 108.2 REMARK 620 3 AUC A 301 C2 86.7 165.1 REMARK 620 N 1 2 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC E 1 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC E 2 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC E 3 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC E 4 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC E 5 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC E 6 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC E 7 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AUC E 8 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 9 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 10 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 11 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 12 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 13 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 14 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 15 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 16 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 17 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 18 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 19 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 20 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 21 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 22 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 23 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 24 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 25 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 26 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 27 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 28 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 29 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 30 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 31 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 32 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 33 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 34 REMARK 800 REMARK 800 SITE_IDENTIFIER: DC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 35 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1E4D RELATED DB: PDB REMARK 900 STRUCTURE OF OXA10 BETA-LACTAMASE AT PH 8.3 DBREF 1E3U A 21 266 UNP P14489 BLP2_PSEAE 21 266 DBREF 1E3U B 21 266 UNP P14489 BLP2_PSEAE 21 266 DBREF 1E3U C 21 266 UNP P14489 BLP2_PSEAE 21 266 DBREF 1E3U D 21 266 UNP P14489 BLP2_PSEAE 21 266 SEQADV 1E3U PRO D 93 UNP P14489 ASP 93 CONFLICT SEQRES 1 A 246 SER ILE THR GLU ASN THR SER TRP ASN LYS GLU PHE SER SEQRES 2 A 246 ALA GLU ALA VAL ASN GLY VAL PHE VAL LEU CYS LYS SER SEQRES 3 A 246 SER SER LYS SER CYS ALA THR ASN ASP LEU ALA ARG ALA SEQRES 4 A 246 SER LYS GLU TYR LEU PRO ALA SER THR PHE LYS ILE PRO SEQRES 5 A 246 ASN ALA ILE ILE GLY LEU GLU THR GLY VAL ILE LYS ASN SEQRES 6 A 246 GLU HIS GLN VAL PHE LYS TRP ASP GLY LYS PRO ARG ALA SEQRES 7 A 246 MET LYS GLN TRP GLU ARG ASP LEU THR LEU ARG GLY ALA SEQRES 8 A 246 ILE GLN VAL SER ALA VAL PRO VAL PHE GLN GLN ILE ALA SEQRES 9 A 246 ARG GLU VAL GLY GLU VAL ARG MET GLN LYS TYR LEU LYS SEQRES 10 A 246 LYS PHE SER TYR GLY ASN GLN ASN ILE SER GLY GLY ILE SEQRES 11 A 246 ASP LYS PHE TRP LEU GLU GLY GLN LEU ARG ILE SER ALA SEQRES 12 A 246 VAL ASN GLN VAL GLU PHE LEU GLU SER LEU TYR LEU ASN SEQRES 13 A 246 LYS LEU SER ALA SER LYS GLU ASN GLN LEU ILE VAL LYS SEQRES 14 A 246 GLU ALA LEU VAL THR GLU ALA ALA PRO GLU TYR LEU VAL SEQRES 15 A 246 HIS SER LYS THR GLY PHE SER GLY VAL GLY THR GLU SER SEQRES 16 A 246 ASN PRO GLY VAL ALA TRP TRP VAL GLY TRP VAL GLU LYS SEQRES 17 A 246 GLU THR GLU VAL TYR PHE PHE ALA PHE ASN MET ASP ILE SEQRES 18 A 246 ASP ASN GLU SER LYS LEU PRO LEU ARG LYS SER ILE PRO SEQRES 19 A 246 THR LYS ILE MET GLU SER GLU GLY ILE ILE GLY GLY SEQRES 1 B 246 SER ILE THR GLU ASN THR SER TRP ASN LYS GLU PHE SER SEQRES 2 B 246 ALA GLU ALA VAL ASN GLY VAL PHE VAL LEU CYS LYS SER SEQRES 3 B 246 SER SER LYS SER CYS ALA THR ASN ASP LEU ALA ARG ALA SEQRES 4 B 246 SER LYS GLU TYR LEU PRO ALA SER THR PHE LYS ILE PRO SEQRES 5 B 246 ASN ALA ILE ILE GLY LEU GLU THR GLY VAL ILE LYS ASN SEQRES 6 B 246 GLU HIS GLN VAL PHE LYS TRP ASP GLY LYS PRO ARG ALA SEQRES 7 B 246 MET LYS GLN TRP GLU ARG ASP LEU THR LEU ARG GLY ALA SEQRES 8 B 246 ILE GLN VAL SER ALA VAL PRO VAL PHE GLN GLN ILE ALA SEQRES 9 B 246 ARG GLU VAL GLY GLU VAL ARG MET GLN LYS TYR LEU LYS SEQRES 10 B 246 LYS PHE SER TYR GLY ASN GLN ASN ILE SER GLY GLY ILE SEQRES 11 B 246 ASP LYS PHE TRP LEU GLU GLY GLN LEU ARG ILE SER ALA SEQRES 12 B 246 VAL ASN GLN VAL GLU PHE LEU GLU SER LEU TYR LEU ASN SEQRES 13 B 246 LYS LEU SER ALA SER LYS GLU ASN GLN LEU ILE VAL LYS SEQRES 14 B 246 GLU ALA LEU VAL THR GLU ALA ALA PRO GLU TYR LEU VAL SEQRES 15 B 246 HIS SER LYS THR GLY PHE SER GLY VAL GLY THR GLU SER SEQRES 16 B 246 ASN PRO GLY VAL ALA TRP TRP VAL GLY TRP VAL GLU LYS SEQRES 17 B 246 GLU THR GLU VAL TYR PHE PHE ALA PHE ASN MET ASP ILE SEQRES 18 B 246 ASP ASN GLU SER LYS LEU PRO LEU ARG LYS SER ILE PRO SEQRES 19 B 246 THR LYS ILE MET GLU SER GLU GLY ILE ILE GLY GLY SEQRES 1 C 246 SER ILE THR GLU ASN THR SER TRP ASN LYS GLU PHE SER SEQRES 2 C 246 ALA GLU ALA VAL ASN GLY VAL PHE VAL LEU CYS LYS SER SEQRES 3 C 246 SER SER LYS SER CYS ALA THR ASN ASP LEU ALA ARG ALA SEQRES 4 C 246 SER LYS GLU TYR LEU PRO ALA SER THR PHE LYS ILE PRO SEQRES 5 C 246 ASN ALA ILE ILE GLY LEU GLU THR GLY VAL ILE LYS ASN SEQRES 6 C 246 GLU HIS GLN VAL PHE LYS TRP ASP GLY LYS PRO ARG ALA SEQRES 7 C 246 MET LYS GLN TRP GLU ARG ASP LEU THR LEU ARG GLY ALA SEQRES 8 C 246 ILE GLN VAL SER ALA VAL PRO VAL PHE GLN GLN ILE ALA SEQRES 9 C 246 ARG GLU VAL GLY GLU VAL ARG MET GLN LYS TYR LEU LYS SEQRES 10 C 246 LYS PHE SER TYR GLY ASN GLN ASN ILE SER GLY GLY ILE SEQRES 11 C 246 ASP LYS PHE TRP LEU GLU GLY GLN LEU ARG ILE SER ALA SEQRES 12 C 246 VAL ASN GLN VAL GLU PHE LEU GLU SER LEU TYR LEU ASN SEQRES 13 C 246 LYS LEU SER ALA SER LYS GLU ASN GLN LEU ILE VAL LYS SEQRES 14 C 246 GLU ALA LEU VAL THR GLU ALA ALA PRO GLU TYR LEU VAL SEQRES 15 C 246 HIS SER LYS THR GLY PHE SER GLY VAL GLY THR GLU SER SEQRES 16 C 246 ASN PRO GLY VAL ALA TRP TRP VAL GLY TRP VAL GLU LYS SEQRES 17 C 246 GLU THR GLU VAL TYR PHE PHE ALA PHE ASN MET ASP ILE SEQRES 18 C 246 ASP ASN GLU SER LYS LEU PRO LEU ARG LYS SER ILE PRO SEQRES 19 C 246 THR LYS ILE MET GLU SER GLU GLY ILE ILE GLY GLY SEQRES 1 D 246 SER ILE THR GLU ASN THR SER TRP ASN LYS GLU PHE SER SEQRES 2 D 246 ALA GLU ALA VAL ASN GLY VAL PHE VAL LEU CYS LYS SER SEQRES 3 D 246 SER SER LYS SER CYS ALA THR ASN ASP LEU ALA ARG ALA SEQRES 4 D 246 SER LYS GLU TYR LEU PRO ALA SER THR PHE LYS ILE PRO SEQRES 5 D 246 ASN ALA ILE ILE GLY LEU GLU THR GLY VAL ILE LYS ASN SEQRES 6 D 246 GLU HIS GLN VAL PHE LYS TRP PRO GLY LYS PRO ARG ALA SEQRES 7 D 246 MET LYS GLN TRP GLU ARG ASP LEU THR LEU ARG GLY ALA SEQRES 8 D 246 ILE GLN VAL SER ALA VAL PRO VAL PHE GLN GLN ILE ALA SEQRES 9 D 246 ARG GLU VAL GLY GLU VAL ARG MET GLN LYS TYR LEU LYS SEQRES 10 D 246 LYS PHE SER TYR GLY ASN GLN ASN ILE SER GLY GLY ILE SEQRES 11 D 246 ASP LYS PHE TRP LEU GLU GLY GLN LEU ARG ILE SER ALA SEQRES 12 D 246 VAL ASN GLN VAL GLU PHE LEU GLU SER LEU TYR LEU ASN SEQRES 13 D 246 LYS LEU SER ALA SER LYS GLU ASN GLN LEU ILE VAL LYS SEQRES 14 D 246 GLU ALA LEU VAL THR GLU ALA ALA PRO GLU TYR LEU VAL SEQRES 15 D 246 HIS SER LYS THR GLY PHE SER GLY VAL GLY THR GLU SER SEQRES 16 D 246 ASN PRO GLY VAL ALA TRP TRP VAL GLY TRP VAL GLU LYS SEQRES 17 D 246 GLU THR GLU VAL TYR PHE PHE ALA PHE ASN MET ASP ILE SEQRES 18 D 246 ASP ASN GLU SER LYS LEU PRO LEU ARG LYS SER ILE PRO SEQRES 19 D 246 THR LYS ILE MET GLU SER GLU GLY ILE ILE GLY GLY HET AUC A 301 5 HET SO4 A 302 5 HET SO4 A 303 5 HET SO4 A 304 5 HET SO4 A 305 5 HET SO4 A 306 5 HET SO4 A 307 5 HET EDO A 308 4 HET EDO A 309 4 HET AUC B 301 5 HET SO4 B 302 5 HET SO4 B 303 5 HET SO4 B 304 5 HET SO4 B 305 5 HET EDO B 306 4 HET EDO B 307 4 HET EDO B 308 4 HET EDO B 309 4 HET EDO B 310 4 HET EDO B 311 4 HET AUC C 301 5 HET AUC C 302 5 HET AUC C 303 5 HET SO4 C 304 5 HET SO4 C 305 5 HET EDO C 306 4 HET EDO C 307 4 HET EDO C 308 4 HET AUC D 301 5 HET AUC D 302 5 HET AUC D 303 5 HET SO4 D 304 5 HET SO4 D 305 5 HET SO4 D 306 5 HET EDO D 307 4 HETNAM AUC GOLD (I) CYANIDE ION HETNAM SO4 SULFATE ION HETNAM EDO 1,2-ETHANEDIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 5 AUC 8(C2 AU N2) FORMUL 6 SO4 15(O4 S 2-) FORMUL 12 EDO 12(C2 H6 O2) FORMUL 40 HOH *949(H2 O) HELIX 1 1 TRP A 28 GLU A 35 1 8 HELIX 2 2 ASP A 55 SER A 60 1 6 HELIX 3 3 PRO A 65 THR A 68 5 4 HELIX 4 4 PHE A 69 THR A 80 1 12 HELIX 5 5 MET A 99 GLU A 103 5 5 HELIX 6 6 LEU A 108 VAL A 114 1 7 HELIX 7 7 ALA A 116 GLY A 128 1 13 HELIX 8 8 GLY A 128 PHE A 139 1 12 HELIX 9 9 ALA A 163 LEU A 175 1 13 HELIX 10 10 SER A 181 LEU A 192 1 12 HELIX 11 11 ASN A 243 LEU A 247 5 5 HELIX 12 12 PRO A 248 GLU A 261 1 14 HELIX 13 13 THR B 26 SER B 33 5 8 HELIX 14 14 ASP B 55 SER B 60 1 6 HELIX 15 15 PRO B 65 THR B 68 5 4 HELIX 16 16 PHE B 69 THR B 80 1 12 HELIX 17 17 MET B 99 GLU B 103 5 5 HELIX 18 18 LEU B 108 VAL B 114 1 7 HELIX 19 19 ALA B 116 GLY B 128 1 13 HELIX 20 20 GLY B 128 PHE B 139 1 12 HELIX 21 21 SER B 162 LEU B 175 1 14 HELIX 22 22 SER B 181 LEU B 192 1 12 HELIX 23 23 ASN B 243 LEU B 247 5 5 HELIX 24 24 PRO B 248 GLU B 261 1 14 HELIX 25 25 TRP C 28 ALA C 34 1 7 HELIX 26 26 ASP C 55 LYS C 61 1 7 HELIX 27 27 PRO C 65 THR C 68 5 4 HELIX 28 28 PHE C 69 THR C 80 1 12 HELIX 29 29 MET C 99 ARG C 104 5 6 HELIX 30 30 LEU C 108 VAL C 114 1 7 HELIX 31 31 ALA C 116 GLY C 128 1 13 HELIX 32 32 GLY C 128 PHE C 139 1 12 HELIX 33 33 ALA C 163 ASN C 176 1 14 HELIX 34 34 SER C 181 LEU C 192 1 12 HELIX 35 35 ASN C 243 LEU C 247 5 5 HELIX 36 36 PRO C 248 GLU C 261 1 14 HELIX 37 37 THR D 26 TRP D 28 5 3 HELIX 38 38 ASN D 29 GLU D 35 1 7 HELIX 39 39 ASP D 55 SER D 60 1 6 HELIX 40 40 PRO D 65 THR D 68 5 4 HELIX 41 41 PHE D 69 GLY D 81 1 13 HELIX 42 42 MET D 99 ARG D 104 5 6 HELIX 43 43 LEU D 108 VAL D 114 1 7 HELIX 44 44 ALA D 116 GLY D 128 1 13 HELIX 45 45 GLY D 128 PHE D 139 1 12 HELIX 46 46 ALA D 163 LEU D 175 1 13 HELIX 47 47 SER D 181 LEU D 192 1 12 HELIX 48 48 ASN D 243 LEU D 247 5 5 HELIX 49 49 PRO D 248 GLU D 261 1 14 SHEET 1 A 6 CYS A 51 THR A 53 0 SHEET 2 A 6 GLY A 39 LYS A 45 -1 N LEU A 43 O ALA A 52 SHEET 3 A 6 GLU A 231 ILE A 241 -1 N ASN A 238 O VAL A 40 SHEET 4 A 6 GLY A 218 LYS A 228 -1 N LYS A 228 O GLU A 231 SHEET 5 A 6 TYR A 200 PHE A 208 -1 N GLY A 207 O TRP A 221 SHEET 6 A 6 VAL A 193 ALA A 197 -1 N ALA A 197 O TYR A 200 SHEET 1 B 6 CYS B 51 THR B 53 0 SHEET 2 B 6 GLY B 39 LYS B 45 -1 N LEU B 43 O ALA B 52 SHEET 3 B 6 GLU B 231 ILE B 241 -1 N ASN B 238 O VAL B 40 SHEET 4 B 6 GLY B 218 LYS B 228 -1 N LYS B 228 O GLU B 231 SHEET 5 B 6 TYR B 200 PHE B 208 -1 N GLY B 207 O TRP B 221 SHEET 6 B 6 VAL B 193 ALA B 197 -1 N ALA B 197 O TYR B 200 SHEET 1 C 6 CYS C 51 THR C 53 0 SHEET 2 C 6 GLY C 39 LYS C 45 -1 N LEU C 43 O ALA C 52 SHEET 3 C 6 GLU C 231 ILE C 241 -1 N ASN C 238 O VAL C 40 SHEET 4 C 6 GLY C 218 LYS C 228 -1 N LYS C 228 O GLU C 231 SHEET 5 C 6 TYR C 200 PHE C 208 -1 N GLY C 207 O TRP C 221 SHEET 6 C 6 VAL C 193 ALA C 197 -1 N ALA C 197 O TYR C 200 SHEET 1 D 6 CYS D 51 THR D 53 0 SHEET 2 D 6 GLY D 39 LYS D 45 -1 N LEU D 43 O ALA D 52 SHEET 3 D 6 GLU D 231 ILE D 241 -1 N ASN D 238 O VAL D 40 SHEET 4 D 6 GLY D 218 LYS D 228 -1 N LYS D 228 O GLU D 231 SHEET 5 D 6 TYR D 200 PHE D 208 -1 N GLY D 207 O TRP D 221 SHEET 6 D 6 VAL D 193 ALA D 197 -1 N ALA D 197 O TYR D 200 SSBOND 1 CYS A 44 CYS A 51 1555 1555 2.03 SSBOND 2 CYS B 44 CYS B 51 1555 1555 2.03 SSBOND 3 CYS C 44 CYS C 51 1555 1555 2.03 SSBOND 4 CYS D 44 CYS D 51 1555 1555 2.03 LINK AU AUC A 301 O HOH A 401 1555 1555 2.26 SITE 1 AC1 9 ALA A 66 SER A 67 PHE A 69 LYS A 70 SITE 2 AC1 9 ASN A 73 PHE A 120 TRP A 154 HOH A 401 SITE 3 AC1 9 HOH A 558 SITE 1 AC2 8 ALA B 66 SER B 67 PHE B 69 LYS B 70 SITE 2 AC2 8 ASN B 73 PHE B 120 TRP B 154 HOH B 569 SITE 1 AC3 6 LYS C 70 ALA C 116 VAL C 117 TRP C 154 SITE 2 AC3 6 HOH C 434 AUC C 302 SITE 1 AC4 9 LYS B 95 HOH B 515 ALA C 66 SER C 67 SITE 2 AC4 9 LYS C 70 ASN C 73 PHE C 120 TRP C 154 SITE 3 AC4 9 AUC C 301 SITE 1 AC5 3 GLN C 133 HOH C 410 EDO C 308 SITE 1 AC6 8 ALA D 66 SER D 67 LYS D 70 ASN D 73 SITE 2 AC6 8 PHE D 120 TRP D 154 AUC D 302 HOH D 542 SITE 1 AC7 6 LYS D 70 ALA D 116 VAL D 117 TRP D 154 SITE 2 AC7 6 HOH D 454 AUC D 301 SITE 1 AC8 3 GLN D 133 HOH D 452 HOH D 539 SITE 1 AC9 9 SER A 115 THR A 206 GLY A 207 PHE A 208 SITE 2 AC9 9 ARG A 250 HOH A 500 HOH A 469 HOH A 411 SITE 3 AC9 9 HOH A 498 SITE 1 BC1 3 ARG A 131 LYS A 134 TYR A 135 SITE 1 BC2 2 ARG A 160 HOH A 542 SITE 1 BC3 6 ILE A 22 SER C 33 ALA C 36 VAL C 37 SITE 2 BC3 6 ASN C 38 EDO C 307 SITE 1 BC4 9 SER B 115 LYS B 205 THR B 206 GLY B 207 SITE 2 BC4 9 PHE B 208 ARG B 250 HOH B 464 HOH B 577 SITE 3 BC4 9 HOH B 450 SITE 1 BC5 3 MET B 99 LYS B 100 GLN B 101 SITE 1 BC6 6 GLU B 35 SER B 245 LYS B 246 HOH B 432 SITE 2 BC6 6 HOH B 401 HOH B 433 SITE 1 BC7 8 PRO B 198 GLU B 199 LEU B 201 GLU B 227 SITE 2 BC7 8 GLU B 229 THR D 107 ARG D 109 HOH B 560 SITE 1 BC8 7 LYS B 95 SER C 67 THR C 206 GLY C 207 SITE 2 BC8 7 PHE C 208 ARG C 250 HOH C 505 SITE 1 BC9 6 HOH A 425 HOH A 436 SER C 181 LYS C 182 SITE 2 BC9 6 HOH C 517 HOH C 514 SITE 1 CC1 6 LYS A 95 SER D 67 THR D 206 GLY D 207 SITE 2 CC1 6 PHE D 208 ARG D 250 SITE 1 CC2 8 GLU B 183 HOH B 516 HOH B 466 SER D 181 SITE 2 CC2 8 LYS D 182 HOH D 464 HOH D 561 HOH D 506 SITE 1 CC3 5 THR D 213 SER D 215 ASN D 216 HOH D 523 SITE 2 CC3 5 HOH D 501 SITE 1 CC4 6 GLY A 128 GLU A 129 VAL A 130 HOH A 518 SITE 2 CC4 6 HOH A 402 HOH A 526 SITE 1 CC5 10 THR A 107 ARG A 109 PRO C 198 GLU C 199 SITE 2 CC5 10 LEU C 201 GLU C 227 GLU C 229 HOH C 452 SITE 3 CC5 10 HOH A 553 HOH A 508 SITE 1 CC6 3 GLU C 195 TYR C 200 HOH C 612 SITE 1 CC7 9 ASN C 29 PHE C 32 VAL C 37 ASN C 38 SITE 2 CC7 9 GLY C 39 ASN C 54 HOH C 408 SO4 A 305 SITE 3 CC7 9 HOH C 441 SITE 1 CC8 6 ASN B 29 VAL B 37 ASN B 38 GLY B 39 SITE 2 CC8 6 ASN B 54 HOH B 565 SITE 1 CC9 1 GLU B 261 SITE 1 DC1 6 THR B 107 ARG B 109 PRO D 198 GLU D 199 SITE 2 DC1 6 GLU D 229 HOH D 433 SITE 1 DC2 5 THR B 80 ARG B 131 LYS B 134 TYR B 135 SITE 2 DC2 5 HOH B 493 SITE 1 DC3 7 GLU A 199 GLU A 227 GLU A 229 THR C 107 SITE 2 DC3 7 HOH C 438 HOH A 447 HOH A 520 SITE 1 DC4 6 ILE C 146 SER C 147 GLY C 148 GLY C 149 SITE 2 DC4 6 ILE C 150 AUC C 303 SITE 1 DC5 7 ALA A 36 PRO A 217 ASP A 240 ASP A 242 SITE 2 DC5 7 HOH A 409 HOH A 413 HOH A 434 SITE 1 DC6 7 GLU B 195 TYR B 200 VAL B 202 MET B 258 SITE 2 DC6 7 GLU B 259 ILE B 263 HOH B 416 SITE 1 DC7 5 PRO B 217 ASP B 240 HOH B 453 HOH B 403 SITE 2 DC7 5 HOH B 402 SITE 1 DC8 2 ASN B 143 ASN B 145 CRYST1 65.530 82.940 101.420 90.00 95.03 90.00 P 1 21 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 0.015260 0.000000 0.001343 0.00000 SCALE2 0.000000 0.012057 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009898 0.00000 MTRIX1 1 -0.983730 0.026540 -0.177670 4.27241 1 MTRIX2 1 -0.023020 -0.999500 -0.021850 28.01285 1 MTRIX3 1 -0.178160 -0.017400 0.983850 -50.32816 1 MTRIX1 2 -0.807930 0.560340 -0.182400 7.38369 1 MTRIX2 2 0.553220 0.614620 -0.562310 30.41618 1 MTRIX3 2 -0.202980 -0.555210 -0.806560 94.75005 1 MTRIX1 3 0.848920 -0.433700 0.302060 -18.97638 1 MTRIX2 3 -0.524780 -0.623800 0.579200 -4.12586 1 MTRIX3 3 -0.062780 -0.650210 -0.757160 41.37533 1 ATOM 1 N ILE A 22 32.287 12.822 57.725 1.00 33.43 N ANISOU 1 N ILE A 22 4250 4178 4273 -11 -14 -11 N ATOM 2 CA ILE A 22 31.682 11.497 57.397 1.00 32.86 C ANISOU 2 CA ILE A 22 4175 4130 4179 12 -7 22 C ATOM 3 C ILE A 22 32.233 10.408 58.306 1.00 32.16 C ANISOU 3 C ILE A 22 4073 4065 4080 -18 11 -5 C ATOM 4 O ILE A 22 33.441 10.302 58.522 1.00 32.20 O ANISOU 4 O ILE A 22 4083 4071 4079 -9 -11 -1 O ATOM 5 CB ILE A 22 31.856 11.148 55.911 1.00 32.94 C ANISOU 5 CB ILE A 22 4198 4136 4181 -19 -17 1 C ATOM 6 CG1 ILE A 22 31.052 9.892 55.552 1.00 32.33 C ANISOU 6 CG1 ILE A 22 4120 4084 4079 19 2 2 C ATOM 7 CG2 ILE A 22 33.321 10.962 55.543 1.00 33.49 C ANISOU 7 CG2 ILE A 22 4243 4221 4261 0 0 7 C ATOM 8 CD1 ILE A 22 30.873 9.680 54.064 1.00 31.76 C ANISOU 8 CD1 ILE A 22 4020 3998 4049 11 -7 7 C ATOM 9 N THR A 23 31.340 9.618 58.895 1.00 31.45 N ANISOU 9 N THR A 23 4005 3953 3991 13 -43 -4 N ATOM 10 CA THR A 23 31.735 8.527 59.774 1.00 30.91 C ANISOU 10 CA THR A 23 3916 3860 3967 -14 -29 -27 C ATOM 11 C THR A 23 31.348 7.179 59.172 1.00 29.96 C ANISOU 11 C THR A 23 3781 3788 3816 20 -26 13 C ATOM 12 O THR A 23 30.352 7.079 58.456 1.00 29.39 O ANISOU 12 O THR A 23 3750 3682 3736 2 -5 1 O ATOM 13 CB THR A 23 31.121 8.637 61.182 1.00 32.64 C ANISOU 13 CB THR A 23 4174 4155 4072 24 38 12 C ATOM 14 OG1 THR A 23 29.692 8.703 61.093 1.00 33.26 O ANISOU 14 OG1 THR A 23 4210 4222 4205 6 1 -9 O ATOM 15 CG2 THR A 23 31.630 9.866 61.915 1.00 33.47 C ANISOU 15 CG2 THR A 23 4267 4200 4251 -15 4 -20 C ATOM 16 N GLU A 24 32.146 6.153 59.454 1.00 29.47 N ANISOU 16 N GLU A 24 3734 3735 3729 -6 -22 -11 N ATOM 17 CA GLU A 24 31.791 4.799 59.045 1.00 29.28 C ANISOU 17 CA GLU A 24 3719 3710 3695 6 -11 5 C ATOM 18 C GLU A 24 30.942 4.135 60.126 1.00 29.48 C ANISOU 18 C GLU A 24 3744 3743 3715 -5 -4 10 C ATOM 19 O GLU A 24 31.307 4.122 61.301 1.00 29.40 O ANISOU 19 O GLU A 24 3723 3732 3715 -25 -14 9 O ATOM 20 CB GLU A 24 33.026 3.956 58.735 1.00 29.37 C ANISOU 20 CB GLU A 24 3703 3750 3705 9 1 24 C ATOM 21 CG GLU A 24 32.716 2.645 58.029 1.00 30.54 C ANISOU 21 CG GLU A 24 3899 3805 3902 -27 -27 -6 C ATOM 22 CD GLU A 24 33.923 2.011 57.368 1.00 31.65 C ANISOU 22 CD GLU A 24 4017 4006 4004 17 28 -5 C ATOM 23 OE1 GLU A 24 34.688 1.307 58.061 1.00 32.01 O ANISOU 23 OE1 GLU A 24 4022 4041 4101 25 -7 17 O ATOM 24 OE2 GLU A 24 34.110 2.210 56.148 1.00 30.91 O ANISOU 24 OE2 GLU A 24 3889 3899 3957 18 -17 12 O ATOM 25 N ASN A 25 29.783 3.629 59.720 1.00 29.66 N ANISOU 25 N ASN A 25 3771 3762 3736 -6 -26 -2 N ATOM 26 CA ASN A 25 28.959 2.809 60.605 1.00 30.35 C ANISOU 26 CA ASN A 25 3896 3833 3801 -35 3 20 C ATOM 27 C ASN A 25 29.084 1.354 60.166 1.00 30.67 C ANISOU 27 C ASN A 25 3921 3861 3870 -30 3 -6 C ATOM 28 O ASN A 25 28.497 0.917 59.181 1.00 30.46 O ANISOU 28 O ASN A 25 3879 3846 3848 -16 10 3 O ATOM 29 CB ASN A 25 27.507 3.267 60.604 1.00 32.61 C ANISOU 29 CB ASN A 25 4022 4137 4230 42 -34 -27 C ATOM 30 CG ASN A 25 26.657 2.683 61.710 1.00 34.50 C ANISOU 30 CG ASN A 25 4387 4402 4321 -44 12 39 C ATOM 31 OD1 ASN A 25 25.774 3.359 62.245 1.00 35.69 O ANISOU 31 OD1 ASN A 25 4516 4529 4514 27 16 -20 O ATOM 32 ND2 ASN A 25 26.887 1.430 62.078 1.00 35.15 N ANISOU 32 ND2 ASN A 25 4478 4431 4446 -8 -17 20 N ATOM 33 N THR A 26 29.840 0.587 60.943 1.00 31.37 N ANISOU 33 N THR A 26 3974 3951 3995 -6 -19 26 N ATOM 34 CA THR A 26 30.170 -0.791 60.613 1.00 32.21 C ANISOU 34 CA THR A 26 4114 4004 4121 -25 41 -23 C ATOM 35 C THR A 26 28.969 -1.721 60.640 1.00 31.81 C ANISOU 35 C THR A 26 4047 3996 4045 1 2 0 C ATOM 36 O THR A 26 28.886 -2.668 59.851 1.00 31.66 O ANISOU 36 O THR A 26 4021 3975 4035 -6 -11 22 O ATOM 37 CB THR A 26 31.264 -1.316 61.569 1.00 34.99 C ANISOU 37 CB THR A 26 4362 4485 4449 36 -96 66 C ATOM 38 OG1 THR A 26 31.604 -2.661 61.217 1.00 36.74 O ANISOU 38 OG1 THR A 26 4670 4606 4682 20 10 -21 O ATOM 39 CG2 THR A 26 30.788 -1.276 63.013 1.00 36.08 C ANISOU 39 CG2 THR A 26 4594 4562 4554 10 4 4 C ATOM 40 N SER A 27 27.989 -1.453 61.495 1.00 31.68 N ANISOU 40 N SER A 27 4016 3994 4025 -1 -23 18 N ATOM 41 CA SER A 27 26.826 -2.305 61.672 1.00 31.73 C ANISOU 41 CA SER A 27 4030 3979 4045 -11 -65 34 C ATOM 42 C SER A 27 25.893 -2.308 60.470 1.00 31.00 C ANISOU 42 C SER A 27 3942 3865 3969 -7 -11 38 C ATOM 43 O SER A 27 25.177 -3.289 60.249 1.00 30.85 O ANISOU 43 O SER A 27 3917 3862 3943 1 -18 29 O ATOM 44 CB SER A 27 26.045 -1.901 62.925 1.00 34.23 C ANISOU 44 CB SER A 27 4357 4409 4239 -10 66 -26 C ATOM 45 OG SER A 27 25.393 -0.657 62.759 1.00 36.19 O ANISOU 45 OG SER A 27 4619 4541 4593 28 -10 18 O ATOM 46 N TRP A 28 25.930 -1.267 59.643 1.00 30.24 N ANISOU 46 N TRP A 28 3835 3799 3855 -3 -27 4 N ATOM 47 CA TRP A 28 25.101 -1.191 58.452 1.00 29.53 C ANISOU 47 CA TRP A 28 3795 3623 3800 -15 -6 74 C ATOM 48 C TRP A 28 25.468 -2.191 57.367 1.00 30.27 C ANISOU 48 C TRP A 28 3892 3766 3845 -15 6 12 C ATOM 49 O TRP A 28 24.635 -2.457 56.493 1.00 30.38 O ANISOU 49 O TRP A 28 3860 3812 3869 10 -2 15 O ATOM 50 CB TRP A 28 25.112 0.220 57.867 1.00 25.53 C ANISOU 50 CB TRP A 28 3167 3333 3200 61 22 -151 C ATOM 51 CG TRP A 28 24.438 1.273 58.688 1.00 22.46 C ANISOU 51 CG TRP A 28 2866 2848 2819 -71 -40 102 C ATOM 52 CD1 TRP A 28 23.723 1.118 59.841 1.00 21.82 C ANISOU 52 CD1 TRP A 28 2732 2736 2822 7 -27 -2 C ATOM 53 CD2 TRP A 28 24.393 2.675 58.383 1.00 20.98 C ANISOU 53 CD2 TRP A 28 2614 2738 2621 -4 5 -14 C ATOM 54 NE1 TRP A 28 23.254 2.329 60.279 1.00 21.20 N ANISOU 54 NE1 TRP A 28 2706 2696 2652 -24 -19 20 N ATOM 55 CE2 TRP A 28 23.649 3.303 59.400 1.00 20.33 C ANISOU 55 CE2 TRP A 28 2569 2575 2581 -9 -50 -23 C ATOM 56 CE3 TRP A 28 24.914 3.460 57.346 1.00 21.03 C ANISOU 56 CE3 TRP A 28 2677 2640 2672 -15 -12 -7 C ATOM 57 CZ2 TRP A 28 23.416 4.676 59.415 1.00 20.12 C ANISOU 57 CZ2 TRP A 28 2538 2582 2525 17 -34 -1 C ATOM 58 CZ3 TRP A 28 24.679 4.820 57.366 1.00 20.57 C ANISOU 58 CZ3 TRP A 28 2579 2632 2606 20 -19 -2 C ATOM 59 CH2 TRP A 28 23.937 5.417 58.395 1.00 20.53 C ANISOU 59 CH2 TRP A 28 2568 2646 2588 -38 3 -3 C ATOM 60 N ASN A 29 26.653 -2.791 57.396 1.00 31.16 N ANISOU 60 N ASN A 29 3936 3923 3980 3 -15 40 N ATOM 61 CA ASN A 29 27.011 -3.860 56.480 1.00 32.45 C ANISOU 61 CA ASN A 29 4174 4055 4101 26 -3 -26 C ATOM 62 C ASN A 29 26.258 -5.157 56.734 1.00 33.03 C ANISOU 62 C ASN A 29 4208 4115 4227 -3 -32 -9 C ATOM 63 O ASN A 29 26.167 -5.991 55.827 1.00 32.67 O ANISOU 63 O ASN A 29 4130 4100 4182 5 -24 17 O ATOM 64 CB ASN A 29 28.521 -4.123 56.510 1.00 34.57 C ANISOU 64 CB ASN A 29 4278 4416 4443 47 -18 -18 C ATOM 65 CG ASN A 29 29.316 -3.008 55.862 1.00 36.16 C ANISOU 65 CG ASN A 29 4632 4525 4583 -9 46 37 C ATOM 66 OD1 ASN A 29 28.953 -2.488 54.807 1.00 35.77 O ANISOU 66 OD1 ASN A 29 4515 4496 4580 3 -12 11 O ATOM 67 ND2 ASN A 29 30.420 -2.636 56.498 1.00 37.39 N ANISOU 67 ND2 ASN A 29 4729 4740 4738 -11 -30 3 N ATOM 68 N LYS A 30 25.685 -5.360 57.914 1.00 34.31 N ANISOU 68 N LYS A 30 4373 4346 4318 22 0 7 N ATOM 69 CA LYS A 30 24.769 -6.460 58.174 1.00 35.95 C ANISOU 69 CA LYS A 30 4546 4457 4656 -47 -46 38 C ATOM 70 C LYS A 30 23.751 -6.643 57.054 1.00 36.19 C ANISOU 70 C LYS A 30 4581 4543 4626 -14 -26 10 C ATOM 71 O LYS A 30 23.586 -7.738 56.516 1.00 36.40 O ANISOU 71 O LYS A 30 4623 4560 4647 0 -23 1 O ATOM 72 CB LYS A 30 24.029 -6.267 59.501 1.00 39.78 C ANISOU 72 CB LYS A 30 5056 5046 5013 -13 193 -69 C ATOM 73 CG LYS A 30 24.812 -6.646 60.745 1.00 43.73 C ANISOU 73 CG LYS A 30 5580 5520 5515 35 -154 45 C ATOM 74 CD LYS A 30 23.911 -6.674 61.973 1.00 46.70 C ANISOU 74 CD LYS A 30 5923 5907 5914 -20 107 -23 C ATOM 75 CE LYS A 30 24.644 -7.197 63.198 1.00 48.65 C ANISOU 75 CE LYS A 30 6189 6140 6157 20 -58 32 C ATOM 76 NZ LYS A 30 23.742 -7.323 64.376 1.00 49.53 N ANISOU 76 NZ LYS A 30 6289 6261 6267 10 16 -1 N ATOM 77 N GLU A 31 23.075 -5.567 56.664 1.00 36.13 N ANISOU 77 N GLU A 31 4567 4574 4587 -8 -3 10 N ATOM 78 CA GLU A 31 22.130 -5.580 55.559 1.00 36.32 C ANISOU 78 CA GLU A 31 4588 4647 4566 -39 20 -6 C ATOM 79 C GLU A 31 22.749 -5.982 54.228 1.00 35.41 C ANISOU 79 C GLU A 31 4454 4485 4515 -34 5 22 C ATOM 80 O GLU A 31 22.083 -6.630 53.414 1.00 35.64 O ANISOU 80 O GLU A 31 4502 4503 4538 -38 -14 24 O ATOM 81 CB GLU A 31 21.468 -4.202 55.433 1.00 39.48 C ANISOU 81 CB GLU A 31 4992 4841 5166 54 -38 81 C ATOM 82 CG GLU A 31 21.059 -3.559 56.741 1.00 42.89 C ANISOU 82 CG GLU A 31 5522 5413 5363 70 -15 -74 C ATOM 83 CD GLU A 31 20.010 -4.311 57.529 1.00 45.35 C ANISOU 83 CD GLU A 31 5706 5707 5819 -34 34 53 C ATOM 84 OE1 GLU A 31 19.353 -5.215 56.969 1.00 45.43 O ANISOU 84 OE1 GLU A 31 5766 5719 5777 -1 1 10 O ATOM 85 OE2 GLU A 31 19.823 -4.006 58.729 1.00 47.01 O ANISOU 85 OE2 GLU A 31 5991 5954 5916 5 10 -8 O ATOM 86 N PHE A 32 23.998 -5.620 53.969 1.00 34.24 N ANISOU 86 N PHE A 32 4378 4303 4330 5 8 -4 N ATOM 87 CA PHE A 32 24.671 -5.935 52.720 1.00 32.90 C ANISOU 87 CA PHE A 32 4140 4110 4251 -62 -24 14 C ATOM 88 C PHE A 32 25.151 -7.378 52.645 1.00 32.85 C ANISOU 88 C PHE A 32 4154 4132 4194 -21 -8 5 C ATOM 89 O PHE A 32 25.085 -8.009 51.587 1.00 32.51 O ANISOU 89 O PHE A 32 4108 4071 4172 5 -3 16 O ATOM 90 CB PHE A 32 25.870 -4.998 52.511 1.00 30.06 C ANISOU 90 CB PHE A 32 3935 3700 3787 120 -28 0 C ATOM 91 CG PHE A 32 25.478 -3.555 52.363 1.00 26.77 C ANISOU 91 CG PHE A 32 3384 3473 3313 -29 -9 -18 C ATOM 92 CD1 PHE A 32 25.240 -2.770 53.475 1.00 25.94 C ANISOU 92 CD1 PHE A 32 3263 3260 3331 3 8 26 C ATOM 93 CD2 PHE A 32 25.356 -2.986 51.107 1.00 25.58 C ANISOU 93 CD2 PHE A 32 3219 3187 3313 5 -3 -10 C ATOM 94 CE1 PHE A 32 24.879 -1.442 53.344 1.00 25.44 C ANISOU 94 CE1 PHE A 32 3191 3241 3235 1 -18 24 C ATOM 95 CE2 PHE A 32 24.994 -1.661 50.970 1.00 24.89 C ANISOU 95 CE2 PHE A 32 3125 3142 3188 -14 0 -10 C ATOM 96 CZ PHE A 32 24.758 -0.888 52.087 1.00 24.86 C ANISOU 96 CZ PHE A 32 3133 3128 3185 -18 8 -5 C ATOM 97 N SER A 33 25.625 -7.919 53.763 1.00 32.99 N ANISOU 97 N SER A 33 4187 4137 4209 -7 -11 9 N ATOM 98 CA SER A 33 26.269 -9.227 53.773 1.00 33.01 C ANISOU 98 CA SER A 33 4175 4129 4240 -16 10 -7 C ATOM 99 C SER A 33 25.306 -10.363 53.466 1.00 32.43 C ANISOU 99 C SER A 33 4105 4084 4134 12 3 3 C ATOM 100 O SER A 33 25.675 -11.326 52.788 1.00 32.34 O ANISOU 100 O SER A 33 4095 4073 4119 -5 -7 1 O ATOM 101 CB SER A 33 26.968 -9.469 55.114 1.00 34.45 C ANISOU 101 CB SER A 33 4420 4341 4328 5 -61 23 C ATOM 102 OG SER A 33 26.063 -9.333 56.195 1.00 35.59 O ANISOU 102 OG SER A 33 4531 4500 4491 24 18 6 O ATOM 103 N ALA A 34 24.064 -10.259 53.922 1.00 31.99 N ANISOU 103 N ALA A 34 4084 4023 4047 -9 -10 0 N ATOM 104 CA ALA A 34 23.064 -11.296 53.720 1.00 31.75 C ANISOU 104 CA ALA A 34 4043 4010 4008 5 -3 7 C ATOM 105 C ALA A 34 22.790 -11.580 52.249 1.00 31.65 C ANISOU 105 C ALA A 34 4039 3984 4003 -1 -9 9 C ATOM 106 O ALA A 34 22.640 -12.741 51.865 1.00 31.59 O ANISOU 106 O ALA A 34 4039 3986 3978 -9 -9 16 O ATOM 107 CB ALA A 34 21.771 -10.913 54.428 1.00 31.73 C ANISOU 107 CB ALA A 34 4040 3992 4025 5 1 15 C ATOM 108 N GLU A 35 22.732 -10.543 51.418 1.00 31.42 N ANISOU 108 N GLU A 35 4004 3966 3969 -19 -5 -8 N ATOM 109 CA GLU A 35 22.494 -10.697 49.992 1.00 31.10 C ANISOU 109 CA GLU A 35 3931 3938 3949 -28 29 -9 C ATOM 110 C GLU A 35 23.791 -10.781 49.193 1.00 30.45 C ANISOU 110 C GLU A 35 3864 3840 3865 -17 -22 -1 C ATOM 111 O GLU A 35 23.763 -10.880 47.965 1.00 30.39 O ANISOU 111 O GLU A 35 3873 3810 3864 -5 9 -11 O ATOM 112 CB GLU A 35 21.679 -9.519 49.453 1.00 32.53 C ANISOU 112 CB GLU A 35 4170 4037 4154 6 -59 52 C ATOM 113 CG GLU A 35 20.395 -9.205 50.188 1.00 34.74 C ANISOU 113 CG GLU A 35 4381 4417 4400 58 43 -5 C ATOM 114 CD GLU A 35 19.339 -10.284 50.052 1.00 36.15 C ANISOU 114 CD GLU A 35 4562 4522 4651 -31 -26 26 C ATOM 115 OE1 GLU A 35 19.370 -11.055 49.072 1.00 36.85 O ANISOU 115 OE1 GLU A 35 4688 4627 4686 2 -12 1 O ATOM 116 OE2 GLU A 35 18.474 -10.349 50.950 1.00 36.81 O ANISOU 116 OE2 GLU A 35 4646 4636 4705 11 9 24 O ATOM 117 N ALA A 36 24.930 -10.689 49.869 1.00 29.78 N ANISOU 117 N ALA A 36 3794 3741 3778 -12 29 22 N ATOM 118 CA ALA A 36 26.227 -10.607 49.214 1.00 29.26 C ANISOU 118 CA ALA A 36 3751 3657 3708 -2 0 43 C ATOM 119 C ALA A 36 26.279 -9.397 48.282 1.00 28.23 C ANISOU 119 C ALA A 36 3591 3535 3599 16 3 -25 C ATOM 120 O ALA A 36 26.703 -9.489 47.131 1.00 28.36 O ANISOU 120 O ALA A 36 3598 3563 3613 4 17 29 O ATOM 121 CB ALA A 36 26.524 -11.895 48.460 1.00 30.37 C ANISOU 121 CB ALA A 36 3881 3768 3889 23 17 -38 C ATOM 122 N VAL A 37 25.848 -8.248 48.794 1.00 27.08 N ANISOU 122 N VAL A 37 3433 3409 3447 -27 -10 69 N ATOM 123 CA VAL A 37 25.772 -7.031 47.999 1.00 25.78 C ANISOU 123 CA VAL A 37 3215 3260 3321 -48 -1 -14 C ATOM 124 C VAL A 37 27.030 -6.190 48.203 1.00 24.24 C ANISOU 124 C VAL A 37 3089 3056 3063 31 25 19 C ATOM 125 O VAL A 37 27.423 -5.912 49.332 1.00 23.99 O ANISOU 125 O VAL A 37 3059 2998 3057 23 17 29 O ATOM 126 CB VAL A 37 24.530 -6.190 48.337 1.00 25.98 C ANISOU 126 CB VAL A 37 3279 3274 3318 12 -2 34 C ATOM 127 CG1 VAL A 37 24.569 -4.829 47.653 1.00 25.82 C ANISOU 127 CG1 VAL A 37 3261 3227 3324 -2 -12 5 C ATOM 128 CG2 VAL A 37 23.262 -6.930 47.935 1.00 26.56 C ANISOU 128 CG2 VAL A 37 3331 3327 3433 -22 -10 10 C ATOM 129 N ASN A 38 27.651 -5.805 47.094 1.00 23.06 N ANISOU 129 N ASN A 38 2907 2854 3000 2 -44 9 N ATOM 130 CA ASN A 38 28.693 -4.784 47.123 1.00 22.09 C ANISOU 130 CA ASN A 38 2830 2736 2826 52 -38 15 C ATOM 131 C ASN A 38 28.069 -3.425 46.812 1.00 20.96 C ANISOU 131 C ASN A 38 2684 2630 2649 -4 -10 -35 C ATOM 132 O ASN A 38 27.683 -3.158 45.673 1.00 20.82 O ANISOU 132 O ASN A 38 2652 2577 2682 4 -34 -11 O ATOM 133 CB ASN A 38 29.801 -5.107 46.125 1.00 22.88 C ANISOU 133 CB ASN A 38 2901 2902 2891 -21 24 -12 C ATOM 134 CG ASN A 38 30.633 -6.299 46.560 1.00 24.37 C ANISOU 134 CG ASN A 38 3075 3040 3145 45 -11 33 C ATOM 135 OD1 ASN A 38 31.020 -6.393 47.724 1.00 25.20 O ANISOU 135 OD1 ASN A 38 3226 3164 3185 44 -33 12 O ATOM 136 ND2 ASN A 38 30.911 -7.205 45.632 1.00 25.26 N ANISOU 136 ND2 ASN A 38 3236 3153 3208 13 -5 -31 N ATOM 137 N GLY A 39 27.968 -2.582 47.834 1.00 20.04 N ANISOU 137 N GLY A 39 2522 2520 2573 27 -20 27 N ATOM 138 CA GLY A 39 27.269 -1.314 47.673 1.00 19.13 C ANISOU 138 CA GLY A 39 2425 2415 2429 -27 -25 -31 C ATOM 139 C GLY A 39 27.590 -0.348 48.803 1.00 18.34 C ANISOU 139 C GLY A 39 2327 2296 2346 22 -3 19 C ATOM 140 O GLY A 39 28.311 -0.678 49.745 1.00 18.49 O ANISOU 140 O GLY A 39 2347 2319 2360 2 -29 23 O ATOM 141 N VAL A 40 27.030 0.852 48.695 1.00 17.27 N ANISOU 141 N VAL A 40 2188 2210 2162 -31 -11 0 N ATOM 142 CA VAL A 40 27.237 1.864 49.722 1.00 16.47 C ANISOU 142 CA VAL A 40 2062 2099 2098 -3 -12 49 C ATOM 143 C VAL A 40 25.940 2.606 50.017 1.00 16.43 C ANISOU 143 C VAL A 40 2073 2109 2061 9 -12 6 C ATOM 144 O VAL A 40 25.141 2.870 49.115 1.00 16.29 O ANISOU 144 O VAL A 40 2071 2106 2010 37 -9 -1 O ATOM 145 CB VAL A 40 28.344 2.849 49.318 1.00 15.72 C ANISOU 145 CB VAL A 40 2029 2016 1929 7 -37 16 C ATOM 146 CG1 VAL A 40 27.922 3.722 48.143 1.00 15.00 C ANISOU 146 CG1 VAL A 40 1888 1891 1918 -11 -7 9 C ATOM 147 CG2 VAL A 40 28.754 3.707 50.505 1.00 15.31 C ANISOU 147 CG2 VAL A 40 1949 1948 1920 0 -14 29 C ATOM 148 N PHE A 41 25.737 2.913 51.288 1.00 15.91 N ANISOU 148 N PHE A 41 2029 1993 2025 -3 -18 21 N ATOM 149 CA PHE A 41 24.665 3.796 51.718 1.00 15.78 C ANISOU 149 CA PHE A 41 1993 1989 2013 -16 -16 15 C ATOM 150 C PHE A 41 25.258 5.009 52.427 1.00 15.84 C ANISOU 150 C PHE A 41 2044 1975 1999 2 -5 14 C ATOM 151 O PHE A 41 26.107 4.871 53.306 1.00 16.42 O ANISOU 151 O PHE A 41 2047 2098 2093 2 -38 -1 O ATOM 152 CB PHE A 41 23.680 3.074 52.635 1.00 16.02 C ANISOU 152 CB PHE A 41 2036 2047 2006 -2 -10 62 C ATOM 153 CG PHE A 41 22.462 3.873 53.000 1.00 16.45 C ANISOU 153 CG PHE A 41 2072 2055 2124 11 -18 16 C ATOM 154 CD1 PHE A 41 21.676 4.440 52.006 1.00 16.32 C ANISOU 154 CD1 PHE A 41 2088 2071 2043 16 1 7 C ATOM 155 CD2 PHE A 41 22.091 4.067 54.317 1.00 17.60 C ANISOU 155 CD2 PHE A 41 2243 2276 2167 1 -21 7 C ATOM 156 CE1 PHE A 41 20.551 5.176 52.318 1.00 16.33 C ANISOU 156 CE1 PHE A 41 2070 2012 2121 -13 -6 -3 C ATOM 157 CE2 PHE A 41 20.965 4.801 54.640 1.00 18.04 C ANISOU 157 CE2 PHE A 41 2276 2302 2277 17 -24 19 C ATOM 158 CZ PHE A 41 20.192 5.357 53.637 1.00 17.45 C ANISOU 158 CZ PHE A 41 2261 2194 2176 4 11 -16 C ATOM 159 N VAL A 42 24.867 6.196 51.987 1.00 15.33 N ANISOU 159 N VAL A 42 1944 1939 1941 -2 -2 -9 N ATOM 160 CA VAL A 42 25.282 7.434 52.640 1.00 15.11 C ANISOU 160 CA VAL A 42 1919 1940 1882 -14 -10 14 C ATOM 161 C VAL A 42 24.048 8.115 53.227 1.00 15.75 C ANISOU 161 C VAL A 42 1967 2038 1981 13 4 -11 C ATOM 162 O VAL A 42 23.089 8.386 52.503 1.00 15.73 O ANISOU 162 O VAL A 42 1977 2037 1964 21 11 8 O ATOM 163 CB VAL A 42 26.008 8.387 51.679 1.00 14.46 C ANISOU 163 CB VAL A 42 1801 1839 1855 33 -61 21 C ATOM 164 CG1 VAL A 42 26.372 9.699 52.364 1.00 14.67 C ANISOU 164 CG1 VAL A 42 1878 1851 1846 11 -23 20 C ATOM 165 CG2 VAL A 42 27.262 7.740 51.111 1.00 14.07 C ANISOU 165 CG2 VAL A 42 1812 1845 1690 -14 -15 -12 C ATOM 166 N LEU A 43 24.076 8.361 54.530 1.00 16.08 N ANISOU 166 N LEU A 43 2023 2091 1993 -14 -36 10 N ATOM 167 CA LEU A 43 22.934 8.951 55.219 1.00 16.63 C ANISOU 167 CA LEU A 43 2092 2154 2074 15 4 13 C ATOM 168 C LEU A 43 23.367 10.159 56.040 1.00 17.59 C ANISOU 168 C LEU A 43 2239 2234 2210 -19 -15 -29 C ATOM 169 O LEU A 43 24.288 10.060 56.852 1.00 18.05 O ANISOU 169 O LEU A 43 2275 2305 2276 -3 -41 20 O ATOM 170 CB LEU A 43 22.264 7.905 56.111 1.00 17.06 C ANISOU 170 CB LEU A 43 2170 2179 2132 -17 -22 43 C ATOM 171 CG LEU A 43 21.076 8.374 56.950 1.00 17.32 C ANISOU 171 CG LEU A 43 2203 2145 2232 15 -10 -14 C ATOM 172 CD1 LEU A 43 19.894 8.749 56.065 1.00 17.91 C ANISOU 172 CD1 LEU A 43 2295 2259 2251 14 -62 -29 C ATOM 173 CD2 LEU A 43 20.675 7.305 57.956 1.00 17.76 C ANISOU 173 CD2 LEU A 43 2256 2287 2204 -18 -19 23 C ATOM 174 N CYS A 44 22.744 11.306 55.787 1.00 18.26 N ANISOU 174 N CYS A 44 2324 2321 2292 39 -17 16 N ATOM 175 CA CYS A 44 23.140 12.554 56.429 1.00 19.64 C ANISOU 175 CA CYS A 44 2508 2443 2513 15 -56 -72 C ATOM 176 C CYS A 44 21.969 13.205 57.151 1.00 20.10 C ANISOU 176 C CYS A 44 2541 2552 2542 22 -11 -37 C ATOM 177 O CYS A 44 20.928 13.469 56.546 1.00 20.31 O ANISOU 177 O CYS A 44 2584 2614 2518 28 -36 -50 O ATOM 178 CB CYS A 44 23.704 13.531 55.391 1.00 22.51 C ANISOU 178 CB CYS A 44 2926 2806 2823 -97 0 97 C ATOM 179 SG CYS A 44 24.897 12.793 54.254 1.00 24.74 S ANISOU 179 SG CYS A 44 3179 3149 3074 58 50 -28 S ATOM 180 N LYS A 45 22.128 13.476 58.442 1.00 20.20 N ANISOU 180 N LYS A 45 2559 2568 2550 8 -49 -4 N ATOM 181 CA LYS A 45 21.093 14.144 59.224 1.00 20.65 C ANISOU 181 CA LYS A 45 2598 2607 2641 3 -1 -14 C ATOM 182 C LYS A 45 21.271 15.652 59.205 1.00 20.71 C ANISOU 182 C LYS A 45 2630 2618 2621 -12 -12 -2 C ATOM 183 O LYS A 45 22.332 16.182 59.550 1.00 20.98 O ANISOU 183 O LYS A 45 2651 2697 2622 -25 -67 28 O ATOM 184 CB LYS A 45 21.119 13.640 60.669 1.00 22.61 C ANISOU 184 CB LYS A 45 2947 2893 2750 -38 -62 59 C ATOM 185 CG LYS A 45 20.080 14.272 61.583 1.00 25.08 C ANISOU 185 CG LYS A 45 3083 3161 3286 43 43 -72 C ATOM 186 CD LYS A 45 20.207 13.713 62.994 1.00 28.98 C ANISOU 186 CD LYS A 45 3810 3654 3547 -28 -62 59 C ATOM 187 CE LYS A 45 19.020 14.104 63.858 1.00 31.86 C ANISOU 187 CE LYS A 45 3962 4049 4093 22 55 -45 C ATOM 188 NZ LYS A 45 19.059 13.416 65.180 1.00 33.61 N ANISOU 188 NZ LYS A 45 4301 4258 4212 5 10 15 N ATOM 189 N SER A 46 20.263 16.394 58.770 1.00 20.56 N ANISOU 189 N SER A 46 2635 2623 2554 -6 -18 -17 N ATOM 190 CA SER A 46 20.224 17.845 58.763 1.00 21.24 C ANISOU 190 CA SER A 46 2764 2653 2652 -1 -35 -23 C ATOM 191 C SER A 46 21.004 18.489 57.621 1.00 21.66 C ANISOU 191 C SER A 46 2813 2714 2701 -26 -26 -16 C ATOM 192 O SER A 46 20.488 19.417 56.988 1.00 21.61 O ANISOU 192 O SER A 46 2832 2685 2694 -48 -35 -12 O ATOM 193 CB ASER A 46 20.713 18.419 60.100 0.50 19.82 C ANISOU 193 CB ASER A 46 2488 2491 2551 -13 52 43 C ATOM 194 CB BSER A 46 20.725 18.423 60.095 0.50 21.48 C ANISOU 194 CB BSER A 46 2765 2740 2657 -8 -29 -28 C ATOM 195 OG ASER A 46 19.872 18.000 61.161 0.50 18.68 O ANISOU 195 OG ASER A 46 2343 2411 2343 -11 -47 -13 O ATOM 196 OG BSER A 46 20.702 19.839 60.063 0.50 22.21 O ANISOU 196 OG BSER A 46 2849 2781 2809 2 -12 -3 O ATOM 197 N SER A 47 22.226 18.063 57.362 1.00 22.65 N ANISOU 197 N SER A 47 2850 2888 2869 5 -61 -35 N ATOM 198 CA SER A 47 23.033 18.572 56.271 1.00 24.18 C ANISOU 198 CA SER A 47 3062 3120 3004 -11 3 36 C ATOM 199 C SER A 47 24.087 17.549 55.867 1.00 24.93 C ANISOU 199 C SER A 47 3154 3142 3175 9 -44 -13 C ATOM 200 O SER A 47 24.240 16.503 56.501 1.00 25.06 O ANISOU 200 O SER A 47 3174 3130 3219 -6 -43 -4 O ATOM 201 CB SER A 47 23.721 19.875 56.693 1.00 26.22 C ANISOU 201 CB SER A 47 3359 3199 3403 -67 10 -26 C ATOM 202 OG SER A 47 24.750 19.587 57.629 1.00 28.03 O ANISOU 202 OG SER A 47 3552 3569 3531 -14 -61 11 O ATOM 203 N SER A 48 24.879 17.882 54.856 1.00 25.92 N ANISOU 203 N SER A 48 3313 3292 3244 -42 -7 11 N ATOM 204 CA SER A 48 25.919 17.009 54.339 1.00 27.26 C ANISOU 204 CA SER A 48 3473 3427 3459 28 49 -6 C ATOM 205 C SER A 48 27.222 17.085 55.125 1.00 28.62 C ANISOU 205 C SER A 48 3581 3640 3653 -6 -22 31 C ATOM 206 O SER A 48 28.200 16.413 54.787 1.00 28.78 O ANISOU 206 O SER A 48 3605 3661 3667 3 -18 11 O ATOM 207 CB SER A 48 26.194 17.350 52.867 1.00 26.68 C ANISOU 207 CB SER A 48 3408 3302 3426 -18 -4 1 C ATOM 208 OG SER A 48 26.651 18.686 52.751 1.00 25.26 O ANISOU 208 OG SER A 48 3213 3231 3152 9 0 13 O ATOM 209 N LYS A 49 27.260 17.878 56.185 1.00 29.94 N ANISOU 209 N LYS A 49 3829 3786 3760 -13 19 -20 N ATOM 210 CA LYS A 49 28.376 17.915 57.115 1.00 31.46 C ANISOU 210 CA LYS A 49 3920 4071 3964 -4 -38 52 C ATOM 211 C LYS A 49 28.314 16.773 58.124 1.00 31.67 C ANISOU 211 C LYS A 49 4003 4017 4015 -18 -8 23 C ATOM 212 O LYS A 49 29.338 16.392 58.697 1.00 32.16 O ANISOU 212 O LYS A 49 4056 4080 4083 3 -39 13 O ATOM 213 CB LYS A 49 28.395 19.262 57.844 1.00 34.78 C ANISOU 213 CB LYS A 49 4434 4321 4459 23 -33 -170 C ATOM 214 CG LYS A 49 28.595 20.462 56.934 1.00 38.40 C ANISOU 214 CG LYS A 49 4869 4857 4865 -53 -1 153 C ATOM 215 CD LYS A 49 28.291 21.780 57.616 1.00 42.32 C ANISOU 215 CD LYS A 49 5447 5180 5454 60 86 -42 C ATOM 216 CE LYS A 49 29.272 22.139 58.713 1.00 44.89 C ANISOU 216 CE LYS A 49 5679 5672 5704 -7 -61 -42 C ATOM 217 NZ LYS A 49 28.978 21.448 59.997 1.00 45.90 N ANISOU 217 NZ LYS A 49 5837 5784 5818 -1 11 14 N ATOM 218 N SER A 50 27.128 16.217 58.348 1.00 31.35 N ANISOU 218 N SER A 50 3998 3929 3983 -12 -24 11 N ATOM 219 CA SER A 50 26.939 15.148 59.319 1.00 30.99 C ANISOU 219 CA SER A 50 3962 3854 3959 -28 -53 -21 C ATOM 220 C SER A 50 26.479 13.856 58.652 1.00 29.87 C ANISOU 220 C SER A 50 3790 3762 3798 32 17 -2 C ATOM 221 O SER A 50 25.310 13.476 58.765 1.00 30.04 O ANISOU 221 O SER A 50 3804 3793 3817 -3 -23 2 O ATOM 222 CB SER A 50 25.918 15.590 60.374 1.00 33.49 C ANISOU 222 CB SER A 50 4204 4333 4188 48 75 4 C ATOM 223 OG SER A 50 26.266 16.852 60.920 1.00 35.75 O ANISOU 223 OG SER A 50 4572 4432 4579 -10 -5 -22 O ATOM 224 N CYS A 51 27.394 13.175 57.964 1.00 28.49 N ANISOU 224 N CYS A 51 3666 3537 3621 -36 -52 -8 N ATOM 225 CA CYS A 51 27.038 11.984 57.203 1.00 27.15 C ANISOU 225 CA CYS A 51 3463 3407 3443 29 -10 52 C ATOM 226 C CYS A 51 27.661 10.714 57.772 1.00 25.92 C ANISOU 226 C CYS A 51 3306 3238 3305 -60 -10 -15 C ATOM 227 O CYS A 51 28.743 10.734 58.355 1.00 26.36 O ANISOU 227 O CYS A 51 3340 3292 3382 7 -44 11 O ATOM 228 CB CYS A 51 27.464 12.118 55.738 1.00 26.70 C ANISOU 228 CB CYS A 51 3357 3363 3424 -1 3 3 C ATOM 229 SG CYS A 51 26.702 13.492 54.854 1.00 26.79 S ANISOU 229 SG CYS A 51 3304 3379 3497 -22 -43 13 S ATOM 230 N ALA A 52 26.966 9.598 57.576 1.00 24.23 N ANISOU 230 N ALA A 52 3123 3069 3014 60 -19 4 N ATOM 231 CA ALA A 52 27.487 8.288 57.944 1.00 22.75 C ANISOU 231 CA ALA A 52 2902 2922 2820 -29 -2 -43 C ATOM 232 C ALA A 52 27.338 7.324 56.769 1.00 21.74 C ANISOU 232 C ALA A 52 2748 2754 2758 33 8 18 C ATOM 233 O ALA A 52 26.460 7.503 55.923 1.00 21.88 O ANISOU 233 O ALA A 52 2796 2770 2750 -2 -34 3 O ATOM 234 CB ALA A 52 26.770 7.743 59.168 1.00 22.14 C ANISOU 234 CB ALA A 52 2828 2793 2790 6 -32 -27 C ATOM 235 N THR A 53 28.177 6.299 56.736 1.00 20.54 N ANISOU 235 N THR A 53 2620 2629 2557 -36 -5 5 N ATOM 236 CA THR A 53 28.165 5.341 55.633 1.00 19.80 C ANISOU 236 CA THR A 53 2485 2550 2488 -8 7 42 C ATOM 237 C THR A 53 28.655 3.980 56.103 1.00 19.93 C ANISOU 237 C THR A 53 2552 2517 2504 -17 -2 3 C ATOM 238 O THR A 53 29.384 3.893 57.093 1.00 20.33 O ANISOU 238 O THR A 53 2591 2594 2538 -9 -30 20 O ATOM 239 CB THR A 53 29.033 5.862 54.472 1.00 18.58 C ANISOU 239 CB THR A 53 2333 2378 2348 -14 -56 -59 C ATOM 240 OG1 THR A 53 28.932 4.981 53.348 1.00 17.60 O ANISOU 240 OG1 THR A 53 2230 2236 2223 4 3 36 O ATOM 241 CG2 THR A 53 30.494 5.963 54.894 1.00 17.72 C ANISOU 241 CG2 THR A 53 2289 2237 2209 -8 -15 21 C ATOM 242 N ASN A 54 28.296 2.920 55.387 1.00 19.52 N ANISOU 242 N ASN A 54 2502 2451 2462 -20 -8 44 N ATOM 243 CA ASN A 54 28.817 1.592 55.668 1.00 19.44 C ANISOU 243 CA ASN A 54 2457 2443 2485 -22 -14 -2 C ATOM 244 C ASN A 54 30.205 1.393 55.067 1.00 19.68 C ANISOU 244 C ASN A 54 2473 2485 2520 -9 0 24 C ATOM 245 O ASN A 54 30.932 0.502 55.504 1.00 20.15 O ANISOU 245 O ASN A 54 2513 2532 2611 4 -52 40 O ATOM 246 CB ASN A 54 27.879 0.506 55.126 1.00 18.68 C ANISOU 246 CB ASN A 54 2413 2380 2305 19 -31 21 C ATOM 247 CG ASN A 54 27.800 0.550 53.610 1.00 17.41 C ANISOU 247 CG ASN A 54 2155 2226 2233 23 -8 -17 C ATOM 248 OD1 ASN A 54 27.411 1.575 53.049 1.00 17.66 O ANISOU 248 OD1 ASN A 54 2273 2192 2247 -53 31 14 O ATOM 249 ND2 ASN A 54 28.184 -0.539 52.961 1.00 17.41 N ANISOU 249 ND2 ASN A 54 2199 2193 2223 8 -70 -17 N ATOM 250 N ASP A 55 30.551 2.191 54.065 1.00 19.20 N ANISOU 250 N ASP A 55 2374 2472 2451 11 -30 14 N ATOM 251 CA ASP A 55 31.795 1.991 53.329 1.00 19.05 C ANISOU 251 CA ASP A 55 2376 2408 2453 -7 -10 55 C ATOM 252 C ASP A 55 32.382 3.337 52.923 1.00 18.48 C ANISOU 252 C ASP A 55 2315 2352 2355 -6 -31 10 C ATOM 253 O ASP A 55 31.958 3.968 51.956 1.00 18.18 O ANISOU 253 O ASP A 55 2295 2312 2300 -16 -6 -6 O ATOM 254 CB ASP A 55 31.580 1.099 52.113 1.00 20.84 C ANISOU 254 CB ASP A 55 2764 2565 2590 -48 -53 -29 C ATOM 255 CG ASP A 55 32.838 0.659 51.400 1.00 23.79 C ANISOU 255 CG ASP A 55 2937 3050 3052 51 48 6 C ATOM 256 OD1 ASP A 55 33.846 1.392 51.394 1.00 24.64 O ANISOU 256 OD1 ASP A 55 3019 3118 3224 -19 -1 -4 O ATOM 257 OD2 ASP A 55 32.843 -0.448 50.812 1.00 25.23 O ANISOU 257 OD2 ASP A 55 3197 3142 3248 23 -3 -63 O ATOM 258 N LEU A 56 33.402 3.758 53.671 1.00 18.37 N ANISOU 258 N LEU A 56 2322 2326 2333 -20 -31 15 N ATOM 259 CA LEU A 56 34.052 5.036 53.407 1.00 18.03 C ANISOU 259 CA LEU A 56 2273 2308 2270 -26 -29 3 C ATOM 260 C LEU A 56 34.689 5.100 52.028 1.00 17.80 C ANISOU 260 C LEU A 56 2253 2268 2243 -17 -55 -14 C ATOM 261 O LEU A 56 34.571 6.128 51.355 1.00 17.85 O ANISOU 261 O LEU A 56 2300 2297 2184 -62 -27 11 O ATOM 262 CB LEU A 56 35.107 5.312 54.486 1.00 18.07 C ANISOU 262 CB LEU A 56 2260 2306 2299 -20 -52 14 C ATOM 263 CG LEU A 56 34.571 5.756 55.852 1.00 19.47 C ANISOU 263 CG LEU A 56 2486 2481 2433 3 49 6 C ATOM 264 CD1 LEU A 56 35.682 5.692 56.893 1.00 20.81 C ANISOU 264 CD1 LEU A 56 2634 2698 2576 -29 -57 -8 C ATOM 265 CD2 LEU A 56 33.990 7.159 55.779 1.00 19.97 C ANISOU 265 CD2 LEU A 56 2514 2515 2559 10 -3 -13 C ATOM 266 N ALA A 57 35.357 4.038 51.595 1.00 17.95 N ANISOU 266 N ALA A 57 2225 2302 2292 -18 -58 -26 N ATOM 267 CA ALA A 57 36.009 4.027 50.289 1.00 18.74 C ANISOU 267 CA ALA A 57 2350 2413 2357 -44 -5 -9 C ATOM 268 C ALA A 57 35.005 4.202 49.154 1.00 19.05 C ANISOU 268 C ALA A 57 2396 2434 2408 -41 -40 0 C ATOM 269 O ALA A 57 35.217 4.999 48.238 1.00 19.99 O ANISOU 269 O ALA A 57 2570 2562 2464 -74 -23 33 O ATOM 270 CB ALA A 57 36.793 2.739 50.091 1.00 20.22 C ANISOU 270 CB ALA A 57 2553 2523 2606 33 0 -18 C ATOM 271 N ARG A 58 33.888 3.484 49.221 1.00 18.26 N ANISOU 271 N ARG A 58 2315 2325 2296 19 -45 5 N ATOM 272 CA ARG A 58 32.907 3.501 48.143 1.00 17.35 C ANISOU 272 CA ARG A 58 2197 2152 2243 9 -3 1 C ATOM 273 C ARG A 58 32.024 4.735 48.158 1.00 16.68 C ANISOU 273 C ARG A 58 2130 2120 2086 -7 -5 -6 C ATOM 274 O ARG A 58 31.455 5.127 47.130 1.00 16.57 O ANISOU 274 O ARG A 58 2101 2096 2099 7 -19 1 O ATOM 275 CB ARG A 58 32.051 2.224 48.199 1.00 17.06 C ANISOU 275 CB ARG A 58 2148 2200 2134 -36 -31 4 C ATOM 276 CG ARG A 58 31.085 2.142 47.028 1.00 16.14 C ANISOU 276 CG ARG A 58 2039 2028 2065 -10 16 22 C ATOM 277 CD ARG A 58 30.513 0.754 46.810 1.00 15.73 C ANISOU 277 CD ARG A 58 1989 2004 1985 15 -69 -6 C ATOM 278 NE ARG A 58 29.532 0.799 45.725 1.00 14.55 N ANISOU 278 NE ARG A 58 1862 1789 1877 -5 2 34 N ATOM 279 CZ ARG A 58 29.421 -0.091 44.753 1.00 15.02 C ANISOU 279 CZ ARG A 58 1928 1900 1880 13 -25 -7 C ATOM 280 NH1 ARG A 58 30.237 -1.135 44.671 1.00 15.43 N ANISOU 280 NH1 ARG A 58 1951 1880 2032 -9 1 -11 N ATOM 281 NH2 ARG A 58 28.488 0.087 43.822 1.00 14.85 N ANISOU 281 NH2 ARG A 58 1823 1827 1994 -7 -43 -1 N ATOM 282 N ALA A 59 31.927 5.424 49.288 1.00 16.17 N ANISOU 282 N ALA A 59 2040 2041 2064 14 -20 9 N ATOM 283 CA ALA A 59 31.090 6.607 49.424 1.00 15.75 C ANISOU 283 CA ALA A 59 2025 1996 1963 -5 5 -6 C ATOM 284 C ALA A 59 31.387 7.673 48.377 1.00 15.62 C ANISOU 284 C ALA A 59 1985 1985 1964 6 -10 2 C ATOM 285 O ALA A 59 30.452 8.329 47.907 1.00 15.65 O ANISOU 285 O ALA A 59 1946 1991 2009 9 1 -12 O ATOM 286 CB ALA A 59 31.229 7.187 50.826 1.00 15.05 C ANISOU 286 CB ALA A 59 1854 1941 1923 -44 -26 22 C ATOM 287 N SER A 60 32.648 7.874 48.005 1.00 15.73 N ANISOU 287 N SER A 60 2005 2004 1967 -28 -3 6 N ATOM 288 CA SER A 60 32.985 8.820 46.953 1.00 16.05 C ANISOU 288 CA SER A 60 2059 2054 1985 19 13 35 C ATOM 289 C SER A 60 33.413 8.160 45.654 1.00 15.59 C ANISOU 289 C SER A 60 1959 2001 1963 -2 -19 25 C ATOM 290 O SER A 60 33.879 8.886 44.767 1.00 15.59 O ANISOU 290 O SER A 60 1957 2066 1900 0 -23 25 O ATOM 291 CB SER A 60 34.078 9.784 47.440 1.00 18.15 C ANISOU 291 CB SER A 60 2234 2309 2351 -130 -55 37 C ATOM 292 OG SER A 60 33.523 10.672 48.397 1.00 20.91 O ANISOU 292 OG SER A 60 2647 2621 2677 33 0 -89 O ATOM 293 N LYS A 61 33.207 6.859 45.489 1.00 15.80 N ANISOU 293 N LYS A 61 1978 2033 1993 -27 -34 27 N ATOM 294 CA LYS A 61 33.431 6.232 44.188 1.00 16.44 C ANISOU 294 CA LYS A 61 2029 2178 2040 16 -13 -8 C ATOM 295 C LYS A 61 32.317 6.626 43.219 1.00 16.24 C ANISOU 295 C LYS A 61 2033 2143 1996 0 -12 0 C ATOM 296 O LYS A 61 31.158 6.752 43.615 1.00 16.04 O ANISOU 296 O LYS A 61 2005 2101 1989 23 -47 24 O ATOM 297 CB LYS A 61 33.539 4.714 44.306 1.00 20.16 C ANISOU 297 CB LYS A 61 2689 2337 2634 -14 61 23 C ATOM 298 CG LYS A 61 34.809 4.257 45.012 1.00 23.56 C ANISOU 298 CG LYS A 61 2879 3068 3005 36 -58 30 C ATOM 299 CD LYS A 61 34.937 2.741 45.016 1.00 26.05 C ANISOU 299 CD LYS A 61 3365 3195 3339 1 30 -13 C ATOM 300 CE LYS A 61 36.226 2.301 45.694 1.00 27.39 C ANISOU 300 CE LYS A 61 3471 3480 3456 13 -27 17 C ATOM 301 NZ LYS A 61 36.435 0.829 45.588 1.00 28.00 N ANISOU 301 NZ LYS A 61 3541 3517 3581 13 -25 6 N ATOM 302 N GLU A 62 32.671 6.842 41.953 1.00 15.76 N ANISOU 302 N GLU A 62 1992 2024 1973 1 -31 -9 N ATOM 303 CA GLU A 62 31.717 7.400 41.001 1.00 15.43 C ANISOU 303 CA GLU A 62 1934 1976 1952 -18 -16 -8 C ATOM 304 C GLU A 62 31.209 6.402 39.976 1.00 15.23 C ANISOU 304 C GLU A 62 1891 1931 1965 -7 0 -9 C ATOM 305 O GLU A 62 31.937 5.597 39.402 1.00 15.61 O ANISOU 305 O GLU A 62 1920 1954 2056 33 -7 -6 O ATOM 306 CB GLU A 62 32.347 8.595 40.277 1.00 16.47 C ANISOU 306 CB GLU A 62 2129 2045 2083 -25 8 74 C ATOM 307 CG GLU A 62 32.810 9.675 41.241 1.00 17.45 C ANISOU 307 CG GLU A 62 2235 2210 2185 32 -13 -70 C ATOM 308 CD GLU A 62 33.422 10.860 40.522 1.00 19.34 C ANISOU 308 CD GLU A 62 2402 2500 2447 -66 16 88 C ATOM 309 OE1 GLU A 62 34.097 10.641 39.498 1.00 19.36 O ANISOU 309 OE1 GLU A 62 2404 2562 2389 -46 -31 59 O ATOM 310 OE2 GLU A 62 33.209 11.991 41.001 1.00 22.48 O ANISOU 310 OE2 GLU A 62 2911 2716 2916 36 -30 -51 O ATOM 311 N TYR A 63 29.890 6.424 39.774 1.00 14.47 N ANISOU 311 N TYR A 63 1852 1849 1795 -25 -10 5 N ATOM 312 CA TYR A 63 29.180 5.466 38.942 1.00 14.25 C ANISOU 312 CA TYR A 63 1833 1809 1773 9 -10 6 C ATOM 313 C TYR A 63 28.235 6.182 37.977 1.00 14.00 C ANISOU 313 C TYR A 63 1752 1790 1778 1 -10 -21 C ATOM 314 O TYR A 63 27.787 7.293 38.245 1.00 14.18 O ANISOU 314 O TYR A 63 1824 1770 1793 -36 -19 -30 O ATOM 315 CB TYR A 63 28.362 4.475 39.787 1.00 14.46 C ANISOU 315 CB TYR A 63 1841 1823 1830 4 11 4 C ATOM 316 CG TYR A 63 29.203 3.692 40.774 1.00 14.65 C ANISOU 316 CG TYR A 63 1829 1861 1878 -1 1 15 C ATOM 317 CD1 TYR A 63 29.852 2.526 40.396 1.00 14.80 C ANISOU 317 CD1 TYR A 63 1842 1867 1913 -9 12 4 C ATOM 318 CD2 TYR A 63 29.376 4.154 42.073 1.00 15.03 C ANISOU 318 CD2 TYR A 63 1909 1903 1900 7 -11 0 C ATOM 319 CE1 TYR A 63 30.636 1.827 41.296 1.00 15.18 C ANISOU 319 CE1 TYR A 63 1907 1934 1926 5 -9 13 C ATOM 320 CE2 TYR A 63 30.169 3.467 42.976 1.00 15.32 C ANISOU 320 CE2 TYR A 63 1946 1923 1953 9 -18 25 C ATOM 321 CZ TYR A 63 30.792 2.304 42.579 1.00 15.24 C ANISOU 321 CZ TYR A 63 1904 1958 1928 7 13 -6 C ATOM 322 OH TYR A 63 31.571 1.615 43.485 1.00 15.62 O ANISOU 322 OH TYR A 63 1992 1989 1955 42 21 15 O ATOM 323 N LEU A 64 27.944 5.554 36.839 1.00 13.72 N ANISOU 323 N LEU A 64 1689 1775 1749 20 -8 -12 N ATOM 324 CA LEU A 64 26.870 6.029 35.966 1.00 13.58 C ANISOU 324 CA LEU A 64 1730 1712 1718 -5 -19 0 C ATOM 325 C LEU A 64 25.626 6.373 36.773 1.00 13.22 C ANISOU 325 C LEU A 64 1730 1664 1629 -9 -29 -16 C ATOM 326 O LEU A 64 25.187 5.577 37.603 1.00 13.80 O ANISOU 326 O LEU A 64 1828 1679 1737 -75 11 -12 O ATOM 327 CB LEU A 64 26.501 4.924 34.972 1.00 13.65 C ANISOU 327 CB LEU A 64 1752 1702 1733 -16 5 -5 C ATOM 328 CG LEU A 64 27.470 4.669 33.820 1.00 13.73 C ANISOU 328 CG LEU A 64 1789 1689 1739 24 13 4 C ATOM 329 CD1 LEU A 64 27.241 3.290 33.220 1.00 13.71 C ANISOU 329 CD1 LEU A 64 1775 1711 1724 -24 2 6 C ATOM 330 CD2 LEU A 64 27.318 5.753 32.763 1.00 13.04 C ANISOU 330 CD2 LEU A 64 1680 1686 1588 -10 14 -33 C ATOM 331 N PRO A 65 25.014 7.521 36.506 1.00 13.19 N ANISOU 331 N PRO A 65 1692 1677 1643 -19 -8 -1 N ATOM 332 CA PRO A 65 23.831 7.954 37.223 1.00 13.12 C ANISOU 332 CA PRO A 65 1663 1659 1663 -4 -24 1 C ATOM 333 C PRO A 65 22.557 7.283 36.740 1.00 13.15 C ANISOU 333 C PRO A 65 1667 1662 1667 -5 -16 -7 C ATOM 334 O PRO A 65 21.583 7.226 37.495 1.00 13.46 O ANISOU 334 O PRO A 65 1683 1731 1700 11 -7 -55 O ATOM 335 CB PRO A 65 23.770 9.461 37.002 1.00 13.10 C ANISOU 335 CB PRO A 65 1633 1671 1673 -10 -13 21 C ATOM 336 CG PRO A 65 24.544 9.688 35.751 1.00 13.42 C ANISOU 336 CG PRO A 65 1719 1720 1659 14 1 24 C ATOM 337 CD PRO A 65 25.602 8.621 35.699 1.00 13.24 C ANISOU 337 CD PRO A 65 1715 1665 1650 -1 -6 19 C ATOM 338 N ALA A 66 22.545 6.811 35.497 1.00 12.96 N ANISOU 338 N ALA A 66 1640 1608 1677 -2 -26 -26 N ATOM 339 CA ALA A 66 21.324 6.225 34.933 1.00 12.71 C ANISOU 339 CA ALA A 66 1614 1562 1653 -4 1 -18 C ATOM 340 C ALA A 66 20.144 7.120 35.258 1.00 12.28 C ANISOU 340 C ALA A 66 1568 1568 1529 -12 -24 -5 C ATOM 341 O ALA A 66 20.325 8.346 35.246 1.00 12.23 O ANISOU 341 O ALA A 66 1602 1578 1465 -59 -51 -39 O ATOM 342 CB ALA A 66 21.142 4.812 35.451 1.00 12.05 C ANISOU 342 CB ALA A 66 1522 1560 1495 28 -38 12 C ATOM 343 N SER A 67 18.965 6.627 35.616 1.00 12.27 N ANISOU 343 N SER A 67 1576 1562 1524 -11 -22 -14 N ATOM 344 CA SER A 67 17.781 7.473 35.723 1.00 12.20 C ANISOU 344 CA SER A 67 1625 1535 1478 27 -31 -13 C ATOM 345 C SER A 67 17.817 8.488 36.855 1.00 11.95 C ANISOU 345 C SER A 67 1550 1507 1483 12 -38 -16 C ATOM 346 O SER A 67 16.988 9.409 36.864 1.00 11.99 O ANISOU 346 O SER A 67 1682 1370 1504 -14 -61 -62 O ATOM 347 CB SER A 67 16.516 6.612 35.826 1.00 14.35 C ANISOU 347 CB SER A 67 1758 1842 1852 -95 31 -19 C ATOM 348 OG SER A 67 15.345 7.405 35.731 1.00 15.80 O ANISOU 348 OG SER A 67 1991 2001 2012 51 -93 -12 O ATOM 349 N THR A 68 18.769 8.430 37.789 1.00 11.54 N ANISOU 349 N THR A 68 1519 1427 1438 -38 -11 3 N ATOM 350 CA THR A 68 18.963 9.524 38.735 1.00 11.35 C ANISOU 350 CA THR A 68 1490 1422 1402 -24 -37 8 C ATOM 351 C THR A 68 19.346 10.829 38.052 1.00 11.00 C ANISOU 351 C THR A 68 1394 1413 1373 -13 -25 2 C ATOM 352 O THR A 68 19.111 11.907 38.612 1.00 11.59 O ANISOU 352 O THR A 68 1490 1373 1541 -20 -34 14 O ATOM 353 CB THR A 68 19.993 9.211 39.839 1.00 11.74 C ANISOU 353 CB THR A 68 1448 1532 1482 -14 -55 -17 C ATOM 354 OG1 THR A 68 21.305 9.089 39.291 1.00 12.16 O ANISOU 354 OG1 THR A 68 1519 1668 1433 2 -16 -17 O ATOM 355 CG2 THR A 68 19.627 7.926 40.566 1.00 13.16 C ANISOU 355 CG2 THR A 68 1747 1603 1651 -31 -11 13 C ATOM 356 N PHE A 69 19.899 10.790 36.844 1.00 10.79 N ANISOU 356 N PHE A 69 1363 1384 1353 -23 -52 -1 N ATOM 357 CA PHE A 69 20.176 11.995 36.072 1.00 11.42 C ANISOU 357 CA PHE A 69 1463 1446 1432 -7 -27 37 C ATOM 358 C PHE A 69 18.930 12.701 35.572 1.00 10.99 C ANISOU 358 C PHE A 69 1436 1399 1343 -19 -20 -5 C ATOM 359 O PHE A 69 19.003 13.884 35.212 1.00 10.26 O ANISOU 359 O PHE A 69 1336 1358 1206 3 -29 -51 O ATOM 360 CB PHE A 69 21.134 11.651 34.927 1.00 12.48 C ANISOU 360 CB PHE A 69 1641 1577 1523 -5 55 22 C ATOM 361 CG PHE A 69 21.650 12.867 34.212 1.00 12.47 C ANISOU 361 CG PHE A 69 1629 1578 1532 -44 9 27 C ATOM 362 CD1 PHE A 69 22.714 13.573 34.754 1.00 12.87 C ANISOU 362 CD1 PHE A 69 1609 1686 1593 -14 -29 -28 C ATOM 363 CD2 PHE A 69 21.061 13.316 33.042 1.00 12.37 C ANISOU 363 CD2 PHE A 69 1583 1563 1554 -5 -22 -25 C ATOM 364 CE1 PHE A 69 23.193 14.701 34.123 1.00 13.84 C ANISOU 364 CE1 PHE A 69 1798 1700 1761 -17 8 -12 C ATOM 365 CE2 PHE A 69 21.539 14.451 32.415 1.00 13.31 C ANISOU 365 CE2 PHE A 69 1749 1661 1648 -18 49 21 C ATOM 366 CZ PHE A 69 22.604 15.143 32.957 1.00 14.33 C ANISOU 366 CZ PHE A 69 1782 1857 1806 -5 -39 -34 C ATOM 367 N LYS A 70 17.737 12.102 35.641 1.00 11.44 N ANISOU 367 N LYS A 70 1410 1514 1422 -8 -15 -10 N ATOM 368 CA LYS A 70 16.505 12.834 35.372 1.00 11.09 C ANISOU 368 CA LYS A 70 1407 1409 1398 -15 3 -33 C ATOM 369 C LYS A 70 16.345 14.048 36.281 1.00 11.25 C ANISOU 369 C LYS A 70 1462 1413 1400 8 -17 -36 C ATOM 370 O LYS A 70 15.755 15.036 35.836 1.00 11.95 O ANISOU 370 O LYS A 70 1620 1420 1501 6 -63 -30 O ATOM 371 CB LYS A 70 15.271 11.928 35.443 1.00 10.87 C ANISOU 371 CB LYS A 70 1403 1361 1365 -5 -5 -32 C ATOM 372 CG LYS A 70 15.298 10.847 34.362 1.00 11.19 C ANISOU 372 CG LYS A 70 1464 1397 1391 -27 -10 -41 C ATOM 373 CD LYS A 70 13.945 10.161 34.241 1.00 11.58 C ANISOU 373 CD LYS A 70 1463 1489 1448 -30 -14 -73 C ATOM 374 CE LYS A 70 13.920 9.274 33.002 1.00 11.43 C ANISOU 374 CE LYS A 70 1517 1454 1372 12 -30 -11 C ATOM 375 NZ LYS A 70 14.720 8.030 33.175 1.00 11.91 N ANISOU 375 NZ LYS A 70 1581 1443 1502 -1 -60 -47 N ATOM 376 N ILE A 71 16.882 14.022 37.496 1.00 11.29 N ANISOU 376 N ILE A 71 1506 1404 1380 -3 -15 -39 N ATOM 377 CA ILE A 71 16.804 15.182 38.378 1.00 11.25 C ANISOU 377 CA ILE A 71 1517 1410 1347 1 -18 -27 C ATOM 378 C ILE A 71 17.468 16.417 37.800 1.00 11.47 C ANISOU 378 C ILE A 71 1509 1439 1411 -22 -13 -33 C ATOM 379 O ILE A 71 16.770 17.401 37.535 1.00 12.57 O ANISOU 379 O ILE A 71 1658 1547 1570 43 -59 -11 O ATOM 380 CB ILE A 71 17.301 14.858 39.796 1.00 11.10 C ANISOU 380 CB ILE A 71 1489 1357 1371 -28 -56 -29 C ATOM 381 CG1 ILE A 71 16.543 13.654 40.365 1.00 11.25 C ANISOU 381 CG1 ILE A 71 1500 1387 1387 10 20 -1 C ATOM 382 CG2 ILE A 71 17.086 16.076 40.689 1.00 10.75 C ANISOU 382 CG2 ILE A 71 1424 1356 1304 -36 -8 -16 C ATOM 383 CD1 ILE A 71 17.135 13.120 41.658 1.00 12.74 C ANISOU 383 CD1 ILE A 71 1707 1637 1499 8 -86 9 C ATOM 384 N PRO A 72 18.766 16.409 37.538 1.00 11.28 N ANISOU 384 N PRO A 72 1496 1433 1356 -28 -40 -11 N ATOM 385 CA PRO A 72 19.453 17.523 36.905 1.00 11.61 C ANISOU 385 CA PRO A 72 1511 1473 1428 -27 -26 10 C ATOM 386 C PRO A 72 18.886 17.828 35.527 1.00 11.80 C ANISOU 386 C PRO A 72 1560 1501 1424 -1 -20 -7 C ATOM 387 O PRO A 72 18.670 18.982 35.171 1.00 12.11 O ANISOU 387 O PRO A 72 1584 1513 1503 20 -49 -29 O ATOM 388 CB PRO A 72 20.907 17.092 36.802 1.00 11.92 C ANISOU 388 CB PRO A 72 1545 1475 1507 15 -22 23 C ATOM 389 CG PRO A 72 20.914 15.621 37.042 1.00 11.83 C ANISOU 389 CG PRO A 72 1533 1456 1505 -19 1 0 C ATOM 390 CD PRO A 72 19.717 15.342 37.915 1.00 11.60 C ANISOU 390 CD PRO A 72 1494 1464 1448 -1 -14 1 C ATOM 391 N ASN A 73 18.623 16.782 34.747 1.00 11.70 N ANISOU 391 N ASN A 73 1524 1473 1450 -20 -9 -8 N ATOM 392 CA ASN A 73 18.093 16.953 33.393 1.00 11.74 C ANISOU 392 CA ASN A 73 1526 1482 1451 -14 -21 -19 C ATOM 393 C ASN A 73 16.757 17.678 33.408 1.00 12.13 C ANISOU 393 C ASN A 73 1527 1566 1515 -24 9 -27 C ATOM 394 O ASN A 73 16.528 18.565 32.577 1.00 13.13 O ANISOU 394 O ASN A 73 1705 1665 1621 27 -40 6 O ATOM 395 CB ASN A 73 17.994 15.594 32.700 1.00 12.30 C ANISOU 395 CB ASN A 73 1669 1444 1562 -24 -19 1 C ATOM 396 CG ASN A 73 18.052 15.627 31.190 1.00 13.60 C ANISOU 396 CG ASN A 73 1798 1727 1641 -26 14 66 C ATOM 397 OD1 ASN A 73 17.855 14.584 30.544 1.00 15.04 O ANISOU 397 OD1 ASN A 73 2021 1882 1812 9 -19 -82 O ATOM 398 ND2 ASN A 73 18.324 16.785 30.609 1.00 11.43 N ANISOU 398 ND2 ASN A 73 1588 1539 1215 8 -50 -103 N ATOM 399 N ALA A 74 15.869 17.342 34.343 1.00 11.49 N ANISOU 399 N ALA A 74 1449 1492 1425 -29 -34 -69 N ATOM 400 CA ALA A 74 14.593 18.039 34.457 1.00 11.59 C ANISOU 400 CA ALA A 74 1491 1460 1451 -4 -29 -25 C ATOM 401 C ALA A 74 14.790 19.513 34.801 1.00 11.91 C ANISOU 401 C ALA A 74 1567 1466 1494 10 -22 -15 C ATOM 402 O ALA A 74 14.159 20.388 34.208 1.00 11.75 O ANISOU 402 O ALA A 74 1679 1387 1400 -14 -43 -48 O ATOM 403 CB ALA A 74 13.718 17.372 35.508 1.00 12.11 C ANISOU 403 CB ALA A 74 1528 1570 1503 -11 10 -6 C ATOM 404 N ILE A 75 15.664 19.791 35.767 1.00 12.16 N ANISOU 404 N ILE A 75 1568 1526 1528 -37 -18 8 N ATOM 405 CA ILE A 75 15.934 21.173 36.153 1.00 12.61 C ANISOU 405 CA ILE A 75 1654 1550 1587 -23 -8 -14 C ATOM 406 C ILE A 75 16.484 21.973 34.975 1.00 12.73 C ANISOU 406 C ILE A 75 1652 1597 1587 -25 -6 -9 C ATOM 407 O ILE A 75 16.015 23.083 34.705 1.00 13.75 O ANISOU 407 O ILE A 75 1793 1688 1745 10 -34 58 O ATOM 408 CB ILE A 75 16.898 21.264 37.349 1.00 13.20 C ANISOU 408 CB ILE A 75 1708 1667 1639 -21 -36 16 C ATOM 409 CG1 ILE A 75 16.306 20.522 38.552 1.00 13.34 C ANISOU 409 CG1 ILE A 75 1701 1699 1671 -11 14 10 C ATOM 410 CG2 ILE A 75 17.145 22.727 37.700 1.00 13.99 C ANISOU 410 CG2 ILE A 75 1856 1691 1769 -15 -38 5 C ATOM 411 CD1 ILE A 75 17.289 20.268 39.675 1.00 14.24 C ANISOU 411 CD1 ILE A 75 1807 1833 1770 0 -50 15 C ATOM 412 N ILE A 76 17.461 21.418 34.275 1.00 12.57 N ANISOU 412 N ILE A 76 1581 1586 1610 -36 -22 3 N ATOM 413 CA ILE A 76 18.043 22.049 33.094 1.00 13.20 C ANISOU 413 CA ILE A 76 1709 1681 1627 -23 14 4 C ATOM 414 C ILE A 76 17.020 22.248 31.985 1.00 13.76 C ANISOU 414 C ILE A 76 1772 1747 1709 13 -27 6 C ATOM 415 O ILE A 76 16.976 23.316 31.365 1.00 14.26 O ANISOU 415 O ILE A 76 1900 1812 1705 -14 -18 40 O ATOM 416 CB ILE A 76 19.250 21.238 32.591 1.00 13.42 C ANISOU 416 CB ILE A 76 1749 1662 1686 14 -9 19 C ATOM 417 CG1 ILE A 76 20.338 21.220 33.671 1.00 13.75 C ANISOU 417 CG1 ILE A 76 1690 1778 1759 -24 -6 5 C ATOM 418 CG2 ILE A 76 19.801 21.808 31.291 1.00 13.83 C ANISOU 418 CG2 ILE A 76 1765 1770 1721 -22 37 -9 C ATOM 419 CD1 ILE A 76 21.355 20.107 33.537 1.00 14.14 C ANISOU 419 CD1 ILE A 76 1838 1772 1764 16 14 -5 C ATOM 420 N GLY A 77 16.175 21.262 31.723 1.00 14.04 N ANISOU 420 N GLY A 77 1800 1757 1777 5 -28 2 N ATOM 421 CA GLY A 77 15.095 21.384 30.752 1.00 14.10 C ANISOU 421 CA GLY A 77 1814 1769 1775 -11 -31 6 C ATOM 422 C GLY A 77 14.182 22.565 31.056 1.00 14.63 C ANISOU 422 C GLY A 77 1898 1825 1835 20 -9 -3 C ATOM 423 O GLY A 77 13.836 23.360 30.178 1.00 14.65 O ANISOU 423 O GLY A 77 1928 1849 1788 10 -27 -7 O ATOM 424 N LEU A 78 13.770 22.692 32.313 1.00 14.75 N ANISOU 424 N LEU A 78 1905 1864 1836 -10 3 22 N ATOM 425 CA LEU A 78 13.003 23.846 32.758 1.00 15.11 C ANISOU 425 CA LEU A 78 1942 1930 1867 18 35 -1 C ATOM 426 C LEU A 78 13.799 25.137 32.646 1.00 15.77 C ANISOU 426 C LEU A 78 2057 1980 1955 -22 33 -18 C ATOM 427 O LEU A 78 13.286 26.127 32.117 1.00 16.37 O ANISOU 427 O LEU A 78 2129 2054 2038 4 -7 8 O ATOM 428 CB LEU A 78 12.529 23.632 34.200 1.00 14.86 C ANISOU 428 CB LEU A 78 1904 1873 1868 -25 18 40 C ATOM 429 CG LEU A 78 11.447 22.566 34.377 1.00 13.82 C ANISOU 429 CG LEU A 78 1743 1789 1720 37 -12 -1 C ATOM 430 CD1 LEU A 78 11.373 22.130 35.838 1.00 14.58 C ANISOU 430 CD1 LEU A 78 1923 1870 1746 -11 -13 10 C ATOM 431 CD2 LEU A 78 10.092 23.067 33.908 1.00 13.18 C ANISOU 431 CD2 LEU A 78 1716 1657 1635 1 -22 -27 C ATOM 432 N GLU A 79 15.050 25.139 33.098 1.00 16.54 N ANISOU 432 N GLU A 79 2110 2139 2034 -2 26 -11 N ATOM 433 CA GLU A 79 15.857 26.355 33.073 1.00 17.92 C ANISOU 433 CA GLU A 79 2303 2207 2298 -51 23 -23 C ATOM 434 C GLU A 79 16.039 26.917 31.670 1.00 18.52 C ANISOU 434 C GLU A 79 2390 2304 2343 -19 14 18 C ATOM 435 O GLU A 79 15.935 28.125 31.456 1.00 18.91 O ANISOU 435 O GLU A 79 2456 2321 2407 -23 5 24 O ATOM 436 CB GLU A 79 17.228 26.113 33.710 1.00 20.01 C ANISOU 436 CB GLU A 79 2412 2515 2676 18 -42 22 C ATOM 437 CG GLU A 79 17.243 26.278 35.217 1.00 23.14 C ANISOU 437 CG GLU A 79 2952 2996 2845 -9 -2 -7 C ATOM 438 CD GLU A 79 16.890 27.689 35.651 1.00 24.38 C ANISOU 438 CD GLU A 79 3108 3084 3073 64 -13 -33 C ATOM 439 OE1 GLU A 79 17.703 28.609 35.433 1.00 26.18 O ANISOU 439 OE1 GLU A 79 3326 3309 3311 -73 14 20 O ATOM 440 OE2 GLU A 79 15.795 27.882 36.214 1.00 23.69 O ANISOU 440 OE2 GLU A 79 3069 2950 2982 -3 -16 -35 O ATOM 441 N THR A 80 16.285 26.047 30.698 1.00 18.92 N ANISOU 441 N THR A 80 2434 2394 2360 0 2 -14 N ATOM 442 CA THR A 80 16.536 26.446 29.323 1.00 19.13 C ANISOU 442 CA THR A 80 2464 2406 2400 -4 34 -7 C ATOM 443 C THR A 80 15.273 26.737 28.531 1.00 19.61 C ANISOU 443 C THR A 80 2484 2472 2495 0 11 4 C ATOM 444 O THR A 80 15.351 27.263 27.415 1.00 20.78 O ANISOU 444 O THR A 80 2697 2640 2559 8 6 45 O ATOM 445 CB THR A 80 17.320 25.320 28.607 1.00 18.48 C ANISOU 445 CB THR A 80 2344 2285 2393 -55 4 24 C ATOM 446 OG1 THR A 80 16.545 24.115 28.685 1.00 16.45 O ANISOU 446 OG1 THR A 80 2169 2107 1973 52 -20 5 O ATOM 447 CG2 THR A 80 18.666 25.101 29.277 1.00 18.46 C ANISOU 447 CG2 THR A 80 2360 2337 2318 1 30 1 C ATOM 448 N GLY A 81 14.105 26.349 29.032 1.00 18.88 N ANISOU 448 N GLY A 81 2425 2372 2377 30 -12 -19 N ATOM 449 CA GLY A 81 12.845 26.587 28.343 1.00 18.65 C ANISOU 449 CA GLY A 81 2394 2322 2369 5 6 -19 C ATOM 450 C GLY A 81 12.454 25.429 27.435 1.00 18.27 C ANISOU 450 C GLY A 81 2334 2306 2303 19 15 0 C ATOM 451 O GLY A 81 11.402 25.450 26.790 1.00 18.55 O ANISOU 451 O GLY A 81 2390 2339 2319 8 -23 -11 O ATOM 452 N VAL A 82 13.273 24.384 27.412 1.00 17.70 N ANISOU 452 N VAL A 82 2311 2222 2192 -15 8 11 N ATOM 453 CA VAL A 82 12.947 23.156 26.690 1.00 17.43 C ANISOU 453 CA VAL A 82 2225 2209 2189 1 4 5 C ATOM 454 C VAL A 82 11.660 22.558 27.244 1.00 17.27 C ANISOU 454 C VAL A 82 2213 2194 2155 0 -8 7 C ATOM 455 O VAL A 82 10.764 22.172 26.498 1.00 17.32 O ANISOU 455 O VAL A 82 2266 2210 2104 3 -24 -15 O ATOM 456 CB VAL A 82 14.109 22.152 26.763 1.00 17.43 C ANISOU 456 CB VAL A 82 2190 2220 2211 -7 -12 10 C ATOM 457 CG1 VAL A 82 13.741 20.784 26.214 1.00 17.47 C ANISOU 457 CG1 VAL A 82 2257 2237 2145 -17 -4 1 C ATOM 458 CG2 VAL A 82 15.316 22.703 26.005 1.00 17.21 C ANISOU 458 CG2 VAL A 82 2226 2160 2154 0 13 -3 C ATOM 459 N ILE A 83 11.563 22.476 28.566 1.00 16.89 N ANISOU 459 N ILE A 83 2162 2133 2124 -17 1 2 N ATOM 460 CA ILE A 83 10.322 22.157 29.258 1.00 16.41 C ANISOU 460 CA ILE A 83 2140 2065 2030 12 -20 36 C ATOM 461 C ILE A 83 9.599 23.444 29.644 1.00 16.59 C ANISOU 461 C ILE A 83 2182 2066 2055 0 14 27 C ATOM 462 O ILE A 83 10.157 24.265 30.370 1.00 16.30 O ANISOU 462 O ILE A 83 2133 2012 2048 40 -15 59 O ATOM 463 CB ILE A 83 10.617 21.340 30.533 1.00 15.01 C ANISOU 463 CB ILE A 83 1903 1860 1940 14 46 -20 C ATOM 464 CG1 ILE A 83 11.467 20.112 30.193 1.00 14.02 C ANISOU 464 CG1 ILE A 83 1825 1788 1713 24 -24 48 C ATOM 465 CG2 ILE A 83 9.322 20.921 31.209 1.00 14.17 C ANISOU 465 CG2 ILE A 83 1815 1734 1833 15 -17 -13 C ATOM 466 CD1 ILE A 83 12.005 19.378 31.407 1.00 12.80 C ANISOU 466 CD1 ILE A 83 1621 1644 1600 -6 -3 -18 C ATOM 467 N LYS A 84 8.370 23.628 29.178 1.00 17.53 N ANISOU 467 N LYS A 84 2238 2241 2181 -14 0 2 N ATOM 468 CA LYS A 84 7.683 24.908 29.324 1.00 19.16 C ANISOU 468 CA LYS A 84 2516 2319 2443 36 71 38 C ATOM 469 C LYS A 84 7.390 25.259 30.775 1.00 19.32 C ANISOU 469 C LYS A 84 2494 2405 2442 -2 6 -12 C ATOM 470 O LYS A 84 7.698 26.358 31.247 1.00 19.58 O ANISOU 470 O LYS A 84 2505 2411 2525 7 -8 -5 O ATOM 471 CB LYS A 84 6.378 24.899 28.519 1.00 23.57 C ANISOU 471 CB LYS A 84 2797 3199 2960 -79 -128 13 C ATOM 472 CG LYS A 84 5.672 26.245 28.481 1.00 28.90 C ANISOU 472 CG LYS A 84 3762 3462 3757 81 95 3 C ATOM 473 CD LYS A 84 4.426 26.194 27.609 1.00 32.99 C ANISOU 473 CD LYS A 84 4102 4301 4131 -39 -80 2 C ATOM 474 CE LYS A 84 3.762 27.558 27.513 1.00 35.99 C ANISOU 474 CE LYS A 84 4570 4473 4633 40 -16 32 C ATOM 475 NZ LYS A 84 3.393 28.094 28.851 1.00 37.20 N ANISOU 475 NZ LYS A 84 4725 4698 4712 23 20 -7 N ATOM 476 N ASN A 85 6.755 24.334 31.483 1.00 19.61 N ANISOU 476 N ASN A 85 2527 2467 2457 -39 -11 9 N ATOM 477 CA ASN A 85 6.439 24.522 32.898 1.00 20.15 C ANISOU 477 CA ASN A 85 2637 2534 2485 -71 10 26 C ATOM 478 C ASN A 85 6.102 23.170 33.509 1.00 19.41 C ANISOU 478 C ASN A 85 2506 2456 2414 -22 16 -19 C ATOM 479 O ASN A 85 6.222 22.142 32.834 1.00 19.10 O ANISOU 479 O ASN A 85 2464 2445 2347 -12 24 -10 O ATOM 480 CB ASN A 85 5.312 25.531 33.080 1.00 23.12 C ANISOU 480 CB ASN A 85 3067 2818 2898 165 41 -8 C ATOM 481 CG ASN A 85 3.909 25.007 32.895 1.00 27.19 C ANISOU 481 CG ASN A 85 3403 3425 3501 -140 -117 -15 C ATOM 482 OD1 ASN A 85 3.654 24.041 32.174 1.00 25.42 O ANISOU 482 OD1 ASN A 85 3187 3284 3185 57 -16 69 O ATOM 483 ND2 ASN A 85 2.954 25.637 33.577 1.00 30.75 N ANISOU 483 ND2 ASN A 85 3861 3883 3941 80 52 -35 N ATOM 484 N GLU A 86 5.587 23.145 34.731 1.00 18.72 N ANISOU 484 N GLU A 86 2397 2339 2375 -15 -18 -47 N ATOM 485 CA GLU A 86 5.287 21.930 35.458 1.00 18.71 C ANISOU 485 CA GLU A 86 2325 2377 2406 -31 -16 -13 C ATOM 486 C GLU A 86 4.152 21.115 34.847 1.00 17.92 C ANISOU 486 C GLU A 86 2296 2263 2251 18 -20 -11 C ATOM 487 O GLU A 86 3.992 19.954 35.228 1.00 17.73 O ANISOU 487 O GLU A 86 2255 2288 2194 3 -16 1 O ATOM 488 CB GLU A 86 4.919 22.239 36.926 1.00 20.65 C ANISOU 488 CB GLU A 86 2734 2647 2466 -47 -24 -36 C ATOM 489 CG GLU A 86 3.496 22.712 37.115 1.00 23.55 C ANISOU 489 CG GLU A 86 2889 2954 3105 7 -10 88 C ATOM 490 CD GLU A 86 3.172 23.540 38.330 1.00 26.60 C ANISOU 490 CD GLU A 86 3452 3248 3406 20 -20 -121 C ATOM 491 OE1 GLU A 86 3.258 24.786 38.256 1.00 24.28 O ANISOU 491 OE1 GLU A 86 3115 3132 2977 11 -70 1 O ATOM 492 OE2 GLU A 86 2.796 22.979 39.385 1.00 29.94 O ANISOU 492 OE2 GLU A 86 3880 3815 3680 -28 7 100 O ATOM 493 N HIS A 87 3.334 21.703 33.981 1.00 17.29 N ANISOU 493 N HIS A 87 2220 2177 2174 5 7 -52 N ATOM 494 CA HIS A 87 2.168 21.027 33.444 1.00 17.25 C ANISOU 494 CA HIS A 87 2208 2197 2150 -1 8 -34 C ATOM 495 C HIS A 87 2.340 20.624 31.983 1.00 16.79 C ANISOU 495 C HIS A 87 2157 2097 2125 4 -17 -19 C ATOM 496 O HIS A 87 1.360 20.216 31.357 1.00 16.37 O ANISOU 496 O HIS A 87 2201 1999 2021 17 -21 -37 O ATOM 497 CB HIS A 87 0.923 21.910 33.587 1.00 18.25 C ANISOU 497 CB HIS A 87 2274 2292 2367 42 -12 -35 C ATOM 498 CG HIS A 87 0.614 22.281 35.006 1.00 18.82 C ANISOU 498 CG HIS A 87 2390 2393 2369 0 -18 -39 C ATOM 499 ND1 HIS A 87 0.548 21.359 36.026 1.00 20.03 N ANISOU 499 ND1 HIS A 87 2620 2479 2512 -47 -7 10 N ATOM 500 CD2 HIS A 87 0.349 23.487 35.565 1.00 18.63 C ANISOU 500 CD2 HIS A 87 2328 2400 2350 29 -28 -35 C ATOM 501 CE1 HIS A 87 0.252 21.978 37.155 1.00 19.99 C ANISOU 501 CE1 HIS A 87 2576 2495 2524 -19 -7 2 C ATOM 502 NE2 HIS A 87 0.126 23.268 36.902 1.00 19.25 N ANISOU 502 NE2 HIS A 87 2471 2452 2391 16 -6 -19 N ATOM 503 N GLN A 88 3.558 20.734 31.461 1.00 16.87 N ANISOU 503 N GLN A 88 2195 2092 2121 4 -3 -18 N ATOM 504 CA GLN A 88 3.802 20.257 30.103 1.00 17.25 C ANISOU 504 CA GLN A 88 2318 2114 2123 34 -41 -13 C ATOM 505 C GLN A 88 3.516 18.760 30.007 1.00 16.60 C ANISOU 505 C GLN A 88 2177 2086 2043 16 -39 -11 C ATOM 506 O GLN A 88 3.956 17.975 30.844 1.00 16.39 O ANISOU 506 O GLN A 88 2153 2081 1992 19 -61 -52 O ATOM 507 CB GLN A 88 5.224 20.542 29.627 1.00 21.38 C ANISOU 507 CB GLN A 88 2530 2768 2826 -61 44 65 C ATOM 508 CG GLN A 88 5.471 20.036 28.209 1.00 24.69 C ANISOU 508 CG GLN A 88 3226 3109 3047 55 -2 -87 C ATOM 509 CD GLN A 88 6.740 20.567 27.586 1.00 27.18 C ANISOU 509 CD GLN A 88 3399 3461 3468 -36 24 57 C ATOM 510 OE1 GLN A 88 7.233 21.630 27.953 1.00 27.77 O ANISOU 510 OE1 GLN A 88 3553 3504 3494 -20 -4 -26 O ATOM 511 NE2 GLN A 88 7.281 19.827 26.622 1.00 28.65 N ANISOU 511 NE2 GLN A 88 3661 3621 3602 22 38 -23 N ATOM 512 N VAL A 89 2.772 18.384 28.974 1.00 16.02 N ANISOU 512 N VAL A 89 2090 1974 2022 -18 -13 1 N ATOM 513 CA VAL A 89 2.520 16.974 28.691 1.00 15.58 C ANISOU 513 CA VAL A 89 2017 1948 1955 37 6 1 C ATOM 514 C VAL A 89 3.475 16.504 27.600 1.00 15.28 C ANISOU 514 C VAL A 89 2002 1895 1907 25 -9 3 C ATOM 515 O VAL A 89 3.616 17.145 26.561 1.00 15.58 O ANISOU 515 O VAL A 89 2058 1886 1976 26 30 30 O ATOM 516 CB VAL A 89 1.059 16.733 28.288 1.00 16.53 C ANISOU 516 CB VAL A 89 2060 2103 2118 -26 -14 10 C ATOM 517 CG1 VAL A 89 0.838 15.322 27.761 1.00 17.32 C ANISOU 517 CG1 VAL A 89 2226 2139 2218 -7 -48 -21 C ATOM 518 CG2 VAL A 89 0.137 16.994 29.476 1.00 16.98 C ANISOU 518 CG2 VAL A 89 2192 2121 2140 0 9 -38 C ATOM 519 N PHE A 90 4.154 15.402 27.869 1.00 14.71 N ANISOU 519 N PHE A 90 1912 1849 1828 8 3 -26 N ATOM 520 CA PHE A 90 5.040 14.767 26.900 1.00 14.52 C ANISOU 520 CA PHE A 90 1899 1806 1813 -3 4 3 C ATOM 521 C PHE A 90 4.252 13.685 26.165 1.00 14.57 C ANISOU 521 C PHE A 90 1874 1836 1826 -19 -2 -2 C ATOM 522 O PHE A 90 3.967 12.628 26.723 1.00 14.28 O ANISOU 522 O PHE A 90 1891 1785 1749 1 -54 -35 O ATOM 523 CB PHE A 90 6.260 14.172 27.606 1.00 15.15 C ANISOU 523 CB PHE A 90 1861 1949 1946 25 16 5 C ATOM 524 CG PHE A 90 7.068 15.225 28.317 1.00 16.04 C ANISOU 524 CG PHE A 90 2064 1994 2036 -9 -32 -39 C ATOM 525 CD1 PHE A 90 6.785 15.575 29.626 1.00 16.42 C ANISOU 525 CD1 PHE A 90 2098 2107 2032 24 -15 9 C ATOM 526 CD2 PHE A 90 8.101 15.867 27.654 1.00 16.92 C ANISOU 526 CD2 PHE A 90 2123 2170 2134 -6 22 15 C ATOM 527 CE1 PHE A 90 7.528 16.552 30.264 1.00 17.25 C ANISOU 527 CE1 PHE A 90 2221 2172 2159 -32 -28 -34 C ATOM 528 CE2 PHE A 90 8.848 16.840 28.291 1.00 17.71 C ANISOU 528 CE2 PHE A 90 2277 2206 2247 -50 -5 -12 C ATOM 529 CZ PHE A 90 8.558 17.183 29.596 1.00 17.96 C ANISOU 529 CZ PHE A 90 2276 2275 2274 -18 22 -10 C ATOM 530 N LYS A 91 3.860 13.995 24.935 1.00 15.15 N ANISOU 530 N LYS A 91 1988 1911 1857 -20 -4 4 N ATOM 531 CA LYS A 91 2.916 13.157 24.210 1.00 15.77 C ANISOU 531 CA LYS A 91 2013 1942 2035 -39 42 -95 C ATOM 532 C LYS A 91 3.588 11.927 23.611 1.00 14.91 C ANISOU 532 C LYS A 91 1917 1873 1874 -37 2 -20 C ATOM 533 O LYS A 91 4.710 12.011 23.110 1.00 15.61 O ANISOU 533 O LYS A 91 1975 1985 1970 -7 43 -37 O ATOM 534 CB LYS A 91 2.230 13.962 23.102 1.00 20.22 C ANISOU 534 CB LYS A 91 2620 2673 2391 -24 -173 167 C ATOM 535 CG LYS A 91 1.359 15.097 23.623 1.00 26.85 C ANISOU 535 CG LYS A 91 3413 3207 3581 80 153 -191 C ATOM 536 CD LYS A 91 0.625 15.767 22.470 1.00 33.46 C ANISOU 536 CD LYS A 91 4314 4301 4098 -9 -155 151 C ATOM 537 CE LYS A 91 -0.345 16.826 22.965 1.00 37.85 C ANISOU 537 CE LYS A 91 4779 4707 4895 63 85 -74 C ATOM 538 NZ LYS A 91 -1.081 17.466 21.837 1.00 40.07 N ANISOU 538 NZ LYS A 91 5089 5065 5069 38 -24 37 N ATOM 539 N TRP A 92 2.886 10.802 23.685 1.00 13.55 N ANISOU 539 N TRP A 92 1804 1715 1630 64 -16 -38 N ATOM 540 CA TRP A 92 3.371 9.592 23.022 1.00 13.09 C ANISOU 540 CA TRP A 92 1738 1613 1624 -14 14 8 C ATOM 541 C TRP A 92 2.980 9.643 21.547 1.00 13.86 C ANISOU 541 C TRP A 92 1802 1774 1690 10 -43 -8 C ATOM 542 O TRP A 92 1.836 9.964 21.240 1.00 14.31 O ANISOU 542 O TRP A 92 1823 1904 1709 62 -6 -40 O ATOM 543 CB TRP A 92 2.794 8.346 23.665 1.00 11.19 C ANISOU 543 CB TRP A 92 1462 1491 1298 48 -39 -59 C ATOM 544 CG TRP A 92 3.303 7.040 23.143 1.00 10.94 C ANISOU 544 CG TRP A 92 1384 1447 1327 29 10 6 C ATOM 545 CD1 TRP A 92 4.592 6.730 22.807 1.00 10.28 C ANISOU 545 CD1 TRP A 92 1344 1306 1257 51 -40 7 C ATOM 546 CD2 TRP A 92 2.536 5.851 22.926 1.00 11.87 C ANISOU 546 CD2 TRP A 92 1572 1488 1448 -5 -31 -40 C ATOM 547 NE1 TRP A 92 4.667 5.430 22.381 1.00 9.89 N ANISOU 547 NE1 TRP A 92 1411 1315 1033 24 -79 24 N ATOM 548 CE2 TRP A 92 3.425 4.863 22.455 1.00 11.65 C ANISOU 548 CE2 TRP A 92 1454 1561 1410 3 -15 17 C ATOM 549 CE3 TRP A 92 1.184 5.525 23.082 1.00 12.81 C ANISOU 549 CE3 TRP A 92 1642 1672 1554 -39 15 -20 C ATOM 550 CZ2 TRP A 92 2.997 3.576 22.135 1.00 13.04 C ANISOU 550 CZ2 TRP A 92 1716 1618 1621 -45 1 -13 C ATOM 551 CZ3 TRP A 92 0.763 4.247 22.766 1.00 13.36 C ANISOU 551 CZ3 TRP A 92 1793 1603 1680 15 27 40 C ATOM 552 CH2 TRP A 92 1.672 3.290 22.289 1.00 13.07 C ANISOU 552 CH2 TRP A 92 1676 1751 1538 22 4 -15 C ATOM 553 N ASP A 93 3.913 9.266 20.685 1.00 14.51 N ANISOU 553 N ASP A 93 1862 1882 1767 7 -1 -15 N ATOM 554 CA ASP A 93 3.672 9.246 19.247 1.00 15.00 C ANISOU 554 CA ASP A 93 1954 1931 1816 -4 -27 -5 C ATOM 555 C ASP A 93 3.062 7.939 18.768 1.00 15.23 C ANISOU 555 C ASP A 93 1997 1907 1880 -10 -8 16 C ATOM 556 O ASP A 93 2.833 7.758 17.566 1.00 15.99 O ANISOU 556 O ASP A 93 2164 2008 1904 -14 -18 -18 O ATOM 557 CB ASP A 93 4.984 9.515 18.501 1.00 15.79 C ANISOU 557 CB ASP A 93 2019 2090 1890 -25 -2 2 C ATOM 558 CG ASP A 93 6.103 8.560 18.845 1.00 16.31 C ANISOU 558 CG ASP A 93 2148 2006 2043 11 4 -30 C ATOM 559 OD1 ASP A 93 5.897 7.591 19.604 1.00 15.88 O ANISOU 559 OD1 ASP A 93 2069 2001 1964 36 -21 -23 O ATOM 560 OD2 ASP A 93 7.233 8.771 18.352 1.00 17.51 O ANISOU 560 OD2 ASP A 93 2225 2221 2207 -55 41 -59 O ATOM 561 N GLY A 94 2.830 6.981 19.659 1.00 14.46 N ANISOU 561 N GLY A 94 1891 1823 1779 6 11 -55 N ATOM 562 CA GLY A 94 2.214 5.716 19.303 1.00 13.91 C ANISOU 562 CA GLY A 94 1780 1808 1697 7 11 2 C ATOM 563 C GLY A 94 3.220 4.692 18.795 1.00 13.70 C ANISOU 563 C GLY A 94 1789 1758 1660 2 0 13 C ATOM 564 O GLY A 94 2.813 3.585 18.439 1.00 14.35 O ANISOU 564 O GLY A 94 1934 1818 1701 -41 5 -11 O ATOM 565 N LYS A 95 4.509 4.989 18.860 1.00 13.40 N ANISOU 565 N LYS A 95 1772 1742 1577 26 -14 -15 N ATOM 566 CA LYS A 95 5.545 4.070 18.405 1.00 13.82 C ANISOU 566 CA LYS A 95 1777 1765 1709 39 -10 -12 C ATOM 567 C LYS A 95 6.141 3.311 19.586 1.00 14.26 C ANISOU 567 C LYS A 95 1861 1810 1746 49 -29 2 C ATOM 568 O LYS A 95 6.098 3.770 20.727 1.00 14.25 O ANISOU 568 O LYS A 95 1861 1794 1758 78 -38 -33 O ATOM 569 CB LYS A 95 6.631 4.817 17.631 1.00 14.27 C ANISOU 569 CB LYS A 95 1797 1791 1833 -16 13 -41 C ATOM 570 CG LYS A 95 6.118 5.680 16.486 1.00 16.73 C ANISOU 570 CG LYS A 95 2162 2090 2103 70 39 156 C ATOM 571 CD LYS A 95 5.476 4.845 15.390 1.00 20.66 C ANISOU 571 CD LYS A 95 2629 2600 2621 -138 -15 -204 C ATOM 572 CE LYS A 95 5.037 5.693 14.210 1.00 25.86 C ANISOU 572 CE LYS A 95 3325 3346 3153 -55 -80 144 C ATOM 573 NZ LYS A 95 4.138 6.810 14.599 1.00 30.00 N ANISOU 573 NZ LYS A 95 3813 3704 3882 79 21 -14 N ATOM 574 N PRO A 96 6.694 2.135 19.319 1.00 14.42 N ANISOU 574 N PRO A 96 1883 1815 1781 34 -12 -31 N ATOM 575 CA PRO A 96 7.183 1.249 20.356 1.00 14.35 C ANISOU 575 CA PRO A 96 1854 1804 1796 10 -13 -26 C ATOM 576 C PRO A 96 8.233 1.911 21.233 1.00 14.40 C ANISOU 576 C PRO A 96 1835 1839 1796 -25 -4 4 C ATOM 577 O PRO A 96 9.144 2.582 20.751 1.00 13.86 O ANISOU 577 O PRO A 96 1807 1788 1670 -31 -54 -3 O ATOM 578 CB PRO A 96 7.763 0.053 19.605 1.00 14.57 C ANISOU 578 CB PRO A 96 1878 1823 1836 28 -9 -31 C ATOM 579 CG PRO A 96 7.067 0.063 18.287 1.00 14.70 C ANISOU 579 CG PRO A 96 1906 1851 1831 8 -11 -23 C ATOM 580 CD PRO A 96 6.759 1.500 17.976 1.00 14.59 C ANISOU 580 CD PRO A 96 1913 1844 1787 8 -4 -29 C ATOM 581 N ARG A 97 8.076 1.732 22.542 1.00 14.32 N ANISOU 581 N ARG A 97 1835 1823 1784 -20 -1 -18 N ATOM 582 CA ARG A 97 9.115 2.106 23.495 1.00 14.52 C ANISOU 582 CA ARG A 97 1858 1854 1805 14 -19 -17 C ATOM 583 C ARG A 97 9.592 0.854 24.219 1.00 14.98 C ANISOU 583 C ARG A 97 1927 1874 1891 21 -15 4 C ATOM 584 O ARG A 97 8.928 -0.182 24.194 1.00 15.20 O ANISOU 584 O ARG A 97 1951 1911 1914 8 -61 -5 O ATOM 585 CB ARG A 97 8.601 3.158 24.478 1.00 14.52 C ANISOU 585 CB ARG A 97 1839 1831 1845 -2 -2 -27 C ATOM 586 CG ARG A 97 8.433 4.521 23.820 1.00 15.57 C ANISOU 586 CG ARG A 97 2076 1930 1910 7 -48 28 C ATOM 587 CD ARG A 97 7.853 5.544 24.787 1.00 16.77 C ANISOU 587 CD ARG A 97 2140 2051 2180 64 17 -43 C ATOM 588 NE ARG A 97 7.926 6.885 24.213 1.00 17.06 N ANISOU 588 NE ARG A 97 2219 2131 2131 0 -23 26 N ATOM 589 CZ ARG A 97 7.534 7.995 24.828 1.00 17.23 C ANISOU 589 CZ ARG A 97 2226 2149 2171 -7 10 4 C ATOM 590 NH1 ARG A 97 7.033 7.946 26.053 1.00 16.76 N ANISOU 590 NH1 ARG A 97 2168 2038 2163 -50 15 -19 N ATOM 591 NH2 ARG A 97 7.647 9.164 24.210 1.00 17.26 N ANISOU 591 NH2 ARG A 97 2287 2140 2132 4 18 -5 N ATOM 592 N ALA A 98 10.728 0.957 24.899 1.00 15.29 N ANISOU 592 N ALA A 98 1966 1917 1924 15 -33 -25 N ATOM 593 CA ALA A 98 11.369 -0.221 25.477 1.00 15.56 C ANISOU 593 CA ALA A 98 1997 1964 1953 22 -42 -5 C ATOM 594 C ALA A 98 10.547 -0.813 26.610 1.00 16.09 C ANISOU 594 C ALA A 98 2079 2027 2009 7 15 -12 C ATOM 595 O ALA A 98 10.577 -2.024 26.853 1.00 16.89 O ANISOU 595 O ALA A 98 2234 2059 2125 19 31 -13 O ATOM 596 CB ALA A 98 12.770 0.148 25.939 1.00 15.56 C ANISOU 596 CB ALA A 98 1943 1962 2006 7 29 -8 C ATOM 597 N MET A 99 9.835 0.030 27.354 1.00 15.82 N ANISOU 597 N MET A 99 2008 1997 2005 1 -12 -2 N ATOM 598 CA MET A 99 8.933 -0.409 28.404 1.00 15.94 C ANISOU 598 CA MET A 99 2025 1989 2043 9 -1 38 C ATOM 599 C MET A 99 7.493 -0.045 28.062 1.00 15.60 C ANISOU 599 C MET A 99 1998 1953 1974 11 24 -2 C ATOM 600 O MET A 99 7.201 1.072 27.634 1.00 15.25 O ANISOU 600 O MET A 99 1934 1897 1965 16 25 -51 O ATOM 601 CB AMET A 99 9.309 0.239 29.742 0.50 17.30 C ANISOU 601 CB AMET A 99 2253 2182 2140 3 -16 -32 C ATOM 602 CB BMET A 99 9.313 0.191 29.758 0.50 18.20 C ANISOU 602 CB BMET A 99 2434 2312 2171 -14 -18 -65 C ATOM 603 CG AMET A 99 10.754 0.030 30.160 0.50 18.63 C ANISOU 603 CG AMET A 99 2314 2405 2361 -1 -5 -7 C ATOM 604 CG BMET A 99 10.714 -0.172 30.222 0.50 20.81 C ANISOU 604 CG BMET A 99 2556 2633 2718 32 -13 11 C ATOM 605 SD AMET A 99 11.158 -1.707 30.417 0.50 20.09 S ANISOU 605 SD AMET A 99 2611 2474 2549 -7 -40 23 S ATOM 606 SD BMET A 99 10.976 0.165 31.970 0.50 23.18 S ANISOU 606 SD BMET A 99 3060 2911 2835 -7 -41 -25 S ATOM 607 CE AMET A 99 10.338 -2.026 31.976 0.50 20.44 C ANISOU 607 CE AMET A 99 2608 2544 2615 10 13 -1 C ATOM 608 CE BMET A 99 10.013 -1.142 32.727 0.50 23.82 C ANISOU 608 CE BMET A 99 3023 3020 3007 -11 8 -1 C ATOM 609 N LYS A 100 6.567 -0.967 28.298 1.00 15.87 N ANISOU 609 N LYS A 100 2057 1986 1988 -14 16 -24 N ATOM 610 CA LYS A 100 5.143 -0.744 28.102 1.00 16.75 C ANISOU 610 CA LYS A 100 2132 2147 2085 105 -1 -57 C ATOM 611 C LYS A 100 4.610 0.414 28.937 1.00 15.90 C ANISOU 611 C LYS A 100 2033 2023 1985 33 -10 -10 C ATOM 612 O LYS A 100 3.740 1.174 28.507 1.00 14.98 O ANISOU 612 O LYS A 100 1969 1926 1797 -4 3 -51 O ATOM 613 CB LYS A 100 4.367 -2.018 28.458 1.00 21.89 C ANISOU 613 CB LYS A 100 2977 2482 2858 -155 83 83 C ATOM 614 CG LYS A 100 2.860 -1.924 28.320 1.00 28.21 C ANISOU 614 CG LYS A 100 3348 3558 3812 19 48 4 C ATOM 615 CD LYS A 100 2.404 -1.972 26.871 1.00 33.20 C ANISOU 615 CD LYS A 100 4346 4213 4057 34 -43 -5 C ATOM 616 CE LYS A 100 0.928 -2.329 26.778 1.00 36.17 C ANISOU 616 CE LYS A 100 4518 4558 4668 -17 8 -2 C ATOM 617 NZ LYS A 100 0.513 -2.622 25.377 1.00 37.24 N ANISOU 617 NZ LYS A 100 4733 4698 4717 -6 -6 6 N ATOM 618 N GLN A 101 5.171 0.606 30.128 1.00 15.82 N ANISOU 618 N GLN A 101 2063 1940 2008 15 -4 19 N ATOM 619 CA GLN A 101 4.772 1.673 31.032 1.00 16.45 C ANISOU 619 CA GLN A 101 2141 1995 2115 -16 64 -30 C ATOM 620 C GLN A 101 5.117 3.062 30.521 1.00 15.59 C ANISOU 620 C GLN A 101 2012 1970 1941 6 29 -16 C ATOM 621 O GLN A 101 4.570 4.051 31.014 1.00 15.76 O ANISOU 621 O GLN A 101 2080 1987 1923 40 2 -13 O ATOM 622 CB GLN A 101 5.399 1.423 32.414 1.00 20.46 C ANISOU 622 CB GLN A 101 2583 2803 2389 92 -109 -21 C ATOM 623 CG GLN A 101 4.939 0.097 33.009 1.00 25.70 C ANISOU 623 CG GLN A 101 3320 3085 3359 -59 77 41 C ATOM 624 CD GLN A 101 5.689 -0.292 34.262 1.00 28.36 C ANISOU 624 CD GLN A 101 3656 3581 3536 -15 -48 56 C ATOM 625 OE1 GLN A 101 6.723 -0.959 34.207 1.00 29.45 O ANISOU 625 OE1 GLN A 101 3727 3751 3713 26 22 5 O ATOM 626 NE2 GLN A 101 5.170 0.116 35.413 1.00 28.71 N ANISOU 626 NE2 GLN A 101 3661 3612 3634 22 12 12 N ATOM 627 N TRP A 102 6.000 3.179 29.535 1.00 14.84 N ANISOU 627 N TRP A 102 1896 1853 1888 -39 -21 9 N ATOM 628 CA TRP A 102 6.308 4.434 28.888 1.00 13.84 C ANISOU 628 CA TRP A 102 1771 1774 1715 10 -33 -25 C ATOM 629 C TRP A 102 5.421 4.714 27.680 1.00 13.29 C ANISOU 629 C TRP A 102 1695 1657 1697 -4 -3 -20 C ATOM 630 O TRP A 102 5.521 5.805 27.117 1.00 12.96 O ANISOU 630 O TRP A 102 1697 1618 1610 47 -58 -35 O ATOM 631 CB TRP A 102 7.762 4.477 28.415 1.00 13.98 C ANISOU 631 CB TRP A 102 1798 1753 1760 28 7 -33 C ATOM 632 CG TRP A 102 8.803 4.180 29.448 1.00 14.76 C ANISOU 632 CG TRP A 102 1817 1904 1887 34 -26 16 C ATOM 633 CD1 TRP A 102 8.690 4.261 30.807 1.00 15.41 C ANISOU 633 CD1 TRP A 102 1965 1957 1935 11 -10 -20 C ATOM 634 CD2 TRP A 102 10.154 3.778 29.184 1.00 13.95 C ANISOU 634 CD2 TRP A 102 1800 1754 1745 22 11 -3 C ATOM 635 NE1 TRP A 102 9.875 3.914 31.402 1.00 15.43 N ANISOU 635 NE1 TRP A 102 1997 2006 1860 51 -3 -2 N ATOM 636 CE2 TRP A 102 10.794 3.615 30.430 1.00 14.88 C ANISOU 636 CE2 TRP A 102 1924 1925 1804 49 -38 0 C ATOM 637 CE3 TRP A 102 10.884 3.532 28.016 1.00 13.42 C ANISOU 637 CE3 TRP A 102 1750 1669 1680 -17 -31 -18 C ATOM 638 CZ2 TRP A 102 12.125 3.222 30.534 1.00 14.67 C ANISOU 638 CZ2 TRP A 102 1877 1880 1816 -16 -48 -1 C ATOM 639 CZ3 TRP A 102 12.204 3.139 28.122 1.00 14.53 C ANISOU 639 CZ3 TRP A 102 1830 1819 1872 34 -4 -33 C ATOM 640 CH2 TRP A 102 12.815 2.989 29.377 1.00 15.54 C ANISOU 640 CH2 TRP A 102 2009 2001 1896 41 -13 -22 C ATOM 641 N GLU A 103 4.597 3.755 27.265 1.00 12.86 N ANISOU 641 N GLU A 103 1646 1653 1588 5 -7 -13 N ATOM 642 CA GLU A 103 3.789 3.946 26.065 1.00 12.58 C ANISOU 642 CA GLU A 103 1609 1579 1593 9 -6 -16 C ATOM 643 C GLU A 103 2.472 4.643 26.352 1.00 12.42 C ANISOU 643 C GLU A 103 1606 1575 1540 7 0 -30 C ATOM 644 O GLU A 103 1.383 4.074 26.295 1.00 12.79 O ANISOU 644 O GLU A 103 1664 1660 1534 -30 -5 -62 O ATOM 645 CB GLU A 103 3.575 2.593 25.370 1.00 12.77 C ANISOU 645 CB GLU A 103 1691 1590 1571 53 -38 -36 C ATOM 646 CG GLU A 103 4.889 2.078 24.798 1.00 13.40 C ANISOU 646 CG GLU A 103 1696 1728 1668 14 35 26 C ATOM 647 CD GLU A 103 4.773 0.733 24.111 1.00 14.98 C ANISOU 647 CD GLU A 103 1989 1872 1831 13 -23 -82 C ATOM 648 OE1 GLU A 103 3.786 0.006 24.332 1.00 16.65 O ANISOU 648 OE1 GLU A 103 2181 1963 2182 -58 37 -61 O ATOM 649 OE2 GLU A 103 5.705 0.405 23.345 1.00 15.66 O ANISOU 649 OE2 GLU A 103 1984 2067 1900 44 -20 -54 O ATOM 650 N ARG A 104 2.564 5.938 26.642 1.00 12.18 N ANISOU 650 N ARG A 104 1593 1545 1491 31 -28 21 N ATOM 651 CA ARG A 104 1.441 6.781 27.009 1.00 12.37 C ANISOU 651 CA ARG A 104 1573 1532 1593 15 -59 -38 C ATOM 652 C ARG A 104 1.895 8.230 27.178 1.00 11.71 C ANISOU 652 C ARG A 104 1498 1507 1445 16 -30 -13 C ATOM 653 O ARG A 104 3.091 8.478 27.323 1.00 11.41 O ANISOU 653 O ARG A 104 1514 1471 1349 -31 -32 -40 O ATOM 654 CB ARG A 104 0.822 6.295 28.326 1.00 15.85 C ANISOU 654 CB ARG A 104 2127 1971 1924 -58 200 53 C ATOM 655 CG ARG A 104 1.838 6.239 29.464 1.00 20.24 C ANISOU 655 CG ARG A 104 2515 2622 2555 28 -185 -35 C ATOM 656 CD ARG A 104 1.205 5.757 30.751 1.00 24.34 C ANISOU 656 CD ARG A 104 3139 3201 2909 39 64 59 C ATOM 657 NE ARG A 104 0.462 4.512 30.605 1.00 27.47 N ANISOU 657 NE ARG A 104 3564 3353 3520 -40 -80 -27 N ATOM 658 CZ ARG A 104 -0.450 4.091 31.476 1.00 30.22 C ANISOU 658 CZ ARG A 104 3803 3889 3791 1 73 45 C ATOM 659 NH1 ARG A 104 -0.737 4.811 32.555 1.00 30.25 N ANISOU 659 NH1 ARG A 104 3839 3790 3864 8 7 -17 N ATOM 660 NH2 ARG A 104 -1.081 2.944 31.268 1.00 31.92 N ANISOU 660 NH2 ARG A 104 4069 3987 4072 -50 -10 -34 N ATOM 661 N ASP A 105 0.956 9.165 27.109 1.00 11.65 N ANISOU 661 N ASP A 105 1553 1444 1429 18 -38 -19 N ATOM 662 CA ASP A 105 1.263 10.554 27.437 1.00 11.87 C ANISOU 662 CA ASP A 105 1568 1485 1456 -20 -26 -34 C ATOM 663 C ASP A 105 1.703 10.625 28.896 1.00 11.65 C ANISOU 663 C ASP A 105 1520 1469 1437 -3 -18 -11 C ATOM 664 O ASP A 105 1.114 9.935 29.731 1.00 11.76 O ANISOU 664 O ASP A 105 1559 1533 1375 -11 -5 -62 O ATOM 665 CB ASP A 105 0.052 11.451 27.213 1.00 13.27 C ANISOU 665 CB ASP A 105 1658 1656 1729 73 15 -56 C ATOM 666 CG ASP A 105 -0.369 11.545 25.760 1.00 15.38 C ANISOU 666 CG ASP A 105 2001 2018 1823 18 -24 -26 C ATOM 667 OD1 ASP A 105 0.336 11.002 24.885 1.00 14.68 O ANISOU 667 OD1 ASP A 105 1837 1922 1819 38 -58 10 O ATOM 668 OD2 ASP A 105 -1.414 12.181 25.497 1.00 16.77 O ANISOU 668 OD2 ASP A 105 2074 2241 2059 96 -21 -47 O ATOM 669 N LEU A 106 2.705 11.443 29.174 1.00 11.50 N ANISOU 669 N LEU A 106 1528 1456 1388 4 -9 -20 N ATOM 670 CA LEU A 106 3.240 11.576 30.521 1.00 11.41 C ANISOU 670 CA LEU A 106 1503 1412 1420 31 -36 -13 C ATOM 671 C LEU A 106 3.403 13.047 30.901 1.00 11.39 C ANISOU 671 C LEU A 106 1501 1417 1411 -6 4 -11 C ATOM 672 O LEU A 106 3.785 13.882 30.081 1.00 10.84 O ANISOU 672 O LEU A 106 1438 1310 1369 11 -52 -40 O ATOM 673 CB LEU A 106 4.599 10.888 30.642 1.00 11.15 C ANISOU 673 CB LEU A 106 1419 1387 1430 -34 -12 -3 C ATOM 674 CG LEU A 106 4.646 9.366 30.535 1.00 10.94 C ANISOU 674 CG LEU A 106 1440 1368 1350 -28 -6 9 C ATOM 675 CD1 LEU A 106 6.058 8.893 30.232 1.00 12.29 C ANISOU 675 CD1 LEU A 106 1518 1570 1580 4 3 -31 C ATOM 676 CD2 LEU A 106 4.109 8.709 31.804 1.00 10.92 C ANISOU 676 CD2 LEU A 106 1459 1408 1283 -16 -23 -27 C ATOM 677 N THR A 107 3.108 13.360 32.163 1.00 11.50 N ANISOU 677 N THR A 107 1544 1434 1392 7 -14 7 N ATOM 678 CA THR A 107 3.517 14.659 32.698 1.00 11.59 C ANISOU 678 CA THR A 107 1492 1472 1439 1 -14 -25 C ATOM 679 C THR A 107 5.004 14.628 33.030 1.00 11.51 C ANISOU 679 C THR A 107 1488 1443 1441 5 -25 -24 C ATOM 680 O THR A 107 5.653 13.582 32.944 1.00 11.32 O ANISOU 680 O THR A 107 1528 1445 1327 13 -30 -84 O ATOM 681 CB THR A 107 2.720 15.007 33.965 1.00 11.25 C ANISOU 681 CB THR A 107 1362 1452 1462 -14 12 18 C ATOM 682 OG1 THR A 107 3.038 14.030 34.966 1.00 11.97 O ANISOU 682 OG1 THR A 107 1558 1574 1418 75 -19 4 O ATOM 683 CG2 THR A 107 1.226 14.988 33.687 1.00 9.93 C ANISOU 683 CG2 THR A 107 1319 1314 1139 -1 -12 -40 C ATOM 684 N LEU A 108 5.547 15.771 33.448 1.00 11.07 N ANISOU 684 N LEU A 108 1408 1439 1359 20 -31 -26 N ATOM 685 CA LEU A 108 6.939 15.806 33.890 1.00 10.82 C ANISOU 685 CA LEU A 108 1387 1381 1343 12 0 -24 C ATOM 686 C LEU A 108 7.122 14.869 35.078 1.00 10.92 C ANISOU 686 C LEU A 108 1413 1391 1345 -1 -11 -16 C ATOM 687 O LEU A 108 8.024 14.029 35.062 1.00 11.10 O ANISOU 687 O LEU A 108 1444 1449 1324 32 13 -75 O ATOM 688 CB LEU A 108 7.392 17.216 34.242 1.00 11.73 C ANISOU 688 CB LEU A 108 1617 1394 1445 -9 -8 -34 C ATOM 689 CG LEU A 108 8.824 17.358 34.767 1.00 13.39 C ANISOU 689 CG LEU A 108 1648 1730 1709 16 -10 2 C ATOM 690 CD1 LEU A 108 9.845 16.867 33.755 1.00 13.38 C ANISOU 690 CD1 LEU A 108 1707 1728 1648 -16 10 16 C ATOM 691 CD2 LEU A 108 9.101 18.807 35.153 1.00 14.89 C ANISOU 691 CD2 LEU A 108 1979 1811 1869 -34 3 -23 C ATOM 692 N ARG A 109 6.255 14.986 36.089 1.00 10.90 N ANISOU 692 N ARG A 109 1421 1353 1367 -2 -1 -21 N ATOM 693 CA ARG A 109 6.339 14.056 37.214 1.00 11.10 C ANISOU 693 CA ARG A 109 1464 1369 1386 6 -6 -1 C ATOM 694 C ARG A 109 6.192 12.612 36.747 1.00 11.07 C ANISOU 694 C ARG A 109 1421 1381 1405 -1 -20 -12 C ATOM 695 O ARG A 109 6.990 11.755 37.138 1.00 11.22 O ANISOU 695 O ARG A 109 1454 1379 1431 23 -32 -37 O ATOM 696 CB AARG A 109 5.318 14.380 38.309 0.50 11.86 C ANISOU 696 CB AARG A 109 1478 1515 1512 12 30 -26 C ATOM 697 CB BARG A 109 5.278 14.380 38.271 0.50 11.58 C ANISOU 697 CB BARG A 109 1463 1457 1482 10 16 -4 C ATOM 698 CG AARG A 109 5.360 13.369 39.443 0.50 13.11 C ANISOU 698 CG AARG A 109 1692 1628 1661 0 -25 55 C ATOM 699 CG BARG A 109 5.318 13.442 39.466 0.50 12.15 C ANISOU 699 CG BARG A 109 1576 1535 1507 7 -3 15 C ATOM 700 CD AARG A 109 4.762 13.889 40.743 0.50 14.55 C ANISOU 700 CD AARG A 109 1839 1874 1815 5 24 -58 C ATOM 701 CD BARG A 109 4.075 13.566 40.340 0.50 12.42 C ANISOU 701 CD BARG A 109 1568 1551 1598 -2 7 -5 C ATOM 702 NE AARG A 109 4.925 12.880 41.793 0.50 15.90 N ANISOU 702 NE AARG A 109 2054 2006 1981 18 3 25 N ATOM 703 NE BARG A 109 3.915 12.368 41.157 0.50 12.40 N ANISOU 703 NE BARG A 109 1566 1597 1550 -15 -7 15 N ATOM 704 CZ AARG A 109 4.175 11.790 41.907 0.50 16.48 C ANISOU 704 CZ AARG A 109 2108 2071 2083 -30 7 9 C ATOM 705 CZ BARG A 109 4.565 12.092 42.281 0.50 12.07 C ANISOU 705 CZ BARG A 109 1516 1535 1534 -48 -13 -12 C ATOM 706 NH1AARG A 109 3.183 11.564 41.056 0.50 16.69 N ANISOU 706 NH1AARG A 109 2118 2129 2092 0 -9 4 N ATOM 707 NH1BARG A 109 5.432 12.951 42.795 0.50 11.01 N ANISOU 707 NH1BARG A 109 1398 1417 1369 29 14 20 N ATOM 708 NH2AARG A 109 4.403 10.919 42.881 0.50 16.47 N ANISOU 708 NH2AARG A 109 2129 2060 2070 -2 -16 -8 N ATOM 709 NH2BARG A 109 4.319 10.943 42.901 0.50 12.48 N ANISOU 709 NH2BARG A 109 1651 1551 1540 -2 -29 10 N ATOM 710 N GLY A 110 5.201 12.331 35.905 1.00 11.00 N ANISOU 710 N GLY A 110 1417 1392 1372 -8 9 -41 N ATOM 711 CA GLY A 110 4.974 10.970 35.430 1.00 11.02 C ANISOU 711 CA GLY A 110 1432 1386 1369 -5 4 -29 C ATOM 712 C GLY A 110 6.213 10.399 34.751 1.00 10.87 C ANISOU 712 C GLY A 110 1402 1390 1338 -19 0 1 C ATOM 713 O GLY A 110 6.644 9.284 35.048 1.00 11.44 O ANISOU 713 O GLY A 110 1499 1447 1402 17 -29 12 O ATOM 714 N ALA A 111 6.807 11.159 33.834 1.00 10.35 N ANISOU 714 N ALA A 111 1352 1326 1254 -14 -36 -29 N ATOM 715 CA ALA A 111 8.003 10.732 33.125 1.00 10.41 C ANISOU 715 CA ALA A 111 1358 1334 1264 -17 -27 -11 C ATOM 716 C ALA A 111 9.174 10.442 34.056 1.00 10.76 C ANISOU 716 C ALA A 111 1403 1355 1331 21 -51 -15 C ATOM 717 O ALA A 111 9.926 9.497 33.838 1.00 10.96 O ANISOU 717 O ALA A 111 1440 1407 1317 51 -90 -61 O ATOM 718 CB ALA A 111 8.385 11.790 32.097 1.00 10.67 C ANISOU 718 CB ALA A 111 1413 1334 1308 -38 2 -2 C ATOM 719 N ILE A 112 9.362 11.254 35.093 1.00 10.96 N ANISOU 719 N ILE A 112 1480 1347 1337 18 -56 -21 N ATOM 720 CA ILE A 112 10.379 10.986 36.105 1.00 10.63 C ANISOU 720 CA ILE A 112 1432 1293 1316 -6 -35 -44 C ATOM 721 C ILE A 112 10.046 9.731 36.897 1.00 10.80 C ANISOU 721 C ILE A 112 1414 1333 1356 -7 -16 -23 C ATOM 722 O ILE A 112 10.887 8.840 37.032 1.00 10.94 O ANISOU 722 O ILE A 112 1377 1381 1400 3 -49 -19 O ATOM 723 CB ILE A 112 10.525 12.203 37.037 1.00 9.64 C ANISOU 723 CB ILE A 112 1242 1223 1199 7 -6 8 C ATOM 724 CG1 ILE A 112 11.079 13.387 36.232 1.00 9.97 C ANISOU 724 CG1 ILE A 112 1340 1222 1225 -23 -9 -2 C ATOM 725 CG2 ILE A 112 11.424 11.911 38.227 1.00 10.21 C ANISOU 725 CG2 ILE A 112 1327 1330 1223 29 -33 21 C ATOM 726 CD1 ILE A 112 11.062 14.695 36.999 1.00 10.82 C ANISOU 726 CD1 ILE A 112 1437 1291 1384 -31 -8 -80 C ATOM 727 N GLN A 113 8.817 9.639 37.395 1.00 10.99 N ANISOU 727 N GLN A 113 1437 1412 1329 -17 -13 -56 N ATOM 728 CA GLN A 113 8.411 8.553 38.278 1.00 11.96 C ANISOU 728 CA GLN A 113 1593 1462 1491 -18 -40 20 C ATOM 729 C GLN A 113 8.398 7.188 37.599 1.00 12.38 C ANISOU 729 C GLN A 113 1653 1510 1542 5 -12 -30 C ATOM 730 O GLN A 113 8.677 6.189 38.275 1.00 12.55 O ANISOU 730 O GLN A 113 1755 1476 1536 48 -43 -87 O ATOM 731 CB AGLN A 113 7.020 8.839 38.855 0.50 15.76 C ANISOU 731 CB AGLN A 113 1759 2123 2106 33 100 114 C ATOM 732 CB BGLN A 113 7.029 8.851 38.868 0.50 12.22 C ANISOU 732 CB BGLN A 113 1679 1485 1479 -35 -21 -2 C ATOM 733 CG AGLN A 113 7.001 9.879 39.960 0.50 20.72 C ANISOU 733 CG AGLN A 113 2700 2502 2670 -13 47 -185 C ATOM 734 CG BGLN A 113 6.975 10.072 39.767 0.50 12.04 C ANISOU 734 CG BGLN A 113 1582 1485 1507 -14 -5 -8 C ATOM 735 CD AGLN A 113 7.397 9.306 41.306 0.50 25.02 C ANISOU 735 CD AGLN A 113 3283 3197 3028 68 -8 64 C ATOM 736 CD BGLN A 113 7.312 9.789 41.213 0.50 12.18 C ANISOU 736 CD BGLN A 113 1597 1523 1507 -24 -46 -58 C ATOM 737 OE1AGLN A 113 6.902 8.255 41.716 0.50 25.98 O ANISOU 737 OE1AGLN A 113 3343 3241 3287 -10 5 16 O ATOM 738 OE1BGLN A 113 7.171 8.668 41.706 0.50 13.72 O ANISOU 738 OE1BGLN A 113 1915 1630 1668 -22 -12 -3 O ATOM 739 NE2AGLN A 113 8.288 10.004 42.001 0.50 26.57 N ANISOU 739 NE2AGLN A 113 3345 3377 3374 -27 -36 -6 N ATOM 740 NE2BGLN A 113 7.759 10.822 41.924 0.50 11.08 N ANISOU 740 NE2BGLN A 113 1431 1384 1394 62 -22 8 N ATOM 741 N VAL A 114 8.058 7.121 36.312 1.00 12.66 N ANISOU 741 N VAL A 114 1644 1599 1566 39 -12 -6 N ATOM 742 CA VAL A 114 8.125 5.840 35.603 1.00 12.89 C ANISOU 742 CA VAL A 114 1630 1646 1622 9 -22 -52 C ATOM 743 C VAL A 114 9.459 5.663 34.891 1.00 12.46 C ANISOU 743 C VAL A 114 1611 1580 1543 -14 -27 -18 C ATOM 744 O VAL A 114 9.699 4.675 34.187 1.00 12.70 O ANISOU 744 O VAL A 114 1655 1533 1639 -40 -49 -40 O ATOM 745 CB VAL A 114 6.955 5.636 34.624 1.00 13.06 C ANISOU 745 CB VAL A 114 1605 1667 1689 -4 -30 -5 C ATOM 746 CG1 VAL A 114 5.617 5.787 35.338 1.00 12.91 C ANISOU 746 CG1 VAL A 114 1629 1751 1527 19 -50 -12 C ATOM 747 CG2 VAL A 114 7.031 6.581 33.438 1.00 13.84 C ANISOU 747 CG2 VAL A 114 1804 1758 1695 -2 -21 2 C ATOM 748 N SER A 115 10.375 6.607 35.058 1.00 12.09 N ANISOU 748 N SER A 115 1577 1514 1503 18 -8 -1 N ATOM 749 CA SER A 115 11.706 6.601 34.489 1.00 12.20 C ANISOU 749 CA SER A 115 1572 1587 1475 -5 -12 -33 C ATOM 750 C SER A 115 11.687 6.457 32.971 1.00 11.78 C ANISOU 750 C SER A 115 1505 1515 1457 16 -24 -36 C ATOM 751 O SER A 115 12.451 5.682 32.397 1.00 11.54 O ANISOU 751 O SER A 115 1477 1529 1377 -6 -63 -59 O ATOM 752 CB SER A 115 12.574 5.508 35.118 1.00 14.21 C ANISOU 752 CB SER A 115 1850 1724 1826 111 -44 22 C ATOM 753 OG SER A 115 12.631 5.652 36.526 1.00 15.99 O ANISOU 753 OG SER A 115 2119 2044 1912 1 55 -43 O ATOM 754 N ALA A 116 10.873 7.283 32.323 1.00 11.80 N ANISOU 754 N ALA A 116 1564 1513 1408 -1 -33 0 N ATOM 755 CA ALA A 116 10.703 7.230 30.873 1.00 11.67 C ANISOU 755 CA ALA A 116 1489 1528 1418 21 -24 -12 C ATOM 756 C ALA A 116 11.880 7.847 30.138 1.00 11.65 C ANISOU 756 C ALA A 116 1514 1462 1452 8 -13 -12 C ATOM 757 O ALA A 116 11.925 9.008 29.728 1.00 11.64 O ANISOU 757 O ALA A 116 1488 1461 1473 24 2 -20 O ATOM 758 CB ALA A 116 9.393 7.915 30.500 1.00 11.44 C ANISOU 758 CB ALA A 116 1504 1456 1386 36 -54 -71 C ATOM 759 N VAL A 117 12.868 6.999 29.857 1.00 11.72 N ANISOU 759 N VAL A 117 1510 1467 1475 -1 -19 -26 N ATOM 760 CA VAL A 117 14.103 7.342 29.181 1.00 12.25 C ANISOU 760 CA VAL A 117 1560 1571 1523 -30 -7 -10 C ATOM 761 C VAL A 117 13.931 8.163 27.921 1.00 12.77 C ANISOU 761 C VAL A 117 1658 1623 1571 -15 0 18 C ATOM 762 O VAL A 117 14.587 9.196 27.763 1.00 12.33 O ANISOU 762 O VAL A 117 1562 1626 1498 -30 -56 -64 O ATOM 763 CB VAL A 117 14.941 6.075 28.905 1.00 13.43 C ANISOU 763 CB VAL A 117 1751 1646 1704 35 1 -37 C ATOM 764 CG1 VAL A 117 16.196 6.388 28.105 1.00 14.70 C ANISOU 764 CG1 VAL A 117 1800 1853 1933 9 34 -4 C ATOM 765 CG2 VAL A 117 15.308 5.412 30.232 1.00 14.53 C ANISOU 765 CG2 VAL A 117 1887 1842 1790 41 -26 14 C ATOM 766 N PRO A 118 13.042 7.767 27.013 1.00 13.55 N ANISOU 766 N PRO A 118 1723 1754 1673 -17 -55 0 N ATOM 767 CA PRO A 118 12.888 8.441 25.734 1.00 13.78 C ANISOU 767 CA PRO A 118 1778 1749 1708 5 -22 8 C ATOM 768 C PRO A 118 12.470 9.894 25.853 1.00 13.72 C ANISOU 768 C PRO A 118 1758 1737 1716 -14 -6 -7 C ATOM 769 O PRO A 118 12.914 10.740 25.070 1.00 13.52 O ANISOU 769 O PRO A 118 1806 1684 1648 -1 -30 -24 O ATOM 770 CB PRO A 118 11.849 7.621 24.984 1.00 13.86 C ANISOU 770 CB PRO A 118 1783 1761 1723 -20 -11 -19 C ATOM 771 CG PRO A 118 11.332 6.607 25.939 1.00 14.38 C ANISOU 771 CG PRO A 118 1821 1821 1820 -22 -13 32 C ATOM 772 CD PRO A 118 12.415 6.422 26.971 1.00 14.17 C ANISOU 772 CD PRO A 118 1837 1783 1766 -31 -21 7 C ATOM 773 N VAL A 119 11.636 10.205 26.843 1.00 13.48 N ANISOU 773 N VAL A 119 1649 1733 1741 6 -33 -15 N ATOM 774 CA VAL A 119 11.260 11.589 27.118 1.00 13.73 C ANISOU 774 CA VAL A 119 1740 1727 1750 -7 -47 -15 C ATOM 775 C VAL A 119 12.486 12.437 27.433 1.00 13.28 C ANISOU 775 C VAL A 119 1745 1658 1645 0 -44 -8 C ATOM 776 O VAL A 119 12.643 13.531 26.890 1.00 13.37 O ANISOU 776 O VAL A 119 1777 1722 1582 -31 -64 19 O ATOM 777 CB VAL A 119 10.239 11.665 28.267 1.00 14.73 C ANISOU 777 CB VAL A 119 1870 1849 1878 -14 47 6 C ATOM 778 CG1 VAL A 119 9.964 13.101 28.692 1.00 14.19 C ANISOU 778 CG1 VAL A 119 1825 1865 1702 58 -14 4 C ATOM 779 CG2 VAL A 119 8.939 10.980 27.853 1.00 14.96 C ANISOU 779 CG2 VAL A 119 1930 1922 1833 -18 -22 -13 C ATOM 780 N PHE A 120 13.357 11.939 28.309 1.00 12.96 N ANISOU 780 N PHE A 120 1680 1619 1627 4 -21 -19 N ATOM 781 CA PHE A 120 14.544 12.681 28.713 1.00 13.00 C ANISOU 781 CA PHE A 120 1680 1657 1604 -12 -26 9 C ATOM 782 C PHE A 120 15.663 12.648 27.693 1.00 13.23 C ANISOU 782 C PHE A 120 1696 1689 1640 -8 -11 -15 C ATOM 783 O PHE A 120 16.465 13.587 27.614 1.00 13.25 O ANISOU 783 O PHE A 120 1736 1698 1601 -29 5 -22 O ATOM 784 CB PHE A 120 14.997 12.184 30.102 1.00 12.98 C ANISOU 784 CB PHE A 120 1669 1676 1588 0 -33 -13 C ATOM 785 CG PHE A 120 14.130 12.822 31.163 1.00 13.32 C ANISOU 785 CG PHE A 120 1688 1738 1634 20 -1 14 C ATOM 786 CD1 PHE A 120 12.902 12.283 31.497 1.00 13.36 C ANISOU 786 CD1 PHE A 120 1704 1742 1631 -13 -21 10 C ATOM 787 CD2 PHE A 120 14.559 13.970 31.807 1.00 14.27 C ANISOU 787 CD2 PHE A 120 1888 1727 1807 -4 16 -8 C ATOM 788 CE1 PHE A 120 12.105 12.878 32.459 1.00 13.60 C ANISOU 788 CE1 PHE A 120 1753 1738 1678 34 -18 10 C ATOM 789 CE2 PHE A 120 13.771 14.568 32.770 1.00 14.17 C ANISOU 789 CE2 PHE A 120 1844 1812 1729 -31 19 2 C ATOM 790 CZ PHE A 120 12.545 14.023 33.099 1.00 14.41 C ANISOU 790 CZ PHE A 120 1830 1808 1838 -51 -30 -29 C ATOM 791 N GLN A 121 15.726 11.621 26.841 1.00 13.44 N ANISOU 791 N GLN A 121 1720 1697 1690 -9 -13 -31 N ATOM 792 CA GLN A 121 16.628 11.674 25.690 1.00 13.55 C ANISOU 792 CA GLN A 121 1771 1700 1679 -3 -6 -16 C ATOM 793 C GLN A 121 16.300 12.870 24.804 1.00 13.17 C ANISOU 793 C GLN A 121 1707 1674 1621 -1 -1 -44 C ATOM 794 O GLN A 121 17.202 13.607 24.406 1.00 13.15 O ANISOU 794 O GLN A 121 1742 1683 1570 -7 -1 -50 O ATOM 795 CB GLN A 121 16.581 10.371 24.890 1.00 14.24 C ANISOU 795 CB GLN A 121 1891 1781 1740 -29 -1 -95 C ATOM 796 CG GLN A 121 17.144 9.176 25.645 1.00 16.47 C ANISOU 796 CG GLN A 121 2134 2068 2056 64 -16 82 C ATOM 797 CD GLN A 121 17.053 7.886 24.858 1.00 18.74 C ANISOU 797 CD GLN A 121 2510 2285 2324 -53 -8 -77 C ATOM 798 OE1 GLN A 121 18.039 7.164 24.695 1.00 21.11 O ANISOU 798 OE1 GLN A 121 2672 2667 2683 83 8 -24 O ATOM 799 NE2 GLN A 121 15.866 7.567 24.363 1.00 19.42 N ANISOU 799 NE2 GLN A 121 2498 2422 2459 33 -5 -75 N ATOM 800 N GLN A 122 15.018 13.088 24.503 1.00 13.36 N ANISOU 800 N GLN A 122 1715 1712 1649 7 1 -37 N ATOM 801 CA GLN A 122 14.629 14.236 23.694 1.00 13.96 C ANISOU 801 CA GLN A 122 1800 1757 1745 26 -12 -4 C ATOM 802 C GLN A 122 14.854 15.562 24.404 1.00 14.11 C ANISOU 802 C GLN A 122 1848 1768 1746 -4 -2 5 C ATOM 803 O GLN A 122 15.283 16.531 23.773 1.00 13.90 O ANISOU 803 O GLN A 122 1787 1800 1695 -67 -8 -14 O ATOM 804 CB GLN A 122 13.181 14.085 23.221 1.00 14.96 C ANISOU 804 CB GLN A 122 1828 1951 1905 -5 -18 -5 C ATOM 805 CG GLN A 122 12.720 15.185 22.280 1.00 15.94 C ANISOU 805 CG GLN A 122 2074 2005 1976 25 14 34 C ATOM 806 CD GLN A 122 13.520 15.224 20.990 1.00 15.85 C ANISOU 806 CD GLN A 122 2001 2063 1959 10 -19 24 C ATOM 807 OE1 GLN A 122 13.969 14.187 20.501 1.00 16.76 O ANISOU 807 OE1 GLN A 122 2201 2131 2037 52 -35 -19 O ATOM 808 NE2 GLN A 122 13.698 16.416 20.440 1.00 15.71 N ANISOU 808 NE2 GLN A 122 2023 2025 1920 -22 -8 -38 N ATOM 809 N ILE A 123 14.599 15.639 25.711 1.00 14.23 N ANISOU 809 N ILE A 123 1873 1799 1735 -14 -27 -3 N ATOM 810 CA ILE A 123 14.945 16.838 26.471 1.00 14.04 C ANISOU 810 CA ILE A 123 1808 1800 1728 -12 -1 -2 C ATOM 811 C ILE A 123 16.430 17.149 26.325 1.00 13.75 C ANISOU 811 C ILE A 123 1791 1755 1680 4 -13 -19 C ATOM 812 O ILE A 123 16.797 18.284 26.014 1.00 14.08 O ANISOU 812 O ILE A 123 1911 1781 1657 5 26 14 O ATOM 813 CB ILE A 123 14.565 16.714 27.952 1.00 13.41 C ANISOU 813 CB ILE A 123 1687 1710 1699 -12 -17 -7 C ATOM 814 CG1 ILE A 123 13.041 16.688 28.115 1.00 13.25 C ANISOU 814 CG1 ILE A 123 1684 1665 1686 -21 -1 -13 C ATOM 815 CG2 ILE A 123 15.140 17.865 28.774 1.00 14.01 C ANISOU 815 CG2 ILE A 123 1852 1725 1747 -44 -16 -33 C ATOM 816 CD1 ILE A 123 12.600 16.149 29.461 1.00 13.88 C ANISOU 816 CD1 ILE A 123 1795 1803 1674 -7 26 -40 C ATOM 817 N ALA A 124 17.285 16.158 26.552 1.00 13.56 N ANISOU 817 N ALA A 124 1771 1729 1654 -6 -33 -20 N ATOM 818 CA ALA A 124 18.725 16.321 26.448 1.00 13.72 C ANISOU 818 CA ALA A 124 1775 1719 1718 -7 -29 -9 C ATOM 819 C ALA A 124 19.158 16.814 25.075 1.00 14.57 C ANISOU 819 C ALA A 124 1871 1860 1806 -34 20 20 C ATOM 820 O ALA A 124 20.002 17.701 24.969 1.00 14.10 O ANISOU 820 O ALA A 124 1887 1768 1704 -32 -62 -23 O ATOM 821 CB ALA A 124 19.433 15.012 26.775 1.00 13.46 C ANISOU 821 CB ALA A 124 1697 1731 1686 24 -53 -65 C ATOM 822 N ARG A 125 18.588 16.251 24.010 1.00 15.36 N ANISOU 822 N ARG A 125 1956 1985 1895 -22 -25 -37 N ATOM 823 CA ARG A 125 18.884 16.721 22.663 1.00 16.30 C ANISOU 823 CA ARG A 125 2089 2107 1998 3 22 30 C ATOM 824 C ARG A 125 18.565 18.197 22.481 1.00 16.71 C ANISOU 824 C ARG A 125 2143 2125 2081 17 -22 5 C ATOM 825 O ARG A 125 19.368 18.935 21.907 1.00 17.64 O ANISOU 825 O ARG A 125 2231 2276 2196 -44 13 14 O ATOM 826 CB ARG A 125 18.091 15.906 21.638 1.00 17.84 C ANISOU 826 CB ARG A 125 2269 2314 2196 -44 -75 -55 C ATOM 827 CG ARG A 125 18.541 14.456 21.540 1.00 19.58 C ANISOU 827 CG ARG A 125 2551 2414 2475 11 -8 -1 C ATOM 828 CD ARG A 125 17.477 13.650 20.807 1.00 19.77 C ANISOU 828 CD ARG A 125 2508 2487 2516 8 -11 0 C ATOM 829 NE ARG A 125 17.702 12.216 20.945 1.00 19.10 N ANISOU 829 NE ARG A 125 2398 2450 2409 -31 -5 -2 N ATOM 830 CZ ARG A 125 16.722 11.337 21.129 1.00 18.26 C ANISOU 830 CZ ARG A 125 2279 2385 2274 30 -13 -31 C ATOM 831 NH1 ARG A 125 15.459 11.744 21.208 1.00 16.66 N ANISOU 831 NH1 ARG A 125 2166 2121 2043 -30 -26 -33 N ATOM 832 NH2 ARG A 125 17.015 10.050 21.245 1.00 19.63 N ANISOU 832 NH2 ARG A 125 2528 2462 2469 55 -32 -13 N ATOM 833 N GLU A 126 17.404 18.628 22.964 1.00 16.71 N ANISOU 833 N GLU A 126 2132 2135 2083 21 -31 2 N ATOM 834 CA GLU A 126 16.976 20.015 22.811 1.00 16.92 C ANISOU 834 CA GLU A 126 2145 2142 2144 10 9 25 C ATOM 835 C GLU A 126 17.793 20.955 23.683 1.00 17.56 C ANISOU 835 C GLU A 126 2252 2218 2201 -11 -13 -12 C ATOM 836 O GLU A 126 18.129 22.067 23.267 1.00 18.38 O ANISOU 836 O GLU A 126 2411 2264 2309 -12 -4 15 O ATOM 837 CB GLU A 126 15.474 20.128 23.089 1.00 16.22 C ANISOU 837 CB GLU A 126 2115 1996 2053 10 22 12 C ATOM 838 CG GLU A 126 14.646 19.297 22.115 1.00 17.85 C ANISOU 838 CG GLU A 126 2397 2241 2144 -46 -93 -46 C ATOM 839 CD GLU A 126 13.153 19.492 22.255 1.00 21.55 C ANISOU 839 CD GLU A 126 2621 2855 2712 0 21 3 C ATOM 840 OE1 GLU A 126 12.726 20.639 22.506 1.00 23.99 O ANISOU 840 OE1 GLU A 126 3061 2988 3065 69 -18 -27 O ATOM 841 OE2 GLU A 126 12.394 18.507 22.111 1.00 22.47 O ANISOU 841 OE2 GLU A 126 2818 2836 2885 -12 0 -42 O ATOM 842 N VAL A 127 18.156 20.520 24.886 1.00 17.64 N ANISOU 842 N VAL A 127 2254 2245 2205 -16 -17 0 N ATOM 843 CA VAL A 127 19.126 21.242 25.706 1.00 17.38 C ANISOU 843 CA VAL A 127 2234 2214 2156 -2 -12 27 C ATOM 844 C VAL A 127 20.431 21.443 24.945 1.00 17.49 C ANISOU 844 C VAL A 127 2227 2222 2198 -10 -26 22 C ATOM 845 O VAL A 127 20.908 22.569 24.823 1.00 17.18 O ANISOU 845 O VAL A 127 2209 2200 2117 6 -25 48 O ATOM 846 CB VAL A 127 19.381 20.505 27.032 1.00 16.35 C ANISOU 846 CB VAL A 127 2037 2071 2106 -3 8 -8 C ATOM 847 CG1 VAL A 127 20.556 21.089 27.799 1.00 16.28 C ANISOU 847 CG1 VAL A 127 2070 2050 2065 -6 -16 22 C ATOM 848 CG2 VAL A 127 18.120 20.548 27.890 1.00 15.64 C ANISOU 848 CG2 VAL A 127 2001 1934 2009 -1 -18 9 C ATOM 849 N GLY A 128 21.009 20.354 24.449 1.00 17.88 N ANISOU 849 N GLY A 128 2291 2259 2244 7 -28 -14 N ATOM 850 CA GLY A 128 22.228 20.406 23.661 1.00 18.47 C ANISOU 850 CA GLY A 128 2356 2328 2333 -11 19 0 C ATOM 851 C GLY A 128 23.473 20.333 24.535 1.00 18.92 C ANISOU 851 C GLY A 128 2413 2369 2407 -15 -21 20 C ATOM 852 O GLY A 128 23.448 20.704 25.708 1.00 19.30 O ANISOU 852 O GLY A 128 2476 2434 2424 -20 -11 16 O ATOM 853 N GLU A 129 24.585 19.904 23.945 1.00 19.49 N ANISOU 853 N GLU A 129 2486 2416 2505 -21 24 3 N ATOM 854 CA GLU A 129 25.816 19.678 24.688 1.00 20.58 C ANISOU 854 CA GLU A 129 2632 2575 2610 -48 -91 43 C ATOM 855 C GLU A 129 26.326 20.919 25.406 1.00 20.30 C ANISOU 855 C GLU A 129 2584 2560 2568 -23 -13 17 C ATOM 856 O GLU A 129 26.721 20.813 26.574 1.00 20.09 O ANISOU 856 O GLU A 129 2551 2529 2551 -37 -11 0 O ATOM 857 CB GLU A 129 26.905 19.117 23.768 1.00 24.68 C ANISOU 857 CB GLU A 129 3215 3083 3078 21 226 -103 C ATOM 858 CG GLU A 129 28.193 18.752 24.487 1.00 30.20 C ANISOU 858 CG GLU A 129 3772 3820 3883 34 -210 72 C ATOM 859 CD GLU A 129 29.317 18.339 23.559 1.00 34.49 C ANISOU 859 CD GLU A 129 4332 4382 4391 25 145 -37 C ATOM 860 OE1 GLU A 129 29.140 18.384 22.324 1.00 35.53 O ANISOU 860 OE1 GLU A 129 4537 4503 4460 17 28 4 O ATOM 861 OE2 GLU A 129 30.394 17.961 24.073 1.00 36.13 O ANISOU 861 OE2 GLU A 129 4510 4575 4645 27 -19 24 O ATOM 862 N VAL A 130 26.340 22.078 24.756 1.00 20.34 N ANISOU 862 N VAL A 130 2613 2574 2542 -5 -5 5 N ATOM 863 CA VAL A 130 26.913 23.274 25.377 1.00 20.61 C ANISOU 863 CA VAL A 130 2604 2625 2601 -4 3 -51 C ATOM 864 C VAL A 130 26.175 23.637 26.658 1.00 19.96 C ANISOU 864 C VAL A 130 2520 2519 2544 -10 -20 3 C ATOM 865 O VAL A 130 26.800 23.825 27.707 1.00 20.06 O ANISOU 865 O VAL A 130 2594 2507 2523 -17 -27 24 O ATOM 866 CB VAL A 130 26.945 24.474 24.416 1.00 22.95 C ANISOU 866 CB VAL A 130 2983 2842 2895 12 6 101 C ATOM 867 CG1 VAL A 130 27.402 25.747 25.118 1.00 24.04 C ANISOU 867 CG1 VAL A 130 3097 2994 3042 -14 -6 -23 C ATOM 868 CG2 VAL A 130 27.866 24.173 23.238 1.00 23.49 C ANISOU 868 CG2 VAL A 130 2967 2968 2991 0 20 26 C ATOM 869 N ARG A 131 24.851 23.728 26.585 1.00 19.13 N ANISOU 869 N ARG A 131 2478 2412 2379 -9 14 10 N ATOM 870 CA ARG A 131 24.052 24.066 27.758 1.00 18.50 C ANISOU 870 CA ARG A 131 2395 2308 2327 4 -21 20 C ATOM 871 C ARG A 131 24.117 22.970 28.813 1.00 18.17 C ANISOU 871 C ARG A 131 2359 2237 2309 -24 8 1 C ATOM 872 O ARG A 131 24.191 23.284 30.004 1.00 18.45 O ANISOU 872 O ARG A 131 2412 2276 2322 -20 -41 20 O ATOM 873 CB ARG A 131 22.609 24.392 27.370 1.00 18.38 C ANISOU 873 CB ARG A 131 2373 2343 2268 -13 -10 -16 C ATOM 874 CG ARG A 131 22.522 25.694 26.581 1.00 19.28 C ANISOU 874 CG ARG A 131 2471 2385 2472 -10 33 24 C ATOM 875 CD ARG A 131 21.096 26.188 26.454 1.00 19.54 C ANISOU 875 CD ARG A 131 2492 2455 2478 5 -30 40 C ATOM 876 NE ARG A 131 20.274 25.325 25.612 1.00 19.73 N ANISOU 876 NE ARG A 131 2563 2491 2443 -13 -36 34 N ATOM 877 CZ ARG A 131 19.057 25.659 25.191 1.00 19.80 C ANISOU 877 CZ ARG A 131 2495 2513 2515 -30 25 0 C ATOM 878 NH1 ARG A 131 18.534 26.828 25.537 1.00 19.98 N ANISOU 878 NH1 ARG A 131 2592 2539 2459 14 14 26 N ATOM 879 NH2 ARG A 131 18.376 24.819 24.422 1.00 19.69 N ANISOU 879 NH2 ARG A 131 2518 2505 2459 -31 -7 30 N ATOM 880 N MET A 132 24.140 21.708 28.397 1.00 17.66 N ANISOU 880 N MET A 132 2283 2207 2221 -25 -12 28 N ATOM 881 CA MET A 132 24.244 20.606 29.352 1.00 17.05 C ANISOU 881 CA MET A 132 2203 2108 2167 -28 -22 -25 C ATOM 882 C MET A 132 25.540 20.696 30.148 1.00 17.36 C ANISOU 882 C MET A 132 2209 2205 2181 -12 -18 -2 C ATOM 883 O MET A 132 25.536 20.622 31.379 1.00 17.05 O ANISOU 883 O MET A 132 2134 2178 2168 -44 5 10 O ATOM 884 CB MET A 132 24.131 19.257 28.644 1.00 15.75 C ANISOU 884 CB MET A 132 2047 2025 1913 -28 1 60 C ATOM 885 CG MET A 132 23.976 18.074 29.592 1.00 15.22 C ANISOU 885 CG MET A 132 1985 1905 1895 -32 -24 -6 C ATOM 886 SD MET A 132 22.356 18.031 30.385 1.00 14.52 S ANISOU 886 SD MET A 132 1976 1888 1654 -6 -75 59 S ATOM 887 CE MET A 132 21.312 17.590 28.993 1.00 14.96 C ANISOU 887 CE MET A 132 1901 1976 1806 -48 -57 -43 C ATOM 888 N GLN A 133 26.661 20.896 29.462 1.00 17.86 N ANISOU 888 N GLN A 133 2262 2289 2235 -17 9 26 N ATOM 889 CA GLN A 133 27.961 21.059 30.098 1.00 18.44 C ANISOU 889 CA GLN A 133 2334 2342 2328 -21 -44 3 C ATOM 890 C GLN A 133 27.964 22.194 31.116 1.00 18.90 C ANISOU 890 C GLN A 133 2425 2363 2391 -15 -11 -14 C ATOM 891 O GLN A 133 28.430 22.038 32.244 1.00 18.87 O ANISOU 891 O GLN A 133 2446 2323 2400 -39 -30 -17 O ATOM 892 CB GLN A 133 29.034 21.344 29.036 1.00 19.68 C ANISOU 892 CB GLN A 133 2459 2507 2512 -22 58 6 C ATOM 893 CG GLN A 133 30.460 21.211 29.554 1.00 20.84 C ANISOU 893 CG GLN A 133 2550 2714 2653 -15 -3 1 C ATOM 894 CD GLN A 133 30.803 19.764 29.857 1.00 22.95 C ANISOU 894 CD GLN A 133 2897 2830 2994 24 -10 26 C ATOM 895 OE1 GLN A 133 31.017 18.966 28.946 1.00 23.74 O ANISOU 895 OE1 GLN A 133 3065 2940 3015 -12 -6 -2 O ATOM 896 NE2 GLN A 133 30.847 19.419 31.139 1.00 24.73 N ANISOU 896 NE2 GLN A 133 3159 3148 3090 -10 -4 43 N ATOM 897 N LYS A 134 27.458 23.352 30.704 1.00 19.35 N ANISOU 897 N LYS A 134 2497 2423 2431 10 -8 20 N ATOM 898 CA LYS A 134 27.362 24.525 31.559 1.00 19.90 C ANISOU 898 CA LYS A 134 2562 2517 2483 -37 11 -45 C ATOM 899 C LYS A 134 26.629 24.248 32.865 1.00 19.64 C ANISOU 899 C LYS A 134 2495 2474 2492 -44 -1 -3 C ATOM 900 O LYS A 134 27.139 24.582 33.940 1.00 19.77 O ANISOU 900 O LYS A 134 2553 2485 2475 -47 0 24 O ATOM 901 CB LYS A 134 26.672 25.663 30.797 1.00 22.30 C ANISOU 901 CB LYS A 134 2828 2773 2872 44 -35 118 C ATOM 902 CG LYS A 134 26.470 26.937 31.594 1.00 24.52 C ANISOU 902 CG LYS A 134 3176 3054 3086 -12 14 -94 C ATOM 903 CD LYS A 134 25.790 28.032 30.789 1.00 26.41 C ANISOU 903 CD LYS A 134 3437 3279 3320 47 -5 36 C ATOM 904 CE LYS A 134 24.343 27.705 30.466 1.00 28.02 C ANISOU 904 CE LYS A 134 3520 3553 3576 -12 7 -17 C ATOM 905 NZ LYS A 134 23.665 28.821 29.745 1.00 28.82 N ANISOU 905 NZ LYS A 134 3696 3646 3611 17 -18 24 N ATOM 906 N TYR A 135 25.442 23.649 32.795 1.00 19.20 N ANISOU 906 N TYR A 135 2446 2430 2419 -5 22 10 N ATOM 907 CA TYR A 135 24.657 23.409 34.004 1.00 18.74 C ANISOU 907 CA TYR A 135 2410 2339 2372 4 -6 31 C ATOM 908 C TYR A 135 25.271 22.350 34.904 1.00 17.97 C ANISOU 908 C TYR A 135 2310 2237 2280 0 15 -29 C ATOM 909 O TYR A 135 25.234 22.506 36.132 1.00 17.72 O ANISOU 909 O TYR A 135 2317 2163 2254 -29 2 10 O ATOM 910 CB TYR A 135 23.208 23.071 33.644 1.00 19.48 C ANISOU 910 CB TYR A 135 2453 2481 2469 -39 -16 6 C ATOM 911 CG TYR A 135 22.420 24.320 33.295 1.00 20.56 C ANISOU 911 CG TYR A 135 2598 2561 2652 0 -12 22 C ATOM 912 CD1 TYR A 135 21.938 25.147 34.300 1.00 21.39 C ANISOU 912 CD1 TYR A 135 2724 2687 2714 -2 35 -15 C ATOM 913 CD2 TYR A 135 22.190 24.678 31.977 1.00 21.03 C ANISOU 913 CD2 TYR A 135 2663 2668 2658 -12 -4 2 C ATOM 914 CE1 TYR A 135 21.226 26.294 34.001 1.00 21.99 C ANISOU 914 CE1 TYR A 135 2817 2729 2807 9 4 -5 C ATOM 915 CE2 TYR A 135 21.479 25.824 31.669 1.00 21.55 C ANISOU 915 CE2 TYR A 135 2749 2709 2730 -9 -19 37 C ATOM 916 CZ TYR A 135 21.002 26.624 32.681 1.00 22.16 C ANISOU 916 CZ TYR A 135 2821 2783 2815 1 11 3 C ATOM 917 OH TYR A 135 20.299 27.768 32.375 1.00 22.78 O ANISOU 917 OH TYR A 135 2875 2854 2926 23 11 40 O ATOM 918 N LEU A 136 25.898 21.317 34.338 1.00 17.13 N ANISOU 918 N LEU A 136 2191 2157 2161 -26 -37 -7 N ATOM 919 CA LEU A 136 26.542 20.310 35.181 1.00 16.72 C ANISOU 919 CA LEU A 136 2153 2102 2098 -23 1 -27 C ATOM 920 C LEU A 136 27.765 20.886 35.890 1.00 17.05 C ANISOU 920 C LEU A 136 2162 2171 2146 -45 -22 12 C ATOM 921 O LEU A 136 28.085 20.463 37.002 1.00 17.04 O ANISOU 921 O LEU A 136 2161 2144 2168 -84 -45 53 O ATOM 922 CB LEU A 136 26.906 19.042 34.423 1.00 15.81 C ANISOU 922 CB LEU A 136 1988 2034 1985 -21 -2 35 C ATOM 923 CG LEU A 136 25.770 18.231 33.796 1.00 15.63 C ANISOU 923 CG LEU A 136 2013 1996 1928 -28 28 -4 C ATOM 924 CD1 LEU A 136 26.276 16.841 33.426 1.00 15.77 C ANISOU 924 CD1 LEU A 136 1999 2002 1990 -16 1 -14 C ATOM 925 CD2 LEU A 136 24.551 18.122 34.704 1.00 14.96 C ANISOU 925 CD2 LEU A 136 1913 1874 1898 1 -15 -29 C ATOM 926 N LYS A 137 28.455 21.832 35.258 1.00 17.33 N ANISOU 926 N LYS A 137 2204 2182 2199 -47 -13 26 N ATOM 927 CA LYS A 137 29.508 22.572 35.949 1.00 17.66 C ANISOU 927 CA LYS A 137 2227 2237 2247 -32 -26 -23 C ATOM 928 C LYS A 137 28.935 23.391 37.098 1.00 17.69 C ANISOU 928 C LYS A 137 2227 2245 2248 -28 14 10 C ATOM 929 O LYS A 137 29.430 23.349 38.227 1.00 18.23 O ANISOU 929 O LYS A 137 2304 2341 2282 -33 -13 12 O ATOM 930 CB LYS A 137 30.248 23.488 34.973 1.00 19.41 C ANISOU 930 CB LYS A 137 2542 2446 2388 29 89 125 C ATOM 931 CG LYS A 137 31.361 24.295 35.626 1.00 23.67 C ANISOU 931 CG LYS A 137 2904 3000 3090 -84 -152 -151 C ATOM 932 CD LYS A 137 32.014 25.248 34.640 1.00 28.27 C ANISOU 932 CD LYS A 137 3628 3524 3588 -113 -27 160 C ATOM 933 CE LYS A 137 32.901 24.516 33.648 1.00 32.49 C ANISOU 933 CE LYS A 137 4117 4129 4099 102 41 -108 C ATOM 934 NZ LYS A 137 33.646 25.458 32.766 1.00 34.89 N ANISOU 934 NZ LYS A 137 4434 4390 4432 -31 42 41 N ATOM 935 N LYS A 138 27.856 24.124 36.834 1.00 17.55 N ANISOU 935 N LYS A 138 2250 2195 2223 -41 23 38 N ATOM 936 CA LYS A 138 27.163 24.891 37.858 1.00 18.34 C ANISOU 936 CA LYS A 138 2397 2261 2309 -53 58 -15 C ATOM 937 C LYS A 138 26.676 24.032 39.017 1.00 17.99 C ANISOU 937 C LYS A 138 2332 2228 2275 -39 5 -5 C ATOM 938 O LYS A 138 26.735 24.454 40.175 1.00 18.11 O ANISOU 938 O LYS A 138 2356 2261 2265 -71 2 30 O ATOM 939 CB LYS A 138 25.976 25.641 37.239 1.00 21.34 C ANISOU 939 CB LYS A 138 2566 2785 2756 84 -90 -31 C ATOM 940 CG LYS A 138 26.400 26.825 36.381 1.00 25.62 C ANISOU 940 CG LYS A 138 3398 3143 3195 -141 58 72 C ATOM 941 CD LYS A 138 25.215 27.715 36.040 1.00 30.11 C ANISOU 941 CD LYS A 138 3713 3867 3861 120 -44 -13 C ATOM 942 CE LYS A 138 25.684 29.014 35.400 1.00 33.24 C ANISOU 942 CE LYS A 138 4291 4119 4218 -62 23 49 C ATOM 943 NZ LYS A 138 24.556 29.954 35.162 1.00 34.50 N ANISOU 943 NZ LYS A 138 4378 4331 4402 30 -1 0 N ATOM 944 N PHE A 139 26.202 22.824 38.727 1.00 17.36 N ANISOU 944 N PHE A 139 2216 2197 2183 -22 -20 11 N ATOM 945 CA PHE A 139 25.697 21.924 39.747 1.00 16.87 C ANISOU 945 CA PHE A 139 2139 2126 2144 -50 -54 -18 C ATOM 946 C PHE A 139 26.772 21.076 40.415 1.00 17.00 C ANISOU 946 C PHE A 139 2176 2137 2148 -20 -21 -6 C ATOM 947 O PHE A 139 26.431 20.284 41.301 1.00 17.12 O ANISOU 947 O PHE A 139 2203 2155 2147 -37 -46 18 O ATOM 948 CB PHE A 139 24.650 20.970 39.169 1.00 15.36 C ANISOU 948 CB PHE A 139 1988 1993 1856 31 8 38 C ATOM 949 CG PHE A 139 23.418 21.558 38.561 1.00 14.95 C ANISOU 949 CG PHE A 139 1915 1898 1868 -13 2 -21 C ATOM 950 CD1 PHE A 139 23.027 22.867 38.757 1.00 15.12 C ANISOU 950 CD1 PHE A 139 1947 1903 1894 4 -13 -5 C ATOM 951 CD2 PHE A 139 22.620 20.752 37.755 1.00 14.99 C ANISOU 951 CD2 PHE A 139 1921 1890 1884 -17 -23 -6 C ATOM 952 CE1 PHE A 139 21.880 23.374 38.184 1.00 15.55 C ANISOU 952 CE1 PHE A 139 1975 2000 1932 2 -27 17 C ATOM 953 CE2 PHE A 139 21.469 21.249 37.174 1.00 15.51 C ANISOU 953 CE2 PHE A 139 1905 1982 2004 1 -15 3 C ATOM 954 CZ PHE A 139 21.098 22.559 37.389 1.00 16.00 C ANISOU 954 CZ PHE A 139 2093 1974 2012 -38 -32 -3 C ATOM 955 N SER A 140 28.022 21.173 39.990 1.00 16.94 N ANISOU 955 N SER A 140 2176 2121 2139 -23 -6 -32 N ATOM 956 CA SER A 140 29.085 20.306 40.484 1.00 17.77 C ANISOU 956 CA SER A 140 2240 2190 2322 8 9 24 C ATOM 957 C SER A 140 28.680 18.838 40.395 1.00 17.25 C ANISOU 957 C SER A 140 2219 2160 2174 -8 -19 -7 C ATOM 958 O SER A 140 28.797 18.080 41.359 1.00 17.27 O ANISOU 958 O SER A 140 2267 2170 2126 -31 2 -27 O ATOM 959 CB SER A 140 29.454 20.672 41.923 1.00 21.14 C ANISOU 959 CB SER A 140 2806 2767 2458 26 -56 -32 C ATOM 960 OG SER A 140 30.066 21.945 41.997 1.00 24.01 O ANISOU 960 OG SER A 140 3124 2927 3072 -57 -8 8 O ATOM 961 N TYR A 141 28.235 18.418 39.210 1.00 16.78 N ANISOU 961 N TYR A 141 2134 2108 2133 -29 6 -11 N ATOM 962 CA TYR A 141 27.593 17.115 39.069 1.00 16.35 C ANISOU 962 CA TYR A 141 2060 2084 2068 -13 -40 -1 C ATOM 963 C TYR A 141 28.588 16.045 38.649 1.00 16.35 C ANISOU 963 C TYR A 141 2069 2065 2076 -30 -14 -2 C ATOM 964 O TYR A 141 28.883 15.854 37.470 1.00 16.61 O ANISOU 964 O TYR A 141 2128 2123 2058 -38 -62 6 O ATOM 965 CB TYR A 141 26.416 17.206 38.086 1.00 15.36 C ANISOU 965 CB TYR A 141 1980 1911 1944 -53 12 4 C ATOM 966 CG TYR A 141 25.519 15.986 38.193 1.00 14.34 C ANISOU 966 CG TYR A 141 1848 1823 1777 10 -6 21 C ATOM 967 CD1 TYR A 141 24.456 15.967 39.088 1.00 14.06 C ANISOU 967 CD1 TYR A 141 1759 1790 1794 21 -39 29 C ATOM 968 CD2 TYR A 141 25.750 14.865 37.414 1.00 14.12 C ANISOU 968 CD2 TYR A 141 1808 1803 1756 -13 -14 23 C ATOM 969 CE1 TYR A 141 23.638 14.854 39.196 1.00 14.14 C ANISOU 969 CE1 TYR A 141 1798 1781 1794 6 -39 3 C ATOM 970 CE2 TYR A 141 24.939 13.747 37.519 1.00 14.28 C ANISOU 970 CE2 TYR A 141 1815 1809 1801 -26 -16 15 C ATOM 971 CZ TYR A 141 23.887 13.749 38.409 1.00 14.34 C ANISOU 971 CZ TYR A 141 1851 1807 1791 -6 -6 -11 C ATOM 972 OH TYR A 141 23.075 12.640 38.508 1.00 14.65 O ANISOU 972 OH TYR A 141 1932 1825 1811 -37 -10 -8 O ATOM 973 N GLY A 142 29.141 15.340 39.632 1.00 16.62 N ANISOU 973 N GLY A 142 2129 2080 2106 -27 -39 2 N ATOM 974 CA GLY A 142 30.042 14.227 39.384 1.00 16.88 C ANISOU 974 CA GLY A 142 2128 2165 2120 9 -43 -17 C ATOM 975 C GLY A 142 31.286 14.650 38.626 1.00 17.17 C ANISOU 975 C GLY A 142 2186 2188 2149 7 -17 16 C ATOM 976 O GLY A 142 31.842 15.729 38.845 1.00 17.97 O ANISOU 976 O GLY A 142 2294 2275 2260 -56 -21 -1 O ATOM 977 N ASN A 143 31.712 13.819 37.675 1.00 17.00 N ANISOU 977 N ASN A 143 2160 2196 2105 -17 -45 8 N ATOM 978 CA ASN A 143 32.909 14.106 36.891 1.00 17.54 C ANISOU 978 CA ASN A 143 2192 2248 2226 -21 -7 -18 C ATOM 979 C ASN A 143 32.613 15.075 35.757 1.00 18.26 C ANISOU 979 C ASN A 143 2338 2319 2280 -25 -20 11 C ATOM 980 O ASN A 143 33.502 15.436 34.986 1.00 18.76 O ANISOU 980 O ASN A 143 2385 2418 2327 -38 6 10 O ATOM 981 CB ASN A 143 33.557 12.828 36.367 1.00 17.41 C ANISOU 981 CB ASN A 143 2194 2226 2194 -20 2 20 C ATOM 982 CG ASN A 143 32.786 12.051 35.330 1.00 17.20 C ANISOU 982 CG ASN A 143 2083 2240 2215 -6 -21 54 C ATOM 983 OD1 ASN A 143 33.274 11.032 34.824 1.00 19.27 O ANISOU 983 OD1 ASN A 143 2535 2372 2412 -8 27 -63 O ATOM 984 ND2 ASN A 143 31.587 12.496 34.985 1.00 14.98 N ANISOU 984 ND2 ASN A 143 1941 1937 1813 -88 9 20 N ATOM 985 N GLN A 144 31.348 15.429 35.557 1.00 18.62 N ANISOU 985 N GLN A 144 2376 2351 2350 3 -13 -6 N ATOM 986 CA GLN A 144 30.911 16.415 34.590 1.00 19.01 C ANISOU 986 CA GLN A 144 2421 2380 2423 7 -46 12 C ATOM 987 C GLN A 144 31.298 16.047 33.163 1.00 19.64 C ANISOU 987 C GLN A 144 2518 2474 2472 -15 3 -3 C ATOM 988 O GLN A 144 31.483 16.916 32.308 1.00 20.22 O ANISOU 988 O GLN A 144 2621 2581 2482 -38 -16 45 O ATOM 989 CB GLN A 144 31.459 17.802 34.941 1.00 19.00 C ANISOU 989 CB GLN A 144 2419 2379 2421 -7 -28 27 C ATOM 990 CG GLN A 144 30.857 18.404 36.200 1.00 21.01 C ANISOU 990 CG GLN A 144 2653 2738 2593 41 70 -27 C ATOM 991 CD GLN A 144 31.585 19.666 36.622 1.00 23.11 C ANISOU 991 CD GLN A 144 2924 2851 3004 -28 -11 -73 C ATOM 992 OE1 GLN A 144 31.897 20.515 35.788 1.00 24.83 O ANISOU 992 OE1 GLN A 144 3180 3092 3161 -47 41 37 O ATOM 993 NE2 GLN A 144 31.850 19.774 37.916 1.00 23.97 N ANISOU 993 NE2 GLN A 144 2974 3063 3070 -6 -33 -59 N ATOM 994 N ASN A 145 31.378 14.753 32.882 1.00 19.60 N ANISOU 994 N ASN A 145 2489 2476 2480 -6 -5 -5 N ATOM 995 CA ASN A 145 31.839 14.261 31.592 1.00 19.87 C ANISOU 995 CA ASN A 145 2522 2548 2479 -30 -7 -15 C ATOM 996 C ASN A 145 30.624 13.746 30.825 1.00 19.67 C ANISOU 996 C ASN A 145 2506 2490 2478 -24 -8 1 C ATOM 997 O ASN A 145 30.101 12.686 31.164 1.00 19.48 O ANISOU 997 O ASN A 145 2475 2492 2433 -21 -20 9 O ATOM 998 CB ASN A 145 32.880 13.166 31.780 1.00 21.56 C ANISOU 998 CB ASN A 145 2732 2682 2777 54 -49 26 C ATOM 999 CG ASN A 145 33.603 12.760 30.515 1.00 23.31 C ANISOU 999 CG ASN A 145 3023 2970 2863 -16 30 -14 C ATOM 1000 OD1 ASN A 145 34.712 12.217 30.575 1.00 25.20 O ANISOU 1000 OD1 ASN A 145 3132 3218 3223 29 6 11 O ATOM 1001 ND2 ASN A 145 32.995 13.001 29.362 1.00 22.47 N ANISOU 1001 ND2 ASN A 145 2848 2843 2845 11 49 5 N ATOM 1002 N ILE A 146 30.183 14.513 29.830 1.00 19.54 N ANISOU 1002 N ILE A 146 2475 2496 2453 -20 0 -6 N ATOM 1003 CA ILE A 146 28.967 14.132 29.112 1.00 19.75 C ANISOU 1003 CA ILE A 146 2476 2541 2487 -16 -12 9 C ATOM 1004 C ILE A 146 29.277 13.543 27.743 1.00 20.23 C ANISOU 1004 C ILE A 146 2574 2580 2533 -18 -2 -15 C ATOM 1005 O ILE A 146 28.390 13.487 26.884 1.00 20.08 O ANISOU 1005 O ILE A 146 2540 2561 2529 -14 10 3 O ATOM 1006 CB ILE A 146 27.971 15.295 28.983 1.00 19.89 C ANISOU 1006 CB ILE A 146 2514 2514 2531 -10 12 -15 C ATOM 1007 CG1 ILE A 146 28.549 16.455 28.171 1.00 20.54 C ANISOU 1007 CG1 ILE A 146 2638 2584 2580 -29 23 21 C ATOM 1008 CG2 ILE A 146 27.545 15.768 30.371 1.00 20.17 C ANISOU 1008 CG2 ILE A 146 2556 2568 2538 -12 -5 -36 C ATOM 1009 CD1 ILE A 146 27.550 17.541 27.827 1.00 21.41 C ANISOU 1009 CD1 ILE A 146 2732 2695 2707 19 -23 11 C ATOM 1010 N SER A 147 30.508 13.084 27.534 1.00 20.80 N ANISOU 1010 N SER A 147 2612 2651 2643 9 -23 8 N ATOM 1011 CA SER A 147 30.825 12.396 26.282 1.00 21.91 C ANISOU 1011 CA SER A 147 2816 2763 2744 20 21 -32 C ATOM 1012 C SER A 147 30.126 11.043 26.243 1.00 22.25 C ANISOU 1012 C SER A 147 2845 2794 2814 -1 0 -2 C ATOM 1013 O SER A 147 29.731 10.501 27.280 1.00 22.21 O ANISOU 1013 O SER A 147 2846 2815 2780 6 -3 -22 O ATOM 1014 CB ASER A 147 32.337 12.196 26.168 0.50 22.53 C ANISOU 1014 CB ASER A 147 2849 2826 2886 -13 -4 -16 C ATOM 1015 CB BSER A 147 32.324 12.280 26.055 0.50 22.98 C ANISOU 1015 CB BSER A 147 2863 2927 2943 9 6 -1 C ATOM 1016 OG ASER A 147 33.041 13.398 26.417 0.50 21.88 O ANISOU 1016 OG ASER A 147 2748 2800 2768 4 26 -9 O ATOM 1017 OG BSER A 147 32.980 11.643 27.129 0.50 23.01 O ANISOU 1017 OG BSER A 147 2931 2904 2907 20 7 -14 O ATOM 1018 N GLY A 148 29.943 10.505 25.041 1.00 22.43 N ANISOU 1018 N GLY A 148 2874 2825 2824 0 9 -3 N ATOM 1019 CA GLY A 148 29.289 9.210 24.885 1.00 22.48 C ANISOU 1019 CA GLY A 148 2863 2836 2843 -1 -11 -6 C ATOM 1020 C GLY A 148 27.950 9.352 24.171 1.00 22.24 C ANISOU 1020 C GLY A 148 2841 2785 2826 21 1 7 C ATOM 1021 O GLY A 148 27.278 8.357 23.893 1.00 22.81 O ANISOU 1021 O GLY A 148 2900 2837 2931 -12 -5 -14 O ATOM 1022 N GLY A 149 27.570 10.587 23.865 1.00 21.30 N ANISOU 1022 N GLY A 149 2672 2744 2677 19 -20 -26 N ATOM 1023 CA GLY A 149 26.354 10.849 23.102 1.00 20.22 C ANISOU 1023 CA GLY A 149 2578 2563 2541 29 47 -37 C ATOM 1024 C GLY A 149 25.359 11.641 23.943 1.00 19.06 C ANISOU 1024 C GLY A 149 2451 2399 2391 5 -17 15 C ATOM 1025 O GLY A 149 25.086 11.304 25.095 1.00 18.54 O ANISOU 1025 O GLY A 149 2388 2332 2324 13 -28 -45 O ATOM 1026 N ILE A 150 24.739 12.654 23.344 1.00 18.37 N ANISOU 1026 N ILE A 150 2351 2344 2285 -14 3 -25 N ATOM 1027 CA ILE A 150 23.907 13.598 24.084 1.00 18.21 C ANISOU 1027 CA ILE A 150 2294 2342 2281 -24 5 -16 C ATOM 1028 C ILE A 150 22.661 12.951 24.668 1.00 17.71 C ANISOU 1028 C ILE A 150 2260 2257 2214 5 -13 -9 C ATOM 1029 O ILE A 150 22.124 13.429 25.671 1.00 17.29 O ANISOU 1029 O ILE A 150 2182 2213 2172 -20 -18 13 O ATOM 1030 CB ILE A 150 23.537 14.808 23.205 1.00 19.78 C ANISOU 1030 CB ILE A 150 2562 2421 2533 23 6 49 C ATOM 1031 CG1 ILE A 150 22.892 15.924 24.033 1.00 19.99 C ANISOU 1031 CG1 ILE A 150 2543 2502 2551 21 9 0 C ATOM 1032 CG2 ILE A 150 22.620 14.398 22.062 1.00 21.20 C ANISOU 1032 CG2 ILE A 150 2700 2718 2635 -17 -58 -6 C ATOM 1033 CD1 ILE A 150 23.829 16.557 25.041 1.00 20.35 C ANISOU 1033 CD1 ILE A 150 2613 2570 2550 -22 -1 -1 C ATOM 1034 N ASP A 151 22.183 11.862 24.074 1.00 17.77 N ANISOU 1034 N ASP A 151 2284 2268 2200 -7 -29 2 N ATOM 1035 CA ASP A 151 21.018 11.151 24.570 1.00 17.94 C ANISOU 1035 CA ASP A 151 2291 2247 2278 -9 -16 -1 C ATOM 1036 C ASP A 151 21.365 9.844 25.268 1.00 17.74 C ANISOU 1036 C ASP A 151 2257 2263 2221 0 -18 -1 C ATOM 1037 O ASP A 151 20.472 9.012 25.457 1.00 17.72 O ANISOU 1037 O ASP A 151 2281 2266 2187 -9 -19 -6 O ATOM 1038 CB ASP A 151 20.043 10.893 23.410 1.00 18.52 C ANISOU 1038 CB ASP A 151 2379 2369 2289 -4 -44 3 C ATOM 1039 CG ASP A 151 20.685 10.181 22.239 1.00 18.56 C ANISOU 1039 CG ASP A 151 2378 2297 2380 21 -7 8 C ATOM 1040 OD1 ASP A 151 21.808 9.657 22.379 1.00 18.29 O ANISOU 1040 OD1 ASP A 151 2289 2418 2241 -18 -9 -34 O ATOM 1041 OD2 ASP A 151 20.063 10.135 21.154 1.00 19.40 O ANISOU 1041 OD2 ASP A 151 2464 2540 2369 -24 0 -30 O ATOM 1042 N LYS A 152 22.617 9.646 25.684 1.00 17.83 N ANISOU 1042 N LYS A 152 2266 2274 2235 1 -36 12 N ATOM 1043 CA LYS A 152 22.962 8.403 26.367 1.00 17.73 C ANISOU 1043 CA LYS A 152 2192 2307 2239 -27 -51 78 C ATOM 1044 C LYS A 152 24.135 8.516 27.321 1.00 16.42 C ANISOU 1044 C LYS A 152 2105 2052 2083 -21 10 14 C ATOM 1045 O LYS A 152 24.523 7.499 27.912 1.00 16.17 O ANISOU 1045 O LYS A 152 2073 2035 2035 15 3 -35 O ATOM 1046 CB LYS A 152 23.230 7.291 25.340 1.00 21.92 C ANISOU 1046 CB LYS A 152 2946 2596 2787 98 -51 -153 C ATOM 1047 CG LYS A 152 24.310 7.635 24.335 1.00 26.84 C ANISOU 1047 CG LYS A 152 3271 3483 3445 -31 89 163 C ATOM 1048 CD LYS A 152 24.339 6.672 23.162 1.00 31.81 C ANISOU 1048 CD LYS A 152 4156 4024 3906 -72 28 -146 C ATOM 1049 CE LYS A 152 25.234 5.476 23.421 1.00 35.69 C ANISOU 1049 CE LYS A 152 4488 4443 4630 58 -30 83 C ATOM 1050 NZ LYS A 152 25.409 4.641 22.199 1.00 38.15 N ANISOU 1050 NZ LYS A 152 4890 4814 4793 8 23 -43 N ATOM 1051 N PHE A 153 24.642 9.714 27.606 1.00 15.74 N ANISOU 1051 N PHE A 153 2011 1999 1969 10 1 13 N ATOM 1052 CA PHE A 153 25.888 9.826 28.361 1.00 15.52 C ANISOU 1052 CA PHE A 153 2001 1947 1950 0 3 -10 C ATOM 1053 C PHE A 153 25.731 9.366 29.805 1.00 15.72 C ANISOU 1053 C PHE A 153 2009 2003 1963 3 3 0 C ATOM 1054 O PHE A 153 26.681 8.875 30.413 1.00 15.92 O ANISOU 1054 O PHE A 153 2052 2062 1935 27 1 -4 O ATOM 1055 CB PHE A 153 26.473 11.232 28.304 1.00 14.93 C ANISOU 1055 CB PHE A 153 1895 1928 1850 8 -25 -2 C ATOM 1056 CG PHE A 153 25.602 12.333 28.829 1.00 15.41 C ANISOU 1056 CG PHE A 153 1972 1950 1931 21 0 -26 C ATOM 1057 CD1 PHE A 153 25.511 12.596 30.188 1.00 14.83 C ANISOU 1057 CD1 PHE A 153 1827 1918 1892 -6 -44 -9 C ATOM 1058 CD2 PHE A 153 24.870 13.120 27.955 1.00 15.44 C ANISOU 1058 CD2 PHE A 153 1956 1977 1934 -14 -16 -5 C ATOM 1059 CE1 PHE A 153 24.703 13.614 30.655 1.00 15.40 C ANISOU 1059 CE1 PHE A 153 1986 1911 1954 -5 -1 -47 C ATOM 1060 CE2 PHE A 153 24.060 14.137 28.414 1.00 15.69 C ANISOU 1060 CE2 PHE A 153 2007 1957 1996 -12 -35 -27 C ATOM 1061 CZ PHE A 153 23.975 14.386 29.772 1.00 16.32 C ANISOU 1061 CZ PHE A 153 2104 2091 2005 18 -11 22 C ATOM 1062 N TRP A 154 24.538 9.509 30.357 1.00 15.53 N ANISOU 1062 N TRP A 154 1981 1998 1923 -9 -21 -8 N ATOM 1063 CA TRP A 154 24.204 9.098 31.705 1.00 16.13 C ANISOU 1063 CA TRP A 154 2057 2080 1992 2 28 4 C ATOM 1064 C TRP A 154 24.034 7.599 31.897 1.00 17.02 C ANISOU 1064 C TRP A 154 2180 2132 2155 2 10 22 C ATOM 1065 O TRP A 154 23.937 7.139 33.039 1.00 17.19 O ANISOU 1065 O TRP A 154 2226 2162 2142 3 -4 3 O ATOM 1066 CB TRP A 154 22.873 9.773 32.070 1.00 16.06 C ANISOU 1066 CB TRP A 154 2018 2114 1969 -12 11 40 C ATOM 1067 CG TRP A 154 21.799 9.524 31.050 1.00 15.56 C ANISOU 1067 CG TRP A 154 1992 1949 1973 50 18 -4 C ATOM 1068 CD1 TRP A 154 21.102 8.369 30.847 1.00 16.53 C ANISOU 1068 CD1 TRP A 154 2087 2085 2110 -55 -2 -1 C ATOM 1069 CD2 TRP A 154 21.265 10.478 30.125 1.00 15.08 C ANISOU 1069 CD2 TRP A 154 1962 1930 1837 -3 24 -17 C ATOM 1070 NE1 TRP A 154 20.182 8.538 29.844 1.00 16.75 N ANISOU 1070 NE1 TRP A 154 2103 2091 2169 -46 -31 44 N ATOM 1071 CE2 TRP A 154 20.260 9.826 29.384 1.00 15.77 C ANISOU 1071 CE2 TRP A 154 1962 2001 2030 -18 -3 -37 C ATOM 1072 CE3 TRP A 154 21.547 11.819 29.849 1.00 15.25 C ANISOU 1072 CE3 TRP A 154 1946 1943 1905 -5 36 -10 C ATOM 1073 CZ2 TRP A 154 19.533 10.473 28.388 1.00 16.40 C ANISOU 1073 CZ2 TRP A 154 2143 2057 2031 -3 -32 -28 C ATOM 1074 CZ3 TRP A 154 20.826 12.458 28.858 1.00 16.05 C ANISOU 1074 CZ3 TRP A 154 2084 2021 1994 21 -14 21 C ATOM 1075 CH2 TRP A 154 19.831 11.782 28.135 1.00 16.68 C ANISOU 1075 CH2 TRP A 154 2107 2103 2128 -52 -7 4 C ATOM 1076 N LEU A 155 23.921 6.844 30.810 1.00 17.75 N ANISOU 1076 N LEU A 155 2280 2276 2189 1 7 -29 N ATOM 1077 CA LEU A 155 23.622 5.423 30.889 1.00 19.26 C ANISOU 1077 CA LEU A 155 2529 2366 2424 -6 29 14 C ATOM 1078 C LEU A 155 24.727 4.588 30.258 1.00 19.63 C ANISOU 1078 C LEU A 155 2534 2437 2489 8 -6 -27 C ATOM 1079 O LEU A 155 25.090 3.534 30.775 1.00 20.15 O ANISOU 1079 O LEU A 155 2644 2468 2543 -12 -34 -3 O ATOM 1080 CB LEU A 155 22.270 5.139 30.237 1.00 21.91 C ANISOU 1080 CB LEU A 155 2636 2930 2759 19 -59 -34 C ATOM 1081 CG LEU A 155 21.758 3.691 30.275 1.00 25.39 C ANISOU 1081 CG LEU A 155 3300 3076 3273 -38 42 27 C ATOM 1082 CD1 LEU A 155 21.553 3.248 31.727 1.00 25.45 C ANISOU 1082 CD1 LEU A 155 3225 3222 3224 1 0 7 C ATOM 1083 CD2 LEU A 155 20.400 3.617 29.555 1.00 27.49 C ANISOU 1083 CD2 LEU A 155 3466 3519 3461 -15 -39 8 C ATOM 1084 N GLU A 156 25.270 5.055 29.139 1.00 20.18 N ANISOU 1084 N GLU A 156 2583 2513 2574 -23 12 11 N ATOM 1085 CA GLU A 156 26.283 4.296 28.413 1.00 21.35 C ANISOU 1085 CA GLU A 156 2683 2644 2787 46 68 33 C ATOM 1086 C GLU A 156 27.574 5.081 28.231 1.00 21.13 C ANISOU 1086 C GLU A 156 2669 2622 2738 -5 10 -8 C ATOM 1087 O GLU A 156 28.562 4.538 27.725 1.00 21.79 O ANISOU 1087 O GLU A 156 2761 2708 2811 28 30 -33 O ATOM 1088 CB GLU A 156 25.750 3.872 27.041 1.00 25.81 C ANISOU 1088 CB GLU A 156 3404 3413 2991 110 -69 -84 C ATOM 1089 CG GLU A 156 24.712 2.766 27.090 1.00 31.61 C ANISOU 1089 CG GLU A 156 3888 3849 4275 -97 87 51 C ATOM 1090 CD GLU A 156 24.201 2.361 25.724 1.00 36.70 C ANISOU 1090 CD GLU A 156 4756 4644 4545 32 -100 -70 C ATOM 1091 OE1 GLU A 156 24.888 2.638 24.719 1.00 38.09 O ANISOU 1091 OE1 GLU A 156 4859 4829 4787 -10 32 9 O ATOM 1092 OE2 GLU A 156 23.107 1.760 25.669 1.00 38.48 O ANISOU 1092 OE2 GLU A 156 4894 4839 4889 -15 -5 -11 O ATOM 1093 N GLY A 157 27.571 6.345 28.633 1.00 20.32 N ANISOU 1093 N GLY A 157 2567 2583 2569 -3 7 18 N ATOM 1094 CA GLY A 157 28.680 7.243 28.370 1.00 20.01 C ANISOU 1094 CA GLY A 157 2538 2555 2510 6 -20 -8 C ATOM 1095 C GLY A 157 29.647 7.373 29.539 1.00 19.54 C ANISOU 1095 C GLY A 157 2507 2453 2465 7 3 2 C ATOM 1096 O GLY A 157 29.834 6.450 30.331 1.00 18.80 O ANISOU 1096 O GLY A 157 2407 2386 2352 10 6 -42 O ATOM 1097 N GLN A 158 30.260 8.551 29.646 1.00 19.43 N ANISOU 1097 N GLN A 158 2486 2456 2442 4 -19 -15 N ATOM 1098 CA GLN A 158 31.383 8.752 30.550 1.00 19.14 C ANISOU 1098 CA GLN A 158 2477 2421 2375 45 -12 -68 C ATOM 1099 C GLN A 158 31.005 9.443 31.854 1.00 17.76 C ANISOU 1099 C GLN A 158 2225 2253 2269 6 -5 10 C ATOM 1100 O GLN A 158 31.876 9.640 32.706 1.00 17.52 O ANISOU 1100 O GLN A 158 2194 2233 2228 22 6 29 O ATOM 1101 CB GLN A 158 32.481 9.566 29.853 1.00 22.33 C ANISOU 1101 CB GLN A 158 2724 2821 2939 -119 11 119 C ATOM 1102 CG GLN A 158 33.059 8.922 28.607 1.00 26.83 C ANISOU 1102 CG GLN A 158 3381 3568 3246 -28 83 -107 C ATOM 1103 CD GLN A 158 33.551 7.510 28.843 1.00 31.81 C ANISOU 1103 CD GLN A 158 4063 3932 4092 116 66 90 C ATOM 1104 OE1 GLN A 158 33.042 6.562 28.240 1.00 34.15 O ANISOU 1104 OE1 GLN A 158 4370 4245 4360 -56 -25 -60 O ATOM 1105 NE2 GLN A 158 34.531 7.364 29.727 1.00 32.74 N ANISOU 1105 NE2 GLN A 158 4160 4152 4129 14 -8 9 N ATOM 1106 N LEU A 159 29.739 9.802 32.011 1.00 16.80 N ANISOU 1106 N LEU A 159 2172 2118 2096 -2 -3 0 N ATOM 1107 CA LEU A 159 29.306 10.519 33.206 1.00 16.05 C ANISOU 1107 CA LEU A 159 2040 2024 2037 -2 -15 28 C ATOM 1108 C LEU A 159 29.307 9.615 34.430 1.00 15.67 C ANISOU 1108 C LEU A 159 1986 2001 1968 3 -15 -11 C ATOM 1109 O LEU A 159 28.828 8.487 34.400 1.00 15.58 O ANISOU 1109 O LEU A 159 1972 2027 1920 -18 -37 15 O ATOM 1110 CB LEU A 159 27.927 11.145 33.005 1.00 15.78 C ANISOU 1110 CB LEU A 159 2022 2023 1952 17 -3 -51 C ATOM 1111 CG LEU A 159 27.395 12.000 34.160 1.00 14.36 C ANISOU 1111 CG LEU A 159 1729 1853 1874 -9 -41 1 C ATOM 1112 CD1 LEU A 159 28.343 13.150 34.474 1.00 13.90 C ANISOU 1112 CD1 LEU A 159 1838 1725 1717 -7 -13 35 C ATOM 1113 CD2 LEU A 159 26.005 12.529 33.835 1.00 12.66 C ANISOU 1113 CD2 LEU A 159 1638 1601 1569 -45 18 16 C ATOM 1114 N ARG A 160 29.921 10.101 35.506 1.00 15.32 N ANISOU 1114 N ARG A 160 1939 1964 1918 18 -10 27 N ATOM 1115 CA ARG A 160 30.041 9.359 36.754 1.00 14.92 C ANISOU 1115 CA ARG A 160 1883 1902 1885 19 -1 2 C ATOM 1116 C ARG A 160 29.749 10.287 37.934 1.00 14.73 C ANISOU 1116 C ARG A 160 1885 1891 1822 -21 -4 29 C ATOM 1117 O ARG A 160 30.146 11.451 37.916 1.00 14.94 O ANISOU 1117 O ARG A 160 1964 1905 1809 -40 -14 46 O ATOM 1118 CB ARG A 160 31.437 8.768 36.928 1.00 14.62 C ANISOU 1118 CB ARG A 160 1837 1852 1865 -16 14 17 C ATOM 1119 CG ARG A 160 31.964 7.815 35.883 1.00 15.40 C ANISOU 1119 CG ARG A 160 1982 1991 1878 34 22 -10 C ATOM 1120 CD ARG A 160 31.210 6.502 35.816 1.00 16.89 C ANISOU 1120 CD ARG A 160 2147 2108 2164 -38 -51 29 C ATOM 1121 NE ARG A 160 31.763 5.601 34.811 1.00 18.53 N ANISOU 1121 NE ARG A 160 2397 2288 2354 56 31 -33 N ATOM 1122 CZ ARG A 160 31.412 5.548 33.533 1.00 19.83 C ANISOU 1122 CZ ARG A 160 2548 2539 2449 39 -44 5 C ATOM 1123 NH1 ARG A 160 30.466 6.341 33.048 1.00 18.93 N ANISOU 1123 NH1 ARG A 160 2373 2451 2370 -20 19 -17 N ATOM 1124 NH2 ARG A 160 32.003 4.682 32.717 1.00 20.14 N ANISOU 1124 NH2 ARG A 160 2589 2587 2475 28 2 -12 N ATOM 1125 N ILE A 161 29.061 9.778 38.950 1.00 14.26 N ANISOU 1125 N ILE A 161 1828 1834 1757 5 -15 12 N ATOM 1126 CA ILE A 161 28.794 10.555 40.158 1.00 13.89 C ANISOU 1126 CA ILE A 161 1793 1755 1729 -13 -37 27 C ATOM 1127 C ILE A 161 28.791 9.620 41.364 1.00 13.51 C ANISOU 1127 C ILE A 161 1746 1707 1680 -18 -32 -6 C ATOM 1128 O ILE A 161 28.481 8.437 41.221 1.00 13.53 O ANISOU 1128 O ILE A 161 1721 1692 1728 7 -53 26 O ATOM 1129 CB ILE A 161 27.483 11.350 40.057 1.00 14.52 C ANISOU 1129 CB ILE A 161 1811 1876 1830 22 30 -36 C ATOM 1130 CG1 ILE A 161 27.335 12.331 41.224 1.00 13.89 C ANISOU 1130 CG1 ILE A 161 1725 1754 1798 17 -26 -4 C ATOM 1131 CG2 ILE A 161 26.276 10.421 39.985 1.00 14.93 C ANISOU 1131 CG2 ILE A 161 1924 1858 1889 -26 -33 7 C ATOM 1132 CD1 ILE A 161 26.204 13.324 41.086 1.00 13.23 C ANISOU 1132 CD1 ILE A 161 1637 1675 1714 -40 -58 -30 C ATOM 1133 N SER A 162 29.178 10.139 42.526 1.00 13.02 N ANISOU 1133 N SER A 162 1654 1670 1623 -17 -33 33 N ATOM 1134 CA SER A 162 29.240 9.324 43.732 1.00 12.43 C ANISOU 1134 CA SER A 162 1553 1613 1556 -34 -46 -13 C ATOM 1135 C SER A 162 28.008 9.507 44.611 1.00 12.32 C ANISOU 1135 C SER A 162 1565 1572 1543 -28 -36 -12 C ATOM 1136 O SER A 162 27.239 10.448 44.438 1.00 12.50 O ANISOU 1136 O SER A 162 1589 1588 1573 -27 -35 -1 O ATOM 1137 CB SER A 162 30.467 9.715 44.564 1.00 11.43 C ANISOU 1137 CB SER A 162 1436 1450 1456 12 17 35 C ATOM 1138 OG SER A 162 30.258 10.938 45.247 1.00 12.10 O ANISOU 1138 OG SER A 162 1535 1534 1529 -8 -58 -52 O ATOM 1139 N ALA A 163 27.876 8.638 45.608 1.00 12.59 N ANISOU 1139 N ALA A 163 1632 1590 1561 -43 1 -4 N ATOM 1140 CA ALA A 163 26.815 8.756 46.600 1.00 12.53 C ANISOU 1140 CA ALA A 163 1600 1589 1572 0 -12 8 C ATOM 1141 C ALA A 163 26.942 10.055 47.389 1.00 12.73 C ANISOU 1141 C ALA A 163 1625 1603 1608 1 -3 1 C ATOM 1142 O ALA A 163 25.958 10.768 47.555 1.00 12.58 O ANISOU 1142 O ALA A 163 1625 1601 1553 -9 25 -44 O ATOM 1143 CB ALA A 163 26.836 7.566 47.548 1.00 12.43 C ANISOU 1143 CB ALA A 163 1595 1547 1581 -25 1 2 C ATOM 1144 N VAL A 164 28.157 10.381 47.834 1.00 12.87 N ANISOU 1144 N VAL A 164 1681 1658 1551 -36 -32 19 N ATOM 1145 CA VAL A 164 28.407 11.655 48.497 1.00 13.33 C ANISOU 1145 CA VAL A 164 1756 1647 1661 -17 14 16 C ATOM 1146 C VAL A 164 27.984 12.834 47.629 1.00 13.29 C ANISOU 1146 C VAL A 164 1703 1677 1668 -9 -13 16 C ATOM 1147 O VAL A 164 27.306 13.740 48.117 1.00 13.63 O ANISOU 1147 O VAL A 164 1782 1664 1731 22 -55 4 O ATOM 1148 CB VAL A 164 29.883 11.786 48.915 1.00 15.37 C ANISOU 1148 CB VAL A 164 1840 2033 1966 42 -46 3 C ATOM 1149 CG1 VAL A 164 30.261 13.213 49.280 1.00 17.35 C ANISOU 1149 CG1 VAL A 164 2222 2116 2256 -30 -13 8 C ATOM 1150 CG2 VAL A 164 30.164 10.862 50.098 1.00 15.72 C ANISOU 1150 CG2 VAL A 164 2014 1948 2009 16 -20 -1 C ATOM 1151 N ASN A 165 28.347 12.822 46.352 1.00 13.26 N ANISOU 1151 N ASN A 165 1717 1676 1647 -34 -49 20 N ATOM 1152 CA ASN A 165 27.985 13.920 45.456 1.00 12.99 C ANISOU 1152 CA ASN A 165 1662 1644 1629 -2 -12 4 C ATOM 1153 C ASN A 165 26.481 13.989 45.231 1.00 12.72 C ANISOU 1153 C ASN A 165 1650 1599 1583 4 -24 2 C ATOM 1154 O ASN A 165 25.914 15.084 45.148 1.00 12.26 O ANISOU 1154 O ASN A 165 1623 1525 1512 -38 -31 -40 O ATOM 1155 CB ASN A 165 28.736 13.788 44.138 1.00 12.77 C ANISOU 1155 CB ASN A 165 1633 1633 1587 8 -41 -37 C ATOM 1156 CG ASN A 165 28.793 15.044 43.301 1.00 13.15 C ANISOU 1156 CG ASN A 165 1692 1697 1608 -78 -1 -9 C ATOM 1157 OD1 ASN A 165 28.007 15.986 43.426 1.00 15.55 O ANISOU 1157 OD1 ASN A 165 2002 1934 1973 93 -93 -37 O ATOM 1158 ND2 ASN A 165 29.770 15.071 42.403 1.00 12.36 N ANISOU 1158 ND2 ASN A 165 1668 1581 1446 -66 -55 30 N ATOM 1159 N GLN A 166 25.810 12.839 45.151 1.00 12.87 N ANISOU 1159 N GLN A 166 1656 1643 1594 -26 -35 18 N ATOM 1160 CA GLN A 166 24.351 12.827 45.056 1.00 12.96 C ANISOU 1160 CA GLN A 166 1648 1637 1640 -19 -15 14 C ATOM 1161 C GLN A 166 23.717 13.530 46.248 1.00 13.23 C ANISOU 1161 C GLN A 166 1680 1675 1670 3 -18 -2 C ATOM 1162 O GLN A 166 22.835 14.374 46.082 1.00 12.77 O ANISOU 1162 O GLN A 166 1679 1580 1593 -30 -53 12 O ATOM 1163 CB GLN A 166 23.823 11.402 44.898 1.00 12.82 C ANISOU 1163 CB GLN A 166 1629 1604 1637 18 -11 15 C ATOM 1164 CG GLN A 166 24.216 10.723 43.599 1.00 12.78 C ANISOU 1164 CG GLN A 166 1575 1631 1650 -5 -52 -36 C ATOM 1165 CD GLN A 166 23.135 10.700 42.540 1.00 12.35 C ANISOU 1165 CD GLN A 166 1542 1534 1615 61 -15 31 C ATOM 1166 OE1 GLN A 166 23.133 9.799 41.690 1.00 13.56 O ANISOU 1166 OE1 GLN A 166 1768 1782 1602 -62 -30 -67 O ATOM 1167 NE2 GLN A 166 22.215 11.650 42.576 1.00 9.90 N ANISOU 1167 NE2 GLN A 166 1336 1342 1084 -42 -83 -60 N ATOM 1168 N VAL A 167 24.173 13.224 47.462 1.00 13.61 N ANISOU 1168 N VAL A 167 1734 1746 1690 -23 -39 18 N ATOM 1169 CA VAL A 167 23.703 13.909 48.662 1.00 14.32 C ANISOU 1169 CA VAL A 167 1803 1810 1829 5 0 -53 C ATOM 1170 C VAL A 167 23.935 15.411 48.612 1.00 14.48 C ANISOU 1170 C VAL A 167 1846 1823 1834 4 -34 -7 C ATOM 1171 O VAL A 167 23.034 16.184 48.947 1.00 14.56 O ANISOU 1171 O VAL A 167 1849 1834 1850 -10 -45 -61 O ATOM 1172 CB VAL A 167 24.371 13.302 49.913 1.00 16.13 C ANISOU 1172 CB VAL A 167 2164 2027 1937 12 -14 88 C ATOM 1173 CG1 VAL A 167 24.204 14.174 51.147 1.00 16.86 C ANISOU 1173 CG1 VAL A 167 2192 2104 2111 13 -3 -26 C ATOM 1174 CG2 VAL A 167 23.775 11.920 50.171 1.00 16.07 C ANISOU 1174 CG2 VAL A 167 2070 2012 2023 10 1 -19 C ATOM 1175 N GLU A 168 25.125 15.848 48.216 1.00 14.94 N ANISOU 1175 N GLU A 168 1907 1884 1884 -33 -30 12 N ATOM 1176 CA GLU A 168 25.431 17.272 48.118 1.00 15.16 C ANISOU 1176 CA GLU A 168 1999 1869 1890 16 -55 9 C ATOM 1177 C GLU A 168 24.514 17.973 47.123 1.00 14.66 C ANISOU 1177 C GLU A 168 1901 1840 1830 -4 -30 -23 C ATOM 1178 O GLU A 168 23.929 19.015 47.412 1.00 14.77 O ANISOU 1178 O GLU A 168 1912 1843 1856 -3 -64 -37 O ATOM 1179 CB GLU A 168 26.895 17.473 47.721 1.00 17.60 C ANISOU 1179 CB GLU A 168 2144 2240 2305 -54 60 -51 C ATOM 1180 CG GLU A 168 27.870 16.926 48.754 1.00 20.45 C ANISOU 1180 CG GLU A 168 2641 2578 2551 43 -119 47 C ATOM 1181 CD GLU A 168 29.306 16.915 48.271 1.00 23.03 C ANISOU 1181 CD GLU A 168 2848 2922 2980 4 61 4 C ATOM 1182 OE1 GLU A 168 29.544 16.838 47.048 1.00 23.79 O ANISOU 1182 OE1 GLU A 168 2997 3043 3000 -17 9 -7 O ATOM 1183 OE2 GLU A 168 30.206 16.971 49.139 1.00 24.21 O ANISOU 1183 OE2 GLU A 168 3045 3025 3127 1 -66 -62 O ATOM 1184 N PHE A 169 24.344 17.367 45.953 1.00 14.03 N ANISOU 1184 N PHE A 169 1782 1770 1780 -7 -9 9 N ATOM 1185 CA PHE A 169 23.440 17.881 44.932 1.00 13.82 C ANISOU 1185 CA PHE A 169 1772 1736 1741 -13 5 2 C ATOM 1186 C PHE A 169 22.002 17.976 45.413 1.00 13.37 C ANISOU 1186 C PHE A 169 1751 1657 1674 -15 -15 1 C ATOM 1187 O PHE A 169 21.331 18.999 45.234 1.00 13.67 O ANISOU 1187 O PHE A 169 1839 1678 1676 8 -67 -12 O ATOM 1188 CB PHE A 169 23.551 16.981 43.692 1.00 14.26 C ANISOU 1188 CB PHE A 169 1816 1827 1774 -4 -3 -43 C ATOM 1189 CG PHE A 169 22.587 17.325 42.595 1.00 14.55 C ANISOU 1189 CG PHE A 169 1888 1822 1818 -21 -31 14 C ATOM 1190 CD1 PHE A 169 22.767 18.463 41.824 1.00 14.49 C ANISOU 1190 CD1 PHE A 169 1910 1788 1806 -78 -24 -15 C ATOM 1191 CD2 PHE A 169 21.501 16.508 42.331 1.00 14.37 C ANISOU 1191 CD2 PHE A 169 1873 1795 1793 -16 -16 19 C ATOM 1192 CE1 PHE A 169 21.879 18.781 40.817 1.00 14.88 C ANISOU 1192 CE1 PHE A 169 1808 1893 1953 -13 -21 2 C ATOM 1193 CE2 PHE A 169 20.609 16.823 41.325 1.00 14.16 C ANISOU 1193 CE2 PHE A 169 1839 1791 1748 -20 4 -3 C ATOM 1194 CZ PHE A 169 20.796 17.958 40.565 1.00 14.19 C ANISOU 1194 CZ PHE A 169 1858 1730 1805 -5 -18 -19 C ATOM 1195 N LEU A 170 21.496 16.919 46.048 1.00 12.77 N ANISOU 1195 N LEU A 170 1659 1639 1555 -25 -29 -25 N ATOM 1196 CA LEU A 170 20.122 16.892 46.524 1.00 12.60 C ANISOU 1196 CA LEU A 170 1656 1562 1568 -19 -18 7 C ATOM 1197 C LEU A 170 19.896 17.868 47.671 1.00 13.02 C ANISOU 1197 C LEU A 170 1708 1630 1610 -12 -5 -16 C ATOM 1198 O LEU A 170 18.827 18.465 47.766 1.00 13.54 O ANISOU 1198 O LEU A 170 1791 1639 1716 38 -66 -23 O ATOM 1199 CB LEU A 170 19.709 15.477 46.935 1.00 12.04 C ANISOU 1199 CB LEU A 170 1490 1545 1538 6 -8 36 C ATOM 1200 CG LEU A 170 19.656 14.456 45.791 1.00 13.60 C ANISOU 1200 CG LEU A 170 1794 1711 1663 29 6 -56 C ATOM 1201 CD1 LEU A 170 19.499 13.050 46.350 1.00 14.55 C ANISOU 1201 CD1 LEU A 170 1873 1750 1907 -27 -22 -25 C ATOM 1202 CD2 LEU A 170 18.529 14.780 44.822 1.00 14.22 C ANISOU 1202 CD2 LEU A 170 1836 1804 1763 20 -37 -46 C ATOM 1203 N GLU A 171 20.889 18.022 48.544 1.00 13.34 N ANISOU 1203 N GLU A 171 1724 1660 1684 -23 -33 -6 N ATOM 1204 CA GLU A 171 20.821 19.042 49.587 1.00 13.96 C ANISOU 1204 CA GLU A 171 1841 1713 1750 2 18 -23 C ATOM 1205 C GLU A 171 20.657 20.433 48.986 1.00 13.58 C ANISOU 1205 C GLU A 171 1735 1711 1713 -9 -25 -21 C ATOM 1206 O GLU A 171 19.811 21.222 49.403 1.00 13.85 O ANISOU 1206 O GLU A 171 1757 1743 1763 6 -45 -51 O ATOM 1207 CB GLU A 171 22.093 18.993 50.441 1.00 16.77 C ANISOU 1207 CB GLU A 171 1996 2210 2168 5 -114 81 C ATOM 1208 CG GLU A 171 22.136 20.041 51.546 1.00 20.58 C ANISOU 1208 CG GLU A 171 2804 2479 2537 -16 35 -96 C ATOM 1209 CD GLU A 171 23.441 19.978 52.323 1.00 23.82 C ANISOU 1209 CD GLU A 171 2974 3027 3051 -4 -91 -12 C ATOM 1210 OE1 GLU A 171 24.506 19.794 51.700 1.00 24.77 O ANISOU 1210 OE1 GLU A 171 3098 3206 3107 -35 5 -28 O ATOM 1211 OE2 GLU A 171 23.398 20.107 53.562 1.00 24.87 O ANISOU 1211 OE2 GLU A 171 3197 3150 3103 -16 -19 -2 O ATOM 1212 N SER A 172 21.487 20.753 48.000 1.00 13.50 N ANISOU 1212 N SER A 172 1751 1704 1675 -9 -40 -19 N ATOM 1213 CA SER A 172 21.392 22.019 47.284 1.00 13.63 C ANISOU 1213 CA SER A 172 1759 1697 1723 -16 -39 -16 C ATOM 1214 C SER A 172 19.999 22.210 46.700 1.00 13.57 C ANISOU 1214 C SER A 172 1753 1684 1721 -18 -46 -22 C ATOM 1215 O SER A 172 19.384 23.262 46.873 1.00 13.87 O ANISOU 1215 O SER A 172 1803 1688 1777 -26 -55 -109 O ATOM 1216 CB SER A 172 22.451 22.105 46.185 1.00 14.85 C ANISOU 1216 CB SER A 172 1923 1845 1876 -12 81 -13 C ATOM 1217 OG SER A 172 23.749 22.146 46.750 1.00 16.94 O ANISOU 1217 OG SER A 172 2119 2131 2185 -15 -104 -6 O ATOM 1218 N LEU A 173 19.476 21.180 46.030 1.00 13.26 N ANISOU 1218 N LEU A 173 1722 1653 1661 -6 -23 -24 N ATOM 1219 CA LEU A 173 18.106 21.225 45.534 1.00 12.93 C ANISOU 1219 CA LEU A 173 1696 1558 1657 -14 -29 -49 C ATOM 1220 C LEU A 173 17.107 21.501 46.647 1.00 13.37 C ANISOU 1220 C LEU A 173 1725 1656 1700 -4 -11 -26 C ATOM 1221 O LEU A 173 16.248 22.379 46.537 1.00 13.51 O ANISOU 1221 O LEU A 173 1768 1643 1722 -2 -15 -28 O ATOM 1222 CB LEU A 173 17.746 19.917 44.819 1.00 11.95 C ANISOU 1222 CB LEU A 173 1544 1500 1496 14 -38 -1 C ATOM 1223 CG LEU A 173 16.315 19.794 44.288 1.00 11.77 C ANISOU 1223 CG LEU A 173 1528 1428 1517 42 -26 4 C ATOM 1224 CD1 LEU A 173 15.997 20.908 43.298 1.00 11.73 C ANISOU 1224 CD1 LEU A 173 1581 1432 1444 -15 -12 -3 C ATOM 1225 CD2 LEU A 173 16.110 18.424 43.648 1.00 12.49 C ANISOU 1225 CD2 LEU A 173 1657 1524 1565 10 -35 -72 C ATOM 1226 N TYR A 174 17.215 20.759 47.746 1.00 13.96 N ANISOU 1226 N TYR A 174 1834 1716 1753 -36 -16 8 N ATOM 1227 CA TYR A 174 16.357 20.929 48.905 1.00 14.62 C ANISOU 1227 CA TYR A 174 1880 1840 1836 -16 5 -41 C ATOM 1228 C TYR A 174 16.332 22.374 49.390 1.00 14.94 C ANISOU 1228 C TYR A 174 1945 1859 1872 14 4 -34 C ATOM 1229 O TYR A 174 15.257 22.926 49.624 1.00 14.61 O ANISOU 1229 O TYR A 174 1932 1835 1784 -8 -8 -54 O ATOM 1230 CB TYR A 174 16.807 19.988 50.030 1.00 15.52 C ANISOU 1230 CB TYR A 174 2039 1863 1995 -10 -32 17 C ATOM 1231 CG TYR A 174 16.010 20.143 51.307 1.00 17.19 C ANISOU 1231 CG TYR A 174 2229 2149 2152 30 48 12 C ATOM 1232 CD1 TYR A 174 14.761 19.557 51.446 1.00 18.27 C ANISOU 1232 CD1 TYR A 174 2302 2278 2363 -28 5 3 C ATOM 1233 CD2 TYR A 174 16.511 20.882 52.370 1.00 17.82 C ANISOU 1233 CD2 TYR A 174 2297 2223 2250 -10 -33 1 C ATOM 1234 CE1 TYR A 174 14.031 19.702 52.612 1.00 19.13 C ANISOU 1234 CE1 TYR A 174 2427 2414 2427 -3 32 17 C ATOM 1235 CE2 TYR A 174 15.791 21.033 53.540 1.00 18.73 C ANISOU 1235 CE2 TYR A 174 2414 2350 2351 31 6 -33 C ATOM 1236 CZ TYR A 174 14.555 20.437 53.655 1.00 19.52 C ANISOU 1236 CZ TYR A 174 2481 2461 2474 -20 -6 -3 C ATOM 1237 OH TYR A 174 13.825 20.588 54.813 1.00 20.59 O ANISOU 1237 OH TYR A 174 2638 2643 2543 18 29 0 O ATOM 1238 N LEU A 175 17.495 23.004 49.499 1.00 15.73 N ANISOU 1238 N LEU A 175 2001 2003 1975 -28 -15 -18 N ATOM 1239 CA LEU A 175 17.628 24.373 49.963 1.00 16.56 C ANISOU 1239 CA LEU A 175 2159 2029 2105 2 -5 -28 C ATOM 1240 C LEU A 175 17.422 25.433 48.896 1.00 17.04 C ANISOU 1240 C LEU A 175 2249 2106 2121 -6 -14 2 C ATOM 1241 O LEU A 175 17.539 26.638 49.152 1.00 17.29 O ANISOU 1241 O LEU A 175 2291 2138 2139 -25 -39 -43 O ATOM 1242 CB LEU A 175 19.041 24.561 50.548 1.00 18.22 C ANISOU 1242 CB LEU A 175 2233 2368 2320 7 -54 -47 C ATOM 1243 CG LEU A 175 19.391 23.642 51.721 1.00 19.25 C ANISOU 1243 CG LEU A 175 2449 2384 2482 -1 -28 37 C ATOM 1244 CD1 LEU A 175 20.863 23.777 52.083 1.00 18.96 C ANISOU 1244 CD1 LEU A 175 2425 2389 2388 -16 5 -39 C ATOM 1245 CD2 LEU A 175 18.504 23.946 52.919 1.00 20.49 C ANISOU 1245 CD2 LEU A 175 2632 2604 2551 -3 20 -13 C ATOM 1246 N ASN A 176 17.122 25.037 47.664 1.00 16.94 N ANISOU 1246 N ASN A 176 2203 2107 2127 -12 -17 -23 N ATOM 1247 CA ASN A 176 16.963 25.916 46.523 1.00 17.14 C ANISOU 1247 CA ASN A 176 2206 2156 2152 -46 -14 -1 C ATOM 1248 C ASN A 176 18.250 26.671 46.196 1.00 16.98 C ANISOU 1248 C ASN A 176 2188 2118 2146 -15 0 -19 C ATOM 1249 O ASN A 176 18.203 27.791 45.689 1.00 17.17 O ANISOU 1249 O ASN A 176 2199 2129 2197 -38 -19 8 O ATOM 1250 CB ASN A 176 15.807 26.902 46.701 1.00 18.65 C ANISOU 1250 CB ASN A 176 2391 2295 2400 38 21 -43 C ATOM 1251 CG ASN A 176 14.498 26.227 47.061 1.00 19.15 C ANISOU 1251 CG ASN A 176 2410 2419 2445 3 9 -9 C ATOM 1252 OD1 ASN A 176 13.963 25.427 46.301 1.00 19.24 O ANISOU 1252 OD1 ASN A 176 2505 2387 2417 -25 4 11 O ATOM 1253 ND2 ASN A 176 14.003 26.552 48.252 1.00 19.31 N ANISOU 1253 ND2 ASN A 176 2524 2396 2417 1 -1 3 N ATOM 1254 N LYS A 177 19.390 26.025 46.397 1.00 16.96 N ANISOU 1254 N LYS A 177 2204 2100 2139 4 -18 -38 N ATOM 1255 CA LYS A 177 20.688 26.649 46.223 1.00 17.94 C ANISOU 1255 CA LYS A 177 2283 2215 2321 -34 51 -26 C ATOM 1256 C LYS A 177 21.367 26.253 44.919 1.00 17.70 C ANISOU 1256 C LYS A 177 2260 2184 2279 -22 0 -31 C ATOM 1257 O LYS A 177 22.484 26.701 44.650 1.00 18.11 O ANISOU 1257 O LYS A 177 2290 2239 2351 -48 5 -31 O ATOM 1258 CB LYS A 177 21.614 26.305 47.396 1.00 21.05 C ANISOU 1258 CB LYS A 177 2600 2697 2699 11 -144 136 C ATOM 1259 CG LYS A 177 21.306 27.047 48.685 1.00 25.54 C ANISOU 1259 CG LYS A 177 3353 3156 3195 -10 121 -124 C ATOM 1260 CD LYS A 177 22.308 26.661 49.764 1.00 29.84 C ANISOU 1260 CD LYS A 177 3694 3832 3810 23 -111 118 C ATOM 1261 CE LYS A 177 22.203 27.563 50.982 1.00 33.74 C ANISOU 1261 CE LYS A 177 4393 4208 4219 -6 68 -97 C ATOM 1262 NZ LYS A 177 23.270 27.254 51.977 1.00 35.88 N ANISOU 1262 NZ LYS A 177 4550 4542 4540 11 -36 7 N ATOM 1263 N LEU A 178 20.729 25.400 44.120 1.00 17.38 N ANISOU 1263 N LEU A 178 2218 2172 2214 -8 -8 -12 N ATOM 1264 CA LEU A 178 21.235 25.164 42.770 1.00 17.22 C ANISOU 1264 CA LEU A 178 2199 2147 2197 -50 -32 -43 C ATOM 1265 C LEU A 178 21.168 26.450 41.958 1.00 17.97 C ANISOU 1265 C LEU A 178 2307 2200 2319 -32 -32 -10 C ATOM 1266 O LEU A 178 20.323 27.310 42.218 1.00 18.00 O ANISOU 1266 O LEU A 178 2302 2207 2331 -34 -20 10 O ATOM 1267 CB LEU A 178 20.435 24.065 42.073 1.00 15.92 C ANISOU 1267 CB LEU A 178 2107 1953 1989 15 3 56 C ATOM 1268 CG LEU A 178 20.562 22.663 42.670 1.00 14.21 C ANISOU 1268 CG LEU A 178 1765 1812 1821 -28 -20 -27 C ATOM 1269 CD1 LEU A 178 19.691 21.683 41.889 1.00 13.95 C ANISOU 1269 CD1 LEU A 178 1790 1764 1745 -43 5 -9 C ATOM 1270 CD2 LEU A 178 22.009 22.193 42.668 1.00 14.15 C ANISOU 1270 CD2 LEU A 178 1753 1809 1815 -47 -48 29 C ATOM 1271 N SER A 179 22.019 26.558 40.941 1.00 18.98 N ANISOU 1271 N SER A 179 2439 2390 2380 -21 1 -16 N ATOM 1272 CA SER A 179 21.961 27.715 40.044 1.00 20.18 C ANISOU 1272 CA SER A 179 2697 2477 2492 31 -99 15 C ATOM 1273 C SER A 179 20.893 27.492 38.977 1.00 19.34 C ANISOU 1273 C SER A 179 2475 2418 2455 24 9 5 C ATOM 1274 O SER A 179 21.114 27.166 37.819 1.00 19.51 O ANISOU 1274 O SER A 179 2499 2433 2480 -6 -20 -42 O ATOM 1275 CB SER A 179 23.330 28.037 39.466 1.00 26.16 C ANISOU 1275 CB SER A 179 3118 3511 3312 -164 130 68 C ATOM 1276 OG SER A 179 24.114 26.874 39.302 1.00 31.33 O ANISOU 1276 OG SER A 179 3958 3881 4067 107 37 5 O ATOM 1277 N ALA A 180 19.663 27.691 39.417 1.00 18.40 N ANISOU 1277 N ALA A 180 2368 2287 2338 -19 -37 13 N ATOM 1278 CA ALA A 180 18.435 27.555 38.668 1.00 18.03 C ANISOU 1278 CA ALA A 180 2296 2260 2295 18 22 15 C ATOM 1279 C ALA A 180 17.386 28.350 39.445 1.00 17.09 C ANISOU 1279 C ALA A 180 2170 2145 2177 -22 -33 26 C ATOM 1280 O ALA A 180 17.624 28.627 40.628 1.00 17.26 O ANISOU 1280 O ALA A 180 2195 2185 2176 -1 -37 30 O ATOM 1281 CB ALA A 180 18.021 26.097 38.546 1.00 19.39 C ANISOU 1281 CB ALA A 180 2537 2333 2498 -43 2 -8 C ATOM 1282 N SER A 181 16.281 28.715 38.816 1.00 16.26 N ANISOU 1282 N SER A 181 2129 2000 2051 -12 8 14 N ATOM 1283 CA SER A 181 15.260 29.472 39.537 1.00 16.02 C ANISOU 1283 CA SER A 181 2088 2006 1994 -34 15 11 C ATOM 1284 C SER A 181 14.729 28.645 40.704 1.00 15.50 C ANISOU 1284 C SER A 181 2006 1931 1952 -1 -1 -8 C ATOM 1285 O SER A 181 14.703 27.416 40.641 1.00 15.48 O ANISOU 1285 O SER A 181 2032 1915 1934 -3 -34 16 O ATOM 1286 CB SER A 181 14.109 29.870 38.615 1.00 16.95 C ANISOU 1286 CB SER A 181 2135 2161 2146 14 -33 2 C ATOM 1287 OG SER A 181 13.348 28.736 38.240 1.00 17.52 O ANISOU 1287 OG SER A 181 2299 2178 2179 -64 12 9 O ATOM 1288 N LYS A 182 14.264 29.322 41.752 1.00 15.24 N ANISOU 1288 N LYS A 182 1945 1904 1941 -24 2 -2 N ATOM 1289 CA LYS A 182 13.580 28.614 42.834 1.00 15.28 C ANISOU 1289 CA LYS A 182 1913 1938 1954 -14 -19 50 C ATOM 1290 C LYS A 182 12.312 27.933 42.333 1.00 14.96 C ANISOU 1290 C LYS A 182 1923 1879 1881 -3 -15 -9 C ATOM 1291 O LYS A 182 12.032 26.793 42.717 1.00 15.20 O ANISOU 1291 O LYS A 182 1955 1921 1901 -57 -15 -1 O ATOM 1292 CB LYS A 182 13.273 29.544 44.012 1.00 18.19 C ANISOU 1292 CB LYS A 182 2409 2254 2248 63 -20 -160 C ATOM 1293 CG LYS A 182 12.511 28.834 45.120 1.00 21.65 C ANISOU 1293 CG LYS A 182 2716 2716 2794 -53 104 99 C ATOM 1294 CD LYS A 182 12.797 29.413 46.498 1.00 25.18 C ANISOU 1294 CD LYS A 182 3284 3234 3050 -11 -41 -76 C ATOM 1295 CE LYS A 182 11.790 28.870 47.501 1.00 26.13 C ANISOU 1295 CE LYS A 182 3304 3317 3307 6 21 13 C ATOM 1296 NZ LYS A 182 12.027 29.355 48.886 1.00 26.07 N ANISOU 1296 NZ LYS A 182 3310 3272 3325 -7 -3 -5 N ATOM 1297 N GLU A 183 11.552 28.592 41.462 1.00 14.79 N ANISOU 1297 N GLU A 183 1908 1832 1879 9 0 -37 N ATOM 1298 CA GLU A 183 10.393 27.984 40.826 1.00 15.16 C ANISOU 1298 CA GLU A 183 1919 1885 1956 -30 26 -84 C ATOM 1299 C GLU A 183 10.713 26.621 40.218 1.00 14.20 C ANISOU 1299 C GLU A 183 1810 1811 1774 -38 5 -9 C ATOM 1300 O GLU A 183 10.031 25.634 40.495 1.00 13.71 O ANISOU 1300 O GLU A 183 1799 1735 1676 -18 -35 -16 O ATOM 1301 CB GLU A 183 9.843 28.884 39.714 1.00 18.92 C ANISOU 1301 CB GLU A 183 2446 2453 2288 -45 -109 181 C ATOM 1302 CG GLU A 183 9.085 30.104 40.205 1.00 24.17 C ANISOU 1302 CG GLU A 183 3046 2962 3176 74 84 -153 C ATOM 1303 CD GLU A 183 8.683 31.016 39.059 1.00 28.20 C ANISOU 1303 CD GLU A 183 3588 3613 3515 12 -39 141 C ATOM 1304 OE1 GLU A 183 8.624 30.545 37.902 1.00 28.51 O ANISOU 1304 OE1 GLU A 183 3662 3568 3603 29 -18 35 O ATOM 1305 OE2 GLU A 183 8.432 32.207 39.327 1.00 30.76 O ANISOU 1305 OE2 GLU A 183 3958 3800 3928 20 27 -33 O ATOM 1306 N ASN A 184 11.753 26.565 39.391 1.00 13.71 N ANISOU 1306 N ASN A 184 1781 1720 1707 -7 -22 -24 N ATOM 1307 CA ASN A 184 12.118 25.326 38.717 1.00 13.59 C ANISOU 1307 CA ASN A 184 1788 1685 1691 4 5 18 C ATOM 1308 C ASN A 184 12.593 24.255 39.686 1.00 13.55 C ANISOU 1308 C ASN A 184 1753 1696 1699 16 -26 4 C ATOM 1309 O ASN A 184 12.247 23.088 39.496 1.00 13.97 O ANISOU 1309 O ASN A 184 1828 1746 1734 -35 -17 -49 O ATOM 1310 CB ASN A 184 13.165 25.581 37.630 1.00 13.12 C ANISOU 1310 CB ASN A 184 1695 1598 1691 13 -11 -12 C ATOM 1311 CG ASN A 184 12.517 26.297 36.452 1.00 13.58 C ANISOU 1311 CG ASN A 184 1755 1710 1696 52 -25 -15 C ATOM 1312 OD1 ASN A 184 11.311 26.151 36.245 1.00 13.57 O ANISOU 1312 OD1 ASN A 184 1780 1748 1630 -22 -2 -21 O ATOM 1313 ND2 ASN A 184 13.315 27.047 35.706 1.00 14.92 N ANISOU 1313 ND2 ASN A 184 2001 1803 1865 -41 22 27 N ATOM 1314 N GLN A 185 13.328 24.634 40.726 1.00 13.30 N ANISOU 1314 N GLN A 185 1731 1648 1674 12 -3 -11 N ATOM 1315 CA GLN A 185 13.707 23.666 41.755 1.00 13.41 C ANISOU 1315 CA GLN A 185 1724 1669 1702 2 -27 -2 C ATOM 1316 C GLN A 185 12.500 23.136 42.505 1.00 13.42 C ANISOU 1316 C GLN A 185 1721 1671 1708 28 -14 -7 C ATOM 1317 O GLN A 185 12.405 21.930 42.765 1.00 13.60 O ANISOU 1317 O GLN A 185 1737 1653 1777 -6 -50 -33 O ATOM 1318 CB GLN A 185 14.740 24.301 42.690 1.00 13.96 C ANISOU 1318 CB GLN A 185 1764 1841 1700 -7 -30 -37 C ATOM 1319 CG GLN A 185 16.043 24.611 41.962 1.00 14.18 C ANISOU 1319 CG GLN A 185 1808 1782 1796 -32 6 -9 C ATOM 1320 CD GLN A 185 17.049 25.306 42.858 1.00 14.91 C ANISOU 1320 CD GLN A 185 1845 1984 1835 39 -105 -7 C ATOM 1321 OE1 GLN A 185 17.223 26.523 42.767 1.00 18.53 O ANISOU 1321 OE1 GLN A 185 2433 2168 2441 -57 -42 21 O ATOM 1322 NE2 GLN A 185 17.704 24.533 43.709 1.00 13.04 N ANISOU 1322 NE2 GLN A 185 1701 1668 1587 -65 20 -74 N ATOM 1323 N LEU A 186 11.542 24.001 42.843 1.00 12.93 N ANISOU 1323 N LEU A 186 1667 1631 1614 -4 -7 -16 N ATOM 1324 CA LEU A 186 10.302 23.565 43.468 1.00 12.84 C ANISOU 1324 CA LEU A 186 1669 1606 1605 -17 -21 6 C ATOM 1325 C LEU A 186 9.498 22.624 42.580 1.00 12.94 C ANISOU 1325 C LEU A 186 1694 1632 1592 -29 -14 -3 C ATOM 1326 O LEU A 186 8.919 21.653 43.072 1.00 12.88 O ANISOU 1326 O LEU A 186 1720 1601 1573 -15 -3 -18 O ATOM 1327 CB LEU A 186 9.442 24.770 43.858 1.00 13.54 C ANISOU 1327 CB LEU A 186 1727 1703 1714 31 15 -23 C ATOM 1328 CG LEU A 186 9.981 25.611 45.022 1.00 14.45 C ANISOU 1328 CG LEU A 186 1927 1743 1819 -29 -95 -9 C ATOM 1329 CD1 LEU A 186 9.246 26.938 45.106 1.00 14.67 C ANISOU 1329 CD1 LEU A 186 1902 1836 1836 34 8 -71 C ATOM 1330 CD2 LEU A 186 9.853 24.843 46.328 1.00 14.26 C ANISOU 1330 CD2 LEU A 186 1845 1833 1740 1 3 -48 C ATOM 1331 N ILE A 187 9.427 22.906 41.281 1.00 12.92 N ANISOU 1331 N ILE A 187 1687 1630 1592 -31 -18 -8 N ATOM 1332 CA ILE A 187 8.742 22.016 40.349 1.00 12.67 C ANISOU 1332 CA ILE A 187 1661 1579 1576 -11 0 -4 C ATOM 1333 C ILE A 187 9.325 20.612 40.384 1.00 12.27 C ANISOU 1333 C ILE A 187 1586 1569 1508 -19 0 13 C ATOM 1334 O ILE A 187 8.580 19.630 40.500 1.00 12.21 O ANISOU 1334 O ILE A 187 1584 1544 1510 -9 -3 26 O ATOM 1335 CB ILE A 187 8.765 22.581 38.918 1.00 13.38 C ANISOU 1335 CB ILE A 187 1815 1663 1608 8 -17 18 C ATOM 1336 CG1 ILE A 187 7.854 23.809 38.837 1.00 13.44 C ANISOU 1336 CG1 ILE A 187 1747 1706 1654 8 -6 -1 C ATOM 1337 CG2 ILE A 187 8.318 21.540 37.896 1.00 13.89 C ANISOU 1337 CG2 ILE A 187 1855 1687 1737 3 -41 -41 C ATOM 1338 CD1 ILE A 187 8.081 24.651 37.600 1.00 13.36 C ANISOU 1338 CD1 ILE A 187 1755 1677 1644 -11 -45 8 C ATOM 1339 N VAL A 188 10.647 20.497 40.280 1.00 12.10 N ANISOU 1339 N VAL A 188 1592 1544 1461 9 -8 24 N ATOM 1340 CA VAL A 188 11.280 19.181 40.237 1.00 12.37 C ANISOU 1340 CA VAL A 188 1620 1550 1532 9 -15 5 C ATOM 1341 C VAL A 188 11.158 18.515 41.603 1.00 12.39 C ANISOU 1341 C VAL A 188 1635 1538 1533 -7 -12 6 C ATOM 1342 O VAL A 188 10.940 17.306 41.673 1.00 12.37 O ANISOU 1342 O VAL A 188 1611 1531 1557 -4 -25 -16 O ATOM 1343 CB VAL A 188 12.741 19.243 39.778 1.00 13.10 C ANISOU 1343 CB VAL A 188 1666 1645 1668 9 41 -34 C ATOM 1344 CG1 VAL A 188 13.370 17.854 39.743 1.00 12.69 C ANISOU 1344 CG1 VAL A 188 1617 1622 1584 4 23 53 C ATOM 1345 CG2 VAL A 188 12.830 19.883 38.396 1.00 14.10 C ANISOU 1345 CG2 VAL A 188 1859 1782 1718 19 -5 3 C ATOM 1346 N LYS A 189 11.236 19.298 42.682 1.00 12.62 N ANISOU 1346 N LYS A 189 1678 1550 1565 -11 3 -12 N ATOM 1347 CA LYS A 189 10.999 18.716 44.006 1.00 12.86 C ANISOU 1347 CA LYS A 189 1664 1638 1585 -8 6 9 C ATOM 1348 C LYS A 189 9.635 18.062 44.112 1.00 12.72 C ANISOU 1348 C LYS A 189 1646 1622 1565 1 -14 -16 C ATOM 1349 O LYS A 189 9.559 16.900 44.541 1.00 13.41 O ANISOU 1349 O LYS A 189 1738 1658 1697 -26 -22 18 O ATOM 1350 CB LYS A 189 11.244 19.749 45.113 1.00 13.98 C ANISOU 1350 CB LYS A 189 1850 1754 1707 -2 24 -67 C ATOM 1351 CG LYS A 189 12.738 19.863 45.405 1.00 16.14 C ANISOU 1351 CG LYS A 189 1966 2077 2089 -27 -45 68 C ATOM 1352 CD LYS A 189 13.019 20.755 46.599 1.00 18.01 C ANISOU 1352 CD LYS A 189 2322 2265 2258 -42 11 -67 C ATOM 1353 CE LYS A 189 12.982 22.226 46.209 1.00 18.97 C ANISOU 1353 CE LYS A 189 2426 2360 2424 37 8 35 C ATOM 1354 NZ LYS A 189 13.302 23.090 47.385 1.00 19.96 N ANISOU 1354 NZ LYS A 189 2561 2499 2525 -23 -55 -24 N ATOM 1355 N GLU A 190 8.548 18.699 43.669 1.00 12.56 N ANISOU 1355 N GLU A 190 1645 1588 1540 -6 0 -30 N ATOM 1356 CA GLU A 190 7.246 18.055 43.781 1.00 12.83 C ANISOU 1356 CA GLU A 190 1668 1619 1588 -38 2 -58 C ATOM 1357 C GLU A 190 7.166 16.813 42.896 1.00 12.32 C ANISOU 1357 C GLU A 190 1588 1549 1544 4 17 -18 C ATOM 1358 O GLU A 190 6.553 15.816 43.279 1.00 12.37 O ANISOU 1358 O GLU A 190 1677 1506 1518 3 16 -60 O ATOM 1359 CB GLU A 190 6.059 18.973 43.483 1.00 14.74 C ANISOU 1359 CB GLU A 190 1858 1840 1903 68 -55 26 C ATOM 1360 CG GLU A 190 4.790 18.358 44.067 1.00 16.30 C ANISOU 1360 CG GLU A 190 2028 2089 2075 -58 26 2 C ATOM 1361 CD GLU A 190 3.522 19.114 43.756 1.00 17.26 C ANISOU 1361 CD GLU A 190 2164 2178 2215 43 33 12 C ATOM 1362 OE1 GLU A 190 2.965 18.898 42.657 1.00 18.80 O ANISOU 1362 OE1 GLU A 190 2413 2437 2292 -37 -30 -28 O ATOM 1363 OE2 GLU A 190 3.072 19.897 44.621 1.00 16.99 O ANISOU 1363 OE2 GLU A 190 2198 2169 2088 6 -63 -21 O ATOM 1364 N ALA A 191 7.843 16.827 41.753 1.00 12.34 N ANISOU 1364 N ALA A 191 1631 1537 1519 6 -3 -5 N ATOM 1365 CA ALA A 191 7.916 15.665 40.877 1.00 12.35 C ANISOU 1365 CA ALA A 191 1625 1537 1533 5 -3 -10 C ATOM 1366 C ALA A 191 8.619 14.471 41.509 1.00 12.66 C ANISOU 1366 C ALA A 191 1643 1596 1571 8 -70 9 C ATOM 1367 O ALA A 191 8.421 13.336 41.066 1.00 13.13 O ANISOU 1367 O ALA A 191 1763 1593 1633 18 -92 30 O ATOM 1368 CB ALA A 191 8.607 16.054 39.574 1.00 12.62 C ANISOU 1368 CB ALA A 191 1600 1629 1564 -4 4 -8 C ATOM 1369 N LEU A 192 9.445 14.687 42.524 1.00 11.89 N ANISOU 1369 N LEU A 192 1587 1468 1462 8 -20 11 N ATOM 1370 CA LEU A 192 10.165 13.636 43.213 1.00 11.34 C ANISOU 1370 CA LEU A 192 1475 1417 1416 -12 -11 -26 C ATOM 1371 C LEU A 192 9.456 13.092 44.442 1.00 11.11 C ANISOU 1371 C LEU A 192 1431 1402 1388 -20 -34 -33 C ATOM 1372 O LEU A 192 9.962 12.126 45.032 1.00 11.53 O ANISOU 1372 O LEU A 192 1498 1407 1476 -2 -52 -18 O ATOM 1373 CB LEU A 192 11.558 14.155 43.607 1.00 11.05 C ANISOU 1373 CB LEU A 192 1482 1336 1380 8 -31 -27 C ATOM 1374 CG LEU A 192 12.472 14.527 42.434 1.00 12.59 C ANISOU 1374 CG LEU A 192 1554 1638 1593 42 77 10 C ATOM 1375 CD1 LEU A 192 13.740 15.205 42.929 1.00 14.47 C ANISOU 1375 CD1 LEU A 192 1735 1833 1929 -46 -60 -25 C ATOM 1376 CD2 LEU A 192 12.815 13.287 41.616 1.00 13.32 C ANISOU 1376 CD2 LEU A 192 1763 1606 1690 2 -46 -45 C ATOM 1377 N VAL A 193 8.328 13.653 44.864 1.00 11.14 N ANISOU 1377 N VAL A 193 1443 1440 1348 -6 -53 -41 N ATOM 1378 CA VAL A 193 7.617 13.081 46.015 1.00 11.66 C ANISOU 1378 CA VAL A 193 1511 1511 1407 -23 -24 4 C ATOM 1379 C VAL A 193 7.207 11.641 45.737 1.00 12.50 C ANISOU 1379 C VAL A 193 1657 1549 1544 -25 -42 -4 C ATOM 1380 O VAL A 193 6.570 11.353 44.719 1.00 12.29 O ANISOU 1380 O VAL A 193 1702 1502 1464 -20 -25 23 O ATOM 1381 CB VAL A 193 6.387 13.914 46.410 1.00 13.08 C ANISOU 1381 CB VAL A 193 1612 1651 1705 34 28 -3 C ATOM 1382 CG1 VAL A 193 5.591 13.233 47.515 1.00 12.99 C ANISOU 1382 CG1 VAL A 193 1737 1632 1568 0 -6 -36 C ATOM 1383 CG2 VAL A 193 6.819 15.305 46.861 1.00 14.38 C ANISOU 1383 CG2 VAL A 193 1897 1736 1832 -42 -22 -33 C ATOM 1384 N THR A 194 7.584 10.719 46.628 1.00 12.88 N ANISOU 1384 N THR A 194 1683 1622 1590 23 -40 22 N ATOM 1385 CA THR A 194 7.211 9.315 46.470 1.00 13.80 C ANISOU 1385 CA THR A 194 1777 1691 1774 -6 -30 -16 C ATOM 1386 C THR A 194 6.449 8.771 47.672 1.00 14.73 C ANISOU 1386 C THR A 194 1890 1841 1865 -22 9 17 C ATOM 1387 O THR A 194 5.843 7.695 47.601 1.00 15.06 O ANISOU 1387 O THR A 194 1930 1865 1926 -47 14 -5 O ATOM 1388 CB THR A 194 8.436 8.421 46.211 1.00 13.46 C ANISOU 1388 CB THR A 194 1722 1716 1677 -24 -25 -12 C ATOM 1389 OG1 THR A 194 9.392 8.617 47.267 1.00 13.43 O ANISOU 1389 OG1 THR A 194 1779 1706 1616 12 -37 7 O ATOM 1390 CG2 THR A 194 9.097 8.743 44.880 1.00 13.44 C ANISOU 1390 CG2 THR A 194 1730 1682 1696 5 -18 17 C ATOM 1391 N GLU A 195 6.480 9.492 48.787 1.00 15.29 N ANISOU 1391 N GLU A 195 1990 1903 1919 -13 3 -26 N ATOM 1392 CA GLU A 195 5.754 9.072 49.985 1.00 15.96 C ANISOU 1392 CA GLU A 195 2056 2013 1994 -46 68 -58 C ATOM 1393 C GLU A 195 5.296 10.311 50.744 1.00 15.34 C ANISOU 1393 C GLU A 195 1982 1943 1904 -31 1 -5 C ATOM 1394 O GLU A 195 6.089 11.233 50.939 1.00 14.77 O ANISOU 1394 O GLU A 195 1979 1869 1766 15 19 -46 O ATOM 1395 CB GLU A 195 6.629 8.159 50.842 1.00 19.67 C ANISOU 1395 CB GLU A 195 2432 2471 2571 130 -163 34 C ATOM 1396 CG GLU A 195 5.922 7.457 51.984 1.00 24.13 C ANISOU 1396 CG GLU A 195 3097 3084 2987 -117 132 32 C ATOM 1397 CD GLU A 195 6.775 6.440 52.714 1.00 27.53 C ANISOU 1397 CD GLU A 195 3525 3386 3551 60 -97 42 C ATOM 1398 OE1 GLU A 195 7.872 6.084 52.238 1.00 28.60 O ANISOU 1398 OE1 GLU A 195 3644 3541 3683 33 13 26 O ATOM 1399 OE2 GLU A 195 6.342 5.977 53.793 1.00 29.38 O ANISOU 1399 OE2 GLU A 195 3763 3696 3703 -25 16 34 O ATOM 1400 N ALA A 196 4.022 10.348 51.121 1.00 15.83 N ANISOU 1400 N ALA A 196 2022 1990 2004 -7 23 12 N ATOM 1401 CA ALA A 196 3.461 11.546 51.738 1.00 16.38 C ANISOU 1401 CA ALA A 196 2118 2059 2047 12 19 -37 C ATOM 1402 C ALA A 196 2.566 11.223 52.931 1.00 16.89 C ANISOU 1402 C ALA A 196 2152 2163 2104 -10 31 -14 C ATOM 1403 O ALA A 196 1.646 10.420 52.853 1.00 17.53 O ANISOU 1403 O ALA A 196 2251 2208 2201 -65 39 20 O ATOM 1404 CB ALA A 196 2.677 12.341 50.702 1.00 17.17 C ANISOU 1404 CB ALA A 196 2196 2147 2183 36 -12 7 C ATOM 1405 N ALA A 197 2.843 11.882 54.044 1.00 16.70 N ANISOU 1405 N ALA A 197 2132 2134 2079 10 13 6 N ATOM 1406 CA ALA A 197 2.005 11.858 55.241 1.00 16.33 C ANISOU 1406 CA ALA A 197 2099 2066 2040 12 -13 -3 C ATOM 1407 C ALA A 197 2.129 13.234 55.887 1.00 16.13 C ANISOU 1407 C ALA A 197 2074 2059 1996 10 -41 12 C ATOM 1408 O ALA A 197 3.015 13.997 55.510 1.00 16.18 O ANISOU 1408 O ALA A 197 2107 2080 1960 -13 -48 2 O ATOM 1409 CB ALA A 197 2.451 10.773 56.202 1.00 16.38 C ANISOU 1409 CB ALA A 197 2147 1988 2090 13 6 -17 C ATOM 1410 N PRO A 198 1.266 13.554 56.838 1.00 16.39 N ANISOU 1410 N PRO A 198 2101 2102 2024 21 -30 5 N ATOM 1411 CA PRO A 198 1.243 14.882 57.431 1.00 16.63 C ANISOU 1411 CA PRO A 198 2146 2099 2073 2 -12 5 C ATOM 1412 C PRO A 198 2.597 15.329 57.942 1.00 16.81 C ANISOU 1412 C PRO A 198 2149 2141 2098 -2 -4 0 C ATOM 1413 O PRO A 198 3.015 16.458 57.661 1.00 17.05 O ANISOU 1413 O PRO A 198 2193 2169 2118 -20 -26 28 O ATOM 1414 CB PRO A 198 0.195 14.760 58.531 1.00 16.82 C ANISOU 1414 CB PRO A 198 2146 2111 2132 -1 3 6 C ATOM 1415 CG PRO A 198 -0.771 13.766 57.976 1.00 16.69 C ANISOU 1415 CG PRO A 198 2126 2110 2105 5 -7 6 C ATOM 1416 CD PRO A 198 0.084 12.758 57.241 1.00 16.56 C ANISOU 1416 CD PRO A 198 2142 2102 2050 0 -12 -3 C ATOM 1417 N GLU A 199 3.300 14.478 58.681 1.00 16.84 N ANISOU 1417 N GLU A 199 2156 2134 2107 20 13 -2 N ATOM 1418 CA GLU A 199 4.607 14.815 59.226 1.00 17.36 C ANISOU 1418 CA GLU A 199 2174 2189 2232 -3 10 -12 C ATOM 1419 C GLU A 199 5.698 13.885 58.706 1.00 17.23 C ANISOU 1419 C GLU A 199 2199 2174 2173 9 -10 -17 C ATOM 1420 O GLU A 199 6.720 13.656 59.347 1.00 17.00 O ANISOU 1420 O GLU A 199 2239 2137 2083 21 -13 -34 O ATOM 1421 CB GLU A 199 4.568 14.790 60.759 1.00 19.77 C ANISOU 1421 CB GLU A 199 2613 2560 2341 -13 -4 8 C ATOM 1422 CG GLU A 199 3.747 15.924 61.362 1.00 21.41 C ANISOU 1422 CG GLU A 199 2670 2707 2759 59 -1 -45 C ATOM 1423 CD GLU A 199 3.578 15.734 62.860 1.00 23.42 C ANISOU 1423 CD GLU A 199 3021 2989 2888 31 42 18 C ATOM 1424 OE1 GLU A 199 4.499 16.129 63.602 1.00 24.45 O ANISOU 1424 OE1 GLU A 199 3138 3155 2998 -12 -25 -31 O ATOM 1425 OE2 GLU A 199 2.538 15.189 63.278 1.00 24.04 O ANISOU 1425 OE2 GLU A 199 3033 3026 3075 -17 6 -10 O ATOM 1426 N TYR A 200 5.489 13.365 57.494 1.00 17.33 N ANISOU 1426 N TYR A 200 2239 2176 2169 8 5 -28 N ATOM 1427 CA TYR A 200 6.480 12.489 56.880 1.00 17.17 C ANISOU 1427 CA TYR A 200 2212 2177 2134 -6 21 1 C ATOM 1428 C TYR A 200 6.406 12.593 55.361 1.00 16.71 C ANISOU 1428 C TYR A 200 2130 2113 2107 -10 26 -10 C ATOM 1429 O TYR A 200 5.362 12.316 54.774 1.00 17.33 O ANISOU 1429 O TYR A 200 2175 2254 2157 -23 -1 0 O ATOM 1430 CB TYR A 200 6.242 11.047 57.311 1.00 17.56 C ANISOU 1430 CB TYR A 200 2261 2195 2215 -17 17 8 C ATOM 1431 CG TYR A 200 7.407 10.139 56.991 1.00 18.10 C ANISOU 1431 CG TYR A 200 2303 2253 2322 0 18 -4 C ATOM 1432 CD1 TYR A 200 8.594 10.231 57.699 1.00 18.66 C ANISOU 1432 CD1 TYR A 200 2340 2366 2385 -6 -7 -13 C ATOM 1433 CD2 TYR A 200 7.317 9.203 55.970 1.00 18.24 C ANISOU 1433 CD2 TYR A 200 2355 2285 2291 -21 28 5 C ATOM 1434 CE1 TYR A 200 9.647 9.396 57.374 1.00 19.10 C ANISOU 1434 CE1 TYR A 200 2391 2424 2441 18 -6 -21 C ATOM 1435 CE2 TYR A 200 8.369 8.354 55.677 1.00 18.70 C ANISOU 1435 CE2 TYR A 200 2393 2344 2369 1 21 6 C ATOM 1436 CZ TYR A 200 9.544 8.444 56.390 1.00 19.20 C ANISOU 1436 CZ TYR A 200 2428 2409 2457 -15 -16 -17 C ATOM 1437 OH TYR A 200 10.607 7.616 56.122 1.00 19.73 O ANISOU 1437 OH TYR A 200 2514 2448 2536 26 -43 -19 O ATOM 1438 N LEU A 201 7.509 12.995 54.751 1.00 15.67 N ANISOU 1438 N LEU A 201 2061 1947 1944 22 -8 -28 N ATOM 1439 CA LEU A 201 7.531 13.227 53.310 1.00 15.21 C ANISOU 1439 CA LEU A 201 1931 1917 1931 18 13 -11 C ATOM 1440 C LEU A 201 8.829 12.704 52.714 1.00 14.42 C ANISOU 1440 C LEU A 201 1878 1814 1786 -8 -18 -6 C ATOM 1441 O LEU A 201 9.908 13.047 53.195 1.00 14.35 O ANISOU 1441 O LEU A 201 1878 1844 1729 -10 4 -31 O ATOM 1442 CB LEU A 201 7.369 14.718 53.013 1.00 15.42 C ANISOU 1442 CB LEU A 201 1973 1928 1957 15 9 -9 C ATOM 1443 CG LEU A 201 7.149 15.101 51.547 1.00 15.60 C ANISOU 1443 CG LEU A 201 1956 2001 1969 0 -16 5 C ATOM 1444 CD1 LEU A 201 5.842 14.521 51.030 1.00 14.77 C ANISOU 1444 CD1 LEU A 201 1904 1880 1827 21 21 48 C ATOM 1445 CD2 LEU A 201 7.182 16.615 51.376 1.00 17.11 C ANISOU 1445 CD2 LEU A 201 2211 2083 2207 -15 36 -5 C ATOM 1446 N VAL A 202 8.734 11.856 51.696 1.00 13.71 N ANISOU 1446 N VAL A 202 1774 1714 1723 13 -3 39 N ATOM 1447 CA VAL A 202 9.909 11.327 51.027 1.00 13.41 C ANISOU 1447 CA VAL A 202 1742 1683 1670 7 -21 42 C ATOM 1448 C VAL A 202 9.986 11.837 49.586 1.00 12.98 C ANISOU 1448 C VAL A 202 1678 1629 1624 6 9 -4 C ATOM 1449 O VAL A 202 9.004 11.778 48.850 1.00 13.36 O ANISOU 1449 O VAL A 202 1712 1700 1665 21 -11 0 O ATOM 1450 CB VAL A 202 9.947 9.790 51.003 1.00 13.04 C ANISOU 1450 CB VAL A 202 1645 1668 1642 -27 3 -25 C ATOM 1451 CG1 VAL A 202 11.240 9.303 50.357 1.00 12.88 C ANISOU 1451 CG1 VAL A 202 1648 1621 1625 38 -33 -17 C ATOM 1452 CG2 VAL A 202 9.804 9.202 52.400 1.00 14.05 C ANISOU 1452 CG2 VAL A 202 1845 1783 1712 -19 -24 30 C ATOM 1453 N HIS A 203 11.141 12.373 49.232 1.00 12.66 N ANISOU 1453 N HIS A 203 1640 1599 1569 38 0 7 N ATOM 1454 CA HIS A 203 11.479 12.660 47.842 1.00 12.29 C ANISOU 1454 CA HIS A 203 1577 1539 1553 12 4 -15 C ATOM 1455 C HIS A 203 12.556 11.665 47.407 1.00 11.97 C ANISOU 1455 C HIS A 203 1541 1519 1488 2 -31 -42 C ATOM 1456 O HIS A 203 13.563 11.550 48.110 1.00 11.75 O ANISOU 1456 O HIS A 203 1525 1508 1431 35 -15 -47 O ATOM 1457 CB HIS A 203 12.039 14.067 47.673 1.00 12.22 C ANISOU 1457 CB HIS A 203 1663 1549 1430 -23 -16 -13 C ATOM 1458 CG HIS A 203 11.098 15.175 48.013 1.00 13.59 C ANISOU 1458 CG HIS A 203 1765 1682 1716 53 -8 -44 C ATOM 1459 ND1 HIS A 203 10.602 16.062 47.080 1.00 14.72 N ANISOU 1459 ND1 HIS A 203 1940 1808 1846 74 -43 5 N ATOM 1460 CD2 HIS A 203 10.567 15.549 49.203 1.00 13.64 C ANISOU 1460 CD2 HIS A 203 1789 1715 1678 -53 26 28 C ATOM 1461 CE1 HIS A 203 9.812 16.922 47.689 1.00 13.93 C ANISOU 1461 CE1 HIS A 203 1732 1748 1811 35 -76 21 C ATOM 1462 NE2 HIS A 203 9.762 16.637 48.976 1.00 15.23 N ANISOU 1462 NE2 HIS A 203 1949 1945 1892 84 9 -18 N ATOM 1463 N SER A 204 12.355 10.962 46.293 1.00 11.40 N ANISOU 1463 N SER A 204 1494 1396 1441 11 -22 4 N ATOM 1464 CA SER A 204 13.359 9.969 45.927 1.00 11.02 C ANISOU 1464 CA SER A 204 1449 1392 1347 1 -1 12 C ATOM 1465 C SER A 204 13.323 9.629 44.444 1.00 11.01 C ANISOU 1465 C SER A 204 1426 1408 1350 -6 -11 -8 C ATOM 1466 O SER A 204 12.377 9.952 43.726 1.00 11.34 O ANISOU 1466 O SER A 204 1461 1485 1361 -8 -34 -49 O ATOM 1467 CB SER A 204 13.185 8.699 46.770 1.00 11.18 C ANISOU 1467 CB SER A 204 1466 1363 1418 -13 38 9 C ATOM 1468 OG SER A 204 12.003 8.015 46.386 1.00 12.18 O ANISOU 1468 OG SER A 204 1490 1557 1579 4 -121 25 O ATOM 1469 N LYS A 205 14.400 8.990 44.019 1.00 10.84 N ANISOU 1469 N LYS A 205 1453 1341 1325 2 -22 3 N ATOM 1470 CA LYS A 205 14.583 8.610 42.625 1.00 11.40 C ANISOU 1470 CA LYS A 205 1537 1427 1369 0 4 -31 C ATOM 1471 C LYS A 205 15.479 7.380 42.527 1.00 11.43 C ANISOU 1471 C LYS A 205 1458 1471 1414 -2 -16 -12 C ATOM 1472 O LYS A 205 16.543 7.322 43.143 1.00 10.97 O ANISOU 1472 O LYS A 205 1482 1450 1235 9 -5 -3 O ATOM 1473 CB LYS A 205 15.200 9.766 41.834 1.00 11.88 C ANISOU 1473 CB LYS A 205 1554 1475 1484 -28 -4 10 C ATOM 1474 CG LYS A 205 15.358 9.483 40.344 1.00 12.71 C ANISOU 1474 CG LYS A 205 1637 1662 1530 -14 7 -30 C ATOM 1475 CD LYS A 205 14.008 9.580 39.642 1.00 13.76 C ANISOU 1475 CD LYS A 205 1715 1778 1734 -23 -64 -14 C ATOM 1476 CE LYS A 205 14.058 8.954 38.260 1.00 13.83 C ANISOU 1476 CE LYS A 205 1725 1772 1759 39 -1 -19 C ATOM 1477 NZ LYS A 205 14.102 7.467 38.320 1.00 14.14 N ANISOU 1477 NZ LYS A 205 1840 1788 1744 -26 8 22 N ATOM 1478 N THR A 206 15.043 6.410 41.727 1.00 11.53 N ANISOU 1478 N THR A 206 1497 1483 1400 -10 -13 -32 N ATOM 1479 CA THR A 206 15.829 5.214 41.463 1.00 12.15 C ANISOU 1479 CA THR A 206 1527 1552 1537 27 -6 -6 C ATOM 1480 C THR A 206 16.702 5.362 40.221 1.00 12.14 C ANISOU 1480 C THR A 206 1566 1540 1506 -6 -25 -3 C ATOM 1481 O THR A 206 16.476 6.230 39.381 1.00 12.00 O ANISOU 1481 O THR A 206 1558 1515 1486 -53 -43 -7 O ATOM 1482 CB THR A 206 14.906 3.996 41.241 1.00 12.98 C ANISOU 1482 CB THR A 206 1633 1639 1658 -33 37 -46 C ATOM 1483 OG1 THR A 206 13.878 4.389 40.321 1.00 14.07 O ANISOU 1483 OG1 THR A 206 1793 1815 1739 -35 -54 7 O ATOM 1484 CG2 THR A 206 14.261 3.562 42.541 1.00 12.55 C ANISOU 1484 CG2 THR A 206 1662 1510 1598 -28 -57 53 C ATOM 1485 N GLY A 207 17.687 4.478 40.103 1.00 12.60 N ANISOU 1485 N GLY A 207 1552 1637 1597 17 -44 -17 N ATOM 1486 CA GLY A 207 18.542 4.410 38.923 1.00 13.23 C ANISOU 1486 CA GLY A 207 1661 1709 1657 8 4 4 C ATOM 1487 C GLY A 207 19.018 2.968 38.719 1.00 13.95 C ANISOU 1487 C GLY A 207 1793 1731 1776 4 2 3 C ATOM 1488 O GLY A 207 19.104 2.190 39.665 1.00 13.76 O ANISOU 1488 O GLY A 207 1755 1775 1698 -17 45 -6 O ATOM 1489 N PHE A 208 19.231 2.599 37.462 1.00 14.38 N ANISOU 1489 N PHE A 208 1857 1818 1787 -36 -27 -13 N ATOM 1490 CA PHE A 208 19.652 1.246 37.113 1.00 15.15 C ANISOU 1490 CA PHE A 208 1949 1884 1924 3 -3 -26 C ATOM 1491 C PHE A 208 20.292 1.266 35.728 1.00 15.84 C ANISOU 1491 C PHE A 208 2046 1997 1976 -5 19 -14 C ATOM 1492 O PHE A 208 19.632 1.590 34.742 1.00 16.26 O ANISOU 1492 O PHE A 208 2064 2056 2058 34 -31 -14 O ATOM 1493 CB PHE A 208 18.475 0.280 37.150 1.00 15.02 C ANISOU 1493 CB PHE A 208 1921 1936 1849 -11 -11 9 C ATOM 1494 CG PHE A 208 18.758 -1.136 36.736 1.00 16.73 C ANISOU 1494 CG PHE A 208 2206 2012 2138 23 32 9 C ATOM 1495 CD1 PHE A 208 19.839 -1.834 37.237 1.00 17.44 C ANISOU 1495 CD1 PHE A 208 2186 2178 2264 16 5 21 C ATOM 1496 CD2 PHE A 208 17.907 -1.783 35.853 1.00 18.25 C ANISOU 1496 CD2 PHE A 208 2335 2333 2266 -41 -59 -18 C ATOM 1497 CE1 PHE A 208 20.085 -3.141 36.864 1.00 17.87 C ANISOU 1497 CE1 PHE A 208 2290 2229 2270 15 38 -12 C ATOM 1498 CE2 PHE A 208 18.146 -3.089 35.470 1.00 19.48 C ANISOU 1498 CE2 PHE A 208 2504 2425 2472 27 -22 -31 C ATOM 1499 CZ PHE A 208 19.235 -3.768 35.976 1.00 18.97 C ANISOU 1499 CZ PHE A 208 2432 2387 2389 -19 -33 -58 C ATOM 1500 N SER A 209 21.574 0.931 35.663 1.00 16.17 N ANISOU 1500 N SER A 209 2055 2020 2068 12 -17 -2 N ATOM 1501 CA SER A 209 22.330 1.101 34.427 1.00 17.24 C ANISOU 1501 CA SER A 209 2176 2211 2163 10 30 29 C ATOM 1502 C SER A 209 22.283 -0.147 33.554 1.00 18.41 C ANISOU 1502 C SER A 209 2380 2312 2302 11 3 -37 C ATOM 1503 O SER A 209 22.734 -0.112 32.408 1.00 18.76 O ANISOU 1503 O SER A 209 2463 2340 2326 34 43 -35 O ATOM 1504 CB SER A 209 23.788 1.444 34.738 1.00 16.92 C ANISOU 1504 CB SER A 209 2184 2141 2103 -5 -18 33 C ATOM 1505 OG SER A 209 24.462 0.314 35.268 1.00 17.13 O ANISOU 1505 OG SER A 209 2183 2109 2217 36 10 -22 O ATOM 1506 N GLY A 210 21.751 -1.234 34.091 1.00 19.07 N ANISOU 1506 N GLY A 210 2422 2395 2427 -14 6 19 N ATOM 1507 CA GLY A 210 21.768 -2.519 33.395 1.00 19.96 C ANISOU 1507 CA GLY A 210 2562 2484 2537 -10 17 -42 C ATOM 1508 C GLY A 210 22.552 -3.518 34.245 1.00 20.89 C ANISOU 1508 C GLY A 210 2660 2654 2623 8 -16 26 C ATOM 1509 O GLY A 210 23.009 -3.155 35.330 1.00 20.63 O ANISOU 1509 O GLY A 210 2617 2624 2597 9 6 30 O ATOM 1510 N VAL A 211 22.685 -4.749 33.764 1.00 22.09 N ANISOU 1510 N VAL A 211 2854 2759 2781 10 16 -61 N ATOM 1511 CA VAL A 211 23.352 -5.781 34.551 1.00 23.42 C ANISOU 1511 CA VAL A 211 3037 2933 2927 56 -31 10 C ATOM 1512 C VAL A 211 24.816 -5.943 34.170 1.00 24.51 C ANISOU 1512 C VAL A 211 3089 3105 3118 31 -14 -34 C ATOM 1513 O VAL A 211 25.529 -6.727 34.800 1.00 24.54 O ANISOU 1513 O VAL A 211 3101 3098 3127 41 7 -27 O ATOM 1514 CB VAL A 211 22.632 -7.137 34.437 1.00 24.56 C ANISOU 1514 CB VAL A 211 3137 3062 3134 -42 -9 2 C ATOM 1515 CG1 VAL A 211 21.255 -7.066 35.085 1.00 24.95 C ANISOU 1515 CG1 VAL A 211 3184 3128 3168 18 12 -7 C ATOM 1516 CG2 VAL A 211 22.510 -7.575 32.985 1.00 24.51 C ANISOU 1516 CG2 VAL A 211 3129 3063 3120 -1 11 5 C ATOM 1517 N GLY A 212 25.272 -5.200 33.169 1.00 25.80 N ANISOU 1517 N GLY A 212 3327 3250 3226 -8 1 21 N ATOM 1518 CA GLY A 212 26.654 -5.298 32.713 1.00 27.26 C ANISOU 1518 CA GLY A 212 3413 3498 3445 -14 30 21 C ATOM 1519 C GLY A 212 27.043 -6.762 32.528 1.00 28.72 C ANISOU 1519 C GLY A 212 3668 3586 3658 11 30 -19 C ATOM 1520 O GLY A 212 26.312 -7.538 31.912 1.00 29.01 O ANISOU 1520 O GLY A 212 3682 3633 3707 9 -5 -27 O ATOM 1521 N THR A 213 28.207 -7.134 33.045 1.00 29.73 N ANISOU 1521 N THR A 213 3729 3784 3782 9 -14 -9 N ATOM 1522 CA THR A 213 28.638 -8.525 33.091 1.00 30.87 C ANISOU 1522 CA THR A 213 3931 3840 3957 11 -6 -4 C ATOM 1523 C THR A 213 28.920 -8.921 34.539 1.00 31.64 C ANISOU 1523 C THR A 213 4032 3996 3995 1 -5 7 C ATOM 1524 O THR A 213 28.779 -8.089 35.437 1.00 31.87 O ANISOU 1524 O THR A 213 4068 3996 4046 7 8 -8 O ATOM 1525 CB THR A 213 29.914 -8.779 32.269 1.00 31.69 C ANISOU 1525 CB THR A 213 3989 4011 4043 11 28 -7 C ATOM 1526 OG1 THR A 213 30.963 -7.928 32.752 1.00 31.65 O ANISOU 1526 OG1 THR A 213 4021 4012 3993 2 14 -8 O ATOM 1527 CG2 THR A 213 29.700 -8.517 30.788 1.00 32.49 C ANISOU 1527 CG2 THR A 213 4146 4110 4090 2 3 1 C ATOM 1528 N GLU A 214 29.345 -10.160 34.764 1.00 32.04 N ANISOU 1528 N GLU A 214 4076 4024 4073 13 6 -2 N ATOM 1529 CA GLU A 214 29.775 -10.573 36.098 1.00 32.49 C ANISOU 1529 CA GLU A 214 4127 4114 4104 8 -7 6 C ATOM 1530 C GLU A 214 31.043 -9.832 36.506 1.00 32.53 C ANISOU 1530 C GLU A 214 4126 4108 4126 7 -3 4 C ATOM 1531 O GLU A 214 31.172 -9.338 37.626 1.00 32.60 O ANISOU 1531 O GLU A 214 4133 4119 4137 15 -7 -6 O ATOM 1532 CB GLU A 214 29.989 -12.086 36.153 1.00 33.42 C ANISOU 1532 CB GLU A 214 4278 4162 4257 9 3 2 C ATOM 1533 N SER A 215 31.990 -9.726 35.578 1.00 32.50 N ANISOU 1533 N SER A 215 4125 4085 4137 -1 -5 4 N ATOM 1534 CA SER A 215 33.245 -9.032 35.812 1.00 32.48 C ANISOU 1534 CA SER A 215 4136 4046 4159 4 -37 14 C ATOM 1535 C SER A 215 33.089 -7.522 35.881 1.00 31.77 C ANISOU 1535 C SER A 215 4014 4008 4049 8 -32 9 C ATOM 1536 O SER A 215 33.807 -6.857 36.635 1.00 31.69 O ANISOU 1536 O SER A 215 4013 3976 4052 8 -14 -1 O ATOM 1537 CB SER A 215 34.256 -9.401 34.718 1.00 34.58 C ANISOU 1537 CB SER A 215 4352 4447 4342 1 70 -33 C ATOM 1538 OG SER A 215 34.607 -10.770 34.821 1.00 36.57 O ANISOU 1538 OG SER A 215 4656 4571 4668 24 16 8 O ATOM 1539 N ASN A 216 32.187 -6.954 35.085 1.00 31.09 N ANISOU 1539 N ASN A 216 3923 3892 3996 2 3 -24 N ATOM 1540 CA ASN A 216 31.944 -5.517 35.079 1.00 30.45 C ANISOU 1540 CA ASN A 216 3750 3873 3947 42 -17 -56 C ATOM 1541 C ASN A 216 30.457 -5.211 35.248 1.00 28.34 C ANISOU 1541 C ASN A 216 3633 3595 3539 -13 9 -3 C ATOM 1542 O ASN A 216 29.751 -4.857 34.306 1.00 28.18 O ANISOU 1542 O ASN A 216 3573 3583 3551 5 16 -13 O ATOM 1543 CB ASN A 216 32.460 -4.874 33.791 1.00 34.80 C ANISOU 1543 CB ASN A 216 4637 4381 4206 -27 59 97 C ATOM 1544 CG ASN A 216 33.968 -4.840 33.670 1.00 40.05 C ANISOU 1544 CG ASN A 216 4913 5170 5133 -7 14 63 C ATOM 1545 OD1 ASN A 216 34.562 -5.674 32.984 1.00 41.66 O ANISOU 1545 OD1 ASN A 216 5286 5237 5306 32 30 -24 O ATOM 1546 ND2 ASN A 216 34.604 -3.885 34.338 1.00 41.16 N ANISOU 1546 ND2 ASN A 216 5204 5209 5226 -14 4 -9 N ATOM 1547 N PRO A 217 29.977 -5.358 36.480 1.00 26.75 N ANISOU 1547 N PRO A 217 3329 3372 3465 11 -14 -15 N ATOM 1548 CA PRO A 217 28.560 -5.258 36.777 1.00 25.40 C ANISOU 1548 CA PRO A 217 3263 3129 3258 30 -16 6 C ATOM 1549 C PRO A 217 27.984 -3.873 36.551 1.00 23.69 C ANISOU 1549 C PRO A 217 2933 3039 3031 -21 -4 -11 C ATOM 1550 O PRO A 217 28.702 -2.874 36.500 1.00 23.58 O ANISOU 1550 O PRO A 217 2917 3002 3039 14 11 -22 O ATOM 1551 CB PRO A 217 28.477 -5.670 38.242 1.00 25.74 C ANISOU 1551 CB PRO A 217 3301 3216 3265 15 3 5 C ATOM 1552 CG PRO A 217 29.788 -5.292 38.828 1.00 26.28 C ANISOU 1552 CG PRO A 217 3323 3310 3352 7 -11 -10 C ATOM 1553 CD PRO A 217 30.798 -5.328 37.718 1.00 26.64 C ANISOU 1553 CD PRO A 217 3363 3354 3404 5 16 -2 C ATOM 1554 N GLY A 218 26.660 -3.815 36.405 1.00 21.81 N ANISOU 1554 N GLY A 218 2844 2671 2772 45 17 -8 N ATOM 1555 CA GLY A 218 25.970 -2.530 36.319 1.00 19.86 C ANISOU 1555 CA GLY A 218 2567 2546 2434 -17 18 -47 C ATOM 1556 C GLY A 218 25.870 -1.912 37.713 1.00 18.07 C ANISOU 1556 C GLY A 218 2283 2244 2337 39 -10 10 C ATOM 1557 O GLY A 218 26.401 -2.458 38.684 1.00 17.83 O ANISOU 1557 O GLY A 218 2279 2197 2300 41 10 -18 O ATOM 1558 N VAL A 219 25.180 -0.781 37.794 1.00 16.53 N ANISOU 1558 N VAL A 219 2089 2146 2047 -17 -9 -30 N ATOM 1559 CA VAL A 219 24.964 -0.110 39.073 1.00 15.46 C ANISOU 1559 CA VAL A 219 1882 1992 2000 8 10 15 C ATOM 1560 C VAL A 219 23.477 0.171 39.262 1.00 14.24 C ANISOU 1560 C VAL A 219 1822 1811 1777 -2 -5 1 C ATOM 1561 O VAL A 219 22.779 0.457 38.288 1.00 13.65 O ANISOU 1561 O VAL A 219 1741 1730 1716 25 55 -20 O ATOM 1562 CB VAL A 219 25.770 1.196 39.174 1.00 16.26 C ANISOU 1562 CB VAL A 219 2093 1980 2107 -29 -12 46 C ATOM 1563 CG1 VAL A 219 25.343 2.190 38.099 1.00 15.74 C ANISOU 1563 CG1 VAL A 219 2017 1958 2004 0 -1 -11 C ATOM 1564 CG2 VAL A 219 25.646 1.828 40.553 1.00 17.92 C ANISOU 1564 CG2 VAL A 219 2265 2317 2229 0 -7 -57 C ATOM 1565 N ALA A 220 23.008 0.053 40.498 1.00 13.53 N ANISOU 1565 N ALA A 220 1679 1705 1755 -19 -10 -8 N ATOM 1566 CA ALA A 220 21.636 0.432 40.827 1.00 13.09 C ANISOU 1566 CA ALA A 220 1687 1598 1689 3 -7 -18 C ATOM 1567 C ALA A 220 21.658 1.497 41.921 1.00 12.83 C ANISOU 1567 C ALA A 220 1653 1596 1626 25 -1 2 C ATOM 1568 O ALA A 220 22.518 1.451 42.793 1.00 13.17 O ANISOU 1568 O ALA A 220 1667 1676 1662 11 -13 -48 O ATOM 1569 CB ALA A 220 20.823 -0.778 41.251 1.00 12.81 C ANISOU 1569 CB ALA A 220 1598 1649 1621 20 46 -5 C ATOM 1570 N TRP A 221 20.729 2.439 41.860 1.00 12.24 N ANISOU 1570 N TRP A 221 1601 1489 1562 -22 -5 -22 N ATOM 1571 CA TRP A 221 20.723 3.591 42.746 1.00 11.56 C ANISOU 1571 CA TRP A 221 1518 1440 1434 12 -4 37 C ATOM 1572 C TRP A 221 19.365 3.772 43.430 1.00 11.67 C ANISOU 1572 C TRP A 221 1529 1463 1443 -8 11 16 C ATOM 1573 O TRP A 221 18.326 3.464 42.850 1.00 12.38 O ANISOU 1573 O TRP A 221 1597 1554 1555 -26 -54 6 O ATOM 1574 CB TRP A 221 20.938 4.888 41.972 1.00 10.92 C ANISOU 1574 CB TRP A 221 1455 1358 1336 -42 -11 -38 C ATOM 1575 CG TRP A 221 22.276 5.220 41.421 1.00 11.29 C ANISOU 1575 CG TRP A 221 1442 1419 1427 9 -4 -3 C ATOM 1576 CD1 TRP A 221 22.752 4.912 40.178 1.00 12.11 C ANISOU 1576 CD1 TRP A 221 1608 1545 1447 12 33 37 C ATOM 1577 CD2 TRP A 221 23.323 5.954 42.075 1.00 12.08 C ANISOU 1577 CD2 TRP A 221 1496 1481 1612 -46 -48 12 C ATOM 1578 NE1 TRP A 221 24.023 5.402 40.019 1.00 13.14 N ANISOU 1578 NE1 TRP A 221 1644 1687 1661 -35 -24 -21 N ATOM 1579 CE2 TRP A 221 24.398 6.043 41.172 1.00 12.68 C ANISOU 1579 CE2 TRP A 221 1623 1589 1604 19 -1 27 C ATOM 1580 CE3 TRP A 221 23.447 6.538 43.340 1.00 12.94 C ANISOU 1580 CE3 TRP A 221 1645 1654 1618 -9 0 7 C ATOM 1581 CZ2 TRP A 221 25.589 6.694 41.486 1.00 13.17 C ANISOU 1581 CZ2 TRP A 221 1650 1684 1670 -6 -16 -20 C ATOM 1582 CZ3 TRP A 221 24.631 7.183 43.656 1.00 13.37 C ANISOU 1582 CZ3 TRP A 221 1645 1708 1727 -5 0 -36 C ATOM 1583 CH2 TRP A 221 25.680 7.256 42.729 1.00 12.86 C ANISOU 1583 CH2 TRP A 221 1638 1635 1612 -9 -32 26 C ATOM 1584 N TRP A 222 19.374 4.341 44.629 1.00 11.31 N ANISOU 1584 N TRP A 222 1478 1385 1436 -29 -17 17 N ATOM 1585 CA TRP A 222 18.189 4.976 45.187 1.00 11.32 C ANISOU 1585 CA TRP A 222 1493 1395 1413 -17 -16 17 C ATOM 1586 C TRP A 222 18.660 6.208 45.963 1.00 11.64 C ANISOU 1586 C TRP A 222 1540 1425 1458 -16 -31 -7 C ATOM 1587 O TRP A 222 19.513 6.066 46.840 1.00 12.18 O ANISOU 1587 O TRP A 222 1585 1531 1513 -10 -62 44 O ATOM 1588 CB TRP A 222 17.375 4.063 46.094 1.00 11.47 C ANISOU 1588 CB TRP A 222 1447 1426 1485 -91 -13 -25 C ATOM 1589 CG TRP A 222 16.020 4.603 46.443 1.00 11.97 C ANISOU 1589 CG TRP A 222 1530 1416 1601 -12 -5 -35 C ATOM 1590 CD1 TRP A 222 15.147 5.230 45.597 1.00 13.23 C ANISOU 1590 CD1 TRP A 222 1623 1732 1671 6 -25 57 C ATOM 1591 CD2 TRP A 222 15.359 4.538 47.709 1.00 13.49 C ANISOU 1591 CD2 TRP A 222 1735 1720 1671 -23 28 -4 C ATOM 1592 NE1 TRP A 222 13.997 5.573 46.259 1.00 13.30 N ANISOU 1592 NE1 TRP A 222 1674 1645 1735 1 3 -10 N ATOM 1593 CE2 TRP A 222 14.101 5.153 47.562 1.00 14.05 C ANISOU 1593 CE2 TRP A 222 1797 1768 1774 3 -26 29 C ATOM 1594 CE3 TRP A 222 15.715 4.018 48.960 1.00 14.02 C ANISOU 1594 CE3 TRP A 222 1882 1736 1707 -23 -9 26 C ATOM 1595 CZ2 TRP A 222 13.195 5.271 48.616 1.00 14.82 C ANISOU 1595 CZ2 TRP A 222 1867 1889 1875 11 30 -10 C ATOM 1596 CZ3 TRP A 222 14.814 4.138 50.004 1.00 14.75 C ANISOU 1596 CZ3 TRP A 222 1882 1875 1847 2 28 5 C ATOM 1597 CH2 TRP A 222 13.569 4.756 49.824 1.00 15.04 C ANISOU 1597 CH2 TRP A 222 1899 1910 1908 9 21 14 C ATOM 1598 N VAL A 223 18.237 7.393 45.536 1.00 11.24 N ANISOU 1598 N VAL A 223 1456 1420 1396 -36 -13 15 N ATOM 1599 CA VAL A 223 18.716 8.625 46.163 1.00 11.34 C ANISOU 1599 CA VAL A 223 1491 1420 1398 -11 -19 1 C ATOM 1600 C VAL A 223 17.527 9.495 46.563 1.00 11.75 C ANISOU 1600 C VAL A 223 1508 1479 1479 1 -12 -3 C ATOM 1601 O VAL A 223 16.439 9.344 46.003 1.00 11.79 O ANISOU 1601 O VAL A 223 1472 1514 1494 16 -6 -6 O ATOM 1602 CB VAL A 223 19.658 9.446 45.267 1.00 11.51 C ANISOU 1602 CB VAL A 223 1424 1534 1416 -45 -17 -26 C ATOM 1603 CG1 VAL A 223 20.878 8.665 44.797 1.00 12.20 C ANISOU 1603 CG1 VAL A 223 1569 1497 1568 51 -49 -33 C ATOM 1604 CG2 VAL A 223 18.916 10.013 44.061 1.00 12.00 C ANISOU 1604 CG2 VAL A 223 1609 1445 1507 48 -36 13 C ATOM 1605 N GLY A 224 17.721 10.398 47.525 1.00 11.90 N ANISOU 1605 N GLY A 224 1547 1488 1488 -1 -31 8 N ATOM 1606 CA GLY A 224 16.641 11.327 47.851 1.00 12.14 C ANISOU 1606 CA GLY A 224 1573 1528 1512 10 -18 -24 C ATOM 1607 C GLY A 224 16.803 11.909 49.251 1.00 12.23 C ANISOU 1607 C GLY A 224 1584 1541 1520 4 -26 -13 C ATOM 1608 O GLY A 224 17.912 11.958 49.775 1.00 11.69 O ANISOU 1608 O GLY A 224 1577 1447 1418 2 -28 -11 O ATOM 1609 N TRP A 225 15.674 12.317 49.820 1.00 12.64 N ANISOU 1609 N TRP A 225 1609 1619 1574 -6 18 13 N ATOM 1610 CA TRP A 225 15.689 12.805 51.198 1.00 13.17 C ANISOU 1610 CA TRP A 225 1692 1681 1630 8 -7 -33 C ATOM 1611 C TRP A 225 14.359 12.532 51.890 1.00 13.51 C ANISOU 1611 C TRP A 225 1698 1721 1714 -9 -11 -11 C ATOM 1612 O TRP A 225 13.308 12.394 51.266 1.00 12.92 O ANISOU 1612 O TRP A 225 1689 1629 1589 2 6 -44 O ATOM 1613 CB TRP A 225 16.066 14.275 51.272 1.00 13.42 C ANISOU 1613 CB TRP A 225 1696 1690 1715 -1 -6 8 C ATOM 1614 CG TRP A 225 15.112 15.249 50.655 1.00 14.08 C ANISOU 1614 CG TRP A 225 1763 1684 1903 24 -48 -14 C ATOM 1615 CD1 TRP A 225 14.051 15.852 51.262 1.00 13.85 C ANISOU 1615 CD1 TRP A 225 1750 1748 1765 -12 -25 13 C ATOM 1616 CD2 TRP A 225 15.145 15.755 49.314 1.00 16.03 C ANISOU 1616 CD2 TRP A 225 2087 1992 2010 -22 -110 67 C ATOM 1617 NE1 TRP A 225 13.414 16.697 50.384 1.00 14.28 N ANISOU 1617 NE1 TRP A 225 1838 1722 1864 8 -85 -1 N ATOM 1618 CE2 TRP A 225 14.071 16.657 49.184 1.00 15.97 C ANISOU 1618 CE2 TRP A 225 1991 2027 2050 -21 52 -69 C ATOM 1619 CE3 TRP A 225 15.979 15.533 48.216 1.00 19.18 C ANISOU 1619 CE3 TRP A 225 2413 2448 2424 20 121 -61 C ATOM 1620 CZ2 TRP A 225 13.801 17.332 47.993 1.00 19.00 C ANISOU 1620 CZ2 TRP A 225 2502 2367 2348 -4 -92 106 C ATOM 1621 CZ3 TRP A 225 15.712 16.204 47.035 1.00 21.65 C ANISOU 1621 CZ3 TRP A 225 2819 2756 2653 37 -6 55 C ATOM 1622 CH2 TRP A 225 14.631 17.092 46.936 1.00 21.71 C ANISOU 1622 CH2 TRP A 225 2770 2809 2670 35 52 -14 C ATOM 1623 N VAL A 226 14.432 12.432 53.214 1.00 14.10 N ANISOU 1623 N VAL A 226 1795 1820 1743 -14 -61 -37 N ATOM 1624 CA VAL A 226 13.248 12.206 54.033 1.00 15.06 C ANISOU 1624 CA VAL A 226 1864 1988 1870 -23 -3 -44 C ATOM 1625 C VAL A 226 13.056 13.366 55.003 1.00 15.64 C ANISOU 1625 C VAL A 226 2003 2025 1916 -4 8 -34 C ATOM 1626 O VAL A 226 13.993 13.787 55.677 1.00 15.87 O ANISOU 1626 O VAL A 226 2053 2025 1953 -31 9 -63 O ATOM 1627 CB VAL A 226 13.307 10.862 54.772 1.00 18.70 C ANISOU 1627 CB VAL A 226 2510 2199 2398 -9 93 101 C ATOM 1628 CG1 VAL A 226 14.644 10.679 55.471 1.00 22.48 C ANISOU 1628 CG1 VAL A 226 2772 2902 2868 15 -79 12 C ATOM 1629 CG2 VAL A 226 12.172 10.723 55.769 1.00 17.63 C ANISOU 1629 CG2 VAL A 226 2319 2184 2194 14 -41 11 C ATOM 1630 N GLU A 227 11.840 13.898 55.016 1.00 16.23 N ANISOU 1630 N GLU A 227 2057 2092 2019 22 4 -2 N ATOM 1631 CA GLU A 227 11.458 14.875 56.035 1.00 17.15 C ANISOU 1631 CA GLU A 227 2196 2185 2135 -10 11 -83 C ATOM 1632 C GLU A 227 10.557 14.188 57.053 1.00 17.65 C ANISOU 1632 C GLU A 227 2236 2255 2214 -8 20 -26 C ATOM 1633 O GLU A 227 9.473 13.711 56.723 1.00 17.66 O ANISOU 1633 O GLU A 227 2234 2291 2184 1 8 -43 O ATOM 1634 CB GLU A 227 10.777 16.086 55.401 1.00 19.65 C ANISOU 1634 CB GLU A 227 2574 2398 2495 123 -108 -34 C ATOM 1635 CG GLU A 227 11.719 16.901 54.528 1.00 23.98 C ANISOU 1635 CG GLU A 227 3035 3044 3033 -141 125 1 C ATOM 1636 CD GLU A 227 11.012 17.965 53.716 1.00 27.69 C ANISOU 1636 CD GLU A 227 3531 3405 3585 86 23 115 C ATOM 1637 OE1 GLU A 227 10.484 17.644 52.630 1.00 30.38 O ANISOU 1637 OE1 GLU A 227 3867 3832 3843 -15 -95 -58 O ATOM 1638 OE2 GLU A 227 10.988 19.134 54.153 1.00 27.55 O ANISOU 1638 OE2 GLU A 227 3548 3460 3459 -1 29 6 O ATOM 1639 N LYS A 228 11.055 14.076 58.280 1.00 18.12 N ANISOU 1639 N LYS A 228 2309 2317 2257 -25 -17 -18 N ATOM 1640 CA LYS A 228 10.285 13.495 59.369 1.00 18.33 C ANISOU 1640 CA LYS A 228 2342 2340 2282 -17 15 -31 C ATOM 1641 C LYS A 228 10.122 14.548 60.467 1.00 18.35 C ANISOU 1641 C LYS A 228 2334 2318 2319 -9 2 -38 C ATOM 1642 O LYS A 228 11.126 14.989 61.024 1.00 18.36 O ANISOU 1642 O LYS A 228 2331 2319 2326 9 -3 -54 O ATOM 1643 CB LYS A 228 10.960 12.253 59.945 1.00 19.90 C ANISOU 1643 CB LYS A 228 2558 2427 2575 58 -76 -32 C ATOM 1644 CG LYS A 228 10.200 11.662 61.123 1.00 23.01 C ANISOU 1644 CG LYS A 228 2950 2945 2848 -103 106 -20 C ATOM 1645 CD LYS A 228 11.054 10.689 61.919 1.00 27.23 C ANISOU 1645 CD LYS A 228 3453 3358 3535 110 -124 51 C ATOM 1646 CE LYS A 228 10.397 10.313 63.234 1.00 31.56 C ANISOU 1646 CE LYS A 228 4125 4010 3855 32 86 44 C ATOM 1647 NZ LYS A 228 9.024 9.769 63.063 1.00 34.53 N ANISOU 1647 NZ LYS A 228 4319 4341 4459 -35 -6 12 N ATOM 1648 N GLU A 229 8.881 14.923 60.736 1.00 18.54 N ANISOU 1648 N GLU A 229 2350 2324 2372 15 2 -32 N ATOM 1649 CA GLU A 229 8.632 16.029 61.670 1.00 19.03 C ANISOU 1649 CA GLU A 229 2432 2340 2458 -5 8 -60 C ATOM 1650 C GLU A 229 9.437 17.239 61.237 1.00 18.86 C ANISOU 1650 C GLU A 229 2424 2356 2385 -4 -14 -24 C ATOM 1651 O GLU A 229 9.233 17.689 60.098 1.00 19.00 O ANISOU 1651 O GLU A 229 2481 2331 2408 11 -52 -10 O ATOM 1652 CB GLU A 229 8.884 15.556 63.102 1.00 22.16 C ANISOU 1652 CB GLU A 229 2955 2863 2601 108 -66 -27 C ATOM 1653 CG GLU A 229 7.833 14.550 63.548 1.00 26.95 C ANISOU 1653 CG GLU A 229 3327 3361 3550 -142 88 -65 C ATOM 1654 CD GLU A 229 8.188 13.745 64.777 1.00 31.92 C ANISOU 1654 CD GLU A 229 4218 3963 3948 22 -62 89 C ATOM 1655 OE1 GLU A 229 9.367 13.377 64.959 1.00 34.29 O ANISOU 1655 OE1 GLU A 229 4318 4318 4391 29 -29 15 O ATOM 1656 OE2 GLU A 229 7.271 13.463 65.580 1.00 33.73 O ANISOU 1656 OE2 GLU A 229 4277 4275 4265 -11 36 51 O ATOM 1657 N THR A 230 10.351 17.759 62.053 1.00 18.52 N ANISOU 1657 N THR A 230 2396 2308 2334 7 14 -30 N ATOM 1658 CA THR A 230 11.097 18.948 61.652 1.00 18.58 C ANISOU 1658 CA THR A 230 2375 2359 2324 0 11 7 C ATOM 1659 C THR A 230 12.540 18.633 61.287 1.00 18.26 C ANISOU 1659 C THR A 230 2350 2324 2264 6 -17 4 C ATOM 1660 O THR A 230 13.367 19.540 61.181 1.00 18.67 O ANISOU 1660 O THR A 230 2433 2341 2320 -26 -20 -46 O ATOM 1661 CB THR A 230 11.068 20.050 62.727 1.00 19.43 C ANISOU 1661 CB THR A 230 2545 2385 2452 29 27 -40 C ATOM 1662 OG1 THR A 230 11.543 19.536 63.976 1.00 20.55 O ANISOU 1662 OG1 THR A 230 2632 2626 2551 49 -45 -6 O ATOM 1663 CG2 THR A 230 9.654 20.576 62.890 1.00 19.64 C ANISOU 1663 CG2 THR A 230 2499 2529 2435 -6 -22 -5 C ATOM 1664 N GLU A 231 12.829 17.357 61.053 1.00 18.08 N ANISOU 1664 N GLU A 231 2309 2327 2235 -6 -23 -30 N ATOM 1665 CA GLU A 231 14.167 16.938 60.673 1.00 18.27 C ANISOU 1665 CA GLU A 231 2324 2347 2269 -15 14 -61 C ATOM 1666 C GLU A 231 14.214 16.518 59.205 1.00 17.75 C ANISOU 1666 C GLU A 231 2248 2255 2240 -4 14 -41 C ATOM 1667 O GLU A 231 13.200 16.106 58.646 1.00 17.40 O ANISOU 1667 O GLU A 231 2264 2202 2148 27 -1 -44 O ATOM 1668 CB GLU A 231 14.670 15.794 61.557 1.00 20.57 C ANISOU 1668 CB GLU A 231 2719 2560 2536 12 -65 69 C ATOM 1669 CG GLU A 231 16.150 15.486 61.358 1.00 23.63 C ANISOU 1669 CG GLU A 231 2924 3053 3001 81 19 8 C ATOM 1670 CD GLU A 231 17.032 16.691 61.633 1.00 26.10 C ANISOU 1670 CD GLU A 231 3312 3195 3409 -74 39 57 C ATOM 1671 OE1 GLU A 231 17.333 16.928 62.822 1.00 29.22 O ANISOU 1671 OE1 GLU A 231 3805 3737 3561 -18 -33 -28 O ATOM 1672 OE2 GLU A 231 17.407 17.396 60.673 1.00 24.02 O ANISOU 1672 OE2 GLU A 231 2992 3077 3059 -4 -52 -76 O ATOM 1673 N VAL A 232 15.392 16.658 58.607 1.00 17.43 N ANISOU 1673 N VAL A 232 2245 2218 2161 10 11 -39 N ATOM 1674 CA VAL A 232 15.585 16.187 57.235 1.00 16.78 C ANISOU 1674 CA VAL A 232 2145 2127 2102 0 -15 -12 C ATOM 1675 C VAL A 232 16.802 15.280 57.154 1.00 16.88 C ANISOU 1675 C VAL A 232 2153 2141 2120 1 -19 -17 C ATOM 1676 O VAL A 232 17.823 15.509 57.799 1.00 16.94 O ANISOU 1676 O VAL A 232 2164 2194 2078 20 -23 -32 O ATOM 1677 CB VAL A 232 15.690 17.348 56.235 1.00 16.93 C ANISOU 1677 CB VAL A 232 2212 2160 2063 -17 8 -24 C ATOM 1678 CG1 VAL A 232 16.878 18.253 56.526 1.00 17.53 C ANISOU 1678 CG1 VAL A 232 2249 2204 2208 -43 7 -9 C ATOM 1679 CG2 VAL A 232 15.776 16.807 54.810 1.00 16.21 C ANISOU 1679 CG2 VAL A 232 2087 2071 2002 -16 -35 0 C ATOM 1680 N TYR A 233 16.664 14.179 56.414 1.00 16.88 N ANISOU 1680 N TYR A 233 2183 2122 2108 6 -35 -3 N ATOM 1681 CA TYR A 233 17.757 13.238 56.214 1.00 17.27 C ANISOU 1681 CA TYR A 233 2188 2209 2166 15 -10 -32 C ATOM 1682 C TYR A 233 18.008 13.082 54.715 1.00 16.99 C ANISOU 1682 C TYR A 233 2136 2171 2149 2 11 -17 C ATOM 1683 O TYR A 233 17.066 12.756 53.992 1.00 17.50 O ANISOU 1683 O TYR A 233 2197 2293 2157 -16 -28 -31 O ATOM 1684 CB TYR A 233 17.457 11.865 56.812 1.00 18.48 C ANISOU 1684 CB TYR A 233 2360 2276 2386 -1 -16 16 C ATOM 1685 CG TYR A 233 17.086 11.882 58.277 1.00 20.16 C ANISOU 1685 CG TYR A 233 2622 2543 2495 -12 25 0 C ATOM 1686 CD1 TYR A 233 15.770 12.096 58.667 1.00 20.97 C ANISOU 1686 CD1 TYR A 233 2654 2656 2659 12 8 -14 C ATOM 1687 CD2 TYR A 233 18.049 11.703 59.260 1.00 20.99 C ANISOU 1687 CD2 TYR A 233 2677 2646 2651 19 -45 4 C ATOM 1688 CE1 TYR A 233 15.419 12.125 60.006 1.00 21.72 C ANISOU 1688 CE1 TYR A 233 2777 2747 2728 4 40 -5 C ATOM 1689 CE2 TYR A 233 17.704 11.730 60.599 1.00 21.67 C ANISOU 1689 CE2 TYR A 233 2783 2740 2710 -6 -12 18 C ATOM 1690 CZ TYR A 233 16.393 11.941 60.962 1.00 22.32 C ANISOU 1690 CZ TYR A 233 2826 2836 2818 4 -5 3 C ATOM 1691 OH TYR A 233 16.051 11.967 62.297 1.00 23.32 O ANISOU 1691 OH TYR A 233 3009 2989 2864 -5 -6 -19 O ATOM 1692 N PHE A 234 19.226 13.338 54.276 1.00 16.22 N ANISOU 1692 N PHE A 234 2068 2072 2023 11 -41 -15 N ATOM 1693 CA PHE A 234 19.611 13.105 52.888 1.00 15.89 C ANISOU 1693 CA PHE A 234 2009 2011 2017 4 -16 -6 C ATOM 1694 C PHE A 234 20.226 11.723 52.720 1.00 15.63 C ANISOU 1694 C PHE A 234 2003 1978 1959 -17 -25 -25 C ATOM 1695 O PHE A 234 21.014 11.299 53.569 1.00 15.70 O ANISOU 1695 O PHE A 234 2019 2027 1917 -5 -21 -30 O ATOM 1696 CB PHE A 234 20.605 14.186 52.432 1.00 15.82 C ANISOU 1696 CB PHE A 234 2047 2009 1956 -34 -7 -42 C ATOM 1697 CG PHE A 234 20.034 15.564 52.632 1.00 16.67 C ANISOU 1697 CG PHE A 234 2111 2068 2153 11 -22 7 C ATOM 1698 CD1 PHE A 234 19.134 16.092 51.723 1.00 16.65 C ANISOU 1698 CD1 PHE A 234 2095 2120 2112 -9 -12 3 C ATOM 1699 CD2 PHE A 234 20.384 16.313 53.746 1.00 17.51 C ANISOU 1699 CD2 PHE A 234 2270 2204 2180 -19 -22 -26 C ATOM 1700 CE1 PHE A 234 18.592 17.348 51.915 1.00 17.77 C ANISOU 1700 CE1 PHE A 234 2309 2137 2308 -12 -27 7 C ATOM 1701 CE2 PHE A 234 19.845 17.569 53.939 1.00 18.21 C ANISOU 1701 CE2 PHE A 234 2340 2251 2327 4 -14 -14 C ATOM 1702 CZ PHE A 234 18.950 18.087 53.025 1.00 18.29 C ANISOU 1702 CZ PHE A 234 2374 2295 2280 6 -23 -22 C ATOM 1703 N PHE A 235 19.868 11.008 51.651 1.00 15.07 N ANISOU 1703 N PHE A 235 1924 1916 1886 -3 6 5 N ATOM 1704 CA PHE A 235 20.415 9.665 51.478 1.00 14.76 C ANISOU 1704 CA PHE A 235 1882 1900 1825 -3 -10 -2 C ATOM 1705 C PHE A 235 20.792 9.377 50.030 1.00 14.24 C ANISOU 1705 C PHE A 235 1809 1797 1803 -3 -7 2 C ATOM 1706 O PHE A 235 20.214 9.921 49.094 1.00 14.06 O ANISOU 1706 O PHE A 235 1811 1775 1754 -15 -5 -21 O ATOM 1707 CB PHE A 235 19.469 8.591 52.007 1.00 15.19 C ANISOU 1707 CB PHE A 235 1905 1947 1921 -40 -27 3 C ATOM 1708 CG PHE A 235 18.182 8.410 51.256 1.00 14.02 C ANISOU 1708 CG PHE A 235 1879 1719 1729 -12 -4 -13 C ATOM 1709 CD1 PHE A 235 18.120 7.569 50.156 1.00 12.69 C ANISOU 1709 CD1 PHE A 235 1650 1536 1635 -25 -26 71 C ATOM 1710 CD2 PHE A 235 17.032 9.065 51.656 1.00 14.77 C ANISOU 1710 CD2 PHE A 235 1855 1916 1841 -2 -8 8 C ATOM 1711 CE1 PHE A 235 16.931 7.398 49.470 1.00 12.34 C ANISOU 1711 CE1 PHE A 235 1647 1528 1515 -26 -17 33 C ATOM 1712 CE2 PHE A 235 15.840 8.894 50.977 1.00 14.19 C ANISOU 1712 CE2 PHE A 235 1875 1756 1762 1 -31 -12 C ATOM 1713 CZ PHE A 235 15.795 8.060 49.877 1.00 13.36 C ANISOU 1713 CZ PHE A 235 1729 1679 1670 50 -6 54 C ATOM 1714 N ALA A 236 21.775 8.500 49.873 1.00 14.03 N ANISOU 1714 N ALA A 236 1808 1788 1735 -3 -10 0 N ATOM 1715 CA ALA A 236 22.122 7.968 48.559 1.00 13.71 C ANISOU 1715 CA ALA A 236 1737 1748 1723 8 7 17 C ATOM 1716 C ALA A 236 22.650 6.545 48.719 1.00 13.76 C ANISOU 1716 C ALA A 236 1768 1720 1739 -25 -4 18 C ATOM 1717 O ALA A 236 23.526 6.280 49.538 1.00 13.96 O ANISOU 1717 O ALA A 236 1793 1723 1790 -30 -51 3 O ATOM 1718 CB ALA A 236 23.141 8.839 47.852 1.00 12.86 C ANISOU 1718 CB ALA A 236 1669 1647 1571 3 -61 -20 C ATOM 1719 N PHE A 237 22.086 5.639 47.934 1.00 13.67 N ANISOU 1719 N PHE A 237 1741 1734 1719 -15 -15 21 N ATOM 1720 CA PHE A 237 22.509 4.249 47.921 1.00 13.99 C ANISOU 1720 CA PHE A 237 1809 1757 1750 3 10 -15 C ATOM 1721 C PHE A 237 22.882 3.867 46.489 1.00 13.48 C ANISOU 1721 C PHE A 237 1731 1685 1706 -7 -11 2 C ATOM 1722 O PHE A 237 22.176 4.248 45.551 1.00 13.69 O ANISOU 1722 O PHE A 237 1792 1696 1714 10 -34 -8 O ATOM 1723 CB PHE A 237 21.388 3.340 48.425 1.00 14.74 C ANISOU 1723 CB PHE A 237 1847 1900 1854 -48 16 18 C ATOM 1724 CG PHE A 237 21.629 1.862 48.308 1.00 16.12 C ANISOU 1724 CG PHE A 237 1992 1982 2150 17 28 -1 C ATOM 1725 CD1 PHE A 237 21.293 1.199 47.140 1.00 17.35 C ANISOU 1725 CD1 PHE A 237 2144 2234 2212 -29 8 -53 C ATOM 1726 CD2 PHE A 237 22.168 1.131 49.358 1.00 17.60 C ANISOU 1726 CD2 PHE A 237 2224 2274 2191 20 -7 54 C ATOM 1727 CE1 PHE A 237 21.503 -0.159 47.001 1.00 19.09 C ANISOU 1727 CE1 PHE A 237 2436 2321 2496 4 17 9 C ATOM 1728 CE2 PHE A 237 22.372 -0.231 49.227 1.00 18.75 C ANISOU 1728 CE2 PHE A 237 2361 2328 2434 13 1 31 C ATOM 1729 CZ PHE A 237 22.041 -0.874 48.051 1.00 19.60 C ANISOU 1729 CZ PHE A 237 2479 2508 2459 25 -7 -9 C ATOM 1730 N ASN A 238 23.973 3.137 46.337 1.00 13.24 N ANISOU 1730 N ASN A 238 1702 1675 1653 -22 -13 8 N ATOM 1731 CA ASN A 238 24.220 2.432 45.080 1.00 13.36 C ANISOU 1731 CA ASN A 238 1708 1717 1653 -21 16 9 C ATOM 1732 C ASN A 238 24.793 1.051 45.382 1.00 14.24 C ANISOU 1732 C ASN A 238 1808 1783 1820 13 -7 6 C ATOM 1733 O ASN A 238 25.244 0.781 46.499 1.00 14.65 O ANISOU 1733 O ASN A 238 1859 1816 1892 -29 -54 37 O ATOM 1734 CB ASN A 238 25.083 3.246 44.128 1.00 13.02 C ANISOU 1734 CB ASN A 238 1607 1630 1709 -30 -24 12 C ATOM 1735 CG ASN A 238 26.505 3.464 44.602 1.00 12.36 C ANISOU 1735 CG ASN A 238 1608 1517 1573 -46 -41 -26 C ATOM 1736 OD1 ASN A 238 27.233 2.502 44.842 1.00 13.26 O ANISOU 1736 OD1 ASN A 238 1645 1665 1728 4 -104 9 O ATOM 1737 ND2 ASN A 238 26.898 4.727 44.723 1.00 10.94 N ANISOU 1737 ND2 ASN A 238 1345 1468 1344 -7 -86 -5 N ATOM 1738 N MET A 239 24.681 0.157 44.412 1.00 14.63 N ANISOU 1738 N MET A 239 1834 1841 1884 -4 -10 -36 N ATOM 1739 CA MET A 239 25.192 -1.198 44.550 1.00 15.13 C ANISOU 1739 CA MET A 239 1894 1894 1961 7 -12 18 C ATOM 1740 C MET A 239 25.574 -1.743 43.177 1.00 15.85 C ANISOU 1740 C MET A 239 2020 2005 1999 9 -14 -15 C ATOM 1741 O MET A 239 25.004 -1.329 42.164 1.00 15.68 O ANISOU 1741 O MET A 239 2002 1940 2015 31 -37 -17 O ATOM 1742 CB MET A 239 24.151 -2.114 45.196 1.00 15.14 C ANISOU 1742 CB MET A 239 2012 1862 1879 -2 27 27 C ATOM 1743 CG MET A 239 22.874 -2.253 44.379 1.00 16.94 C ANISOU 1743 CG MET A 239 2098 2211 2127 -2 -42 -46 C ATOM 1744 SD MET A 239 21.719 -3.429 45.105 1.00 18.99 S ANISOU 1744 SD MET A 239 2443 2356 2418 -152 78 -29 S ATOM 1745 CE MET A 239 20.606 -3.709 43.732 1.00 20.46 C ANISOU 1745 CE MET A 239 2567 2662 2545 -28 -33 -4 C ATOM 1746 N ASP A 240 26.552 -2.641 43.156 1.00 16.15 N ANISOU 1746 N ASP A 240 2037 2015 2084 11 -31 26 N ATOM 1747 CA ASP A 240 26.832 -3.397 41.937 1.00 16.96 C ANISOU 1747 CA ASP A 240 2194 2118 2134 -29 -5 -7 C ATOM 1748 C ASP A 240 25.669 -4.364 41.709 1.00 17.12 C ANISOU 1748 C ASP A 240 2169 2128 2207 -8 0 -1 C ATOM 1749 O ASP A 240 25.147 -4.903 42.685 1.00 16.77 O ANISOU 1749 O ASP A 240 2135 2054 2182 -9 -24 -18 O ATOM 1750 CB ASP A 240 28.143 -4.165 42.045 1.00 18.65 C ANISOU 1750 CB ASP A 240 2322 2358 2406 68 8 -3 C ATOM 1751 CG ASP A 240 29.348 -3.279 42.286 1.00 19.81 C ANISOU 1751 CG ASP A 240 2517 2472 2538 -71 -3 8 C ATOM 1752 OD1 ASP A 240 29.286 -2.069 41.988 1.00 19.08 O ANISOU 1752 OD1 ASP A 240 2396 2419 2435 26 -61 -50 O ATOM 1753 OD2 ASP A 240 30.368 -3.805 42.781 1.00 21.21 O ANISOU 1753 OD2 ASP A 240 2598 2711 2751 24 -23 -5 O ATOM 1754 N ILE A 241 25.275 -4.538 40.458 1.00 17.48 N ANISOU 1754 N ILE A 241 2217 2201 2223 25 14 -10 N ATOM 1755 CA ILE A 241 24.199 -5.484 40.144 1.00 18.30 C ANISOU 1755 CA ILE A 241 2266 2318 2370 -6 -18 -16 C ATOM 1756 C ILE A 241 24.512 -6.179 38.826 1.00 18.95 C ANISOU 1756 C ILE A 241 2384 2422 2395 7 2 -21 C ATOM 1757 O ILE A 241 24.799 -5.520 37.826 1.00 18.68 O ANISOU 1757 O ILE A 241 2354 2365 2377 11 28 -55 O ATOM 1758 CB ILE A 241 22.833 -4.782 40.135 1.00 17.40 C ANISOU 1758 CB ILE A 241 2200 2151 2259 -67 -15 11 C ATOM 1759 CG1 ILE A 241 21.696 -5.748 39.780 1.00 16.10 C ANISOU 1759 CG1 ILE A 241 2035 2037 2047 53 2 9 C ATOM 1760 CG2 ILE A 241 22.828 -3.586 39.194 1.00 16.80 C ANISOU 1760 CG2 ILE A 241 2103 2151 2129 -2 3 -17 C ATOM 1761 CD1 ILE A 241 20.314 -5.180 40.050 1.00 15.68 C ANISOU 1761 CD1 ILE A 241 1951 2005 2003 -19 -44 -30 C ATOM 1762 N ASP A 242 24.505 -7.509 38.839 1.00 19.89 N ANISOU 1762 N ASP A 242 2527 2472 2559 1 -3 0 N ATOM 1763 CA ASP A 242 24.720 -8.284 37.619 1.00 20.70 C ANISOU 1763 CA ASP A 242 2670 2602 2594 -12 13 -31 C ATOM 1764 C ASP A 242 23.531 -9.206 37.360 1.00 21.02 C ANISOU 1764 C ASP A 242 2683 2638 2664 -13 3 -8 C ATOM 1765 O ASP A 242 23.524 -10.006 36.425 1.00 21.36 O ANISOU 1765 O ASP A 242 2752 2678 2686 -6 -8 -15 O ATOM 1766 CB ASP A 242 26.013 -9.082 37.670 1.00 22.06 C ANISOU 1766 CB ASP A 242 2716 2776 2889 19 -15 -54 C ATOM 1767 CG ASP A 242 26.096 -10.178 38.705 1.00 24.33 C ANISOU 1767 CG ASP A 242 3181 3014 3047 -12 -13 37 C ATOM 1768 OD1 ASP A 242 25.109 -10.477 39.402 1.00 25.16 O ANISOU 1768 OD1 ASP A 242 3220 3151 3186 -15 25 19 O ATOM 1769 OD2 ASP A 242 27.192 -10.776 38.833 1.00 25.65 O ANISOU 1769 OD2 ASP A 242 3287 3169 3288 39 -29 10 O ATOM 1770 N ASN A 243 22.528 -9.084 38.218 1.00 21.07 N ANISOU 1770 N ASN A 243 2681 2642 2684 5 8 -22 N ATOM 1771 CA ASN A 243 21.311 -9.883 38.118 1.00 21.48 C ANISOU 1771 CA ASN A 243 2697 2722 2741 -8 0 -47 C ATOM 1772 C ASN A 243 20.112 -8.989 38.391 1.00 21.34 C ANISOU 1772 C ASN A 243 2697 2696 2715 -11 -4 -19 C ATOM 1773 O ASN A 243 19.969 -8.445 39.490 1.00 21.36 O ANISOU 1773 O ASN A 243 2706 2692 2716 -5 -13 -25 O ATOM 1774 CB ASN A 243 21.389 -11.052 39.095 1.00 23.56 C ANISOU 1774 CB ASN A 243 3105 2920 2927 66 1 50 C ATOM 1775 CG ASN A 243 20.148 -11.905 39.203 1.00 26.35 C ANISOU 1775 CG ASN A 243 3283 3292 3438 -70 8 -31 C ATOM 1776 OD1 ASN A 243 19.168 -11.733 38.479 1.00 26.48 O ANISOU 1776 OD1 ASN A 243 3361 3306 3393 -13 -20 -51 O ATOM 1777 ND2 ASN A 243 20.176 -12.854 40.137 1.00 27.64 N ANISOU 1777 ND2 ASN A 243 3528 3462 3512 -6 12 17 N ATOM 1778 N GLU A 244 19.198 -8.879 37.427 1.00 21.17 N ANISOU 1778 N GLU A 244 2701 2647 2695 -30 11 -12 N ATOM 1779 CA GLU A 244 18.073 -7.958 37.561 1.00 22.10 C ANISOU 1779 CA GLU A 244 2768 2741 2888 -4 89 -9 C ATOM 1780 C GLU A 244 17.113 -8.350 38.669 1.00 20.97 C ANISOU 1780 C GLU A 244 2672 2588 2709 -12 -19 -21 C ATOM 1781 O GLU A 244 16.418 -7.502 39.240 1.00 21.11 O ANISOU 1781 O GLU A 244 2669 2606 2744 -20 -39 -49 O ATOM 1782 CB GLU A 244 17.341 -7.788 36.224 1.00 27.02 C ANISOU 1782 CB GLU A 244 3519 3618 3128 -69 -123 11 C ATOM 1783 CG GLU A 244 16.379 -6.614 36.210 1.00 32.68 C ANISOU 1783 CG GLU A 244 4062 3979 4375 78 59 -43 C ATOM 1784 CD GLU A 244 15.847 -6.249 34.841 1.00 37.58 C ANISOU 1784 CD GLU A 244 4842 4792 4646 -29 -84 70 C ATOM 1785 OE1 GLU A 244 16.373 -6.735 33.820 1.00 38.58 O ANISOU 1785 OE1 GLU A 244 4910 4886 4861 14 31 -7 O ATOM 1786 OE2 GLU A 244 14.882 -5.453 34.780 1.00 39.36 O ANISOU 1786 OE2 GLU A 244 4974 4958 5024 32 -19 28 O ATOM 1787 N SER A 245 17.071 -9.612 39.069 1.00 20.22 N ANISOU 1787 N SER A 245 2577 2582 2524 -26 -3 -42 N ATOM 1788 CA SER A 245 16.352 -10.112 40.220 1.00 20.30 C ANISOU 1788 CA SER A 245 2564 2665 2485 -26 -17 -58 C ATOM 1789 C SER A 245 16.670 -9.405 41.529 1.00 18.90 C ANISOU 1789 C SER A 245 2347 2422 2413 -17 9 -5 C ATOM 1790 O SER A 245 15.816 -9.308 42.414 1.00 18.39 O ANISOU 1790 O SER A 245 2293 2308 2387 -1 -15 -24 O ATOM 1791 CB SER A 245 16.657 -11.612 40.377 1.00 25.07 C ANISOU 1791 CB SER A 245 3249 2893 3385 45 -14 -25 C ATOM 1792 OG SER A 245 16.255 -12.092 41.646 1.00 29.13 O ANISOU 1792 OG SER A 245 3796 3675 3595 -2 48 34 O ATOM 1793 N LYS A 246 17.886 -8.902 41.700 1.00 17.92 N ANISOU 1793 N LYS A 246 2345 2211 2252 -5 -13 -29 N ATOM 1794 CA LYS A 246 18.332 -8.258 42.919 1.00 17.54 C ANISOU 1794 CA LYS A 246 2333 2121 2210 20 7 -2 C ATOM 1795 C LYS A 246 17.941 -6.794 43.027 1.00 16.32 C ANISOU 1795 C LYS A 246 2107 2053 2040 -2 -28 -3 C ATOM 1796 O LYS A 246 18.208 -6.156 44.050 1.00 15.93 O ANISOU 1796 O LYS A 246 2039 2002 2013 4 -5 2 O ATOM 1797 CB LYS A 246 19.862 -8.362 43.024 1.00 21.26 C ANISOU 1797 CB LYS A 246 2469 2877 2732 -37 4 -23 C ATOM 1798 CG LYS A 246 20.378 -9.781 43.174 1.00 26.49 C ANISOU 1798 CG LYS A 246 3336 3161 3567 82 -21 -26 C ATOM 1799 CD LYS A 246 20.206 -10.277 44.601 1.00 31.27 C ANISOU 1799 CD LYS A 246 4071 4000 3811 -64 43 26 C ATOM 1800 CE LYS A 246 21.164 -11.421 44.896 1.00 34.60 C ANISOU 1800 CE LYS A 246 4343 4301 4502 68 -8 11 C ATOM 1801 NZ LYS A 246 21.171 -11.769 46.344 1.00 36.73 N ANISOU 1801 NZ LYS A 246 4694 4650 4613 25 -1 16 N ATOM 1802 N LEU A 247 17.226 -6.254 42.045 1.00 15.72 N ANISOU 1802 N LEU A 247 2045 1932 1995 8 5 -28 N ATOM 1803 CA LEU A 247 16.972 -4.828 41.935 1.00 14.91 C ANISOU 1803 CA LEU A 247 1894 1901 1871 8 15 -16 C ATOM 1804 C LEU A 247 16.267 -4.184 43.109 1.00 14.07 C ANISOU 1804 C LEU A 247 1789 1762 1793 -21 -18 14 C ATOM 1805 O LEU A 247 16.682 -3.098 43.541 1.00 13.83 O ANISOU 1805 O LEU A 247 1779 1754 1721 -12 10 8 O ATOM 1806 CB LEU A 247 16.226 -4.518 40.625 1.00 15.47 C ANISOU 1806 CB LEU A 247 1988 2006 1883 9 -4 -7 C ATOM 1807 CG LEU A 247 16.210 -3.037 40.236 1.00 15.95 C ANISOU 1807 CG LEU A 247 1983 2033 2044 -12 6 17 C ATOM 1808 CD1 LEU A 247 17.617 -2.524 39.965 1.00 14.69 C ANISOU 1808 CD1 LEU A 247 1936 1830 1814 10 16 6 C ATOM 1809 CD2 LEU A 247 15.302 -2.798 39.040 1.00 16.40 C ANISOU 1809 CD2 LEU A 247 2110 2065 2058 6 -39 11 C ATOM 1810 N PRO A 248 15.270 -4.824 43.716 1.00 13.79 N ANISOU 1810 N PRO A 248 1747 1751 1741 -13 -18 -25 N ATOM 1811 CA PRO A 248 14.542 -4.269 44.838 1.00 13.66 C ANISOU 1811 CA PRO A 248 1756 1703 1731 -15 -9 -12 C ATOM 1812 C PRO A 248 15.375 -3.972 46.070 1.00 13.59 C ANISOU 1812 C PRO A 248 1781 1679 1702 -9 -3 2 C ATOM 1813 O PRO A 248 14.977 -3.146 46.897 1.00 13.72 O ANISOU 1813 O PRO A 248 1841 1682 1691 24 -5 11 O ATOM 1814 CB PRO A 248 13.476 -5.311 45.164 1.00 13.71 C ANISOU 1814 CB PRO A 248 1774 1712 1724 -20 12 0 C ATOM 1815 CG PRO A 248 13.257 -6.052 43.894 1.00 13.40 C ANISOU 1815 CG PRO A 248 1735 1650 1708 -19 -2 19 C ATOM 1816 CD PRO A 248 14.540 -5.974 43.121 1.00 13.57 C ANISOU 1816 CD PRO A 248 1733 1684 1741 7 5 -8 C ATOM 1817 N LEU A 249 16.550 -4.569 46.213 1.00 13.75 N ANISOU 1817 N LEU A 249 1789 1681 1755 -13 -6 -2 N ATOM 1818 CA LEU A 249 17.494 -4.262 47.272 1.00 14.50 C ANISOU 1818 CA LEU A 249 1842 1843 1822 -7 -51 7 C ATOM 1819 C LEU A 249 17.965 -2.817 47.264 1.00 15.10 C ANISOU 1819 C LEU A 249 1951 1879 1909 -26 -13 32 C ATOM 1820 O LEU A 249 18.320 -2.288 48.327 1.00 16.10 O ANISOU 1820 O LEU A 249 2120 2027 1971 -25 -11 -39 O ATOM 1821 CB LEU A 249 18.700 -5.205 47.197 1.00 14.59 C ANISOU 1821 CB LEU A 249 1876 1829 1838 2 -8 -9 C ATOM 1822 CG LEU A 249 18.381 -6.700 47.294 1.00 15.34 C ANISOU 1822 CG LEU A 249 1965 1867 1997 2 5 2 C ATOM 1823 CD1 LEU A 249 19.633 -7.522 47.036 1.00 14.90 C ANISOU 1823 CD1 LEU A 249 1890 1845 1928 -33 7 37 C ATOM 1824 CD2 LEU A 249 17.785 -7.036 48.655 1.00 16.20 C ANISOU 1824 CD2 LEU A 249 2088 2030 2039 -30 9 25 C ATOM 1825 N ARG A 250 17.934 -2.124 46.126 1.00 14.56 N ANISOU 1825 N ARG A 250 1857 1816 1857 -23 1 -12 N ATOM 1826 CA ARG A 250 18.242 -0.704 46.097 1.00 14.07 C ANISOU 1826 CA ARG A 250 1805 1790 1749 -11 24 11 C ATOM 1827 C ARG A 250 17.297 0.126 46.958 1.00 14.03 C ANISOU 1827 C ARG A 250 1789 1771 1768 -2 1 3 C ATOM 1828 O ARG A 250 17.713 1.201 47.397 1.00 14.48 O ANISOU 1828 O ARG A 250 1847 1827 1829 -74 -61 1 O ATOM 1829 CB ARG A 250 18.257 -0.153 44.673 1.00 13.62 C ANISOU 1829 CB ARG A 250 1717 1729 1729 9 -8 3 C ATOM 1830 CG ARG A 250 16.881 -0.088 44.027 1.00 14.08 C ANISOU 1830 CG ARG A 250 1772 1814 1765 -8 -54 37 C ATOM 1831 CD ARG A 250 17.017 0.191 42.534 1.00 13.68 C ANISOU 1831 CD ARG A 250 1709 1740 1749 -8 -13 17 C ATOM 1832 NE ARG A 250 15.698 0.195 41.906 1.00 13.28 N ANISOU 1832 NE ARG A 250 1751 1658 1638 -10 -60 -36 N ATOM 1833 CZ ARG A 250 15.461 0.582 40.660 1.00 12.38 C ANISOU 1833 CZ ARG A 250 1634 1471 1597 -36 23 -14 C ATOM 1834 NH1 ARG A 250 16.453 1.005 39.891 1.00 11.95 N ANISOU 1834 NH1 ARG A 250 1614 1381 1546 -25 24 -88 N ATOM 1835 NH2 ARG A 250 14.216 0.534 40.203 1.00 13.39 N ANISOU 1835 NH2 ARG A 250 1670 1640 1778 41 -16 35 N ATOM 1836 N LYS A 251 16.057 -0.294 47.176 1.00 13.80 N ANISOU 1836 N LYS A 251 1778 1744 1721 -23 -11 -30 N ATOM 1837 CA LYS A 251 15.190 0.374 48.139 1.00 14.34 C ANISOU 1837 CA LYS A 251 1834 1808 1808 18 27 -23 C ATOM 1838 C LYS A 251 15.135 -0.359 49.475 1.00 14.73 C ANISOU 1838 C LYS A 251 1901 1850 1846 -4 3 6 C ATOM 1839 O LYS A 251 15.038 0.309 50.513 1.00 14.90 O ANISOU 1839 O LYS A 251 1971 1872 1817 -7 -23 36 O ATOM 1840 CB LYS A 251 13.772 0.544 47.589 1.00 15.73 C ANISOU 1840 CB LYS A 251 1893 2057 2026 -43 -54 -34 C ATOM 1841 CG LYS A 251 13.647 1.528 46.436 1.00 18.30 C ANISOU 1841 CG LYS A 251 2471 2236 2245 -44 25 57 C ATOM 1842 CD LYS A 251 12.178 1.748 46.091 1.00 22.62 C ANISOU 1842 CD LYS A 251 2684 2958 2951 19 -30 -72 C ATOM 1843 CE LYS A 251 12.008 2.716 44.936 1.00 26.67 C ANISOU 1843 CE LYS A 251 3530 3294 3311 3 24 78 C ATOM 1844 NZ LYS A 251 10.595 2.804 44.476 1.00 29.77 N ANISOU 1844 NZ LYS A 251 3683 3779 3848 25 -26 -8 N ATOM 1845 N SER A 252 15.202 -1.690 49.469 1.00 14.89 N ANISOU 1845 N SER A 252 1905 1866 1885 8 -14 23 N ATOM 1846 CA SER A 252 14.982 -2.426 50.718 1.00 15.20 C ANISOU 1846 CA SER A 252 1951 1924 1902 -7 2 28 C ATOM 1847 C SER A 252 16.163 -2.287 51.670 1.00 15.22 C ANISOU 1847 C SER A 252 1947 1913 1923 -10 -7 20 C ATOM 1848 O SER A 252 15.932 -2.140 52.878 1.00 15.51 O ANISOU 1848 O SER A 252 1974 1967 1952 -13 15 20 O ATOM 1849 CB SER A 252 14.631 -3.888 50.467 1.00 16.26 C ANISOU 1849 CB SER A 252 2146 1965 2066 -63 -1 44 C ATOM 1850 OG SER A 252 15.677 -4.606 49.855 1.00 18.22 O ANISOU 1850 OG SER A 252 2358 2221 2343 61 43 -19 O ATOM 1851 N ILE A 253 17.395 -2.285 51.163 1.00 15.23 N ANISOU 1851 N ILE A 253 1952 1928 1905 7 -5 6 N ATOM 1852 CA ILE A 253 18.547 -2.126 52.058 1.00 15.79 C ANISOU 1852 CA ILE A 253 2002 2009 1987 -11 -38 -1 C ATOM 1853 C ILE A 253 18.541 -0.774 52.748 1.00 16.02 C ANISOU 1853 C ILE A 253 2040 2014 2031 -11 -26 -2 C ATOM 1854 O ILE A 253 18.563 -0.708 53.979 1.00 16.28 O ANISOU 1854 O ILE A 253 2093 2046 2046 -5 2 -13 O ATOM 1855 CB ILE A 253 19.879 -2.441 51.362 1.00 16.57 C ANISOU 1855 CB ILE A 253 2067 2095 2132 -9 12 -28 C ATOM 1856 CG1 ILE A 253 19.918 -3.936 51.030 1.00 16.23 C ANISOU 1856 CG1 ILE A 253 2062 2077 2029 -1 1 -6 C ATOM 1857 CG2 ILE A 253 21.069 -2.051 52.229 1.00 16.53 C ANISOU 1857 CG2 ILE A 253 2057 2137 2089 8 3 46 C ATOM 1858 CD1 ILE A 253 21.124 -4.398 50.251 1.00 15.94 C ANISOU 1858 CD1 ILE A 253 2049 1988 2020 -1 -9 -20 C ATOM 1859 N PRO A 254 18.456 0.322 51.999 1.00 16.34 N ANISOU 1859 N PRO A 254 2088 2034 2087 -11 -11 10 N ATOM 1860 CA PRO A 254 18.379 1.654 52.568 1.00 16.60 C ANISOU 1860 CA PRO A 254 2140 2051 2114 10 -2 10 C ATOM 1861 C PRO A 254 17.211 1.845 53.519 1.00 16.48 C ANISOU 1861 C PRO A 254 2132 2048 2082 13 -17 22 C ATOM 1862 O PRO A 254 17.323 2.494 54.561 1.00 16.46 O ANISOU 1862 O PRO A 254 2120 2048 2085 25 -28 18 O ATOM 1863 CB PRO A 254 18.222 2.571 51.360 1.00 16.90 C ANISOU 1863 CB PRO A 254 2201 2098 2123 0 3 22 C ATOM 1864 CG PRO A 254 18.662 1.799 50.178 1.00 16.76 C ANISOU 1864 CG PRO A 254 2172 2089 2107 3 -15 24 C ATOM 1865 CD PRO A 254 18.687 0.345 50.536 1.00 16.50 C ANISOU 1865 CD PRO A 254 2117 2063 2090 -10 -18 -2 C ATOM 1866 N THR A 255 16.046 1.311 53.152 1.00 16.61 N ANISOU 1866 N THR A 255 2148 2055 2108 0 -22 -4 N ATOM 1867 CA THR A 255 14.848 1.427 53.975 1.00 17.44 C ANISOU 1867 CA THR A 255 2230 2214 2182 3 32 20 C ATOM 1868 C THR A 255 15.057 0.724 55.310 1.00 17.43 C ANISOU 1868 C THR A 255 2235 2205 2183 -2 12 14 C ATOM 1869 O THR A 255 14.782 1.306 56.358 1.00 17.54 O ANISOU 1869 O THR A 255 2281 2234 2151 -6 -4 25 O ATOM 1870 CB THR A 255 13.604 0.890 53.251 1.00 18.48 C ANISOU 1870 CB THR A 255 2312 2346 2362 -38 -20 -9 C ATOM 1871 OG1 THR A 255 13.407 1.660 52.051 1.00 19.27 O ANISOU 1871 OG1 THR A 255 2485 2493 2343 37 5 -14 O ATOM 1872 CG2 THR A 255 12.356 1.004 54.110 1.00 18.61 C ANISOU 1872 CG2 THR A 255 2369 2348 2356 16 3 -6 C ATOM 1873 N LYS A 256 15.589 -0.493 55.273 1.00 17.57 N ANISOU 1873 N LYS A 256 2228 2224 2225 6 5 3 N ATOM 1874 CA LYS A 256 15.928 -1.211 56.497 1.00 18.10 C ANISOU 1874 CA LYS A 256 2298 2306 2273 -6 -9 34 C ATOM 1875 C LYS A 256 16.927 -0.446 57.351 1.00 18.28 C ANISOU 1875 C LYS A 256 2309 2332 2305 -18 -2 8 C ATOM 1876 O LYS A 256 16.746 -0.347 58.571 1.00 18.85 O ANISOU 1876 O LYS A 256 2413 2418 2332 -25 22 17 O ATOM 1877 CB LYS A 256 16.452 -2.610 56.165 1.00 19.40 C ANISOU 1877 CB LYS A 256 2557 2402 2414 69 44 16 C ATOM 1878 CG LYS A 256 15.371 -3.562 55.668 1.00 21.88 C ANISOU 1878 CG LYS A 256 2712 2822 2779 -111 -53 -7 C ATOM 1879 CD LYS A 256 15.930 -4.967 55.498 1.00 25.28 C ANISOU 1879 CD LYS A 256 3304 3115 3187 130 46 32 C ATOM 1880 CE LYS A 256 14.856 -5.953 55.079 1.00 28.96 C ANISOU 1880 CE LYS A 256 3590 3566 3846 -105 2 -48 C ATOM 1881 NZ LYS A 256 14.376 -5.711 53.692 1.00 32.13 N ANISOU 1881 NZ LYS A 256 4104 4071 4035 -1 -24 17 N ATOM 1882 N ILE A 257 17.977 0.109 56.748 1.00 17.91 N ANISOU 1882 N ILE A 257 2293 2262 2249 -14 -13 11 N ATOM 1883 CA ILE A 257 18.924 0.922 57.510 1.00 17.90 C ANISOU 1883 CA ILE A 257 2258 2283 2258 -37 5 25 C ATOM 1884 C ILE A 257 18.226 2.119 58.136 1.00 18.40 C ANISOU 1884 C ILE A 257 2330 2335 2326 -13 17 3 C ATOM 1885 O ILE A 257 18.357 2.358 59.342 1.00 18.80 O ANISOU 1885 O ILE A 257 2437 2368 2339 -2 -19 14 O ATOM 1886 CB ILE A 257 20.129 1.358 56.661 1.00 16.80 C ANISOU 1886 CB ILE A 257 2201 2141 2042 -12 -44 -3 C ATOM 1887 CG1 ILE A 257 20.939 0.125 56.256 1.00 17.65 C ANISOU 1887 CG1 ILE A 257 2206 2239 2263 28 -10 13 C ATOM 1888 CG2 ILE A 257 21.005 2.348 57.414 1.00 16.76 C ANISOU 1888 CG2 ILE A 257 2157 2119 2092 -17 -8 -1 C ATOM 1889 CD1 ILE A 257 22.075 0.378 55.290 1.00 18.01 C ANISOU 1889 CD1 ILE A 257 2275 2315 2252 -9 3 31 C ATOM 1890 N MET A 258 17.449 2.865 57.357 1.00 18.95 N ANISOU 1890 N MET A 258 2418 2411 2370 -1 -11 42 N ATOM 1891 CA MET A 258 16.794 4.065 57.865 1.00 19.72 C ANISOU 1891 CA MET A 258 2552 2470 2472 49 -54 2 C ATOM 1892 C MET A 258 15.744 3.751 58.919 1.00 21.24 C ANISOU 1892 C MET A 258 2708 2718 2645 30 28 20 C ATOM 1893 O MET A 258 15.609 4.495 59.895 1.00 21.43 O ANISOU 1893 O MET A 258 2742 2730 2671 14 22 -9 O ATOM 1894 CB MET A 258 16.202 4.888 56.717 1.00 18.31 C ANISOU 1894 CB MET A 258 2240 2365 2352 -21 38 -8 C ATOM 1895 CG MET A 258 17.262 5.648 55.935 1.00 16.94 C ANISOU 1895 CG MET A 258 2175 2105 2156 32 -75 38 C ATOM 1896 SD MET A 258 16.597 6.740 54.672 1.00 16.22 S ANISOU 1896 SD MET A 258 2108 2013 2043 24 -59 -25 S ATOM 1897 CE MET A 258 16.189 5.590 53.366 1.00 15.96 C ANISOU 1897 CE MET A 258 2062 1981 2022 0 -14 -4 C ATOM 1898 N GLU A 259 15.012 2.652 58.764 1.00 22.64 N ANISOU 1898 N GLU A 259 2899 2808 2894 -20 -37 -21 N ATOM 1899 CA GLU A 259 14.068 2.217 59.789 1.00 24.62 C ANISOU 1899 CA GLU A 259 3122 3130 3103 2 82 40 C ATOM 1900 C GLU A 259 14.772 1.818 61.075 1.00 25.46 C ANISOU 1900 C GLU A 259 3266 3227 3182 -14 -8 30 C ATOM 1901 O GLU A 259 14.287 2.148 62.164 1.00 25.92 O ANISOU 1901 O GLU A 259 3317 3295 3238 -15 27 12 O ATOM 1902 CB GLU A 259 13.167 1.105 59.243 1.00 26.78 C ANISOU 1902 CB GLU A 259 3404 3301 3470 -97 7 -54 C ATOM 1903 CG GLU A 259 12.226 1.610 58.157 1.00 29.00 C ANISOU 1903 CG GLU A 259 3703 3703 3613 75 -3 48 C ATOM 1904 CD GLU A 259 11.224 0.594 57.663 1.00 30.99 C ANISOU 1904 CD GLU A 259 3924 3920 3933 -62 -7 -44 C ATOM 1905 OE1 GLU A 259 11.374 -0.613 57.945 1.00 31.98 O ANISOU 1905 OE1 GLU A 259 4107 4008 4035 -2 5 25 O ATOM 1906 OE2 GLU A 259 10.258 0.991 56.973 1.00 31.63 O ANISOU 1906 OE2 GLU A 259 3973 4003 4042 8 15 17 O ATOM 1907 N SER A 260 15.952 1.213 61.007 1.00 26.25 N ANISOU 1907 N SER A 260 3317 3321 3335 -2 28 0 N ATOM 1908 CA SER A 260 16.723 0.854 62.190 1.00 27.29 C ANISOU 1908 CA SER A 260 3461 3472 3436 -7 -30 39 C ATOM 1909 C SER A 260 17.249 2.074 62.941 1.00 28.00 C ANISOU 1909 C SER A 260 3567 3536 3535 -14 -24 -15 C ATOM 1910 O SER A 260 17.495 2.015 64.147 1.00 28.41 O ANISOU 1910 O SER A 260 3628 3616 3551 -4 -16 9 O ATOM 1911 CB SER A 260 17.895 -0.059 61.820 1.00 28.33 C ANISOU 1911 CB SER A 260 3606 3569 3590 50 -2 -12 C ATOM 1912 OG SER A 260 18.958 0.683 61.250 1.00 29.47 O ANISOU 1912 OG SER A 260 3714 3750 3732 -17 5 39 O ATOM 1913 N GLU A 261 17.431 3.190 62.248 1.00 28.23 N ANISOU 1913 N GLU A 261 3594 3572 3561 -7 -23 15 N ATOM 1914 CA GLU A 261 17.812 4.455 62.844 1.00 28.81 C ANISOU 1914 CA GLU A 261 3683 3609 3655 5 -29 -20 C ATOM 1915 C GLU A 261 16.625 5.288 63.305 1.00 29.02 C ANISOU 1915 C GLU A 261 3698 3658 3672 6 2 -2 C ATOM 1916 O GLU A 261 16.826 6.382 63.841 1.00 29.11 O ANISOU 1916 O GLU A 261 3706 3675 3682 -11 21 -7 O ATOM 1917 CB GLU A 261 18.626 5.277 61.833 1.00 30.02 C ANISOU 1917 CB GLU A 261 3876 3773 3759 -62 14 23 C ATOM 1918 CG GLU A 261 19.968 4.661 61.484 1.00 32.36 C ANISOU 1918 CG GLU A 261 4063 4059 4172 37 74 -1 C ATOM 1919 CD GLU A 261 20.970 4.738 62.621 1.00 34.66 C ANISOU 1919 CD GLU A 261 4367 4454 4348 -31 -70 22 C ATOM 1920 OE1 GLU A 261 20.796 5.590 63.515 1.00 35.66 O ANISOU 1920 OE1 GLU A 261 4506 4515 4529 -6 -9 -36 O ATOM 1921 OE2 GLU A 261 21.933 3.945 62.616 1.00 35.74 O ANISOU 1921 OE2 GLU A 261 4515 4526 4539 30 -12 1 O ATOM 1922 N GLY A 262 15.402 4.830 63.064 1.00 29.11 N ANISOU 1922 N GLY A 262 3713 3672 3677 -12 -2 6 N ATOM 1923 CA GLY A 262 14.229 5.511 63.599 1.00 29.52 C ANISOU 1923 CA GLY A 262 3743 3729 3746 -3 15 1 C ATOM 1924 C GLY A 262 13.593 6.425 62.571 1.00 29.76 C ANISOU 1924 C GLY A 262 3773 3761 3772 1 3 9 C ATOM 1925 O GLY A 262 12.541 7.024 62.816 1.00 29.92 O ANISOU 1925 O GLY A 262 3787 3796 3784 0 22 -27 O ATOM 1926 N ILE A 263 14.184 6.494 61.380 1.00 29.61 N ANISOU 1926 N ILE A 263 3764 3732 3754 -4 13 3 N ATOM 1927 CA ILE A 263 13.620 7.222 60.255 1.00 29.81 C ANISOU 1927 CA ILE A 263 3790 3790 3745 6 62 29 C ATOM 1928 C ILE A 263 12.461 6.383 59.712 1.00 30.91 C ANISOU 1928 C ILE A 263 3932 3885 3926 -35 -26 11 C ATOM 1929 O ILE A 263 12.499 5.561 58.820 1.00 30.83 O ANISOU 1929 O ILE A 263 3911 3867 3935 -3 -11 24 O ATOM 1930 CB ILE A 263 14.607 7.541 59.144 1.00 26.85 C ANISOU 1930 CB ILE A 263 3393 3341 3469 -24 -132 -43 C ATOM 1931 CG1 ILE A 263 15.815 8.215 59.801 1.00 24.86 C ANISOU 1931 CG1 ILE A 263 3157 3160 3127 32 48 35 C ATOM 1932 CG2 ILE A 263 13.993 8.447 58.091 1.00 26.69 C ANISOU 1932 CG2 ILE A 263 3396 3369 3377 1 -8 -15 C ATOM 1933 CD1 ILE A 263 17.020 8.338 58.903 1.00 23.93 C ANISOU 1933 CD1 ILE A 263 3036 3022 3036 -4 -24 -21 C ATOM 1934 N ILE A 264 11.395 6.684 60.426 1.00 32.16 N ANISOU 1934 N ILE A 264 4063 4069 4088 33 33 -2 N ATOM 1935 CA ILE A 264 10.141 5.997 60.384 1.00 33.12 C ANISOU 1935 CA ILE A 264 4136 4198 4249 -8 1 11 C ATOM 1936 C ILE A 264 10.179 4.768 59.515 1.00 33.99 C ANISOU 1936 C ILE A 264 4309 4286 4321 13 9 -33 C ATOM 1937 O ILE A 264 9.755 3.700 59.998 1.00 34.65 O ANISOU 1937 O ILE A 264 4427 4353 4386 14 19 14 O ATOM 1938 CB ILE A 264 8.976 6.966 60.079 1.00 32.70 C ANISOU 1938 CB ILE A 264 4157 4100 4167 -26 -2 20 C ATOM 1939 CG1 ILE A 264 8.265 6.636 58.730 1.00 32.90 C ANISOU 1939 CG1 ILE A 264 4182 4156 4164 -5 -1 -8 C ATOM 1940 CG2 ILE A 264 9.425 8.407 60.223 1.00 32.68 C ANISOU 1940 CG2 ILE A 264 4163 4092 4162 0 -22 -18 C ATOM 1941 CD1 ILE A 264 6.816 7.124 58.753 1.00 33.25 C ANISOU 1941 CD1 ILE A 264 4216 4204 4212 -1 -2 4 C TER 1942 ILE A 264 ATOM 1943 N ILE B 22 -37.197 12.702 0.050 1.00 28.86 N ANISOU 1943 N ILE B 22 3645 3637 3684 -8 -16 20 N ATOM 1944 CA ILE B 22 -36.547 14.047 -0.001 1.00 28.97 C ANISOU 1944 CA ILE B 22 3674 3644 3690 -16 -7 10 C ATOM 1945 C ILE B 22 -37.399 15.097 0.696 1.00 29.24 C ANISOU 1945 C ILE B 22 3709 3661 3738 -6 4 5 C ATOM 1946 O ILE B 22 -38.621 15.130 0.551 1.00 29.65 O ANISOU 1946 O ILE B 22 3726 3726 3815 -4 1 27 O ATOM 1947 CB ILE B 22 -36.224 14.462 -1.445 1.00 28.57 C ANISOU 1947 CB ILE B 22 3632 3544 3681 -36 9 -9 C ATOM 1948 CG1 ILE B 22 -35.454 15.784 -1.474 1.00 27.15 C ANISOU 1948 CG1 ILE B 22 3436 3449 3431 27 19 18 C ATOM 1949 CG2 ILE B 22 -37.493 14.558 -2.283 1.00 29.34 C ANISOU 1949 CG2 ILE B 22 3697 3724 3728 15 -5 2 C ATOM 1950 CD1 ILE B 22 -34.898 16.162 -2.828 1.00 26.61 C ANISOU 1950 CD1 ILE B 22 3360 3365 3386 3 2 -17 C ATOM 1951 N THR B 23 -36.750 15.960 1.468 1.00 29.12 N ANISOU 1951 N THR B 23 3672 3647 3745 -16 7 12 N ATOM 1952 CA THR B 23 -37.433 16.996 2.232 1.00 29.42 C ANISOU 1952 CA THR B 23 3683 3668 3829 -7 33 4 C ATOM 1953 C THR B 23 -36.936 18.388 1.858 1.00 28.90 C ANISOU 1953 C THR B 23 3635 3635 3710 11 18 10 C ATOM 1954 O THR B 23 -35.902 18.511 1.199 1.00 28.29 O ANISOU 1954 O THR B 23 3609 3536 3604 18 0 27 O ATOM 1955 CB THR B 23 -37.242 16.767 3.743 1.00 32.49 C ANISOU 1955 CB THR B 23 4161 4188 3995 -34 -67 52 C ATOM 1956 OG1 THR B 23 -37.997 17.739 4.477 1.00 35.02 O ANISOU 1956 OG1 THR B 23 4438 4420 4449 63 35 -35 O ATOM 1957 CG2 THR B 23 -35.775 16.871 4.129 1.00 31.97 C ANISOU 1957 CG2 THR B 23 4081 4011 4054 15 13 8 C ATOM 1958 N GLU B 24 -37.652 19.424 2.289 1.00 28.73 N ANISOU 1958 N GLU B 24 3626 3625 3665 6 8 15 N ATOM 1959 CA GLU B 24 -37.264 20.790 1.959 1.00 28.81 C ANISOU 1959 CA GLU B 24 3631 3633 3683 3 6 18 C ATOM 1960 C GLU B 24 -36.750 21.537 3.184 1.00 29.13 C ANISOU 1960 C GLU B 24 3690 3684 3695 7 0 2 C ATOM 1961 O GLU B 24 -37.368 21.576 4.245 1.00 29.38 O ANISOU 1961 O GLU B 24 3678 3757 3727 13 19 10 O ATOM 1962 CB GLU B 24 -38.411 21.565 1.305 1.00 28.60 C ANISOU 1962 CB GLU B 24 3607 3611 3649 -2 12 4 C ATOM 1963 CG GLU B 24 -37.971 22.859 0.637 1.00 29.02 C ANISOU 1963 CG GLU B 24 3694 3625 3706 -14 35 -2 C ATOM 1964 CD GLU B 24 -39.043 23.516 -0.208 1.00 30.12 C ANISOU 1964 CD GLU B 24 3854 3863 3728 -17 -57 21 C ATOM 1965 OE1 GLU B 24 -39.176 23.154 -1.396 1.00 27.84 O ANISOU 1965 OE1 GLU B 24 3481 3474 3622 4 -11 52 O ATOM 1966 OE2 GLU B 24 -39.755 24.407 0.307 1.00 32.19 O ANISOU 1966 OE2 GLU B 24 4073 4048 4111 72 21 -9 O ATOM 1967 N ASN B 25 -35.571 22.128 3.032 1.00 29.27 N ANISOU 1967 N ASN B 25 3720 3690 3710 0 16 22 N ATOM 1968 CA ASN B 25 -34.989 23.001 4.046 1.00 29.75 C ANISOU 1968 CA ASN B 25 3816 3735 3752 -22 23 -3 C ATOM 1969 C ASN B 25 -34.972 24.424 3.498 1.00 29.59 C ANISOU 1969 C ASN B 25 3768 3732 3743 -8 9 0 C ATOM 1970 O ASN B 25 -34.096 24.779 2.708 1.00 29.40 O ANISOU 1970 O ASN B 25 3735 3713 3723 -4 -6 8 O ATOM 1971 CB ASN B 25 -33.587 22.524 4.409 1.00 31.75 C ANISOU 1971 CB ASN B 25 3941 4034 4088 56 11 55 C ATOM 1972 CG ASN B 25 -32.950 23.238 5.577 1.00 33.30 C ANISOU 1972 CG ASN B 25 4245 4221 4188 -43 9 -32 C ATOM 1973 OD1 ASN B 25 -33.281 24.378 5.900 1.00 33.60 O ANISOU 1973 OD1 ASN B 25 4278 4230 4259 -4 18 10 O ATOM 1974 ND2 ASN B 25 -32.010 22.563 6.236 1.00 34.32 N ANISOU 1974 ND2 ASN B 25 4327 4349 4363 7 6 27 N ATOM 1975 N THR B 26 -35.928 25.246 3.927 1.00 29.71 N ANISOU 1975 N THR B 26 3785 3740 3761 -2 13 -3 N ATOM 1976 CA THR B 26 -36.116 26.560 3.322 1.00 29.89 C ANISOU 1976 CA THR B 26 3845 3741 3770 -24 -5 -7 C ATOM 1977 C THR B 26 -35.150 27.599 3.870 1.00 29.36 C ANISOU 1977 C THR B 26 3747 3704 3702 17 1 6 C ATOM 1978 O THR B 26 -34.978 28.666 3.277 1.00 29.44 O ANISOU 1978 O THR B 26 3751 3720 3716 22 15 15 O ATOM 1979 CB THR B 26 -37.562 27.070 3.466 1.00 32.09 C ANISOU 1979 CB THR B 26 3986 4093 4115 68 22 22 C ATOM 1980 OG1 THR B 26 -37.882 27.270 4.847 1.00 32.46 O ANISOU 1980 OG1 THR B 26 4124 4085 4123 26 15 -3 O ATOM 1981 CG2 THR B 26 -38.537 26.071 2.859 1.00 33.10 C ANISOU 1981 CG2 THR B 26 4187 4145 4244 -9 -14 -13 C ATOM 1982 N SER B 27 -34.452 27.289 4.958 1.00 28.67 N ANISOU 1982 N SER B 27 3614 3612 3668 -5 30 -22 N ATOM 1983 CA SER B 27 -33.431 28.152 5.520 1.00 28.40 C ANISOU 1983 CA SER B 27 3565 3578 3646 11 66 -19 C ATOM 1984 C SER B 27 -32.163 28.198 4.676 1.00 27.25 C ANISOU 1984 C SER B 27 3476 3401 3477 12 2 -29 C ATOM 1985 O SER B 27 -31.382 29.147 4.788 1.00 27.11 O ANISOU 1985 O SER B 27 3449 3404 3448 16 26 -15 O ATOM 1986 CB SER B 27 -33.071 27.702 6.941 1.00 30.78 C ANISOU 1986 CB SER B 27 3950 3949 3796 -19 -33 50 C ATOM 1987 OG SER B 27 -32.268 26.535 6.906 1.00 32.19 O ANISOU 1987 OG SER B 27 4098 4055 4079 21 17 17 O ATOM 1988 N TRP B 28 -31.946 27.211 3.814 1.00 26.38 N ANISOU 1988 N TRP B 28 3340 3326 3357 -2 26 23 N ATOM 1989 CA TRP B 28 -30.841 27.229 2.868 1.00 25.46 C ANISOU 1989 CA TRP B 28 3293 3133 3249 13 2 -53 C ATOM 1990 C TRP B 28 -30.996 28.294 1.792 1.00 25.82 C ANISOU 1990 C TRP B 28 3304 3220 3285 7 7 -1 C ATOM 1991 O TRP B 28 -29.998 28.761 1.232 1.00 25.85 O ANISOU 1991 O TRP B 28 3309 3225 3287 15 22 8 O ATOM 1992 CB TRP B 28 -30.654 25.870 2.202 1.00 22.49 C ANISOU 1992 CB TRP B 28 2829 2902 2814 13 -11 148 C ATOM 1993 CG TRP B 28 -30.181 24.751 3.075 1.00 20.05 C ANISOU 1993 CG TRP B 28 2528 2548 2542 -33 22 -69 C ATOM 1994 CD1 TRP B 28 -29.726 24.815 4.361 1.00 20.24 C ANISOU 1994 CD1 TRP B 28 2566 2556 2569 24 10 11 C ATOM 1995 CD2 TRP B 28 -30.083 23.371 2.689 1.00 18.95 C ANISOU 1995 CD2 TRP B 28 2345 2474 2382 -14 13 18 C ATOM 1996 NE1 TRP B 28 -29.373 23.565 4.802 1.00 19.74 N ANISOU 1996 NE1 TRP B 28 2555 2504 2440 -22 -11 -9 N ATOM 1997 CE2 TRP B 28 -29.577 22.660 3.794 1.00 19.14 C ANISOU 1997 CE2 TRP B 28 2411 2459 2403 -10 10 22 C ATOM 1998 CE3 TRP B 28 -30.375 22.664 1.518 1.00 19.43 C ANISOU 1998 CE3 TRP B 28 2470 2465 2447 -14 0 -5 C ATOM 1999 CZ2 TRP B 28 -29.361 21.285 3.769 1.00 20.13 C ANISOU 1999 CZ2 TRP B 28 2539 2521 2590 3 15 1 C ATOM 2000 CZ3 TRP B 28 -30.160 21.299 1.492 1.00 19.92 C ANISOU 2000 CZ3 TRP B 28 2525 2495 2549 0 10 -24 C ATOM 2001 CH2 TRP B 28 -29.659 20.620 2.613 1.00 20.70 C ANISOU 2001 CH2 TRP B 28 2660 2617 2588 -4 0 7 C ATOM 2002 N ASN B 29 -32.216 28.737 1.513 1.00 26.11 N ANISOU 2002 N ASN B 29 3310 3295 3317 15 16 -6 N ATOM 2003 CA ASN B 29 -32.485 29.810 0.571 1.00 26.47 C ANISOU 2003 CA ASN B 29 3372 3330 3356 12 5 13 C ATOM 2004 C ASN B 29 -31.800 31.125 0.895 1.00 26.56 C ANISOU 2004 C ASN B 29 3365 3347 3382 6 5 -4 C ATOM 2005 O ASN B 29 -31.528 31.922 -0.011 1.00 26.76 O ANISOU 2005 O ASN B 29 3388 3379 3399 -2 5 8 O ATOM 2006 CB ASN B 29 -34.001 30.035 0.448 1.00 27.16 C ANISOU 2006 CB ASN B 29 3409 3466 3444 34 26 37 C ATOM 2007 CG ASN B 29 -34.674 28.927 -0.336 1.00 28.37 C ANISOU 2007 CG ASN B 29 3647 3550 3585 -15 -23 -17 C ATOM 2008 OD1 ASN B 29 -34.090 28.383 -1.274 1.00 28.14 O ANISOU 2008 OD1 ASN B 29 3575 3504 3613 -8 10 29 O ATOM 2009 ND2 ASN B 29 -35.901 28.583 0.037 1.00 29.61 N ANISOU 2009 ND2 ASN B 29 3701 3783 3766 -23 16 -9 N ATOM 2010 N LYS B 30 -31.477 31.399 2.150 1.00 26.62 N ANISOU 2010 N LYS B 30 3347 3352 3415 5 2 -3 N ATOM 2011 CA LYS B 30 -30.679 32.532 2.572 1.00 27.05 C ANISOU 2011 CA LYS B 30 3346 3362 3568 5 35 0 C ATOM 2012 C LYS B 30 -29.298 32.631 1.949 1.00 25.92 C ANISOU 2012 C LYS B 30 3295 3222 3331 24 7 -26 C ATOM 2013 O LYS B 30 -28.780 33.746 1.815 1.00 26.04 O ANISOU 2013 O LYS B 30 3323 3243 3327 8 27 -43 O ATOM 2014 CB LYS B 30 -30.543 32.527 4.102 1.00 31.87 C ANISOU 2014 CB LYS B 30 4194 4125 3790 -78 -65 69 C ATOM 2015 CG LYS B 30 -31.538 33.381 4.855 1.00 36.11 C ANISOU 2015 CG LYS B 30 4680 4471 4570 94 124 -52 C ATOM 2016 CD LYS B 30 -32.971 33.266 4.387 1.00 40.20 C ANISOU 2016 CD LYS B 30 4963 5213 5100 33 -55 -22 C ATOM 2017 CE LYS B 30 -33.575 31.895 4.633 1.00 43.11 C ANISOU 2017 CE LYS B 30 5533 5354 5495 -25 34 14 C ATOM 2018 NZ LYS B 30 -34.925 31.766 4.014 1.00 44.40 N ANISOU 2018 NZ LYS B 30 5620 5606 5644 -6 -8 4 N ATOM 2019 N GLU B 31 -28.673 31.533 1.543 1.00 24.73 N ANISOU 2019 N GLU B 31 3127 3151 3118 -12 -2 25 N ATOM 2020 CA GLU B 31 -27.378 31.573 0.879 1.00 24.03 C ANISOU 2020 CA GLU B 31 3078 3025 3026 1 -20 8 C ATOM 2021 C GLU B 31 -27.455 32.067 -0.557 1.00 23.60 C ANISOU 2021 C GLU B 31 2980 2984 3002 -7 -11 -3 C ATOM 2022 O GLU B 31 -26.451 32.499 -1.128 1.00 23.62 O ANISOU 2022 O GLU B 31 2973 2995 3006 2 -4 -7 O ATOM 2023 CB GLU B 31 -26.724 30.188 0.937 1.00 24.07 C ANISOU 2023 CB GLU B 31 3053 3034 3060 13 10 -15 C ATOM 2024 CG GLU B 31 -26.449 29.695 2.348 1.00 25.24 C ANISOU 2024 CG GLU B 31 3242 3186 3161 20 21 55 C ATOM 2025 CD GLU B 31 -25.338 30.437 3.059 1.00 26.52 C ANISOU 2025 CD GLU B 31 3334 3312 3429 -47 -1 -12 C ATOM 2026 OE1 GLU B 31 -24.634 31.255 2.431 1.00 25.38 O ANISOU 2026 OE1 GLU B 31 3208 3181 3253 33 -33 -32 O ATOM 2027 OE2 GLU B 31 -25.149 30.196 4.272 1.00 28.49 O ANISOU 2027 OE2 GLU B 31 3661 3625 3537 -4 -8 10 O ATOM 2028 N PHE B 32 -28.634 32.041 -1.163 1.00 23.22 N ANISOU 2028 N PHE B 32 2946 2939 2939 -2 9 -4 N ATOM 2029 CA PHE B 32 -28.860 32.479 -2.527 1.00 22.99 C ANISOU 2029 CA PHE B 32 2895 2909 2930 -36 -28 -12 C ATOM 2030 C PHE B 32 -29.218 33.960 -2.610 1.00 23.54 C ANISOU 2030 C PHE B 32 2992 2947 3005 -15 -13 11 C ATOM 2031 O PHE B 32 -29.242 34.561 -3.684 1.00 23.32 O ANISOU 2031 O PHE B 32 2986 2898 2978 -8 17 -13 O ATOM 2032 CB PHE B 32 -30.006 31.670 -3.143 1.00 21.33 C ANISOU 2032 CB PHE B 32 2752 2618 2736 71 41 12 C ATOM 2033 CG PHE B 32 -29.805 30.189 -3.244 1.00 18.76 C ANISOU 2033 CG PHE B 32 2352 2468 2309 -6 35 0 C ATOM 2034 CD1 PHE B 32 -29.915 29.365 -2.136 1.00 18.55 C ANISOU 2034 CD1 PHE B 32 2335 2361 2350 0 -20 0 C ATOM 2035 CD2 PHE B 32 -29.522 29.606 -4.470 1.00 17.43 C ANISOU 2035 CD2 PHE B 32 2187 2199 2238 2 -8 38 C ATOM 2036 CE1 PHE B 32 -29.732 28.001 -2.244 1.00 18.57 C ANISOU 2036 CE1 PHE B 32 2330 2365 2361 -1 -14 -6 C ATOM 2037 CE2 PHE B 32 -29.337 28.244 -4.584 1.00 17.41 C ANISOU 2037 CE2 PHE B 32 2141 2199 2273 -7 -3 19 C ATOM 2038 CZ PHE B 32 -29.445 27.435 -3.468 1.00 18.14 C ANISOU 2038 CZ PHE B 32 2261 2329 2304 -20 10 52 C ATOM 2039 N SER B 33 -29.507 34.572 -1.469 1.00 24.19 N ANISOU 2039 N SER B 33 3078 3049 3063 -17 1 -8 N ATOM 2040 CA SER B 33 -30.113 35.888 -1.393 1.00 25.22 C ANISOU 2040 CA SER B 33 3181 3104 3296 2 -28 22 C ATOM 2041 C SER B 33 -29.200 37.041 -1.769 1.00 24.73 C ANISOU 2041 C SER B 33 3127 3092 3178 4 -25 -2 C ATOM 2042 O SER B 33 -29.612 37.934 -2.521 1.00 24.79 O ANISOU 2042 O SER B 33 3167 3088 3165 8 -12 -10 O ATOM 2043 CB SER B 33 -30.638 36.103 0.038 1.00 29.51 C ANISOU 2043 CB SER B 33 3791 3906 3515 -15 70 -13 C ATOM 2044 OG SER B 33 -31.102 37.431 0.199 1.00 33.08 O ANISOU 2044 OG SER B 33 4243 4119 4209 54 31 -5 O ATOM 2045 N ALA B 34 -27.962 37.053 -1.287 1.00 24.19 N ANISOU 2045 N ALA B 34 3095 3020 3076 -5 11 -5 N ATOM 2046 CA ALA B 34 -27.064 38.184 -1.491 1.00 23.98 C ANISOU 2046 CA ALA B 34 3069 3020 3022 0 17 -20 C ATOM 2047 C ALA B 34 -26.780 38.450 -2.964 1.00 23.55 C ANISOU 2047 C ALA B 34 3002 2951 2996 -1 0 -19 C ATOM 2048 O ALA B 34 -26.713 39.607 -3.389 1.00 24.06 O ANISOU 2048 O ALA B 34 3071 2986 3086 -20 -2 5 O ATOM 2049 CB ALA B 34 -25.756 37.971 -0.744 1.00 24.56 C ANISOU 2049 CB ALA B 34 3096 3098 3138 3 -16 -3 C ATOM 2050 N GLU B 35 -26.607 37.393 -3.749 1.00 22.82 N ANISOU 2050 N GLU B 35 2890 2894 2886 -25 -2 24 N ATOM 2051 CA GLU B 35 -26.379 37.508 -5.178 1.00 22.51 C ANISOU 2051 CA GLU B 35 2856 2841 2854 -38 -39 4 C ATOM 2052 C GLU B 35 -27.615 37.180 -6.003 1.00 21.82 C ANISOU 2052 C GLU B 35 2775 2745 2770 -12 18 5 C ATOM 2053 O GLU B 35 -27.498 36.946 -7.209 1.00 21.71 O ANISOU 2053 O GLU B 35 2792 2692 2764 -24 -12 -3 O ATOM 2054 CB GLU B 35 -25.224 36.589 -5.594 1.00 24.15 C ANISOU 2054 CB GLU B 35 3089 3034 3052 77 64 -14 C ATOM 2055 CG GLU B 35 -23.872 37.042 -5.070 1.00 26.62 C ANISOU 2055 CG GLU B 35 3269 3436 3411 -7 -44 -53 C ATOM 2056 CD GLU B 35 -23.377 38.317 -5.718 1.00 29.04 C ANISOU 2056 CD GLU B 35 3734 3612 3689 13 32 67 C ATOM 2057 OE1 GLU B 35 -23.788 38.645 -6.850 1.00 28.63 O ANISOU 2057 OE1 GLU B 35 3633 3613 3632 -26 11 -5 O ATOM 2058 OE2 GLU B 35 -22.547 39.004 -5.086 1.00 30.48 O ANISOU 2058 OE2 GLU B 35 3880 3840 3862 -54 -37 -19 O ATOM 2059 N ALA B 36 -28.787 37.126 -5.380 1.00 21.32 N ANISOU 2059 N ALA B 36 2706 2671 2724 -11 -30 -16 N ATOM 2060 CA ALA B 36 -30.040 36.930 -6.101 1.00 20.78 C ANISOU 2060 CA ALA B 36 2669 2567 2660 7 -3 -18 C ATOM 2061 C ALA B 36 -29.959 35.751 -7.066 1.00 20.16 C ANISOU 2061 C ALA B 36 2579 2509 2571 19 -8 24 C ATOM 2062 O ALA B 36 -30.258 35.868 -8.252 1.00 20.24 O ANISOU 2062 O ALA B 36 2615 2498 2579 21 -13 23 O ATOM 2063 CB ALA B 36 -30.425 38.207 -6.837 1.00 20.82 C ANISOU 2063 CB ALA B 36 2626 2601 2683 14 0 3 C ATOM 2064 N VAL B 37 -29.584 34.584 -6.543 1.00 19.16 N ANISOU 2064 N VAL B 37 2421 2405 2456 0 8 -42 N ATOM 2065 CA VAL B 37 -29.404 33.400 -7.372 1.00 18.17 C ANISOU 2065 CA VAL B 37 2258 2307 2340 1 -23 18 C ATOM 2066 C VAL B 37 -30.667 32.543 -7.363 1.00 17.79 C ANISOU 2066 C VAL B 37 2253 2249 2259 4 -15 3 C ATOM 2067 O VAL B 37 -31.223 32.222 -6.317 1.00 17.98 O ANISOU 2067 O VAL B 37 2243 2287 2302 3 0 21 O ATOM 2068 CB VAL B 37 -28.186 32.569 -6.940 1.00 16.86 C ANISOU 2068 CB VAL B 37 2192 2066 2148 -56 1 -14 C ATOM 2069 CG1 VAL B 37 -28.086 31.255 -7.702 1.00 16.20 C ANISOU 2069 CG1 VAL B 37 2057 2048 2050 4 -4 8 C ATOM 2070 CG2 VAL B 37 -26.906 33.372 -7.152 1.00 17.00 C ANISOU 2070 CG2 VAL B 37 2099 2200 2159 -18 -35 32 C ATOM 2071 N ASN B 38 -31.119 32.200 -8.562 1.00 17.29 N ANISOU 2071 N ASN B 38 2201 2133 2235 -24 -2 18 N ATOM 2072 CA ASN B 38 -32.170 31.205 -8.740 1.00 16.80 C ANISOU 2072 CA ASN B 38 2175 2037 2172 25 25 -1 C ATOM 2073 C ASN B 38 -31.519 29.846 -8.983 1.00 15.18 C ANISOU 2073 C ASN B 38 1920 1948 1898 -15 -13 31 C ATOM 2074 O ASN B 38 -30.945 29.594 -10.042 1.00 14.40 O ANISOU 2074 O ASN B 38 1761 1869 1841 17 -75 72 O ATOM 2075 CB ASN B 38 -33.105 31.591 -9.886 1.00 19.08 C ANISOU 2075 CB ASN B 38 2398 2514 2336 -6 -88 83 C ATOM 2076 CG ASN B 38 -33.914 32.831 -9.543 1.00 21.89 C ANISOU 2076 CG ASN B 38 2781 2683 2855 49 2 -44 C ATOM 2077 OD1 ASN B 38 -34.479 32.918 -8.453 1.00 22.82 O ANISOU 2077 OD1 ASN B 38 2868 2890 2912 64 15 14 O ATOM 2078 ND2 ASN B 38 -33.967 33.786 -10.462 1.00 22.91 N ANISOU 2078 ND2 ASN B 38 2933 2807 2964 35 -34 31 N ATOM 2079 N GLY B 39 -31.589 28.989 -7.958 1.00 14.56 N ANISOU 2079 N GLY B 39 1818 1827 1887 -2 -3 3 N ATOM 2080 CA GLY B 39 -30.908 27.704 -8.061 1.00 13.95 C ANISOU 2080 CA GLY B 39 1747 1767 1788 -23 -19 41 C ATOM 2081 C GLY B 39 -31.436 26.686 -7.061 1.00 13.45 C ANISOU 2081 C GLY B 39 1692 1703 1716 3 -1 2 C ATOM 2082 O GLY B 39 -32.322 26.977 -6.259 1.00 13.91 O ANISOU 2082 O GLY B 39 1718 1780 1786 -5 46 29 O ATOM 2083 N VAL B 40 -30.872 25.486 -7.125 1.00 12.71 N ANISOU 2083 N VAL B 40 1580 1658 1591 -37 -16 36 N ATOM 2084 CA VAL B 40 -31.251 24.427 -6.198 1.00 12.24 C ANISOU 2084 CA VAL B 40 1532 1557 1564 -2 -22 3 C ATOM 2085 C VAL B 40 -30.007 23.700 -5.696 1.00 12.40 C ANISOU 2085 C VAL B 40 1533 1635 1544 22 2 18 C ATOM 2086 O VAL B 40 -29.039 23.484 -6.429 1.00 11.89 O ANISOU 2086 O VAL B 40 1445 1580 1493 -28 -20 82 O ATOM 2087 CB VAL B 40 -32.231 23.437 -6.851 1.00 11.87 C ANISOU 2087 CB VAL B 40 1514 1518 1479 6 -2 17 C ATOM 2088 CG1 VAL B 40 -31.566 22.694 -7.999 1.00 11.29 C ANISOU 2088 CG1 VAL B 40 1427 1391 1473 -40 -8 24 C ATOM 2089 CG2 VAL B 40 -32.787 22.465 -5.816 1.00 12.34 C ANISOU 2089 CG2 VAL B 40 1529 1584 1576 -48 3 46 C ATOM 2090 N PHE B 41 -30.053 23.326 -4.425 1.00 12.44 N ANISOU 2090 N PHE B 41 1546 1629 1550 9 -30 24 N ATOM 2091 CA PHE B 41 -29.040 22.449 -3.850 1.00 12.37 C ANISOU 2091 CA PHE B 41 1571 1541 1586 11 -16 2 C ATOM 2092 C PHE B 41 -29.730 21.201 -3.299 1.00 13.00 C ANISOU 2092 C PHE B 41 1673 1621 1646 -25 -1 35 C ATOM 2093 O PHE B 41 -30.685 21.334 -2.531 1.00 14.11 O ANISOU 2093 O PHE B 41 1747 1834 1779 24 38 41 O ATOM 2094 CB PHE B 41 -28.282 23.150 -2.729 1.00 12.21 C ANISOU 2094 CB PHE B 41 1520 1561 1556 -44 16 34 C ATOM 2095 CG PHE B 41 -27.130 22.355 -2.178 1.00 13.45 C ANISOU 2095 CG PHE B 41 1676 1716 1717 49 -36 38 C ATOM 2096 CD1 PHE B 41 -26.150 21.860 -3.023 1.00 13.55 C ANISOU 2096 CD1 PHE B 41 1806 1704 1640 -19 40 6 C ATOM 2097 CD2 PHE B 41 -27.030 22.101 -0.822 1.00 13.86 C ANISOU 2097 CD2 PHE B 41 1779 1769 1721 21 17 3 C ATOM 2098 CE1 PHE B 41 -25.087 21.132 -2.530 1.00 15.56 C ANISOU 2098 CE1 PHE B 41 1951 2011 1952 43 -69 31 C ATOM 2099 CE2 PHE B 41 -25.969 21.367 -0.321 1.00 14.15 C ANISOU 2099 CE2 PHE B 41 1785 1775 1815 5 -44 -22 C ATOM 2100 CZ PHE B 41 -24.995 20.887 -1.171 1.00 14.86 C ANISOU 2100 CZ PHE B 41 1898 1853 1895 19 39 15 C ATOM 2101 N VAL B 42 -29.267 20.039 -3.724 1.00 12.85 N ANISOU 2101 N VAL B 42 1628 1622 1633 -29 -23 28 N ATOM 2102 CA VAL B 42 -29.731 18.777 -3.150 1.00 13.07 C ANISOU 2102 CA VAL B 42 1668 1643 1654 -2 4 45 C ATOM 2103 C VAL B 42 -28.579 18.133 -2.378 1.00 13.50 C ANISOU 2103 C VAL B 42 1674 1736 1720 13 -12 18 C ATOM 2104 O VAL B 42 -27.479 18.008 -2.913 1.00 13.42 O ANISOU 2104 O VAL B 42 1690 1727 1681 25 3 72 O ATOM 2105 CB VAL B 42 -30.239 17.806 -4.225 1.00 13.68 C ANISOU 2105 CB VAL B 42 1694 1701 1803 -9 -23 -28 C ATOM 2106 CG1 VAL B 42 -30.712 16.492 -3.616 1.00 14.64 C ANISOU 2106 CG1 VAL B 42 1879 1807 1877 -3 10 57 C ATOM 2107 CG2 VAL B 42 -31.363 18.423 -5.050 1.00 14.02 C ANISOU 2107 CG2 VAL B 42 1751 1780 1797 0 -17 42 C ATOM 2108 N LEU B 43 -28.839 17.726 -1.143 1.00 14.03 N ANISOU 2108 N LEU B 43 1770 1812 1749 -27 0 38 N ATOM 2109 CA LEU B 43 -27.809 17.138 -0.294 1.00 14.81 C ANISOU 2109 CA LEU B 43 1852 1895 1880 20 -28 35 C ATOM 2110 C LEU B 43 -28.355 15.892 0.397 1.00 15.63 C ANISOU 2110 C LEU B 43 1990 1989 1959 -22 10 61 C ATOM 2111 O LEU B 43 -29.430 15.958 0.995 1.00 15.77 O ANISOU 2111 O LEU B 43 2012 2052 1928 6 12 77 O ATOM 2112 CB LEU B 43 -27.347 18.155 0.749 1.00 15.26 C ANISOU 2112 CB LEU B 43 1949 1965 1884 -10 15 -3 C ATOM 2113 CG LEU B 43 -26.270 17.687 1.734 1.00 16.31 C ANISOU 2113 CG LEU B 43 1988 2127 2083 29 -17 37 C ATOM 2114 CD1 LEU B 43 -24.970 17.378 1.006 1.00 15.44 C ANISOU 2114 CD1 LEU B 43 1968 1924 1975 21 -16 49 C ATOM 2115 CD2 LEU B 43 -26.064 18.732 2.817 1.00 17.10 C ANISOU 2115 CD2 LEU B 43 2121 2185 2193 8 -11 -21 C ATOM 2116 N CYS B 44 -27.655 14.768 0.271 1.00 16.43 N ANISOU 2116 N CYS B 44 2070 2081 2093 28 4 33 N ATOM 2117 CA CYS B 44 -28.137 13.517 0.849 1.00 17.45 C ANISOU 2117 CA CYS B 44 2208 2172 2250 17 28 104 C ATOM 2118 C CYS B 44 -27.076 12.897 1.755 1.00 17.75 C ANISOU 2118 C CYS B 44 2221 2265 2260 25 -12 46 C ATOM 2119 O CYS B 44 -25.958 12.648 1.306 1.00 17.46 O ANISOU 2119 O CYS B 44 2187 2257 2189 14 -26 127 O ATOM 2120 CB CYS B 44 -28.537 12.512 -0.234 1.00 20.03 C ANISOU 2120 CB CYS B 44 2624 2476 2511 -50 -40 -70 C ATOM 2121 SG CYS B 44 -29.499 13.193 -1.598 1.00 21.86 S ANISOU 2121 SG CYS B 44 2715 2818 2772 37 -94 96 S ATOM 2122 N LYS B 45 -27.433 12.640 3.008 1.00 18.11 N ANISOU 2122 N LYS B 45 2297 2282 2304 5 22 52 N ATOM 2123 CA LYS B 45 -26.513 11.998 3.946 1.00 18.61 C ANISOU 2123 CA LYS B 45 2309 2331 2432 0 -30 70 C ATOM 2124 C LYS B 45 -26.662 10.486 3.919 1.00 18.23 C ANISOU 2124 C LYS B 45 2282 2314 2330 -2 -7 33 C ATOM 2125 O LYS B 45 -27.757 9.939 4.083 1.00 18.49 O ANISOU 2125 O LYS B 45 2259 2406 2358 -5 -10 38 O ATOM 2126 CB LYS B 45 -26.754 12.529 5.362 1.00 22.05 C ANISOU 2126 CB LYS B 45 2885 2816 2678 -24 77 -112 C ATOM 2127 CG LYS B 45 -25.916 11.853 6.440 1.00 25.38 C ANISOU 2127 CG LYS B 45 3168 3215 3259 44 -95 130 C ATOM 2128 CD LYS B 45 -26.210 12.463 7.802 1.00 29.21 C ANISOU 2128 CD LYS B 45 3797 3685 3617 -12 87 -91 C ATOM 2129 CE LYS B 45 -25.292 11.904 8.877 1.00 31.97 C ANISOU 2129 CE LYS B 45 3999 4059 4088 34 -75 69 C ATOM 2130 NZ LYS B 45 -25.525 12.577 10.186 1.00 34.14 N ANISOU 2130 NZ LYS B 45 4356 4362 4253 9 18 -23 N ATOM 2131 N SER B 46 -25.582 9.763 3.668 1.00 17.83 N ANISOU 2131 N SER B 46 2263 2271 2241 -7 -19 51 N ATOM 2132 CA SER B 46 -25.504 8.317 3.637 1.00 18.41 C ANISOU 2132 CA SER B 46 2359 2298 2338 1 -20 9 C ATOM 2133 C SER B 46 -26.031 7.682 2.352 1.00 18.32 C ANISOU 2133 C SER B 46 2360 2280 2320 -14 24 15 C ATOM 2134 O SER B 46 -25.356 6.821 1.790 1.00 17.92 O ANISOU 2134 O SER B 46 2353 2187 2267 -28 28 74 O ATOM 2135 CB ASER B 46 -26.219 7.691 4.843 0.50 18.66 C ANISOU 2135 CB ASER B 46 2345 2369 2374 -5 3 -3 C ATOM 2136 CB BSER B 46 -26.236 7.687 4.830 0.50 19.15 C ANISOU 2136 CB BSER B 46 2414 2408 2454 -4 50 30 C ATOM 2137 OG ASER B 46 -26.003 6.290 4.874 0.50 19.09 O ANISOU 2137 OG ASER B 46 2401 2398 2453 -13 12 35 O ATOM 2138 OG BSER B 46 -25.590 8.013 6.045 0.50 20.40 O ANISOU 2138 OG BSER B 46 2573 2643 2534 0 -15 5 O ATOM 2139 N SER B 47 -27.231 8.036 1.922 1.00 19.01 N ANISOU 2139 N SER B 47 2394 2407 2421 0 6 29 N ATOM 2140 CA SER B 47 -27.817 7.522 0.697 1.00 19.70 C ANISOU 2140 CA SER B 47 2470 2540 2473 1 -13 -8 C ATOM 2141 C SER B 47 -28.883 8.488 0.185 1.00 19.93 C ANISOU 2141 C SER B 47 2514 2490 2567 0 31 21 C ATOM 2142 O SER B 47 -29.252 9.442 0.873 1.00 19.42 O ANISOU 2142 O SER B 47 2446 2396 2538 -8 17 80 O ATOM 2143 CB SER B 47 -28.455 6.150 0.927 1.00 20.91 C ANISOU 2143 CB SER B 47 2704 2579 2661 -7 5 15 C ATOM 2144 OG SER B 47 -29.751 6.288 1.490 1.00 21.82 O ANISOU 2144 OG SER B 47 2714 2742 2835 -8 -2 57 O ATOM 2145 N SER B 48 -29.472 8.157 -0.956 1.00 20.96 N ANISOU 2145 N SER B 48 2644 2681 2639 -28 -9 3 N ATOM 2146 CA SER B 48 -30.533 8.950 -1.557 1.00 21.85 C ANISOU 2146 CA SER B 48 2775 2765 2761 32 -44 23 C ATOM 2147 C SER B 48 -31.910 8.719 -0.951 1.00 23.00 C ANISOU 2147 C SER B 48 2857 2941 2941 -3 3 -8 C ATOM 2148 O SER B 48 -32.888 9.316 -1.413 1.00 23.17 O ANISOU 2148 O SER B 48 2882 2981 2939 -7 -35 6 O ATOM 2149 CB SER B 48 -30.597 8.675 -3.066 1.00 21.52 C ANISOU 2149 CB SER B 48 2677 2739 2760 34 21 -7 C ATOM 2150 OG SER B 48 -30.842 7.301 -3.313 1.00 22.06 O ANISOU 2150 OG SER B 48 2774 2779 2830 -53 -5 19 O ATOM 2151 N LYS B 49 -32.027 7.905 0.090 1.00 23.92 N ANISOU 2151 N LYS B 49 3030 3054 3006 -1 -32 30 N ATOM 2152 CA LYS B 49 -33.233 7.824 0.897 1.00 25.15 C ANISOU 2152 CA LYS B 49 3105 3295 3157 13 17 -48 C ATOM 2153 C LYS B 49 -33.305 8.933 1.943 1.00 24.94 C ANISOU 2153 C LYS B 49 3132 3177 3166 -11 -10 3 C ATOM 2154 O LYS B 49 -34.344 9.105 2.586 1.00 25.33 O ANISOU 2154 O LYS B 49 3181 3210 3235 0 23 19 O ATOM 2155 CB LYS B 49 -33.329 6.474 1.613 1.00 29.60 C ANISOU 2155 CB LYS B 49 3765 3666 3814 -61 -5 245 C ATOM 2156 CG LYS B 49 -33.145 5.251 0.740 1.00 34.58 C ANISOU 2156 CG LYS B 49 4443 4325 4369 86 3 -193 C ATOM 2157 CD LYS B 49 -33.643 3.979 1.402 1.00 38.83 C ANISOU 2157 CD LYS B 49 4953 4749 5050 -62 83 47 C ATOM 2158 CE LYS B 49 -32.973 3.687 2.730 1.00 41.95 C ANISOU 2158 CE LYS B 49 5419 5285 5237 19 -39 22 C ATOM 2159 NZ LYS B 49 -31.487 3.707 2.624 1.00 43.87 N ANISOU 2159 NZ LYS B 49 5532 5534 5604 3 4 -1 N ATOM 2160 N SER B 50 -32.222 9.669 2.150 1.00 24.59 N ANISOU 2160 N SER B 50 3107 3126 3112 1 3 14 N ATOM 2161 CA SER B 50 -32.168 10.754 3.113 1.00 24.61 C ANISOU 2161 CA SER B 50 3106 3088 3155 -16 28 17 C ATOM 2162 C SER B 50 -31.657 12.044 2.473 1.00 24.45 C ANISOU 2162 C SER B 50 3089 3071 3128 2 -15 35 C ATOM 2163 O SER B 50 -30.549 12.496 2.770 1.00 24.73 O ANISOU 2163 O SER B 50 3104 3120 3172 -12 -22 46 O ATOM 2164 CB SER B 50 -31.261 10.376 4.289 1.00 26.06 C ANISOU 2164 CB SER B 50 3290 3369 3244 13 -55 -1 C ATOM 2165 OG SER B 50 -31.726 9.227 4.967 1.00 27.99 O ANISOU 2165 OG SER B 50 3584 3505 3545 -31 -5 62 O ATOM 2166 N CYS B 51 -32.462 12.641 1.602 1.00 23.73 N ANISOU 2166 N CYS B 51 3011 2952 3054 -18 34 31 N ATOM 2167 CA CYS B 51 -32.066 13.855 0.899 1.00 22.96 C ANISOU 2167 CA CYS B 51 2896 2874 2953 10 16 -10 C ATOM 2168 C CYS B 51 -32.814 15.085 1.407 1.00 22.03 C ANISOU 2168 C CYS B 51 2782 2761 2828 -35 -3 42 C ATOM 2169 O CYS B 51 -33.958 15.001 1.857 1.00 22.20 O ANISOU 2169 O CYS B 51 2787 2824 2826 -11 -3 75 O ATOM 2170 CB CYS B 51 -32.313 13.710 -0.602 1.00 23.56 C ANISOU 2170 CB CYS B 51 2983 2993 2976 -22 -7 4 C ATOM 2171 SG CYS B 51 -31.367 12.423 -1.439 1.00 23.50 S ANISOU 2171 SG CYS B 51 2828 2939 3163 -30 -40 23 S ATOM 2172 N ALA B 52 -32.162 16.240 1.324 1.00 20.81 N ANISOU 2172 N ALA B 52 2604 2649 2655 48 12 25 N ATOM 2173 CA ALA B 52 -32.793 17.522 1.599 1.00 19.74 C ANISOU 2173 CA ALA B 52 2474 2533 2494 -21 31 67 C ATOM 2174 C ALA B 52 -32.466 18.526 0.493 1.00 18.72 C ANISOU 2174 C ALA B 52 2343 2380 2390 23 4 5 C ATOM 2175 O ALA B 52 -31.447 18.390 -0.181 1.00 18.35 O ANISOU 2175 O ALA B 52 2308 2349 2315 32 -25 37 O ATOM 2176 CB ALA B 52 -32.349 18.076 2.941 1.00 20.62 C ANISOU 2176 CB ALA B 52 2581 2660 2592 -27 -5 -10 C ATOM 2177 N THR B 53 -33.323 19.525 0.323 1.00 18.20 N ANISOU 2177 N THR B 53 2302 2330 2282 -2 23 39 N ATOM 2178 CA THR B 53 -33.098 20.548 -0.698 1.00 17.52 C ANISOU 2178 CA THR B 53 2201 2243 2211 -12 -12 -3 C ATOM 2179 C THR B 53 -33.686 21.885 -0.278 1.00 17.70 C ANISOU 2179 C THR B 53 2249 2240 2236 -10 -9 18 C ATOM 2180 O THR B 53 -34.554 21.945 0.593 1.00 18.08 O ANISOU 2180 O THR B 53 2276 2312 2283 12 14 18 O ATOM 2181 CB THR B 53 -33.690 20.101 -2.048 1.00 16.29 C ANISOU 2181 CB THR B 53 1987 2064 2137 -32 44 57 C ATOM 2182 OG1 THR B 53 -33.470 21.110 -3.044 1.00 16.22 O ANISOU 2182 OG1 THR B 53 2013 2085 2065 15 -2 55 O ATOM 2183 CG2 THR B 53 -35.187 19.846 -1.920 1.00 14.91 C ANISOU 2183 CG2 THR B 53 1899 1898 1869 1 -25 34 C ATOM 2184 N ASN B 54 -33.245 22.975 -0.907 1.00 17.38 N ANISOU 2184 N ASN B 54 2213 2200 2190 7 -11 13 N ATOM 2185 CA ASN B 54 -33.830 24.285 -0.648 1.00 17.23 C ANISOU 2185 CA ASN B 54 2198 2193 2154 1 -1 21 C ATOM 2186 C ASN B 54 -35.105 24.491 -1.465 1.00 16.92 C ANISOU 2186 C ASN B 54 2154 2116 2160 -25 16 22 C ATOM 2187 O ASN B 54 -35.910 25.357 -1.128 1.00 17.56 O ANISOU 2187 O ASN B 54 2173 2194 2305 23 5 40 O ATOM 2188 CB ASN B 54 -32.844 25.415 -0.963 1.00 17.59 C ANISOU 2188 CB ASN B 54 2245 2226 2214 -23 15 15 C ATOM 2189 CG ASN B 54 -32.531 25.468 -2.450 1.00 17.23 C ANISOU 2189 CG ASN B 54 2204 2157 2187 15 -3 -10 C ATOM 2190 OD1 ASN B 54 -32.072 24.469 -2.999 1.00 16.41 O ANISOU 2190 OD1 ASN B 54 2077 2142 2015 -32 -8 8 O ATOM 2191 ND2 ASN B 54 -32.800 26.607 -3.074 1.00 17.28 N ANISOU 2191 ND2 ASN B 54 2192 2192 2181 -32 27 51 N ATOM 2192 N ASP B 55 -35.259 23.716 -2.530 1.00 16.52 N ANISOU 2192 N ASP B 55 2093 2091 2092 -41 8 69 N ATOM 2193 CA ASP B 55 -36.379 23.896 -3.449 1.00 17.00 C ANISOU 2193 CA ASP B 55 2140 2160 2159 -12 -32 16 C ATOM 2194 C ASP B 55 -36.778 22.581 -4.100 1.00 16.98 C ANISOU 2194 C ASP B 55 2149 2157 2147 19 -12 10 C ATOM 2195 O ASP B 55 -36.208 22.141 -5.098 1.00 16.26 O ANISOU 2195 O ASP B 55 2067 2033 2077 -22 -22 62 O ATOM 2196 CB ASP B 55 -36.003 24.939 -4.505 1.00 17.96 C ANISOU 2196 CB ASP B 55 2329 2216 2279 -54 38 42 C ATOM 2197 CG ASP B 55 -37.148 25.342 -5.410 1.00 20.39 C ANISOU 2197 CG ASP B 55 2537 2592 2619 53 -88 61 C ATOM 2198 OD1 ASP B 55 -38.198 24.668 -5.408 1.00 21.44 O ANISOU 2198 OD1 ASP B 55 2605 2704 2837 3 -91 106 O ATOM 2199 OD2 ASP B 55 -37.006 26.350 -6.137 1.00 20.55 O ANISOU 2199 OD2 ASP B 55 2553 2624 2633 -2 -25 59 O ATOM 2200 N LEU B 56 -37.830 21.956 -3.568 1.00 17.64 N ANISOU 2200 N LEU B 56 2194 2276 2233 8 -1 64 N ATOM 2201 CA LEU B 56 -38.311 20.678 -4.065 1.00 18.66 C ANISOU 2201 CA LEU B 56 2345 2343 2401 -25 1 9 C ATOM 2202 C LEU B 56 -38.776 20.712 -5.513 1.00 19.50 C ANISOU 2202 C LEU B 56 2458 2506 2446 -26 -9 2 C ATOM 2203 O LEU B 56 -38.596 19.722 -6.232 1.00 19.64 O ANISOU 2203 O LEU B 56 2505 2494 2463 -14 -32 18 O ATOM 2204 CB LEU B 56 -39.443 20.161 -3.165 1.00 18.81 C ANISOU 2204 CB LEU B 56 2369 2378 2399 3 7 39 C ATOM 2205 CG LEU B 56 -38.986 19.607 -1.811 1.00 18.77 C ANISOU 2205 CG LEU B 56 2394 2359 2378 23 -4 -9 C ATOM 2206 CD1 LEU B 56 -40.156 19.527 -0.847 1.00 19.26 C ANISOU 2206 CD1 LEU B 56 2436 2431 2451 -12 21 2 C ATOM 2207 CD2 LEU B 56 -38.331 18.245 -1.989 1.00 17.89 C ANISOU 2207 CD2 LEU B 56 2272 2268 2256 -23 -14 20 C ATOM 2208 N ALA B 57 -39.361 21.816 -5.959 1.00 20.22 N ANISOU 2208 N ALA B 57 2518 2585 2580 -6 -2 33 N ATOM 2209 CA ALA B 57 -39.792 21.962 -7.343 1.00 20.58 C ANISOU 2209 CA ALA B 57 2569 2667 2584 -32 15 19 C ATOM 2210 C ALA B 57 -38.617 21.953 -8.316 1.00 19.79 C ANISOU 2210 C ALA B 57 2485 2509 2525 -58 -21 13 C ATOM 2211 O ALA B 57 -38.642 21.245 -9.325 1.00 19.97 O ANISOU 2211 O ALA B 57 2500 2558 2529 -58 11 16 O ATOM 2212 CB ALA B 57 -40.588 23.250 -7.521 1.00 22.67 C ANISOU 2212 CB ALA B 57 2845 2807 2960 62 11 20 C ATOM 2213 N ARG B 58 -37.571 22.718 -8.002 1.00 18.52 N ANISOU 2213 N ARG B 58 2340 2340 2356 17 33 61 N ATOM 2214 CA ARG B 58 -36.424 22.808 -8.899 1.00 17.17 C ANISOU 2214 CA ARG B 58 2204 2102 2218 -4 -36 25 C ATOM 2215 C ARG B 58 -35.517 21.596 -8.800 1.00 16.23 C ANISOU 2215 C ARG B 58 2059 2050 2059 -46 -13 16 C ATOM 2216 O ARG B 58 -34.814 21.236 -9.747 1.00 15.85 O ANISOU 2216 O ARG B 58 2004 1960 2060 -23 -24 41 O ATOM 2217 CB ARG B 58 -35.628 24.098 -8.645 1.00 16.08 C ANISOU 2217 CB ARG B 58 2033 2084 1992 16 25 -8 C ATOM 2218 CG ARG B 58 -34.637 24.365 -9.774 1.00 15.09 C ANISOU 2218 CG ARG B 58 1922 1852 1960 -44 -16 9 C ATOM 2219 CD ARG B 58 -33.803 25.614 -9.535 1.00 13.94 C ANISOU 2219 CD ARG B 58 1762 1790 1744 21 -25 20 C ATOM 2220 NE ARG B 58 -32.699 25.666 -10.485 1.00 13.74 N ANISOU 2220 NE ARG B 58 1677 1819 1723 9 -64 13 N ATOM 2221 CZ ARG B 58 -32.521 26.531 -11.470 1.00 14.76 C ANISOU 2221 CZ ARG B 58 1857 1879 1873 -42 27 48 C ATOM 2222 NH1 ARG B 58 -33.376 27.521 -11.681 1.00 15.91 N ANISOU 2222 NH1 ARG B 58 2025 1944 2077 13 -30 50 N ATOM 2223 NH2 ARG B 58 -31.458 26.409 -12.255 1.00 14.11 N ANISOU 2223 NH2 ARG B 58 1802 1743 1818 1 -7 42 N ATOM 2224 N ALA B 59 -35.554 20.882 -7.678 1.00 16.06 N ANISOU 2224 N ALA B 59 1988 2042 2071 -7 -14 31 N ATOM 2225 CA ALA B 59 -34.753 19.678 -7.491 1.00 15.69 C ANISOU 2225 CA ALA B 59 1985 1968 2009 -41 -12 32 C ATOM 2226 C ALA B 59 -34.935 18.633 -8.579 1.00 15.67 C ANISOU 2226 C ALA B 59 1988 1992 1975 2 16 27 C ATOM 2227 O ALA B 59 -33.976 17.923 -8.910 1.00 15.72 O ANISOU 2227 O ALA B 59 1979 1959 2035 2 -22 36 O ATOM 2228 CB ALA B 59 -35.077 19.090 -6.121 1.00 15.67 C ANISOU 2228 CB ALA B 59 1953 2019 1982 5 -20 34 C ATOM 2229 N SER B 60 -36.135 18.474 -9.136 1.00 15.79 N ANISOU 2229 N SER B 60 2004 2007 1988 0 1 43 N ATOM 2230 CA SER B 60 -36.347 17.555 -10.243 1.00 16.53 C ANISOU 2230 CA SER B 60 2106 2097 2077 28 -19 -18 C ATOM 2231 C SER B 60 -36.479 18.235 -11.601 1.00 16.74 C ANISOU 2231 C SER B 60 2115 2136 2107 10 -26 8 C ATOM 2232 O SER B 60 -36.680 17.515 -12.587 1.00 16.84 O ANISOU 2232 O SER B 60 2134 2173 2091 -9 -64 29 O ATOM 2233 CB ASER B 60 -37.638 16.755 -9.993 0.50 16.11 C ANISOU 2233 CB ASER B 60 2096 2001 2024 84 -28 -10 C ATOM 2234 CB BSER B 60 -37.561 16.658 -9.980 0.50 19.32 C ANISOU 2234 CB BSER B 60 2322 2436 2583 -118 68 -18 C ATOM 2235 OG ASER B 60 -38.744 17.645 -10.035 0.50 14.54 O ANISOU 2235 OG ASER B 60 1842 1815 1868 -67 3 -13 O ATOM 2236 OG BSER B 60 -37.207 15.695 -9.000 0.50 22.14 O ANISOU 2236 OG BSER B 60 2867 2787 2758 1 -12 58 O ATOM 2237 N LYS B 61 -36.311 19.546 -11.669 1.00 16.99 N ANISOU 2237 N LYS B 61 2103 2172 2180 -29 -40 25 N ATOM 2238 CA LYS B 61 -36.254 20.211 -12.973 1.00 17.36 C ANISOU 2238 CA LYS B 61 2134 2314 2149 -18 -17 21 C ATOM 2239 C LYS B 61 -35.003 19.770 -13.727 1.00 16.96 C ANISOU 2239 C LYS B 61 2120 2201 2121 -14 -26 21 C ATOM 2240 O LYS B 61 -33.925 19.652 -13.142 1.00 17.03 O ANISOU 2240 O LYS B 61 2109 2177 2186 -15 -37 69 O ATOM 2241 CB LYS B 61 -36.306 21.727 -12.820 1.00 21.06 C ANISOU 2241 CB LYS B 61 2862 2466 2673 -11 -48 12 C ATOM 2242 CG LYS B 61 -37.673 22.277 -12.427 1.00 25.64 C ANISOU 2242 CG LYS B 61 3076 3407 3261 60 47 8 C ATOM 2243 CD LYS B 61 -37.598 23.780 -12.205 1.00 30.33 C ANISOU 2243 CD LYS B 61 3976 3657 3892 -32 -36 -10 C ATOM 2244 CE LYS B 61 -38.870 24.347 -11.607 1.00 32.99 C ANISOU 2244 CE LYS B 61 4143 4166 4225 13 70 -20 C ATOM 2245 NZ LYS B 61 -39.900 24.660 -12.633 1.00 34.06 N ANISOU 2245 NZ LYS B 61 4302 4319 4319 18 -13 8 N ATOM 2246 N GLU B 62 -35.129 19.518 -15.025 1.00 16.42 N ANISOU 2246 N GLU B 62 2055 2081 2102 -6 -11 18 N ATOM 2247 CA GLU B 62 -34.043 18.927 -15.800 1.00 16.09 C ANISOU 2247 CA GLU B 62 2025 2054 2035 -17 -11 47 C ATOM 2248 C GLU B 62 -33.322 19.939 -16.676 1.00 15.95 C ANISOU 2248 C GLU B 62 1966 2044 2052 -35 -23 36 C ATOM 2249 O GLU B 62 -33.943 20.701 -17.417 1.00 16.49 O ANISOU 2249 O GLU B 62 2017 2145 2105 -31 -65 63 O ATOM 2250 CB GLU B 62 -34.586 17.763 -16.635 1.00 16.83 C ANISOU 2250 CB GLU B 62 2131 2119 2144 -13 -49 -20 C ATOM 2251 CG GLU B 62 -35.153 16.647 -15.764 1.00 18.43 C ANISOU 2251 CG GLU B 62 2340 2354 2310 -8 28 112 C ATOM 2252 CD GLU B 62 -35.634 15.453 -16.559 1.00 20.82 C ANISOU 2252 CD GLU B 62 2666 2597 2649 -64 -18 -95 C ATOM 2253 OE1 GLU B 62 -35.897 15.597 -17.769 1.00 21.72 O ANISOU 2253 OE1 GLU B 62 2761 2757 2735 -38 -40 17 O ATOM 2254 OE2 GLU B 62 -35.753 14.358 -15.967 1.00 22.32 O ANISOU 2254 OE2 GLU B 62 2895 2741 2845 -13 -44 25 O ATOM 2255 N TYR B 63 -31.994 20.004 -16.537 1.00 14.89 N ANISOU 2255 N TYR B 63 1918 1881 1858 -46 -3 38 N ATOM 2256 CA TYR B 63 -31.188 20.991 -17.249 1.00 14.16 C ANISOU 2256 CA TYR B 63 1831 1794 1754 -4 -23 -1 C ATOM 2257 C TYR B 63 -30.078 20.330 -18.058 1.00 13.63 C ANISOU 2257 C TYR B 63 1726 1732 1720 -27 -45 38 C ATOM 2258 O TYR B 63 -29.686 19.189 -17.801 1.00 13.60 O ANISOU 2258 O TYR B 63 1707 1721 1740 -16 -55 7 O ATOM 2259 CB TYR B 63 -30.563 22.016 -16.291 1.00 14.21 C ANISOU 2259 CB TYR B 63 1817 1783 1798 -5 -53 10 C ATOM 2260 CG TYR B 63 -31.566 22.770 -15.450 1.00 14.57 C ANISOU 2260 CG TYR B 63 1837 1852 1847 -8 -17 5 C ATOM 2261 CD1 TYR B 63 -32.150 23.949 -15.899 1.00 14.93 C ANISOU 2261 CD1 TYR B 63 1874 1860 1939 -4 1 31 C ATOM 2262 CD2 TYR B 63 -31.953 22.286 -14.206 1.00 14.68 C ANISOU 2262 CD2 TYR B 63 1853 1872 1854 -33 -24 11 C ATOM 2263 CE1 TYR B 63 -33.073 24.628 -15.126 1.00 15.09 C ANISOU 2263 CE1 TYR B 63 1922 1893 1920 5 -12 6 C ATOM 2264 CE2 TYR B 63 -32.876 22.956 -13.431 1.00 15.02 C ANISOU 2264 CE2 TYR B 63 1900 1892 1915 -13 -22 -5 C ATOM 2265 CZ TYR B 63 -33.442 24.124 -13.899 1.00 15.16 C ANISOU 2265 CZ TYR B 63 1930 1925 1903 -1 -37 1 C ATOM 2266 OH TYR B 63 -34.362 24.787 -13.121 1.00 15.45 O ANISOU 2266 OH TYR B 63 1899 2016 1955 15 -50 1 O ATOM 2267 N LEU B 64 -29.568 21.047 -19.060 1.00 13.28 N ANISOU 2267 N LEU B 64 1642 1735 1671 -6 -50 26 N ATOM 2268 CA LEU B 64 -28.383 20.600 -19.784 1.00 13.16 C ANISOU 2268 CA LEU B 64 1660 1689 1652 17 -46 31 C ATOM 2269 C LEU B 64 -27.280 20.254 -18.784 1.00 12.90 C ANISOU 2269 C LEU B 64 1664 1645 1591 -1 -30 46 C ATOM 2270 O LEU B 64 -26.988 21.062 -17.906 1.00 13.33 O ANISOU 2270 O LEU B 64 1780 1663 1621 -19 -77 64 O ATOM 2271 CB LEU B 64 -27.857 21.710 -20.697 1.00 13.61 C ANISOU 2271 CB LEU B 64 1773 1685 1712 -37 -26 12 C ATOM 2272 CG LEU B 64 -28.648 21.992 -21.974 1.00 14.33 C ANISOU 2272 CG LEU B 64 1826 1825 1793 20 -61 35 C ATOM 2273 CD1 LEU B 64 -28.314 23.378 -22.510 1.00 15.58 C ANISOU 2273 CD1 LEU B 64 2044 1916 1961 -42 1 50 C ATOM 2274 CD2 LEU B 64 -28.358 20.923 -23.017 1.00 14.91 C ANISOU 2274 CD2 LEU B 64 1906 1861 1896 15 -33 4 C ATOM 2275 N PRO B 65 -26.639 19.112 -18.966 1.00 13.02 N ANISOU 2275 N PRO B 65 1650 1670 1627 -10 -18 22 N ATOM 2276 CA PRO B 65 -25.592 18.676 -18.051 1.00 13.18 C ANISOU 2276 CA PRO B 65 1671 1695 1642 -7 -30 17 C ATOM 2277 C PRO B 65 -24.279 19.409 -18.258 1.00 13.15 C ANISOU 2277 C PRO B 65 1672 1697 1628 -15 -7 14 C ATOM 2278 O PRO B 65 -23.465 19.513 -17.334 1.00 13.18 O ANISOU 2278 O PRO B 65 1646 1727 1633 -27 4 49 O ATOM 2279 CB PRO B 65 -25.442 17.184 -18.320 1.00 13.58 C ANISOU 2279 CB PRO B 65 1746 1714 1698 6 -25 6 C ATOM 2280 CG PRO B 65 -25.995 16.985 -19.691 1.00 13.62 C ANISOU 2280 CG PRO B 65 1758 1731 1687 22 -12 -6 C ATOM 2281 CD PRO B 65 -27.085 18.010 -19.851 1.00 13.10 C ANISOU 2281 CD PRO B 65 1715 1652 1611 -9 8 17 C ATOM 2282 N ALA B 66 -24.056 19.908 -19.466 1.00 12.94 N ANISOU 2282 N ALA B 66 1610 1690 1617 -31 -7 6 N ATOM 2283 CA ALA B 66 -22.786 20.528 -19.833 1.00 12.01 C ANISOU 2283 CA ALA B 66 1526 1531 1506 23 -51 16 C ATOM 2284 C ALA B 66 -21.629 19.630 -19.420 1.00 11.35 C ANISOU 2284 C ALA B 66 1474 1430 1407 -20 -34 5 C ATOM 2285 O ALA B 66 -21.679 18.414 -19.632 1.00 10.74 O ANISOU 2285 O ALA B 66 1394 1392 1295 -2 -48 81 O ATOM 2286 CB ALA B 66 -22.698 21.921 -19.236 1.00 12.40 C ANISOU 2286 CB ALA B 66 1619 1567 1523 15 -69 0 C ATOM 2287 N SER B 67 -20.584 20.179 -18.801 1.00 11.10 N ANISOU 2287 N SER B 67 1414 1446 1358 4 -22 44 N ATOM 2288 CA SER B 67 -19.392 19.393 -18.500 1.00 11.17 C ANISOU 2288 CA SER B 67 1408 1445 1391 4 -9 31 C ATOM 2289 C SER B 67 -19.605 18.347 -17.420 1.00 11.18 C ANISOU 2289 C SER B 67 1422 1427 1400 -32 -20 13 C ATOM 2290 O SER B 67 -18.787 17.419 -17.323 1.00 11.53 O ANISOU 2290 O SER B 67 1535 1400 1447 -25 16 81 O ATOM 2291 CB SER B 67 -18.209 20.294 -18.124 1.00 11.73 C ANISOU 2291 CB SER B 67 1542 1484 1431 -72 -34 10 C ATOM 2292 OG SER B 67 -17.018 19.524 -18.069 1.00 13.86 O ANISOU 2292 OG SER B 67 1714 1774 1778 43 -26 90 O ATOM 2293 N THR B 68 -20.702 18.383 -16.662 1.00 11.48 N ANISOU 2293 N THR B 68 1464 1511 1385 -53 -17 15 N ATOM 2294 CA THR B 68 -21.019 17.260 -15.777 1.00 11.69 C ANISOU 2294 CA THR B 68 1528 1462 1452 -11 -21 35 C ATOM 2295 C THR B 68 -21.262 15.967 -16.541 1.00 11.95 C ANISOU 2295 C THR B 68 1540 1504 1495 -23 -43 9 C ATOM 2296 O THR B 68 -21.093 14.876 -15.981 1.00 12.57 O ANISOU 2296 O THR B 68 1678 1509 1589 -5 -60 12 O ATOM 2297 CB THR B 68 -22.200 17.513 -14.826 1.00 12.43 C ANISOU 2297 CB THR B 68 1561 1556 1607 -5 30 14 C ATOM 2298 OG1 THR B 68 -23.438 17.581 -15.547 1.00 14.05 O ANISOU 2298 OG1 THR B 68 1720 1884 1733 -8 -95 50 O ATOM 2299 CG2 THR B 68 -22.007 18.794 -14.032 1.00 12.29 C ANISOU 2299 CG2 THR B 68 1567 1562 1541 2 8 18 C ATOM 2300 N PHE B 69 -21.603 16.020 -17.825 1.00 11.88 N ANISOU 2300 N PHE B 69 1527 1516 1472 -7 -10 -5 N ATOM 2301 CA PHE B 69 -21.690 14.859 -18.687 1.00 11.80 C ANISOU 2301 CA PHE B 69 1517 1498 1468 3 -17 -1 C ATOM 2302 C PHE B 69 -20.376 14.141 -18.928 1.00 11.65 C ANISOU 2302 C PHE B 69 1486 1482 1458 -22 -21 1 C ATOM 2303 O PHE B 69 -20.367 12.965 -19.328 1.00 11.56 O ANISOU 2303 O PHE B 69 1518 1457 1418 16 -41 43 O ATOM 2304 CB PHE B 69 -22.343 15.240 -20.034 1.00 12.46 C ANISOU 2304 CB PHE B 69 1655 1552 1527 0 -57 36 C ATOM 2305 CG PHE B 69 -22.740 13.994 -20.789 1.00 12.70 C ANISOU 2305 CG PHE B 69 1660 1556 1609 15 -21 -6 C ATOM 2306 CD1 PHE B 69 -23.844 13.257 -20.388 1.00 13.39 C ANISOU 2306 CD1 PHE B 69 1689 1675 1725 -7 -37 45 C ATOM 2307 CD2 PHE B 69 -21.993 13.557 -21.867 1.00 12.68 C ANISOU 2307 CD2 PHE B 69 1692 1588 1539 26 -29 51 C ATOM 2308 CE1 PHE B 69 -24.203 12.106 -21.067 1.00 13.76 C ANISOU 2308 CE1 PHE B 69 1794 1715 1719 20 -26 2 C ATOM 2309 CE2 PHE B 69 -22.349 12.404 -22.544 1.00 13.49 C ANISOU 2309 CE2 PHE B 69 1786 1648 1693 -34 -32 4 C ATOM 2310 CZ PHE B 69 -23.456 11.681 -22.148 1.00 13.62 C ANISOU 2310 CZ PHE B 69 1701 1746 1726 28 -23 45 C ATOM 2311 N LYS B 70 -19.220 14.727 -18.628 1.00 11.65 N ANISOU 2311 N LYS B 70 1458 1529 1440 8 -65 -18 N ATOM 2312 CA LYS B 70 -17.947 14.032 -18.681 1.00 11.09 C ANISOU 2312 CA LYS B 70 1425 1400 1388 -36 -34 -2 C ATOM 2313 C LYS B 70 -17.896 12.818 -17.754 1.00 11.27 C ANISOU 2313 C LYS B 70 1461 1421 1402 -9 -53 11 C ATOM 2314 O LYS B 70 -17.124 11.905 -18.051 1.00 11.41 O ANISOU 2314 O LYS B 70 1507 1400 1427 8 -91 26 O ATOM 2315 CB LYS B 70 -16.790 14.989 -18.357 1.00 10.14 C ANISOU 2315 CB LYS B 70 1350 1254 1250 30 -11 39 C ATOM 2316 CG LYS B 70 -16.671 16.075 -19.427 1.00 10.87 C ANISOU 2316 CG LYS B 70 1460 1355 1317 -5 -65 90 C ATOM 2317 CD LYS B 70 -15.363 16.835 -19.306 1.00 11.87 C ANISOU 2317 CD LYS B 70 1515 1444 1550 -45 36 3 C ATOM 2318 CE LYS B 70 -15.155 17.723 -20.526 1.00 12.66 C ANISOU 2318 CE LYS B 70 1630 1629 1553 -36 32 47 C ATOM 2319 NZ LYS B 70 -15.960 18.974 -20.447 1.00 13.86 N ANISOU 2319 NZ LYS B 70 1777 1697 1792 -6 -10 5 N ATOM 2320 N ILE B 71 -18.673 12.804 -16.681 1.00 11.43 N ANISOU 2320 N ILE B 71 1490 1442 1413 -49 -36 42 N ATOM 2321 CA ILE B 71 -18.685 11.640 -15.795 1.00 11.71 C ANISOU 2321 CA ILE B 71 1568 1469 1413 -10 -25 65 C ATOM 2322 C ILE B 71 -19.194 10.403 -16.511 1.00 12.16 C ANISOU 2322 C ILE B 71 1609 1518 1495 -23 -11 28 C ATOM 2323 O ILE B 71 -18.443 9.446 -16.715 1.00 12.29 O ANISOU 2323 O ILE B 71 1614 1549 1508 -12 -37 4 O ATOM 2324 CB ILE B 71 -19.431 11.922 -14.482 1.00 11.71 C ANISOU 2324 CB ILE B 71 1543 1421 1485 -13 -5 -24 C ATOM 2325 CG1 ILE B 71 -18.800 13.125 -13.773 1.00 11.25 C ANISOU 2325 CG1 ILE B 71 1487 1451 1338 -16 -9 7 C ATOM 2326 CG2 ILE B 71 -19.372 10.690 -13.588 1.00 11.98 C ANISOU 2326 CG2 ILE B 71 1542 1488 1520 -11 14 29 C ATOM 2327 CD1 ILE B 71 -19.528 13.593 -12.538 1.00 10.42 C ANISOU 2327 CD1 ILE B 71 1298 1318 1341 5 -35 13 C ATOM 2328 N PRO B 72 -20.428 10.416 -17.000 1.00 13.05 N ANISOU 2328 N PRO B 72 1662 1662 1634 -13 -34 35 N ATOM 2329 CA PRO B 72 -20.966 9.301 -17.766 1.00 13.31 C ANISOU 2329 CA PRO B 72 1702 1681 1673 -10 -51 19 C ATOM 2330 C PRO B 72 -20.159 9.018 -19.017 1.00 13.41 C ANISOU 2330 C PRO B 72 1679 1704 1713 -8 -39 18 C ATOM 2331 O PRO B 72 -19.844 7.867 -19.331 1.00 13.82 O ANISOU 2331 O PRO B 72 1772 1718 1761 14 -54 16 O ATOM 2332 CB PRO B 72 -22.396 9.710 -18.091 1.00 13.50 C ANISOU 2332 CB PRO B 72 1696 1724 1709 2 -8 0 C ATOM 2333 CG PRO B 72 -22.463 11.175 -17.839 1.00 13.60 C ANISOU 2333 CG PRO B 72 1727 1715 1725 -11 -18 12 C ATOM 2334 CD PRO B 72 -21.467 11.434 -16.729 1.00 13.31 C ANISOU 2334 CD PRO B 72 1697 1673 1687 -3 -14 34 C ATOM 2335 N ASN B 73 -19.778 10.062 -19.754 1.00 13.60 N ANISOU 2335 N ASN B 73 1721 1750 1698 -21 -55 38 N ATOM 2336 CA ASN B 73 -19.029 9.899 -20.996 1.00 13.76 C ANISOU 2336 CA ASN B 73 1726 1761 1739 -17 -33 -2 C ATOM 2337 C ASN B 73 -17.692 9.207 -20.769 1.00 13.89 C ANISOU 2337 C ASN B 73 1763 1762 1754 1 -34 -7 C ATOM 2338 O ASN B 73 -17.296 8.336 -21.547 1.00 14.04 O ANISOU 2338 O ASN B 73 1791 1786 1757 16 -65 -17 O ATOM 2339 CB ASN B 73 -18.856 11.265 -21.661 1.00 14.68 C ANISOU 2339 CB ASN B 73 1880 1799 1899 -49 20 23 C ATOM 2340 CG ASN B 73 -18.640 11.227 -23.157 1.00 15.78 C ANISOU 2340 CG ASN B 73 2123 1937 1936 -13 -33 -117 C ATOM 2341 OD1 ASN B 73 -18.360 12.263 -23.775 1.00 17.60 O ANISOU 2341 OD1 ASN B 73 2318 2185 2185 -15 -46 100 O ATOM 2342 ND2 ASN B 73 -18.763 10.059 -23.775 1.00 12.93 N ANISOU 2342 ND2 ASN B 73 1653 1685 1577 32 -35 89 N ATOM 2343 N ALA B 74 -16.982 9.556 -19.698 1.00 13.81 N ANISOU 2343 N ALA B 74 1737 1784 1725 -11 -35 28 N ATOM 2344 CA ALA B 74 -15.743 8.877 -19.342 1.00 13.29 C ANISOU 2344 CA ALA B 74 1743 1651 1657 -6 -36 -18 C ATOM 2345 C ALA B 74 -15.974 7.398 -19.042 1.00 13.44 C ANISOU 2345 C ALA B 74 1754 1675 1678 -13 -23 1 C ATOM 2346 O ALA B 74 -15.218 6.554 -19.525 1.00 13.64 O ANISOU 2346 O ALA B 74 1791 1621 1770 -23 -8 7 O ATOM 2347 CB ALA B 74 -15.084 9.561 -18.150 1.00 12.77 C ANISOU 2347 CB ALA B 74 1642 1604 1605 33 -35 21 C ATOM 2348 N ILE B 75 -17.000 7.080 -18.266 1.00 13.53 N ANISOU 2348 N ILE B 75 1744 1699 1699 -19 -28 -4 N ATOM 2349 CA ILE B 75 -17.318 5.690 -17.946 1.00 13.89 C ANISOU 2349 CA ILE B 75 1789 1730 1760 -9 -8 23 C ATOM 2350 C ILE B 75 -17.627 4.903 -19.213 1.00 14.42 C ANISOU 2350 C ILE B 75 1864 1808 1805 -19 -22 -13 C ATOM 2351 O ILE B 75 -17.081 3.826 -19.439 1.00 14.76 O ANISOU 2351 O ILE B 75 1893 1852 1862 9 -43 13 O ATOM 2352 CB ILE B 75 -18.492 5.587 -16.959 1.00 13.65 C ANISOU 2352 CB ILE B 75 1754 1707 1725 -4 -30 1 C ATOM 2353 CG1 ILE B 75 -18.165 6.363 -15.679 1.00 13.72 C ANISOU 2353 CG1 ILE B 75 1801 1686 1727 10 -15 4 C ATOM 2354 CG2 ILE B 75 -18.791 4.125 -16.649 1.00 13.87 C ANISOU 2354 CG2 ILE B 75 1758 1745 1766 -42 14 31 C ATOM 2355 CD1 ILE B 75 -19.331 6.536 -14.733 1.00 14.56 C ANISOU 2355 CD1 ILE B 75 1833 1869 1829 15 7 13 C ATOM 2356 N ILE B 76 -18.484 5.460 -20.068 1.00 15.00 N ANISOU 2356 N ILE B 76 1894 1882 1923 -10 -56 1 N ATOM 2357 CA ILE B 76 -18.806 4.839 -21.348 1.00 15.43 C ANISOU 2357 CA ILE B 76 1984 1969 1909 -3 -10 -8 C ATOM 2358 C ILE B 76 -17.588 4.690 -22.242 1.00 15.19 C ANISOU 2358 C ILE B 76 1953 1910 1908 0 -29 24 C ATOM 2359 O ILE B 76 -17.394 3.651 -22.882 1.00 15.40 O ANISOU 2359 O ILE B 76 2006 1900 1946 -8 -43 30 O ATOM 2360 CB ILE B 76 -19.907 5.648 -22.068 1.00 16.76 C ANISOU 2360 CB ILE B 76 2100 2130 2139 65 -37 47 C ATOM 2361 CG1 ILE B 76 -21.165 5.655 -21.204 1.00 16.41 C ANISOU 2361 CG1 ILE B 76 2083 2060 2092 -20 -33 -3 C ATOM 2362 CG2 ILE B 76 -20.187 5.080 -23.449 1.00 17.74 C ANISOU 2362 CG2 ILE B 76 2321 2218 2202 14 -6 -9 C ATOM 2363 CD1 ILE B 76 -22.202 6.690 -21.567 1.00 16.48 C ANISOU 2363 CD1 ILE B 76 2115 2067 2079 -7 -36 0 C ATOM 2364 N GLY B 77 -16.739 5.713 -22.295 1.00 15.19 N ANISOU 2364 N GLY B 77 1955 1891 1926 5 -39 22 N ATOM 2365 CA GLY B 77 -15.490 5.662 -23.034 1.00 15.63 C ANISOU 2365 CA GLY B 77 2000 1964 1975 -7 -6 -6 C ATOM 2366 C GLY B 77 -14.628 4.476 -22.611 1.00 16.29 C ANISOU 2366 C GLY B 77 2077 2045 2068 34 -16 12 C ATOM 2367 O GLY B 77 -14.099 3.748 -23.449 1.00 16.46 O ANISOU 2367 O GLY B 77 2148 2067 2038 20 -13 9 O ATOM 2368 N LEU B 78 -14.481 4.278 -21.306 1.00 16.75 N ANISOU 2368 N LEU B 78 2163 2114 2088 -6 -31 9 N ATOM 2369 CA LEU B 78 -13.736 3.143 -20.777 1.00 16.91 C ANISOU 2369 CA LEU B 78 2182 2141 2102 24 -26 6 C ATOM 2370 C LEU B 78 -14.418 1.821 -21.089 1.00 17.55 C ANISOU 2370 C LEU B 78 2267 2192 2210 -8 -16 1 C ATOM 2371 O LEU B 78 -13.778 0.887 -21.576 1.00 17.92 O ANISOU 2371 O LEU B 78 2337 2229 2244 4 3 -28 O ATOM 2372 CB LEU B 78 -13.533 3.329 -19.267 1.00 16.38 C ANISOU 2372 CB LEU B 78 2079 2061 2084 -15 -27 16 C ATOM 2373 CG LEU B 78 -12.531 4.422 -18.878 1.00 15.80 C ANISOU 2373 CG LEU B 78 2059 1978 1965 16 8 30 C ATOM 2374 CD1 LEU B 78 -12.754 4.881 -17.445 1.00 15.76 C ANISOU 2374 CD1 LEU B 78 2080 1948 1958 -19 -8 13 C ATOM 2375 CD2 LEU B 78 -11.102 3.936 -19.075 1.00 16.57 C ANISOU 2375 CD2 LEU B 78 2086 2076 2135 18 -2 0 C ATOM 2376 N GLU B 79 -15.721 1.731 -20.864 1.00 18.08 N ANISOU 2376 N GLU B 79 2291 2312 2267 -7 -33 18 N ATOM 2377 CA GLU B 79 -16.485 0.514 -21.094 1.00 18.95 C ANISOU 2377 CA GLU B 79 2465 2320 2413 -26 -25 10 C ATOM 2378 C GLU B 79 -16.393 0.003 -22.526 1.00 19.27 C ANISOU 2378 C GLU B 79 2488 2405 2430 -12 -22 -7 C ATOM 2379 O GLU B 79 -16.224 -1.192 -22.773 1.00 19.35 O ANISOU 2379 O GLU B 79 2497 2416 2439 3 -29 -10 O ATOM 2380 CB GLU B 79 -17.963 0.743 -20.757 1.00 21.19 C ANISOU 2380 CB GLU B 79 2570 2671 2809 15 -1 -30 C ATOM 2381 CG GLU B 79 -18.313 0.601 -19.289 1.00 24.13 C ANISOU 2381 CG GLU B 79 3081 3124 2963 -13 24 -1 C ATOM 2382 CD GLU B 79 -17.977 -0.776 -18.743 1.00 25.76 C ANISOU 2382 CD GLU B 79 3264 3268 3256 62 -28 76 C ATOM 2383 OE1 GLU B 79 -18.589 -1.772 -19.179 1.00 27.72 O ANISOU 2383 OE1 GLU B 79 3539 3452 3543 -66 -42 -36 O ATOM 2384 OE2 GLU B 79 -17.095 -0.857 -17.868 1.00 24.50 O ANISOU 2384 OE2 GLU B 79 3163 3026 3120 -30 11 25 O ATOM 2385 N THR B 80 -16.515 0.918 -23.481 1.00 19.38 N ANISOU 2385 N THR B 80 2489 2409 2467 -7 -16 13 N ATOM 2386 CA THR B 80 -16.479 0.597 -24.896 1.00 19.71 C ANISOU 2386 CA THR B 80 2546 2452 2489 -17 -26 -4 C ATOM 2387 C THR B 80 -15.079 0.348 -25.428 1.00 20.38 C ANISOU 2387 C THR B 80 2574 2570 2598 3 -22 -10 C ATOM 2388 O THR B 80 -14.915 -0.170 -26.537 1.00 21.39 O ANISOU 2388 O THR B 80 2762 2706 2661 23 -49 -64 O ATOM 2389 CB THR B 80 -17.124 1.736 -25.722 1.00 19.48 C ANISOU 2389 CB THR B 80 2455 2437 2509 -9 -7 -19 C ATOM 2390 OG1 THR B 80 -16.404 2.952 -25.478 1.00 19.29 O ANISOU 2390 OG1 THR B 80 2532 2388 2410 -7 -17 25 O ATOM 2391 CG2 THR B 80 -18.583 1.910 -25.343 1.00 18.78 C ANISOU 2391 CG2 THR B 80 2430 2333 2373 23 -17 -36 C ATOM 2392 N GLY B 81 -14.042 0.769 -24.704 1.00 19.99 N ANISOU 2392 N GLY B 81 2560 2501 2533 10 -6 -34 N ATOM 2393 CA GLY B 81 -12.668 0.569 -25.130 1.00 19.90 C ANISOU 2393 CA GLY B 81 2556 2499 2506 -3 -15 -10 C ATOM 2394 C GLY B 81 -12.145 1.738 -25.952 1.00 19.76 C ANISOU 2394 C GLY B 81 2530 2478 2498 11 -16 -12 C ATOM 2395 O GLY B 81 -11.002 1.739 -26.414 1.00 20.08 O ANISOU 2395 O GLY B 81 2527 2530 2574 22 -26 2 O ATOM 2396 N VAL B 82 -12.974 2.763 -26.121 1.00 19.28 N ANISOU 2396 N VAL B 82 2488 2435 2401 -22 -44 -3 N ATOM 2397 CA VAL B 82 -12.565 4.016 -26.744 1.00 19.02 C ANISOU 2397 CA VAL B 82 2454 2407 2366 -26 -33 -25 C ATOM 2398 C VAL B 82 -11.425 4.641 -25.945 1.00 18.60 C ANISOU 2398 C VAL B 82 2380 2367 2322 -10 1 -4 C ATOM 2399 O VAL B 82 -10.436 5.100 -26.506 1.00 18.60 O ANISOU 2399 O VAL B 82 2393 2417 2258 -19 -18 15 O ATOM 2400 CB VAL B 82 -13.757 4.982 -26.844 1.00 20.32 C ANISOU 2400 CB VAL B 82 2531 2553 2638 31 11 34 C ATOM 2401 CG1 VAL B 82 -13.327 6.384 -27.253 1.00 20.25 C ANISOU 2401 CG1 VAL B 82 2625 2530 2538 -7 -18 -5 C ATOM 2402 CG2 VAL B 82 -14.775 4.442 -27.848 1.00 21.28 C ANISOU 2402 CG2 VAL B 82 2712 2663 2709 -30 -40 -14 C ATOM 2403 N ILE B 83 -11.584 4.673 -24.627 1.00 18.20 N ANISOU 2403 N ILE B 83 2337 2293 2285 -17 -13 -25 N ATOM 2404 CA ILE B 83 -10.482 4.994 -23.722 1.00 17.99 C ANISOU 2404 CA ILE B 83 2322 2302 2213 -3 24 -54 C ATOM 2405 C ILE B 83 -9.824 3.700 -23.252 1.00 18.80 C ANISOU 2405 C ILE B 83 2476 2333 2335 -4 -16 -23 C ATOM 2406 O ILE B 83 -10.493 2.858 -22.657 1.00 18.53 O ANISOU 2406 O ILE B 83 2453 2294 2294 4 -36 -28 O ATOM 2407 CB ILE B 83 -10.997 5.792 -22.511 1.00 15.16 C ANISOU 2407 CB ILE B 83 1866 1852 2042 1 -114 66 C ATOM 2408 CG1 ILE B 83 -11.808 7.004 -22.988 1.00 13.27 C ANISOU 2408 CG1 ILE B 83 1673 1734 1633 9 44 -21 C ATOM 2409 CG2 ILE B 83 -9.840 6.231 -21.628 1.00 13.97 C ANISOU 2409 CG2 ILE B 83 1830 1727 1753 -34 25 -3 C ATOM 2410 CD1 ILE B 83 -12.584 7.705 -21.894 1.00 11.54 C ANISOU 2410 CD1 ILE B 83 1488 1447 1450 -33 -70 26 C ATOM 2411 N LYS B 84 -8.532 3.538 -23.504 1.00 20.31 N ANISOU 2411 N LYS B 84 2571 2591 2555 -12 12 -30 N ATOM 2412 CA LYS B 84 -7.855 2.266 -23.286 1.00 22.14 C ANISOU 2412 CA LYS B 84 2899 2693 2820 49 -61 -10 C ATOM 2413 C LYS B 84 -7.804 1.879 -21.812 1.00 22.60 C ANISOU 2413 C LYS B 84 2929 2809 2848 -2 -30 12 C ATOM 2414 O LYS B 84 -8.139 0.760 -21.420 1.00 22.98 O ANISOU 2414 O LYS B 84 2952 2823 2955 0 -43 25 O ATOM 2415 CB LYS B 84 -6.427 2.312 -23.829 1.00 26.62 C ANISOU 2415 CB LYS B 84 3100 3398 3615 -5 54 -62 C ATOM 2416 CG LYS B 84 -6.245 2.781 -25.253 1.00 33.12 C ANISOU 2416 CG LYS B 84 4232 4280 4070 60 96 198 C ATOM 2417 CD LYS B 84 -6.838 1.828 -26.274 1.00 37.74 C ANISOU 2417 CD LYS B 84 4867 4658 4814 -68 -154 -122 C ATOM 2418 CE LYS B 84 -6.019 1.809 -27.555 1.00 42.06 C ANISOU 2418 CE LYS B 84 5317 5431 5232 24 65 -36 C ATOM 2419 NZ LYS B 84 -5.765 3.169 -28.099 1.00 44.60 N ANISOU 2419 NZ LYS B 84 5692 5575 5678 -9 16 33 N ATOM 2420 N ASN B 85 -7.324 2.806 -20.990 1.00 22.69 N ANISOU 2420 N ASN B 85 2937 2833 2849 -14 -10 -2 N ATOM 2421 CA ASN B 85 -7.277 2.597 -19.547 1.00 22.91 C ANISOU 2421 CA ASN B 85 2996 2857 2853 -58 8 -34 C ATOM 2422 C ASN B 85 -7.144 3.937 -18.837 1.00 21.98 C ANISOU 2422 C ASN B 85 2831 2767 2751 -22 -15 28 C ATOM 2423 O ASN B 85 -7.204 4.998 -19.461 1.00 21.42 O ANISOU 2423 O ASN B 85 2750 2706 2683 1 -19 -4 O ATOM 2424 CB ASN B 85 -6.129 1.664 -19.166 1.00 26.20 C ANISOU 2424 CB ASN B 85 3336 3257 3360 142 -82 31 C ATOM 2425 CG ASN B 85 -4.776 2.135 -19.658 1.00 29.50 C ANISOU 2425 CG ASN B 85 3638 3777 3795 -79 21 47 C ATOM 2426 OD1 ASN B 85 -4.378 3.278 -19.444 1.00 29.44 O ANISOU 2426 OD1 ASN B 85 3760 3720 3707 6 -17 16 O ATOM 2427 ND2 ASN B 85 -4.057 1.240 -20.329 1.00 31.30 N ANISOU 2427 ND2 ASN B 85 4016 3929 3948 33 28 -33 N ATOM 2428 N GLU B 86 -6.854 3.886 -17.543 1.00 21.43 N ANISOU 2428 N GLU B 86 2737 2676 2730 -41 4 5 N ATOM 2429 CA GLU B 86 -6.737 5.078 -16.715 1.00 21.17 C ANISOU 2429 CA GLU B 86 2627 2664 2753 -27 18 -9 C ATOM 2430 C GLU B 86 -5.560 5.960 -17.107 1.00 19.95 C ANISOU 2430 C GLU B 86 2539 2526 2516 29 -3 -6 C ATOM 2431 O GLU B 86 -5.589 7.149 -16.785 1.00 20.17 O ANISOU 2431 O GLU B 86 2580 2554 2530 35 -12 -27 O ATOM 2432 CB AGLU B 86 -6.598 4.638 -15.248 0.50 24.70 C ANISOU 2432 CB AGLU B 86 3274 3205 2906 -58 7 58 C ATOM 2433 CB BGLU B 86 -6.631 4.683 -15.234 0.50 22.02 C ANISOU 2433 CB BGLU B 86 2759 2768 2841 -10 -2 -10 C ATOM 2434 CG AGLU B 86 -5.480 3.623 -15.070 0.50 28.25 C ANISOU 2434 CG AGLU B 86 3492 3590 3653 87 -25 -43 C ATOM 2435 CG BGLU B 86 -5.228 4.355 -14.775 0.50 21.66 C ANISOU 2435 CG BGLU B 86 2756 2709 2763 2 -2 -10 C ATOM 2436 CD AGLU B 86 -5.698 2.664 -13.922 0.50 30.97 C ANISOU 2436 CD AGLU B 86 4050 3842 3876 15 12 44 C ATOM 2437 CD BGLU B 86 -5.121 3.468 -13.557 0.50 22.14 C ANISOU 2437 CD BGLU B 86 2822 2753 2837 -15 17 30 C ATOM 2438 OE1AGLU B 86 -6.856 2.277 -13.662 0.50 32.87 O ANISOU 2438 OE1AGLU B 86 4135 4147 4206 -17 12 0 O ATOM 2439 OE1BGLU B 86 -5.240 2.236 -13.728 0.50 21.19 O ANISOU 2439 OE1BGLU B 86 2682 2702 2666 22 6 0 O ATOM 2440 OE2AGLU B 86 -4.694 2.291 -13.278 0.50 31.57 O ANISOU 2440 OE2AGLU B 86 4016 3966 4013 11 -2 1 O ATOM 2441 OE2BGLU B 86 -4.900 3.976 -12.437 0.50 22.79 O ANISOU 2441 OE2BGLU B 86 2924 2857 2878 -12 26 -1 O ATOM 2442 N HIS B 87 -4.530 5.425 -17.752 1.00 18.93 N ANISOU 2442 N HIS B 87 2430 2380 2383 -16 -48 48 N ATOM 2443 CA HIS B 87 -3.335 6.179 -18.076 1.00 18.78 C ANISOU 2443 CA HIS B 87 2409 2379 2348 4 -9 29 C ATOM 2444 C HIS B 87 -3.248 6.593 -19.542 1.00 18.48 C ANISOU 2444 C HIS B 87 2363 2328 2331 -6 8 10 C ATOM 2445 O HIS B 87 -2.184 7.055 -19.970 1.00 18.25 O ANISOU 2445 O HIS B 87 2358 2327 2248 1 12 12 O ATOM 2446 CB HIS B 87 -2.070 5.389 -17.715 1.00 19.27 C ANISOU 2446 CB HIS B 87 2415 2441 2467 19 -11 15 C ATOM 2447 CG HIS B 87 -2.013 4.974 -16.278 1.00 19.92 C ANISOU 2447 CG HIS B 87 2539 2513 2515 -6 7 42 C ATOM 2448 ND1 HIS B 87 -2.133 5.866 -15.233 1.00 20.57 N ANISOU 2448 ND1 HIS B 87 2624 2598 2594 -7 4 -13 N ATOM 2449 CD2 HIS B 87 -1.836 3.752 -15.722 1.00 19.12 C ANISOU 2449 CD2 HIS B 87 2363 2453 2449 17 1 13 C ATOM 2450 CE1 HIS B 87 -2.047 5.205 -14.091 1.00 20.46 C ANISOU 2450 CE1 HIS B 87 2592 2569 2611 -11 -15 2 C ATOM 2451 NE2 HIS B 87 -1.859 3.927 -14.358 1.00 19.91 N ANISOU 2451 NE2 HIS B 87 2527 2545 2491 1 -19 -10 N ATOM 2452 N GLN B 88 -4.335 6.463 -20.296 1.00 18.41 N ANISOU 2452 N GLN B 88 2407 2269 2320 -20 3 6 N ATOM 2453 CA GLN B 88 -4.312 6.956 -21.670 1.00 18.89 C ANISOU 2453 CA GLN B 88 2530 2280 2367 8 73 26 C ATOM 2454 C GLN B 88 -4.047 8.461 -21.692 1.00 17.40 C ANISOU 2454 C GLN B 88 2253 2196 2163 31 18 20 C ATOM 2455 O GLN B 88 -4.618 9.214 -20.907 1.00 16.87 O ANISOU 2455 O GLN B 88 2209 2138 2063 11 8 61 O ATOM 2456 CB GLN B 88 -5.603 6.653 -22.427 1.00 23.19 C ANISOU 2456 CB GLN B 88 2737 2990 3083 -47 -130 -56 C ATOM 2457 CG GLN B 88 -5.518 7.101 -23.885 1.00 27.89 C ANISOU 2457 CG GLN B 88 3667 3511 3419 24 72 84 C ATOM 2458 CD GLN B 88 -6.736 6.693 -24.681 1.00 30.82 C ANISOU 2458 CD GLN B 88 3839 3966 3903 -44 -53 -60 C ATOM 2459 OE1 GLN B 88 -7.304 5.631 -24.438 1.00 31.68 O ANISOU 2459 OE1 GLN B 88 4080 3965 3994 -3 -6 24 O ATOM 2460 NE2 GLN B 88 -7.142 7.528 -25.629 1.00 32.32 N ANISOU 2460 NE2 GLN B 88 4116 4065 4098 14 -15 31 N ATOM 2461 N VAL B 89 -3.171 8.882 -22.596 1.00 16.74 N ANISOU 2461 N VAL B 89 2192 2091 2075 12 -23 -12 N ATOM 2462 CA VAL B 89 -2.903 10.307 -22.780 1.00 16.69 C ANISOU 2462 CA VAL B 89 2175 2088 2078 27 -26 19 C ATOM 2463 C VAL B 89 -3.620 10.803 -24.035 1.00 16.51 C ANISOU 2463 C VAL B 89 2151 2060 2063 44 -19 6 C ATOM 2464 O VAL B 89 -3.468 10.211 -25.101 1.00 17.20 O ANISOU 2464 O VAL B 89 2292 2159 2083 56 -38 -6 O ATOM 2465 CB VAL B 89 -1.402 10.607 -22.879 1.00 17.74 C ANISOU 2465 CB VAL B 89 2227 2245 2268 -12 -4 5 C ATOM 2466 CG1 VAL B 89 -1.132 12.039 -23.318 1.00 17.63 C ANISOU 2466 CG1 VAL B 89 2250 2238 2212 -1 -9 3 C ATOM 2467 CG2 VAL B 89 -0.730 10.356 -21.527 1.00 18.89 C ANISOU 2467 CG2 VAL B 89 2424 2433 2319 16 -37 40 C ATOM 2468 N PHE B 90 -4.387 11.868 -23.874 1.00 15.53 N ANISOU 2468 N PHE B 90 2032 1975 1893 -6 -22 32 N ATOM 2469 CA PHE B 90 -5.061 12.507 -25.002 1.00 15.07 C ANISOU 2469 CA PHE B 90 1937 1889 1901 -3 -1 13 C ATOM 2470 C PHE B 90 -4.145 13.593 -25.553 1.00 14.81 C ANISOU 2470 C PHE B 90 1931 1844 1853 15 -32 17 C ATOM 2471 O PHE B 90 -3.959 14.637 -24.932 1.00 14.35 O ANISOU 2471 O PHE B 90 1899 1832 1721 28 -41 42 O ATOM 2472 CB PHE B 90 -6.414 13.073 -24.571 1.00 15.26 C ANISOU 2472 CB PHE B 90 1919 1931 1947 30 -55 23 C ATOM 2473 CG PHE B 90 -7.306 12.015 -23.979 1.00 16.43 C ANISOU 2473 CG PHE B 90 2091 2026 2126 -28 22 39 C ATOM 2474 CD1 PHE B 90 -7.262 11.731 -22.625 1.00 17.22 C ANISOU 2474 CD1 PHE B 90 2220 2182 2142 3 -13 -13 C ATOM 2475 CD2 PHE B 90 -8.169 11.296 -24.789 1.00 16.82 C ANISOU 2475 CD2 PHE B 90 2174 2140 2076 -1 -39 11 C ATOM 2476 CE1 PHE B 90 -8.077 10.749 -22.091 1.00 17.91 C ANISOU 2476 CE1 PHE B 90 2308 2241 2256 -20 10 28 C ATOM 2477 CE2 PHE B 90 -8.987 10.315 -24.260 1.00 17.66 C ANISOU 2477 CE2 PHE B 90 2247 2215 2250 -41 -17 28 C ATOM 2478 CZ PHE B 90 -8.936 10.041 -22.909 1.00 18.17 C ANISOU 2478 CZ PHE B 90 2324 2316 2262 -23 4 3 C ATOM 2479 N LYS B 91 -3.549 13.302 -26.704 1.00 15.25 N ANISOU 2479 N LYS B 91 1990 1915 1891 22 -16 -4 N ATOM 2480 CA LYS B 91 -2.497 14.141 -27.256 1.00 16.20 C ANISOU 2480 CA LYS B 91 2092 2002 2059 -52 -57 82 C ATOM 2481 C LYS B 91 -3.084 15.375 -27.938 1.00 15.94 C ANISOU 2481 C LYS B 91 2074 1974 2007 -21 -33 24 C ATOM 2482 O LYS B 91 -4.091 15.284 -28.633 1.00 16.34 O ANISOU 2482 O LYS B 91 2124 2051 2034 -33 -50 34 O ATOM 2483 CB LYS B 91 -1.646 13.367 -28.264 1.00 20.08 C ANISOU 2483 CB LYS B 91 2542 2640 2449 -21 168 -149 C ATOM 2484 CG LYS B 91 -0.890 12.180 -27.692 1.00 26.12 C ANISOU 2484 CG LYS B 91 3376 3132 3418 51 -162 170 C ATOM 2485 CD LYS B 91 0.009 11.560 -28.755 1.00 32.11 C ANISOU 2485 CD LYS B 91 4038 4185 3979 4 148 -138 C ATOM 2486 CE LYS B 91 0.635 10.264 -28.272 1.00 36.83 C ANISOU 2486 CE LYS B 91 4709 4541 4743 44 -71 96 C ATOM 2487 NZ LYS B 91 1.491 9.635 -29.316 1.00 39.11 N ANISOU 2487 NZ LYS B 91 4973 4937 4949 29 45 -20 N ATOM 2488 N TRP B 92 -2.442 16.514 -27.706 1.00 15.43 N ANISOU 2488 N TRP B 92 2052 1926 1886 4 -19 37 N ATOM 2489 CA TRP B 92 -2.809 17.736 -28.410 1.00 15.02 C ANISOU 2489 CA TRP B 92 2019 1850 1836 -9 5 -21 C ATOM 2490 C TRP B 92 -2.150 17.739 -29.789 1.00 15.08 C ANISOU 2490 C TRP B 92 1936 1929 1865 18 10 -25 C ATOM 2491 O TRP B 92 -0.967 17.439 -29.906 1.00 14.81 O ANISOU 2491 O TRP B 92 1901 1992 1734 6 -35 6 O ATOM 2492 CB TRP B 92 -2.354 18.963 -27.639 1.00 13.87 C ANISOU 2492 CB TRP B 92 1777 1852 1639 -22 -14 36 C ATOM 2493 CG TRP B 92 -2.753 20.289 -28.204 1.00 14.59 C ANISOU 2493 CG TRP B 92 1869 1859 1815 38 29 2 C ATOM 2494 CD1 TRP B 92 -3.952 20.641 -28.753 1.00 14.63 C ANISOU 2494 CD1 TRP B 92 1881 1871 1805 49 19 -15 C ATOM 2495 CD2 TRP B 92 -1.933 21.464 -28.253 1.00 15.38 C ANISOU 2495 CD2 TRP B 92 2035 1913 1897 -35 25 12 C ATOM 2496 NE1 TRP B 92 -3.928 21.956 -29.143 1.00 15.12 N ANISOU 2496 NE1 TRP B 92 1998 1916 1830 -19 -5 32 N ATOM 2497 CE2 TRP B 92 -2.702 22.489 -28.836 1.00 16.07 C ANISOU 2497 CE2 TRP B 92 1983 2057 2064 17 -23 1 C ATOM 2498 CE3 TRP B 92 -0.623 21.747 -27.849 1.00 16.77 C ANISOU 2498 CE3 TRP B 92 2093 2154 2124 -15 -23 -24 C ATOM 2499 CZ2 TRP B 92 -2.198 23.773 -29.035 1.00 16.64 C ANISOU 2499 CZ2 TRP B 92 2165 2102 2054 -15 7 39 C ATOM 2500 CZ3 TRP B 92 -0.127 23.021 -28.051 1.00 17.80 C ANISOU 2500 CZ3 TRP B 92 2330 2203 2230 -19 -24 25 C ATOM 2501 CH2 TRP B 92 -0.914 24.018 -28.642 1.00 17.19 C ANISOU 2501 CH2 TRP B 92 2193 2186 2153 -28 -6 -4 C ATOM 2502 N ASP B 93 -2.914 18.151 -30.794 1.00 15.45 N ANISOU 2502 N ASP B 93 2031 1933 1906 2 -17 17 N ATOM 2503 CA ASP B 93 -2.396 18.166 -32.160 1.00 15.95 C ANISOU 2503 CA ASP B 93 2056 2034 1971 -1 25 22 C ATOM 2504 C ASP B 93 -1.703 19.476 -32.495 1.00 15.89 C ANISOU 2504 C ASP B 93 2054 1996 1987 10 0 0 C ATOM 2505 O ASP B 93 -1.239 19.662 -33.623 1.00 16.31 O ANISOU 2505 O ASP B 93 2119 2080 1998 -8 -6 54 O ATOM 2506 CB ASP B 93 -3.541 17.892 -33.140 1.00 17.04 C ANISOU 2506 CB ASP B 93 2161 2231 2083 -5 -44 -44 C ATOM 2507 CG ASP B 93 -4.710 18.841 -33.004 1.00 17.27 C ANISOU 2507 CG ASP B 93 2221 2189 2153 10 11 36 C ATOM 2508 OD1 ASP B 93 -4.619 19.853 -32.276 1.00 17.58 O ANISOU 2508 OD1 ASP B 93 2295 2183 2200 -25 -10 37 O ATOM 2509 OD2 ASP B 93 -5.762 18.580 -33.630 1.00 18.08 O ANISOU 2509 OD2 ASP B 93 2361 2371 2139 -87 -53 66 O ATOM 2510 N GLY B 94 -1.647 20.412 -31.552 1.00 15.54 N ANISOU 2510 N GLY B 94 2027 1958 1921 -8 -35 49 N ATOM 2511 CA GLY B 94 -0.970 21.680 -31.762 1.00 15.29 C ANISOU 2511 CA GLY B 94 1986 1935 1887 7 -23 10 C ATOM 2512 C GLY B 94 -1.891 22.719 -32.388 1.00 14.84 C ANISOU 2512 C GLY B 94 1953 1909 1776 1 -6 -15 C ATOM 2513 O GLY B 94 -1.444 23.837 -32.643 1.00 15.23 O ANISOU 2513 O GLY B 94 2052 1914 1823 -25 -7 -43 O ATOM 2514 N LYS B 95 -3.173 22.411 -32.526 1.00 15.00 N ANISOU 2514 N LYS B 95 1948 1953 1797 4 35 3 N ATOM 2515 CA LYS B 95 -4.103 23.341 -33.166 1.00 15.90 C ANISOU 2515 CA LYS B 95 2055 2005 1982 28 -19 39 C ATOM 2516 C LYS B 95 -4.895 24.095 -32.108 1.00 16.70 C ANISOU 2516 C LYS B 95 2146 2115 2083 27 27 -5 C ATOM 2517 O LYS B 95 -5.052 23.616 -30.982 1.00 16.96 O ANISOU 2517 O LYS B 95 2232 2107 2105 19 -49 55 O ATOM 2518 CB LYS B 95 -5.051 22.597 -34.106 1.00 16.40 C ANISOU 2518 CB LYS B 95 2110 2039 2082 -18 -29 7 C ATOM 2519 CG LYS B 95 -4.352 21.804 -35.197 1.00 16.81 C ANISOU 2519 CG LYS B 95 2130 2150 2106 20 -30 -30 C ATOM 2520 CD LYS B 95 -3.716 22.722 -36.231 1.00 18.76 C ANISOU 2520 CD LYS B 95 2434 2380 2315 -81 -43 98 C ATOM 2521 CE LYS B 95 -2.833 21.939 -37.191 1.00 21.46 C ANISOU 2521 CE LYS B 95 2663 2773 2718 49 25 -46 C ATOM 2522 NZ LYS B 95 -2.285 22.836 -38.253 1.00 23.20 N ANISOU 2522 NZ LYS B 95 2968 2978 2871 -29 13 65 N ATOM 2523 N PRO B 96 -5.418 25.260 -32.476 1.00 17.00 N ANISOU 2523 N PRO B 96 2207 2114 2137 0 1 16 N ATOM 2524 CA PRO B 96 -6.103 26.125 -31.532 1.00 17.38 C ANISOU 2524 CA PRO B 96 2255 2178 2169 23 7 4 C ATOM 2525 C PRO B 96 -7.305 25.458 -30.891 1.00 17.75 C ANISOU 2525 C PRO B 96 2264 2261 2220 -7 -3 6 C ATOM 2526 O PRO B 96 -8.110 24.798 -31.552 1.00 18.17 O ANISOU 2526 O PRO B 96 2375 2256 2273 -30 -29 -16 O ATOM 2527 CB PRO B 96 -6.512 27.338 -32.364 1.00 17.49 C ANISOU 2527 CB PRO B 96 2274 2167 2207 26 19 4 C ATOM 2528 CG PRO B 96 -5.521 27.385 -33.474 1.00 17.62 C ANISOU 2528 CG PRO B 96 2285 2190 2218 -1 25 21 C ATOM 2529 CD PRO B 96 -5.111 25.967 -33.745 1.00 17.16 C ANISOU 2529 CD PRO B 96 2224 2164 2132 -19 -8 13 C ATOM 2530 N ARG B 97 -7.422 25.608 -29.572 1.00 17.56 N ANISOU 2530 N ARG B 97 2231 2232 2208 7 -2 5 N ATOM 2531 CA ARG B 97 -8.635 25.211 -28.864 1.00 17.55 C ANISOU 2531 CA ARG B 97 2231 2234 2204 -1 -16 5 C ATOM 2532 C ARG B 97 -9.299 26.438 -28.258 1.00 17.51 C ANISOU 2532 C ARG B 97 2237 2218 2200 2 -32 21 C ATOM 2533 O ARG B 97 -8.683 27.501 -28.155 1.00 17.37 O ANISOU 2533 O ARG B 97 2256 2193 2152 14 -46 31 O ATOM 2534 CB ARG B 97 -8.323 24.153 -27.800 1.00 18.06 C ANISOU 2534 CB ARG B 97 2335 2294 2232 4 5 43 C ATOM 2535 CG ARG B 97 -8.127 22.771 -28.417 1.00 19.31 C ANISOU 2535 CG ARG B 97 2530 2342 2465 19 27 19 C ATOM 2536 CD ARG B 97 -7.667 21.753 -27.382 1.00 19.51 C ANISOU 2536 CD ARG B 97 2489 2435 2489 24 -50 25 C ATOM 2537 NE ARG B 97 -7.539 20.428 -27.987 1.00 19.88 N ANISOU 2537 NE ARG B 97 2519 2498 2537 0 -6 -41 N ATOM 2538 CZ ARG B 97 -7.248 19.321 -27.311 1.00 21.12 C ANISOU 2538 CZ ARG B 97 2735 2611 2677 18 -13 38 C ATOM 2539 NH1 ARG B 97 -7.050 19.366 -25.999 1.00 21.02 N ANISOU 2539 NH1 ARG B 97 2686 2623 2676 -20 -17 5 N ATOM 2540 NH2 ARG B 97 -7.158 18.166 -27.957 1.00 21.28 N ANISOU 2540 NH2 ARG B 97 2793 2667 2625 20 11 6 N ATOM 2541 N ALA B 98 -10.546 26.295 -27.827 1.00 17.73 N ANISOU 2541 N ALA B 98 2268 2266 2201 12 -1 21 N ATOM 2542 CA ALA B 98 -11.339 27.421 -27.349 1.00 17.98 C ANISOU 2542 CA ALA B 98 2306 2261 2266 15 -5 15 C ATOM 2543 C ALA B 98 -10.775 28.013 -26.065 1.00 18.36 C ANISOU 2543 C ALA B 98 2370 2311 2294 4 -25 5 C ATOM 2544 O ALA B 98 -10.928 29.206 -25.794 1.00 19.09 O ANISOU 2544 O ALA B 98 2497 2355 2400 30 -32 4 O ATOM 2545 CB ALA B 98 -12.787 26.994 -27.146 1.00 18.62 C ANISOU 2545 CB ALA B 98 2352 2363 2362 -16 4 25 C ATOM 2546 N MET B 99 -10.187 27.172 -25.219 1.00 18.08 N ANISOU 2546 N MET B 99 2334 2265 2269 -10 -20 -5 N ATOM 2547 CA MET B 99 -9.471 27.625 -24.035 1.00 17.94 C ANISOU 2547 CA MET B 99 2290 2229 2299 3 -32 -20 C ATOM 2548 C MET B 99 -7.996 27.260 -24.110 1.00 17.46 C ANISOU 2548 C MET B 99 2274 2176 2183 5 -23 7 C ATOM 2549 O MET B 99 -7.609 26.132 -24.422 1.00 17.17 O ANISOU 2549 O MET B 99 2231 2148 2144 -6 -77 4 O ATOM 2550 CB AMET B 99 -10.111 27.047 -22.770 0.50 19.54 C ANISOU 2550 CB AMET B 99 2541 2469 2415 -38 26 23 C ATOM 2551 CB BMET B 99 -10.071 26.993 -22.774 0.50 19.53 C ANISOU 2551 CB BMET B 99 2552 2458 2411 -25 26 25 C ATOM 2552 CG AMET B 99 -11.510 27.591 -22.510 0.50 21.16 C ANISOU 2552 CG AMET B 99 2653 2665 2720 26 -9 -15 C ATOM 2553 CG BMET B 99 -11.560 27.203 -22.571 0.50 21.42 C ANISOU 2553 CG BMET B 99 2654 2757 2728 -11 0 -1 C ATOM 2554 SD AMET B 99 -12.269 26.881 -21.046 0.50 22.19 S ANISOU 2554 SD AMET B 99 2886 2777 2767 -7 27 5 S ATOM 2555 SD BMET B 99 -12.005 28.938 -22.377 0.50 23.04 S ANISOU 2555 SD BMET B 99 2960 2860 2935 51 20 -9 S ATOM 2556 CE AMET B 99 -13.769 27.853 -20.922 0.50 23.03 C ANISOU 2556 CE AMET B 99 2922 2902 2928 14 -4 3 C ATOM 2557 CE BMET B 99 -13.771 28.817 -22.111 0.50 23.58 C ANISOU 2557 CE BMET B 99 3001 2972 2988 -3 -6 -1 C ATOM 2558 N LYS B 100 -7.128 28.203 -23.756 1.00 17.63 N ANISOU 2558 N LYS B 100 2273 2220 2204 7 -38 10 N ATOM 2559 CA LYS B 100 -5.688 28.005 -23.706 1.00 18.36 C ANISOU 2559 CA LYS B 100 2322 2400 2255 94 7 77 C ATOM 2560 C LYS B 100 -5.286 26.880 -22.761 1.00 17.35 C ANISOU 2560 C LYS B 100 2200 2224 2168 7 -8 -12 C ATOM 2561 O LYS B 100 -4.341 26.125 -23.001 1.00 16.45 O ANISOU 2561 O LYS B 100 2182 2082 1986 -11 -62 8 O ATOM 2562 CB LYS B 100 -5.005 29.305 -23.261 1.00 24.22 C ANISOU 2562 CB LYS B 100 3314 2763 3126 -141 -67 -94 C ATOM 2563 CG LYS B 100 -3.491 29.276 -23.381 1.00 31.04 C ANISOU 2563 CG LYS B 100 3728 4046 4020 64 41 67 C ATOM 2564 CD LYS B 100 -2.858 30.490 -22.714 1.00 34.92 C ANISOU 2564 CD LYS B 100 4554 4298 4416 -36 -63 -58 C ATOM 2565 CE LYS B 100 -1.382 30.599 -23.065 1.00 37.90 C ANISOU 2565 CE LYS B 100 4746 4845 4810 -44 22 -6 C ATOM 2566 NZ LYS B 100 -0.640 29.354 -22.713 1.00 39.21 N ANISOU 2566 NZ LYS B 100 4984 4932 4981 25 -6 -2 N ATOM 2567 N GLN B 101 -6.031 26.712 -21.674 1.00 17.19 N ANISOU 2567 N GLN B 101 2251 2119 2161 -9 -14 -25 N ATOM 2568 CA GLN B 101 -5.844 25.628 -20.724 1.00 17.32 C ANISOU 2568 CA GLN B 101 2264 2121 2194 -34 -88 -5 C ATOM 2569 C GLN B 101 -6.043 24.236 -21.295 1.00 16.42 C ANISOU 2569 C GLN B 101 2141 2082 2017 16 -42 7 C ATOM 2570 O GLN B 101 -5.584 23.252 -20.701 1.00 16.42 O ANISOU 2570 O GLN B 101 2159 2149 1930 39 -31 32 O ATOM 2571 CB GLN B 101 -6.791 25.857 -19.531 1.00 20.85 C ANISOU 2571 CB GLN B 101 2561 2791 2568 41 118 35 C ATOM 2572 CG GLN B 101 -6.514 27.171 -18.812 1.00 24.96 C ANISOU 2572 CG GLN B 101 3250 3037 3196 -47 -64 -58 C ATOM 2573 CD GLN B 101 -7.592 27.528 -17.810 1.00 27.24 C ANISOU 2573 CD GLN B 101 3491 3469 3390 -13 65 -34 C ATOM 2574 OE1 GLN B 101 -8.456 28.369 -18.067 1.00 28.75 O ANISOU 2574 OE1 GLN B 101 3646 3612 3665 40 -36 -4 O ATOM 2575 NE2 GLN B 101 -7.559 26.887 -16.648 1.00 26.64 N ANISOU 2575 NE2 GLN B 101 3401 3345 3375 40 -7 -32 N ATOM 2576 N TRP B 102 -6.716 24.083 -22.430 1.00 15.50 N ANISOU 2576 N TRP B 102 2013 1929 1947 3 -3 26 N ATOM 2577 CA TRP B 102 -6.861 22.818 -23.114 1.00 14.77 C ANISOU 2577 CA TRP B 102 1865 1882 1865 9 -11 41 C ATOM 2578 C TRP B 102 -5.776 22.538 -24.147 1.00 14.55 C ANISOU 2578 C TRP B 102 1880 1815 1832 5 -12 26 C ATOM 2579 O TRP B 102 -5.737 21.438 -24.715 1.00 14.50 O ANISOU 2579 O TRP B 102 1919 1807 1784 4 -9 36 O ATOM 2580 CB TRP B 102 -8.206 22.734 -23.840 1.00 14.31 C ANISOU 2580 CB TRP B 102 1855 1815 1769 -15 -7 50 C ATOM 2581 CG TRP B 102 -9.417 22.984 -23.002 1.00 15.06 C ANISOU 2581 CG TRP B 102 1888 1951 1883 24 12 8 C ATOM 2582 CD1 TRP B 102 -9.550 22.863 -21.648 1.00 15.16 C ANISOU 2582 CD1 TRP B 102 1932 1937 1892 4 -27 25 C ATOM 2583 CD2 TRP B 102 -10.710 23.372 -23.490 1.00 15.05 C ANISOU 2583 CD2 TRP B 102 1897 1916 1905 -2 -18 35 C ATOM 2584 NE1 TRP B 102 -10.827 23.166 -21.263 1.00 15.41 N ANISOU 2584 NE1 TRP B 102 2007 1978 1869 47 43 51 N ATOM 2585 CE2 TRP B 102 -11.564 23.482 -22.378 1.00 15.53 C ANISOU 2585 CE2 TRP B 102 1988 2009 1904 14 -12 -9 C ATOM 2586 CE3 TRP B 102 -11.219 23.643 -24.766 1.00 14.92 C ANISOU 2586 CE3 TRP B 102 1890 1893 1884 -33 -3 34 C ATOM 2587 CZ2 TRP B 102 -12.903 23.852 -22.499 1.00 15.92 C ANISOU 2587 CZ2 TRP B 102 2005 2026 2018 0 5 42 C ATOM 2588 CZ3 TRP B 102 -12.545 24.007 -24.881 1.00 15.06 C ANISOU 2588 CZ3 TRP B 102 1923 1831 1969 9 -14 58 C ATOM 2589 CH2 TRP B 102 -13.373 24.108 -23.755 1.00 16.37 C ANISOU 2589 CH2 TRP B 102 2116 2102 2003 -10 20 5 C ATOM 2590 N GLU B 103 -4.914 23.504 -24.430 1.00 14.35 N ANISOU 2590 N GLU B 103 1805 1825 1821 18 -25 -10 N ATOM 2591 CA GLU B 103 -3.894 23.344 -25.460 1.00 14.33 C ANISOU 2591 CA GLU B 103 1828 1833 1783 20 -36 -6 C ATOM 2592 C GLU B 103 -2.642 22.677 -24.913 1.00 14.22 C ANISOU 2592 C GLU B 103 1810 1802 1790 1 -28 6 C ATOM 2593 O GLU B 103 -1.585 23.273 -24.742 1.00 14.87 O ANISOU 2593 O GLU B 103 1879 1887 1882 -48 -42 10 O ATOM 2594 CB GLU B 103 -3.583 24.708 -26.081 1.00 15.75 C ANISOU 2594 CB GLU B 103 2026 1940 2019 -57 -6 51 C ATOM 2595 CG GLU B 103 -4.783 25.288 -26.826 1.00 17.08 C ANISOU 2595 CG GLU B 103 2160 2171 2157 41 -80 -1 C ATOM 2596 CD GLU B 103 -4.474 26.627 -27.466 1.00 18.97 C ANISOU 2596 CD GLU B 103 2448 2342 2418 -32 23 70 C ATOM 2597 OE1 GLU B 103 -3.513 27.294 -27.030 1.00 19.73 O ANISOU 2597 OE1 GLU B 103 2584 2489 2425 -84 -61 73 O ATOM 2598 OE2 GLU B 103 -5.202 27.009 -28.405 1.00 19.82 O ANISOU 2598 OE2 GLU B 103 2625 2445 2462 -38 -62 48 O ATOM 2599 N ARG B 104 -2.746 21.376 -24.667 1.00 13.90 N ANISOU 2599 N ARG B 104 1765 1778 1740 11 -37 -8 N ATOM 2600 CA ARG B 104 -1.712 20.552 -24.074 1.00 13.94 C ANISOU 2600 CA ARG B 104 1775 1711 1810 10 6 31 C ATOM 2601 C ARG B 104 -2.180 19.096 -24.032 1.00 13.31 C ANISOU 2601 C ARG B 104 1700 1698 1659 0 -10 21 C ATOM 2602 O ARG B 104 -3.388 18.857 -24.108 1.00 12.97 O ANISOU 2602 O ARG B 104 1702 1660 1567 -18 -28 91 O ATOM 2603 CB ARG B 104 -1.407 21.016 -22.644 1.00 16.76 C ANISOU 2603 CB ARG B 104 2243 2142 1984 -18 -141 -33 C ATOM 2604 CG ARG B 104 -2.642 21.022 -21.751 1.00 20.28 C ANISOU 2604 CG ARG B 104 2494 2621 2590 16 86 42 C ATOM 2605 CD ARG B 104 -2.337 21.635 -20.398 1.00 23.51 C ANISOU 2605 CD ARG B 104 3060 3046 2827 22 -47 -60 C ATOM 2606 NE ARG B 104 -1.621 22.904 -20.504 1.00 25.97 N ANISOU 2606 NE ARG B 104 3301 3222 3345 -36 43 14 N ATOM 2607 CZ ARG B 104 -0.809 23.348 -19.550 1.00 27.38 C ANISOU 2607 CZ ARG B 104 3450 3498 3455 -4 -44 -34 C ATOM 2608 NH1 ARG B 104 -0.623 22.620 -18.454 1.00 27.69 N ANISOU 2608 NH1 ARG B 104 3524 3494 3504 -30 3 10 N ATOM 2609 NH2 ARG B 104 -0.182 24.505 -19.695 1.00 28.30 N ANISOU 2609 NH2 ARG B 104 3613 3550 3591 -25 -8 17 N ATOM 2610 N ASP B 105 -1.239 18.163 -23.965 1.00 13.17 N ANISOU 2610 N ASP B 105 1726 1646 1633 -11 -33 10 N ATOM 2611 CA ASP B 105 -1.606 16.767 -23.729 1.00 13.07 C ANISOU 2611 CA ASP B 105 1707 1660 1598 -38 -8 9 C ATOM 2612 C ASP B 105 -2.319 16.688 -22.381 1.00 12.66 C ANISOU 2612 C ASP B 105 1632 1592 1587 -3 -14 11 C ATOM 2613 O ASP B 105 -1.936 17.408 -21.458 1.00 13.15 O ANISOU 2613 O ASP B 105 1766 1658 1574 -4 -6 0 O ATOM 2614 CB ASP B 105 -0.401 15.840 -23.727 1.00 14.50 C ANISOU 2614 CB ASP B 105 1807 1822 1879 33 -61 26 C ATOM 2615 CG ASP B 105 0.352 15.775 -25.039 1.00 16.52 C ANISOU 2615 CG ASP B 105 2140 2152 1985 4 29 2 C ATOM 2616 OD1 ASP B 105 -0.140 16.309 -26.055 1.00 16.24 O ANISOU 2616 OD1 ASP B 105 2142 2081 1948 -18 23 -5 O ATOM 2617 OD2 ASP B 105 1.453 15.184 -25.052 1.00 17.55 O ANISOU 2617 OD2 ASP B 105 2238 2345 2085 82 43 15 O ATOM 2618 N LEU B 106 -3.319 15.830 -22.277 1.00 11.98 N ANISOU 2618 N LEU B 106 1534 1574 1443 42 -10 21 N ATOM 2619 CA LEU B 106 -4.073 15.678 -21.040 1.00 11.88 C ANISOU 2619 CA LEU B 106 1500 1499 1513 10 18 44 C ATOM 2620 C LEU B 106 -4.253 14.209 -20.685 1.00 11.46 C ANISOU 2620 C LEU B 106 1473 1456 1425 35 -22 21 C ATOM 2621 O LEU B 106 -4.410 13.359 -21.560 1.00 11.62 O ANISOU 2621 O LEU B 106 1597 1427 1392 40 -53 77 O ATOM 2622 CB LEU B 106 -5.443 16.348 -21.170 1.00 11.99 C ANISOU 2622 CB LEU B 106 1528 1484 1544 31 -25 40 C ATOM 2623 CG LEU B 106 -5.448 17.877 -21.277 1.00 12.04 C ANISOU 2623 CG LEU B 106 1558 1467 1549 10 -3 -10 C ATOM 2624 CD1 LEU B 106 -6.765 18.365 -21.861 1.00 13.09 C ANISOU 2624 CD1 LEU B 106 1639 1717 1616 10 -73 33 C ATOM 2625 CD2 LEU B 106 -5.169 18.518 -19.927 1.00 12.18 C ANISOU 2625 CD2 LEU B 106 1604 1484 1539 24 -6 21 C ATOM 2626 N THR B 107 -4.217 13.902 -19.386 1.00 11.53 N ANISOU 2626 N THR B 107 1481 1455 1444 12 -15 25 N ATOM 2627 CA THR B 107 -4.658 12.578 -18.949 1.00 11.66 C ANISOU 2627 CA THR B 107 1459 1459 1511 7 -16 29 C ATOM 2628 C THR B 107 -6.180 12.541 -18.894 1.00 11.30 C ANISOU 2628 C THR B 107 1448 1426 1417 0 -1 23 C ATOM 2629 O THR B 107 -6.824 13.575 -19.081 1.00 11.32 O ANISOU 2629 O THR B 107 1494 1469 1338 31 -4 68 O ATOM 2630 CB THR B 107 -4.082 12.233 -17.567 1.00 12.92 C ANISOU 2630 CB THR B 107 1669 1688 1550 -21 -58 45 C ATOM 2631 OG1 THR B 107 -4.650 13.105 -16.584 1.00 13.88 O ANISOU 2631 OG1 THR B 107 1694 1853 1726 62 -10 -12 O ATOM 2632 CG2 THR B 107 -2.572 12.394 -17.582 1.00 12.95 C ANISOU 2632 CG2 THR B 107 1669 1725 1526 3 -9 33 C ATOM 2633 N LEU B 108 -6.755 11.378 -18.604 1.00 10.90 N ANISOU 2633 N LEU B 108 1393 1427 1321 9 -46 30 N ATOM 2634 CA LEU B 108 -8.200 11.304 -18.408 1.00 10.68 C ANISOU 2634 CA LEU B 108 1398 1401 1258 21 4 41 C ATOM 2635 C LEU B 108 -8.629 12.224 -17.273 1.00 10.52 C ANISOU 2635 C LEU B 108 1367 1319 1310 -2 -24 18 C ATOM 2636 O LEU B 108 -9.526 13.048 -17.453 1.00 10.20 O ANISOU 2636 O LEU B 108 1378 1324 1175 1 -39 72 O ATOM 2637 CB LEU B 108 -8.661 9.870 -18.176 1.00 12.55 C ANISOU 2637 CB LEU B 108 1745 1450 1574 -18 -13 21 C ATOM 2638 CG LEU B 108 -10.153 9.673 -17.900 1.00 15.42 C ANISOU 2638 CG LEU B 108 1867 1987 2006 0 10 2 C ATOM 2639 CD1 LEU B 108 -11.000 10.143 -19.073 1.00 16.08 C ANISOU 2639 CD1 LEU B 108 2043 2058 2010 -8 -34 16 C ATOM 2640 CD2 LEU B 108 -10.434 8.215 -17.571 1.00 16.89 C ANISOU 2640 CD2 LEU B 108 2218 2057 2142 -31 -21 17 C ATOM 2641 N ARG B 109 -7.974 12.128 -16.111 1.00 10.60 N ANISOU 2641 N ARG B 109 1409 1286 1333 9 -46 18 N ATOM 2642 CA ARG B 109 -8.269 13.034 -15.011 1.00 10.77 C ANISOU 2642 CA ARG B 109 1391 1367 1335 8 -2 9 C ATOM 2643 C ARG B 109 -8.065 14.493 -15.409 1.00 10.62 C ANISOU 2643 C ARG B 109 1359 1358 1320 -16 -26 -21 C ATOM 2644 O ARG B 109 -8.929 15.324 -15.123 1.00 11.10 O ANISOU 2644 O ARG B 109 1383 1448 1386 14 -14 -28 O ATOM 2645 CB AARG B 109 -7.394 12.713 -13.790 0.50 11.41 C ANISOU 2645 CB AARG B 109 1452 1485 1400 11 -36 22 C ATOM 2646 CB BARG B 109 -7.441 12.713 -13.760 0.50 11.28 C ANISOU 2646 CB BARG B 109 1442 1461 1382 10 -27 12 C ATOM 2647 CG AARG B 109 -7.651 13.644 -12.619 0.50 12.09 C ANISOU 2647 CG AARG B 109 1552 1556 1486 22 -27 -23 C ATOM 2648 CG BARG B 109 -7.720 13.700 -12.638 0.50 11.73 C ANISOU 2648 CG BARG B 109 1513 1508 1435 25 -26 -15 C ATOM 2649 CD AARG B 109 -6.615 13.495 -11.509 0.50 11.46 C ANISOU 2649 CD AARG B 109 1482 1433 1439 14 1 4 C ATOM 2650 CD BARG B 109 -7.320 13.185 -11.263 0.50 11.39 C ANISOU 2650 CD BARG B 109 1460 1444 1423 -8 2 18 C ATOM 2651 NE AARG B 109 -6.621 14.695 -10.678 0.50 11.13 N ANISOU 2651 NE AARG B 109 1463 1430 1336 9 -34 18 N ATOM 2652 NE BARG B 109 -7.725 14.154 -10.243 0.50 11.21 N ANISOU 2652 NE BARG B 109 1378 1458 1421 33 8 31 N ATOM 2653 CZ AARG B 109 -7.488 14.999 -9.724 0.50 11.57 C ANISOU 2653 CZ AARG B 109 1457 1503 1435 6 4 6 C ATOM 2654 CZ BARG B 109 -7.129 15.319 -10.027 0.50 12.56 C ANISOU 2654 CZ BARG B 109 1600 1561 1612 -30 -26 1 C ATOM 2655 NH1AARG B 109 -8.475 14.180 -9.392 0.50 12.14 N ANISOU 2655 NH1AARG B 109 1518 1543 1551 -39 -10 -26 N ATOM 2656 NH1BARG B 109 -6.072 15.679 -10.745 0.50 13.06 N ANISOU 2656 NH1BARG B 109 1642 1668 1651 -22 15 2 N ATOM 2657 NH2AARG B 109 -7.352 16.151 -9.073 0.50 12.59 N ANISOU 2657 NH2AARG B 109 1642 1553 1591 -5 -8 -20 N ATOM 2658 NH2BARG B 109 -7.581 16.136 -9.084 0.50 13.11 N ANISOU 2658 NH2BARG B 109 1686 1650 1644 7 -6 -8 N ATOM 2659 N GLY B 110 -6.958 14.817 -16.070 1.00 10.62 N ANISOU 2659 N GLY B 110 1379 1355 1302 -6 -18 24 N ATOM 2660 CA GLY B 110 -6.689 16.193 -16.469 1.00 10.61 C ANISOU 2660 CA GLY B 110 1369 1351 1311 -5 -13 16 C ATOM 2661 C GLY B 110 -7.790 16.725 -17.383 1.00 10.69 C ANISOU 2661 C GLY B 110 1374 1379 1309 -1 -19 11 C ATOM 2662 O GLY B 110 -8.302 17.827 -17.189 1.00 10.76 O ANISOU 2662 O GLY B 110 1431 1396 1261 18 -55 14 O ATOM 2663 N ALA B 111 -8.188 15.929 -18.372 1.00 10.73 N ANISOU 2663 N ALA B 111 1401 1375 1303 -31 -11 30 N ATOM 2664 CA ALA B 111 -9.234 16.339 -19.307 1.00 10.67 C ANISOU 2664 CA ALA B 111 1387 1367 1299 -22 -13 18 C ATOM 2665 C ALA B 111 -10.559 16.623 -18.621 1.00 10.90 C ANISOU 2665 C ALA B 111 1431 1382 1327 -9 17 21 C ATOM 2666 O ALA B 111 -11.279 17.567 -18.946 1.00 11.63 O ANISOU 2666 O ALA B 111 1584 1502 1332 50 46 103 O ATOM 2667 CB ALA B 111 -9.389 15.262 -20.375 1.00 10.84 C ANISOU 2667 CB ALA B 111 1421 1397 1301 -7 30 -5 C ATOM 2668 N ILE B 112 -10.929 15.806 -17.638 1.00 10.71 N ANISOU 2668 N ILE B 112 1384 1319 1365 -20 -2 33 N ATOM 2669 CA ILE B 112 -12.127 16.010 -16.845 1.00 10.41 C ANISOU 2669 CA ILE B 112 1390 1255 1309 -13 -9 25 C ATOM 2670 C ILE B 112 -11.998 17.262 -15.987 1.00 10.17 C ANISOU 2670 C ILE B 112 1312 1274 1277 -22 2 16 C ATOM 2671 O ILE B 112 -12.872 18.129 -15.970 1.00 10.46 O ANISOU 2671 O ILE B 112 1315 1327 1334 -10 -41 51 O ATOM 2672 CB ILE B 112 -12.417 14.777 -15.966 1.00 10.03 C ANISOU 2672 CB ILE B 112 1324 1249 1239 -3 -56 36 C ATOM 2673 CG1 ILE B 112 -12.737 13.575 -16.865 1.00 10.93 C ANISOU 2673 CG1 ILE B 112 1505 1305 1345 -22 -85 10 C ATOM 2674 CG2 ILE B 112 -13.551 15.044 -14.993 1.00 11.03 C ANISOU 2674 CG2 ILE B 112 1436 1356 1398 22 -1 -27 C ATOM 2675 CD1 ILE B 112 -12.822 12.255 -16.123 1.00 11.20 C ANISOU 2675 CD1 ILE B 112 1459 1281 1515 -36 -19 20 C ATOM 2676 N GLN B 113 -10.873 17.374 -15.283 1.00 10.55 N ANISOU 2676 N GLN B 113 1345 1352 1313 -28 -22 42 N ATOM 2677 CA GLN B 113 -10.678 18.454 -14.326 1.00 11.43 C ANISOU 2677 CA GLN B 113 1488 1379 1477 -10 2 -25 C ATOM 2678 C GLN B 113 -10.533 19.825 -14.969 1.00 11.70 C ANISOU 2678 C GLN B 113 1535 1440 1471 6 -20 29 C ATOM 2679 O GLN B 113 -10.920 20.805 -14.319 1.00 11.79 O ANISOU 2679 O GLN B 113 1647 1385 1448 41 -15 98 O ATOM 2680 CB GLN B 113 -9.463 18.150 -13.444 1.00 13.54 C ANISOU 2680 CB GLN B 113 1588 1811 1746 4 -98 -8 C ATOM 2681 CG GLN B 113 -9.600 16.937 -12.540 1.00 16.74 C ANISOU 2681 CG GLN B 113 2236 1979 2146 -56 -47 96 C ATOM 2682 CD GLN B 113 -10.209 17.267 -11.192 1.00 20.25 C ANISOU 2682 CD GLN B 113 2608 2640 2445 -4 102 -4 C ATOM 2683 OE1 GLN B 113 -10.142 18.407 -10.731 1.00 22.25 O ANISOU 2683 OE1 GLN B 113 3007 2705 2743 9 27 4 O ATOM 2684 NE2 GLN B 113 -10.796 16.262 -10.550 1.00 20.05 N ANISOU 2684 NE2 GLN B 113 2556 2570 2492 33 15 27 N ATOM 2685 N VAL B 114 -10.013 19.937 -16.190 1.00 12.10 N ANISOU 2685 N VAL B 114 1552 1520 1523 1 2 -11 N ATOM 2686 CA VAL B 114 -9.986 21.230 -16.870 1.00 12.43 C ANISOU 2686 CA VAL B 114 1587 1569 1567 -31 -21 28 C ATOM 2687 C VAL B 114 -11.173 21.391 -17.816 1.00 12.42 C ANISOU 2687 C VAL B 114 1590 1574 1556 -20 -16 22 C ATOM 2688 O VAL B 114 -11.293 22.394 -18.526 1.00 12.63 O ANISOU 2688 O VAL B 114 1626 1556 1618 -37 -59 23 O ATOM 2689 CB VAL B 114 -8.681 21.512 -17.629 1.00 12.50 C ANISOU 2689 CB VAL B 114 1600 1596 1553 36 16 -14 C ATOM 2690 CG1 VAL B 114 -7.475 21.410 -16.700 1.00 13.51 C ANISOU 2690 CG1 VAL B 114 1695 1806 1630 -38 -49 21 C ATOM 2691 CG2 VAL B 114 -8.502 20.594 -18.827 1.00 11.04 C ANISOU 2691 CG2 VAL B 114 1417 1356 1422 -4 12 91 C ATOM 2692 N SER B 115 -12.060 20.407 -17.826 1.00 12.23 N ANISOU 2692 N SER B 115 1574 1533 1540 -7 -40 17 N ATOM 2693 CA SER B 115 -13.272 20.429 -18.632 1.00 12.40 C ANISOU 2693 CA SER B 115 1578 1581 1551 -19 -35 23 C ATOM 2694 C SER B 115 -12.950 20.576 -20.115 1.00 12.44 C ANISOU 2694 C SER B 115 1581 1589 1555 -9 -27 12 C ATOM 2695 O SER B 115 -13.582 21.367 -20.819 1.00 12.81 O ANISOU 2695 O SER B 115 1655 1656 1555 -7 -47 27 O ATOM 2696 CB SER B 115 -14.210 21.542 -18.161 1.00 13.48 C ANISOU 2696 CB SER B 115 1647 1734 1740 43 -5 -2 C ATOM 2697 OG SER B 115 -14.555 21.377 -16.799 1.00 14.79 O ANISOU 2697 OG SER B 115 1899 1934 1787 -5 -25 14 O ATOM 2698 N ALA B 116 -12.017 19.764 -20.601 1.00 12.46 N ANISOU 2698 N ALA B 116 1614 1591 1530 -8 -25 -22 N ATOM 2699 CA ALA B 116 -11.563 19.824 -21.981 1.00 12.76 C ANISOU 2699 CA ALA B 116 1613 1646 1588 3 2 8 C ATOM 2700 C ALA B 116 -12.608 19.235 -22.921 1.00 13.09 C ANISOU 2700 C ALA B 116 1682 1620 1672 -15 -31 -5 C ATOM 2701 O ALA B 116 -12.563 18.084 -23.344 1.00 12.86 O ANISOU 2701 O ALA B 116 1646 1586 1656 10 -67 25 O ATOM 2702 CB ALA B 116 -10.231 19.106 -22.154 1.00 12.26 C ANISOU 2702 CB ALA B 116 1613 1614 1431 15 6 80 C ATOM 2703 N VAL B 117 -13.512 20.107 -23.371 1.00 13.47 N ANISOU 2703 N VAL B 117 1687 1691 1739 2 -7 41 N ATOM 2704 CA VAL B 117 -14.600 19.743 -24.263 1.00 14.21 C ANISOU 2704 CA VAL B 117 1824 1814 1760 -21 -42 -12 C ATOM 2705 C VAL B 117 -14.170 18.963 -25.490 1.00 14.22 C ANISOU 2705 C VAL B 117 1822 1812 1771 3 -30 -4 C ATOM 2706 O VAL B 117 -14.741 17.900 -25.752 1.00 14.34 O ANISOU 2706 O VAL B 117 1884 1836 1727 -47 -32 3 O ATOM 2707 CB VAL B 117 -15.420 20.986 -24.656 1.00 15.68 C ANISOU 2707 CB VAL B 117 2009 1911 2038 72 -14 0 C ATOM 2708 CG1 VAL B 117 -16.525 20.650 -25.643 1.00 16.79 C ANISOU 2708 CG1 VAL B 117 2186 2077 2117 -34 -68 0 C ATOM 2709 CG2 VAL B 117 -16.010 21.628 -23.406 1.00 15.91 C ANISOU 2709 CG2 VAL B 117 2031 2036 1977 22 -2 36 C ATOM 2710 N PRO B 118 -13.174 19.419 -26.238 1.00 14.36 N ANISOU 2710 N PRO B 118 1851 1823 1780 23 -16 30 N ATOM 2711 CA PRO B 118 -12.738 18.764 -27.458 1.00 14.63 C ANISOU 2711 CA PRO B 118 1887 1841 1833 15 -14 -3 C ATOM 2712 C PRO B 118 -12.310 17.321 -27.281 1.00 14.21 C ANISOU 2712 C PRO B 118 1844 1800 1755 -9 -27 -5 C ATOM 2713 O PRO B 118 -12.598 16.464 -28.127 1.00 13.97 O ANISOU 2713 O PRO B 118 1848 1772 1690 5 -29 17 O ATOM 2714 CB PRO B 118 -11.585 19.613 -27.971 1.00 15.05 C ANISOU 2714 CB PRO B 118 1926 1928 1865 -14 12 19 C ATOM 2715 CG PRO B 118 -11.310 20.645 -26.942 1.00 15.49 C ANISOU 2715 CG PRO B 118 1965 1937 1985 -8 18 -26 C ATOM 2716 CD PRO B 118 -12.543 20.753 -26.091 1.00 15.12 C ANISOU 2716 CD PRO B 118 1947 1885 1914 -14 9 -9 C ATOM 2717 N VAL B 119 -11.631 17.004 -26.180 1.00 13.94 N ANISOU 2717 N VAL B 119 1790 1750 1756 -12 -27 -15 N ATOM 2718 CA VAL B 119 -11.306 15.613 -25.866 1.00 13.91 C ANISOU 2718 CA VAL B 119 1784 1767 1736 -8 -5 17 C ATOM 2719 C VAL B 119 -12.564 14.763 -25.803 1.00 13.27 C ANISOU 2719 C VAL B 119 1745 1690 1608 23 -30 39 C ATOM 2720 O VAL B 119 -12.617 13.674 -26.376 1.00 13.73 O ANISOU 2720 O VAL B 119 1885 1737 1594 17 -37 36 O ATOM 2721 CB VAL B 119 -10.509 15.534 -24.553 1.00 14.09 C ANISOU 2721 CB VAL B 119 1729 1836 1789 15 -24 28 C ATOM 2722 CG1 VAL B 119 -10.283 14.100 -24.105 1.00 14.69 C ANISOU 2722 CG1 VAL B 119 1910 1827 1843 11 9 -23 C ATOM 2723 CG2 VAL B 119 -9.178 16.257 -24.747 1.00 13.80 C ANISOU 2723 CG2 VAL B 119 1804 1736 1703 -39 -14 23 C ATOM 2724 N PHE B 120 -13.593 15.246 -25.109 1.00 13.31 N ANISOU 2724 N PHE B 120 1732 1685 1639 27 -39 37 N ATOM 2725 CA PHE B 120 -14.792 14.448 -24.901 1.00 13.76 C ANISOU 2725 CA PHE B 120 1738 1781 1710 16 8 40 C ATOM 2726 C PHE B 120 -15.735 14.468 -26.090 1.00 14.15 C ANISOU 2726 C PHE B 120 1807 1822 1747 -9 -31 6 C ATOM 2727 O PHE B 120 -16.481 13.510 -26.293 1.00 13.94 O ANISOU 2727 O PHE B 120 1800 1789 1706 7 -60 81 O ATOM 2728 CB PHE B 120 -15.483 14.895 -23.606 1.00 13.60 C ANISOU 2728 CB PHE B 120 1785 1682 1700 -8 -5 1 C ATOM 2729 CG PHE B 120 -14.814 14.225 -22.428 1.00 14.36 C ANISOU 2729 CG PHE B 120 1861 1827 1767 2 -38 36 C ATOM 2730 CD1 PHE B 120 -13.684 14.773 -21.847 1.00 14.58 C ANISOU 2730 CD1 PHE B 120 1883 1854 1801 -27 -14 6 C ATOM 2731 CD2 PHE B 120 -15.328 13.038 -21.937 1.00 14.43 C ANISOU 2731 CD2 PHE B 120 1841 1834 1808 -9 -13 22 C ATOM 2732 CE1 PHE B 120 -13.075 14.134 -20.778 1.00 14.79 C ANISOU 2732 CE1 PHE B 120 1902 1870 1849 -20 -1 43 C ATOM 2733 CE2 PHE B 120 -14.728 12.405 -20.865 1.00 13.97 C ANISOU 2733 CE2 PHE B 120 1762 1803 1744 -42 -14 -9 C ATOM 2734 CZ PHE B 120 -13.602 12.956 -20.287 1.00 13.44 C ANISOU 2734 CZ PHE B 120 1719 1751 1637 11 -15 -37 C ATOM 2735 N GLN B 121 -15.656 15.504 -26.926 1.00 14.79 N ANISOU 2735 N GLN B 121 1949 1870 1801 -11 -24 31 N ATOM 2736 CA GLN B 121 -16.341 15.463 -28.220 1.00 14.84 C ANISOU 2736 CA GLN B 121 1949 1852 1836 -11 -39 4 C ATOM 2737 C GLN B 121 -15.856 14.290 -29.063 1.00 14.39 C ANISOU 2737 C GLN B 121 1879 1818 1770 -1 -18 49 C ATOM 2738 O GLN B 121 -16.670 13.577 -29.655 1.00 14.89 O ANISOU 2738 O GLN B 121 2007 1835 1814 -26 -45 20 O ATOM 2739 CB GLN B 121 -16.148 16.773 -28.986 1.00 14.76 C ANISOU 2739 CB GLN B 121 1902 1931 1776 -28 -13 62 C ATOM 2740 CG GLN B 121 -16.881 17.952 -28.367 1.00 16.67 C ANISOU 2740 CG GLN B 121 2162 2114 2059 53 6 -52 C ATOM 2741 CD GLN B 121 -16.588 19.264 -29.069 1.00 18.27 C ANISOU 2741 CD GLN B 121 2430 2281 2232 -17 15 47 C ATOM 2742 OE1 GLN B 121 -15.445 19.539 -29.425 1.00 19.45 O ANISOU 2742 OE1 GLN B 121 2479 2491 2419 -74 -61 142 O ATOM 2743 NE2 GLN B 121 -17.627 20.067 -29.264 1.00 19.70 N ANISOU 2743 NE2 GLN B 121 2578 2452 2456 65 -14 26 N ATOM 2744 N GLN B 122 -14.549 14.070 -29.114 1.00 14.31 N ANISOU 2744 N GLN B 122 1887 1805 1745 6 4 42 N ATOM 2745 CA GLN B 122 -13.984 12.963 -29.873 1.00 14.59 C ANISOU 2745 CA GLN B 122 1904 1847 1792 23 -18 3 C ATOM 2746 C GLN B 122 -14.291 11.614 -29.237 1.00 15.14 C ANISOU 2746 C GLN B 122 1992 1881 1879 0 -6 20 C ATOM 2747 O GLN B 122 -14.573 10.654 -29.956 1.00 15.07 O ANISOU 2747 O GLN B 122 1956 1906 1863 -24 -57 45 O ATOM 2748 CB GLN B 122 -12.478 13.144 -30.056 1.00 15.38 C ANISOU 2748 CB GLN B 122 1938 1964 1942 -4 -10 10 C ATOM 2749 CG GLN B 122 -11.821 12.080 -30.917 1.00 16.18 C ANISOU 2749 CG GLN B 122 2110 1985 2053 6 12 -40 C ATOM 2750 CD GLN B 122 -12.371 12.008 -32.328 1.00 16.99 C ANISOU 2750 CD GLN B 122 2176 2154 2127 46 -43 62 C ATOM 2751 OE1 GLN B 122 -12.406 10.930 -32.926 1.00 18.68 O ANISOU 2751 OE1 GLN B 122 2489 2335 2274 -33 -52 -59 O ATOM 2752 NE2 GLN B 122 -12.795 13.145 -32.860 1.00 15.05 N ANISOU 2752 NE2 GLN B 122 1950 2005 1764 -42 -29 -25 N ATOM 2753 N ILE B 123 -14.241 11.525 -27.906 1.00 15.33 N ANISOU 2753 N ILE B 123 2016 1925 1882 -24 -21 -2 N ATOM 2754 CA ILE B 123 -14.707 10.314 -27.227 1.00 15.33 C ANISOU 2754 CA ILE B 123 1987 1933 1903 2 -6 8 C ATOM 2755 C ILE B 123 -16.126 9.959 -27.641 1.00 15.56 C ANISOU 2755 C ILE B 123 2003 1977 1931 -6 -2 8 C ATOM 2756 O ILE B 123 -16.400 8.816 -28.013 1.00 15.97 O ANISOU 2756 O ILE B 123 2122 1980 1964 10 -19 20 O ATOM 2757 CB ILE B 123 -14.609 10.450 -25.697 1.00 15.73 C ANISOU 2757 CB ILE B 123 2001 2057 1921 -8 -18 5 C ATOM 2758 CG1 ILE B 123 -13.130 10.448 -25.291 1.00 15.22 C ANISOU 2758 CG1 ILE B 123 1967 1955 1860 4 -2 -18 C ATOM 2759 CG2 ILE B 123 -15.354 9.338 -24.974 1.00 16.58 C ANISOU 2759 CG2 ILE B 123 2097 2096 2107 -67 -14 8 C ATOM 2760 CD1 ILE B 123 -12.878 10.950 -23.885 1.00 14.85 C ANISOU 2760 CD1 ILE B 123 1960 1851 1829 -10 -20 15 C ATOM 2761 N ALA B 124 -17.042 10.921 -27.582 1.00 15.76 N ANISOU 2761 N ALA B 124 2005 1984 1997 1 7 2 N ATOM 2762 CA ALA B 124 -18.429 10.697 -27.958 1.00 16.18 C ANISOU 2762 CA ALA B 124 2031 2044 2072 28 -21 6 C ATOM 2763 C ALA B 124 -18.571 10.217 -29.396 1.00 16.94 C ANISOU 2763 C ALA B 124 2183 2133 2120 14 -34 -14 C ATOM 2764 O ALA B 124 -19.339 9.288 -29.649 1.00 17.08 O ANISOU 2764 O ALA B 124 2214 2152 2124 -7 -68 30 O ATOM 2765 CB ALA B 124 -19.248 11.962 -27.741 1.00 14.99 C ANISOU 2765 CB ALA B 124 1918 1895 1885 -69 -1 19 C ATOM 2766 N ARG B 125 -17.859 10.830 -30.337 1.00 17.81 N ANISOU 2766 N ARG B 125 2277 2280 2209 2 14 22 N ATOM 2767 CA ARG B 125 -17.903 10.399 -31.731 1.00 18.52 C ANISOU 2767 CA ARG B 125 2411 2360 2267 -11 -7 -11 C ATOM 2768 C ARG B 125 -17.503 8.939 -31.895 1.00 19.08 C ANISOU 2768 C ARG B 125 2450 2409 2389 15 10 -20 C ATOM 2769 O ARG B 125 -18.170 8.183 -32.603 1.00 19.69 O ANISOU 2769 O ARG B 125 2527 2509 2447 -15 -13 -60 O ATOM 2770 CB ARG B 125 -16.983 11.267 -32.595 1.00 19.03 C ANISOU 2770 CB ARG B 125 2427 2459 2343 -34 14 4 C ATOM 2771 CG ARG B 125 -17.377 12.735 -32.634 1.00 20.44 C ANISOU 2771 CG ARG B 125 2611 2551 2603 26 -28 -6 C ATOM 2772 CD ARG B 125 -16.228 13.573 -33.182 1.00 21.31 C ANISOU 2772 CD ARG B 125 2694 2679 2725 -16 9 10 C ATOM 2773 NE ARG B 125 -16.512 14.999 -33.092 1.00 21.51 N ANISOU 2773 NE ARG B 125 2782 2681 2710 -34 -38 17 N ATOM 2774 CZ ARG B 125 -15.623 15.920 -32.729 1.00 20.38 C ANISOU 2774 CZ ARG B 125 2587 2614 2545 24 5 41 C ATOM 2775 NH1 ARG B 125 -14.382 15.577 -32.409 1.00 19.68 N ANISOU 2775 NH1 ARG B 125 2523 2508 2446 -17 25 24 N ATOM 2776 NH2 ARG B 125 -15.993 17.191 -32.685 1.00 20.74 N ANISOU 2776 NH2 ARG B 125 2643 2620 2619 4 -19 2 N ATOM 2777 N GLU B 126 -16.426 8.530 -31.238 1.00 19.19 N ANISOU 2777 N GLU B 126 2470 2419 2403 7 0 -8 N ATOM 2778 CA GLU B 126 -15.949 7.156 -31.290 1.00 19.27 C ANISOU 2778 CA GLU B 126 2499 2412 2413 -6 2 3 C ATOM 2779 C GLU B 126 -16.866 6.195 -30.547 1.00 19.11 C ANISOU 2779 C GLU B 126 2463 2400 2396 -2 -14 -6 C ATOM 2780 O GLU B 126 -17.020 5.048 -30.977 1.00 19.19 O ANISOU 2780 O GLU B 126 2494 2392 2404 -11 -3 -6 O ATOM 2781 CB GLU B 126 -14.513 7.072 -30.766 1.00 20.41 C ANISOU 2781 CB GLU B 126 2572 2608 2575 10 -58 -5 C ATOM 2782 CG GLU B 126 -13.510 7.832 -31.619 1.00 21.57 C ANISOU 2782 CG GLU B 126 2760 2707 2728 -23 37 27 C ATOM 2783 CD GLU B 126 -12.080 7.721 -31.135 1.00 22.75 C ANISOU 2783 CD GLU B 126 2843 2889 2913 -35 -19 -2 C ATOM 2784 OE1 GLU B 126 -11.708 6.669 -30.575 1.00 23.85 O ANISOU 2784 OE1 GLU B 126 3031 2990 3040 26 -42 41 O ATOM 2785 OE2 GLU B 126 -11.310 8.690 -31.317 1.00 21.77 O ANISOU 2785 OE2 GLU B 126 2734 2822 2715 17 -48 25 O ATOM 2786 N VAL B 127 -17.492 6.629 -29.458 1.00 18.87 N ANISOU 2786 N VAL B 127 2409 2386 2376 -4 -27 3 N ATOM 2787 CA VAL B 127 -18.531 5.843 -28.798 1.00 18.87 C ANISOU 2787 CA VAL B 127 2400 2397 2373 0 -24 -4 C ATOM 2788 C VAL B 127 -19.673 5.587 -29.782 1.00 19.12 C ANISOU 2788 C VAL B 127 2436 2417 2412 0 -46 -9 C ATOM 2789 O VAL B 127 -20.089 4.446 -29.987 1.00 18.99 O ANISOU 2789 O VAL B 127 2433 2414 2368 11 -66 -12 O ATOM 2790 CB VAL B 127 -19.066 6.523 -27.531 1.00 18.31 C ANISOU 2790 CB VAL B 127 2246 2359 2352 15 -46 11 C ATOM 2791 CG1 VAL B 127 -20.305 5.834 -26.975 1.00 18.64 C ANISOU 2791 CG1 VAL B 127 2361 2363 2357 -30 -11 24 C ATOM 2792 CG2 VAL B 127 -17.988 6.545 -26.446 1.00 18.12 C ANISOU 2792 CG2 VAL B 127 2314 2306 2265 -25 -51 -9 C ATOM 2793 N GLY B 128 -20.169 6.668 -30.377 1.00 19.15 N ANISOU 2793 N GLY B 128 2452 2412 2414 14 -24 -6 N ATOM 2794 CA GLY B 128 -21.255 6.562 -31.343 1.00 19.41 C ANISOU 2794 CA GLY B 128 2475 2448 2450 -10 -41 -1 C ATOM 2795 C GLY B 128 -22.619 6.578 -30.671 1.00 19.67 C ANISOU 2795 C GLY B 128 2513 2482 2477 -12 -13 -2 C ATOM 2796 O GLY B 128 -22.804 6.169 -29.525 1.00 19.50 O ANISOU 2796 O GLY B 128 2477 2498 2434 -22 -99 -1 O ATOM 2797 N GLU B 129 -23.629 7.006 -31.427 1.00 20.11 N ANISOU 2797 N GLU B 129 2576 2526 2538 -1 -51 2 N ATOM 2798 CA GLU B 129 -24.974 7.189 -30.912 1.00 20.91 C ANISOU 2798 CA GLU B 129 2664 2621 2661 -41 59 -28 C ATOM 2799 C GLU B 129 -25.581 5.923 -30.325 1.00 20.55 C ANISOU 2799 C GLU B 129 2604 2609 2595 -14 -8 -2 C ATOM 2800 O GLU B 129 -26.212 5.993 -29.269 1.00 20.25 O ANISOU 2800 O GLU B 129 2563 2568 2562 -16 -30 -17 O ATOM 2801 CB GLU B 129 -25.893 7.722 -32.021 1.00 24.19 C ANISOU 2801 CB GLU B 129 3161 3059 2971 40 -156 59 C ATOM 2802 CG GLU B 129 -27.317 7.987 -31.566 1.00 28.38 C ANISOU 2802 CG GLU B 129 3473 3635 3675 -13 100 -37 C ATOM 2803 CD GLU B 129 -28.225 8.465 -32.682 1.00 31.02 C ANISOU 2803 CD GLU B 129 3941 3922 3921 24 -89 44 C ATOM 2804 OE1 GLU B 129 -27.766 8.583 -33.836 1.00 31.94 O ANISOU 2804 OE1 GLU B 129 4082 4073 3980 0 -23 -6 O ATOM 2805 OE2 GLU B 129 -29.413 8.728 -32.393 1.00 31.78 O ANISOU 2805 OE2 GLU B 129 3998 4019 4059 3 -19 14 O ATOM 2806 N VAL B 130 -25.437 4.786 -30.997 1.00 20.78 N ANISOU 2806 N VAL B 130 2636 2625 2635 15 -24 -3 N ATOM 2807 CA VAL B 130 -26.079 3.554 -30.543 1.00 21.32 C ANISOU 2807 CA VAL B 130 2695 2694 2711 -15 -19 47 C ATOM 2808 C VAL B 130 -25.589 3.167 -29.154 1.00 21.18 C ANISOU 2808 C VAL B 130 2682 2681 2686 -12 -9 5 C ATOM 2809 O VAL B 130 -26.393 2.941 -28.248 1.00 21.11 O ANISOU 2809 O VAL B 130 2696 2682 2642 -51 -36 8 O ATOM 2810 CB VAL B 130 -25.851 2.397 -31.531 1.00 23.08 C ANISOU 2810 CB VAL B 130 2975 2875 2920 15 0 -69 C ATOM 2811 CG1 VAL B 130 -26.479 1.103 -31.033 1.00 23.86 C ANISOU 2811 CG1 VAL B 130 3056 2985 3026 -30 -15 0 C ATOM 2812 CG2 VAL B 130 -26.412 2.767 -32.898 1.00 23.98 C ANISOU 2812 CG2 VAL B 130 3070 3039 3001 -6 -29 -7 C ATOM 2813 N ARG B 131 -24.271 3.125 -28.975 1.00 21.10 N ANISOU 2813 N ARG B 131 2688 2646 2683 -2 -34 1 N ATOM 2814 CA ARG B 131 -23.711 2.762 -27.677 1.00 20.74 C ANISOU 2814 CA ARG B 131 2644 2604 2630 -7 -2 -14 C ATOM 2815 C ARG B 131 -24.008 3.831 -26.635 1.00 20.44 C ANISOU 2815 C ARG B 131 2606 2562 2597 -17 -22 4 C ATOM 2816 O ARG B 131 -24.392 3.509 -25.508 1.00 20.50 O ANISOU 2816 O ARG B 131 2600 2588 2601 -44 -13 -7 O ATOM 2817 CB ARG B 131 -22.214 2.471 -27.786 1.00 20.62 C ANISOU 2817 CB ARG B 131 2637 2615 2582 -1 32 6 C ATOM 2818 CG ARG B 131 -21.925 1.207 -28.585 1.00 21.25 C ANISOU 2818 CG ARG B 131 2731 2643 2699 -2 -9 -25 C ATOM 2819 CD ARG B 131 -20.478 0.774 -28.487 1.00 21.51 C ANISOU 2819 CD ARG B 131 2746 2724 2701 8 -14 -28 C ATOM 2820 NE ARG B 131 -19.557 1.683 -29.153 1.00 21.84 N ANISOU 2820 NE ARG B 131 2792 2781 2725 -4 -21 11 N ATOM 2821 CZ ARG B 131 -18.274 1.427 -29.376 1.00 22.00 C ANISOU 2821 CZ ARG B 131 2796 2786 2776 -10 -11 -11 C ATOM 2822 NH1 ARG B 131 -17.743 0.275 -28.984 1.00 22.40 N ANISOU 2822 NH1 ARG B 131 2862 2810 2839 0 -41 -5 N ATOM 2823 NH2 ARG B 131 -17.514 2.320 -29.996 1.00 21.79 N ANISOU 2823 NH2 ARG B 131 2809 2721 2749 -3 -22 -31 N ATOM 2824 N MET B 132 -23.903 5.103 -27.009 1.00 20.08 N ANISOU 2824 N MET B 132 2573 2531 2526 -4 -41 -8 N ATOM 2825 CA MET B 132 -24.227 6.190 -26.087 1.00 19.86 C ANISOU 2825 CA MET B 132 2577 2443 2527 1 -27 37 C ATOM 2826 C MET B 132 -25.655 6.092 -25.572 1.00 20.32 C ANISOU 2826 C MET B 132 2611 2528 2581 -3 -5 11 C ATOM 2827 O MET B 132 -25.913 6.248 -24.376 1.00 20.64 O ANISOU 2827 O MET B 132 2661 2597 2584 0 -22 27 O ATOM 2828 CB MET B 132 -23.993 7.547 -26.752 1.00 18.21 C ANISOU 2828 CB MET B 132 2350 2325 2246 12 -12 -72 C ATOM 2829 CG MET B 132 -24.070 8.729 -25.795 1.00 16.35 C ANISOU 2829 CG MET B 132 1999 2182 2031 -1 -104 12 C ATOM 2830 SD MET B 132 -22.621 8.833 -24.720 1.00 15.63 S ANISOU 2830 SD MET B 132 2094 1977 1867 -116 -147 53 S ATOM 2831 CE MET B 132 -21.372 9.376 -25.882 1.00 16.33 C ANISOU 2831 CE MET B 132 2092 2073 2041 -21 -23 13 C ATOM 2832 N GLN B 133 -26.616 5.835 -26.459 1.00 20.73 N ANISOU 2832 N GLN B 133 2640 2603 2636 2 -32 5 N ATOM 2833 CA GLN B 133 -27.999 5.628 -26.066 1.00 21.03 C ANISOU 2833 CA GLN B 133 2675 2645 2672 -16 5 8 C ATOM 2834 C GLN B 133 -28.146 4.445 -25.112 1.00 20.65 C ANISOU 2834 C GLN B 133 2605 2641 2599 -33 -35 -13 C ATOM 2835 O GLN B 133 -28.836 4.545 -24.098 1.00 20.32 O ANISOU 2835 O GLN B 133 2555 2594 2572 -52 -56 -4 O ATOM 2836 CB GLN B 133 -28.890 5.417 -27.297 1.00 22.28 C ANISOU 2836 CB GLN B 133 2879 2842 2744 -27 -62 -10 C ATOM 2837 CG GLN B 133 -30.377 5.461 -26.984 1.00 24.22 C ANISOU 2837 CG GLN B 133 3002 3124 3076 -11 -11 16 C ATOM 2838 CD GLN B 133 -30.883 6.861 -26.707 1.00 25.65 C ANISOU 2838 CD GLN B 133 3243 3193 3308 -2 -19 -7 C ATOM 2839 OE1 GLN B 133 -31.281 7.191 -25.590 1.00 26.63 O ANISOU 2839 OE1 GLN B 133 3352 3414 3353 -28 -4 -17 O ATOM 2840 NE2 GLN B 133 -30.870 7.699 -27.739 1.00 25.77 N ANISOU 2840 NE2 GLN B 133 3255 3204 3333 12 -29 9 N ATOM 2841 N LYS B 134 -27.503 3.332 -25.436 1.00 21.15 N ANISOU 2841 N LYS B 134 2669 2679 2689 -15 -54 -13 N ATOM 2842 CA LYS B 134 -27.542 2.132 -24.613 1.00 21.96 C ANISOU 2842 CA LYS B 134 2808 2783 2754 -60 -36 53 C ATOM 2843 C LYS B 134 -27.100 2.407 -23.181 1.00 21.71 C ANISOU 2843 C LYS B 134 2753 2751 2745 -36 -11 16 C ATOM 2844 O LYS B 134 -27.828 2.102 -22.235 1.00 21.40 O ANISOU 2844 O LYS B 134 2737 2718 2676 -12 -16 -32 O ATOM 2845 CB LYS B 134 -26.673 1.031 -25.230 1.00 24.82 C ANISOU 2845 CB LYS B 134 3133 3126 3171 76 35 -103 C ATOM 2846 CG LYS B 134 -26.650 -0.271 -24.448 1.00 27.21 C ANISOU 2846 CG LYS B 134 3524 3383 3433 -42 -18 67 C ATOM 2847 CD LYS B 134 -25.786 -1.330 -25.106 1.00 28.72 C ANISOU 2847 CD LYS B 134 3691 3591 3631 29 22 -22 C ATOM 2848 CE LYS B 134 -24.303 -1.018 -25.022 1.00 29.74 C ANISOU 2848 CE LYS B 134 3751 3765 3782 -2 -20 11 C ATOM 2849 NZ LYS B 134 -23.489 -1.992 -25.804 1.00 30.12 N ANISOU 2849 NZ LYS B 134 3846 3791 3806 15 -1 2 N ATOM 2850 N TYR B 135 -25.917 2.993 -23.010 1.00 21.51 N ANISOU 2850 N TYR B 135 2750 2714 2711 -26 -24 -5 N ATOM 2851 CA TYR B 135 -25.395 3.250 -21.673 1.00 20.83 C ANISOU 2851 CA TYR B 135 2649 2616 2649 12 13 -10 C ATOM 2852 C TYR B 135 -26.198 4.275 -20.895 1.00 19.82 C ANISOU 2852 C TYR B 135 2514 2494 2524 -24 -38 31 C ATOM 2853 O TYR B 135 -26.367 4.109 -19.682 1.00 19.38 O ANISOU 2853 O TYR B 135 2445 2420 2499 -46 -9 8 O ATOM 2854 CB TYR B 135 -23.918 3.657 -21.726 1.00 21.32 C ANISOU 2854 CB TYR B 135 2684 2705 2712 -27 1 -6 C ATOM 2855 CG TYR B 135 -23.019 2.469 -22.003 1.00 21.75 C ANISOU 2855 CG TYR B 135 2726 2744 2793 -15 -12 -13 C ATOM 2856 CD1 TYR B 135 -22.696 1.562 -21.004 1.00 22.20 C ANISOU 2856 CD1 TYR B 135 2813 2808 2814 -30 -30 9 C ATOM 2857 CD2 TYR B 135 -22.506 2.257 -23.273 1.00 22.16 C ANISOU 2857 CD2 TYR B 135 2797 2824 2800 -30 -13 -15 C ATOM 2858 CE1 TYR B 135 -21.881 0.474 -21.264 1.00 22.93 C ANISOU 2858 CE1 TYR B 135 2890 2885 2938 2 -22 7 C ATOM 2859 CE2 TYR B 135 -21.690 1.176 -23.541 1.00 23.04 C ANISOU 2859 CE2 TYR B 135 2905 2909 2939 7 3 -25 C ATOM 2860 CZ TYR B 135 -21.381 0.288 -22.534 1.00 23.57 C ANISOU 2860 CZ TYR B 135 2998 2989 2970 -9 -17 2 C ATOM 2861 OH TYR B 135 -20.568 -0.787 -22.813 1.00 24.80 O ANISOU 2861 OH TYR B 135 3145 3084 3193 34 -23 -31 O ATOM 2862 N LEU B 136 -26.722 5.313 -21.546 1.00 19.14 N ANISOU 2862 N LEU B 136 2415 2397 2462 -43 -27 -23 N ATOM 2863 CA LEU B 136 -27.557 6.277 -20.834 1.00 19.07 C ANISOU 2863 CA LEU B 136 2415 2382 2450 -9 -27 17 C ATOM 2864 C LEU B 136 -28.869 5.673 -20.357 1.00 19.08 C ANISOU 2864 C LEU B 136 2418 2406 2426 6 -11 26 C ATOM 2865 O LEU B 136 -29.379 6.081 -19.309 1.00 18.83 O ANISOU 2865 O LEU B 136 2381 2352 2424 -14 -33 18 O ATOM 2866 CB LEU B 136 -27.780 7.533 -21.677 1.00 18.81 C ANISOU 2866 CB LEU B 136 2389 2411 2349 -11 -15 24 C ATOM 2867 CG LEU B 136 -26.546 8.391 -21.971 1.00 18.91 C ANISOU 2867 CG LEU B 136 2415 2397 2373 -23 -5 -6 C ATOM 2868 CD1 LEU B 136 -26.966 9.735 -22.548 1.00 19.35 C ANISOU 2868 CD1 LEU B 136 2500 2439 2414 -10 -14 14 C ATOM 2869 CD2 LEU B 136 -25.682 8.607 -20.735 1.00 19.23 C ANISOU 2869 CD2 LEU B 136 2436 2456 2416 -27 -36 26 C ATOM 2870 N LYS B 137 -29.429 4.708 -21.085 1.00 19.62 N ANISOU 2870 N LYS B 137 2502 2453 2501 -4 -31 8 N ATOM 2871 CA LYS B 137 -30.557 3.938 -20.571 1.00 20.26 C ANISOU 2871 CA LYS B 137 2543 2555 2600 6 16 71 C ATOM 2872 C LYS B 137 -30.136 3.127 -19.348 1.00 19.98 C ANISOU 2872 C LYS B 137 2536 2506 2550 -18 -2 14 C ATOM 2873 O LYS B 137 -30.802 3.171 -18.315 1.00 19.94 O ANISOU 2873 O LYS B 137 2524 2531 2522 -45 -31 35 O ATOM 2874 CB LYS B 137 -31.149 3.018 -21.638 1.00 23.11 C ANISOU 2874 CB LYS B 137 3024 2903 2855 27 -109 -112 C ATOM 2875 CG LYS B 137 -32.245 2.104 -21.114 1.00 27.01 C ANISOU 2875 CG LYS B 137 3387 3363 3512 -40 118 107 C ATOM 2876 CD LYS B 137 -32.988 1.386 -22.227 1.00 31.07 C ANISOU 2876 CD LYS B 137 3997 3947 3862 -110 -27 -101 C ATOM 2877 CE LYS B 137 -34.035 2.289 -22.861 1.00 34.13 C ANISOU 2877 CE LYS B 137 4331 4276 4362 81 2 57 C ATOM 2878 NZ LYS B 137 -34.938 1.546 -23.782 1.00 35.69 N ANISOU 2878 NZ LYS B 137 4518 4527 4516 -21 -18 -12 N ATOM 2879 N LYS B 138 -29.011 2.427 -19.452 1.00 19.98 N ANISOU 2879 N LYS B 138 2564 2485 2541 -19 -43 -3 N ATOM 2880 CA LYS B 138 -28.505 1.627 -18.342 1.00 20.30 C ANISOU 2880 CA LYS B 138 2668 2526 2518 -64 -58 7 C ATOM 2881 C LYS B 138 -28.240 2.469 -17.103 1.00 19.43 C ANISOU 2881 C LYS B 138 2502 2409 2470 -36 -19 24 C ATOM 2882 O LYS B 138 -28.548 2.049 -15.982 1.00 19.34 O ANISOU 2882 O LYS B 138 2467 2386 2496 -46 -19 38 O ATOM 2883 CB LYS B 138 -27.240 0.871 -18.754 1.00 24.19 C ANISOU 2883 CB LYS B 138 2887 3141 3162 110 70 65 C ATOM 2884 CG LYS B 138 -27.510 -0.258 -19.738 1.00 29.08 C ANISOU 2884 CG LYS B 138 3844 3609 3597 -118 -35 -94 C ATOM 2885 CD LYS B 138 -26.306 -1.174 -19.881 1.00 33.39 C ANISOU 2885 CD LYS B 138 4147 4246 4292 114 17 39 C ATOM 2886 CE LYS B 138 -26.692 -2.455 -20.606 1.00 36.05 C ANISOU 2886 CE LYS B 138 4637 4506 4554 -51 -14 -47 C ATOM 2887 NZ LYS B 138 -25.583 -3.449 -20.592 1.00 36.99 N ANISOU 2887 NZ LYS B 138 4694 4661 4700 10 0 -4 N ATOM 2888 N PHE B 139 -27.704 3.677 -17.280 1.00 18.54 N ANISOU 2888 N PHE B 139 2371 2362 2313 -14 -24 14 N ATOM 2889 CA PHE B 139 -27.433 4.563 -16.160 1.00 17.83 C ANISOU 2889 CA PHE B 139 2234 2253 2286 -18 0 31 C ATOM 2890 C PHE B 139 -28.638 5.364 -15.691 1.00 17.58 C ANISOU 2890 C PHE B 139 2208 2243 2227 -31 -16 22 C ATOM 2891 O PHE B 139 -28.528 6.132 -14.726 1.00 17.76 O ANISOU 2891 O PHE B 139 2206 2242 2301 -60 -61 -9 O ATOM 2892 CB PHE B 139 -26.311 5.552 -16.495 1.00 17.24 C ANISOU 2892 CB PHE B 139 2207 2183 2159 3 15 1 C ATOM 2893 CG PHE B 139 -24.999 4.996 -16.947 1.00 17.02 C ANISOU 2893 CG PHE B 139 2160 2162 2145 -25 -12 4 C ATOM 2894 CD1 PHE B 139 -24.621 3.681 -16.742 1.00 17.23 C ANISOU 2894 CD1 PHE B 139 2202 2178 2168 -26 -24 -5 C ATOM 2895 CD2 PHE B 139 -24.106 5.833 -17.606 1.00 16.95 C ANISOU 2895 CD2 PHE B 139 2196 2173 2071 -20 -9 25 C ATOM 2896 CE1 PHE B 139 -23.405 3.205 -17.175 1.00 17.71 C ANISOU 2896 CE1 PHE B 139 2265 2199 2263 18 -5 -15 C ATOM 2897 CE2 PHE B 139 -22.881 5.368 -18.042 1.00 17.63 C ANISOU 2897 CE2 PHE B 139 2226 2261 2212 4 -27 -21 C ATOM 2898 CZ PHE B 139 -22.528 4.051 -17.828 1.00 18.26 C ANISOU 2898 CZ PHE B 139 2344 2290 2304 -25 -10 20 C ATOM 2899 N SER B 140 -29.774 5.263 -16.370 1.00 17.10 N ANISOU 2899 N SER B 140 2181 2125 2190 -28 -17 49 N ATOM 2900 CA SER B 140 -30.930 6.105 -16.100 1.00 17.18 C ANISOU 2900 CA SER B 140 2189 2112 2228 -24 -48 -23 C ATOM 2901 C SER B 140 -30.534 7.579 -16.048 1.00 16.18 C ANISOU 2901 C SER B 140 2027 2061 2059 17 -43 -6 C ATOM 2902 O SER B 140 -30.869 8.299 -15.110 1.00 15.40 O ANISOU 2902 O SER B 140 1899 1917 2036 -26 -95 3 O ATOM 2903 CB SER B 140 -31.642 5.677 -14.816 1.00 19.80 C ANISOU 2903 CB SER B 140 2537 2588 2399 -37 47 48 C ATOM 2904 OG SER B 140 -32.119 4.345 -14.939 1.00 21.71 O ANISOU 2904 OG SER B 140 2779 2673 2796 -38 -11 1 O ATOM 2905 N TYR B 141 -29.866 8.034 -17.105 1.00 16.28 N ANISOU 2905 N TYR B 141 2034 2080 2070 -13 -48 8 N ATOM 2906 CA TYR B 141 -29.272 9.367 -17.099 1.00 16.64 C ANISOU 2906 CA TYR B 141 2106 2092 2122 -29 -15 5 C ATOM 2907 C TYR B 141 -30.213 10.406 -17.694 1.00 16.90 C ANISOU 2907 C TYR B 141 2124 2144 2153 -14 -25 13 C ATOM 2908 O TYR B 141 -30.304 10.543 -18.912 1.00 17.17 O ANISOU 2908 O TYR B 141 2142 2226 2155 -6 -2 -2 O ATOM 2909 CB TYR B 141 -27.937 9.347 -17.855 1.00 16.60 C ANISOU 2909 CB TYR B 141 2111 2079 2116 -19 -12 10 C ATOM 2910 CG TYR B 141 -27.128 10.597 -17.563 1.00 16.56 C ANISOU 2910 CG TYR B 141 2126 2073 2092 -26 -24 11 C ATOM 2911 CD1 TYR B 141 -26.278 10.658 -16.468 1.00 16.54 C ANISOU 2911 CD1 TYR B 141 2113 2080 2093 -23 -18 21 C ATOM 2912 CD2 TYR B 141 -27.241 11.714 -18.377 1.00 16.21 C ANISOU 2912 CD2 TYR B 141 2073 2044 2043 -26 -30 -11 C ATOM 2913 CE1 TYR B 141 -25.549 11.803 -16.200 1.00 16.14 C ANISOU 2913 CE1 TYR B 141 2077 2029 2028 4 -7 11 C ATOM 2914 CE2 TYR B 141 -26.522 12.863 -18.112 1.00 16.01 C ANISOU 2914 CE2 TYR B 141 2034 2015 2034 -12 -21 7 C ATOM 2915 CZ TYR B 141 -25.672 12.898 -17.026 1.00 16.19 C ANISOU 2915 CZ TYR B 141 2082 2039 2030 -7 -30 21 C ATOM 2916 OH TYR B 141 -24.960 14.047 -16.772 1.00 16.21 O ANISOU 2916 OH TYR B 141 2057 2079 2022 -28 -81 37 O ATOM 2917 N GLY B 142 -30.917 11.130 -16.834 1.00 17.30 N ANISOU 2917 N GLY B 142 2189 2195 2191 -8 -5 -1 N ATOM 2918 CA GLY B 142 -31.763 12.242 -17.243 1.00 17.61 C ANISOU 2918 CA GLY B 142 2232 2213 2248 -2 -13 15 C ATOM 2919 C GLY B 142 -32.899 11.789 -18.148 1.00 18.22 C ANISOU 2919 C GLY B 142 2324 2290 2309 -31 -47 12 C ATOM 2920 O GLY B 142 -33.479 10.715 -17.988 1.00 18.05 O ANISOU 2920 O GLY B 142 2292 2311 2254 -55 -72 22 O ATOM 2921 N ASN B 143 -33.186 12.595 -19.170 1.00 18.46 N ANISOU 2921 N ASN B 143 2372 2305 2337 -17 -36 26 N ATOM 2922 CA ASN B 143 -34.260 12.268 -20.106 1.00 18.81 C ANISOU 2922 CA ASN B 143 2401 2354 2390 -28 -52 24 C ATOM 2923 C ASN B 143 -33.775 11.312 -21.181 1.00 19.31 C ANISOU 2923 C ASN B 143 2485 2422 2429 -27 -11 13 C ATOM 2924 O ASN B 143 -34.529 10.860 -22.046 1.00 19.35 O ANISOU 2924 O ASN B 143 2467 2444 2439 -54 -32 47 O ATOM 2925 CB ASN B 143 -34.849 13.542 -20.707 1.00 18.38 C ANISOU 2925 CB ASN B 143 2315 2352 2315 -1 -34 -15 C ATOM 2926 CG ASN B 143 -33.893 14.335 -21.566 1.00 18.85 C ANISOU 2926 CG ASN B 143 2345 2361 2457 -12 -8 6 C ATOM 2927 OD1 ASN B 143 -32.724 13.983 -21.728 1.00 18.23 O ANISOU 2927 OD1 ASN B 143 2338 2252 2336 27 -8 4 O ATOM 2928 ND2 ASN B 143 -34.391 15.432 -22.138 1.00 18.97 N ANISOU 2928 ND2 ASN B 143 2385 2409 2414 0 -49 17 N ATOM 2929 N GLN B 144 -32.473 11.036 -21.218 1.00 19.98 N ANISOU 2929 N GLN B 144 2519 2542 2529 -14 -26 24 N ATOM 2930 CA GLN B 144 -31.861 10.063 -22.100 1.00 20.84 C ANISOU 2930 CA GLN B 144 2622 2635 2660 24 12 -11 C ATOM 2931 C GLN B 144 -32.011 10.461 -23.566 1.00 21.60 C ANISOU 2931 C GLN B 144 2747 2751 2708 6 -20 21 C ATOM 2932 O GLN B 144 -32.039 9.614 -24.454 1.00 22.31 O ANISOU 2932 O GLN B 144 2885 2837 2756 -11 -22 -13 O ATOM 2933 CB GLN B 144 -32.446 8.668 -21.867 1.00 21.42 C ANISOU 2933 CB GLN B 144 2702 2678 2759 -13 -31 14 C ATOM 2934 CG GLN B 144 -32.165 8.096 -20.488 1.00 21.92 C ANISOU 2934 CG GLN B 144 2812 2773 2744 20 -6 -3 C ATOM 2935 CD GLN B 144 -32.847 6.761 -20.264 1.00 22.67 C ANISOU 2935 CD GLN B 144 2842 2854 2917 -9 -4 25 C ATOM 2936 OE1 GLN B 144 -32.951 5.952 -21.187 1.00 23.51 O ANISOU 2936 OE1 GLN B 144 3046 2899 2989 -23 -26 5 O ATOM 2937 NE2 GLN B 144 -33.313 6.530 -19.044 1.00 22.69 N ANISOU 2937 NE2 GLN B 144 2854 2876 2891 -19 -38 15 N ATOM 2938 N ASN B 145 -32.080 11.762 -23.813 1.00 21.78 N ANISOU 2938 N ASN B 145 2761 2760 2755 -23 -28 22 N ATOM 2939 CA ASN B 145 -32.327 12.289 -25.150 1.00 21.83 C ANISOU 2939 CA ASN B 145 2784 2760 2751 -18 -23 14 C ATOM 2940 C ASN B 145 -31.018 12.870 -25.670 1.00 21.74 C ANISOU 2940 C ASN B 145 2767 2747 2746 6 -21 11 C ATOM 2941 O ASN B 145 -30.588 13.922 -25.201 1.00 22.16 O ANISOU 2941 O ASN B 145 2797 2791 2832 -23 -48 0 O ATOM 2942 CB ASN B 145 -33.433 13.335 -25.106 1.00 22.48 C ANISOU 2942 CB ASN B 145 2851 2799 2889 6 2 -25 C ATOM 2943 CG ASN B 145 -33.928 13.806 -26.455 1.00 23.75 C ANISOU 2943 CG ASN B 145 3076 3023 2923 -24 15 4 C ATOM 2944 OD1 ASN B 145 -35.029 14.362 -26.558 1.00 25.79 O ANISOU 2944 OD1 ASN B 145 3219 3270 3312 40 -48 10 O ATOM 2945 ND2 ASN B 145 -33.148 13.609 -27.506 1.00 22.31 N ANISOU 2945 ND2 ASN B 145 2853 2803 2822 -28 -71 -9 N ATOM 2946 N ILE B 146 -30.387 12.172 -26.608 1.00 21.63 N ANISOU 2946 N ILE B 146 2757 2743 2717 0 -39 1 N ATOM 2947 CA ILE B 146 -29.077 12.602 -27.091 1.00 22.16 C ANISOU 2947 CA ILE B 146 2817 2818 2782 -25 7 -5 C ATOM 2948 C ILE B 146 -29.180 13.228 -28.477 1.00 22.36 C ANISOU 2948 C ILE B 146 2857 2839 2801 -14 -3 2 C ATOM 2949 O ILE B 146 -28.179 13.362 -29.180 1.00 22.12 O ANISOU 2949 O ILE B 146 2846 2821 2738 -6 -29 7 O ATOM 2950 CB ILE B 146 -28.054 11.456 -27.075 1.00 23.11 C ANISOU 2950 CB ILE B 146 2900 2931 2952 39 -1 23 C ATOM 2951 CG1 ILE B 146 -28.482 10.315 -28.002 1.00 24.44 C ANISOU 2951 CG1 ILE B 146 3153 3000 3132 -16 -4 -25 C ATOM 2952 CG2 ILE B 146 -27.869 10.938 -25.653 1.00 23.25 C ANISOU 2952 CG2 ILE B 146 2943 2941 2949 -30 -12 7 C ATOM 2953 CD1 ILE B 146 -27.396 9.281 -28.229 1.00 24.51 C ANISOU 2953 CD1 ILE B 146 3091 3104 3119 -1 -10 -9 C ATOM 2954 N SER B 147 -30.388 13.626 -28.863 1.00 22.96 N ANISOU 2954 N SER B 147 2902 2897 2924 4 -24 -13 N ATOM 2955 CA SER B 147 -30.597 14.406 -30.074 1.00 23.74 C ANISOU 2955 CA SER B 147 3075 2980 2965 -1 -7 11 C ATOM 2956 C SER B 147 -29.883 15.752 -29.972 1.00 23.88 C ANISOU 2956 C SER B 147 3062 2995 3015 0 -7 8 C ATOM 2957 O SER B 147 -29.796 16.328 -28.886 1.00 23.94 O ANISOU 2957 O SER B 147 3060 3000 3036 35 -35 -7 O ATOM 2958 CB SER B 147 -32.087 14.668 -30.308 1.00 25.85 C ANISOU 2958 CB SER B 147 3193 3337 3292 73 -34 13 C ATOM 2959 OG SER B 147 -32.840 13.475 -30.245 1.00 28.04 O ANISOU 2959 OG SER B 147 3522 3528 3603 -52 -30 15 O ATOM 2960 N GLY B 148 -29.400 16.245 -31.106 1.00 23.88 N ANISOU 2960 N GLY B 148 3052 2995 3026 -14 -15 9 N ATOM 2961 CA GLY B 148 -28.743 17.550 -31.126 1.00 23.54 C ANISOU 2961 CA GLY B 148 2998 2967 2980 13 0 13 C ATOM 2962 C GLY B 148 -27.330 17.436 -31.680 1.00 23.18 C ANISOU 2962 C GLY B 148 2966 2900 2940 24 -20 1 C ATOM 2963 O GLY B 148 -26.663 18.450 -31.876 1.00 23.64 O ANISOU 2963 O GLY B 148 3035 2940 3007 -3 -25 25 O ATOM 2964 N GLY B 149 -26.876 16.214 -31.932 1.00 22.32 N ANISOU 2964 N GLY B 149 2816 2862 2803 10 -16 16 N ATOM 2965 CA GLY B 149 -25.553 15.992 -32.504 1.00 21.38 C ANISOU 2965 CA GLY B 149 2751 2698 2676 7 -43 34 C ATOM 2966 C GLY B 149 -24.667 15.241 -31.514 1.00 20.66 C ANISOU 2966 C GLY B 149 2638 2594 2619 9 3 -2 C ATOM 2967 O GLY B 149 -24.649 15.560 -30.326 1.00 20.50 O ANISOU 2967 O GLY B 149 2614 2581 2591 24 -35 48 O ATOM 2968 N ILE B 150 -23.895 14.278 -32.002 1.00 20.18 N ANISOU 2968 N ILE B 150 2571 2559 2539 2 -30 22 N ATOM 2969 CA ILE B 150 -23.155 13.361 -31.141 1.00 19.80 C ANISOU 2969 CA ILE B 150 2524 2481 2519 -18 -23 -2 C ATOM 2970 C ILE B 150 -22.067 14.056 -30.336 1.00 19.42 C ANISOU 2970 C ILE B 150 2501 2427 2453 -10 -7 14 C ATOM 2971 O ILE B 150 -21.712 13.606 -29.244 1.00 19.34 O ANISOU 2971 O ILE B 150 2511 2386 2453 -2 -21 1 O ATOM 2972 CB ILE B 150 -22.562 12.202 -31.965 1.00 20.06 C ANISOU 2972 CB ILE B 150 2555 2558 2509 8 14 -15 C ATOM 2973 CG1 ILE B 150 -21.994 11.099 -31.070 1.00 20.77 C ANISOU 2973 CG1 ILE B 150 2667 2596 2629 5 -18 21 C ATOM 2974 CG2 ILE B 150 -21.485 12.699 -32.920 1.00 19.92 C ANISOU 2974 CG2 ILE B 150 2469 2507 2594 -12 -7 -18 C ATOM 2975 CD1 ILE B 150 -23.021 10.383 -30.222 1.00 21.14 C ANISOU 2975 CD1 ILE B 150 2695 2672 2667 -1 12 19 C ATOM 2976 N ASP B 151 -21.529 15.158 -30.849 1.00 19.11 N ANISOU 2976 N ASP B 151 2431 2404 2427 -18 -28 -9 N ATOM 2977 CA ASP B 151 -20.470 15.890 -30.172 1.00 18.71 C ANISOU 2977 CA ASP B 151 2390 2358 2359 -12 11 0 C ATOM 2978 C ASP B 151 -20.960 17.169 -29.508 1.00 18.34 C ANISOU 2978 C ASP B 151 2335 2334 2298 -15 2 22 C ATOM 2979 O ASP B 151 -20.124 18.003 -29.143 1.00 18.60 O ANISOU 2979 O ASP B 151 2408 2388 2273 -59 -23 20 O ATOM 2980 CB ASP B 151 -19.337 16.185 -31.158 1.00 18.07 C ANISOU 2980 CB ASP B 151 2363 2245 2259 -17 -31 -6 C ATOM 2981 CG ASP B 151 -19.750 17.038 -32.340 1.00 17.63 C ANISOU 2981 CG ASP B 151 2262 2212 2225 -15 -24 -25 C ATOM 2982 OD1 ASP B 151 -20.896 17.528 -32.385 1.00 17.85 O ANISOU 2982 OD1 ASP B 151 2297 2357 2130 25 -36 49 O ATOM 2983 OD2 ASP B 151 -18.910 17.232 -33.245 1.00 18.11 O ANISOU 2983 OD2 ASP B 151 2289 2426 2164 -20 -76 9 O ATOM 2984 N LYS B 152 -22.266 17.331 -29.304 1.00 18.12 N ANISOU 2984 N LYS B 152 2314 2309 2262 -4 -9 22 N ATOM 2985 CA LYS B 152 -22.771 18.529 -28.651 1.00 18.13 C ANISOU 2985 CA LYS B 152 2260 2354 2275 -34 4 -56 C ATOM 2986 C LYS B 152 -24.064 18.338 -27.879 1.00 17.11 C ANISOU 2986 C LYS B 152 2221 2152 2127 -6 -37 -2 C ATOM 2987 O LYS B 152 -24.602 19.328 -27.365 1.00 16.81 O ANISOU 2987 O LYS B 152 2236 2134 2019 -24 -39 16 O ATOM 2988 CB LYS B 152 -22.950 19.647 -29.699 1.00 22.04 C ANISOU 2988 CB LYS B 152 3018 2574 2783 39 66 142 C ATOM 2989 CG LYS B 152 -24.226 19.514 -30.503 1.00 27.77 C ANISOU 2989 CG LYS B 152 3362 3658 3531 -52 -85 -89 C ATOM 2990 CD LYS B 152 -24.537 20.705 -31.385 1.00 32.00 C ANISOU 2990 CD LYS B 152 4073 3891 4195 30 -27 119 C ATOM 2991 CE LYS B 152 -24.478 20.346 -32.860 1.00 36.20 C ANISOU 2991 CE LYS B 152 4663 4603 4490 -42 48 -65 C ATOM 2992 NZ LYS B 152 -25.259 21.312 -33.684 1.00 38.35 N ANISOU 2992 NZ LYS B 152 4862 4840 4867 36 -28 36 N ATOM 2993 N PHE B 153 -24.589 17.120 -27.727 1.00 16.65 N ANISOU 2993 N PHE B 153 2152 2143 2032 -10 -14 24 N ATOM 2994 CA PHE B 153 -25.948 16.965 -27.205 1.00 16.85 C ANISOU 2994 CA PHE B 153 2151 2146 2107 2 -18 23 C ATOM 2995 C PHE B 153 -26.075 17.351 -25.739 1.00 16.93 C ANISOU 2995 C PHE B 153 2145 2162 2125 16 0 11 C ATOM 2996 O PHE B 153 -27.135 17.782 -25.277 1.00 16.56 O ANISOU 2996 O PHE B 153 2116 2119 2057 -4 -8 27 O ATOM 2997 CB PHE B 153 -26.484 15.557 -27.452 1.00 17.37 C ANISOU 2997 CB PHE B 153 2238 2154 2208 11 -12 14 C ATOM 2998 CG PHE B 153 -25.699 14.454 -26.801 1.00 16.92 C ANISOU 2998 CG PHE B 153 2174 2115 2142 6 -4 -6 C ATOM 2999 CD1 PHE B 153 -25.902 14.132 -25.467 1.00 17.07 C ANISOU 2999 CD1 PHE B 153 2187 2133 2168 -5 -3 9 C ATOM 3000 CD2 PHE B 153 -24.760 13.741 -27.524 1.00 16.87 C ANISOU 3000 CD2 PHE B 153 2137 2167 2104 0 -15 -2 C ATOM 3001 CE1 PHE B 153 -25.173 13.122 -24.870 1.00 16.89 C ANISOU 3001 CE1 PHE B 153 2143 2145 2130 -28 -11 28 C ATOM 3002 CE2 PHE B 153 -24.033 12.724 -26.933 1.00 17.12 C ANISOU 3002 CE2 PHE B 153 2174 2155 2177 8 -15 -10 C ATOM 3003 CZ PHE B 153 -24.243 12.416 -25.604 1.00 17.41 C ANISOU 3003 CZ PHE B 153 2190 2217 2208 -6 2 7 C ATOM 3004 N TRP B 154 -24.997 17.240 -24.971 1.00 17.05 N ANISOU 3004 N TRP B 154 2175 2159 2145 -6 -27 14 N ATOM 3005 CA TRP B 154 -24.937 17.662 -23.586 1.00 17.21 C ANISOU 3005 CA TRP B 154 2200 2189 2149 18 -26 15 C ATOM 3006 C TRP B 154 -24.867 19.167 -23.366 1.00 17.66 C ANISOU 3006 C TRP B 154 2256 2224 2230 16 -19 -7 C ATOM 3007 O TRP B 154 -25.011 19.629 -22.227 1.00 17.37 O ANISOU 3007 O TRP B 154 2217 2209 2173 2 -53 40 O ATOM 3008 CB TRP B 154 -23.676 17.041 -22.948 1.00 17.10 C ANISOU 3008 CB TRP B 154 2160 2179 2156 24 10 -1 C ATOM 3009 CG TRP B 154 -22.444 17.314 -23.759 1.00 16.59 C ANISOU 3009 CG TRP B 154 2122 2087 2093 70 -9 -10 C ATOM 3010 CD1 TRP B 154 -21.725 18.474 -23.800 1.00 18.68 C ANISOU 3010 CD1 TRP B 154 2355 2306 2438 -61 2 -10 C ATOM 3011 CD2 TRP B 154 -21.786 16.407 -24.647 1.00 15.08 C ANISOU 3011 CD2 TRP B 154 1955 1968 1805 11 -107 37 C ATOM 3012 NE1 TRP B 154 -20.662 18.346 -24.659 1.00 18.51 N ANISOU 3012 NE1 TRP B 154 2387 2260 2388 24 -6 -1 N ATOM 3013 CE2 TRP B 154 -20.676 17.082 -25.192 1.00 16.83 C ANISOU 3013 CE2 TRP B 154 2111 2186 2098 -61 -25 31 C ATOM 3014 CE3 TRP B 154 -22.026 15.084 -25.033 1.00 15.96 C ANISOU 3014 CE3 TRP B 154 2065 2015 1983 -12 -38 16 C ATOM 3015 CZ2 TRP B 154 -19.807 16.480 -26.096 1.00 17.44 C ANISOU 3015 CZ2 TRP B 154 2218 2187 2222 4 5 7 C ATOM 3016 CZ3 TRP B 154 -21.165 14.490 -25.936 1.00 17.03 C ANISOU 3016 CZ3 TRP B 154 2143 2155 2172 32 16 -31 C ATOM 3017 CH2 TRP B 154 -20.068 15.187 -26.460 1.00 17.52 C ANISOU 3017 CH2 TRP B 154 2207 2192 2259 -27 -18 18 C ATOM 3018 N LEU B 155 -24.617 19.941 -24.420 1.00 18.37 N ANISOU 3018 N LEU B 155 2370 2360 2248 -6 -12 26 N ATOM 3019 CA LEU B 155 -24.373 21.370 -24.277 1.00 19.66 C ANISOU 3019 CA LEU B 155 2596 2418 2456 9 -26 -4 C ATOM 3020 C LEU B 155 -25.383 22.188 -25.070 1.00 20.20 C ANISOU 3020 C LEU B 155 2617 2496 2563 23 -21 24 C ATOM 3021 O LEU B 155 -25.832 23.240 -24.611 1.00 20.44 O ANISOU 3021 O LEU B 155 2643 2534 2588 43 0 21 O ATOM 3022 CB LEU B 155 -22.942 21.679 -24.707 1.00 22.64 C ANISOU 3022 CB LEU B 155 2739 2995 2870 26 73 58 C ATOM 3023 CG LEU B 155 -22.239 22.915 -24.156 1.00 26.27 C ANISOU 3023 CG LEU B 155 3336 3241 3405 -94 -8 -67 C ATOM 3024 CD1 LEU B 155 -22.826 24.185 -24.755 1.00 27.59 C ANISOU 3024 CD1 LEU B 155 3518 3454 3509 27 -11 22 C ATOM 3025 CD2 LEU B 155 -22.293 22.977 -22.637 1.00 27.46 C ANISOU 3025 CD2 LEU B 155 3484 3477 3473 -17 3 -4 C ATOM 3026 N GLU B 156 -25.749 21.705 -26.250 1.00 20.78 N ANISOU 3026 N GLU B 156 2686 2594 2615 16 -36 -7 N ATOM 3027 CA GLU B 156 -26.644 22.435 -27.139 1.00 21.24 C ANISOU 3027 CA GLU B 156 2690 2633 2747 29 -96 -23 C ATOM 3028 C GLU B 156 -27.833 21.592 -27.578 1.00 20.95 C ANISOU 3028 C GLU B 156 2670 2584 2705 4 -38 25 C ATOM 3029 O GLU B 156 -28.756 22.114 -28.210 1.00 21.66 O ANISOU 3029 O GLU B 156 2693 2735 2803 8 -78 43 O ATOM 3030 CB GLU B 156 -25.875 22.942 -28.364 1.00 25.19 C ANISOU 3030 CB GLU B 156 3237 3323 3011 55 97 102 C ATOM 3031 CG GLU B 156 -25.027 24.174 -28.096 1.00 30.20 C ANISOU 3031 CG GLU B 156 3810 3689 3976 -64 -122 -70 C ATOM 3032 CD GLU B 156 -24.229 24.634 -29.297 1.00 34.52 C ANISOU 3032 CD GLU B 156 4400 4398 4319 11 107 82 C ATOM 3033 OE1 GLU B 156 -24.535 24.199 -30.425 1.00 35.41 O ANISOU 3033 OE1 GLU B 156 4541 4462 4450 -14 -6 12 O ATOM 3034 OE2 GLU B 156 -23.290 25.436 -29.111 1.00 36.14 O ANISOU 3034 OE2 GLU B 156 4587 4515 4631 -32 -6 2 O ATOM 3035 N GLY B 157 -27.824 20.305 -27.248 1.00 19.74 N ANISOU 3035 N GLY B 157 2476 2527 2498 -31 -36 2 N ATOM 3036 CA GLY B 157 -28.874 19.397 -27.679 1.00 18.86 C ANISOU 3036 CA GLY B 157 2421 2393 2352 19 -8 17 C ATOM 3037 C GLY B 157 -30.012 19.265 -26.681 1.00 18.36 C ANISOU 3037 C GLY B 157 2369 2293 2314 17 -34 11 C ATOM 3038 O GLY B 157 -30.336 20.181 -25.923 1.00 18.16 O ANISOU 3038 O GLY B 157 2377 2309 2216 29 -45 30 O ATOM 3039 N GLN B 158 -30.630 18.081 -26.664 1.00 18.07 N ANISOU 3039 N GLN B 158 2327 2295 2242 13 -39 19 N ATOM 3040 CA GLN B 158 -31.880 17.872 -25.957 1.00 18.54 C ANISOU 3040 CA GLN B 158 2397 2347 2298 46 35 66 C ATOM 3041 C GLN B 158 -31.705 17.105 -24.651 1.00 17.70 C ANISOU 3041 C GLN B 158 2241 2240 2245 22 -11 18 C ATOM 3042 O GLN B 158 -32.703 16.826 -23.987 1.00 17.83 O ANISOU 3042 O GLN B 158 2264 2303 2207 -8 -38 41 O ATOM 3043 CB GLN B 158 -32.874 17.137 -26.865 1.00 21.96 C ANISOU 3043 CB GLN B 158 2726 2773 2843 -118 -76 -117 C ATOM 3044 CG GLN B 158 -33.203 17.875 -28.154 1.00 25.72 C ANISOU 3044 CG GLN B 158 3286 3376 3112 -12 -61 81 C ATOM 3045 CD GLN B 158 -33.694 19.288 -27.908 1.00 29.15 C ANISOU 3045 CD GLN B 158 3732 3598 3744 53 -49 -34 C ATOM 3046 OE1 GLN B 158 -34.627 19.503 -27.133 1.00 30.05 O ANISOU 3046 OE1 GLN B 158 3831 3821 3767 8 -1 -11 O ATOM 3047 NE2 GLN B 158 -33.060 20.259 -28.555 1.00 30.09 N ANISOU 3047 NE2 GLN B 158 3833 3783 3818 -14 -8 25 N ATOM 3048 N LEU B 159 -30.461 16.801 -24.291 1.00 16.98 N ANISOU 3048 N LEU B 159 2215 2138 2098 -12 -34 32 N ATOM 3049 CA LEU B 159 -30.214 16.056 -23.058 1.00 15.98 C ANISOU 3049 CA LEU B 159 2041 2004 2026 16 -4 -16 C ATOM 3050 C LEU B 159 -30.443 16.951 -21.849 1.00 15.40 C ANISOU 3050 C LEU B 159 1944 1952 1954 0 -31 21 C ATOM 3051 O LEU B 159 -30.000 18.096 -21.807 1.00 15.11 O ANISOU 3051 O LEU B 159 1934 1932 1876 3 -54 33 O ATOM 3052 CB LEU B 159 -28.812 15.458 -23.020 1.00 15.56 C ANISOU 3052 CB LEU B 159 1982 1983 1948 -26 4 65 C ATOM 3053 CG LEU B 159 -28.470 14.587 -21.806 1.00 15.24 C ANISOU 3053 CG LEU B 159 1943 1922 1925 18 -25 11 C ATOM 3054 CD1 LEU B 159 -29.402 13.389 -21.709 1.00 15.78 C ANISOU 3054 CD1 LEU B 159 2003 2035 1959 -42 -1 30 C ATOM 3055 CD2 LEU B 159 -27.021 14.127 -21.879 1.00 15.40 C ANISOU 3055 CD2 LEU B 159 1940 1980 1932 0 -12 5 C ATOM 3056 N ARG B 160 -31.200 16.441 -20.885 1.00 15.39 N ANISOU 3056 N ARG B 160 1950 1958 1939 -8 -35 31 N ATOM 3057 CA ARG B 160 -31.574 17.187 -19.692 1.00 15.76 C ANISOU 3057 CA ARG B 160 2033 1989 1965 0 -11 15 C ATOM 3058 C ARG B 160 -31.495 16.252 -18.479 1.00 15.73 C ANISOU 3058 C ARG B 160 2035 1982 1961 -6 -49 9 C ATOM 3059 O ARG B 160 -31.909 15.100 -18.599 1.00 16.13 O ANISOU 3059 O ARG B 160 2099 2021 2008 -43 -102 36 O ATOM 3060 CB ARG B 160 -32.990 17.740 -19.777 1.00 17.11 C ANISOU 3060 CB ARG B 160 2077 2214 2212 26 -20 26 C ATOM 3061 CG ARG B 160 -33.331 18.713 -20.880 1.00 18.09 C ANISOU 3061 CG ARG B 160 2294 2298 2283 16 -11 76 C ATOM 3062 CD ARG B 160 -32.748 20.098 -20.676 1.00 18.78 C ANISOU 3062 CD ARG B 160 2368 2368 2397 -16 -13 -17 C ATOM 3063 NE ARG B 160 -33.100 20.990 -21.782 1.00 20.22 N ANISOU 3063 NE ARG B 160 2588 2563 2532 -15 -73 76 N ATOM 3064 CZ ARG B 160 -32.505 21.001 -22.968 1.00 21.18 C ANISOU 3064 CZ ARG B 160 2682 2702 2665 2 28 -9 C ATOM 3065 NH1 ARG B 160 -31.497 20.186 -23.236 1.00 20.75 N ANISOU 3065 NH1 ARG B 160 2667 2620 2597 1 -28 33 N ATOM 3066 NH2 ARG B 160 -32.915 21.853 -23.904 1.00 22.14 N ANISOU 3066 NH2 ARG B 160 2861 2801 2749 11 -25 42 N ATOM 3067 N ILE B 161 -30.972 16.735 -17.361 1.00 15.07 N ANISOU 3067 N ILE B 161 1962 1879 1885 2 -16 35 N ATOM 3068 CA ILE B 161 -30.913 15.927 -16.143 1.00 14.35 C ANISOU 3068 CA ILE B 161 1802 1821 1829 -7 -7 -6 C ATOM 3069 C ILE B 161 -31.147 16.815 -14.928 1.00 13.56 C ANISOU 3069 C ILE B 161 1661 1759 1733 8 -20 49 C ATOM 3070 O ILE B 161 -30.780 17.994 -14.937 1.00 13.59 O ANISOU 3070 O ILE B 161 1668 1783 1712 -25 -65 55 O ATOM 3071 CB ILE B 161 -29.575 15.178 -16.024 1.00 13.96 C ANISOU 3071 CB ILE B 161 1795 1777 1733 8 25 36 C ATOM 3072 CG1 ILE B 161 -29.575 14.230 -14.819 1.00 14.18 C ANISOU 3072 CG1 ILE B 161 1811 1784 1793 5 -1 62 C ATOM 3073 CG2 ILE B 161 -28.418 16.167 -15.935 1.00 15.30 C ANISOU 3073 CG2 ILE B 161 1918 1930 1963 -56 -36 18 C ATOM 3074 CD1 ILE B 161 -28.409 13.266 -14.790 1.00 14.24 C ANISOU 3074 CD1 ILE B 161 1825 1799 1786 7 -12 15 C ATOM 3075 N SER B 162 -31.791 16.278 -13.896 1.00 13.01 N ANISOU 3075 N SER B 162 1570 1700 1675 26 -48 28 N ATOM 3076 CA SER B 162 -32.083 17.038 -12.696 1.00 12.79 C ANISOU 3076 CA SER B 162 1579 1622 1660 9 -40 40 C ATOM 3077 C SER B 162 -31.000 16.873 -11.628 1.00 12.29 C ANISOU 3077 C SER B 162 1545 1559 1564 -35 0 29 C ATOM 3078 O SER B 162 -30.165 15.980 -11.718 1.00 12.39 O ANISOU 3078 O SER B 162 1591 1525 1592 -35 -30 61 O ATOM 3079 CB SER B 162 -33.405 16.570 -12.083 1.00 13.40 C ANISOU 3079 CB SER B 162 1621 1698 1771 7 0 63 C ATOM 3080 OG SER B 162 -33.252 15.310 -11.458 1.00 12.74 O ANISOU 3080 OG SER B 162 1518 1646 1676 -76 5 46 O ATOM 3081 N ALA B 163 -31.071 17.715 -10.605 1.00 12.19 N ANISOU 3081 N ALA B 163 1537 1552 1543 -49 -5 45 N ATOM 3082 CA ALA B 163 -30.186 17.602 -9.451 1.00 12.33 C ANISOU 3082 CA ALA B 163 1579 1556 1550 -25 -34 2 C ATOM 3083 C ALA B 163 -30.431 16.304 -8.688 1.00 12.87 C ANISOU 3083 C ALA B 163 1660 1613 1619 2 -14 41 C ATOM 3084 O ALA B 163 -29.481 15.634 -8.281 1.00 12.39 O ANISOU 3084 O ALA B 163 1613 1587 1506 -18 6 53 O ATOM 3085 CB ALA B 163 -30.376 18.793 -8.522 1.00 12.09 C ANISOU 3085 CB ALA B 163 1520 1526 1548 19 -6 29 C ATOM 3086 N VAL B 164 -31.698 15.924 -8.524 1.00 13.93 N ANISOU 3086 N VAL B 164 1729 1773 1790 -42 0 18 N ATOM 3087 CA VAL B 164 -32.007 14.627 -7.915 1.00 14.44 C ANISOU 3087 CA VAL B 164 1869 1785 1832 -33 -18 32 C ATOM 3088 C VAL B 164 -31.394 13.475 -8.691 1.00 14.20 C ANISOU 3088 C VAL B 164 1770 1805 1821 -36 -1 39 C ATOM 3089 O VAL B 164 -30.811 12.560 -8.101 1.00 14.11 O ANISOU 3089 O VAL B 164 1717 1834 1808 -42 -10 53 O ATOM 3090 CB VAL B 164 -33.528 14.432 -7.762 1.00 16.39 C ANISOU 3090 CB VAL B 164 1966 2117 2143 -15 64 9 C ATOM 3091 CG1 VAL B 164 -33.875 12.995 -7.395 1.00 17.62 C ANISOU 3091 CG1 VAL B 164 2244 2165 2285 -26 7 33 C ATOM 3092 CG2 VAL B 164 -34.060 15.399 -6.714 1.00 16.60 C ANISOU 3092 CG2 VAL B 164 2091 2105 2111 0 9 9 C ATOM 3093 N ASN B 165 -31.510 13.483 -10.014 1.00 14.31 N ANISOU 3093 N ASN B 165 1781 1821 1837 -44 -23 21 N ATOM 3094 CA ASN B 165 -30.980 12.423 -10.860 1.00 14.56 C ANISOU 3094 CA ASN B 165 1835 1796 1902 -5 11 53 C ATOM 3095 C ASN B 165 -29.457 12.395 -10.839 1.00 14.67 C ANISOU 3095 C ASN B 165 1840 1835 1898 -15 0 30 C ATOM 3096 O ASN B 165 -28.856 11.316 -10.877 1.00 14.70 O ANISOU 3096 O ASN B 165 1780 1843 1962 -29 -20 51 O ATOM 3097 CB ASN B 165 -31.518 12.578 -12.279 1.00 16.24 C ANISOU 3097 CB ASN B 165 2071 2120 1978 -27 -47 1 C ATOM 3098 CG ASN B 165 -31.341 11.367 -13.160 1.00 16.93 C ANISOU 3098 CG ASN B 165 2171 2128 2133 -29 7 -23 C ATOM 3099 OD1 ASN B 165 -30.531 10.472 -12.913 1.00 17.78 O ANISOU 3099 OD1 ASN B 165 2176 2268 2312 -12 -25 63 O ATOM 3100 ND2 ASN B 165 -32.127 11.325 -14.233 1.00 16.88 N ANISOU 3100 ND2 ASN B 165 2152 2080 2180 1 -38 67 N ATOM 3101 N GLN B 166 -28.815 13.558 -10.751 1.00 14.49 N ANISOU 3101 N GLN B 166 1852 1811 1842 1 -33 63 N ATOM 3102 CA GLN B 166 -27.367 13.612 -10.578 1.00 14.74 C ANISOU 3102 CA GLN B 166 1864 1864 1872 -15 -22 50 C ATOM 3103 C GLN B 166 -26.941 12.901 -9.296 1.00 14.70 C ANISOU 3103 C GLN B 166 1878 1848 1858 7 0 37 C ATOM 3104 O GLN B 166 -26.026 12.079 -9.325 1.00 14.43 O ANISOU 3104 O GLN B 166 1802 1825 1855 -34 -15 32 O ATOM 3105 CB GLN B 166 -26.867 15.056 -10.587 1.00 14.73 C ANISOU 3105 CB GLN B 166 1881 1862 1853 -20 -49 24 C ATOM 3106 CG GLN B 166 -26.995 15.762 -11.923 1.00 14.49 C ANISOU 3106 CG GLN B 166 1813 1887 1805 12 37 9 C ATOM 3107 CD GLN B 166 -25.743 15.750 -12.769 1.00 13.31 C ANISOU 3107 CD GLN B 166 1692 1644 1721 -16 -31 7 C ATOM 3108 OE1 GLN B 166 -24.911 14.854 -12.678 1.00 12.93 O ANISOU 3108 OE1 GLN B 166 1664 1732 1517 5 -18 85 O ATOM 3109 NE2 GLN B 166 -25.593 16.765 -13.622 1.00 13.19 N ANISOU 3109 NE2 GLN B 166 1675 1760 1575 -61 -18 13 N ATOM 3110 N VAL B 167 -27.608 13.194 -8.182 1.00 14.73 N ANISOU 3110 N VAL B 167 1869 1870 1856 -7 -6 33 N ATOM 3111 CA VAL B 167 -27.290 12.525 -6.917 1.00 14.82 C ANISOU 3111 CA VAL B 167 1851 1874 1906 -20 -43 63 C ATOM 3112 C VAL B 167 -27.483 11.021 -7.009 1.00 14.71 C ANISOU 3112 C VAL B 167 1830 1865 1894 2 -28 24 C ATOM 3113 O VAL B 167 -26.638 10.236 -6.563 1.00 14.43 O ANISOU 3113 O VAL B 167 1816 1797 1869 -19 -35 17 O ATOM 3114 CB VAL B 167 -28.109 13.127 -5.762 1.00 16.87 C ANISOU 3114 CB VAL B 167 2177 2154 2078 83 2 -66 C ATOM 3115 CG1 VAL B 167 -28.007 12.290 -4.494 1.00 18.31 C ANISOU 3115 CG1 VAL B 167 2383 2324 2250 -21 57 68 C ATOM 3116 CG2 VAL B 167 -27.643 14.549 -5.476 1.00 17.88 C ANISOU 3116 CG2 VAL B 167 2264 2268 2264 -45 -35 18 C ATOM 3117 N GLU B 168 -28.594 10.573 -7.588 1.00 14.73 N ANISOU 3117 N GLU B 168 1861 1862 1873 -2 -34 17 N ATOM 3118 CA GLU B 168 -28.837 9.148 -7.790 1.00 14.99 C ANISOU 3118 CA GLU B 168 1914 1866 1916 12 18 3 C ATOM 3119 C GLU B 168 -27.761 8.485 -8.635 1.00 14.38 C ANISOU 3119 C GLU B 168 1824 1811 1829 -29 -9 31 C ATOM 3120 O GLU B 168 -27.261 7.405 -8.311 1.00 14.59 O ANISOU 3120 O GLU B 168 1778 1847 1917 -27 -11 52 O ATOM 3121 CB GLU B 168 -30.218 8.956 -8.429 1.00 17.07 C ANISOU 3121 CB GLU B 168 2086 2217 2182 -51 -102 -14 C ATOM 3122 CG GLU B 168 -31.342 9.464 -7.541 1.00 18.40 C ANISOU 3122 CG GLU B 168 2374 2309 2308 12 61 -7 C ATOM 3123 CD GLU B 168 -32.695 9.450 -8.221 1.00 20.90 C ANISOU 3123 CD GLU B 168 2545 2693 2703 -13 -72 -9 C ATOM 3124 OE1 GLU B 168 -32.748 9.330 -9.462 1.00 22.16 O ANISOU 3124 OE1 GLU B 168 2784 2870 2767 -7 -31 38 O ATOM 3125 OE2 GLU B 168 -33.709 9.559 -7.500 1.00 21.55 O ANISOU 3125 OE2 GLU B 168 2669 2808 2710 0 -10 7 O ATOM 3126 N PHE B 169 -27.385 9.118 -9.738 1.00 13.79 N ANISOU 3126 N PHE B 169 1714 1750 1775 -10 -32 10 N ATOM 3127 CA PHE B 169 -26.331 8.648 -10.615 1.00 13.63 C ANISOU 3127 CA PHE B 169 1713 1714 1753 -9 -33 12 C ATOM 3128 C PHE B 169 -24.989 8.583 -9.887 1.00 13.60 C ANISOU 3128 C PHE B 169 1713 1715 1738 -19 -34 9 C ATOM 3129 O PHE B 169 -24.272 7.586 -9.986 1.00 13.56 O ANISOU 3129 O PHE B 169 1697 1717 1737 -36 -43 10 O ATOM 3130 CB PHE B 169 -26.217 9.556 -11.845 1.00 14.18 C ANISOU 3130 CB PHE B 169 1754 1836 1797 12 4 58 C ATOM 3131 CG PHE B 169 -25.052 9.244 -12.737 1.00 13.01 C ANISOU 3131 CG PHE B 169 1758 1559 1625 3 -15 31 C ATOM 3132 CD1 PHE B 169 -25.066 8.125 -13.554 1.00 12.39 C ANISOU 3132 CD1 PHE B 169 1602 1564 1540 -3 -40 28 C ATOM 3133 CD2 PHE B 169 -23.933 10.062 -12.755 1.00 13.71 C ANISOU 3133 CD2 PHE B 169 1705 1784 1721 -9 -52 35 C ATOM 3134 CE1 PHE B 169 -23.996 7.831 -14.374 1.00 12.86 C ANISOU 3134 CE1 PHE B 169 1643 1643 1602 15 -5 34 C ATOM 3135 CE2 PHE B 169 -22.859 9.771 -13.572 1.00 14.08 C ANISOU 3135 CE2 PHE B 169 1824 1792 1735 8 5 4 C ATOM 3136 CZ PHE B 169 -22.884 8.656 -14.384 1.00 13.83 C ANISOU 3136 CZ PHE B 169 1770 1711 1772 -42 -33 32 C ATOM 3137 N LEU B 170 -24.667 9.636 -9.144 1.00 13.46 N ANISOU 3137 N LEU B 170 1727 1676 1713 -22 -43 50 N ATOM 3138 CA LEU B 170 -23.396 9.699 -8.428 1.00 13.47 C ANISOU 3138 CA LEU B 170 1717 1690 1710 -21 -41 41 C ATOM 3139 C LEU B 170 -23.336 8.691 -7.288 1.00 13.57 C ANISOU 3139 C LEU B 170 1726 1696 1734 2 -19 45 C ATOM 3140 O LEU B 170 -22.282 8.092 -7.050 1.00 13.37 O ANISOU 3140 O LEU B 170 1716 1696 1668 -10 -41 97 O ATOM 3141 CB LEU B 170 -23.143 11.112 -7.904 1.00 13.72 C ANISOU 3141 CB LEU B 170 1751 1721 1740 17 -47 -11 C ATOM 3142 CG LEU B 170 -22.873 12.183 -8.966 1.00 14.58 C ANISOU 3142 CG LEU B 170 1888 1859 1792 9 20 37 C ATOM 3143 CD1 LEU B 170 -22.948 13.570 -8.344 1.00 15.13 C ANISOU 3143 CD1 LEU B 170 1928 1872 1949 -30 -5 11 C ATOM 3144 CD2 LEU B 170 -21.519 11.965 -9.624 1.00 15.05 C ANISOU 3144 CD2 LEU B 170 1874 1966 1879 16 3 52 C ATOM 3145 N GLU B 171 -24.457 8.491 -6.604 1.00 13.91 N ANISOU 3145 N GLU B 171 1768 1742 1775 -11 -5 51 N ATOM 3146 CA GLU B 171 -24.537 7.440 -5.588 1.00 14.29 C ANISOU 3146 CA GLU B 171 1857 1750 1822 -12 -18 64 C ATOM 3147 C GLU B 171 -24.261 6.070 -6.189 1.00 14.15 C ANISOU 3147 C GLU B 171 1792 1782 1800 -13 0 35 C ATOM 3148 O GLU B 171 -23.484 5.294 -5.615 1.00 14.11 O ANISOU 3148 O GLU B 171 1723 1749 1890 -7 30 38 O ATOM 3149 CB GLU B 171 -25.898 7.476 -4.895 1.00 16.00 C ANISOU 3149 CB GLU B 171 1949 2087 2043 11 43 12 C ATOM 3150 CG GLU B 171 -26.139 6.296 -3.958 1.00 17.84 C ANISOU 3150 CG GLU B 171 2337 2142 2300 -13 -19 81 C ATOM 3151 CD GLU B 171 -27.523 6.318 -3.344 1.00 19.85 C ANISOU 3151 CD GLU B 171 2476 2537 2529 -9 54 2 C ATOM 3152 OE1 GLU B 171 -28.511 6.473 -4.094 1.00 20.84 O ANISOU 3152 OE1 GLU B 171 2607 2630 2680 -16 -52 59 O ATOM 3153 OE2 GLU B 171 -27.632 6.179 -2.108 1.00 19.85 O ANISOU 3153 OE2 GLU B 171 2455 2560 2528 22 -32 54 O ATOM 3154 N SER B 172 -24.868 5.748 -7.328 1.00 14.17 N ANISOU 3154 N SER B 172 1778 1790 1817 -15 -2 45 N ATOM 3155 CA SER B 172 -24.584 4.484 -8.000 1.00 14.70 C ANISOU 3155 CA SER B 172 1898 1827 1859 -20 29 21 C ATOM 3156 C SER B 172 -23.103 4.343 -8.320 1.00 15.14 C ANISOU 3156 C SER B 172 1912 1887 1953 -13 13 17 C ATOM 3157 O SER B 172 -22.500 3.302 -8.057 1.00 15.61 O ANISOU 3157 O SER B 172 1960 1923 2049 -18 -38 63 O ATOM 3158 CB SER B 172 -25.440 4.333 -9.259 1.00 16.12 C ANISOU 3158 CB SER B 172 2102 2055 1969 -10 -63 49 C ATOM 3159 OG SER B 172 -26.816 4.346 -8.906 1.00 18.76 O ANISOU 3159 OG SER B 172 2235 2378 2514 -7 3 41 O ATOM 3160 N LEU B 173 -22.491 5.383 -8.885 1.00 14.94 N ANISOU 3160 N LEU B 173 1894 1859 1925 -6 16 1 N ATOM 3161 CA LEU B 173 -21.058 5.371 -9.150 1.00 14.83 C ANISOU 3161 CA LEU B 173 1876 1852 1907 -30 -12 22 C ATOM 3162 C LEU B 173 -20.238 5.120 -7.892 1.00 14.76 C ANISOU 3162 C LEU B 173 1868 1827 1912 -24 -7 29 C ATOM 3163 O LEU B 173 -19.367 4.252 -7.881 1.00 14.46 O ANISOU 3163 O LEU B 173 1843 1778 1874 -51 -34 73 O ATOM 3164 CB LEU B 173 -20.641 6.689 -9.812 1.00 15.24 C ANISOU 3164 CB LEU B 173 1872 1911 2006 -29 11 79 C ATOM 3165 CG LEU B 173 -19.141 6.865 -10.067 1.00 13.81 C ANISOU 3165 CG LEU B 173 1800 1685 1761 26 38 -5 C ATOM 3166 CD1 LEU B 173 -18.610 5.814 -11.033 1.00 12.63 C ANISOU 3166 CD1 LEU B 173 1664 1492 1643 -3 -61 47 C ATOM 3167 CD2 LEU B 173 -18.877 8.269 -10.594 1.00 13.67 C ANISOU 3167 CD2 LEU B 173 1731 1705 1757 -10 -8 46 C ATOM 3168 N TYR B 174 -20.507 5.854 -6.823 1.00 15.27 N ANISOU 3168 N TYR B 174 1981 1915 1906 -22 -4 25 N ATOM 3169 CA TYR B 174 -19.843 5.681 -5.536 1.00 15.59 C ANISOU 3169 CA TYR B 174 2008 1958 1957 -30 -35 34 C ATOM 3170 C TYR B 174 -19.926 4.243 -5.036 1.00 15.74 C ANISOU 3170 C TYR B 174 2025 1974 1980 9 -18 43 C ATOM 3171 O TYR B 174 -18.931 3.691 -4.561 1.00 15.36 O ANISOU 3171 O TYR B 174 2035 1899 1904 -17 -42 46 O ATOM 3172 CB TYR B 174 -20.465 6.631 -4.514 1.00 16.26 C ANISOU 3172 CB TYR B 174 2071 2009 2096 -4 2 2 C ATOM 3173 CG TYR B 174 -19.963 6.484 -3.097 1.00 17.28 C ANISOU 3173 CG TYR B 174 2237 2176 2152 17 -20 -9 C ATOM 3174 CD1 TYR B 174 -18.805 7.128 -2.681 1.00 18.02 C ANISOU 3174 CD1 TYR B 174 2277 2270 2301 -24 -10 8 C ATOM 3175 CD2 TYR B 174 -20.653 5.712 -2.171 1.00 18.11 C ANISOU 3175 CD2 TYR B 174 2322 2272 2285 -18 17 27 C ATOM 3176 CE1 TYR B 174 -18.344 7.007 -1.384 1.00 18.57 C ANISOU 3176 CE1 TYR B 174 2346 2357 2350 -9 -34 0 C ATOM 3177 CE2 TYR B 174 -20.196 5.580 -0.873 1.00 18.73 C ANISOU 3177 CE2 TYR B 174 2399 2380 2338 -4 -1 26 C ATOM 3178 CZ TYR B 174 -19.049 6.233 -0.485 1.00 19.14 C ANISOU 3178 CZ TYR B 174 2433 2425 2414 -22 -8 25 C ATOM 3179 OH TYR B 174 -18.582 6.108 0.804 1.00 19.90 O ANISOU 3179 OH TYR B 174 2550 2558 2453 13 -25 16 O ATOM 3180 N LEU B 175 -21.094 3.622 -5.174 1.00 16.22 N ANISOU 3180 N LEU B 175 2041 2072 2048 -8 -27 37 N ATOM 3181 CA LEU B 175 -21.314 2.256 -4.723 1.00 17.06 C ANISOU 3181 CA LEU B 175 2185 2108 2188 -15 -28 42 C ATOM 3182 C LEU B 175 -20.891 1.205 -5.732 1.00 17.53 C ANISOU 3182 C LEU B 175 2233 2200 2226 -2 -23 0 C ATOM 3183 O LEU B 175 -21.009 0.000 -5.494 1.00 18.18 O ANISOU 3183 O LEU B 175 2300 2258 2348 -14 -43 68 O ATOM 3184 CB LEU B 175 -22.796 2.062 -4.367 1.00 18.02 C ANISOU 3184 CB LEU B 175 2239 2304 2302 -34 -11 54 C ATOM 3185 CG LEU B 175 -23.337 2.921 -3.221 1.00 19.61 C ANISOU 3185 CG LEU B 175 2509 2442 2499 16 27 -37 C ATOM 3186 CD1 LEU B 175 -24.837 2.721 -3.059 1.00 20.33 C ANISOU 3186 CD1 LEU B 175 2553 2568 2603 -22 0 40 C ATOM 3187 CD2 LEU B 175 -22.614 2.597 -1.921 1.00 20.54 C ANISOU 3187 CD2 LEU B 175 2648 2587 2568 3 -2 38 C ATOM 3188 N ASN B 176 -20.392 1.609 -6.895 1.00 17.86 N ANISOU 3188 N ASN B 176 2265 2260 2259 -15 -10 24 N ATOM 3189 CA ASN B 176 -19.997 0.735 -7.983 1.00 18.39 C ANISOU 3189 CA ASN B 176 2352 2310 2324 -1 19 5 C ATOM 3190 C ASN B 176 -21.179 -0.050 -8.548 1.00 18.84 C ANISOU 3190 C ASN B 176 2428 2347 2382 -24 -16 11 C ATOM 3191 O ASN B 176 -21.034 -1.182 -9.009 1.00 18.75 O ANISOU 3191 O ASN B 176 2411 2324 2390 -24 -34 22 O ATOM 3192 CB ASN B 176 -18.882 -0.227 -7.561 1.00 19.28 C ANISOU 3192 CB ASN B 176 2432 2390 2505 56 3 0 C ATOM 3193 CG ASN B 176 -17.645 0.478 -7.043 1.00 20.04 C ANISOU 3193 CG ASN B 176 2486 2551 2576 -7 15 -18 C ATOM 3194 OD1 ASN B 176 -16.966 1.203 -7.768 1.00 19.64 O ANISOU 3194 OD1 ASN B 176 2509 2493 2460 43 -90 62 O ATOM 3195 ND2 ASN B 176 -17.367 0.264 -5.758 1.00 21.35 N ANISOU 3195 ND2 ASN B 176 2732 2698 2683 -4 -46 52 N ATOM 3196 N LYS B 177 -22.343 0.588 -8.588 1.00 19.69 N ANISOU 3196 N LYS B 177 2482 2452 2549 13 -24 66 N ATOM 3197 CA LYS B 177 -23.575 -0.076 -8.987 1.00 20.46 C ANISOU 3197 CA LYS B 177 2585 2543 2645 -42 -66 35 C ATOM 3198 C LYS B 177 -24.024 0.275 -10.396 1.00 20.66 C ANISOU 3198 C LYS B 177 2619 2591 2639 -32 -31 45 C ATOM 3199 O LYS B 177 -25.055 -0.234 -10.850 1.00 20.88 O ANISOU 3199 O LYS B 177 2642 2616 2674 -28 -75 52 O ATOM 3200 CB LYS B 177 -24.686 0.247 -7.981 1.00 22.72 C ANISOU 3200 CB LYS B 177 2793 2909 2931 19 49 -94 C ATOM 3201 CG LYS B 177 -24.624 -0.585 -6.709 1.00 26.12 C ANISOU 3201 CG LYS B 177 3430 3234 3260 -30 -83 84 C ATOM 3202 CD LYS B 177 -25.765 -0.223 -5.771 1.00 29.61 C ANISOU 3202 CD LYS B 177 3654 3810 3787 38 47 -84 C ATOM 3203 CE LYS B 177 -25.946 -1.259 -4.675 1.00 32.68 C ANISOU 3203 CE LYS B 177 4229 4089 4099 -21 -25 69 C ATOM 3204 NZ LYS B 177 -27.058 -0.888 -3.753 1.00 34.24 N ANISOU 3204 NZ LYS B 177 4309 4343 4358 7 32 6 N ATOM 3205 N LEU B 178 -23.289 1.138 -11.095 1.00 20.44 N ANISOU 3205 N LEU B 178 2567 2578 2621 -31 -37 25 N ATOM 3206 CA LEU B 178 -23.592 1.384 -12.502 1.00 20.07 C ANISOU 3206 CA LEU B 178 2547 2497 2581 -33 13 16 C ATOM 3207 C LEU B 178 -23.331 0.132 -13.327 1.00 20.00 C ANISOU 3207 C LEU B 178 2541 2494 2563 -17 -2 19 C ATOM 3208 O LEU B 178 -22.515 -0.713 -12.948 1.00 19.73 O ANISOU 3208 O LEU B 178 2490 2490 2519 -42 -23 20 O ATOM 3209 CB LEU B 178 -22.770 2.550 -13.053 1.00 19.28 C ANISOU 3209 CB LEU B 178 2407 2433 2485 12 -27 9 C ATOM 3210 CG LEU B 178 -23.047 3.921 -12.431 1.00 19.34 C ANISOU 3210 CG LEU B 178 2446 2443 2458 -28 -20 -3 C ATOM 3211 CD1 LEU B 178 -22.056 4.945 -12.968 1.00 19.49 C ANISOU 3211 CD1 LEU B 178 2466 2449 2492 -18 -14 47 C ATOM 3212 CD2 LEU B 178 -24.476 4.376 -12.689 1.00 19.50 C ANISOU 3212 CD2 LEU B 178 2465 2453 2492 -5 14 36 C ATOM 3213 N SER B 179 -23.972 0.034 -14.488 1.00 20.32 N ANISOU 3213 N SER B 179 2574 2544 2603 -15 -32 14 N ATOM 3214 CA SER B 179 -23.716 -1.059 -15.420 1.00 20.79 C ANISOU 3214 CA SER B 179 2658 2584 2659 14 25 4 C ATOM 3215 C SER B 179 -22.428 -0.839 -16.202 1.00 20.44 C ANISOU 3215 C SER B 179 2596 2565 2606 0 -34 2 C ATOM 3216 O SER B 179 -22.402 -0.455 -17.366 1.00 20.89 O ANISOU 3216 O SER B 179 2685 2637 2617 -24 -49 2 O ATOM 3217 CB SER B 179 -24.894 -1.222 -16.386 1.00 22.93 C ANISOU 3217 CB SER B 179 2917 2916 2879 -25 -136 -13 C ATOM 3218 OG SER B 179 -26.103 -1.347 -15.663 1.00 25.58 O ANISOU 3218 OG SER B 179 3161 3326 3234 -12 36 -19 O ATOM 3219 N ALA B 180 -21.314 -1.098 -15.539 1.00 19.90 N ANISOU 3219 N ALA B 180 2524 2493 2543 3 10 2 N ATOM 3220 CA ALA B 180 -19.966 -0.892 -16.021 1.00 19.10 C ANISOU 3220 CA ALA B 180 2460 2391 2408 10 -44 10 C ATOM 3221 C ALA B 180 -19.041 -1.645 -15.060 1.00 18.30 C ANISOU 3221 C ALA B 180 2345 2272 2335 -12 -6 -24 C ATOM 3222 O ALA B 180 -19.479 -1.894 -13.934 1.00 18.08 O ANISOU 3222 O ALA B 180 2291 2252 2327 -17 -44 1 O ATOM 3223 CB ALA B 180 -19.613 0.586 -16.049 1.00 19.86 C ANISOU 3223 CB ALA B 180 2564 2424 2558 -4 -34 8 C ATOM 3224 N SER B 181 -17.843 -1.998 -15.495 1.00 18.18 N ANISOU 3224 N SER B 181 2307 2254 2347 -4 -59 1 N ATOM 3225 CA SER B 181 -16.942 -2.729 -14.599 1.00 17.79 C ANISOU 3225 CA SER B 181 2282 2232 2243 -2 -15 5 C ATOM 3226 C SER B 181 -16.687 -1.902 -13.346 1.00 17.73 C ANISOU 3226 C SER B 181 2283 2211 2241 1 -36 14 C ATOM 3227 O SER B 181 -16.748 -0.670 -13.407 1.00 17.86 O ANISOU 3227 O SER B 181 2305 2217 2263 6 -44 44 O ATOM 3228 CB SER B 181 -15.626 -3.057 -15.294 1.00 18.03 C ANISOU 3228 CB SER B 181 2310 2299 2242 9 -1 0 C ATOM 3229 OG SER B 181 -14.875 -1.889 -15.567 1.00 18.47 O ANISOU 3229 OG SER B 181 2381 2325 2313 -29 -27 -31 O ATOM 3230 N LYS B 182 -16.372 -2.562 -12.228 1.00 17.26 N ANISOU 3230 N LYS B 182 2200 2161 2195 -21 -17 -11 N ATOM 3231 CA LYS B 182 -15.982 -1.804 -11.037 1.00 17.17 C ANISOU 3231 CA LYS B 182 2150 2160 2215 -28 -13 -33 C ATOM 3232 C LYS B 182 -14.662 -1.080 -11.285 1.00 16.22 C ANISOU 3232 C LYS B 182 2093 2053 2016 15 -36 12 C ATOM 3233 O LYS B 182 -14.508 0.059 -10.838 1.00 16.28 O ANISOU 3233 O LYS B 182 2123 2024 2038 -21 -63 57 O ATOM 3234 CB LYS B 182 -15.907 -2.661 -9.773 1.00 19.44 C ANISOU 3234 CB LYS B 182 2540 2426 2423 5 2 114 C ATOM 3235 CG LYS B 182 -15.391 -1.904 -8.559 1.00 21.22 C ANISOU 3235 CG LYS B 182 2700 2681 2683 2 -46 -78 C ATOM 3236 CD LYS B 182 -15.787 -2.533 -7.233 1.00 23.27 C ANISOU 3236 CD LYS B 182 3003 2948 2890 -24 31 38 C ATOM 3237 CE LYS B 182 -15.039 -1.867 -6.085 1.00 23.67 C ANISOU 3237 CE LYS B 182 3018 3016 2962 -3 -21 9 C ATOM 3238 NZ LYS B 182 -15.438 -2.402 -4.750 1.00 23.40 N ANISOU 3238 NZ LYS B 182 2956 2960 2974 -7 -19 26 N ATOM 3239 N GLU B 183 -13.728 -1.708 -11.988 1.00 16.02 N ANISOU 3239 N GLU B 183 2035 2063 1989 4 -60 38 N ATOM 3240 CA GLU B 183 -12.501 -1.053 -12.415 1.00 16.48 C ANISOU 3240 CA GLU B 183 2092 2073 2095 -47 -78 91 C ATOM 3241 C GLU B 183 -12.757 0.310 -13.050 1.00 15.78 C ANISOU 3241 C GLU B 183 2006 1998 1993 -31 -54 14 C ATOM 3242 O GLU B 183 -12.192 1.313 -12.615 1.00 15.75 O ANISOU 3242 O GLU B 183 1966 1971 2047 -20 -71 22 O ATOM 3243 CB GLU B 183 -11.742 -1.916 -13.427 1.00 20.50 C ANISOU 3243 CB GLU B 183 2617 2678 2496 -10 119 -172 C ATOM 3244 CG GLU B 183 -11.077 -3.151 -12.851 1.00 25.80 C ANISOU 3244 CG GLU B 183 3269 3138 3397 24 -138 163 C ATOM 3245 CD GLU B 183 -10.279 -3.920 -13.887 1.00 30.41 C ANISOU 3245 CD GLU B 183 3818 3921 3816 22 71 -132 C ATOM 3246 OE1 GLU B 183 -10.020 -3.385 -14.987 1.00 31.00 O ANISOU 3246 OE1 GLU B 183 3969 3888 3920 4 16 -30 O ATOM 3247 OE2 GLU B 183 -9.900 -5.076 -13.602 1.00 33.59 O ANISOU 3247 OE2 GLU B 183 4298 4127 4339 23 -24 35 O ATOM 3248 N ASN B 184 -13.632 0.357 -14.056 1.00 15.10 N ANISOU 3248 N ASN B 184 1939 1894 1905 -9 -9 28 N ATOM 3249 CA ASN B 184 -13.863 1.608 -14.777 1.00 14.70 C ANISOU 3249 CA ASN B 184 1876 1865 1846 12 -46 -16 C ATOM 3250 C ASN B 184 -14.534 2.654 -13.908 1.00 14.24 C ANISOU 3250 C ASN B 184 1792 1836 1782 -12 -32 15 C ATOM 3251 O ASN B 184 -14.219 3.840 -14.007 1.00 14.81 O ANISOU 3251 O ASN B 184 1894 1864 1870 -24 -39 72 O ATOM 3252 CB ASN B 184 -14.663 1.352 -16.061 1.00 14.14 C ANISOU 3252 CB ASN B 184 1876 1735 1763 -24 -7 10 C ATOM 3253 CG ASN B 184 -13.797 0.654 -17.093 1.00 13.95 C ANISOU 3253 CG ASN B 184 1825 1685 1790 13 -6 48 C ATOM 3254 OD1 ASN B 184 -12.568 0.766 -17.060 1.00 14.67 O ANISOU 3254 OD1 ASN B 184 1879 1802 1891 -31 -57 45 O ATOM 3255 ND2 ASN B 184 -14.423 -0.062 -18.016 1.00 14.87 N ANISOU 3255 ND2 ASN B 184 1972 1766 1910 -25 -70 14 N ATOM 3256 N GLN B 185 -15.433 2.231 -13.024 1.00 13.65 N ANISOU 3256 N GLN B 185 1721 1738 1727 1 -62 4 N ATOM 3257 CA GLN B 185 -16.045 3.143 -12.064 1.00 13.63 C ANISOU 3257 CA GLN B 185 1722 1741 1716 8 -38 21 C ATOM 3258 C GLN B 185 -15.016 3.694 -11.090 1.00 13.65 C ANISOU 3258 C GLN B 185 1737 1711 1740 13 -40 3 C ATOM 3259 O GLN B 185 -15.010 4.889 -10.783 1.00 14.05 O ANISOU 3259 O GLN B 185 1807 1704 1826 31 -47 39 O ATOM 3260 CB GLN B 185 -17.193 2.426 -11.350 1.00 14.16 C ANISOU 3260 CB GLN B 185 1828 1745 1807 -41 4 39 C ATOM 3261 CG GLN B 185 -18.300 2.039 -12.332 1.00 15.56 C ANISOU 3261 CG GLN B 185 1920 2009 1983 -40 -69 24 C ATOM 3262 CD GLN B 185 -19.456 1.337 -11.653 1.00 15.56 C ANISOU 3262 CD GLN B 185 1882 2072 1956 50 18 -1 C ATOM 3263 OE1 GLN B 185 -19.627 0.123 -11.798 1.00 18.97 O ANISOU 3263 OE1 GLN B 185 2465 2234 2510 -12 -62 -5 O ATOM 3264 NE2 GLN B 185 -20.253 2.097 -10.918 1.00 13.61 N ANISOU 3264 NE2 GLN B 185 1805 1681 1686 -45 -76 68 N ATOM 3265 N LEU B 186 -14.096 2.842 -10.636 1.00 13.36 N ANISOU 3265 N LEU B 186 1738 1656 1684 -17 -42 31 N ATOM 3266 CA LEU B 186 -13.017 3.294 -9.764 1.00 13.41 C ANISOU 3266 CA LEU B 186 1709 1665 1721 -41 -17 2 C ATOM 3267 C LEU B 186 -12.080 4.268 -10.465 1.00 13.20 C ANISOU 3267 C LEU B 186 1704 1665 1647 -22 -16 5 C ATOM 3268 O LEU B 186 -11.657 5.264 -9.865 1.00 13.25 O ANISOU 3268 O LEU B 186 1784 1598 1654 -31 -50 52 O ATOM 3269 CB LEU B 186 -12.243 2.093 -9.213 1.00 14.26 C ANISOU 3269 CB LEU B 186 1836 1800 1782 44 -83 14 C ATOM 3270 CG LEU B 186 -13.010 1.233 -8.201 1.00 15.85 C ANISOU 3270 CG LEU B 186 1995 1972 2055 -44 43 30 C ATOM 3271 CD1 LEU B 186 -12.266 -0.064 -7.929 1.00 15.84 C ANISOU 3271 CD1 LEU B 186 2006 2030 1981 1 -34 31 C ATOM 3272 CD2 LEU B 186 -13.240 1.995 -6.904 1.00 16.52 C ANISOU 3272 CD2 LEU B 186 2159 2053 2064 17 0 22 C ATOM 3273 N ILE B 187 -11.755 4.010 -11.723 1.00 12.90 N ANISOU 3273 N ILE B 187 1601 1651 1649 -6 -13 10 N ATOM 3274 CA ILE B 187 -10.925 4.916 -12.510 1.00 12.86 C ANISOU 3274 CA ILE B 187 1653 1620 1614 -1 -11 15 C ATOM 3275 C ILE B 187 -11.546 6.302 -12.590 1.00 12.86 C ANISOU 3275 C ILE B 187 1654 1622 1608 -3 -32 13 C ATOM 3276 O ILE B 187 -10.870 7.309 -12.371 1.00 12.91 O ANISOU 3276 O ILE B 187 1660 1679 1566 -23 -110 -5 O ATOM 3277 CB ILE B 187 -10.671 4.353 -13.921 1.00 13.47 C ANISOU 3277 CB ILE B 187 1755 1718 1645 -14 16 -8 C ATOM 3278 CG1 ILE B 187 -9.719 3.158 -13.839 1.00 14.16 C ANISOU 3278 CG1 ILE B 187 1803 1796 1782 20 -2 -17 C ATOM 3279 CG2 ILE B 187 -10.116 5.417 -14.859 1.00 13.71 C ANISOU 3279 CG2 ILE B 187 1763 1703 1745 -29 19 8 C ATOM 3280 CD1 ILE B 187 -9.607 2.349 -15.112 1.00 13.99 C ANISOU 3280 CD1 ILE B 187 1801 1757 1758 21 7 -2 C ATOM 3281 N VAL B 188 -12.834 6.371 -12.925 1.00 12.97 N ANISOU 3281 N VAL B 188 1650 1619 1658 2 -3 -15 N ATOM 3282 CA VAL B 188 -13.509 7.663 -13.036 1.00 13.17 C ANISOU 3282 CA VAL B 188 1690 1648 1665 24 -26 12 C ATOM 3283 C VAL B 188 -13.643 8.333 -11.679 1.00 13.02 C ANISOU 3283 C VAL B 188 1673 1632 1642 5 -21 25 C ATOM 3284 O VAL B 188 -13.497 9.554 -11.576 1.00 13.29 O ANISOU 3284 O VAL B 188 1707 1643 1699 -19 -75 53 O ATOM 3285 CB VAL B 188 -14.861 7.516 -13.751 1.00 13.37 C ANISOU 3285 CB VAL B 188 1719 1686 1674 -1 -30 -24 C ATOM 3286 CG1 VAL B 188 -15.614 8.836 -13.812 1.00 13.93 C ANISOU 3286 CG1 VAL B 188 1765 1729 1798 20 -30 10 C ATOM 3287 CG2 VAL B 188 -14.620 6.976 -15.160 1.00 12.93 C ANISOU 3287 CG2 VAL B 188 1683 1600 1631 25 -20 34 C ATOM 3288 N LYS B 189 -13.864 7.563 -10.611 1.00 12.99 N ANISOU 3288 N LYS B 189 1674 1639 1622 -11 -11 10 N ATOM 3289 CA LYS B 189 -13.905 8.148 -9.272 1.00 12.90 C ANISOU 3289 CA LYS B 189 1642 1635 1625 -7 -17 6 C ATOM 3290 C LYS B 189 -12.604 8.837 -8.907 1.00 12.47 C ANISOU 3290 C LYS B 189 1619 1574 1545 14 -20 37 C ATOM 3291 O LYS B 189 -12.651 9.990 -8.456 1.00 12.55 O ANISOU 3291 O LYS B 189 1605 1624 1537 -4 -37 -14 O ATOM 3292 CB LYS B 189 -14.313 7.091 -8.242 1.00 14.25 C ANISOU 3292 CB LYS B 189 1885 1770 1761 -21 -8 98 C ATOM 3293 CG LYS B 189 -15.829 6.912 -8.204 1.00 16.53 C ANISOU 3293 CG LYS B 189 1985 2128 2168 29 -9 -45 C ATOM 3294 CD LYS B 189 -16.266 6.001 -7.076 1.00 19.31 C ANISOU 3294 CD LYS B 189 2467 2455 2416 -44 45 90 C ATOM 3295 CE LYS B 189 -16.072 4.534 -7.414 1.00 20.94 C ANISOU 3295 CE LYS B 189 2668 2575 2714 16 -5 -18 C ATOM 3296 NZ LYS B 189 -16.576 3.667 -6.306 1.00 22.04 N ANISOU 3296 NZ LYS B 189 2824 2758 2793 -13 47 35 N ATOM 3297 N GLU B 190 -11.440 8.232 -9.161 1.00 12.35 N ANISOU 3297 N GLU B 190 1601 1570 1523 -10 -17 50 N ATOM 3298 CA GLU B 190 -10.197 8.905 -8.782 1.00 12.69 C ANISOU 3298 CA GLU B 190 1628 1589 1603 -44 -15 32 C ATOM 3299 C GLU B 190 -9.980 10.154 -9.628 1.00 12.14 C ANISOU 3299 C GLU B 190 1540 1569 1506 -9 -3 16 C ATOM 3300 O GLU B 190 -9.518 11.178 -9.118 1.00 12.49 O ANISOU 3300 O GLU B 190 1633 1586 1527 -31 -53 62 O ATOM 3301 CB GLU B 190 -8.954 8.015 -8.823 1.00 14.91 C ANISOU 3301 CB GLU B 190 1835 1833 1999 97 2 5 C ATOM 3302 CG GLU B 190 -7.793 8.693 -8.091 1.00 16.30 C ANISOU 3302 CG GLU B 190 2064 2118 2011 -59 -44 4 C ATOM 3303 CD GLU B 190 -6.489 7.936 -8.193 1.00 17.61 C ANISOU 3303 CD GLU B 190 2207 2239 2246 33 -44 -18 C ATOM 3304 OE1 GLU B 190 -5.791 8.070 -9.222 1.00 18.59 O ANISOU 3304 OE1 GLU B 190 2327 2402 2335 -2 -2 83 O ATOM 3305 OE2 GLU B 190 -6.144 7.207 -7.238 1.00 17.80 O ANISOU 3305 OE2 GLU B 190 2311 2189 2264 -35 -12 29 O ATOM 3306 N ALA B 191 -10.441 10.147 -10.877 1.00 12.02 N ANISOU 3306 N ALA B 191 1540 1527 1499 20 21 6 N ATOM 3307 CA ALA B 191 -10.415 11.313 -11.742 1.00 12.00 C ANISOU 3307 CA ALA B 191 1547 1514 1497 -1 9 2 C ATOM 3308 C ALA B 191 -11.252 12.481 -11.232 1.00 11.95 C ANISOU 3308 C ALA B 191 1526 1537 1478 -11 18 -7 C ATOM 3309 O ALA B 191 -11.036 13.627 -11.644 1.00 12.76 O ANISOU 3309 O ALA B 191 1727 1586 1536 -33 -51 26 O ATOM 3310 CB ALA B 191 -10.921 10.927 -13.135 1.00 13.00 C ANISOU 3310 CB ALA B 191 1683 1711 1545 -23 -9 -25 C ATOM 3311 N LEU B 192 -12.231 12.220 -10.381 1.00 10.92 N ANISOU 3311 N LEU B 192 1431 1408 1311 8 -49 21 N ATOM 3312 CA LEU B 192 -13.112 13.219 -9.819 1.00 11.15 C ANISOU 3312 CA LEU B 192 1463 1397 1374 -5 -32 -7 C ATOM 3313 C LEU B 192 -12.647 13.776 -8.481 1.00 10.81 C ANISOU 3313 C LEU B 192 1405 1378 1325 -20 3 31 C ATOM 3314 O LEU B 192 -13.274 14.704 -7.959 1.00 11.09 O ANISOU 3314 O LEU B 192 1384 1403 1428 8 13 54 O ATOM 3315 CB LEU B 192 -14.524 12.626 -9.678 1.00 11.93 C ANISOU 3315 CB LEU B 192 1512 1492 1530 -27 14 16 C ATOM 3316 CG LEU B 192 -15.226 12.312 -11.005 1.00 13.17 C ANISOU 3316 CG LEU B 192 1723 1692 1589 9 -45 -22 C ATOM 3317 CD1 LEU B 192 -16.519 11.549 -10.765 1.00 14.66 C ANISOU 3317 CD1 LEU B 192 1816 1882 1873 -30 -9 0 C ATOM 3318 CD2 LEU B 192 -15.502 13.595 -11.782 1.00 14.35 C ANISOU 3318 CD2 LEU B 192 1867 1751 1834 9 -36 46 C ATOM 3319 N VAL B 193 -11.561 13.259 -7.915 1.00 11.01 N ANISOU 3319 N VAL B 193 1414 1377 1392 -9 12 45 N ATOM 3320 CA VAL B 193 -11.080 13.827 -6.650 1.00 11.72 C ANISOU 3320 CA VAL B 193 1507 1495 1451 -26 -33 13 C ATOM 3321 C VAL B 193 -10.685 15.285 -6.821 1.00 11.94 C ANISOU 3321 C VAL B 193 1517 1510 1508 -12 -16 12 C ATOM 3322 O VAL B 193 -9.909 15.594 -7.725 1.00 12.21 O ANISOU 3322 O VAL B 193 1575 1497 1566 -17 12 69 O ATOM 3323 CB VAL B 193 -9.894 13.023 -6.089 1.00 13.02 C ANISOU 3323 CB VAL B 193 1599 1642 1706 49 -63 26 C ATOM 3324 CG1 VAL B 193 -9.313 13.721 -4.869 1.00 13.50 C ANISOU 3324 CG1 VAL B 193 1739 1721 1668 7 6 -7 C ATOM 3325 CG2 VAL B 193 -10.351 11.614 -5.746 1.00 13.56 C ANISOU 3325 CG2 VAL B 193 1739 1676 1739 -7 -4 -21 C ATOM 3326 N THR B 194 -11.202 16.173 -5.971 1.00 12.37 N ANISOU 3326 N THR B 194 1558 1567 1577 12 -14 -14 N ATOM 3327 CA THR B 194 -10.877 17.590 -6.076 1.00 13.35 C ANISOU 3327 CA THR B 194 1714 1614 1746 14 -13 28 C ATOM 3328 C THR B 194 -10.357 18.173 -4.769 1.00 14.29 C ANISOU 3328 C THR B 194 1842 1776 1812 -12 -41 -2 C ATOM 3329 O THR B 194 -9.792 19.273 -4.762 1.00 14.72 O ANISOU 3329 O THR B 194 1915 1812 1866 -44 -34 54 O ATOM 3330 CB THR B 194 -12.074 18.443 -6.544 1.00 13.25 C ANISOU 3330 CB THR B 194 1616 1683 1736 -1 10 1 C ATOM 3331 OG1 THR B 194 -13.197 18.207 -5.683 1.00 12.65 O ANISOU 3331 OG1 THR B 194 1686 1476 1645 13 30 51 O ATOM 3332 CG2 THR B 194 -12.453 18.129 -7.980 1.00 13.93 C ANISOU 3332 CG2 THR B 194 1816 1732 1745 1 20 29 C ATOM 3333 N GLU B 195 -10.557 17.466 -3.662 1.00 14.90 N ANISOU 3333 N GLU B 195 1952 1830 1880 -27 7 36 N ATOM 3334 CA GLU B 195 -10.021 17.913 -2.376 1.00 16.11 C ANISOU 3334 CA GLU B 195 2092 2048 1982 -49 -90 42 C ATOM 3335 C GLU B 195 -9.660 16.699 -1.527 1.00 15.76 C ANISOU 3335 C GLU B 195 2030 2003 1958 -23 -21 14 C ATOM 3336 O GLU B 195 -10.455 15.766 -1.446 1.00 15.54 O ANISOU 3336 O GLU B 195 1978 1992 1934 1 -57 28 O ATOM 3337 CB GLU B 195 -11.027 18.805 -1.656 1.00 19.98 C ANISOU 3337 CB GLU B 195 2445 2468 2679 131 135 -10 C ATOM 3338 CG GLU B 195 -10.528 19.478 -0.393 1.00 24.65 C ANISOU 3338 CG GLU B 195 3191 3172 3005 -97 -123 -32 C ATOM 3339 CD GLU B 195 -11.559 20.369 0.271 1.00 28.20 C ANISOU 3339 CD GLU B 195 3524 3519 3672 69 75 -22 C ATOM 3340 OE1 GLU B 195 -12.615 20.655 -0.332 1.00 28.21 O ANISOU 3340 OE1 GLU B 195 3593 3515 3613 8 -1 18 O ATOM 3341 OE2 GLU B 195 -11.328 20.803 1.421 1.00 30.47 O ANISOU 3341 OE2 GLU B 195 3898 3855 3823 -8 -25 -46 O ATOM 3342 N ALA B 196 -8.465 16.707 -0.942 1.00 15.86 N ANISOU 3342 N ALA B 196 2036 1991 1998 -2 -39 -25 N ATOM 3343 CA ALA B 196 -7.989 15.538 -0.212 1.00 16.12 C ANISOU 3343 CA ALA B 196 2074 2031 2020 21 5 9 C ATOM 3344 C ALA B 196 -7.353 15.886 1.132 1.00 16.89 C ANISOU 3344 C ALA B 196 2170 2164 2084 0 -26 -6 C ATOM 3345 O ALA B 196 -6.494 16.750 1.233 1.00 17.82 O ANISOU 3345 O ALA B 196 2264 2290 2218 -64 -11 -22 O ATOM 3346 CB ALA B 196 -6.986 14.770 -1.065 1.00 15.52 C ANISOU 3346 CB ALA B 196 1995 1973 1929 12 -31 48 C ATOM 3347 N ALA B 197 -7.787 15.180 2.164 1.00 16.88 N ANISOU 3347 N ALA B 197 2140 2177 2095 17 -18 14 N ATOM 3348 CA ALA B 197 -7.176 15.193 3.490 1.00 16.59 C ANISOU 3348 CA ALA B 197 2117 2099 2086 5 -4 -11 C ATOM 3349 C ALA B 197 -7.413 13.821 4.114 1.00 16.50 C ANISOU 3349 C ALA B 197 2090 2101 2079 3 19 -10 C ATOM 3350 O ALA B 197 -8.202 13.034 3.593 1.00 16.03 O ANISOU 3350 O ALA B 197 2092 2063 1937 23 38 -18 O ATOM 3351 CB ALA B 197 -7.769 16.286 4.360 1.00 16.40 C ANISOU 3351 CB ALA B 197 2090 2089 2053 2 8 7 C ATOM 3352 N PRO B 198 -6.748 13.516 5.222 1.00 17.07 N ANISOU 3352 N PRO B 198 2149 2191 2147 26 -9 11 N ATOM 3353 CA PRO B 198 -6.788 12.180 5.793 1.00 17.45 C ANISOU 3353 CA PRO B 198 2223 2209 2199 -2 -6 12 C ATOM 3354 C PRO B 198 -8.189 11.670 6.058 1.00 17.57 C ANISOU 3354 C PRO B 198 2225 2241 2212 11 5 -4 C ATOM 3355 O PRO B 198 -8.513 10.524 5.720 1.00 18.51 O ANISOU 3355 O PRO B 198 2418 2282 2333 -22 1 2 O ATOM 3356 CB PRO B 198 -5.959 12.315 7.067 1.00 17.74 C ANISOU 3356 CB PRO B 198 2242 2267 2233 -13 -28 16 C ATOM 3357 CG PRO B 198 -4.959 13.372 6.731 1.00 17.89 C ANISOU 3357 CG PRO B 198 2283 2251 2263 -13 -24 26 C ATOM 3358 CD PRO B 198 -5.674 14.342 5.824 1.00 17.63 C ANISOU 3358 CD PRO B 198 2234 2224 2240 -9 -25 0 C ATOM 3359 N GLU B 199 -9.042 12.489 6.667 1.00 16.94 N ANISOU 3359 N GLU B 199 2147 2201 2087 -12 -26 19 N ATOM 3360 CA GLU B 199 -10.418 12.091 6.939 1.00 16.73 C ANISOU 3360 CA GLU B 199 2114 2150 2093 28 -20 20 C ATOM 3361 C GLU B 199 -11.411 12.985 6.211 1.00 16.44 C ANISOU 3361 C GLU B 199 2079 2118 2049 17 8 25 C ATOM 3362 O GLU B 199 -12.535 13.187 6.667 1.00 16.11 O ANISOU 3362 O GLU B 199 2023 2101 1997 10 -29 83 O ATOM 3363 CB GLU B 199 -10.673 12.084 8.448 1.00 17.74 C ANISOU 3363 CB GLU B 199 2300 2292 2147 -23 21 -3 C ATOM 3364 CG GLU B 199 -10.005 10.917 9.172 1.00 19.13 C ANISOU 3364 CG GLU B 199 2376 2391 2503 65 5 30 C ATOM 3365 CD GLU B 199 -10.075 11.105 10.678 1.00 21.89 C ANISOU 3365 CD GLU B 199 2879 2794 2644 36 -19 10 C ATOM 3366 OE1 GLU B 199 -11.072 10.658 11.277 1.00 23.84 O ANISOU 3366 OE1 GLU B 199 3011 3110 2938 -10 58 48 O ATOM 3367 OE2 GLU B 199 -9.145 11.707 11.250 1.00 23.12 O ANISOU 3367 OE2 GLU B 199 2923 2978 2885 -12 -21 -8 O ATOM 3368 N TYR B 200 -10.994 13.519 5.063 1.00 16.44 N ANISOU 3368 N TYR B 200 2085 2120 2040 15 -10 31 N ATOM 3369 CA TYR B 200 -11.892 14.369 4.278 1.00 16.23 C ANISOU 3369 CA TYR B 200 2065 2091 2011 0 -16 11 C ATOM 3370 C TYR B 200 -11.546 14.267 2.799 1.00 15.92 C ANISOU 3370 C TYR B 200 2004 2058 1988 -19 -40 14 C ATOM 3371 O TYR B 200 -10.428 14.592 2.400 1.00 16.55 O ANISOU 3371 O TYR B 200 2046 2186 2058 -68 -23 20 O ATOM 3372 CB TYR B 200 -11.802 15.814 4.760 1.00 17.12 C ANISOU 3372 CB TYR B 200 2220 2146 2137 -10 3 -15 C ATOM 3373 CG TYR B 200 -12.935 16.694 4.272 1.00 18.18 C ANISOU 3373 CG TYR B 200 2305 2291 2312 32 -34 13 C ATOM 3374 CD1 TYR B 200 -14.191 16.584 4.850 1.00 18.80 C ANISOU 3374 CD1 TYR B 200 2354 2404 2386 -1 -2 7 C ATOM 3375 CD2 TYR B 200 -12.755 17.619 3.255 1.00 18.55 C ANISOU 3375 CD2 TYR B 200 2378 2345 2326 -10 -26 17 C ATOM 3376 CE1 TYR B 200 -15.244 17.375 4.428 1.00 19.29 C ANISOU 3376 CE1 TYR B 200 2420 2437 2473 13 -7 29 C ATOM 3377 CE2 TYR B 200 -13.805 18.415 2.828 1.00 18.81 C ANISOU 3377 CE2 TYR B 200 2417 2359 2370 17 -20 -1 C ATOM 3378 CZ TYR B 200 -15.043 18.287 3.414 1.00 19.27 C ANISOU 3378 CZ TYR B 200 2440 2435 2448 -10 -7 14 C ATOM 3379 OH TYR B 200 -16.102 19.068 3.009 1.00 19.92 O ANISOU 3379 OH TYR B 200 2508 2521 2540 18 -28 28 O ATOM 3380 N LEU B 201 -12.490 13.781 2.000 1.00 15.01 N ANISOU 3380 N LEU B 201 1921 1932 1851 18 13 20 N ATOM 3381 CA LEU B 201 -12.233 13.604 0.571 1.00 14.11 C ANISOU 3381 CA LEU B 201 1741 1816 1806 11 -44 8 C ATOM 3382 C LEU B 201 -13.423 14.109 -0.233 1.00 13.42 C ANISOU 3382 C LEU B 201 1717 1718 1666 -20 -18 49 C ATOM 3383 O LEU B 201 -14.555 13.734 0.063 1.00 13.26 O ANISOU 3383 O LEU B 201 1701 1766 1571 10 -31 129 O ATOM 3384 CB LEU B 201 -11.974 12.131 0.260 1.00 14.63 C ANISOU 3384 CB LEU B 201 1842 1846 1869 62 -23 18 C ATOM 3385 CG LEU B 201 -11.475 11.811 -1.150 1.00 15.41 C ANISOU 3385 CG LEU B 201 2003 1962 1890 -4 2 22 C ATOM 3386 CD1 LEU B 201 -10.107 12.435 -1.390 1.00 15.34 C ANISOU 3386 CD1 LEU B 201 1955 1970 1903 17 -42 19 C ATOM 3387 CD2 LEU B 201 -11.419 10.307 -1.377 1.00 15.96 C ANISOU 3387 CD2 LEU B 201 2051 1988 2026 16 -11 10 C ATOM 3388 N VAL B 202 -13.180 14.959 -1.221 1.00 12.84 N ANISOU 3388 N VAL B 202 1608 1682 1591 6 -14 15 N ATOM 3389 CA VAL B 202 -14.262 15.479 -2.052 1.00 12.52 C ANISOU 3389 CA VAL B 202 1596 1629 1532 1 -20 -29 C ATOM 3390 C VAL B 202 -14.084 14.993 -3.491 1.00 11.84 C ANISOU 3390 C VAL B 202 1518 1516 1466 20 -20 45 C ATOM 3391 O VAL B 202 -12.992 15.107 -4.037 1.00 12.09 O ANISOU 3391 O VAL B 202 1522 1577 1494 21 -39 100 O ATOM 3392 CB VAL B 202 -14.316 17.014 -2.061 1.00 13.54 C ANISOU 3392 CB VAL B 202 1802 1658 1684 6 -19 -18 C ATOM 3393 CG1 VAL B 202 -15.423 17.527 -2.979 1.00 15.05 C ANISOU 3393 CG1 VAL B 202 1841 1969 1910 57 -55 18 C ATOM 3394 CG2 VAL B 202 -14.502 17.582 -0.660 1.00 13.47 C ANISOU 3394 CG2 VAL B 202 1675 1772 1672 32 40 -2 C ATOM 3395 N HIS B 203 -15.139 14.431 -4.058 1.00 11.71 N ANISOU 3395 N HIS B 203 1538 1493 1420 20 -24 36 N ATOM 3396 CA HIS B 203 -15.198 14.152 -5.489 1.00 11.52 C ANISOU 3396 CA HIS B 203 1490 1479 1408 42 -7 33 C ATOM 3397 C HIS B 203 -16.208 15.123 -6.106 1.00 11.48 C ANISOU 3397 C HIS B 203 1429 1475 1456 10 11 63 C ATOM 3398 O HIS B 203 -17.307 15.206 -5.554 1.00 11.24 O ANISOU 3398 O HIS B 203 1405 1415 1450 58 4 100 O ATOM 3399 CB HIS B 203 -15.674 12.734 -5.784 1.00 12.92 C ANISOU 3399 CB HIS B 203 1688 1578 1642 -39 7 33 C ATOM 3400 CG HIS B 203 -14.774 11.652 -5.285 1.00 13.95 C ANISOU 3400 CG HIS B 203 1774 1769 1757 44 -44 78 C ATOM 3401 ND1 HIS B 203 -14.093 10.790 -6.114 1.00 15.56 N ANISOU 3401 ND1 HIS B 203 2020 1960 1931 108 -25 -8 N ATOM 3402 CD2 HIS B 203 -14.448 11.293 -4.021 1.00 13.11 C ANISOU 3402 CD2 HIS B 203 1643 1702 1635 -21 32 -14 C ATOM 3403 CE1 HIS B 203 -13.395 9.948 -5.372 1.00 14.42 C ANISOU 3403 CE1 HIS B 203 1804 1848 1829 14 24 -5 C ATOM 3404 NE2 HIS B 203 -13.587 10.232 -4.101 1.00 13.98 N ANISOU 3404 NE2 HIS B 203 1830 1707 1774 25 -25 78 N ATOM 3405 N SER B 204 -15.830 15.840 -7.162 1.00 11.22 N ANISOU 3405 N SER B 204 1453 1425 1386 25 -37 39 N ATOM 3406 CA SER B 204 -16.775 16.838 -7.669 1.00 10.98 C ANISOU 3406 CA SER B 204 1416 1386 1369 24 -25 0 C ATOM 3407 C SER B 204 -16.526 17.152 -9.136 1.00 11.11 C ANISOU 3407 C SER B 204 1420 1412 1388 4 -2 19 C ATOM 3408 O SER B 204 -15.465 16.880 -9.694 1.00 11.11 O ANISOU 3408 O SER B 204 1451 1461 1308 -17 12 41 O ATOM 3409 CB SER B 204 -16.740 18.114 -6.827 1.00 10.84 C ANISOU 3409 CB SER B 204 1418 1342 1360 39 -21 31 C ATOM 3410 OG SER B 204 -15.515 18.808 -6.960 1.00 12.07 O ANISOU 3410 OG SER B 204 1464 1525 1598 3 -39 40 O ATOM 3411 N LYS B 205 -17.558 17.724 -9.750 1.00 11.35 N ANISOU 3411 N LYS B 205 1454 1468 1392 14 -8 44 N ATOM 3412 CA LYS B 205 -17.460 18.156 -11.143 1.00 11.15 C ANISOU 3412 CA LYS B 205 1438 1432 1366 19 -8 21 C ATOM 3413 C LYS B 205 -18.327 19.389 -11.372 1.00 11.24 C ANISOU 3413 C LYS B 205 1440 1431 1400 9 -1 24 C ATOM 3414 O LYS B 205 -19.446 19.453 -10.880 1.00 10.84 O ANISOU 3414 O LYS B 205 1417 1416 1287 23 -47 38 O ATOM 3415 CB LYS B 205 -17.895 17.012 -12.061 1.00 11.72 C ANISOU 3415 CB LYS B 205 1534 1486 1434 -24 -14 -12 C ATOM 3416 CG LYS B 205 -17.743 17.330 -13.544 1.00 11.91 C ANISOU 3416 CG LYS B 205 1500 1562 1463 -4 -5 47 C ATOM 3417 CD LYS B 205 -16.285 17.291 -13.968 1.00 12.03 C ANISOU 3417 CD LYS B 205 1504 1618 1451 -9 -12 21 C ATOM 3418 CE LYS B 205 -16.091 17.875 -15.357 1.00 11.67 C ANISOU 3418 CE LYS B 205 1495 1447 1491 -5 28 32 C ATOM 3419 NZ LYS B 205 -16.205 19.359 -15.374 1.00 10.86 N ANISOU 3419 NZ LYS B 205 1331 1421 1375 -17 -57 -9 N ATOM 3420 N THR B 206 -17.795 20.355 -12.115 1.00 11.64 N ANISOU 3420 N THR B 206 1511 1473 1438 -16 -31 68 N ATOM 3421 CA THR B 206 -18.540 21.554 -12.469 1.00 11.63 C ANISOU 3421 CA THR B 206 1478 1476 1465 9 -28 7 C ATOM 3422 C THR B 206 -19.161 21.407 -13.859 1.00 11.74 C ANISOU 3422 C THR B 206 1519 1498 1443 18 -10 7 C ATOM 3423 O THR B 206 -18.747 20.557 -14.642 1.00 11.41 O ANISOU 3423 O THR B 206 1495 1452 1390 16 -57 31 O ATOM 3424 CB THR B 206 -17.631 22.798 -12.480 1.00 12.01 C ANISOU 3424 CB THR B 206 1625 1457 1483 -11 1 -48 C ATOM 3425 OG1 THR B 206 -16.412 22.484 -13.166 1.00 12.52 O ANISOU 3425 OG1 THR B 206 1585 1598 1575 -31 -6 -15 O ATOM 3426 CG2 THR B 206 -17.308 23.268 -11.074 1.00 10.73 C ANISOU 3426 CG2 THR B 206 1413 1283 1383 -38 -23 65 C ATOM 3427 N GLY B 207 -20.156 22.240 -14.141 1.00 11.92 N ANISOU 3427 N GLY B 207 1506 1535 1489 9 -30 26 N ATOM 3428 CA GLY B 207 -20.751 22.306 -15.478 1.00 12.36 C ANISOU 3428 CA GLY B 207 1594 1587 1514 7 -37 12 C ATOM 3429 C GLY B 207 -21.261 23.726 -15.724 1.00 12.28 C ANISOU 3429 C GLY B 207 1570 1557 1538 -7 -10 -14 C ATOM 3430 O GLY B 207 -21.543 24.471 -14.791 1.00 11.80 O ANISOU 3430 O GLY B 207 1560 1542 1382 11 -48 42 O ATOM 3431 N PHE B 208 -21.236 24.159 -16.978 1.00 13.05 N ANISOU 3431 N PHE B 208 1706 1661 1590 -35 -8 0 N ATOM 3432 CA PHE B 208 -21.656 25.508 -17.349 1.00 13.56 C ANISOU 3432 CA PHE B 208 1741 1706 1705 8 -9 11 C ATOM 3433 C PHE B 208 -22.064 25.508 -18.820 1.00 14.09 C ANISOU 3433 C PHE B 208 1817 1808 1729 5 -5 37 C ATOM 3434 O PHE B 208 -21.230 25.238 -19.683 1.00 14.14 O ANISOU 3434 O PHE B 208 1860 1831 1680 30 -26 13 O ATOM 3435 CB PHE B 208 -20.539 26.511 -17.098 1.00 14.39 C ANISOU 3435 CB PHE B 208 1824 1796 1849 -35 -51 3 C ATOM 3436 CG PHE B 208 -20.749 27.918 -17.568 1.00 14.04 C ANISOU 3436 CG PHE B 208 1802 1774 1758 6 -54 -52 C ATOM 3437 CD1 PHE B 208 -21.901 28.617 -17.266 1.00 13.25 C ANISOU 3437 CD1 PHE B 208 1757 1703 1574 -13 -52 -3 C ATOM 3438 CD2 PHE B 208 -19.764 28.555 -18.311 1.00 15.45 C ANISOU 3438 CD2 PHE B 208 1965 1972 1931 -22 14 54 C ATOM 3439 CE1 PHE B 208 -22.079 29.922 -17.689 1.00 13.85 C ANISOU 3439 CE1 PHE B 208 1771 1736 1754 -1 -48 21 C ATOM 3440 CE2 PHE B 208 -19.933 29.857 -18.744 1.00 15.77 C ANISOU 3440 CE2 PHE B 208 2010 1950 2031 32 32 -16 C ATOM 3441 CZ PHE B 208 -21.093 30.538 -18.434 1.00 14.34 C ANISOU 3441 CZ PHE B 208 1867 1804 1778 -30 -20 49 C ATOM 3442 N SER B 209 -23.338 25.785 -19.084 1.00 14.48 N ANISOU 3442 N SER B 209 1844 1828 1830 -15 -20 68 N ATOM 3443 CA SER B 209 -23.855 25.615 -20.438 1.00 14.93 C ANISOU 3443 CA SER B 209 1894 1903 1876 -36 -37 17 C ATOM 3444 C SER B 209 -23.673 26.880 -21.272 1.00 15.73 C ANISOU 3444 C SER B 209 2076 1939 1960 -36 -12 34 C ATOM 3445 O SER B 209 -23.924 26.849 -22.478 1.00 16.62 O ANISOU 3445 O SER B 209 2256 2054 2004 -18 -70 39 O ATOM 3446 CB SER B 209 -25.334 25.226 -20.411 1.00 14.58 C ANISOU 3446 CB SER B 209 1853 1834 1854 36 14 -22 C ATOM 3447 OG SER B 209 -26.136 26.327 -20.038 1.00 13.43 O ANISOU 3447 OG SER B 209 1771 1665 1664 -23 -31 51 O ATOM 3448 N GLY B 210 -23.223 27.963 -20.658 1.00 15.47 N ANISOU 3448 N GLY B 210 2007 1931 1940 -5 -23 23 N ATOM 3449 CA GLY B 210 -23.136 29.253 -21.342 1.00 15.52 C ANISOU 3449 CA GLY B 210 1984 1933 1982 -19 -4 18 C ATOM 3450 C GLY B 210 -24.073 30.242 -20.657 1.00 15.61 C ANISOU 3450 C GLY B 210 1978 1990 1964 -3 -10 12 C ATOM 3451 O GLY B 210 -24.727 29.870 -19.682 1.00 15.34 O ANISOU 3451 O GLY B 210 1919 1973 1937 -6 -61 48 O ATOM 3452 N VAL B 211 -24.137 31.483 -21.136 1.00 16.23 N ANISOU 3452 N VAL B 211 2104 2030 2034 -43 -20 54 N ATOM 3453 CA VAL B 211 -24.922 32.501 -20.449 1.00 17.45 C ANISOU 3453 CA VAL B 211 2248 2192 2191 31 27 10 C ATOM 3454 C VAL B 211 -26.324 32.653 -21.028 1.00 18.46 C ANISOU 3454 C VAL B 211 2303 2336 2376 20 10 47 C ATOM 3455 O VAL B 211 -27.132 33.418 -20.500 1.00 17.77 O ANISOU 3455 O VAL B 211 2262 2235 2254 -25 -18 58 O ATOM 3456 CB VAL B 211 -24.214 33.869 -20.446 1.00 18.79 C ANISOU 3456 CB VAL B 211 2386 2314 2440 -51 -32 -21 C ATOM 3457 CG1 VAL B 211 -22.874 33.774 -19.724 1.00 18.87 C ANISOU 3457 CG1 VAL B 211 2421 2353 2397 12 -43 -5 C ATOM 3458 CG2 VAL B 211 -24.024 34.401 -21.856 1.00 19.98 C ANISOU 3458 CG2 VAL B 211 2554 2512 2524 -24 15 27 C ATOM 3459 N GLY B 212 -26.616 31.926 -22.100 1.00 20.23 N ANISOU 3459 N GLY B 212 2644 2528 2513 -35 2 -28 N ATOM 3460 CA GLY B 212 -27.923 31.999 -22.744 1.00 22.33 C ANISOU 3460 CA GLY B 212 2766 2901 2819 -12 -48 -2 C ATOM 3461 C GLY B 212 -28.318 33.455 -22.973 1.00 24.15 C ANISOU 3461 C GLY B 212 3106 2996 3074 7 -41 27 C ATOM 3462 O GLY B 212 -27.518 34.256 -23.456 1.00 24.52 O ANISOU 3462 O GLY B 212 3144 3066 3107 -10 -26 57 O ATOM 3463 N THR B 213 -29.557 33.788 -22.635 1.00 25.39 N ANISOU 3463 N THR B 213 3170 3251 3226 4 -12 13 N ATOM 3464 CA THR B 213 -30.038 35.163 -22.661 1.00 26.87 C ANISOU 3464 CA THR B 213 3408 3333 3467 22 -24 9 C ATOM 3465 C THR B 213 -30.576 35.548 -21.286 1.00 28.02 C ANISOU 3465 C THR B 213 3564 3565 3516 -7 -10 -12 C ATOM 3466 O THR B 213 -30.542 34.729 -20.364 1.00 28.35 O ANISOU 3466 O THR B 213 3636 3555 3578 -15 -8 10 O ATOM 3467 CB THR B 213 -31.169 35.365 -23.688 1.00 27.14 C ANISOU 3467 CB THR B 213 3438 3422 3452 22 -25 22 C ATOM 3468 OG1 THR B 213 -32.233 34.447 -23.389 1.00 27.37 O ANISOU 3468 OG1 THR B 213 3453 3483 3463 -2 -49 21 O ATOM 3469 CG2 THR B 213 -30.699 35.134 -25.114 1.00 27.91 C ANISOU 3469 CG2 THR B 213 3542 3542 3519 8 9 -10 C ATOM 3470 N GLU B 214 -31.101 36.761 -21.142 1.00 28.90 N ANISOU 3470 N GLU B 214 3661 3642 3677 21 -34 14 N ATOM 3471 CA GLU B 214 -31.752 37.150 -19.892 1.00 30.03 C ANISOU 3471 CA GLU B 214 3764 3917 3731 -26 2 -4 C ATOM 3472 C GLU B 214 -33.049 36.375 -19.692 1.00 29.76 C ANISOU 3472 C GLU B 214 3759 3808 3741 0 -9 2 C ATOM 3473 O GLU B 214 -33.344 35.882 -18.605 1.00 29.61 O ANISOU 3473 O GLU B 214 3732 3772 3747 1 -28 14 O ATOM 3474 CB GLU B 214 -32.007 38.655 -19.857 1.00 35.17 C ANISOU 3474 CB GLU B 214 4506 4165 4691 33 -52 60 C ATOM 3475 CG GLU B 214 -32.414 39.184 -18.491 1.00 40.54 C ANISOU 3475 CG GLU B 214 5148 5295 4961 41 39 -39 C ATOM 3476 CD GLU B 214 -32.260 40.687 -18.367 1.00 45.26 C ANISOU 3476 CD GLU B 214 5827 5562 5806 -16 -53 -9 C ATOM 3477 OE1 GLU B 214 -31.344 41.259 -18.996 1.00 46.22 O ANISOU 3477 OE1 GLU B 214 5871 5820 5872 -11 6 9 O ATOM 3478 OE2 GLU B 214 -33.056 41.308 -17.631 1.00 46.40 O ANISOU 3478 OE2 GLU B 214 5890 5856 5882 14 15 -18 O ATOM 3479 N SER B 215 -33.832 36.239 -20.760 1.00 29.35 N ANISOU 3479 N SER B 215 3717 3679 3757 -14 -5 13 N ATOM 3480 CA SER B 215 -35.093 35.513 -20.707 1.00 29.04 C ANISOU 3480 CA SER B 215 3695 3592 3747 8 32 -9 C ATOM 3481 C SER B 215 -34.887 34.007 -20.633 1.00 27.85 C ANISOU 3481 C SER B 215 3492 3533 3556 19 19 -10 C ATOM 3482 O SER B 215 -35.663 33.303 -19.981 1.00 28.02 O ANISOU 3482 O SER B 215 3523 3543 3581 10 0 16 O ATOM 3483 CB SER B 215 -35.943 35.848 -21.939 1.00 31.25 C ANISOU 3483 CB SER B 215 3959 3974 3939 -1 -98 48 C ATOM 3484 OG SER B 215 -35.308 35.341 -23.103 1.00 33.27 O ANISOU 3484 OG SER B 215 4237 4229 4175 11 30 -36 O ATOM 3485 N ASN B 216 -33.867 33.488 -21.306 1.00 26.72 N ANISOU 3485 N ASN B 216 3380 3322 3449 -6 -36 27 N ATOM 3486 CA ASN B 216 -33.547 32.068 -21.297 1.00 25.35 C ANISOU 3486 CA ASN B 216 3096 3264 3270 14 -33 41 C ATOM 3487 C ASN B 216 -32.095 31.832 -20.882 1.00 23.21 C ANISOU 3487 C ASN B 216 2981 2952 2886 -10 3 -9 C ATOM 3488 O ASN B 216 -31.215 31.582 -21.706 1.00 22.69 O ANISOU 3488 O ASN B 216 2880 2893 2847 10 -51 1 O ATOM 3489 CB ASN B 216 -33.782 31.441 -22.674 1.00 28.37 C ANISOU 3489 CB ASN B 216 3781 3556 3444 2 6 -54 C ATOM 3490 CG ASN B 216 -35.242 31.346 -23.061 1.00 32.50 C ANISOU 3490 CG ASN B 216 4006 4170 4173 -13 -48 -37 C ATOM 3491 OD1 ASN B 216 -36.035 30.695 -22.379 1.00 32.97 O ANISOU 3491 OD1 ASN B 216 4167 4172 4189 -21 -13 14 O ATOM 3492 ND2 ASN B 216 -35.603 32.009 -24.155 1.00 33.86 N ANISOU 3492 ND2 ASN B 216 4310 4258 4296 7 -35 35 N ATOM 3493 N PRO B 217 -31.839 31.943 -19.583 1.00 21.62 N ANISOU 3493 N PRO B 217 2682 2727 2807 11 -9 27 N ATOM 3494 CA PRO B 217 -30.485 31.863 -19.053 1.00 20.49 C ANISOU 3494 CA PRO B 217 2629 2533 2623 29 8 -3 C ATOM 3495 C PRO B 217 -29.847 30.502 -19.253 1.00 19.16 C ANISOU 3495 C PRO B 217 2360 2453 2467 -20 -27 26 C ATOM 3496 O PRO B 217 -30.526 29.513 -19.535 1.00 19.19 O ANISOU 3496 O PRO B 217 2350 2460 2483 -14 -49 21 O ATOM 3497 CB PRO B 217 -30.665 32.203 -17.580 1.00 20.67 C ANISOU 3497 CB PRO B 217 2649 2579 2625 29 2 -8 C ATOM 3498 CG PRO B 217 -32.043 31.751 -17.245 1.00 21.13 C ANISOU 3498 CG PRO B 217 2680 2647 2701 -3 -4 -2 C ATOM 3499 CD PRO B 217 -32.853 31.907 -18.502 1.00 21.61 C ANISOU 3499 CD PRO B 217 2721 2730 2759 21 -25 11 C ATOM 3500 N GLY B 218 -28.519 30.441 -19.151 1.00 17.46 N ANISOU 3500 N GLY B 218 2283 2128 2221 20 -16 24 N ATOM 3501 CA GLY B 218 -27.815 29.162 -19.124 1.00 15.80 C ANISOU 3501 CA GLY B 218 2037 2039 1927 -37 -10 31 C ATOM 3502 C GLY B 218 -27.924 28.547 -17.729 1.00 14.41 C ANISOU 3502 C GLY B 218 1806 1819 1852 17 -14 -13 C ATOM 3503 O GLY B 218 -28.580 29.093 -16.840 1.00 13.83 O ANISOU 3503 O GLY B 218 1722 1775 1757 19 -90 4 O ATOM 3504 N VAL B 219 -27.261 27.412 -17.549 1.00 13.43 N ANISOU 3504 N VAL B 219 1688 1764 1651 -9 -13 22 N ATOM 3505 CA VAL B 219 -27.247 26.737 -16.250 1.00 12.89 C ANISOU 3505 CA VAL B 219 1594 1662 1642 -6 -30 19 C ATOM 3506 C VAL B 219 -25.804 26.494 -15.823 1.00 12.28 C ANISOU 3506 C VAL B 219 1554 1606 1505 -3 -5 -5 C ATOM 3507 O VAL B 219 -24.932 26.284 -16.668 1.00 11.80 O ANISOU 3507 O VAL B 219 1428 1606 1451 -44 -46 88 O ATOM 3508 CB VAL B 219 -28.050 25.429 -16.300 1.00 13.04 C ANISOU 3508 CB VAL B 219 1694 1630 1630 1 0 -3 C ATOM 3509 CG1 VAL B 219 -27.444 24.446 -17.292 1.00 12.10 C ANISOU 3509 CG1 VAL B 219 1546 1582 1470 -18 -20 61 C ATOM 3510 CG2 VAL B 219 -28.154 24.789 -14.921 1.00 13.41 C ANISOU 3510 CG2 VAL B 219 1723 1725 1646 -77 -7 24 C ATOM 3511 N ALA B 220 -25.536 26.567 -14.525 1.00 11.97 N ANISOU 3511 N ALA B 220 1470 1580 1497 -36 -9 22 N ATOM 3512 CA ALA B 220 -24.228 26.199 -13.994 1.00 11.48 C ANISOU 3512 CA ALA B 220 1479 1410 1472 -20 -14 29 C ATOM 3513 C ALA B 220 -24.428 25.125 -12.921 1.00 11.61 C ANISOU 3513 C ALA B 220 1484 1483 1443 0 -9 51 C ATOM 3514 O ALA B 220 -25.405 25.189 -12.177 1.00 11.81 O ANISOU 3514 O ALA B 220 1521 1528 1439 26 -11 38 O ATOM 3515 CB ALA B 220 -23.506 27.395 -13.402 1.00 10.38 C ANISOU 3515 CB ALA B 220 1301 1381 1261 42 -13 39 C ATOM 3516 N TRP B 221 -23.511 24.176 -12.870 1.00 11.65 N ANISOU 3516 N TRP B 221 1526 1438 1461 -6 -17 38 N ATOM 3517 CA TRP B 221 -23.600 23.052 -11.960 1.00 11.24 C ANISOU 3517 CA TRP B 221 1412 1437 1421 -7 -44 38 C ATOM 3518 C TRP B 221 -22.360 22.913 -11.064 1.00 10.96 C ANISOU 3518 C TRP B 221 1381 1445 1340 -30 -14 47 C ATOM 3519 O TRP B 221 -21.242 23.239 -11.439 1.00 10.50 O ANISOU 3519 O TRP B 221 1355 1400 1233 -39 -38 55 O ATOM 3520 CB TRP B 221 -23.656 21.731 -12.712 1.00 11.46 C ANISOU 3520 CB TRP B 221 1515 1424 1415 52 1 43 C ATOM 3521 CG TRP B 221 -24.837 21.381 -13.544 1.00 13.02 C ANISOU 3521 CG TRP B 221 1613 1692 1642 -80 -37 8 C ATOM 3522 CD1 TRP B 221 -25.034 21.691 -14.860 1.00 13.71 C ANISOU 3522 CD1 TRP B 221 1785 1732 1691 3 -37 38 C ATOM 3523 CD2 TRP B 221 -25.983 20.621 -13.136 1.00 12.66 C ANISOU 3523 CD2 TRP B 221 1587 1578 1646 -22 -1 36 C ATOM 3524 NE1 TRP B 221 -26.234 21.182 -15.290 1.00 14.34 N ANISOU 3524 NE1 TRP B 221 1827 1861 1762 -78 2 39 N ATOM 3525 CE2 TRP B 221 -26.835 20.516 -14.250 1.00 13.63 C ANISOU 3525 CE2 TRP B 221 1716 1778 1687 -13 -33 28 C ATOM 3526 CE3 TRP B 221 -26.369 20.025 -11.930 1.00 12.82 C ANISOU 3526 CE3 TRP B 221 1545 1704 1622 -10 -39 42 C ATOM 3527 CZ2 TRP B 221 -28.051 19.840 -14.203 1.00 13.73 C ANISOU 3527 CZ2 TRP B 221 1747 1745 1725 -27 -18 85 C ATOM 3528 CZ3 TRP B 221 -27.577 19.351 -11.884 1.00 12.24 C ANISOU 3528 CZ3 TRP B 221 1570 1502 1580 -9 4 79 C ATOM 3529 CH2 TRP B 221 -28.406 19.267 -13.010 1.00 13.04 C ANISOU 3529 CH2 TRP B 221 1648 1675 1632 -46 -26 7 C ATOM 3530 N TRP B 222 -22.581 22.304 -9.901 1.00 10.75 N ANISOU 3530 N TRP B 222 1319 1430 1336 -13 -36 63 N ATOM 3531 CA TRP B 222 -21.473 21.666 -9.180 1.00 10.20 C ANISOU 3531 CA TRP B 222 1284 1311 1281 10 10 38 C ATOM 3532 C TRP B 222 -22.047 20.411 -8.528 1.00 10.32 C ANISOU 3532 C TRP B 222 1320 1329 1273 -16 -11 34 C ATOM 3533 O TRP B 222 -23.031 20.533 -7.796 1.00 10.48 O ANISOU 3533 O TRP B 222 1279 1415 1287 -16 -38 60 O ATOM 3534 CB TRP B 222 -20.872 22.612 -8.152 1.00 11.53 C ANISOU 3534 CB TRP B 222 1467 1418 1495 -81 -31 -26 C ATOM 3535 CG TRP B 222 -19.597 22.108 -7.537 1.00 13.15 C ANISOU 3535 CG TRP B 222 1584 1648 1764 16 -70 25 C ATOM 3536 CD1 TRP B 222 -18.533 21.552 -8.185 1.00 14.07 C ANISOU 3536 CD1 TRP B 222 1737 1815 1793 15 46 0 C ATOM 3537 CD2 TRP B 222 -19.248 22.146 -6.149 1.00 14.65 C ANISOU 3537 CD2 TRP B 222 1874 1881 1812 -5 -44 9 C ATOM 3538 NE1 TRP B 222 -17.543 21.231 -7.286 1.00 15.13 N ANISOU 3538 NE1 TRP B 222 1886 1991 1870 5 -35 30 N ATOM 3539 CE2 TRP B 222 -17.960 21.588 -6.028 1.00 15.22 C ANISOU 3539 CE2 TRP B 222 1895 1969 1918 14 17 6 C ATOM 3540 CE3 TRP B 222 -19.904 22.602 -5.002 1.00 15.34 C ANISOU 3540 CE3 TRP B 222 1969 1968 1891 -20 43 -7 C ATOM 3541 CZ2 TRP B 222 -17.314 21.468 -4.797 1.00 15.65 C ANISOU 3541 CZ2 TRP B 222 1960 2014 1971 0 -28 11 C ATOM 3542 CZ3 TRP B 222 -19.264 22.477 -3.780 1.00 16.27 C ANISOU 3542 CZ3 TRP B 222 2036 2107 2037 0 -53 23 C ATOM 3543 CH2 TRP B 222 -17.982 21.913 -3.693 1.00 15.99 C ANISOU 3543 CH2 TRP B 222 2052 2005 2020 20 -5 -4 C ATOM 3544 N VAL B 223 -21.539 19.240 -8.872 1.00 10.76 N ANISOU 3544 N VAL B 223 1368 1373 1347 8 -24 16 N ATOM 3545 CA VAL B 223 -22.082 17.982 -8.367 1.00 11.24 C ANISOU 3545 CA VAL B 223 1448 1407 1415 -12 -14 38 C ATOM 3546 C VAL B 223 -20.959 17.123 -7.784 1.00 11.67 C ANISOU 3546 C VAL B 223 1445 1518 1469 5 -18 52 C ATOM 3547 O VAL B 223 -19.808 17.283 -8.188 1.00 11.52 O ANISOU 3547 O VAL B 223 1447 1566 1363 -4 -20 64 O ATOM 3548 CB VAL B 223 -22.814 17.147 -9.431 1.00 11.57 C ANISOU 3548 CB VAL B 223 1512 1404 1478 28 6 -39 C ATOM 3549 CG1 VAL B 223 -23.974 17.895 -10.076 1.00 12.29 C ANISOU 3549 CG1 VAL B 223 1529 1638 1502 21 -29 39 C ATOM 3550 CG2 VAL B 223 -21.861 16.655 -10.512 1.00 10.50 C ANISOU 3550 CG2 VAL B 223 1312 1324 1351 32 -65 54 C ATOM 3551 N GLY B 224 -21.285 16.220 -6.858 1.00 11.91 N ANISOU 3551 N GLY B 224 1516 1520 1490 2 -18 51 N ATOM 3552 CA GLY B 224 -20.264 15.270 -6.407 1.00 11.93 C ANISOU 3552 CA GLY B 224 1520 1549 1465 25 4 40 C ATOM 3553 C GLY B 224 -20.669 14.600 -5.101 1.00 12.10 C ANISOU 3553 C GLY B 224 1514 1577 1506 10 13 68 C ATOM 3554 O GLY B 224 -21.851 14.471 -4.804 1.00 11.49 O ANISOU 3554 O GLY B 224 1478 1516 1373 -2 -33 127 O ATOM 3555 N TRP B 225 -19.664 14.207 -4.318 1.00 12.63 N ANISOU 3555 N TRP B 225 1580 1680 1538 -4 -38 58 N ATOM 3556 CA TRP B 225 -19.931 13.714 -2.971 1.00 12.61 C ANISOU 3556 CA TRP B 225 1575 1677 1539 -12 -19 33 C ATOM 3557 C TRP B 225 -18.760 14.058 -2.051 1.00 12.49 C ANISOU 3557 C TRP B 225 1548 1666 1532 13 -19 52 C ATOM 3558 O TRP B 225 -17.630 14.241 -2.496 1.00 11.69 O ANISOU 3558 O TRP B 225 1497 1626 1318 48 -82 152 O ATOM 3559 CB TRP B 225 -20.214 12.223 -2.929 1.00 14.22 C ANISOU 3559 CB TRP B 225 1862 1744 1797 -55 -18 3 C ATOM 3560 CG TRP B 225 -19.137 11.312 -3.421 1.00 15.37 C ANISOU 3560 CG TRP B 225 1889 1864 2087 20 -5 58 C ATOM 3561 CD1 TRP B 225 -18.137 10.739 -2.684 1.00 15.38 C ANISOU 3561 CD1 TRP B 225 1907 1951 1985 4 -24 34 C ATOM 3562 CD2 TRP B 225 -18.960 10.838 -4.761 1.00 18.37 C ANISOU 3562 CD2 TRP B 225 2380 2318 2282 11 81 -68 C ATOM 3563 NE1 TRP B 225 -17.349 9.952 -3.483 1.00 16.14 N ANISOU 3563 NE1 TRP B 225 2045 1950 2138 16 14 -1 N ATOM 3564 CE2 TRP B 225 -17.833 9.997 -4.766 1.00 18.06 C ANISOU 3564 CE2 TRP B 225 2347 2253 2261 -27 -63 71 C ATOM 3565 CE3 TRP B 225 -19.647 11.057 -5.962 1.00 20.89 C ANISOU 3565 CE3 TRP B 225 2659 2729 2549 6 -111 43 C ATOM 3566 CZ2 TRP B 225 -17.372 9.367 -5.920 1.00 20.11 C ANISOU 3566 CZ2 TRP B 225 2599 2521 2522 12 68 -72 C ATOM 3567 CZ3 TRP B 225 -19.186 10.433 -7.105 1.00 22.14 C ANISOU 3567 CZ3 TRP B 225 2875 2794 2744 49 -3 -9 C ATOM 3568 CH2 TRP B 225 -18.059 9.599 -7.078 1.00 21.95 C ANISOU 3568 CH2 TRP B 225 2768 2844 2729 3 -37 16 C ATOM 3569 N VAL B 226 -19.080 14.185 -0.770 1.00 12.80 N ANISOU 3569 N VAL B 226 1632 1680 1550 4 -9 21 N ATOM 3570 CA VAL B 226 -18.082 14.474 0.253 1.00 12.90 C ANISOU 3570 CA VAL B 226 1606 1685 1612 -25 -16 31 C ATOM 3571 C VAL B 226 -18.008 13.295 1.223 1.00 13.64 C ANISOU 3571 C VAL B 226 1746 1778 1659 -14 -4 61 C ATOM 3572 O VAL B 226 -19.033 12.855 1.738 1.00 13.47 O ANISOU 3572 O VAL B 226 1718 1800 1601 -16 -60 100 O ATOM 3573 CB VAL B 226 -18.415 15.747 1.047 1.00 13.95 C ANISOU 3573 CB VAL B 226 1781 1720 1799 18 -32 -3 C ATOM 3574 CG1 VAL B 226 -17.371 16.008 2.127 1.00 14.01 C ANISOU 3574 CG1 VAL B 226 1838 1722 1762 -9 -33 -4 C ATOM 3575 CG2 VAL B 226 -18.530 16.963 0.138 1.00 14.34 C ANISOU 3575 CG2 VAL B 226 1813 1827 1811 -26 22 75 C ATOM 3576 N GLU B 227 -16.800 12.789 1.437 1.00 14.47 N ANISOU 3576 N GLU B 227 1814 1903 1783 23 -31 51 N ATOM 3577 CA GLU B 227 -16.595 11.795 2.493 1.00 15.42 C ANISOU 3577 CA GLU B 227 1997 1972 1890 -33 -32 97 C ATOM 3578 C GLU B 227 -15.910 12.489 3.665 1.00 16.03 C ANISOU 3578 C GLU B 227 2035 2099 1957 -18 -52 34 C ATOM 3579 O GLU B 227 -14.787 12.974 3.514 1.00 15.90 O ANISOU 3579 O GLU B 227 2041 2161 1840 -27 -38 35 O ATOM 3580 CB GLU B 227 -15.784 10.611 1.983 1.00 17.71 C ANISOU 3580 CB GLU B 227 2255 2210 2264 105 61 53 C ATOM 3581 CG GLU B 227 -16.511 9.774 0.941 1.00 21.43 C ANISOU 3581 CG GLU B 227 2762 2734 2647 -135 -112 -29 C ATOM 3582 CD GLU B 227 -15.627 8.724 0.305 1.00 24.80 C ANISOU 3582 CD GLU B 227 3138 3108 3178 90 -17 -84 C ATOM 3583 OE1 GLU B 227 -14.748 9.073 -0.512 1.00 26.84 O ANISOU 3583 OE1 GLU B 227 3358 3372 3470 -28 65 44 O ATOM 3584 OE2 GLU B 227 -15.809 7.531 0.615 1.00 25.87 O ANISOU 3584 OE2 GLU B 227 3301 3231 3298 -15 -46 39 O ATOM 3585 N LYS B 228 -16.603 12.575 4.791 1.00 16.59 N ANISOU 3585 N LYS B 228 2083 2173 2049 5 5 39 N ATOM 3586 CA LYS B 228 -16.038 13.155 6.002 1.00 17.19 C ANISOU 3586 CA LYS B 228 2185 2230 2117 -46 -42 40 C ATOM 3587 C LYS B 228 -16.051 12.091 7.101 1.00 16.98 C ANISOU 3587 C LYS B 228 2147 2175 2129 -18 -15 26 C ATOM 3588 O LYS B 228 -17.118 11.600 7.462 1.00 16.65 O ANISOU 3588 O LYS B 228 2120 2130 2075 -2 -56 54 O ATOM 3589 CB LYS B 228 -16.809 14.388 6.461 1.00 20.01 C ANISOU 3589 CB LYS B 228 2520 2410 2673 87 77 48 C ATOM 3590 CG LYS B 228 -16.326 15.001 7.767 1.00 24.59 C ANISOU 3590 CG LYS B 228 3194 3178 2973 -112 -106 -10 C ATOM 3591 CD LYS B 228 -17.299 16.056 8.272 1.00 29.03 C ANISOU 3591 CD LYS B 228 3617 3574 3839 84 50 -17 C ATOM 3592 CE LYS B 228 -17.090 16.378 9.741 1.00 32.90 C ANISOU 3592 CE LYS B 228 4261 4174 4064 42 -7 -20 C ATOM 3593 NZ LYS B 228 -15.788 17.062 9.968 1.00 34.18 N ANISOU 3593 NZ LYS B 228 4363 4288 4337 3 -11 -3 N ATOM 3594 N GLU B 229 -14.869 11.765 7.616 1.00 17.07 N ANISOU 3594 N GLU B 229 2162 2154 2171 12 -17 27 N ATOM 3595 CA GLU B 229 -14.781 10.680 8.601 1.00 17.26 C ANISOU 3595 CA GLU B 229 2181 2113 2265 -16 -39 47 C ATOM 3596 C GLU B 229 -15.445 9.440 8.026 1.00 16.53 C ANISOU 3596 C GLU B 229 2083 2101 2098 20 -10 33 C ATOM 3597 O GLU B 229 -15.013 9.002 6.951 1.00 16.30 O ANISOU 3597 O GLU B 229 2057 2076 2061 35 6 82 O ATOM 3598 CB GLU B 229 -15.372 11.143 9.932 1.00 20.77 C ANISOU 3598 CB GLU B 229 2697 2732 2462 125 105 37 C ATOM 3599 CG GLU B 229 -14.566 12.271 10.562 1.00 25.87 C ANISOU 3599 CG GLU B 229 3272 3158 3402 -148 -143 33 C ATOM 3600 CD GLU B 229 -15.280 12.957 11.708 1.00 30.99 C ANISOU 3600 CD GLU B 229 4024 3874 3877 34 133 -95 C ATOM 3601 OE1 GLU B 229 -16.430 13.408 11.531 1.00 33.06 O ANISOU 3601 OE1 GLU B 229 4152 4171 4239 31 -2 -17 O ATOM 3602 OE2 GLU B 229 -14.682 13.048 12.801 1.00 32.98 O ANISOU 3602 OE2 GLU B 229 4226 4208 4098 7 -35 -38 O ATOM 3603 N THR B 230 -16.470 8.884 8.663 1.00 16.27 N ANISOU 3603 N THR B 230 2083 2064 2034 17 -35 51 N ATOM 3604 CA THR B 230 -17.094 7.674 8.145 1.00 16.77 C ANISOU 3604 CA THR B 230 2142 2116 2114 -6 -26 8 C ATOM 3605 C THR B 230 -18.453 7.930 7.506 1.00 16.83 C ANISOU 3605 C THR B 230 2140 2123 2132 5 -19 22 C ATOM 3606 O THR B 230 -19.185 6.974 7.231 1.00 17.38 O ANISOU 3606 O THR B 230 2220 2164 2218 -41 -49 90 O ATOM 3607 CB THR B 230 -17.269 6.595 9.234 1.00 17.87 C ANISOU 3607 CB THR B 230 2330 2213 2245 14 -23 86 C ATOM 3608 OG1 THR B 230 -17.977 7.163 10.339 1.00 19.45 O ANISOU 3608 OG1 THR B 230 2480 2521 2388 27 71 44 O ATOM 3609 CG2 THR B 230 -15.911 6.086 9.678 1.00 17.93 C ANISOU 3609 CG2 THR B 230 2292 2333 2189 5 12 57 C ATOM 3610 N GLU B 231 -18.767 9.193 7.243 1.00 16.60 N ANISOU 3610 N GLU B 231 2111 2136 2060 -5 -10 71 N ATOM 3611 CA GLU B 231 -20.022 9.524 6.577 1.00 16.67 C ANISOU 3611 CA GLU B 231 2107 2175 2051 -30 -11 88 C ATOM 3612 C GLU B 231 -19.776 9.934 5.126 1.00 15.84 C ANISOU 3612 C GLU B 231 1990 2038 1991 -11 -22 39 C ATOM 3613 O GLU B 231 -18.696 10.409 4.787 1.00 14.94 O ANISOU 3613 O GLU B 231 1924 1936 1816 13 -83 68 O ATOM 3614 CB GLU B 231 -20.769 10.647 7.298 1.00 19.34 C ANISOU 3614 CB GLU B 231 2510 2395 2441 58 74 -45 C ATOM 3615 CG GLU B 231 -22.206 10.837 6.824 1.00 21.44 C ANISOU 3615 CG GLU B 231 2680 2789 2678 62 -43 21 C ATOM 3616 CD GLU B 231 -23.031 9.569 6.908 1.00 23.27 C ANISOU 3616 CD GLU B 231 2924 2898 3020 -14 -61 -47 C ATOM 3617 OE1 GLU B 231 -23.035 8.782 5.938 1.00 22.20 O ANISOU 3617 OE1 GLU B 231 2768 2869 2796 -16 7 64 O ATOM 3618 OE2 GLU B 231 -23.676 9.332 7.952 1.00 26.10 O ANISOU 3618 OE2 GLU B 231 3298 3395 3221 -25 58 41 O ATOM 3619 N VAL B 232 -20.790 9.722 4.292 1.00 15.92 N ANISOU 3619 N VAL B 232 2008 2077 1965 -16 -22 62 N ATOM 3620 CA VAL B 232 -20.735 10.201 2.909 1.00 15.36 C ANISOU 3620 CA VAL B 232 1915 1999 1921 11 -1 37 C ATOM 3621 C VAL B 232 -21.944 11.087 2.638 1.00 15.16 C ANISOU 3621 C VAL B 232 1905 1977 1878 -6 -1 47 C ATOM 3622 O VAL B 232 -23.047 10.834 3.118 1.00 14.39 O ANISOU 3622 O VAL B 232 1817 1916 1735 62 -71 118 O ATOM 3623 CB VAL B 232 -20.648 9.054 1.894 1.00 16.39 C ANISOU 3623 CB VAL B 232 2112 2046 2068 -17 -33 -17 C ATOM 3624 CG1 VAL B 232 -21.871 8.151 1.963 1.00 16.27 C ANISOU 3624 CG1 VAL B 232 2094 2022 2064 7 -24 20 C ATOM 3625 CG2 VAL B 232 -20.473 9.600 0.480 1.00 17.17 C ANISOU 3625 CG2 VAL B 232 2209 2177 2140 -8 14 46 C ATOM 3626 N TYR B 233 -21.719 12.183 1.916 1.00 15.56 N ANISOU 3626 N TYR B 233 2011 1958 1944 9 22 40 N ATOM 3627 CA TYR B 233 -22.770 13.129 1.576 1.00 16.02 C ANISOU 3627 CA TYR B 233 2014 2097 1976 35 -6 52 C ATOM 3628 C TYR B 233 -22.792 13.330 0.060 1.00 15.30 C ANISOU 3628 C TYR B 233 1901 1980 1932 -6 -39 51 C ATOM 3629 O TYR B 233 -21.782 13.775 -0.478 1.00 15.43 O ANISOU 3629 O TYR B 233 1863 2078 1922 50 -22 70 O ATOM 3630 CB TYR B 233 -22.539 14.488 2.236 1.00 18.01 C ANISOU 3630 CB TYR B 233 2291 2176 2377 1 -2 -12 C ATOM 3631 CG TYR B 233 -22.480 14.463 3.746 1.00 20.46 C ANISOU 3631 CG TYR B 233 2696 2559 2518 -16 -6 -2 C ATOM 3632 CD1 TYR B 233 -21.279 14.263 4.413 1.00 21.69 C ANISOU 3632 CD1 TYR B 233 2737 2734 2769 10 -29 10 C ATOM 3633 CD2 TYR B 233 -23.634 14.631 4.499 1.00 21.99 C ANISOU 3633 CD2 TYR B 233 2764 2791 2801 14 49 1 C ATOM 3634 CE1 TYR B 233 -21.230 14.235 5.796 1.00 22.87 C ANISOU 3634 CE1 TYR B 233 2928 2900 2861 0 -32 20 C ATOM 3635 CE2 TYR B 233 -23.594 14.609 5.879 1.00 22.90 C ANISOU 3635 CE2 TYR B 233 2926 2906 2871 -4 31 -4 C ATOM 3636 CZ TYR B 233 -22.389 14.409 6.519 1.00 23.73 C ANISOU 3636 CZ TYR B 233 2983 3024 3010 7 4 8 C ATOM 3637 OH TYR B 233 -22.348 14.385 7.895 1.00 25.14 O ANISOU 3637 OH TYR B 233 3220 3238 3094 -7 5 9 O ATOM 3638 N PHE B 234 -23.901 13.007 -0.587 1.00 14.32 N ANISOU 3638 N PHE B 234 1854 1826 1758 -12 11 54 N ATOM 3639 CA PHE B 234 -23.999 13.234 -2.030 1.00 13.30 C ANISOU 3639 CA PHE B 234 1693 1643 1717 -7 -2 24 C ATOM 3640 C PHE B 234 -24.633 14.592 -2.289 1.00 12.69 C ANISOU 3640 C PHE B 234 1612 1615 1594 -19 25 48 C ATOM 3641 O PHE B 234 -25.524 15.003 -1.542 1.00 12.80 O ANISOU 3641 O PHE B 234 1647 1650 1567 -7 52 95 O ATOM 3642 CB PHE B 234 -24.810 12.117 -2.691 1.00 12.74 C ANISOU 3642 CB PHE B 234 1668 1649 1524 5 14 -8 C ATOM 3643 CG PHE B 234 -24.252 10.750 -2.392 1.00 13.70 C ANISOU 3643 CG PHE B 234 1754 1724 1726 29 -82 16 C ATOM 3644 CD1 PHE B 234 -23.222 10.233 -3.157 1.00 14.84 C ANISOU 3644 CD1 PHE B 234 1812 1891 1937 9 -2 -12 C ATOM 3645 CD2 PHE B 234 -24.752 10.000 -1.340 1.00 15.09 C ANISOU 3645 CD2 PHE B 234 1933 1870 1929 -38 26 54 C ATOM 3646 CE1 PHE B 234 -22.695 8.984 -2.886 1.00 15.72 C ANISOU 3646 CE1 PHE B 234 1967 1948 2059 24 16 35 C ATOM 3647 CE2 PHE B 234 -24.226 8.749 -1.065 1.00 15.49 C ANISOU 3647 CE2 PHE B 234 2053 1911 1922 16 -23 14 C ATOM 3648 CZ PHE B 234 -23.202 8.242 -1.838 1.00 15.76 C ANISOU 3648 CZ PHE B 234 1970 1998 2021 7 -21 41 C ATOM 3649 N PHE B 235 -24.168 15.305 -3.320 1.00 11.95 N ANISOU 3649 N PHE B 235 1479 1529 1534 -19 -13 17 N ATOM 3650 CA PHE B 235 -24.734 16.634 -3.549 1.00 11.86 C ANISOU 3650 CA PHE B 235 1516 1513 1477 -14 -6 14 C ATOM 3651 C PHE B 235 -24.828 16.966 -5.033 1.00 11.88 C ANISOU 3651 C PHE B 235 1521 1511 1484 -2 1 28 C ATOM 3652 O PHE B 235 -24.052 16.490 -5.856 1.00 11.85 O ANISOU 3652 O PHE B 235 1471 1562 1470 20 -26 42 O ATOM 3653 CB PHE B 235 -23.938 17.701 -2.801 1.00 11.99 C ANISOU 3653 CB PHE B 235 1529 1517 1510 -2 -11 -8 C ATOM 3654 CG PHE B 235 -22.572 18.006 -3.336 1.00 12.15 C ANISOU 3654 CG PHE B 235 1574 1478 1565 -45 31 34 C ATOM 3655 CD1 PHE B 235 -22.407 18.942 -4.344 1.00 12.20 C ANISOU 3655 CD1 PHE B 235 1611 1606 1419 -5 -49 38 C ATOM 3656 CD2 PHE B 235 -21.440 17.391 -2.826 1.00 13.47 C ANISOU 3656 CD2 PHE B 235 1708 1767 1643 14 -54 46 C ATOM 3657 CE1 PHE B 235 -21.155 19.245 -4.838 1.00 13.36 C ANISOU 3657 CE1 PHE B 235 1682 1755 1641 -23 17 21 C ATOM 3658 CE2 PHE B 235 -20.184 17.688 -3.314 1.00 14.43 C ANISOU 3658 CE2 PHE B 235 1768 1839 1875 31 14 37 C ATOM 3659 CZ PHE B 235 -20.036 18.616 -4.331 1.00 14.62 C ANISOU 3659 CZ PHE B 235 1807 1885 1863 56 -11 46 C ATOM 3660 N ALA B 236 -25.823 17.786 -5.349 1.00 11.91 N ANISOU 3660 N ALA B 236 1515 1558 1453 6 -17 48 N ATOM 3661 CA ALA B 236 -25.898 18.413 -6.667 1.00 11.59 C ANISOU 3661 CA ALA B 236 1521 1466 1416 -20 -34 3 C ATOM 3662 C ALA B 236 -26.451 19.829 -6.536 1.00 11.60 C ANISOU 3662 C ALA B 236 1502 1475 1430 -4 -13 22 C ATOM 3663 O ALA B 236 -27.452 20.086 -5.873 1.00 12.02 O ANISOU 3663 O ALA B 236 1513 1599 1453 11 -2 101 O ATOM 3664 CB ALA B 236 -26.767 17.592 -7.606 1.00 10.71 C ANISOU 3664 CB ALA B 236 1290 1367 1414 10 -18 41 C ATOM 3665 N PHE B 237 -25.764 20.762 -7.184 1.00 11.66 N ANISOU 3665 N PHE B 237 1494 1460 1477 -23 -27 16 N ATOM 3666 CA PHE B 237 -26.177 22.154 -7.210 1.00 11.84 C ANISOU 3666 CA PHE B 237 1519 1491 1488 10 -17 0 C ATOM 3667 C PHE B 237 -26.335 22.607 -8.662 1.00 12.15 C ANISOU 3667 C PHE B 237 1550 1549 1517 -13 -6 35 C ATOM 3668 O PHE B 237 -25.474 22.285 -9.480 1.00 12.14 O ANISOU 3668 O PHE B 237 1517 1569 1528 -6 -29 30 O ATOM 3669 CB PHE B 237 -25.132 23.036 -6.521 1.00 11.63 C ANISOU 3669 CB PHE B 237 1441 1524 1453 -22 23 31 C ATOM 3670 CG PHE B 237 -25.484 24.498 -6.514 1.00 13.34 C ANISOU 3670 CG PHE B 237 1685 1619 1763 9 -4 22 C ATOM 3671 CD1 PHE B 237 -26.291 25.017 -5.516 1.00 14.06 C ANISOU 3671 CD1 PHE B 237 1775 1806 1761 10 -6 -19 C ATOM 3672 CD2 PHE B 237 -25.010 25.349 -7.500 1.00 12.93 C ANISOU 3672 CD2 PHE B 237 1580 1633 1700 -8 -48 24 C ATOM 3673 CE1 PHE B 237 -26.622 26.355 -5.499 1.00 14.10 C ANISOU 3673 CE1 PHE B 237 1799 1785 1775 -34 -11 -6 C ATOM 3674 CE2 PHE B 237 -25.340 26.692 -7.484 1.00 13.42 C ANISOU 3674 CE2 PHE B 237 1710 1666 1724 12 -28 3 C ATOM 3675 CZ PHE B 237 -26.148 27.193 -6.488 1.00 13.55 C ANISOU 3675 CZ PHE B 237 1706 1747 1695 19 -50 -2 C ATOM 3676 N ASN B 238 -27.421 23.318 -8.949 1.00 12.46 N ANISOU 3676 N ASN B 238 1596 1561 1577 0 -27 49 N ATOM 3677 CA ASN B 238 -27.464 24.055 -10.214 1.00 12.43 C ANISOU 3677 CA ASN B 238 1607 1579 1538 -36 -21 23 C ATOM 3678 C ASN B 238 -28.084 25.427 -9.987 1.00 12.65 C ANISOU 3678 C ASN B 238 1590 1629 1587 -10 -20 5 C ATOM 3679 O ASN B 238 -28.738 25.685 -8.976 1.00 12.55 O ANISOU 3679 O ASN B 238 1550 1638 1579 22 -37 42 O ATOM 3680 CB ASN B 238 -28.151 23.295 -11.337 1.00 11.71 C ANISOU 3680 CB ASN B 238 1523 1440 1485 -26 15 61 C ATOM 3681 CG ASN B 238 -29.623 23.022 -11.143 1.00 11.78 C ANISOU 3681 CG ASN B 238 1493 1514 1471 3 -50 -6 C ATOM 3682 OD1 ASN B 238 -30.433 23.934 -10.963 1.00 11.98 O ANISOU 3682 OD1 ASN B 238 1509 1525 1519 3 -2 71 O ATOM 3683 ND2 ASN B 238 -29.987 21.742 -11.194 1.00 12.76 N ANISOU 3683 ND2 ASN B 238 1615 1575 1657 -61 -46 76 N ATOM 3684 N MET B 239 -27.823 26.318 -10.939 1.00 12.61 N ANISOU 3684 N MET B 239 1570 1608 1613 -20 -44 14 N ATOM 3685 CA MET B 239 -28.332 27.677 -10.864 1.00 12.94 C ANISOU 3685 CA MET B 239 1629 1628 1661 -9 -16 9 C ATOM 3686 C MET B 239 -28.533 28.244 -12.266 1.00 13.29 C ANISOU 3686 C MET B 239 1669 1728 1652 -5 -16 0 C ATOM 3687 O MET B 239 -27.817 27.873 -13.194 1.00 13.14 O ANISOU 3687 O MET B 239 1680 1708 1603 23 -28 40 O ATOM 3688 CB MET B 239 -27.358 28.581 -10.102 1.00 12.35 C ANISOU 3688 CB MET B 239 1645 1536 1513 7 -17 51 C ATOM 3689 CG MET B 239 -25.959 28.582 -10.705 1.00 13.57 C ANISOU 3689 CG MET B 239 1707 1744 1707 10 30 61 C ATOM 3690 SD MET B 239 -24.824 29.673 -9.829 1.00 15.75 S ANISOU 3690 SD MET B 239 2073 2012 1898 -215 -172 146 S ATOM 3691 CE MET B 239 -25.508 31.280 -10.217 1.00 18.56 C ANISOU 3691 CE MET B 239 2392 2211 2450 62 -51 34 C ATOM 3692 N ASP B 240 -29.506 29.142 -12.376 1.00 13.91 N ANISOU 3692 N ASP B 240 1743 1741 1800 11 3 27 N ATOM 3693 CA ASP B 240 -29.634 29.940 -13.591 1.00 14.48 C ANISOU 3693 CA ASP B 240 1853 1847 1802 -13 -4 42 C ATOM 3694 C ASP B 240 -28.445 30.897 -13.680 1.00 14.73 C ANISOU 3694 C ASP B 240 1892 1823 1881 -5 -23 36 C ATOM 3695 O ASP B 240 -28.054 31.500 -12.683 1.00 14.83 O ANISOU 3695 O ASP B 240 1957 1850 1828 -11 -31 92 O ATOM 3696 CB ASP B 240 -30.930 30.740 -13.598 1.00 15.58 C ANISOU 3696 CB ASP B 240 1988 1940 1994 77 -31 18 C ATOM 3697 CG ASP B 240 -32.171 29.881 -13.716 1.00 16.71 C ANISOU 3697 CG ASP B 240 2164 2097 2089 -65 -8 28 C ATOM 3698 OD1 ASP B 240 -32.064 28.703 -14.109 1.00 16.44 O ANISOU 3698 OD1 ASP B 240 2099 2058 2089 -49 -67 71 O ATOM 3699 OD2 ASP B 240 -33.267 30.403 -13.414 1.00 19.30 O ANISOU 3699 OD2 ASP B 240 2287 2505 2543 45 21 56 O ATOM 3700 N ILE B 241 -27.912 31.025 -14.893 1.00 15.07 N ANISOU 3700 N ILE B 241 1921 1916 1888 40 -32 36 N ATOM 3701 CA ILE B 241 -26.793 31.946 -15.086 1.00 16.36 C ANISOU 3701 CA ILE B 241 2084 2058 2075 -42 29 24 C ATOM 3702 C ILE B 241 -26.892 32.647 -16.437 1.00 16.88 C ANISOU 3702 C ILE B 241 2147 2155 2111 -5 -1 45 C ATOM 3703 O ILE B 241 -27.027 32.012 -17.474 1.00 16.87 O ANISOU 3703 O ILE B 241 2179 2136 2096 -8 -6 71 O ATOM 3704 CB ILE B 241 -25.442 31.244 -14.899 1.00 17.28 C ANISOU 3704 CB ILE B 241 2168 2253 2146 23 -15 37 C ATOM 3705 CG1 ILE B 241 -24.299 32.264 -14.992 1.00 17.63 C ANISOU 3705 CG1 ILE B 241 2234 2244 2221 4 40 18 C ATOM 3706 CG2 ILE B 241 -25.213 30.115 -15.887 1.00 17.37 C ANISOU 3706 CG2 ILE B 241 2176 2229 2195 -31 -11 27 C ATOM 3707 CD1 ILE B 241 -22.985 31.753 -14.433 1.00 17.83 C ANISOU 3707 CD1 ILE B 241 2265 2311 2199 2 19 53 C ATOM 3708 N ASP B 242 -26.849 33.978 -16.376 1.00 17.47 N ANISOU 3708 N ASP B 242 2222 2189 2227 -17 1 14 N ATOM 3709 CA ASP B 242 -26.848 34.796 -17.586 1.00 18.05 C ANISOU 3709 CA ASP B 242 2327 2273 2256 -15 -18 34 C ATOM 3710 C ASP B 242 -25.632 35.714 -17.641 1.00 18.37 C ANISOU 3710 C ASP B 242 2344 2320 2316 -28 -27 30 C ATOM 3711 O ASP B 242 -25.521 36.562 -18.532 1.00 18.69 O ANISOU 3711 O ASP B 242 2390 2356 2356 -61 -23 57 O ATOM 3712 CB ASP B 242 -28.131 35.607 -17.710 1.00 18.86 C ANISOU 3712 CB ASP B 242 2350 2398 2419 5 -38 38 C ATOM 3713 CG ASP B 242 -28.332 36.749 -16.749 1.00 20.36 C ANISOU 3713 CG ASP B 242 2676 2528 2533 -25 4 -14 C ATOM 3714 OD1 ASP B 242 -27.403 37.166 -16.029 1.00 20.37 O ANISOU 3714 OD1 ASP B 242 2656 2517 2566 -24 -7 26 O ATOM 3715 OD2 ASP B 242 -29.466 37.286 -16.702 1.00 22.42 O ANISOU 3715 OD2 ASP B 242 2779 2806 2932 18 -14 -10 O ATOM 3716 N ASN B 243 -24.729 35.581 -16.679 1.00 18.29 N ANISOU 3716 N ASN B 243 2320 2297 2331 -38 -24 35 N ATOM 3717 CA ASN B 243 -23.500 36.371 -16.678 1.00 17.86 C ANISOU 3717 CA ASN B 243 2255 2271 2259 4 -16 40 C ATOM 3718 C ASN B 243 -22.350 35.524 -16.157 1.00 17.34 C ANISOU 3718 C ASN B 243 2220 2191 2175 -27 -14 15 C ATOM 3719 O ASN B 243 -22.444 34.977 -15.053 1.00 17.09 O ANISOU 3719 O ASN B 243 2221 2156 2115 -42 -37 -20 O ATOM 3720 CB ASN B 243 -23.673 37.627 -15.827 1.00 18.80 C ANISOU 3720 CB ASN B 243 2450 2372 2323 37 -27 -5 C ATOM 3721 CG ASN B 243 -22.613 38.674 -16.107 1.00 20.51 C ANISOU 3721 CG ASN B 243 2571 2575 2648 -58 -7 -11 C ATOM 3722 OD1 ASN B 243 -21.416 38.410 -16.006 1.00 20.17 O ANISOU 3722 OD1 ASN B 243 2572 2497 2595 -26 -6 59 O ATOM 3723 ND2 ASN B 243 -23.063 39.870 -16.474 1.00 21.66 N ANISOU 3723 ND2 ASN B 243 2860 2660 2709 8 3 21 N ATOM 3724 N GLU B 244 -21.248 35.450 -16.897 1.00 17.20 N ANISOU 3724 N GLU B 244 2214 2174 2148 -31 -41 -22 N ATOM 3725 CA GLU B 244 -20.100 34.646 -16.509 1.00 17.99 C ANISOU 3725 CA GLU B 244 2329 2177 2329 -1 -126 -1 C ATOM 3726 C GLU B 244 -19.454 35.087 -15.203 1.00 17.30 C ANISOU 3726 C GLU B 244 2225 2129 2218 2 -11 2 C ATOM 3727 O GLU B 244 -18.792 34.283 -14.535 1.00 17.32 O ANISOU 3727 O GLU B 244 2203 2148 2229 -14 -10 16 O ATOM 3728 CB GLU B 244 -19.023 34.628 -17.600 1.00 23.32 C ANISOU 3728 CB GLU B 244 2798 3142 2922 6 194 127 C ATOM 3729 CG GLU B 244 -19.189 33.544 -18.648 1.00 29.60 C ANISOU 3729 CG GLU B 244 3965 3579 3703 -67 -110 -117 C ATOM 3730 CD GLU B 244 -17.912 33.237 -19.403 1.00 34.18 C ANISOU 3730 CD GLU B 244 4267 4309 4412 30 126 -7 C ATOM 3731 OE1 GLU B 244 -16.830 33.171 -18.783 1.00 35.38 O ANISOU 3731 OE1 GLU B 244 4454 4518 4470 9 -10 -3 O ATOM 3732 OE2 GLU B 244 -17.983 33.053 -20.636 1.00 36.24 O ANISOU 3732 OE2 GLU B 244 4633 4590 4544 -7 -15 -12 O ATOM 3733 N SER B 245 -19.648 36.330 -14.781 1.00 16.64 N ANISOU 3733 N SER B 245 2151 2094 2077 -31 -17 30 N ATOM 3734 CA SER B 245 -19.124 36.833 -13.524 1.00 16.32 C ANISOU 3734 CA SER B 245 2088 2081 2030 -21 9 33 C ATOM 3735 C SER B 245 -19.725 36.143 -12.304 1.00 15.57 C ANISOU 3735 C SER B 245 1946 1988 1984 -33 -24 7 C ATOM 3736 O SER B 245 -19.067 36.059 -11.264 1.00 15.66 O ANISOU 3736 O SER B 245 1959 1991 2000 -24 -50 -5 O ATOM 3737 CB ASER B 245 -19.365 38.343 -13.411 0.50 17.50 C ANISOU 3737 CB ASER B 245 2249 2159 2242 18 -20 0 C ATOM 3738 CB BSER B 245 -19.351 38.344 -13.413 0.50 17.34 C ANISOU 3738 CB BSER B 245 2235 2149 2206 4 -12 12 C ATOM 3739 OG ASER B 245 -18.568 39.048 -14.342 0.50 18.30 O ANISOU 3739 OG ASER B 245 2313 2319 2322 -29 22 7 O ATOM 3740 OG BSER B 245 -20.715 38.606 -13.132 0.50 17.92 O ANISOU 3740 OG BSER B 245 2274 2214 2322 6 1 -8 O ATOM 3741 N LYS B 246 -20.925 35.595 -12.406 1.00 14.77 N ANISOU 3741 N LYS B 246 1875 1903 1834 -2 -9 30 N ATOM 3742 CA LYS B 246 -21.601 34.889 -11.331 1.00 14.41 C ANISOU 3742 CA LYS B 246 1860 1834 1781 -4 -34 11 C ATOM 3743 C LYS B 246 -21.174 33.443 -11.154 1.00 14.47 C ANISOU 3743 C LYS B 246 1820 1855 1825 7 -21 6 C ATOM 3744 O LYS B 246 -21.605 32.738 -10.237 1.00 15.15 O ANISOU 3744 O LYS B 246 1901 1926 1931 -52 -30 69 O ATOM 3745 CB LYS B 246 -23.115 34.895 -11.607 1.00 15.61 C ANISOU 3745 CB LYS B 246 1897 2049 1985 -45 -7 25 C ATOM 3746 CG LYS B 246 -23.724 36.283 -11.643 1.00 17.46 C ANISOU 3746 CG LYS B 246 2223 2153 2256 25 -41 41 C ATOM 3747 CD LYS B 246 -24.277 36.675 -10.285 1.00 19.50 C ANISOU 3747 CD LYS B 246 2489 2528 2393 -30 6 -53 C ATOM 3748 CE LYS B 246 -25.061 37.978 -10.352 1.00 21.46 C ANISOU 3748 CE LYS B 246 2748 2633 2774 18 -27 2 C ATOM 3749 NZ LYS B 246 -25.621 38.318 -9.011 1.00 22.66 N ANISOU 3749 NZ LYS B 246 2897 2837 2875 2 44 -17 N ATOM 3750 N LEU B 247 -20.273 32.970 -11.996 1.00 14.04 N ANISOU 3750 N LEU B 247 1818 1764 1751 -11 -53 11 N ATOM 3751 CA LEU B 247 -19.853 31.584 -12.070 1.00 14.37 C ANISOU 3751 CA LEU B 247 1860 1781 1821 -2 -94 31 C ATOM 3752 C LEU B 247 -19.393 30.957 -10.775 1.00 13.63 C ANISOU 3752 C LEU B 247 1767 1679 1734 -46 -37 -2 C ATOM 3753 O LEU B 247 -19.846 29.854 -10.424 1.00 13.09 O ANISOU 3753 O LEU B 247 1698 1672 1602 -15 -38 32 O ATOM 3754 CB LEU B 247 -18.809 31.518 -13.194 1.00 18.08 C ANISOU 3754 CB LEU B 247 2189 2509 2171 -2 104 68 C ATOM 3755 CG LEU B 247 -18.641 30.205 -13.945 1.00 22.19 C ANISOU 3755 CG LEU B 247 2851 2716 2866 -31 26 -99 C ATOM 3756 CD1 LEU B 247 -17.985 29.224 -12.995 1.00 24.45 C ANISOU 3756 CD1 LEU B 247 3120 3034 3134 47 -62 27 C ATOM 3757 CD2 LEU B 247 -19.949 29.630 -14.463 1.00 21.91 C ANISOU 3757 CD2 LEU B 247 2817 2746 2763 -5 -26 -5 C ATOM 3758 N PRO B 248 -18.561 31.609 -9.963 1.00 13.33 N ANISOU 3758 N PRO B 248 1721 1691 1655 -21 -20 21 N ATOM 3759 CA PRO B 248 -18.025 31.016 -8.752 1.00 12.85 C ANISOU 3759 CA PRO B 248 1647 1617 1619 -34 -1 -2 C ATOM 3760 C PRO B 248 -19.063 30.678 -7.699 1.00 12.29 C ANISOU 3760 C PRO B 248 1582 1536 1553 -14 -41 -7 C ATOM 3761 O PRO B 248 -18.826 29.866 -6.800 1.00 12.07 O ANISOU 3761 O PRO B 248 1603 1451 1532 -60 -86 -32 O ATOM 3762 CB PRO B 248 -17.017 32.027 -8.219 1.00 13.16 C ANISOU 3762 CB PRO B 248 1694 1647 1657 -45 -30 -11 C ATOM 3763 CG PRO B 248 -17.113 33.226 -9.085 1.00 13.59 C ANISOU 3763 CG PRO B 248 1789 1659 1717 -17 -39 -1 C ATOM 3764 CD PRO B 248 -17.801 32.823 -10.358 1.00 13.69 C ANISOU 3764 CD PRO B 248 1792 1688 1720 -37 -42 5 C ATOM 3765 N LEU B 249 -20.248 31.279 -7.761 1.00 12.23 N ANISOU 3765 N LEU B 249 1579 1553 1514 5 -11 -10 N ATOM 3766 CA LEU B 249 -21.376 30.986 -6.897 1.00 12.47 C ANISOU 3766 CA LEU B 249 1555 1598 1584 -8 -15 2 C ATOM 3767 C LEU B 249 -21.851 29.547 -6.993 1.00 12.39 C ANISOU 3767 C LEU B 249 1579 1589 1541 -9 -26 -13 C ATOM 3768 O LEU B 249 -22.423 29.009 -6.034 1.00 13.11 O ANISOU 3768 O LEU B 249 1691 1743 1547 -26 -14 -15 O ATOM 3769 CB LEU B 249 -22.538 31.945 -7.204 1.00 12.97 C ANISOU 3769 CB LEU B 249 1645 1607 1675 42 -1 2 C ATOM 3770 CG LEU B 249 -22.270 33.431 -6.944 1.00 13.91 C ANISOU 3770 CG LEU B 249 1818 1650 1818 34 -27 3 C ATOM 3771 CD1 LEU B 249 -23.368 34.308 -7.529 1.00 13.45 C ANISOU 3771 CD1 LEU B 249 1683 1709 1717 -25 -47 -29 C ATOM 3772 CD2 LEU B 249 -22.120 33.688 -5.451 1.00 15.64 C ANISOU 3772 CD2 LEU B 249 2060 1962 1919 6 -29 -34 C ATOM 3773 N ARG B 250 -21.592 28.843 -8.100 1.00 12.15 N ANISOU 3773 N ARG B 250 1578 1536 1503 4 -25 33 N ATOM 3774 CA ARG B 250 -21.903 27.430 -8.219 1.00 12.23 C ANISOU 3774 CA ARG B 250 1601 1554 1490 -3 -16 -12 C ATOM 3775 C ARG B 250 -21.120 26.587 -7.215 1.00 12.60 C ANISOU 3775 C ARG B 250 1620 1583 1583 19 -30 12 C ATOM 3776 O ARG B 250 -21.580 25.490 -6.886 1.00 13.58 O ANISOU 3776 O ARG B 250 1765 1669 1724 -45 -8 41 O ATOM 3777 CB ARG B 250 -21.642 26.908 -9.634 1.00 11.82 C ANISOU 3777 CB ARG B 250 1454 1562 1474 5 -12 -4 C ATOM 3778 CG ARG B 250 -20.174 26.878 -10.027 1.00 11.39 C ANISOU 3778 CG ARG B 250 1444 1490 1394 3 12 -26 C ATOM 3779 CD ARG B 250 -20.000 26.500 -11.492 1.00 11.15 C ANISOU 3779 CD ARG B 250 1433 1421 1384 14 -20 -13 C ATOM 3780 NE ARG B 250 -18.597 26.499 -11.885 1.00 11.32 N ANISOU 3780 NE ARG B 250 1462 1403 1437 -18 9 48 N ATOM 3781 CZ ARG B 250 -18.134 26.104 -13.066 1.00 12.24 C ANISOU 3781 CZ ARG B 250 1573 1602 1475 0 -28 -35 C ATOM 3782 NH1 ARG B 250 -18.963 25.683 -14.011 1.00 11.53 N ANISOU 3782 NH1 ARG B 250 1494 1441 1445 0 -52 50 N ATOM 3783 NH2 ARG B 250 -16.826 26.175 -13.301 1.00 13.12 N ANISOU 3783 NH2 ARG B 250 1610 1733 1640 -16 -26 0 N ATOM 3784 N LYS B 251 -19.959 27.048 -6.761 1.00 12.60 N ANISOU 3784 N LYS B 251 1628 1584 1574 7 -22 15 N ATOM 3785 CA LYS B 251 -19.259 26.357 -5.684 1.00 12.93 C ANISOU 3785 CA LYS B 251 1708 1623 1582 14 -43 26 C ATOM 3786 C LYS B 251 -19.498 27.008 -4.326 1.00 13.06 C ANISOU 3786 C LYS B 251 1694 1649 1619 -5 -20 -3 C ATOM 3787 O LYS B 251 -19.632 26.281 -3.333 1.00 13.40 O ANISOU 3787 O LYS B 251 1770 1697 1626 -61 -32 6 O ATOM 3788 CB LYS B 251 -17.759 26.287 -5.957 1.00 15.29 C ANISOU 3788 CB LYS B 251 1817 1996 1995 -22 37 74 C ATOM 3789 CG LYS B 251 -17.366 25.332 -7.073 1.00 18.05 C ANISOU 3789 CG LYS B 251 2443 2227 2187 -16 -2 -69 C ATOM 3790 CD LYS B 251 -15.848 25.172 -7.106 1.00 22.75 C ANISOU 3790 CD LYS B 251 2698 2959 2987 10 -12 79 C ATOM 3791 CE LYS B 251 -15.425 24.234 -8.224 1.00 26.39 C ANISOU 3791 CE LYS B 251 3446 3270 3312 19 26 -79 C ATOM 3792 NZ LYS B 251 -13.942 24.158 -8.348 1.00 28.88 N ANISOU 3792 NZ LYS B 251 3578 3649 3748 11 -4 8 N ATOM 3793 N SER B 252 -19.551 28.335 -4.273 1.00 12.89 N ANISOU 3793 N SER B 252 1608 1649 1639 15 -27 6 N ATOM 3794 CA SER B 252 -19.604 29.012 -2.977 1.00 13.57 C ANISOU 3794 CA SER B 252 1749 1734 1673 3 -12 -11 C ATOM 3795 C SER B 252 -20.933 28.815 -2.263 1.00 14.07 C ANISOU 3795 C SER B 252 1773 1811 1762 -6 3 0 C ATOM 3796 O SER B 252 -20.924 28.557 -1.053 1.00 14.47 O ANISOU 3796 O SER B 252 1856 1866 1775 8 19 -10 O ATOM 3797 CB SER B 252 -19.240 30.488 -3.097 1.00 14.28 C ANISOU 3797 CB SER B 252 1819 1753 1855 -3 -17 -22 C ATOM 3798 OG SER B 252 -20.164 31.230 -3.862 1.00 14.98 O ANISOU 3798 OG SER B 252 1948 1872 1872 8 -53 50 O ATOM 3799 N ILE B 253 -22.056 28.856 -2.974 1.00 14.35 N ANISOU 3799 N ILE B 253 1786 1857 1809 16 -8 35 N ATOM 3800 CA ILE B 253 -23.354 28.660 -2.330 1.00 14.25 C ANISOU 3800 CA ILE B 253 1780 1835 1801 -7 -26 -2 C ATOM 3801 C ILE B 253 -23.470 27.289 -1.690 1.00 14.52 C ANISOU 3801 C ILE B 253 1835 1848 1835 4 -26 6 C ATOM 3802 O ILE B 253 -23.773 27.186 -0.495 1.00 15.09 O ANISOU 3802 O ILE B 253 1889 1979 1864 8 -17 3 O ATOM 3803 CB ILE B 253 -24.521 28.977 -3.283 1.00 13.76 C ANISOU 3803 CB ILE B 253 1711 1722 1796 1 18 15 C ATOM 3804 CG1 ILE B 253 -24.515 30.478 -3.590 1.00 13.12 C ANISOU 3804 CG1 ILE B 253 1673 1682 1631 -7 16 -26 C ATOM 3805 CG2 ILE B 253 -25.852 28.557 -2.675 1.00 12.95 C ANISOU 3805 CG2 ILE B 253 1674 1655 1592 1 -26 8 C ATOM 3806 CD1 ILE B 253 -25.525 30.940 -4.614 1.00 13.60 C ANISOU 3806 CD1 ILE B 253 1733 1746 1689 9 14 45 C ATOM 3807 N PRO B 254 -23.215 26.219 -2.439 1.00 14.38 N ANISOU 3807 N PRO B 254 1821 1831 1811 1 -13 19 N ATOM 3808 CA PRO B 254 -23.275 24.870 -1.904 1.00 14.81 C ANISOU 3808 CA PRO B 254 1904 1832 1889 7 -9 2 C ATOM 3809 C PRO B 254 -22.242 24.611 -0.822 1.00 15.38 C ANISOU 3809 C PRO B 254 1956 1958 1929 6 -29 7 C ATOM 3810 O PRO B 254 -22.514 23.881 0.138 1.00 15.77 O ANISOU 3810 O PRO B 254 2002 1994 1996 -9 -10 40 O ATOM 3811 CB PRO B 254 -23.077 23.951 -3.097 1.00 14.78 C ANISOU 3811 CB PRO B 254 1930 1835 1850 -4 -8 23 C ATOM 3812 CG PRO B 254 -22.767 24.812 -4.259 1.00 14.49 C ANISOU 3812 CG PRO B 254 1858 1797 1852 -6 6 18 C ATOM 3813 CD PRO B 254 -23.176 26.217 -3.920 1.00 14.36 C ANISOU 3813 CD PRO B 254 1839 1808 1809 -2 -4 -16 C ATOM 3814 N THR B 255 -21.054 25.198 -0.956 1.00 15.84 N ANISOU 3814 N THR B 255 1981 2012 2023 -6 -17 14 N ATOM 3815 CA THR B 255 -20.025 25.033 0.074 1.00 16.24 C ANISOU 3815 CA THR B 255 2034 2083 2054 -6 -44 4 C ATOM 3816 C THR B 255 -20.490 25.672 1.375 1.00 16.82 C ANISOU 3816 C THR B 255 2136 2161 2094 -8 -17 -10 C ATOM 3817 O THR B 255 -20.416 25.034 2.429 1.00 16.95 O ANISOU 3817 O THR B 255 2168 2154 2119 -22 10 16 O ATOM 3818 CB THR B 255 -18.670 25.588 -0.382 1.00 16.29 C ANISOU 3818 CB THR B 255 2083 2059 2047 -2 33 -26 C ATOM 3819 OG1 THR B 255 -18.214 24.847 -1.525 1.00 15.40 O ANISOU 3819 OG1 THR B 255 1940 1963 1947 -9 -45 19 O ATOM 3820 CG2 THR B 255 -17.620 25.469 0.713 1.00 17.82 C ANISOU 3820 CG2 THR B 255 2235 2295 2240 12 -70 19 C ATOM 3821 N LYS B 256 -21.029 26.889 1.305 1.00 17.24 N ANISOU 3821 N LYS B 256 2184 2193 2174 0 -22 -17 N ATOM 3822 CA LYS B 256 -21.559 27.544 2.499 1.00 17.96 C ANISOU 3822 CA LYS B 256 2250 2363 2212 -14 15 -37 C ATOM 3823 C LYS B 256 -22.696 26.745 3.121 1.00 18.03 C ANISOU 3823 C LYS B 256 2256 2331 2263 -6 0 -8 C ATOM 3824 O LYS B 256 -22.731 26.594 4.347 1.00 18.22 O ANISOU 3824 O LYS B 256 2260 2389 2273 1 -29 -12 O ATOM 3825 CB LYS B 256 -21.997 28.979 2.203 1.00 20.70 C ANISOU 3825 CB LYS B 256 2779 2535 2549 122 -33 -12 C ATOM 3826 CG LYS B 256 -20.835 29.900 1.850 1.00 24.70 C ANISOU 3826 CG LYS B 256 3060 3270 3055 -166 27 -11 C ATOM 3827 CD LYS B 256 -21.275 31.353 1.798 1.00 30.43 C ANISOU 3827 CD LYS B 256 3992 3710 3859 152 -51 -6 C ATOM 3828 CE LYS B 256 -20.109 32.277 1.483 1.00 34.41 C ANISOU 3828 CE LYS B 256 4285 4416 4372 -107 24 19 C ATOM 3829 NZ LYS B 256 -20.503 33.714 1.559 1.00 36.69 N ANISOU 3829 NZ LYS B 256 4682 4580 4680 5 0 15 N ATOM 3830 N ILE B 257 -23.619 26.219 2.317 1.00 17.94 N ANISOU 3830 N ILE B 257 2279 2289 2249 1 -4 -15 N ATOM 3831 CA ILE B 257 -24.659 25.341 2.845 1.00 18.27 C ANISOU 3831 CA ILE B 257 2322 2313 2306 -13 3 2 C ATOM 3832 C ILE B 257 -24.056 24.143 3.572 1.00 18.85 C ANISOU 3832 C ILE B 257 2416 2371 2375 21 -1 17 C ATOM 3833 O ILE B 257 -24.442 23.850 4.705 1.00 18.98 O ANISOU 3833 O ILE B 257 2444 2405 2364 36 -14 31 O ATOM 3834 CB ILE B 257 -25.635 24.857 1.758 1.00 18.32 C ANISOU 3834 CB ILE B 257 2343 2297 2323 -27 -5 6 C ATOM 3835 CG1 ILE B 257 -26.389 26.050 1.162 1.00 18.74 C ANISOU 3835 CG1 ILE B 257 2364 2379 2378 16 -18 10 C ATOM 3836 CG2 ILE B 257 -26.620 23.841 2.321 1.00 17.87 C ANISOU 3836 CG2 ILE B 257 2276 2259 2255 17 9 -9 C ATOM 3837 CD1 ILE B 257 -27.220 25.710 -0.058 1.00 18.54 C ANISOU 3837 CD1 ILE B 257 2330 2373 2343 23 -1 24 C ATOM 3838 N MET B 258 -23.123 23.439 2.939 1.00 19.05 N ANISOU 3838 N MET B 258 2403 2426 2409 21 9 -10 N ATOM 3839 CA MET B 258 -22.534 22.250 3.547 1.00 19.77 C ANISOU 3839 CA MET B 258 2533 2470 2511 59 45 9 C ATOM 3840 C MET B 258 -21.745 22.578 4.805 1.00 21.12 C ANISOU 3840 C MET B 258 2699 2697 2629 25 -21 -17 C ATOM 3841 O MET B 258 -21.804 21.833 5.790 1.00 21.42 O ANISOU 3841 O MET B 258 2750 2725 2665 5 -17 7 O ATOM 3842 CB MET B 258 -21.676 21.497 2.527 1.00 17.73 C ANISOU 3842 CB MET B 258 2249 2260 2228 -42 -97 49 C ATOM 3843 CG MET B 258 -22.515 20.741 1.509 1.00 16.16 C ANISOU 3843 CG MET B 258 2110 1984 2046 40 27 52 C ATOM 3844 SD MET B 258 -21.576 19.667 0.426 1.00 14.65 S ANISOU 3844 SD MET B 258 1848 1967 1753 109 -127 192 S ATOM 3845 CE MET B 258 -21.022 20.794 -0.849 1.00 14.52 C ANISOU 3845 CE MET B 258 1880 1860 1778 -41 -14 32 C ATOM 3846 N GLU B 259 -21.040 23.705 4.817 1.00 22.35 N ANISOU 3846 N GLU B 259 2844 2786 2860 -23 16 5 N ATOM 3847 CA GLU B 259 -20.324 24.152 6.006 1.00 23.85 C ANISOU 3847 CA GLU B 259 3051 3037 2975 -19 -65 -16 C ATOM 3848 C GLU B 259 -21.249 24.526 7.151 1.00 24.79 C ANISOU 3848 C GLU B 259 3166 3158 3096 9 7 -19 C ATOM 3849 O GLU B 259 -20.917 24.296 8.319 1.00 25.14 O ANISOU 3849 O GLU B 259 3224 3211 3117 13 -24 -14 O ATOM 3850 CB GLU B 259 -19.404 25.328 5.658 1.00 24.92 C ANISOU 3850 CB GLU B 259 3183 3104 3182 -54 -32 11 C ATOM 3851 CG GLU B 259 -18.277 24.921 4.721 1.00 26.36 C ANISOU 3851 CG GLU B 259 3367 3378 3272 60 6 -29 C ATOM 3852 CD GLU B 259 -17.297 26.036 4.422 1.00 28.36 C ANISOU 3852 CD GLU B 259 3578 3598 3598 -71 -10 29 C ATOM 3853 OE1 GLU B 259 -17.559 27.203 4.775 1.00 30.11 O ANISOU 3853 OE1 GLU B 259 3882 3725 3835 13 -9 -34 O ATOM 3854 OE2 GLU B 259 -16.242 25.739 3.821 1.00 28.74 O ANISOU 3854 OE2 GLU B 259 3629 3652 3641 -3 -19 -23 O ATOM 3855 N SER B 260 -22.437 25.045 6.859 1.00 25.34 N ANISOU 3855 N SER B 260 3202 3217 3209 10 -33 -1 N ATOM 3856 CA SER B 260 -23.429 25.342 7.881 1.00 26.07 C ANISOU 3856 CA SER B 260 3286 3336 3284 17 9 -13 C ATOM 3857 C SER B 260 -23.976 24.076 8.528 1.00 26.90 C ANISOU 3857 C SER B 260 3419 3399 3403 1 6 35 C ATOM 3858 O SER B 260 -24.413 24.103 9.680 1.00 27.05 O ANISOU 3858 O SER B 260 3465 3404 3407 23 14 15 O ATOM 3859 CB SER B 260 -24.585 26.157 7.298 1.00 25.92 C ANISOU 3859 CB SER B 260 3320 3262 3267 4 4 9 C ATOM 3860 OG SER B 260 -25.455 25.323 6.549 1.00 26.05 O ANISOU 3860 OG SER B 260 3348 3278 3273 -13 0 24 O ATOM 3861 N GLU B 261 -23.952 22.961 7.804 1.00 27.60 N ANISOU 3861 N GLU B 261 3525 3489 3473 17 2 -23 N ATOM 3862 CA GLU B 261 -24.429 21.680 8.291 1.00 28.62 C ANISOU 3862 CA GLU B 261 3662 3572 3641 -13 25 22 C ATOM 3863 C GLU B 261 -23.332 20.848 8.945 1.00 29.17 C ANISOU 3863 C GLU B 261 3714 3677 3693 13 -11 15 C ATOM 3864 O GLU B 261 -23.583 19.728 9.396 1.00 29.55 O ANISOU 3864 O GLU B 261 3780 3729 3716 -6 -18 47 O ATOM 3865 CB GLU B 261 -25.052 20.881 7.137 1.00 29.63 C ANISOU 3865 CB GLU B 261 3824 3722 3711 -49 5 -28 C ATOM 3866 CG GLU B 261 -26.307 21.513 6.561 1.00 31.37 C ANISOU 3866 CG GLU B 261 3980 3950 3990 25 -69 3 C ATOM 3867 CD GLU B 261 -27.489 21.515 7.508 1.00 33.06 C ANISOU 3867 CD GLU B 261 4151 4222 4189 4 37 -17 C ATOM 3868 OE1 GLU B 261 -27.568 20.626 8.383 1.00 34.08 O ANISOU 3868 OE1 GLU B 261 4327 4288 4333 0 5 43 O ATOM 3869 OE2 GLU B 261 -28.360 22.402 7.387 1.00 32.97 O ANISOU 3869 OE2 GLU B 261 4187 4193 4148 3 -3 1 O ATOM 3870 N GLY B 262 -22.107 21.356 8.963 1.00 29.40 N ANISOU 3870 N GLY B 262 3745 3716 3710 -18 5 9 N ATOM 3871 CA GLY B 262 -21.001 20.696 9.640 1.00 29.96 C ANISOU 3871 CA GLY B 262 3799 3777 3808 2 -19 15 C ATOM 3872 C GLY B 262 -20.113 19.906 8.692 1.00 30.49 C ANISOU 3872 C GLY B 262 3859 3836 3891 10 7 -9 C ATOM 3873 O GLY B 262 -19.073 19.385 9.104 1.00 30.24 O ANISOU 3873 O GLY B 262 3867 3813 3809 -4 -20 -1 O ATOM 3874 N ILE B 263 -20.530 19.811 7.431 1.00 31.22 N ANISOU 3874 N ILE B 263 3984 3948 3928 -4 -46 6 N ATOM 3875 CA ILE B 263 -19.716 19.145 6.430 1.00 32.19 C ANISOU 3875 CA ILE B 263 4139 4104 3990 33 -43 -50 C ATOM 3876 C ILE B 263 -18.532 20.061 6.114 1.00 34.04 C ANISOU 3876 C ILE B 263 4331 4288 4315 -49 28 -23 C ATOM 3877 O ILE B 263 -18.628 21.064 5.420 1.00 34.11 O ANISOU 3877 O ILE B 263 4292 4316 4352 -19 9 -11 O ATOM 3878 CB ILE B 263 -20.421 18.842 5.111 1.00 29.08 C ANISOU 3878 CB ILE B 263 3637 3620 3791 10 94 24 C ATOM 3879 CG1 ILE B 263 -21.703 18.089 5.453 1.00 27.40 C ANISOU 3879 CG1 ILE B 263 3516 3462 3431 12 -34 1 C ATOM 3880 CG2 ILE B 263 -19.547 18.018 4.179 1.00 27.93 C ANISOU 3880 CG2 ILE B 263 3552 3503 3557 -22 -12 26 C ATOM 3881 CD1 ILE B 263 -22.731 18.041 4.350 1.00 26.75 C ANISOU 3881 CD1 ILE B 263 3385 3355 3422 5 2 18 C ATOM 3882 N ILE B 264 -17.439 19.609 6.692 1.00 35.49 N ANISOU 3882 N ILE B 264 4508 4492 4486 48 -31 1 N ATOM 3883 CA ILE B 264 -16.240 20.418 6.700 1.00 36.89 C ANISOU 3883 CA ILE B 264 4653 4669 4694 -38 9 -2 C ATOM 3884 C ILE B 264 -15.227 19.777 7.628 1.00 37.57 C ANISOU 3884 C ILE B 264 4746 4759 4771 -14 -29 11 C ATOM 3885 O ILE B 264 -14.436 18.957 7.147 1.00 38.00 O ANISOU 3885 O ILE B 264 4814 4804 4818 11 -19 -7 O ATOM 3886 CB ILE B 264 -16.505 21.855 7.173 1.00 37.46 C ANISOU 3886 CB ILE B 264 4773 4696 4764 18 -11 -10 C ATOM 3887 CG1 ILE B 264 -15.484 22.786 6.497 1.00 38.01 C ANISOU 3887 CG1 ILE B 264 4823 4810 4808 4 14 18 C ATOM 3888 CG2 ILE B 264 -16.419 22.000 8.690 1.00 37.65 C ANISOU 3888 CG2 ILE B 264 4791 4750 4765 2 5 1 C ATOM 3889 CD1 ILE B 264 -15.556 24.239 6.880 1.00 38.48 C ANISOU 3889 CD1 ILE B 264 4896 4843 4880 -6 1 0 C TER 3890 ILE B 264 ATOM 3891 N ILE C 22 -21.738 24.115 34.541 1.00 22.26 N ANISOU 3891 N ILE C 22 2863 2745 2848 -8 -9 47 N ATOM 3892 CA ILE C 22 -21.853 23.053 35.584 1.00 21.53 C ANISOU 3892 CA ILE C 22 2719 2693 2770 -23 -9 21 C ATOM 3893 C ILE C 22 -23.151 22.274 35.420 1.00 20.81 C ANISOU 3893 C ILE C 22 2666 2589 2651 12 -15 12 C ATOM 3894 O ILE C 22 -24.235 22.850 35.307 1.00 21.15 O ANISOU 3894 O ILE C 22 2684 2628 2723 17 -22 37 O ATOM 3895 CB ILE C 22 -21.720 23.622 37.005 1.00 22.76 C ANISOU 3895 CB ILE C 22 2947 2871 2829 -10 -25 -3 C ATOM 3896 CG1 ILE C 22 -21.780 22.506 38.052 1.00 22.66 C ANISOU 3896 CG1 ILE C 22 2888 2872 2848 -29 -1 21 C ATOM 3897 CG2 ILE C 22 -22.785 24.673 37.279 1.00 23.54 C ANISOU 3897 CG2 ILE C 22 2998 2980 2966 20 10 -8 C ATOM 3898 CD1 ILE C 22 -21.331 22.938 39.434 1.00 22.96 C ANISOU 3898 CD1 ILE C 22 2954 2881 2888 -17 -6 -19 C ATOM 3899 N THR C 23 -23.035 20.949 35.378 1.00 19.78 N ANISOU 3899 N THR C 23 2492 2542 2483 -29 -45 24 N ATOM 3900 CA THR C 23 -24.205 20.099 35.194 1.00 19.05 C ANISOU 3900 CA THR C 23 2429 2434 2376 -12 5 87 C ATOM 3901 C THR C 23 -24.567 19.404 36.503 1.00 17.87 C ANISOU 3901 C THR C 23 2220 2296 2273 -11 -14 16 C ATOM 3902 O THR C 23 -23.711 19.222 37.369 1.00 17.95 O ANISOU 3902 O THR C 23 2238 2346 2236 -5 -5 15 O ATOM 3903 CB THR C 23 -23.984 19.040 34.102 1.00 21.24 C ANISOU 3903 CB THR C 23 2762 2684 2623 -34 42 -85 C ATOM 3904 OG1 THR C 23 -22.934 18.159 34.521 1.00 23.86 O ANISOU 3904 OG1 THR C 23 3029 2959 3077 61 -8 41 O ATOM 3905 CG2 THR C 23 -23.590 19.693 32.786 1.00 21.82 C ANISOU 3905 CG2 THR C 23 2818 2788 2685 -17 6 10 C ATOM 3906 N GLU C 24 -25.837 19.044 36.636 1.00 16.68 N ANISOU 3906 N GLU C 24 2161 2128 2050 1 -45 35 N ATOM 3907 CA GLU C 24 -26.282 18.326 37.829 1.00 15.99 C ANISOU 3907 CA GLU C 24 2033 2028 2016 8 -37 -11 C ATOM 3908 C GLU C 24 -26.301 16.827 37.559 1.00 16.15 C ANISOU 3908 C GLU C 24 2085 2023 2029 11 -51 18 C ATOM 3909 O GLU C 24 -26.802 16.364 36.535 1.00 16.73 O ANISOU 3909 O GLU C 24 2181 2144 2033 13 -56 -12 O ATOM 3910 CB GLU C 24 -27.644 18.828 38.292 1.00 16.04 C ANISOU 3910 CB GLU C 24 2016 2080 2000 -28 -20 -18 C ATOM 3911 CG GLU C 24 -27.996 18.425 39.718 1.00 16.22 C ANISOU 3911 CG GLU C 24 2073 2096 1996 -39 -56 1 C ATOM 3912 CD GLU C 24 -29.226 19.167 40.208 1.00 17.87 C ANISOU 3912 CD GLU C 24 2216 2267 2308 34 -13 -33 C ATOM 3913 OE1 GLU C 24 -30.312 18.910 39.640 1.00 17.83 O ANISOU 3913 OE1 GLU C 24 2203 2330 2241 25 -24 -5 O ATOM 3914 OE2 GLU C 24 -29.101 20.000 41.131 1.00 18.51 O ANISOU 3914 OE2 GLU C 24 2401 2390 2242 33 -102 -19 O ATOM 3915 N ASN C 25 -25.705 16.075 38.478 1.00 15.42 N ANISOU 3915 N ASN C 25 1967 1924 1970 -15 -39 -12 N ATOM 3916 CA ASN C 25 -25.762 14.621 38.440 1.00 14.77 C ANISOU 3916 CA ASN C 25 1881 1893 1838 -15 -30 -24 C ATOM 3917 C ASN C 25 -26.417 14.113 39.720 1.00 14.70 C ANISOU 3917 C ASN C 25 1881 1853 1850 3 -27 -2 C ATOM 3918 O ASN C 25 -25.776 13.812 40.727 1.00 14.50 O ANISOU 3918 O ASN C 25 1862 1850 1795 -15 -4 -7 O ATOM 3919 CB ASN C 25 -24.382 14.001 38.249 1.00 15.24 C ANISOU 3919 CB ASN C 25 1887 2013 1892 -12 -7 -24 C ATOM 3920 CG ASN C 25 -24.423 12.516 37.958 1.00 16.69 C ANISOU 3920 CG ASN C 25 2173 2083 2085 47 -27 -37 C ATOM 3921 OD1 ASN C 25 -25.380 11.818 38.296 1.00 18.81 O ANISOU 3921 OD1 ASN C 25 2421 2331 2395 -99 31 3 O ATOM 3922 ND2 ASN C 25 -23.373 12.013 37.321 1.00 16.38 N ANISOU 3922 ND2 ASN C 25 2109 2112 2004 -9 -27 -2 N ATOM 3923 N THR C 26 -27.736 13.959 39.659 1.00 14.98 N ANISOU 3923 N THR C 26 1907 1895 1888 -42 -40 -8 N ATOM 3924 CA THR C 26 -28.538 13.559 40.805 1.00 15.56 C ANISOU 3924 CA THR C 26 2007 1970 1936 -48 -5 5 C ATOM 3925 C THR C 26 -28.365 12.100 41.183 1.00 15.62 C ANISOU 3925 C THR C 26 1969 1980 1984 -14 -11 0 C ATOM 3926 O THR C 26 -28.734 11.710 42.301 1.00 15.73 O ANISOU 3926 O THR C 26 1961 2030 1986 -31 -43 29 O ATOM 3927 CB THR C 26 -30.031 13.846 40.556 1.00 17.04 C ANISOU 3927 CB THR C 26 2081 2186 2206 3 13 0 C ATOM 3928 OG1 THR C 26 -30.402 13.247 39.305 1.00 18.33 O ANISOU 3928 OG1 THR C 26 2338 2370 2259 -58 -59 -1 O ATOM 3929 CG2 THR C 26 -30.318 15.335 40.512 1.00 17.64 C ANISOU 3929 CG2 THR C 26 2214 2225 2261 19 -20 -4 C ATOM 3930 N SER C 27 -27.744 11.280 40.337 1.00 15.70 N ANISOU 3930 N SER C 27 1984 2003 1976 -24 -22 -15 N ATOM 3931 CA SER C 27 -27.456 9.892 40.677 1.00 16.38 C ANISOU 3931 CA SER C 27 2089 2051 2085 -1 -36 31 C ATOM 3932 C SER C 27 -26.428 9.767 41.795 1.00 16.25 C ANISOU 3932 C SER C 27 2076 2033 2065 -14 -23 -1 C ATOM 3933 O SER C 27 -26.361 8.726 42.453 1.00 16.18 O ANISOU 3933 O SER C 27 2104 2071 1972 -15 -25 -5 O ATOM 3934 CB SER C 27 -27.003 9.094 39.450 1.00 18.42 C ANISOU 3934 CB SER C 27 2424 2270 2304 2 45 -91 C ATOM 3935 OG SER C 27 -25.648 9.350 39.129 1.00 19.82 O ANISOU 3935 OG SER C 27 2489 2567 2474 16 43 -64 O ATOM 3936 N TRP C 28 -25.656 10.811 42.071 1.00 16.04 N ANISOU 3936 N TRP C 28 2040 2048 2007 -9 -37 -7 N ATOM 3937 CA TRP C 28 -24.763 10.851 43.212 1.00 15.57 C ANISOU 3937 CA TRP C 28 1983 1972 1962 -30 -6 -6 C ATOM 3938 C TRP C 28 -25.470 11.024 44.547 1.00 15.48 C ANISOU 3938 C TRP C 28 1965 1965 1951 -2 -22 -11 C ATOM 3939 O TRP C 28 -24.864 10.688 45.573 1.00 15.37 O ANISOU 3939 O TRP C 28 1990 1957 1893 -14 -12 -30 O ATOM 3940 CB TRP C 28 -23.728 11.968 43.052 1.00 15.29 C ANISOU 3940 CB TRP C 28 1925 1985 1898 -14 15 -1 C ATOM 3941 CG TRP C 28 -22.830 11.847 41.863 1.00 13.77 C ANISOU 3941 CG TRP C 28 1724 1746 1763 4 -83 8 C ATOM 3942 CD1 TRP C 28 -22.665 10.767 41.042 1.00 14.53 C ANISOU 3942 CD1 TRP C 28 1879 1834 1808 39 -19 -21 C ATOM 3943 CD2 TRP C 28 -21.938 12.857 41.374 1.00 13.83 C ANISOU 3943 CD2 TRP C 28 1758 1793 1703 10 -38 45 C ATOM 3944 NE1 TRP C 28 -21.741 11.048 40.067 1.00 15.30 N ANISOU 3944 NE1 TRP C 28 1918 1986 1909 -49 -15 17 N ATOM 3945 CE2 TRP C 28 -21.279 12.324 40.249 1.00 14.69 C ANISOU 3945 CE2 TRP C 28 1866 1876 1840 52 13 -6 C ATOM 3946 CE3 TRP C 28 -21.638 14.162 41.777 1.00 14.89 C ANISOU 3946 CE3 TRP C 28 1903 1872 1882 -29 -34 -1 C ATOM 3947 CZ2 TRP C 28 -20.338 13.053 39.523 1.00 15.15 C ANISOU 3947 CZ2 TRP C 28 1912 1947 1897 -13 -36 37 C ATOM 3948 CZ3 TRP C 28 -20.704 14.884 41.057 1.00 15.17 C ANISOU 3948 CZ3 TRP C 28 1873 1989 1901 -4 -19 33 C ATOM 3949 CH2 TRP C 28 -20.066 14.323 39.941 1.00 15.39 C ANISOU 3949 CH2 TRP C 28 1962 1956 1928 35 -41 2 C ATOM 3950 N ASN C 29 -26.719 11.473 44.590 1.00 15.35 N ANISOU 3950 N ASN C 29 1945 1958 1929 -12 -18 -21 N ATOM 3951 CA ASN C 29 -27.413 11.695 45.849 1.00 15.72 C ANISOU 3951 CA ASN C 29 1981 2010 1980 10 12 -6 C ATOM 3952 C ASN C 29 -27.528 10.451 46.717 1.00 16.46 C ANISOU 3952 C ASN C 29 2111 2067 2075 -2 1 33 C ATOM 3953 O ASN C 29 -27.491 10.578 47.947 1.00 16.71 O ANISOU 3953 O ASN C 29 2144 2113 2094 -14 -9 -14 O ATOM 3954 CB ASN C 29 -28.802 12.298 45.635 1.00 14.78 C ANISOU 3954 CB ASN C 29 1938 1904 1772 -22 14 22 C ATOM 3955 CG ASN C 29 -28.776 13.748 45.207 1.00 14.94 C ANISOU 3955 CG ASN C 29 1895 1850 1931 -43 0 -60 C ATOM 3956 OD1 ASN C 29 -29.661 14.205 44.476 1.00 16.58 O ANISOU 3956 OD1 ASN C 29 2066 2196 2038 58 -83 -65 O ATOM 3957 ND2 ASN C 29 -27.778 14.496 45.657 1.00 13.19 N ANISOU 3957 ND2 ASN C 29 1699 1650 1660 37 7 83 N ATOM 3958 N LYS C 30 -27.616 9.254 46.143 1.00 16.91 N ANISOU 3958 N LYS C 30 2151 2131 2142 -12 -9 -17 N ATOM 3959 CA LYS C 30 -27.668 8.019 46.912 1.00 18.00 C ANISOU 3959 CA LYS C 30 2272 2270 2298 7 4 95 C ATOM 3960 C LYS C 30 -26.468 7.800 47.821 1.00 17.92 C ANISOU 3960 C LYS C 30 2266 2273 2270 -5 3 27 C ATOM 3961 O LYS C 30 -26.584 7.149 48.866 1.00 17.97 O ANISOU 3961 O LYS C 30 2284 2251 2294 -4 -4 42 O ATOM 3962 CB LYS C 30 -27.819 6.813 45.968 1.00 21.35 C ANISOU 3962 CB LYS C 30 2866 2518 2728 -69 -108 -71 C ATOM 3963 CG LYS C 30 -26.590 6.544 45.118 1.00 26.22 C ANISOU 3963 CG LYS C 30 3216 3470 3276 39 103 68 C ATOM 3964 CD LYS C 30 -26.655 5.220 44.379 1.00 31.18 C ANISOU 3964 CD LYS C 30 4042 3746 4057 -27 74 -81 C ATOM 3965 CE LYS C 30 -27.447 5.321 43.088 1.00 34.81 C ANISOU 3965 CE LYS C 30 4383 4472 4374 -16 -60 41 C ATOM 3966 NZ LYS C 30 -27.278 4.098 42.252 1.00 36.44 N ANISOU 3966 NZ LYS C 30 4651 4574 4622 8 6 -18 N ATOM 3967 N GLU C 31 -25.290 8.310 47.478 1.00 17.80 N ANISOU 3967 N GLU C 31 2260 2255 2250 -1 -6 9 N ATOM 3968 CA GLU C 31 -24.117 8.259 48.332 1.00 17.69 C ANISOU 3968 CA GLU C 31 2278 2211 2231 27 -27 -16 C ATOM 3969 C GLU C 31 -24.253 9.123 49.580 1.00 17.45 C ANISOU 3969 C GLU C 31 2229 2177 2225 23 -20 -2 C ATOM 3970 O GLU C 31 -23.636 8.834 50.610 1.00 17.82 O ANISOU 3970 O GLU C 31 2296 2230 2243 22 -39 5 O ATOM 3971 CB GLU C 31 -22.869 8.681 47.548 1.00 19.56 C ANISOU 3971 CB GLU C 31 2391 2513 2527 -32 29 66 C ATOM 3972 CG GLU C 31 -22.581 7.823 46.328 1.00 22.02 C ANISOU 3972 CG GLU C 31 2803 2893 2670 -12 26 -64 C ATOM 3973 CD GLU C 31 -22.192 6.395 46.638 1.00 25.55 C ANISOU 3973 CD GLU C 31 3283 3113 3312 36 -9 48 C ATOM 3974 OE1 GLU C 31 -21.966 6.043 47.816 1.00 25.83 O ANISOU 3974 OE1 GLU C 31 3320 3206 3287 -17 1 0 O ATOM 3975 OE2 GLU C 31 -22.105 5.590 45.684 1.00 26.91 O ANISOU 3975 OE2 GLU C 31 3471 3369 3384 -12 7 -58 O ATOM 3976 N PHE C 32 -25.023 10.197 49.501 1.00 16.76 N ANISOU 3976 N PHE C 32 2162 2099 2108 -16 -2 10 N ATOM 3977 CA PHE C 32 -25.304 11.041 50.652 1.00 16.67 C ANISOU 3977 CA PHE C 32 2142 2053 2138 -9 -12 5 C ATOM 3978 C PHE C 32 -26.432 10.465 51.497 1.00 17.01 C ANISOU 3978 C PHE C 32 2165 2144 2155 -24 1 1 C ATOM 3979 O PHE C 32 -26.324 10.350 52.716 1.00 17.42 O ANISOU 3979 O PHE C 32 2226 2218 2175 -23 -29 -13 O ATOM 3980 CB PHE C 32 -25.685 12.448 50.192 1.00 15.51 C ANISOU 3980 CB PHE C 32 1945 2034 1915 -5 -2 9 C ATOM 3981 CG PHE C 32 -24.567 13.163 49.488 1.00 14.94 C ANISOU 3981 CG PHE C 32 1906 1863 1906 7 -41 21 C ATOM 3982 CD1 PHE C 32 -24.315 12.953 48.143 1.00 15.96 C ANISOU 3982 CD1 PHE C 32 2058 2011 1996 -17 35 -14 C ATOM 3983 CD2 PHE C 32 -23.768 14.054 50.185 1.00 14.93 C ANISOU 3983 CD2 PHE C 32 1904 1871 1898 8 -2 -8 C ATOM 3984 CE1 PHE C 32 -23.286 13.615 47.500 1.00 15.38 C ANISOU 3984 CE1 PHE C 32 1960 1908 1977 11 -30 -2 C ATOM 3985 CE2 PHE C 32 -22.741 14.713 49.544 1.00 15.11 C ANISOU 3985 CE2 PHE C 32 1900 1893 1949 5 23 -30 C ATOM 3986 CZ PHE C 32 -22.496 14.501 48.205 1.00 15.00 C ANISOU 3986 CZ PHE C 32 1930 1873 1896 -9 -17 51 C ATOM 3987 N SER C 33 -27.516 10.047 50.837 1.00 17.06 N ANISOU 3987 N SER C 33 2171 2187 2124 -25 -3 12 N ATOM 3988 CA SER C 33 -28.674 9.541 51.569 1.00 16.88 C ANISOU 3988 CA SER C 33 2149 2136 2129 -9 -7 7 C ATOM 3989 C SER C 33 -28.354 8.252 52.307 1.00 16.88 C ANISOU 3989 C SER C 33 2150 2134 2128 -12 -10 4 C ATOM 3990 O SER C 33 -28.868 8.050 53.409 1.00 16.73 O ANISOU 3990 O SER C 33 2126 2143 2088 -7 -51 20 O ATOM 3991 CB ASER C 33 -29.884 9.380 50.651 0.50 17.21 C ANISOU 3991 CB ASER C 33 2168 2187 2184 -2 -28 -7 C ATOM 3992 CB BSER C 33 -29.851 9.304 50.620 0.50 16.65 C ANISOU 3992 CB BSER C 33 2141 2068 2116 11 2 -18 C ATOM 3993 OG ASER C 33 -30.375 10.668 50.305 0.50 17.49 O ANISOU 3993 OG ASER C 33 2193 2215 2236 12 -15 6 O ATOM 3994 OG BSER C 33 -29.551 8.259 49.711 0.50 16.07 O ANISOU 3994 OG BSER C 33 2052 2041 2014 12 -16 8 O ATOM 3995 N ALA C 34 -27.486 7.406 51.761 1.00 17.24 N ANISOU 3995 N ALA C 34 2184 2175 2191 16 -2 -3 N ATOM 3996 CA ALA C 34 -27.088 6.163 52.397 1.00 17.40 C ANISOU 3996 CA ALA C 34 2219 2166 2225 23 20 -7 C ATOM 3997 C ALA C 34 -26.483 6.375 53.780 1.00 18.43 C ANISOU 3997 C ALA C 34 2372 2345 2286 -5 -27 4 C ATOM 3998 O ALA C 34 -26.614 5.515 54.651 1.00 18.84 O ANISOU 3998 O ALA C 34 2424 2333 2402 -14 -46 54 O ATOM 3999 CB ALA C 34 -26.087 5.407 51.528 1.00 15.94 C ANISOU 3999 CB ALA C 34 2003 2054 2000 -52 -62 38 C ATOM 4000 N GLU C 35 -25.796 7.491 53.974 1.00 18.92 N ANISOU 4000 N GLU C 35 2458 2348 2385 -12 -35 17 N ATOM 4001 CA GLU C 35 -25.215 7.855 55.258 1.00 19.52 C ANISOU 4001 CA GLU C 35 2540 2454 2423 0 -45 -12 C ATOM 4002 C GLU C 35 -26.044 8.887 56.002 1.00 19.40 C ANISOU 4002 C GLU C 35 2477 2451 2442 -11 -22 13 C ATOM 4003 O GLU C 35 -25.623 9.443 57.023 1.00 19.82 O ANISOU 4003 O GLU C 35 2529 2548 2455 -47 -38 15 O ATOM 4004 CB GLU C 35 -23.800 8.390 55.000 1.00 22.00 C ANISOU 4004 CB GLU C 35 2682 2821 2855 -88 -15 56 C ATOM 4005 CG GLU C 35 -22.907 7.444 54.216 1.00 24.26 C ANISOU 4005 CG GLU C 35 3049 3118 3050 -2 40 -101 C ATOM 4006 CD GLU C 35 -22.536 6.187 54.978 1.00 27.24 C ANISOU 4006 CD GLU C 35 3509 3391 3449 8 -42 95 C ATOM 4007 OE1 GLU C 35 -22.719 6.151 56.211 1.00 27.05 O ANISOU 4007 OE1 GLU C 35 3463 3372 3443 -31 -16 39 O ATOM 4008 OE2 GLU C 35 -22.054 5.227 54.343 1.00 29.03 O ANISOU 4008 OE2 GLU C 35 3754 3602 3673 58 -8 -36 O ATOM 4009 N ALA C 36 -27.227 9.210 55.495 1.00 19.08 N ANISOU 4009 N ALA C 36 2438 2404 2407 -20 -3 8 N ATOM 4010 CA ALA C 36 -28.142 10.176 56.079 1.00 18.93 C ANISOU 4010 CA ALA C 36 2404 2387 2400 -25 -21 9 C ATOM 4011 C ALA C 36 -27.510 11.544 56.296 1.00 18.74 C ANISOU 4011 C ALA C 36 2386 2371 2365 -8 -2 18 C ATOM 4012 O ALA C 36 -27.701 12.188 57.332 1.00 19.43 O ANISOU 4012 O ALA C 36 2504 2465 2413 -21 19 -15 O ATOM 4013 CB ALA C 36 -28.719 9.637 57.384 1.00 19.66 C ANISOU 4013 CB ALA C 36 2496 2550 2424 -11 19 0 C ATOM 4014 N VAL C 37 -26.751 12.019 55.308 1.00 18.10 N ANISOU 4014 N VAL C 37 2290 2265 2322 -21 -48 9 N ATOM 4015 CA VAL C 37 -26.124 13.329 55.412 1.00 17.86 C ANISOU 4015 CA VAL C 37 2311 2221 2253 4 -20 16 C ATOM 4016 C VAL C 37 -26.603 14.252 54.296 1.00 17.20 C ANISOU 4016 C VAL C 37 2204 2157 2173 -15 5 -15 C ATOM 4017 O VAL C 37 -27.007 13.825 53.217 1.00 17.66 O ANISOU 4017 O VAL C 37 2284 2249 2178 2 -22 -8 O ATOM 4018 CB VAL C 37 -24.590 13.282 55.415 1.00 19.19 C ANISOU 4018 CB VAL C 37 2368 2438 2484 3 33 -9 C ATOM 4019 CG1 VAL C 37 -24.047 12.528 56.624 1.00 21.06 C ANISOU 4019 CG1 VAL C 37 2704 2701 2596 8 -42 54 C ATOM 4020 CG2 VAL C 37 -24.066 12.654 54.135 1.00 19.29 C ANISOU 4020 CG2 VAL C 37 2432 2473 2424 17 -32 -17 C ATOM 4021 N ASN C 38 -26.599 15.539 54.607 1.00 16.49 N ANISOU 4021 N ASN C 38 2081 2122 2065 -19 -6 13 N ATOM 4022 CA ASN C 38 -26.857 16.583 53.627 1.00 16.47 C ANISOU 4022 CA ASN C 38 2066 2138 2054 -62 -9 37 C ATOM 4023 C ASN C 38 -25.535 17.197 53.185 1.00 15.52 C ANISOU 4023 C ASN C 38 1992 2027 1878 4 8 2 C ATOM 4024 O ASN C 38 -24.769 17.681 54.021 1.00 16.07 O ANISOU 4024 O ASN C 38 2040 2131 1936 3 -36 1 O ATOM 4025 CB ASN C 38 -27.769 17.663 54.207 1.00 19.18 C ANISOU 4025 CB ASN C 38 2551 2319 2418 130 -10 -79 C ATOM 4026 CG ASN C 38 -29.125 17.115 54.605 1.00 23.47 C ANISOU 4026 CG ASN C 38 2829 2966 3121 -14 52 66 C ATOM 4027 OD1 ASN C 38 -29.752 16.378 53.843 1.00 25.56 O ANISOU 4027 OD1 ASN C 38 3158 3245 3310 -44 -44 -40 O ATOM 4028 ND2 ASN C 38 -29.583 17.467 55.797 1.00 25.88 N ANISOU 4028 ND2 ASN C 38 3271 3321 3242 24 53 5 N ATOM 4029 N GLY C 39 -25.271 17.170 51.881 1.00 14.08 N ANISOU 4029 N GLY C 39 1739 1814 1796 -28 -34 -1 N ATOM 4030 CA GLY C 39 -24.031 17.766 51.401 1.00 12.99 C ANISOU 4030 CA GLY C 39 1671 1706 1558 18 -23 -16 C ATOM 4031 C GLY C 39 -24.006 17.952 49.891 1.00 12.46 C ANISOU 4031 C GLY C 39 1564 1624 1546 -9 -13 17 C ATOM 4032 O GLY C 39 -24.985 17.708 49.187 1.00 12.65 O ANISOU 4032 O GLY C 39 1580 1654 1574 -32 -11 -53 O ATOM 4033 N VAL C 40 -22.826 18.354 49.433 1.00 11.59 N ANISOU 4033 N VAL C 40 1527 1481 1395 36 -11 17 N ATOM 4034 CA VAL C 40 -22.613 18.598 48.010 1.00 11.28 C ANISOU 4034 CA VAL C 40 1461 1438 1385 11 -6 -8 C ATOM 4035 C VAL C 40 -21.210 18.166 47.603 1.00 11.06 C ANISOU 4035 C VAL C 40 1432 1397 1372 -12 -14 -21 C ATOM 4036 O VAL C 40 -20.239 18.280 48.354 1.00 11.15 O ANISOU 4036 O VAL C 40 1489 1425 1321 14 -39 -54 O ATOM 4037 CB VAL C 40 -22.861 20.070 47.648 1.00 11.87 C ANISOU 4037 CB VAL C 40 1547 1452 1512 -25 -52 24 C ATOM 4038 CG1 VAL C 40 -21.823 20.986 48.283 1.00 12.29 C ANISOU 4038 CG1 VAL C 40 1639 1464 1566 -22 -79 -24 C ATOM 4039 CG2 VAL C 40 -22.883 20.233 46.133 1.00 13.66 C ANISOU 4039 CG2 VAL C 40 1864 1734 1591 0 -4 38 C ATOM 4040 N PHE C 41 -21.115 17.602 46.406 1.00 10.68 N ANISOU 4040 N PHE C 41 1396 1339 1321 -12 -2 24 N ATOM 4041 CA PHE C 41 -19.838 17.306 45.778 1.00 10.51 C ANISOU 4041 CA PHE C 41 1373 1295 1323 22 -17 10 C ATOM 4042 C PHE C 41 -19.784 18.009 44.420 1.00 10.84 C ANISOU 4042 C PHE C 41 1423 1352 1343 7 -11 19 C ATOM 4043 O PHE C 41 -20.747 17.924 43.658 1.00 11.40 O ANISOU 4043 O PHE C 41 1524 1449 1356 23 -50 8 O ATOM 4044 CB PHE C 41 -19.632 15.806 45.577 1.00 10.08 C ANISOU 4044 CB PHE C 41 1315 1281 1236 -53 -20 -27 C ATOM 4045 CG PHE C 41 -18.253 15.386 45.168 1.00 10.21 C ANISOU 4045 CG PHE C 41 1305 1296 1280 -28 -34 -20 C ATOM 4046 CD1 PHE C 41 -17.129 15.838 45.846 1.00 9.56 C ANISOU 4046 CD1 PHE C 41 1227 1221 1185 -37 20 7 C ATOM 4047 CD2 PHE C 41 -18.064 14.519 44.105 1.00 10.85 C ANISOU 4047 CD2 PHE C 41 1429 1331 1361 -26 49 -42 C ATOM 4048 CE1 PHE C 41 -15.860 15.447 45.475 1.00 9.56 C ANISOU 4048 CE1 PHE C 41 1281 1168 1182 47 -6 40 C ATOM 4049 CE2 PHE C 41 -16.795 14.115 43.732 1.00 11.00 C ANISOU 4049 CE2 PHE C 41 1370 1357 1452 -24 -25 29 C ATOM 4050 CZ PHE C 41 -15.688 14.580 44.413 1.00 10.26 C ANISOU 4050 CZ PHE C 41 1412 1276 1211 3 -10 -3 C ATOM 4051 N VAL C 42 -18.698 18.720 44.179 1.00 10.75 N ANISOU 4051 N VAL C 42 1452 1312 1322 10 33 -1 N ATOM 4052 CA VAL C 42 -18.430 19.324 42.878 1.00 11.12 C ANISOU 4052 CA VAL C 42 1487 1377 1361 -8 2 32 C ATOM 4053 C VAL C 42 -17.156 18.719 42.299 1.00 11.53 C ANISOU 4053 C VAL C 42 1497 1448 1436 18 -29 8 C ATOM 4054 O VAL C 42 -16.113 18.698 42.959 1.00 11.30 O ANISOU 4054 O VAL C 42 1459 1449 1384 5 -11 -5 O ATOM 4055 CB VAL C 42 -18.280 20.852 42.981 1.00 11.31 C ANISOU 4055 CB VAL C 42 1495 1397 1406 -9 22 -16 C ATOM 4056 CG1 VAL C 42 -17.961 21.463 41.624 1.00 10.89 C ANISOU 4056 CG1 VAL C 42 1411 1314 1414 6 -69 47 C ATOM 4057 CG2 VAL C 42 -19.531 21.489 43.563 1.00 11.37 C ANISOU 4057 CG2 VAL C 42 1410 1516 1396 -16 -46 -31 C ATOM 4058 N LEU C 43 -17.249 18.219 41.074 1.00 11.71 N ANISOU 4058 N LEU C 43 1581 1417 1450 11 -18 -6 N ATOM 4059 CA LEU C 43 -16.139 17.531 40.424 1.00 12.33 C ANISOU 4059 CA LEU C 43 1553 1549 1583 2 6 -4 C ATOM 4060 C LEU C 43 -15.961 18.057 39.003 1.00 12.91 C ANISOU 4060 C LEU C 43 1666 1650 1591 2 6 -16 C ATOM 4061 O LEU C 43 -16.926 18.107 38.234 1.00 13.70 O ANISOU 4061 O LEU C 43 1806 1805 1595 27 -50 -40 O ATOM 4062 CB LEU C 43 -16.418 16.028 40.393 1.00 12.66 C ANISOU 4062 CB LEU C 43 1625 1547 1637 28 -44 9 C ATOM 4063 CG LEU C 43 -15.400 15.135 39.685 1.00 12.99 C ANISOU 4063 CG LEU C 43 1646 1640 1651 -11 14 -37 C ATOM 4064 CD1 LEU C 43 -14.065 15.157 40.413 1.00 13.46 C ANISOU 4064 CD1 LEU C 43 1685 1709 1719 14 -23 43 C ATOM 4065 CD2 LEU C 43 -15.931 13.708 39.580 1.00 13.53 C ANISOU 4065 CD2 LEU C 43 1756 1657 1727 -13 -47 -14 C ATOM 4066 N CYS C 44 -14.752 18.494 38.674 1.00 12.99 N ANISOU 4066 N CYS C 44 1660 1684 1591 27 24 -38 N ATOM 4067 CA CYS C 44 -14.503 19.126 37.381 1.00 13.80 C ANISOU 4067 CA CYS C 44 1765 1830 1647 16 10 14 C ATOM 4068 C CYS C 44 -13.336 18.443 36.679 1.00 13.97 C ANISOU 4068 C CYS C 44 1793 1802 1714 30 -3 -29 C ATOM 4069 O CYS C 44 -12.248 18.327 37.243 1.00 14.43 O ANISOU 4069 O CYS C 44 1855 1905 1724 72 -28 -84 O ATOM 4070 CB CYS C 44 -14.211 20.619 37.528 1.00 17.17 C ANISOU 4070 CB CYS C 44 2301 1977 2247 -51 -52 43 C ATOM 4071 SG CYS C 44 -15.310 21.508 38.644 1.00 19.49 S ANISOU 4071 SG CYS C 44 2599 2467 2339 82 -22 -112 S ATOM 4072 N LYS C 45 -13.565 17.997 35.447 1.00 13.68 N ANISOU 4072 N LYS C 45 1783 1725 1689 38 -36 31 N ATOM 4073 CA LYS C 45 -12.506 17.408 34.639 1.00 13.80 C ANISOU 4073 CA LYS C 45 1769 1746 1729 29 -27 17 C ATOM 4074 C LYS C 45 -11.813 18.467 33.803 1.00 13.82 C ANISOU 4074 C LYS C 45 1797 1715 1739 13 -30 -15 C ATOM 4075 O LYS C 45 -12.469 19.219 33.074 1.00 14.00 O ANISOU 4075 O LYS C 45 1882 1722 1716 -11 -78 0 O ATOM 4076 CB LYS C 45 -13.090 16.325 33.720 1.00 15.11 C ANISOU 4076 CB LYS C 45 1964 1908 1868 -71 -92 -30 C ATOM 4077 CG LYS C 45 -12.052 15.615 32.863 1.00 18.10 C ANISOU 4077 CG LYS C 45 2265 2346 2266 109 79 -12 C ATOM 4078 CD LYS C 45 -12.711 14.506 32.051 1.00 21.44 C ANISOU 4078 CD LYS C 45 2761 2655 2729 -107 -94 -51 C ATOM 4079 CE LYS C 45 -11.688 13.782 31.189 1.00 24.57 C ANISOU 4079 CE LYS C 45 3067 3135 3132 71 74 -42 C ATOM 4080 NZ LYS C 45 -12.337 12.751 30.330 1.00 26.24 N ANISOU 4080 NZ LYS C 45 3387 3265 3319 -23 -34 -38 N ATOM 4081 N SER C 46 -10.501 18.593 33.908 1.00 13.97 N ANISOU 4081 N SER C 46 1803 1756 1749 14 -35 -33 N ATOM 4082 CA SER C 46 -9.660 19.482 33.133 1.00 15.10 C ANISOU 4082 CA SER C 46 1917 1919 1903 -32 15 3 C ATOM 4083 C SER C 46 -9.687 20.936 33.600 1.00 15.43 C ANISOU 4083 C SER C 46 2024 1930 1909 -15 -17 28 C ATOM 4084 O SER C 46 -8.628 21.548 33.764 1.00 16.05 O ANISOU 4084 O SER C 46 2099 2050 1950 -56 -79 21 O ATOM 4085 CB ASER C 46 -10.016 19.415 31.642 0.50 16.46 C ANISOU 4085 CB ASER C 46 2158 2131 1966 11 -40 1 C ATOM 4086 CB BSER C 46 -10.026 19.440 31.643 0.50 14.98 C ANISOU 4086 CB BSER C 46 1938 1836 1916 9 16 -8 C ATOM 4087 OG ASER C 46 -8.982 19.968 30.849 0.50 17.23 O ANISOU 4087 OG ASER C 46 2187 2179 2181 -8 3 9 O ATOM 4088 OG BSER C 46 -9.816 18.139 31.126 0.50 14.08 O ANISOU 4088 OG BSER C 46 1796 1798 1755 4 -12 -5 O ATOM 4089 N SER C 47 -10.863 21.514 33.739 1.00 15.94 N ANISOU 4089 N SER C 47 2047 2036 1974 -7 10 4 N ATOM 4090 CA SER C 47 -11.034 22.885 34.183 1.00 16.78 C ANISOU 4090 CA SER C 47 2174 2087 2115 20 -20 -26 C ATOM 4091 C SER C 47 -12.397 23.060 34.837 1.00 17.36 C ANISOU 4091 C SER C 47 2207 2201 2189 -12 -6 15 C ATOM 4092 O SER C 47 -13.262 22.182 34.794 1.00 17.25 O ANISOU 4092 O SER C 47 2247 2132 2174 -3 -12 18 O ATOM 4093 CB SER C 47 -10.926 23.851 32.996 1.00 17.29 C ANISOU 4093 CB SER C 47 2212 2136 2222 -13 -11 27 C ATOM 4094 OG SER C 47 -12.121 23.794 32.225 1.00 17.61 O ANISOU 4094 OG SER C 47 2292 2218 2180 36 -49 24 O ATOM 4095 N SER C 48 -12.640 24.260 35.355 1.00 18.06 N ANISOU 4095 N SER C 48 2359 2225 2278 -3 -30 10 N ATOM 4096 CA SER C 48 -13.900 24.619 35.984 1.00 19.48 C ANISOU 4096 CA SER C 48 2458 2439 2505 10 46 -2 C ATOM 4097 C SER C 48 -14.996 24.966 34.986 1.00 20.66 C ANISOU 4097 C SER C 48 2601 2592 2658 21 -40 12 C ATOM 4098 O SER C 48 -16.107 25.335 35.376 1.00 21.04 O ANISOU 4098 O SER C 48 2623 2626 2744 27 -26 -13 O ATOM 4099 CB SER C 48 -13.675 25.806 36.933 1.00 20.47 C ANISOU 4099 CB SER C 48 2653 2551 2574 -3 5 -52 C ATOM 4100 OG SER C 48 -13.189 26.924 36.204 1.00 21.26 O ANISOU 4100 OG SER C 48 2774 2625 2680 -18 -20 11 O ATOM 4101 N LYS C 49 -14.736 24.828 33.694 1.00 21.82 N ANISOU 4101 N LYS C 49 2818 2729 2744 14 13 -20 N ATOM 4102 CA LYS C 49 -15.753 24.919 32.659 1.00 23.10 C ANISOU 4102 CA LYS C 49 2910 2887 2977 32 -101 -38 C ATOM 4103 C LYS C 49 -16.426 23.581 32.387 1.00 22.94 C ANISOU 4103 C LYS C 49 2925 2856 2934 19 -36 12 C ATOM 4104 O LYS C 49 -17.386 23.512 31.616 1.00 23.11 O ANISOU 4104 O LYS C 49 2961 2895 2926 9 -40 54 O ATOM 4105 CB LYS C 49 -15.121 25.464 31.371 1.00 27.29 C ANISOU 4105 CB LYS C 49 3479 3630 3262 41 85 95 C ATOM 4106 CG LYS C 49 -14.453 26.818 31.548 1.00 32.79 C ANISOU 4106 CG LYS C 49 4175 3970 4312 -55 -96 -57 C ATOM 4107 CD LYS C 49 -13.698 27.236 30.296 1.00 37.08 C ANISOU 4107 CD LYS C 49 4677 4815 4596 30 62 49 C ATOM 4108 CE LYS C 49 -13.075 28.613 30.465 1.00 40.35 C ANISOU 4108 CE LYS C 49 5136 5006 5189 -21 -50 -25 C ATOM 4109 NZ LYS C 49 -12.270 29.005 29.275 1.00 41.80 N ANISOU 4109 NZ LYS C 49 5299 5280 5302 -4 15 3 N ATOM 4110 N SER C 50 -15.941 22.501 32.990 1.00 22.43 N ANISOU 4110 N SER C 50 2885 2813 2823 -24 -25 5 N ATOM 4111 CA SER C 50 -16.529 21.178 32.836 1.00 21.78 C ANISOU 4111 CA SER C 50 2791 2787 2696 -25 -2 57 C ATOM 4112 C SER C 50 -16.790 20.531 34.197 1.00 20.63 C ANISOU 4112 C SER C 50 2622 2630 2585 26 21 -23 C ATOM 4113 O SER C 50 -16.154 19.534 34.549 1.00 21.07 O ANISOU 4113 O SER C 50 2715 2683 2608 47 -18 1 O ATOM 4114 CB SER C 50 -15.625 20.271 32.000 1.00 23.29 C ANISOU 4114 CB SER C 50 2963 2884 3004 46 9 -45 C ATOM 4115 OG SER C 50 -15.389 20.785 30.702 1.00 25.49 O ANISOU 4115 OG SER C 50 3277 3285 3122 0 6 16 O ATOM 4116 N CYS C 51 -17.727 21.091 34.956 1.00 18.99 N ANISOU 4116 N CYS C 51 2413 2422 2378 -46 -38 68 N ATOM 4117 CA CYS C 51 -18.018 20.601 36.297 1.00 17.91 C ANISOU 4117 CA CYS C 51 2218 2286 2302 -35 -37 27 C ATOM 4118 C CYS C 51 -19.350 19.863 36.373 1.00 16.58 C ANISOU 4118 C CYS C 51 2150 2092 2059 11 -18 73 C ATOM 4119 O CYS C 51 -20.283 20.121 35.614 1.00 16.77 O ANISOU 4119 O CYS C 51 2206 2144 2023 -8 -45 89 O ATOM 4120 CB CYS C 51 -18.044 21.753 37.308 1.00 19.47 C ANISOU 4120 CB CYS C 51 2510 2401 2487 55 0 -46 C ATOM 4121 SG CYS C 51 -16.499 22.664 37.477 1.00 20.47 S ANISOU 4121 SG CYS C 51 2598 2504 2677 1 -90 31 S ATOM 4122 N ALA C 52 -19.444 18.938 37.325 1.00 14.97 N ANISOU 4122 N ALA C 52 1880 1951 1855 0 -29 -16 N ATOM 4123 CA ALA C 52 -20.699 18.282 37.658 1.00 14.43 C ANISOU 4123 CA ALA C 52 1855 1868 1758 19 -31 -5 C ATOM 4124 C ALA C 52 -20.884 18.291 39.178 1.00 13.79 C ANISOU 4124 C ALA C 52 1746 1770 1725 -15 -17 23 C ATOM 4125 O ALA C 52 -19.898 18.327 39.915 1.00 13.61 O ANISOU 4125 O ALA C 52 1773 1777 1623 -20 -21 35 O ATOM 4126 CB ALA C 52 -20.744 16.859 37.135 1.00 15.01 C ANISOU 4126 CB ALA C 52 2006 1867 1829 -3 -28 12 C ATOM 4127 N THR C 53 -22.132 18.282 39.616 1.00 13.43 N ANISOU 4127 N THR C 53 1745 1698 1661 -4 -12 -4 N ATOM 4128 CA THR C 53 -22.425 18.280 41.051 1.00 13.30 C ANISOU 4128 CA THR C 53 1702 1695 1658 2 -4 5 C ATOM 4129 C THR C 53 -23.704 17.509 41.322 1.00 13.18 C ANISOU 4129 C THR C 53 1727 1651 1629 -12 -1 19 C ATOM 4130 O THR C 53 -24.600 17.468 40.471 1.00 13.73 O ANISOU 4130 O THR C 53 1809 1700 1710 -7 -62 37 O ATOM 4131 CB THR C 53 -22.544 19.725 41.568 1.00 13.32 C ANISOU 4131 CB THR C 53 1726 1723 1611 5 -9 -26 C ATOM 4132 OG1 THR C 53 -22.830 19.736 42.974 1.00 12.32 O ANISOU 4132 OG1 THR C 53 1601 1558 1524 55 -79 11 O ATOM 4133 CG2 THR C 53 -23.664 20.468 40.847 1.00 13.54 C ANISOU 4133 CG2 THR C 53 1791 1647 1705 -4 -43 6 C ATOM 4134 N ASN C 54 -23.856 16.940 42.517 1.00 12.51 N ANISOU 4134 N ASN C 54 1638 1540 1576 -28 -20 -15 N ATOM 4135 CA ASN C 54 -25.116 16.298 42.881 1.00 12.32 C ANISOU 4135 CA ASN C 54 1616 1564 1502 -11 -17 27 C ATOM 4136 C ASN C 54 -26.240 17.301 43.119 1.00 12.97 C ANISOU 4136 C ASN C 54 1658 1644 1627 14 -5 3 C ATOM 4137 O ASN C 54 -27.416 16.940 43.008 1.00 13.17 O ANISOU 4137 O ASN C 54 1674 1658 1672 12 -48 -19 O ATOM 4138 CB ASN C 54 -24.942 15.402 44.113 1.00 12.23 C ANISOU 4138 CB ASN C 54 1661 1501 1483 -16 -63 3 C ATOM 4139 CG ASN C 54 -24.600 16.217 45.351 1.00 11.79 C ANISOU 4139 CG ASN C 54 1526 1491 1464 3 6 -14 C ATOM 4140 OD1 ASN C 54 -23.591 16.921 45.341 1.00 12.21 O ANISOU 4140 OD1 ASN C 54 1654 1483 1504 -63 -94 -25 O ATOM 4141 ND2 ASN C 54 -25.441 16.127 46.370 1.00 11.68 N ANISOU 4141 ND2 ASN C 54 1490 1532 1415 7 -51 10 N ATOM 4142 N ASP C 55 -25.911 18.548 43.433 1.00 13.54 N ANISOU 4142 N ASP C 55 1738 1692 1717 3 -46 -33 N ATOM 4143 CA ASP C 55 -26.904 19.531 43.856 1.00 13.83 C ANISOU 4143 CA ASP C 55 1734 1718 1805 13 -59 -29 C ATOM 4144 C ASP C 55 -26.460 20.928 43.443 1.00 14.12 C ANISOU 4144 C ASP C 55 1805 1740 1820 11 -69 -4 C ATOM 4145 O ASP C 55 -25.614 21.552 44.088 1.00 13.72 O ANISOU 4145 O ASP C 55 1805 1663 1743 -1 -46 -2 O ATOM 4146 CB ASP C 55 -27.098 19.435 45.365 1.00 16.59 C ANISOU 4146 CB ASP C 55 2241 2124 1937 -28 -8 42 C ATOM 4147 CG ASP C 55 -28.148 20.335 45.966 1.00 18.66 C ANISOU 4147 CG ASP C 55 2279 2356 2454 31 6 -40 C ATOM 4148 OD1 ASP C 55 -28.526 21.364 45.378 1.00 19.21 O ANISOU 4148 OD1 ASP C 55 2432 2423 2443 -3 -40 -1 O ATOM 4149 OD2 ASP C 55 -28.622 20.019 47.084 1.00 20.76 O ANISOU 4149 OD2 ASP C 55 2657 2676 2555 -3 42 -4 O ATOM 4150 N LEU C 56 -27.050 21.453 42.371 1.00 14.38 N ANISOU 4150 N LEU C 56 1903 1780 1782 12 -74 -19 N ATOM 4151 CA LEU C 56 -26.667 22.764 41.859 1.00 14.79 C ANISOU 4151 CA LEU C 56 1931 1807 1880 -3 -5 -28 C ATOM 4152 C LEU C 56 -26.890 23.867 42.888 1.00 14.26 C ANISOU 4152 C LEU C 56 1831 1799 1789 17 -14 8 C ATOM 4153 O LEU C 56 -26.064 24.775 43.014 1.00 14.74 O ANISOU 4153 O LEU C 56 1896 1865 1840 -10 -53 -43 O ATOM 4154 CB LEU C 56 -27.445 23.078 40.576 1.00 17.10 C ANISOU 4154 CB LEU C 56 2215 2215 2066 51 -123 43 C ATOM 4155 CG LEU C 56 -26.989 22.352 39.310 1.00 18.38 C ANISOU 4155 CG LEU C 56 2359 2319 2306 29 25 -53 C ATOM 4156 CD1 LEU C 56 -28.037 22.478 38.213 1.00 19.69 C ANISOU 4156 CD1 LEU C 56 2524 2518 2441 6 -66 -2 C ATOM 4157 CD2 LEU C 56 -25.649 22.888 38.827 1.00 18.88 C ANISOU 4157 CD2 LEU C 56 2398 2408 2367 17 -3 26 C ATOM 4158 N ALA C 57 -27.997 23.807 43.615 1.00 13.82 N ANISOU 4158 N ALA C 57 1810 1742 1698 41 -43 2 N ATOM 4159 CA ALA C 57 -28.300 24.809 44.633 1.00 13.89 C ANISOU 4159 CA ALA C 57 1826 1726 1724 17 -40 -12 C ATOM 4160 C ALA C 57 -27.238 24.813 45.729 1.00 14.08 C ANISOU 4160 C ALA C 57 1827 1761 1763 6 -51 15 C ATOM 4161 O ALA C 57 -26.682 25.867 46.057 1.00 14.61 O ANISOU 4161 O ALA C 57 1914 1807 1830 -20 -70 -19 O ATOM 4162 CB ALA C 57 -29.668 24.557 45.244 1.00 15.23 C ANISOU 4162 CB ALA C 57 1891 1979 1919 -2 -2 -18 C ATOM 4163 N ARG C 58 -26.941 23.635 46.284 1.00 13.47 N ANISOU 4163 N ARG C 58 1698 1747 1672 -2 -56 -1 N ATOM 4164 CA ARG C 58 -25.969 23.603 47.380 1.00 12.76 C ANISOU 4164 CA ARG C 58 1648 1605 1596 -12 -17 21 C ATOM 4165 C ARG C 58 -24.560 23.891 46.895 1.00 12.44 C ANISOU 4165 C ARG C 58 1621 1550 1554 5 -34 -6 C ATOM 4166 O ARG C 58 -23.760 24.507 47.612 1.00 12.22 O ANISOU 4166 O ARG C 58 1634 1482 1528 -3 -57 28 O ATOM 4167 CB ARG C 58 -26.015 22.285 48.162 1.00 12.40 C ANISOU 4167 CB ARG C 58 1609 1571 1530 3 -63 1 C ATOM 4168 CG ARG C 58 -25.077 22.363 49.365 1.00 11.99 C ANISOU 4168 CG ARG C 58 1536 1501 1518 6 -38 -44 C ATOM 4169 CD ARG C 58 -25.333 21.290 50.409 1.00 13.13 C ANISOU 4169 CD ARG C 58 1729 1672 1588 -34 -2 17 C ATOM 4170 NE ARG C 58 -24.314 21.436 51.455 1.00 14.06 N ANISOU 4170 NE ARG C 58 1765 1849 1730 17 -69 20 N ATOM 4171 CZ ARG C 58 -24.529 21.334 52.757 1.00 13.60 C ANISOU 4171 CZ ARG C 58 1693 1754 1720 18 -30 30 C ATOM 4172 NH1 ARG C 58 -25.736 21.070 53.230 1.00 13.58 N ANISOU 4172 NH1 ARG C 58 1735 1747 1678 -6 12 -52 N ATOM 4173 NH2 ARG C 58 -23.505 21.516 53.588 1.00 13.37 N ANISOU 4173 NH2 ARG C 58 1754 1713 1615 -21 -24 -8 N ATOM 4174 N ALA C 59 -24.223 23.532 45.660 1.00 12.19 N ANISOU 4174 N ALA C 59 1567 1532 1532 5 -40 14 N ATOM 4175 CA ALA C 59 -22.915 23.798 45.086 1.00 12.21 C ANISOU 4175 CA ALA C 59 1572 1540 1525 -9 -17 -17 C ATOM 4176 C ALA C 59 -22.529 25.271 45.135 1.00 11.88 C ANISOU 4176 C ALA C 59 1528 1534 1453 -14 -2 11 C ATOM 4177 O ALA C 59 -21.343 25.581 45.273 1.00 11.63 O ANISOU 4177 O ALA C 59 1507 1539 1374 41 -81 8 O ATOM 4178 CB ALA C 59 -22.853 23.298 43.644 1.00 13.12 C ANISOU 4178 CB ALA C 59 1729 1701 1556 57 8 -34 C ATOM 4179 N SER C 60 -23.485 26.188 45.010 1.00 12.46 N ANISOU 4179 N SER C 60 1584 1591 1561 17 -46 6 N ATOM 4180 CA SER C 60 -23.207 27.613 45.092 1.00 13.12 C ANISOU 4180 CA SER C 60 1728 1613 1645 1 -24 -19 C ATOM 4181 C SER C 60 -23.549 28.233 46.442 1.00 13.04 C ANISOU 4181 C SER C 60 1684 1623 1649 28 -23 -2 C ATOM 4182 O SER C 60 -23.296 29.435 46.596 1.00 13.37 O ANISOU 4182 O SER C 60 1761 1655 1665 -2 -91 -40 O ATOM 4183 CB ASER C 60 -23.967 28.357 43.985 0.50 14.51 C ANISOU 4183 CB ASER C 60 1903 1789 1820 51 -70 62 C ATOM 4184 CB BSER C 60 -23.959 28.349 43.975 0.50 13.03 C ANISOU 4184 CB BSER C 60 1656 1635 1660 24 27 -14 C ATOM 4185 OG ASER C 60 -25.357 28.367 44.253 0.50 16.39 O ANISOU 4185 OG ASER C 60 2038 2078 2113 5 18 44 O ATOM 4186 OG BSER C 60 -23.438 27.975 42.711 0.50 12.29 O ANISOU 4186 OG BSER C 60 1640 1511 1517 43 -60 46 O ATOM 4187 N LYS C 61 -24.089 27.481 47.391 1.00 13.04 N ANISOU 4187 N LYS C 61 1687 1652 1615 28 -25 -16 N ATOM 4188 CA LYS C 61 -24.292 28.028 48.736 1.00 13.31 C ANISOU 4188 CA LYS C 61 1698 1710 1647 40 -34 -48 C ATOM 4189 C LYS C 61 -22.956 28.203 49.450 1.00 13.12 C ANISOU 4189 C LYS C 61 1685 1661 1639 20 -19 -21 C ATOM 4190 O LYS C 61 -22.025 27.431 49.231 1.00 13.15 O ANISOU 4190 O LYS C 61 1700 1603 1692 8 -18 -8 O ATOM 4191 CB LYS C 61 -25.228 27.153 49.566 1.00 15.23 C ANISOU 4191 CB LYS C 61 2068 1837 1883 -63 73 20 C ATOM 4192 CG LYS C 61 -26.702 27.365 49.250 1.00 19.51 C ANISOU 4192 CG LYS C 61 2348 2520 2547 78 -91 -58 C ATOM 4193 CD LYS C 61 -27.581 26.442 50.078 1.00 22.95 C ANISOU 4193 CD LYS C 61 2999 2838 2884 -92 74 49 C ATOM 4194 CE LYS C 61 -29.050 26.808 49.958 1.00 26.30 C ANISOU 4194 CE LYS C 61 3242 3329 3424 38 18 7 C ATOM 4195 NZ LYS C 61 -29.498 26.884 48.542 1.00 27.53 N ANISOU 4195 NZ LYS C 61 3517 3449 3496 12 -18 -12 N ATOM 4196 N GLU C 62 -22.864 29.223 50.299 1.00 13.12 N ANISOU 4196 N GLU C 62 1686 1672 1626 -1 -48 -13 N ATOM 4197 CA GLU C 62 -21.576 29.575 50.900 1.00 13.18 C ANISOU 4197 CA GLU C 62 1649 1708 1650 21 -13 -20 C ATOM 4198 C GLU C 62 -21.503 29.162 52.359 1.00 13.31 C ANISOU 4198 C GLU C 62 1666 1725 1668 41 -11 12 C ATOM 4199 O GLU C 62 -22.398 29.444 53.156 1.00 13.73 O ANISOU 4199 O GLU C 62 1705 1838 1674 80 -10 7 O ATOM 4200 CB GLU C 62 -21.332 31.077 50.731 1.00 14.55 C ANISOU 4200 CB GLU C 62 1847 1775 1907 -14 -36 13 C ATOM 4201 CG GLU C 62 -21.230 31.509 49.276 1.00 16.27 C ANISOU 4201 CG GLU C 62 2077 2137 1968 22 27 -2 C ATOM 4202 CD GLU C 62 -20.966 32.990 49.112 1.00 18.81 C ANISOU 4202 CD GLU C 62 2470 2258 2418 -8 -40 -5 C ATOM 4203 OE1 GLU C 62 -21.547 33.794 49.869 1.00 19.34 O ANISOU 4203 OE1 GLU C 62 2533 2329 2487 77 -15 13 O ATOM 4204 OE2 GLU C 62 -20.174 33.360 48.223 1.00 20.54 O ANISOU 4204 OE2 GLU C 62 2720 2525 2557 -1 76 6 O ATOM 4205 N TYR C 63 -20.438 28.453 52.721 1.00 12.70 N ANISOU 4205 N TYR C 63 1648 1631 1546 22 -3 8 N ATOM 4206 CA TYR C 63 -20.233 27.918 54.057 1.00 12.31 C ANISOU 4206 CA TYR C 63 1572 1569 1538 -15 -19 -11 C ATOM 4207 C TYR C 63 -18.922 28.414 54.660 1.00 11.54 C ANISOU 4207 C TYR C 63 1498 1465 1424 26 7 -6 C ATOM 4208 O TYR C 63 -17.993 28.810 53.951 1.00 10.76 O ANISOU 4208 O TYR C 63 1405 1397 1288 19 -74 -51 O ATOM 4209 CB TYR C 63 -20.231 26.379 54.037 1.00 12.62 C ANISOU 4209 CB TYR C 63 1635 1578 1582 25 0 -2 C ATOM 4210 CG TYR C 63 -21.559 25.808 53.581 1.00 13.56 C ANISOU 4210 CG TYR C 63 1719 1696 1737 -24 -21 -10 C ATOM 4211 CD1 TYR C 63 -22.594 25.598 54.483 1.00 14.50 C ANISOU 4211 CD1 TYR C 63 1800 1865 1846 -28 28 14 C ATOM 4212 CD2 TYR C 63 -21.777 25.519 52.242 1.00 13.78 C ANISOU 4212 CD2 TYR C 63 1762 1727 1746 -2 -4 -15 C ATOM 4213 CE1 TYR C 63 -23.812 25.092 54.063 1.00 14.99 C ANISOU 4213 CE1 TYR C 63 1879 1928 1888 -39 -26 -10 C ATOM 4214 CE2 TYR C 63 -22.993 25.017 51.813 1.00 14.29 C ANISOU 4214 CE2 TYR C 63 1825 1781 1824 -21 -25 -34 C ATOM 4215 CZ TYR C 63 -24.000 24.803 52.727 1.00 14.85 C ANISOU 4215 CZ TYR C 63 1886 1871 1883 -9 25 -44 C ATOM 4216 OH TYR C 63 -25.211 24.305 52.305 1.00 15.54 O ANISOU 4216 OH TYR C 63 1920 1939 2045 2 9 -98 O ATOM 4217 N LEU C 64 -18.848 28.429 55.992 1.00 11.64 N ANISOU 4217 N LEU C 64 1503 1482 1439 30 -11 -20 N ATOM 4218 CA LEU C 64 -17.565 28.661 56.656 1.00 11.71 C ANISOU 4218 CA LEU C 64 1489 1509 1451 20 1 -7 C ATOM 4219 C LEU C 64 -16.492 27.772 56.042 1.00 11.30 C ANISOU 4219 C LEU C 64 1491 1434 1370 -1 -10 -5 C ATOM 4220 O LEU C 64 -16.664 26.555 55.948 1.00 11.38 O ANISOU 4220 O LEU C 64 1500 1438 1386 -35 -43 -4 O ATOM 4221 CB LEU C 64 -17.690 28.312 58.144 1.00 12.48 C ANISOU 4221 CB LEU C 64 1680 1584 1478 23 -14 14 C ATOM 4222 CG LEU C 64 -18.419 29.340 59.014 1.00 13.21 C ANISOU 4222 CG LEU C 64 1717 1612 1688 16 36 -26 C ATOM 4223 CD1 LEU C 64 -18.954 28.681 60.273 1.00 13.74 C ANISOU 4223 CD1 LEU C 64 1757 1744 1718 -22 16 10 C ATOM 4224 CD2 LEU C 64 -17.469 30.484 59.342 1.00 13.48 C ANISOU 4224 CD2 LEU C 64 1754 1714 1654 -13 -20 -84 C ATOM 4225 N PRO C 65 -15.362 28.363 55.678 1.00 11.37 N ANISOU 4225 N PRO C 65 1472 1434 1416 26 -1 -22 N ATOM 4226 CA PRO C 65 -14.257 27.606 55.113 1.00 10.94 C ANISOU 4226 CA PRO C 65 1416 1390 1350 29 -23 5 C ATOM 4227 C PRO C 65 -13.573 26.763 56.180 1.00 11.19 C ANISOU 4227 C PRO C 65 1431 1416 1403 64 -41 -1 C ATOM 4228 O PRO C 65 -13.049 25.699 55.860 1.00 10.69 O ANISOU 4228 O PRO C 65 1445 1302 1314 21 -61 32 O ATOM 4229 CB PRO C 65 -13.335 28.635 54.490 1.00 10.94 C ANISOU 4229 CB PRO C 65 1435 1379 1341 6 -51 -17 C ATOM 4230 CG PRO C 65 -13.731 29.938 55.094 1.00 11.44 C ANISOU 4230 CG PRO C 65 1475 1429 1443 20 -12 -48 C ATOM 4231 CD PRO C 65 -15.184 29.823 55.463 1.00 11.48 C ANISOU 4231 CD PRO C 65 1481 1447 1433 -10 -1 -12 C ATOM 4232 N ALA C 66 -13.613 27.217 57.428 1.00 11.82 N ANISOU 4232 N ALA C 66 1538 1506 1445 80 -40 -32 N ATOM 4233 CA ALA C 66 -12.930 26.497 58.504 1.00 11.65 C ANISOU 4233 CA ALA C 66 1524 1503 1399 42 -23 -30 C ATOM 4234 C ALA C 66 -11.519 26.157 58.049 1.00 11.22 C ANISOU 4234 C ALA C 66 1487 1439 1336 -7 -29 -36 C ATOM 4235 O ALA C 66 -10.851 27.008 57.457 1.00 11.24 O ANISOU 4235 O ALA C 66 1543 1486 1242 -12 -40 -36 O ATOM 4236 CB ALA C 66 -13.736 25.274 58.895 1.00 12.99 C ANISOU 4236 CB ALA C 66 1688 1616 1631 -34 11 0 C ATOM 4237 N SER C 67 -11.047 24.931 58.261 1.00 11.63 N ANISOU 4237 N SER C 67 1533 1482 1403 28 6 -28 N ATOM 4238 CA SER C 67 -9.660 24.574 58.018 1.00 11.19 C ANISOU 4238 CA SER C 67 1468 1392 1391 -26 -34 -45 C ATOM 4239 C SER C 67 -9.267 24.525 56.552 1.00 11.18 C ANISOU 4239 C SER C 67 1431 1422 1395 17 -29 -6 C ATOM 4240 O SER C 67 -8.064 24.505 56.260 1.00 11.30 O ANISOU 4240 O SER C 67 1433 1459 1403 -28 -31 7 O ATOM 4241 CB SER C 67 -9.277 23.277 58.740 1.00 13.06 C ANISOU 4241 CB SER C 67 1789 1551 1620 77 -77 28 C ATOM 4242 OG SER C 67 -10.404 22.523 59.126 1.00 15.12 O ANISOU 4242 OG SER C 67 1869 1988 1889 -32 -67 27 O ATOM 4243 N THR C 68 -10.200 24.627 55.597 1.00 10.94 N ANISOU 4243 N THR C 68 1460 1348 1350 -5 -32 -39 N ATOM 4244 CA THR C 68 -9.805 24.898 54.216 1.00 11.01 C ANISOU 4244 CA THR C 68 1421 1399 1365 -20 -19 -12 C ATOM 4245 C THR C 68 -9.220 26.290 54.041 1.00 10.81 C ANISOU 4245 C THR C 68 1408 1356 1346 20 -11 -20 C ATOM 4246 O THR C 68 -8.487 26.555 53.081 1.00 10.36 O ANISOU 4246 O THR C 68 1342 1236 1358 -49 -22 -36 O ATOM 4247 CB THR C 68 -10.955 24.701 53.208 1.00 11.31 C ANISOU 4247 CB THR C 68 1354 1416 1528 -12 -46 10 C ATOM 4248 OG1 THR C 68 -11.939 25.715 53.399 1.00 10.17 O ANISOU 4248 OG1 THR C 68 1296 1266 1304 -102 -68 -80 O ATOM 4249 CG2 THR C 68 -11.583 23.322 53.370 1.00 10.94 C ANISOU 4249 CG2 THR C 68 1471 1365 1319 -8 -7 14 C ATOM 4250 N PHE C 69 -9.465 27.213 54.977 1.00 10.77 N ANISOU 4250 N PHE C 69 1427 1323 1342 37 -44 -8 N ATOM 4251 CA PHE C 69 -8.835 28.520 54.962 1.00 10.85 C ANISOU 4251 CA PHE C 69 1372 1365 1386 7 -18 -38 C ATOM 4252 C PHE C 69 -7.331 28.481 55.176 1.00 10.48 C ANISOU 4252 C PHE C 69 1357 1322 1302 13 -14 -3 C ATOM 4253 O PHE C 69 -6.635 29.439 54.803 1.00 10.43 O ANISOU 4253 O PHE C 69 1381 1316 1266 23 -34 31 O ATOM 4254 CB PHE C 69 -9.482 29.450 56.005 1.00 10.53 C ANISOU 4254 CB PHE C 69 1374 1291 1338 -13 -8 -3 C ATOM 4255 CG PHE C 69 -9.105 30.888 55.746 1.00 10.07 C ANISOU 4255 CG PHE C 69 1307 1271 1250 -16 -16 -4 C ATOM 4256 CD1 PHE C 69 -9.632 31.563 54.661 1.00 10.34 C ANISOU 4256 CD1 PHE C 69 1306 1328 1295 -2 -61 0 C ATOM 4257 CD2 PHE C 69 -8.217 31.548 56.580 1.00 9.73 C ANISOU 4257 CD2 PHE C 69 1280 1229 1187 18 -20 23 C ATOM 4258 CE1 PHE C 69 -9.285 32.877 54.407 1.00 11.33 C ANISOU 4258 CE1 PHE C 69 1485 1372 1446 -49 -44 -20 C ATOM 4259 CE2 PHE C 69 -7.863 32.860 56.330 1.00 10.53 C ANISOU 4259 CE2 PHE C 69 1395 1268 1337 -33 -24 -35 C ATOM 4260 CZ PHE C 69 -8.393 33.528 55.244 1.00 10.79 C ANISOU 4260 CZ PHE C 69 1420 1323 1358 31 -28 -35 C ATOM 4261 N LYS C 70 -6.746 27.391 55.672 1.00 9.88 N ANISOU 4261 N LYS C 70 1326 1261 1168 7 -4 -85 N ATOM 4262 CA LYS C 70 -5.295 27.260 55.741 1.00 10.24 C ANISOU 4262 CA LYS C 70 1325 1319 1247 -13 -15 -65 C ATOM 4263 C LYS C 70 -4.619 27.444 54.391 1.00 10.35 C ANISOU 4263 C LYS C 70 1322 1334 1275 -10 -3 -36 C ATOM 4264 O LYS C 70 -3.480 27.911 54.341 1.00 9.91 O ANISOU 4264 O LYS C 70 1345 1193 1226 -29 3 -69 O ATOM 4265 CB LYS C 70 -4.894 25.921 56.382 1.00 12.21 C ANISOU 4265 CB LYS C 70 1586 1425 1629 26 -82 18 C ATOM 4266 CG LYS C 70 -5.435 25.773 57.794 1.00 14.44 C ANISOU 4266 CG LYS C 70 1822 1918 1749 -40 -15 -32 C ATOM 4267 CD LYS C 70 -5.356 24.362 58.341 1.00 17.48 C ANISOU 4267 CD LYS C 70 2336 2108 2199 -3 -33 49 C ATOM 4268 CE LYS C 70 -3.975 24.023 58.864 1.00 18.08 C ANISOU 4268 CE LYS C 70 2307 2203 2359 -15 -6 22 C ATOM 4269 NZ LYS C 70 -3.998 22.856 59.796 1.00 17.21 N ANISOU 4269 NZ LYS C 70 2272 2187 2082 21 -59 -37 N ATOM 4270 N ILE C 71 -5.274 27.097 53.281 1.00 10.82 N ANISOU 4270 N ILE C 71 1445 1358 1309 -13 -40 -49 N ATOM 4271 CA ILE C 71 -4.697 27.362 51.966 1.00 11.06 C ANISOU 4271 CA ILE C 71 1493 1378 1330 -27 -19 -21 C ATOM 4272 C ILE C 71 -4.423 28.828 51.704 1.00 10.98 C ANISOU 4272 C ILE C 71 1442 1390 1338 -16 -22 12 C ATOM 4273 O ILE C 71 -3.257 29.228 51.591 1.00 10.40 O ANISOU 4273 O ILE C 71 1411 1281 1260 21 -40 59 O ATOM 4274 CB ILE C 71 -5.538 26.693 50.860 1.00 11.23 C ANISOU 4274 CB ILE C 71 1513 1398 1355 -40 -32 -34 C ATOM 4275 CG1 ILE C 71 -5.691 25.208 51.188 1.00 11.36 C ANISOU 4275 CG1 ILE C 71 1508 1431 1378 17 -47 31 C ATOM 4276 CG2 ILE C 71 -4.866 26.920 49.515 1.00 12.17 C ANISOU 4276 CG2 ILE C 71 1584 1568 1470 12 56 -8 C ATOM 4277 CD1 ILE C 71 -6.436 24.382 50.165 1.00 11.93 C ANISOU 4277 CD1 ILE C 71 1567 1483 1484 9 -44 -49 C ATOM 4278 N PRO C 72 -5.439 29.681 51.669 1.00 11.66 N ANISOU 4278 N PRO C 72 1526 1435 1469 19 -27 -1 N ATOM 4279 CA PRO C 72 -5.240 31.108 51.452 1.00 11.74 C ANISOU 4279 CA PRO C 72 1526 1440 1495 5 -20 -8 C ATOM 4280 C PRO C 72 -4.423 31.752 52.558 1.00 12.11 C ANISOU 4280 C PRO C 72 1572 1518 1509 -28 -19 -29 C ATOM 4281 O PRO C 72 -3.578 32.605 52.277 1.00 12.20 O ANISOU 4281 O PRO C 72 1586 1565 1485 -55 -25 -36 O ATOM 4282 CB PRO C 72 -6.641 31.690 51.368 1.00 11.83 C ANISOU 4282 CB PRO C 72 1503 1493 1498 -16 -38 -3 C ATOM 4283 CG PRO C 72 -7.533 30.670 51.986 1.00 12.07 C ANISOU 4283 CG PRO C 72 1577 1457 1550 4 4 17 C ATOM 4284 CD PRO C 72 -6.874 29.338 51.676 1.00 11.91 C ANISOU 4284 CD PRO C 72 1543 1452 1529 3 -11 -28 C ATOM 4285 N ASN C 73 -4.620 31.332 53.806 1.00 12.18 N ANISOU 4285 N ASN C 73 1588 1514 1525 -15 -14 -28 N ATOM 4286 CA ASN C 73 -3.880 31.901 54.933 1.00 12.12 C ANISOU 4286 CA ASN C 73 1553 1519 1534 -4 -24 -9 C ATOM 4287 C ASN C 73 -2.389 31.628 54.797 1.00 11.94 C ANISOU 4287 C ASN C 73 1543 1487 1507 -9 -26 -15 C ATOM 4288 O ASN C 73 -1.578 32.527 55.027 1.00 12.05 O ANISOU 4288 O ASN C 73 1536 1538 1507 -33 -21 -29 O ATOM 4289 CB ASN C 73 -4.453 31.371 56.243 1.00 12.84 C ANISOU 4289 CB ASN C 73 1651 1679 1547 -42 4 -18 C ATOM 4290 CG ASN C 73 -4.241 32.243 57.460 1.00 13.23 C ANISOU 4290 CG ASN C 73 1764 1512 1752 -53 -6 -71 C ATOM 4291 OD1 ASN C 73 -4.470 31.788 58.588 1.00 15.84 O ANISOU 4291 OD1 ASN C 73 2174 2002 1841 -46 8 -18 O ATOM 4292 ND2 ASN C 73 -3.812 33.479 57.268 1.00 10.26 N ANISOU 4292 ND2 ASN C 73 1355 1408 1135 -1 -57 -41 N ATOM 4293 N ALA C 74 -2.001 30.427 54.370 1.00 11.71 N ANISOU 4293 N ALA C 74 1477 1498 1474 17 -50 -35 N ATOM 4294 CA ALA C 74 -0.594 30.103 54.156 1.00 11.66 C ANISOU 4294 CA ALA C 74 1505 1456 1469 4 14 -36 C ATOM 4295 C ALA C 74 -0.001 30.918 53.010 1.00 11.93 C ANISOU 4295 C ALA C 74 1528 1517 1488 -13 7 -7 C ATOM 4296 O ALA C 74 1.100 31.450 53.136 1.00 12.34 O ANISOU 4296 O ALA C 74 1557 1587 1546 -31 -37 15 O ATOM 4297 CB ALA C 74 -0.426 28.617 53.872 1.00 11.50 C ANISOU 4297 CB ALA C 74 1433 1413 1523 2 -59 22 C ATOM 4298 N ILE C 75 -0.722 31.021 51.895 1.00 11.93 N ANISOU 4298 N ILE C 75 1543 1490 1499 -15 -7 2 N ATOM 4299 CA ILE C 75 -0.265 31.811 50.755 1.00 11.88 C ANISOU 4299 CA ILE C 75 1559 1477 1479 6 5 -16 C ATOM 4300 C ILE C 75 -0.054 33.270 51.147 1.00 12.32 C ANISOU 4300 C ILE C 75 1598 1510 1573 -27 11 -34 C ATOM 4301 O ILE C 75 0.966 33.873 50.816 1.00 12.57 O ANISOU 4301 O ILE C 75 1620 1524 1633 -49 27 -101 O ATOM 4302 CB ILE C 75 -1.255 31.712 49.582 1.00 11.78 C ANISOU 4302 CB ILE C 75 1531 1418 1528 -16 -10 15 C ATOM 4303 CG1 ILE C 75 -1.337 30.253 49.110 1.00 11.33 C ANISOU 4303 CG1 ILE C 75 1444 1432 1431 -30 -4 -26 C ATOM 4304 CG2 ILE C 75 -0.850 32.610 48.425 1.00 11.87 C ANISOU 4304 CG2 ILE C 75 1600 1459 1453 -20 -7 -13 C ATOM 4305 CD1 ILE C 75 -2.460 29.999 48.122 1.00 11.88 C ANISOU 4305 CD1 ILE C 75 1533 1533 1448 -41 -47 11 C ATOM 4306 N ILE C 76 -1.033 33.837 51.843 1.00 12.38 N ANISOU 4306 N ILE C 76 1637 1493 1576 4 16 -22 N ATOM 4307 CA ILE C 76 -0.953 35.224 52.297 1.00 12.39 C ANISOU 4307 CA ILE C 76 1623 1521 1563 0 0 -37 C ATOM 4308 C ILE C 76 0.161 35.404 53.316 1.00 12.56 C ANISOU 4308 C ILE C 76 1619 1559 1596 -2 -9 -7 C ATOM 4309 O ILE C 76 0.916 36.378 53.248 1.00 12.47 O ANISOU 4309 O ILE C 76 1605 1532 1600 1 -22 -35 O ATOM 4310 CB ILE C 76 -2.309 35.678 52.857 1.00 12.51 C ANISOU 4310 CB ILE C 76 1600 1571 1581 10 -12 14 C ATOM 4311 CG1 ILE C 76 -3.379 35.609 51.761 1.00 12.52 C ANISOU 4311 CG1 ILE C 76 1610 1540 1605 -13 -19 -56 C ATOM 4312 CG2 ILE C 76 -2.226 37.088 53.429 1.00 13.56 C ANISOU 4312 CG2 ILE C 76 1775 1631 1745 28 -24 -34 C ATOM 4313 CD1 ILE C 76 -4.795 35.659 52.292 1.00 13.90 C ANISOU 4313 CD1 ILE C 76 1692 1783 1807 -18 35 -43 C ATOM 4314 N GLY C 77 0.321 34.451 54.232 1.00 12.58 N ANISOU 4314 N GLY C 77 1645 1570 1563 19 11 -15 N ATOM 4315 CA GLY C 77 1.466 34.435 55.136 1.00 13.03 C ANISOU 4315 CA GLY C 77 1667 1658 1627 14 -14 -31 C ATOM 4316 C GLY C 77 2.798 34.536 54.406 1.00 13.25 C ANISOU 4316 C GLY C 77 1690 1670 1673 -4 8 -36 C ATOM 4317 O GLY C 77 3.664 35.347 54.749 1.00 13.54 O ANISOU 4317 O GLY C 77 1740 1681 1723 -25 -4 -38 O ATOM 4318 N LEU C 78 2.997 33.708 53.382 1.00 13.02 N ANISOU 4318 N LEU C 78 1678 1638 1632 -8 -24 -30 N ATOM 4319 CA LEU C 78 4.198 33.759 52.563 1.00 13.12 C ANISOU 4319 CA LEU C 78 1698 1645 1643 -11 -6 -61 C ATOM 4320 C LEU C 78 4.324 35.062 51.785 1.00 14.06 C ANISOU 4320 C LEU C 78 1848 1717 1778 -10 12 -9 C ATOM 4321 O LEU C 78 5.399 35.666 51.762 1.00 14.62 O ANISOU 4321 O LEU C 78 1871 1789 1894 -21 1 -30 O ATOM 4322 CB LEU C 78 4.223 32.567 51.601 1.00 11.99 C ANISOU 4322 CB LEU C 78 1539 1505 1513 -10 -26 31 C ATOM 4323 CG LEU C 78 4.485 31.202 52.241 1.00 11.83 C ANISOU 4323 CG LEU C 78 1525 1431 1540 -14 -72 -48 C ATOM 4324 CD1 LEU C 78 4.022 30.094 51.303 1.00 11.42 C ANISOU 4324 CD1 LEU C 78 1543 1406 1391 24 2 -53 C ATOM 4325 CD2 LEU C 78 5.955 31.029 52.584 1.00 11.91 C ANISOU 4325 CD2 LEU C 78 1518 1436 1571 -9 -29 -73 C ATOM 4326 N GLU C 79 3.245 35.529 51.167 1.00 14.87 N ANISOU 4326 N GLU C 79 1901 1844 1906 13 -23 -46 N ATOM 4327 CA GLU C 79 3.281 36.727 50.340 1.00 15.81 C ANISOU 4327 CA GLU C 79 2063 1962 1983 -5 22 24 C ATOM 4328 C GLU C 79 3.676 37.978 51.118 1.00 16.55 C ANISOU 4328 C GLU C 79 2140 2028 2118 -19 1 -21 C ATOM 4329 O GLU C 79 4.394 38.841 50.608 1.00 16.32 O ANISOU 4329 O GLU C 79 2095 2009 2096 -10 -6 -39 O ATOM 4330 CB GLU C 79 1.918 36.981 49.688 1.00 17.45 C ANISOU 4330 CB GLU C 79 2148 2179 2304 29 -37 38 C ATOM 4331 CG GLU C 79 1.688 36.192 48.413 1.00 19.46 C ANISOU 4331 CG GLU C 79 2500 2508 2387 8 -42 -40 C ATOM 4332 CD GLU C 79 2.661 36.582 47.315 1.00 20.41 C ANISOU 4332 CD GLU C 79 2523 2662 2572 0 36 -28 C ATOM 4333 OE1 GLU C 79 2.580 37.721 46.810 1.00 23.22 O ANISOU 4333 OE1 GLU C 79 3104 2765 2954 22 -43 -24 O ATOM 4334 OE2 GLU C 79 3.507 35.739 46.956 1.00 19.63 O ANISOU 4334 OE2 GLU C 79 2466 2509 2484 -50 -25 -15 O ATOM 4335 N THR C 80 3.184 38.081 52.347 1.00 17.33 N ANISOU 4335 N THR C 80 2225 2197 2164 1 34 8 N ATOM 4336 CA THR C 80 3.421 39.239 53.190 1.00 17.99 C ANISOU 4336 CA THR C 80 2326 2256 2253 -6 25 -25 C ATOM 4337 C THR C 80 4.739 39.176 53.944 1.00 18.96 C ANISOU 4337 C THR C 80 2393 2392 2419 3 -22 1 C ATOM 4338 O THR C 80 5.136 40.163 54.573 1.00 19.99 O ANISOU 4338 O THR C 80 2567 2456 2572 -38 -30 -54 O ATOM 4339 CB THR C 80 2.287 39.396 54.229 1.00 17.37 C ANISOU 4339 CB THR C 80 2228 2181 2190 -6 -29 -34 C ATOM 4340 OG1 THR C 80 2.170 38.181 54.982 1.00 17.67 O ANISOU 4340 OG1 THR C 80 2238 2186 2290 -13 -22 -31 O ATOM 4341 CG2 THR C 80 0.970 39.720 53.547 1.00 17.95 C ANISOU 4341 CG2 THR C 80 2242 2268 2311 -6 -32 2 C ATOM 4342 N GLY C 81 5.383 38.015 53.974 1.00 18.90 N ANISOU 4342 N GLY C 81 2408 2390 2383 8 -8 -17 N ATOM 4343 CA GLY C 81 6.646 37.858 54.682 1.00 18.91 C ANISOU 4343 CA GLY C 81 2410 2379 2397 10 -5 -11 C ATOM 4344 C GLY C 81 6.448 37.362 56.106 1.00 18.61 C ANISOU 4344 C GLY C 81 2370 2324 2376 4 7 -28 C ATOM 4345 O GLY C 81 7.419 37.116 56.826 1.00 19.04 O ANISOU 4345 O GLY C 81 2384 2419 2429 -24 -27 -55 O ATOM 4346 N VAL C 82 5.200 37.176 56.521 1.00 18.14 N ANISOU 4346 N VAL C 82 2351 2231 2312 -24 -14 -36 N ATOM 4347 CA VAL C 82 4.878 36.646 57.843 1.00 18.08 C ANISOU 4347 CA VAL C 82 2314 2265 2292 -30 -18 -45 C ATOM 4348 C VAL C 82 5.442 35.239 57.998 1.00 18.44 C ANISOU 4348 C VAL C 82 2356 2296 2354 -16 -26 -10 C ATOM 4349 O VAL C 82 5.982 34.888 59.045 1.00 18.58 O ANISOU 4349 O VAL C 82 2393 2313 2353 -27 -36 -36 O ATOM 4350 CB VAL C 82 3.362 36.689 58.098 1.00 17.92 C ANISOU 4350 CB VAL C 82 2318 2270 2221 -7 1 -28 C ATOM 4351 CG1 VAL C 82 2.953 35.898 59.330 1.00 17.52 C ANISOU 4351 CG1 VAL C 82 2224 2197 2234 -34 -10 -30 C ATOM 4352 CG2 VAL C 82 2.903 38.139 58.248 1.00 18.49 C ANISOU 4352 CG2 VAL C 82 2401 2278 2346 -7 -2 6 C ATOM 4353 N ILE C 83 5.289 34.416 56.966 1.00 18.67 N ANISOU 4353 N ILE C 83 2384 2326 2385 -28 -22 -43 N ATOM 4354 CA ILE C 83 6.018 33.161 56.845 1.00 18.93 C ANISOU 4354 CA ILE C 83 2435 2316 2441 -40 -67 -52 C ATOM 4355 C ILE C 83 7.257 33.374 55.979 1.00 20.29 C ANISOU 4355 C ILE C 83 2631 2513 2565 -53 41 -16 C ATOM 4356 O ILE C 83 7.137 33.825 54.841 1.00 19.81 O ANISOU 4356 O ILE C 83 2530 2451 2548 -55 -7 -29 O ATOM 4357 CB ILE C 83 5.135 32.064 56.220 1.00 16.81 C ANISOU 4357 CB ILE C 83 2084 2157 2147 37 57 13 C ATOM 4358 CG1 ILE C 83 3.845 31.893 57.023 1.00 14.83 C ANISOU 4358 CG1 ILE C 83 1953 1806 1877 -11 -42 -33 C ATOM 4359 CG2 ILE C 83 5.898 30.748 56.144 1.00 17.25 C ANISOU 4359 CG2 ILE C 83 2179 2134 2239 19 -3 -23 C ATOM 4360 CD1 ILE C 83 2.775 31.065 56.343 1.00 15.16 C ANISOU 4360 CD1 ILE C 83 1927 1919 1914 -13 -44 -37 C ATOM 4361 N LYS C 84 8.437 33.055 56.505 1.00 22.36 N ANISOU 4361 N LYS C 84 2833 2804 2860 33 -72 1 N ATOM 4362 CA LYS C 84 9.683 33.385 55.826 1.00 24.67 C ANISOU 4362 CA LYS C 84 3117 3086 3171 -54 130 5 C ATOM 4363 C LYS C 84 9.870 32.613 54.526 1.00 25.02 C ANISOU 4363 C LYS C 84 3166 3151 3190 2 39 -11 C ATOM 4364 O LYS C 84 10.181 33.202 53.489 1.00 25.49 O ANISOU 4364 O LYS C 84 3230 3215 3239 -11 24 31 O ATOM 4365 CB LYS C 84 10.891 33.143 56.741 1.00 29.72 C ANISOU 4365 CB LYS C 84 3746 3820 3727 100 -249 7 C ATOM 4366 CG LYS C 84 12.195 33.651 56.142 1.00 34.70 C ANISOU 4366 CG LYS C 84 4342 4375 4467 -68 179 27 C ATOM 4367 CD LYS C 84 13.351 33.581 57.123 1.00 38.76 C ANISOU 4367 CD LYS C 84 4827 5047 4853 -24 -77 -7 C ATOM 4368 CE LYS C 84 13.853 32.160 57.312 1.00 41.89 C ANISOU 4368 CE LYS C 84 5368 5190 5358 16 34 6 C ATOM 4369 NZ LYS C 84 14.999 32.093 58.261 1.00 43.08 N ANISOU 4369 NZ LYS C 84 5464 5425 5481 2 -13 0 N ATOM 4370 N ASN C 85 9.726 31.294 54.582 1.00 25.20 N ANISOU 4370 N ASN C 85 3200 3162 3214 4 13 5 N ATOM 4371 CA ASN C 85 9.811 30.464 53.385 1.00 25.61 C ANISOU 4371 CA ASN C 85 3302 3193 3237 -7 -24 -4 C ATOM 4372 C ASN C 85 9.295 29.062 53.672 1.00 25.26 C ANISOU 4372 C ASN C 85 3213 3181 3202 11 -9 -2 C ATOM 4373 O ASN C 85 8.746 28.785 54.738 1.00 24.98 O ANISOU 4373 O ASN C 85 3164 3135 3190 24 -14 4 O ATOM 4374 CB ASN C 85 11.238 30.417 52.842 1.00 28.03 C ANISOU 4374 CB ASN C 85 3470 3607 3574 -2 93 -9 C ATOM 4375 CG ASN C 85 12.267 29.863 53.800 1.00 29.46 C ANISOU 4375 CG ASN C 85 3734 3733 3728 41 -31 16 C ATOM 4376 OD1 ASN C 85 12.034 28.896 54.526 1.00 29.53 O ANISOU 4376 OD1 ASN C 85 3718 3735 3765 9 5 17 O ATOM 4377 ND2 ASN C 85 13.445 30.479 53.816 1.00 30.11 N ANISOU 4377 ND2 ASN C 85 3809 3791 3839 -5 1 10 N ATOM 4378 N GLU C 86 9.539 28.142 52.744 1.00 25.15 N ANISOU 4378 N GLU C 86 3176 3187 3191 16 -10 14 N ATOM 4379 CA GLU C 86 9.086 26.767 52.848 1.00 25.42 C ANISOU 4379 CA GLU C 86 3192 3205 3263 11 -38 42 C ATOM 4380 C GLU C 86 9.712 25.991 53.997 1.00 24.74 C ANISOU 4380 C GLU C 86 3117 3122 3160 -13 -8 -7 C ATOM 4381 O GLU C 86 9.109 25.022 54.462 1.00 24.66 O ANISOU 4381 O GLU C 86 3105 3142 3124 -18 -10 -15 O ATOM 4382 CB GLU C 86 9.369 26.024 51.529 1.00 28.32 C ANISOU 4382 CB GLU C 86 3743 3574 3444 33 -28 -88 C ATOM 4383 CG GLU C 86 10.708 26.403 50.918 1.00 32.00 C ANISOU 4383 CG GLU C 86 3902 4130 4125 -36 5 51 C ATOM 4384 CD GLU C 86 11.098 25.546 49.735 1.00 34.51 C ANISOU 4384 CD GLU C 86 4377 4398 4336 45 -16 -87 C ATOM 4385 OE1 GLU C 86 10.984 24.304 49.817 1.00 36.04 O ANISOU 4385 OE1 GLU C 86 4596 4512 4586 -4 -6 37 O ATOM 4386 OE2 GLU C 86 11.526 26.106 48.709 1.00 35.91 O ANISOU 4386 OE2 GLU C 86 4584 4509 4549 -19 31 16 O ATOM 4387 N HIS C 87 10.901 26.374 54.450 1.00 24.13 N ANISOU 4387 N HIS C 87 3079 3051 3039 23 -8 6 N ATOM 4388 CA HIS C 87 11.596 25.660 55.505 1.00 23.64 C ANISOU 4388 CA HIS C 87 3022 2995 2964 6 10 -18 C ATOM 4389 C HIS C 87 11.453 26.306 56.877 1.00 23.37 C ANISOU 4389 C HIS C 87 2983 2959 2939 13 -11 -2 C ATOM 4390 O HIS C 87 12.135 25.879 57.813 1.00 22.82 O ANISOU 4390 O HIS C 87 2922 2923 2824 13 22 -59 O ATOM 4391 CB HIS C 87 13.087 25.510 55.157 1.00 23.90 C ANISOU 4391 CB HIS C 87 3020 3012 3049 -3 -2 24 C ATOM 4392 CG HIS C 87 13.285 24.802 53.850 1.00 24.78 C ANISOU 4392 CG HIS C 87 3144 3169 3102 21 -8 -13 C ATOM 4393 ND1 HIS C 87 12.701 23.580 53.590 1.00 25.77 N ANISOU 4393 ND1 HIS C 87 3320 3208 3262 2 -9 -14 N ATOM 4394 CD2 HIS C 87 13.980 25.134 52.740 1.00 24.58 C ANISOU 4394 CD2 HIS C 87 3065 3151 3124 0 -2 -9 C ATOM 4395 CE1 HIS C 87 13.029 23.189 52.372 1.00 25.22 C ANISOU 4395 CE1 HIS C 87 3186 3179 3219 11 -2 14 C ATOM 4396 NE2 HIS C 87 13.807 24.112 51.838 1.00 24.99 N ANISOU 4396 NE2 HIS C 87 3180 3139 3177 13 5 -11 N ATOM 4397 N GLN C 88 10.572 27.291 57.023 1.00 23.45 N ANISOU 4397 N GLN C 88 3002 2963 2943 4 7 -3 N ATOM 4398 CA GLN C 88 10.316 27.842 58.352 1.00 23.76 C ANISOU 4398 CA GLN C 88 3062 3020 2946 -51 12 -3 C ATOM 4399 C GLN C 88 9.759 26.761 59.274 1.00 23.29 C ANISOU 4399 C GLN C 88 2972 2964 2913 -11 -3 -13 C ATOM 4400 O GLN C 88 8.869 26.005 58.888 1.00 23.25 O ANISOU 4400 O GLN C 88 2953 3001 2881 1 -15 -20 O ATOM 4401 CB GLN C 88 9.360 29.033 58.316 1.00 26.25 C ANISOU 4401 CB GLN C 88 3304 3228 3440 62 -23 33 C ATOM 4402 CG GLN C 88 9.032 29.557 59.709 1.00 29.13 C ANISOU 4402 CG GLN C 88 3728 3758 3581 -11 22 -30 C ATOM 4403 CD GLN C 88 8.460 30.953 59.716 1.00 31.24 C ANISOU 4403 CD GLN C 88 3972 3868 4030 14 -21 -12 C ATOM 4404 OE1 GLN C 88 8.590 31.699 58.747 1.00 31.72 O ANISOU 4404 OE1 GLN C 88 4049 4006 3997 0 -3 -7 O ATOM 4405 NE2 GLN C 88 7.821 31.324 60.823 1.00 32.40 N ANISOU 4405 NE2 GLN C 88 4110 4117 4082 -19 20 -19 N ATOM 4406 N VAL C 89 10.291 26.694 60.489 1.00 22.86 N ANISOU 4406 N VAL C 89 2928 2860 2899 -13 -5 -23 N ATOM 4407 CA VAL C 89 9.743 25.814 61.514 1.00 22.90 C ANISOU 4407 CA VAL C 89 2930 2881 2889 11 -29 9 C ATOM 4408 C VAL C 89 8.927 26.633 62.511 1.00 23.53 C ANISOU 4408 C VAL C 89 3014 2968 2958 15 5 -20 C ATOM 4409 O VAL C 89 9.413 27.643 63.024 1.00 23.84 O ANISOU 4409 O VAL C 89 3047 3034 2978 -42 2 -31 O ATOM 4410 CB VAL C 89 10.841 25.034 62.251 1.00 21.68 C ANISOU 4410 CB VAL C 89 2784 2735 2720 -36 50 -7 C ATOM 4411 CG1 VAL C 89 10.289 24.265 63.443 1.00 20.27 C ANISOU 4411 CG1 VAL C 89 2582 2549 2569 29 -19 -54 C ATOM 4412 CG2 VAL C 89 11.543 24.071 61.300 1.00 22.12 C ANISOU 4412 CG2 VAL C 89 2824 2801 2777 32 25 -29 C ATOM 4413 N PHE C 90 7.696 26.205 62.757 1.00 24.16 N ANISOU 4413 N PHE C 90 3043 3074 3061 -26 -26 -6 N ATOM 4414 CA PHE C 90 6.865 26.839 63.777 1.00 25.26 C ANISOU 4414 CA PHE C 90 3153 3214 3230 6 29 -51 C ATOM 4415 C PHE C 90 7.105 26.143 65.114 1.00 26.76 C ANISOU 4415 C PHE C 90 3414 3373 3381 22 38 50 C ATOM 4416 O PHE C 90 6.663 25.018 65.339 1.00 25.94 O ANISOU 4416 O PHE C 90 3343 3320 3193 11 -5 -18 O ATOM 4417 CB PHE C 90 5.386 26.801 63.397 1.00 24.43 C ANISOU 4417 CB PHE C 90 3123 3115 3045 11 21 8 C ATOM 4418 CG PHE C 90 5.098 27.477 62.085 1.00 24.13 C ANISOU 4418 CG PHE C 90 3079 3032 3056 16 -6 0 C ATOM 4419 CD1 PHE C 90 4.886 28.844 62.025 1.00 23.90 C ANISOU 4419 CD1 PHE C 90 3029 3015 3038 4 2 -14 C ATOM 4420 CD2 PHE C 90 5.047 26.743 60.913 1.00 24.15 C ANISOU 4420 CD2 PHE C 90 3114 2971 3090 11 -11 -6 C ATOM 4421 CE1 PHE C 90 4.623 29.466 60.821 1.00 24.48 C ANISOU 4421 CE1 PHE C 90 3148 3069 3084 8 10 19 C ATOM 4422 CE2 PHE C 90 4.789 27.360 59.704 1.00 24.45 C ANISOU 4422 CE2 PHE C 90 3140 3093 3057 6 -20 -25 C ATOM 4423 CZ PHE C 90 4.574 28.723 59.658 1.00 25.00 C ANISOU 4423 CZ PHE C 90 3229 3120 3152 -10 -10 -17 C ATOM 4424 N LYS C 91 7.851 26.821 65.982 1.00 28.96 N ANISOU 4424 N LYS C 91 3680 3621 3702 -53 -26 -90 N ATOM 4425 CA LYS C 91 8.252 26.233 67.252 1.00 31.58 C ANISOU 4425 CA LYS C 91 4105 3966 3928 34 -58 46 C ATOM 4426 C LYS C 91 7.203 26.479 68.331 1.00 33.13 C ANISOU 4426 C LYS C 91 4202 4221 4165 31 14 -42 C ATOM 4427 O LYS C 91 6.612 27.554 68.422 1.00 33.02 O ANISOU 4427 O LYS C 91 4212 4187 4147 6 4 -31 O ATOM 4428 CB LYS C 91 9.606 26.785 67.704 1.00 34.00 C ANISOU 4428 CB LYS C 91 4272 4288 4357 -72 -108 5 C ATOM 4429 CG LYS C 91 10.766 26.352 66.822 1.00 36.87 C ANISOU 4429 CG LYS C 91 4689 4687 4634 60 95 -8 C ATOM 4430 CD LYS C 91 12.075 26.970 67.289 1.00 39.14 C ANISOU 4430 CD LYS C 91 4937 4953 4980 -56 -59 6 C ATOM 4431 CE LYS C 91 13.244 26.469 66.454 1.00 40.56 C ANISOU 4431 CE LYS C 91 5145 5132 5135 35 31 -13 C ATOM 4432 NZ LYS C 91 14.521 27.138 66.828 1.00 41.17 N ANISOU 4432 NZ LYS C 91 5225 5189 5230 -11 -7 -9 N ATOM 4433 N TRP C 92 6.968 25.446 69.134 1.00 34.92 N ANISOU 4433 N TRP C 92 4471 4356 4439 -23 -35 56 N ATOM 4434 CA TRP C 92 6.129 25.608 70.321 1.00 36.96 C ANISOU 4434 CA TRP C 92 4692 4705 4647 21 71 23 C ATOM 4435 C TRP C 92 6.944 26.292 71.415 1.00 38.54 C ANISOU 4435 C TRP C 92 4882 4919 4843 -38 -34 7 C ATOM 4436 O TRP C 92 8.082 25.904 71.678 1.00 38.31 O ANISOU 4436 O TRP C 92 4878 4871 4806 -13 -9 -8 O ATOM 4437 CB TRP C 92 5.606 24.255 70.771 1.00 37.91 C ANISOU 4437 CB TRP C 92 4821 4724 4857 -14 -15 14 C ATOM 4438 CG TRP C 92 4.868 24.227 72.072 1.00 38.98 C ANISOU 4438 CG TRP C 92 4940 4942 4928 -14 24 -6 C ATOM 4439 CD1 TRP C 92 3.731 24.907 72.399 1.00 39.05 C ANISOU 4439 CD1 TRP C 92 4956 4911 4970 6 0 4 C ATOM 4440 CD2 TRP C 92 5.211 23.446 73.225 1.00 39.39 C ANISOU 4440 CD2 TRP C 92 5023 4956 4987 -12 -14 13 C ATOM 4441 NE1 TRP C 92 3.351 24.609 73.684 1.00 39.44 N ANISOU 4441 NE1 TRP C 92 5017 4988 4982 -7 3 -9 N ATOM 4442 CE2 TRP C 92 4.244 23.711 74.213 1.00 39.75 C ANISOU 4442 CE2 TRP C 92 5038 5015 5051 7 4 1 C ATOM 4443 CE3 TRP C 92 6.246 22.551 73.516 1.00 39.76 C ANISOU 4443 CE3 TRP C 92 5037 5007 5064 8 -6 -6 C ATOM 4444 CZ2 TRP C 92 4.281 23.115 75.472 1.00 40.01 C ANISOU 4444 CZ2 TRP C 92 5090 5055 5059 -3 -4 2 C ATOM 4445 CZ3 TRP C 92 6.281 21.961 74.764 1.00 40.09 C ANISOU 4445 CZ3 TRP C 92 5090 5054 5090 4 -6 11 C ATOM 4446 CH2 TRP C 92 5.304 22.246 75.728 1.00 40.20 C ANISOU 4446 CH2 TRP C 92 5112 5068 5096 5 -3 -4 C ATOM 4447 N ASP C 93 6.373 27.332 72.013 1.00 40.19 N ANISOU 4447 N ASP C 93 5093 5066 5111 40 51 -8 N ATOM 4448 CA ASP C 93 7.002 27.972 73.164 1.00 41.87 C ANISOU 4448 CA ASP C 93 5291 5354 5262 -43 -28 -33 C ATOM 4449 C ASP C 93 6.839 27.130 74.424 1.00 42.22 C ANISOU 4449 C ASP C 93 5356 5359 5326 -10 0 -5 C ATOM 4450 O ASP C 93 6.652 25.919 74.407 1.00 42.47 O ANISOU 4450 O ASP C 93 5388 5363 5386 -4 4 -5 O ATOM 4451 CB ASP C 93 6.440 29.374 73.392 1.00 44.76 C ANISOU 4451 CB ASP C 93 5819 5493 5693 42 11 -23 C ATOM 4452 CG ASP C 93 4.929 29.448 73.350 1.00 47.78 C ANISOU 4452 CG ASP C 93 5990 6097 6069 6 -3 -22 C ATOM 4453 OD1 ASP C 93 4.252 28.433 73.621 1.00 48.41 O ANISOU 4453 OD1 ASP C 93 6168 6082 6142 -5 14 -8 O ATOM 4454 OD2 ASP C 93 4.399 30.538 73.038 1.00 48.63 O ANISOU 4454 OD2 ASP C 93 6192 6108 6176 8 4 -1 O ATOM 4455 N ARG C 97 -1.885 24.774 76.167 1.00 43.90 N ANISOU 4455 N ARG C 97 5586 5521 5575 -18 6 9 N ATOM 4456 CA ARG C 97 -2.685 24.137 75.130 1.00 43.82 C ANISOU 4456 CA ARG C 97 5561 5499 5590 -25 -15 27 C ATOM 4457 C ARG C 97 -3.409 22.915 75.678 1.00 43.09 C ANISOU 4457 C ARG C 97 5449 5448 5476 1 -16 -3 C ATOM 4458 O ARG C 97 -2.831 22.092 76.385 1.00 42.94 O ANISOU 4458 O ARG C 97 5433 5434 5447 -11 0 1 O ATOM 4459 CB ARG C 97 -1.808 23.751 73.936 1.00 45.23 C ANISOU 4459 CB ARG C 97 5744 5759 5682 43 16 -35 C ATOM 4460 CG ARG C 97 -0.900 24.869 73.448 1.00 46.82 C ANISOU 4460 CG ARG C 97 5936 5920 5933 -60 17 2 C ATOM 4461 CD ARG C 97 -1.686 26.114 73.070 1.00 48.17 C ANISOU 4461 CD ARG C 97 6123 6063 6117 44 -14 10 C ATOM 4462 NE ARG C 97 -0.815 27.268 72.888 1.00 48.81 N ANISOU 4462 NE ARG C 97 6198 6164 6184 -29 -3 -9 N ATOM 4463 CZ ARG C 97 -1.223 28.519 72.729 1.00 49.30 C ANISOU 4463 CZ ARG C 97 6287 6204 6241 10 -7 -1 C ATOM 4464 NH1 ARG C 97 -2.514 28.823 72.726 1.00 49.62 N ANISOU 4464 NH1 ARG C 97 6298 6263 6291 2 5 -11 N ATOM 4465 NH2 ARG C 97 -0.328 29.487 72.571 1.00 49.59 N ANISOU 4465 NH2 ARG C 97 6295 6263 6285 -11 0 1 N ATOM 4466 N ALA C 98 -4.681 22.779 75.308 1.00 42.27 N ANISOU 4466 N ALA C 98 5402 5302 5358 -14 12 11 N ATOM 4467 CA ALA C 98 -5.481 21.624 75.698 1.00 41.39 C ANISOU 4467 CA ALA C 98 5282 5227 5219 18 -2 -25 C ATOM 4468 C ALA C 98 -5.471 20.552 74.614 1.00 40.52 C ANISOU 4468 C ALA C 98 5136 5130 5131 2 16 27 C ATOM 4469 O ALA C 98 -6.192 19.558 74.679 1.00 40.37 O ANISOU 4469 O ALA C 98 5114 5116 5109 8 10 11 O ATOM 4470 CB ALA C 98 -6.907 22.058 76.005 1.00 41.57 C ANISOU 4470 CB ALA C 98 5272 5240 5283 4 -12 7 C ATOM 4471 N MET C 99 -4.668 20.768 73.577 1.00 39.65 N ANISOU 4471 N MET C 99 5049 4987 5031 16 -25 -11 N ATOM 4472 CA MET C 99 -4.358 19.745 72.593 1.00 38.88 C ANISOU 4472 CA MET C 99 4927 4917 4927 4 -20 38 C ATOM 4473 C MET C 99 -2.872 19.405 72.674 1.00 38.55 C ANISOU 4473 C MET C 99 4909 4843 4896 9 -2 9 C ATOM 4474 O MET C 99 -2.030 20.302 72.750 1.00 38.65 O ANISOU 4474 O MET C 99 4879 4876 4930 9 -4 9 O ATOM 4475 CB MET C 99 -4.705 20.211 71.181 1.00 37.30 C ANISOU 4475 CB MET C 99 4648 4687 4838 26 16 -12 C ATOM 4476 CG MET C 99 -6.132 20.690 70.991 1.00 35.32 C ANISOU 4476 CG MET C 99 4506 4399 4516 -80 19 26 C ATOM 4477 SD MET C 99 -7.361 19.391 71.195 1.00 32.51 S ANISOU 4477 SD MET C 99 4115 4226 4011 59 -64 8 S ATOM 4478 CE MET C 99 -7.020 18.387 69.750 1.00 32.24 C ANISOU 4478 CE MET C 99 4105 4045 4101 -2 16 0 C ATOM 4479 N LYS C 100 -2.554 18.115 72.634 1.00 38.00 N ANISOU 4479 N LYS C 100 4795 4818 4826 10 11 17 N ATOM 4480 CA LYS C 100 -1.167 17.672 72.510 1.00 37.12 C ANISOU 4480 CA LYS C 100 4734 4697 4672 -24 9 19 C ATOM 4481 C LYS C 100 -0.597 18.126 71.172 1.00 36.02 C ANISOU 4481 C LYS C 100 4574 4533 4577 2 -44 -8 C ATOM 4482 O LYS C 100 0.526 18.611 71.060 1.00 35.97 O ANISOU 4482 O LYS C 100 4573 4519 4577 14 2 9 O ATOM 4483 CB LYS C 100 -1.066 16.153 72.645 1.00 37.68 C ANISOU 4483 CB LYS C 100 4789 4720 4806 12 0 1 C ATOM 4484 N GLN C 101 -1.407 18.030 70.126 1.00 34.88 N ANISOU 4484 N GLN C 101 4470 4348 4436 -6 41 29 N ATOM 4485 CA GLN C 101 -1.195 18.647 68.837 1.00 33.51 C ANISOU 4485 CA GLN C 101 4257 4148 4327 -24 4 -37 C ATOM 4486 C GLN C 101 -0.464 19.978 68.848 1.00 31.97 C ANISOU 4486 C GLN C 101 4065 4026 4057 47 20 -41 C ATOM 4487 O GLN C 101 0.470 20.168 68.063 1.00 31.55 O ANISOU 4487 O GLN C 101 4036 3944 4008 20 -3 -41 O ATOM 4488 CB GLN C 101 -2.564 18.855 68.159 1.00 34.18 C ANISOU 4488 CB GLN C 101 4315 4317 4355 7 -15 -1 C ATOM 4489 N TRP C 102 -0.854 20.933 69.691 1.00 30.56 N ANISOU 4489 N TRP C 102 3849 3837 3926 -11 -14 31 N ATOM 4490 CA TRP C 102 -0.337 22.291 69.615 1.00 29.17 C ANISOU 4490 CA TRP C 102 3647 3721 3714 74 12 -22 C ATOM 4491 C TRP C 102 0.917 22.504 70.453 1.00 28.87 C ANISOU 4491 C TRP C 102 3661 3656 3654 17 17 -14 C ATOM 4492 O TRP C 102 1.387 23.636 70.592 1.00 28.75 O ANISOU 4492 O TRP C 102 3669 3654 3601 2 12 5 O ATOM 4493 CB TRP C 102 -1.423 23.298 69.995 1.00 26.33 C ANISOU 4493 CB TRP C 102 3286 3440 3280 -103 -105 4 C ATOM 4494 CG TRP C 102 -2.743 23.107 69.312 1.00 23.32 C ANISOU 4494 CG TRP C 102 3040 2921 2900 17 65 -47 C ATOM 4495 CD1 TRP C 102 -2.981 22.504 68.109 1.00 21.42 C ANISOU 4495 CD1 TRP C 102 2663 2707 2770 5 18 57 C ATOM 4496 CD2 TRP C 102 -4.021 23.555 69.783 1.00 22.51 C ANISOU 4496 CD2 TRP C 102 2901 2865 2787 -38 -55 -11 C ATOM 4497 NE1 TRP C 102 -4.317 22.525 67.817 1.00 19.84 N ANISOU 4497 NE1 TRP C 102 2590 2459 2490 -26 -21 20 N ATOM 4498 CE2 TRP C 102 -4.982 23.172 68.827 1.00 20.75 C ANISOU 4498 CE2 TRP C 102 2703 2597 2585 21 45 13 C ATOM 4499 CE3 TRP C 102 -4.449 24.236 70.929 1.00 22.70 C ANISOU 4499 CE3 TRP C 102 2916 2845 2867 24 -4 -4 C ATOM 4500 CZ2 TRP C 102 -6.340 23.443 68.979 1.00 21.73 C ANISOU 4500 CZ2 TRP C 102 2733 2740 2783 -6 -15 21 C ATOM 4501 CZ3 TRP C 102 -5.796 24.508 71.075 1.00 22.90 C ANISOU 4501 CZ3 TRP C 102 2914 2874 2913 -14 8 -13 C ATOM 4502 CH2 TRP C 102 -6.728 24.114 70.103 1.00 22.91 C ANISOU 4502 CH2 TRP C 102 2931 2913 2862 29 9 -10 C ATOM 4503 N GLU C 103 1.494 21.434 70.982 1.00 28.96 N ANISOU 4503 N GLU C 103 3669 3650 3684 12 19 -10 N ATOM 4504 CA GLU C 103 2.741 21.475 71.719 1.00 29.30 C ANISOU 4504 CA GLU C 103 3690 3693 3750 17 -1 -41 C ATOM 4505 C GLU C 103 3.891 20.803 70.973 1.00 28.91 C ANISOU 4505 C GLU C 103 3668 3674 3644 8 -2 -3 C ATOM 4506 O GLU C 103 4.834 20.317 71.604 1.00 29.13 O ANISOU 4506 O GLU C 103 3684 3716 3667 19 -7 2 O ATOM 4507 CB GLU C 103 2.570 20.800 73.086 1.00 31.69 C ANISOU 4507 CB GLU C 103 4113 3988 3938 -42 -32 93 C ATOM 4508 CG GLU C 103 1.542 21.452 73.989 1.00 34.23 C ANISOU 4508 CG GLU C 103 4282 4335 4389 39 46 -57 C ATOM 4509 CD GLU C 103 1.455 20.814 75.361 1.00 36.28 C ANISOU 4509 CD GLU C 103 4623 4623 4540 -17 -2 40 C ATOM 4510 OE1 GLU C 103 2.045 19.734 75.570 1.00 37.04 O ANISOU 4510 OE1 GLU C 103 4717 4654 4701 1 2 16 O ATOM 4511 OE2 GLU C 103 0.788 21.404 76.238 1.00 36.45 O ANISOU 4511 OE2 GLU C 103 4665 4607 4579 0 -11 4 O ATOM 4512 N ARG C 104 3.840 20.789 69.646 1.00 28.32 N ANISOU 4512 N ARG C 104 3562 3595 3601 25 35 16 N ATOM 4513 CA ARG C 104 4.934 20.206 68.867 1.00 27.54 C ANISOU 4513 CA ARG C 104 3484 3514 3465 -6 29 84 C ATOM 4514 C ARG C 104 5.521 21.239 67.914 1.00 26.00 C ANISOU 4514 C ARG C 104 3232 3355 3294 34 10 -8 C ATOM 4515 O ARG C 104 4.848 22.211 67.569 1.00 26.27 O ANISOU 4515 O ARG C 104 3304 3349 3329 33 -3 13 O ATOM 4516 CB ARG C 104 4.447 18.964 68.121 1.00 30.31 C ANISOU 4516 CB ARG C 104 3939 3701 3875 -59 20 -65 C ATOM 4517 CG ARG C 104 3.253 19.212 67.222 1.00 32.74 C ANISOU 4517 CG ARG C 104 4119 4197 4123 46 -34 22 C ATOM 4518 CD ARG C 104 2.535 17.929 66.814 1.00 34.51 C ANISOU 4518 CD ARG C 104 4411 4306 4394 -41 9 -6 C ATOM 4519 NE ARG C 104 1.164 18.228 66.430 1.00 35.25 N ANISOU 4519 NE ARG C 104 4470 4473 4450 10 -12 9 N ATOM 4520 CZ ARG C 104 0.241 17.465 65.877 1.00 35.55 C ANISOU 4520 CZ ARG C 104 4501 4475 4532 -7 -14 6 C ATOM 4521 NH1 ARG C 104 0.479 16.199 65.562 1.00 35.46 N ANISOU 4521 NH1 ARG C 104 4512 4468 4493 -10 9 9 N ATOM 4522 NH2 ARG C 104 -0.958 17.987 65.626 1.00 35.03 N ANISOU 4522 NH2 ARG C 104 4455 4424 4430 -27 -2 -2 N ATOM 4523 N ASP C 105 6.778 21.053 67.519 1.00 24.02 N ANISOU 4523 N ASP C 105 3128 3062 2936 -39 -22 48 N ATOM 4524 CA ASP C 105 7.361 21.878 66.465 1.00 22.04 C ANISOU 4524 CA ASP C 105 2860 2806 2710 5 -80 -63 C ATOM 4525 C ASP C 105 6.837 21.367 65.123 1.00 20.16 C ANISOU 4525 C ASP C 105 2607 2523 2530 20 -4 45 C ATOM 4526 O ASP C 105 6.739 20.155 64.938 1.00 19.19 O ANISOU 4526 O ASP C 105 2491 2503 2297 12 -36 23 O ATOM 4527 CB ASP C 105 8.883 21.825 66.463 1.00 23.61 C ANISOU 4527 CB ASP C 105 2927 3022 3021 19 16 -1 C ATOM 4528 CG ASP C 105 9.532 22.441 67.686 1.00 25.06 C ANISOU 4528 CG ASP C 105 3189 3203 3128 -16 -42 -44 C ATOM 4529 OD1 ASP C 105 8.809 22.963 68.558 1.00 25.14 O ANISOU 4529 OD1 ASP C 105 3198 3207 3148 25 -37 -19 O ATOM 4530 OD2 ASP C 105 10.780 22.398 67.761 1.00 25.29 O ANISOU 4530 OD2 ASP C 105 3206 3274 3128 -7 -41 -79 O ATOM 4531 N LEU C 106 6.501 22.282 64.224 1.00 18.98 N ANISOU 4531 N LEU C 106 2420 2466 2326 -11 -25 -39 N ATOM 4532 CA LEU C 106 5.924 21.894 62.943 1.00 17.67 C ANISOU 4532 CA LEU C 106 2225 2269 2220 -17 42 9 C ATOM 4533 C LEU C 106 6.596 22.622 61.782 1.00 16.76 C ANISOU 4533 C LEU C 106 2157 2125 2088 4 -13 -40 C ATOM 4534 O LEU C 106 6.927 23.799 61.870 1.00 16.55 O ANISOU 4534 O LEU C 106 2111 2145 2034 -23 -38 -72 O ATOM 4535 CB LEU C 106 4.428 22.205 62.911 1.00 17.11 C ANISOU 4535 CB LEU C 106 2199 2200 2102 -20 -26 1 C ATOM 4536 CG LEU C 106 3.485 21.412 63.811 1.00 16.70 C ANISOU 4536 CG LEU C 106 2140 2162 2045 11 -19 -26 C ATOM 4537 CD1 LEU C 106 2.092 22.024 63.776 1.00 17.36 C ANISOU 4537 CD1 LEU C 106 2170 2278 2149 37 -13 0 C ATOM 4538 CD2 LEU C 106 3.444 19.940 63.429 1.00 17.35 C ANISOU 4538 CD2 LEU C 106 2211 2181 2199 -10 -14 -4 C ATOM 4539 N THR C 107 6.764 21.911 60.667 1.00 16.02 N ANISOU 4539 N THR C 107 2032 2047 2006 9 7 15 N ATOM 4540 CA THR C 107 7.108 22.590 59.414 1.00 15.70 C ANISOU 4540 CA THR C 107 2006 1989 1972 16 1 -13 C ATOM 4541 C THR C 107 5.860 23.251 58.841 1.00 15.33 C ANISOU 4541 C THR C 107 1985 1916 1923 -8 6 -24 C ATOM 4542 O THR C 107 4.766 23.073 59.377 1.00 15.22 O ANISOU 4542 O THR C 107 1957 1924 1901 -22 -26 -44 O ATOM 4543 CB THR C 107 7.674 21.598 58.385 1.00 15.22 C ANISOU 4543 CB THR C 107 1936 1851 1996 6 -4 19 C ATOM 4544 OG1 THR C 107 6.625 20.713 57.971 1.00 14.73 O ANISOU 4544 OG1 THR C 107 1872 1905 1820 56 -59 -14 O ATOM 4545 CG2 THR C 107 8.819 20.795 58.979 1.00 14.93 C ANISOU 4545 CG2 THR C 107 1934 1876 1861 6 -37 -29 C ATOM 4546 N LEU C 108 6.013 23.988 57.740 1.00 15.27 N ANISOU 4546 N LEU C 108 1993 1908 1901 6 -28 -39 N ATOM 4547 CA LEU C 108 4.849 24.605 57.107 1.00 15.22 C ANISOU 4547 CA LEU C 108 1948 1918 1914 -2 -11 -38 C ATOM 4548 C LEU C 108 3.897 23.524 56.614 1.00 14.81 C ANISOU 4548 C LEU C 108 1896 1882 1850 29 -15 -25 C ATOM 4549 O LEU C 108 2.698 23.552 56.894 1.00 14.51 O ANISOU 4549 O LEU C 108 1898 1797 1818 -22 7 -32 O ATOM 4550 CB LEU C 108 5.276 25.539 55.979 1.00 16.87 C ANISOU 4550 CB LEU C 108 2249 2047 2116 -54 79 39 C ATOM 4551 CG LEU C 108 4.161 26.151 55.128 1.00 19.10 C ANISOU 4551 CG LEU C 108 2411 2422 2423 29 -45 25 C ATOM 4552 CD1 LEU C 108 3.179 26.950 55.971 1.00 19.62 C ANISOU 4552 CD1 LEU C 108 2527 2452 2474 13 15 -16 C ATOM 4553 CD2 LEU C 108 4.767 27.025 54.037 1.00 19.73 C ANISOU 4553 CD2 LEU C 108 2512 2475 2509 17 33 32 C ATOM 4554 N ARG C 109 4.436 22.522 55.915 1.00 14.57 N ANISOU 4554 N ARG C 109 1862 1886 1788 21 -33 -10 N ATOM 4555 CA ARG C 109 3.628 21.378 55.520 1.00 14.50 C ANISOU 4555 CA ARG C 109 1873 1826 1808 18 -34 37 C ATOM 4556 C ARG C 109 2.973 20.685 56.706 1.00 14.17 C ANISOU 4556 C ARG C 109 1807 1791 1785 16 -22 -17 C ATOM 4557 O ARG C 109 1.779 20.373 56.674 1.00 14.03 O ANISOU 4557 O ARG C 109 1784 1831 1718 39 -60 -19 O ATOM 4558 CB ARG C 109 4.479 20.389 54.712 1.00 15.89 C ANISOU 4558 CB ARG C 109 2065 2042 1930 66 35 -52 C ATOM 4559 CG ARG C 109 3.691 19.158 54.306 1.00 17.35 C ANISOU 4559 CG ARG C 109 2180 2174 2238 -23 -5 -19 C ATOM 4560 CD ARG C 109 4.580 18.108 53.638 1.00 17.15 C ANISOU 4560 CD ARG C 109 2156 2162 2197 1 -12 2 C ATOM 4561 NE ARG C 109 3.863 16.838 53.684 1.00 16.97 N ANISOU 4561 NE ARG C 109 2103 2152 2194 16 1 -59 N ATOM 4562 CZ ARG C 109 2.958 16.426 52.808 1.00 16.64 C ANISOU 4562 CZ ARG C 109 2136 2047 2140 -8 -18 -25 C ATOM 4563 NH1 ARG C 109 2.654 17.155 51.742 1.00 17.81 N ANISOU 4563 NH1 ARG C 109 2295 2251 2221 -11 -4 55 N ATOM 4564 NH2 ARG C 109 2.378 15.252 53.018 1.00 15.78 N ANISOU 4564 NH2 ARG C 109 2037 2003 1957 34 -21 6 N ATOM 4565 N GLY C 110 3.729 20.439 57.777 1.00 13.96 N ANISOU 4565 N GLY C 110 1826 1743 1733 29 0 -8 N ATOM 4566 CA GLY C 110 3.159 19.828 58.973 1.00 13.99 C ANISOU 4566 CA GLY C 110 1822 1715 1780 15 9 3 C ATOM 4567 C GLY C 110 2.024 20.670 59.543 1.00 13.79 C ANISOU 4567 C GLY C 110 1757 1741 1740 11 -17 23 C ATOM 4568 O GLY C 110 0.953 20.145 59.850 1.00 13.79 O ANISOU 4568 O GLY C 110 1760 1727 1754 -6 -55 16 O ATOM 4569 N ALA C 111 2.234 21.982 59.660 1.00 13.72 N ANISOU 4569 N ALA C 111 1772 1760 1680 14 -73 -25 N ATOM 4570 CA ALA C 111 1.209 22.876 60.181 1.00 14.03 C ANISOU 4570 CA ALA C 111 1811 1790 1729 17 -15 -23 C ATOM 4571 C ALA C 111 -0.043 22.893 59.315 1.00 14.28 C ANISOU 4571 C ALA C 111 1805 1837 1786 13 -7 0 C ATOM 4572 O ALA C 111 -1.155 22.933 59.838 1.00 14.16 O ANISOU 4572 O ALA C 111 1788 1839 1752 62 -18 -6 O ATOM 4573 CB ALA C 111 1.759 24.289 60.336 1.00 15.18 C ANISOU 4573 CB ALA C 111 1999 1842 1925 -27 17 -33 C ATOM 4574 N ILE C 112 0.110 22.839 57.995 1.00 14.70 N ANISOU 4574 N ILE C 112 1911 1876 1799 1 -10 3 N ATOM 4575 CA ILE C 112 -1.044 22.748 57.101 1.00 15.06 C ANISOU 4575 CA ILE C 112 1917 1925 1878 4 -23 9 C ATOM 4576 C ILE C 112 -1.792 21.438 57.269 1.00 15.13 C ANISOU 4576 C ILE C 112 1941 1935 1875 -5 -22 -3 C ATOM 4577 O ILE C 112 -3.029 21.427 57.238 1.00 14.99 O ANISOU 4577 O ILE C 112 1940 1896 1861 4 -33 15 O ATOM 4578 CB ILE C 112 -0.592 22.987 55.647 1.00 15.42 C ANISOU 4578 CB ILE C 112 2000 1966 1893 7 7 -29 C ATOM 4579 CG1 ILE C 112 -0.155 24.451 55.510 1.00 16.25 C ANISOU 4579 CG1 ILE C 112 2077 2033 2064 -4 3 38 C ATOM 4580 CG2 ILE C 112 -1.684 22.652 54.645 1.00 15.96 C ANISOU 4580 CG2 ILE C 112 2062 2062 1940 13 -40 5 C ATOM 4581 CD1 ILE C 112 0.606 24.769 54.244 1.00 16.42 C ANISOU 4581 CD1 ILE C 112 2090 2088 2063 -7 28 -9 C ATOM 4582 N GLN C 113 -1.093 20.331 57.516 1.00 15.61 N ANISOU 4582 N GLN C 113 2044 1952 1936 13 -40 -6 N ATOM 4583 CA GLN C 113 -1.736 19.025 57.489 1.00 15.93 C ANISOU 4583 CA GLN C 113 2061 1994 1997 -22 -51 11 C ATOM 4584 C GLN C 113 -2.214 18.530 58.839 1.00 16.34 C ANISOU 4584 C GLN C 113 2123 2056 2030 -20 -12 0 C ATOM 4585 O GLN C 113 -3.019 17.593 58.876 1.00 16.61 O ANISOU 4585 O GLN C 113 2189 2098 2025 -56 -5 -20 O ATOM 4586 CB GLN C 113 -0.802 18.007 56.821 1.00 17.16 C ANISOU 4586 CB GLN C 113 2192 2122 2207 27 5 -47 C ATOM 4587 CG GLN C 113 -0.550 18.368 55.361 1.00 19.41 C ANISOU 4587 CG GLN C 113 2584 2451 2339 -29 36 -12 C ATOM 4588 CD GLN C 113 -0.657 17.196 54.413 1.00 18.69 C ANISOU 4588 CD GLN C 113 2419 2255 2426 -66 12 56 C ATOM 4589 OE1 GLN C 113 -0.411 17.348 53.210 1.00 20.43 O ANISOU 4589 OE1 GLN C 113 2651 2638 2472 8 16 34 O ATOM 4590 NE2 GLN C 113 -1.035 16.032 54.923 1.00 14.89 N ANISOU 4590 NE2 GLN C 113 1934 2016 1707 80 -73 -47 N ATOM 4591 N VAL C 114 -1.751 19.123 59.940 1.00 16.27 N ANISOU 4591 N VAL C 114 2128 2025 2027 19 -26 -13 N ATOM 4592 CA VAL C 114 -2.240 18.728 61.254 1.00 16.57 C ANISOU 4592 CA VAL C 114 2137 2067 2091 4 29 -4 C ATOM 4593 C VAL C 114 -2.983 19.872 61.943 1.00 16.41 C ANISOU 4593 C VAL C 114 2132 2051 2050 -2 6 -3 C ATOM 4594 O VAL C 114 -3.021 20.997 61.448 1.00 16.75 O ANISOU 4594 O VAL C 114 2216 2083 2066 18 -1 27 O ATOM 4595 CB VAL C 114 -1.129 18.232 62.198 1.00 17.75 C ANISOU 4595 CB VAL C 114 2208 2267 2270 27 -38 18 C ATOM 4596 CG1 VAL C 114 -0.327 17.104 61.561 1.00 18.29 C ANISOU 4596 CG1 VAL C 114 2351 2309 2288 33 14 -10 C ATOM 4597 CG2 VAL C 114 -0.218 19.372 62.627 1.00 17.93 C ANISOU 4597 CG2 VAL C 114 2279 2274 2260 12 -22 -4 C ATOM 4598 N SER C 115 -3.568 19.569 63.095 1.00 16.17 N ANISOU 4598 N SER C 115 2086 2034 2025 11 -10 -6 N ATOM 4599 CA SER C 115 -4.209 20.595 63.915 1.00 16.25 C ANISOU 4599 CA SER C 115 2090 2010 2075 -3 -12 -23 C ATOM 4600 C SER C 115 -3.155 21.534 64.500 1.00 16.20 C ANISOU 4600 C SER C 115 2073 2033 2051 -1 -19 -9 C ATOM 4601 O SER C 115 -2.272 21.087 65.233 1.00 16.60 O ANISOU 4601 O SER C 115 2110 2107 2089 44 -40 -30 O ATOM 4602 CB SER C 115 -5.025 19.963 65.038 1.00 16.56 C ANISOU 4602 CB SER C 115 2122 2085 2087 -8 -27 9 C ATOM 4603 OG SER C 115 -5.583 20.968 65.868 1.00 17.29 O ANISOU 4603 OG SER C 115 2194 2233 2142 2 42 -37 O ATOM 4604 N ALA C 116 -3.259 22.818 64.180 1.00 15.70 N ANISOU 4604 N ALA C 116 1999 1998 1969 -12 -5 -33 N ATOM 4605 CA ALA C 116 -2.215 23.775 64.554 1.00 15.56 C ANISOU 4605 CA ALA C 116 2001 1955 1955 -7 -9 9 C ATOM 4606 C ALA C 116 -2.823 25.154 64.774 1.00 15.34 C ANISOU 4606 C ALA C 116 1996 1948 1885 -22 5 7 C ATOM 4607 O ALA C 116 -2.374 26.178 64.262 1.00 15.09 O ANISOU 4607 O ALA C 116 2060 1898 1776 10 -11 22 O ATOM 4608 CB ALA C 116 -1.138 23.800 63.476 1.00 15.87 C ANISOU 4608 CB ALA C 116 2063 2028 1941 11 -4 -12 C ATOM 4609 N VAL C 117 -3.864 25.193 65.605 1.00 15.02 N ANISOU 4609 N VAL C 117 1953 1940 1813 17 -27 48 N ATOM 4610 CA VAL C 117 -4.688 26.376 65.788 1.00 15.01 C ANISOU 4610 CA VAL C 117 1963 1911 1827 -11 6 0 C ATOM 4611 C VAL C 117 -3.902 27.617 66.157 1.00 15.15 C ANISOU 4611 C VAL C 117 1980 1900 1877 8 -16 -22 C ATOM 4612 O VAL C 117 -4.074 28.659 65.522 1.00 14.98 O ANISOU 4612 O VAL C 117 1990 1891 1811 15 -19 -35 O ATOM 4613 CB VAL C 117 -5.853 26.110 66.758 1.00 15.17 C ANISOU 4613 CB VAL C 117 1947 1923 1895 0 19 1 C ATOM 4614 CG1 VAL C 117 -6.617 27.380 67.088 1.00 15.00 C ANISOU 4614 CG1 VAL C 117 1966 1902 1831 0 7 19 C ATOM 4615 CG2 VAL C 117 -6.805 25.096 66.122 1.00 15.94 C ANISOU 4615 CG2 VAL C 117 1987 2021 2047 -38 -1 -27 C ATOM 4616 N PRO C 118 -3.004 27.538 67.134 1.00 15.53 N ANISOU 4616 N PRO C 118 2007 1953 1940 12 -45 -23 N ATOM 4617 CA PRO C 118 -2.175 28.671 67.506 1.00 15.73 C ANISOU 4617 CA PRO C 118 2003 1989 1986 -22 -21 6 C ATOM 4618 C PRO C 118 -1.373 29.253 66.358 1.00 15.33 C ANISOU 4618 C PRO C 118 1953 1957 1914 21 -36 -9 C ATOM 4619 O PRO C 118 -1.274 30.475 66.237 1.00 15.70 O ANISOU 4619 O PRO C 118 2032 1988 1946 -37 -11 13 O ATOM 4620 CB PRO C 118 -1.280 28.108 68.604 1.00 15.90 C ANISOU 4620 CB PRO C 118 2029 1996 2018 -12 -46 -4 C ATOM 4621 CG PRO C 118 -2.094 27.038 69.243 1.00 16.16 C ANISOU 4621 CG PRO C 118 2070 2038 2031 -25 -32 6 C ATOM 4622 CD PRO C 118 -2.973 26.464 68.159 1.00 15.88 C ANISOU 4622 CD PRO C 118 2056 1993 1986 -7 -19 -1 C ATOM 4623 N VAL C 119 -0.796 28.417 65.499 1.00 15.11 N ANISOU 4623 N VAL C 119 1912 1979 1849 3 -42 0 N ATOM 4624 CA VAL C 119 -0.017 28.872 64.358 1.00 14.87 C ANISOU 4624 CA VAL C 119 1898 1910 1843 -13 -50 -1 C ATOM 4625 C VAL C 119 -0.834 29.757 63.424 1.00 14.65 C ANISOU 4625 C VAL C 119 1879 1838 1848 -20 -22 -6 C ATOM 4626 O VAL C 119 -0.395 30.841 63.038 1.00 14.11 O ANISOU 4626 O VAL C 119 1853 1779 1730 -12 -77 -36 O ATOM 4627 CB VAL C 119 0.531 27.670 63.562 1.00 15.99 C ANISOU 4627 CB VAL C 119 2055 2008 2012 12 27 -57 C ATOM 4628 CG1 VAL C 119 1.237 28.108 62.287 1.00 15.79 C ANISOU 4628 CG1 VAL C 119 1991 1978 2030 -12 5 -15 C ATOM 4629 CG2 VAL C 119 1.476 26.840 64.422 1.00 17.47 C ANISOU 4629 CG2 VAL C 119 2246 2218 2174 53 -22 41 C ATOM 4630 N PHE C 120 -2.017 29.279 63.034 1.00 14.58 N ANISOU 4630 N PHE C 120 1862 1826 1853 13 -40 -28 N ATOM 4631 CA PHE C 120 -2.795 29.979 62.013 1.00 14.57 C ANISOU 4631 CA PHE C 120 1886 1817 1833 15 -20 -4 C ATOM 4632 C PHE C 120 -3.512 31.194 62.565 1.00 14.47 C ANISOU 4632 C PHE C 120 1901 1809 1790 24 -20 6 C ATOM 4633 O PHE C 120 -3.669 32.193 61.852 1.00 14.08 O ANISOU 4633 O PHE C 120 1920 1734 1697 -8 -28 -48 O ATOM 4634 CB PHE C 120 -3.743 28.997 61.307 1.00 15.11 C ANISOU 4634 CB PHE C 120 1941 1930 1869 -32 -46 -21 C ATOM 4635 CG PHE C 120 -2.934 28.124 60.378 1.00 15.87 C ANISOU 4635 CG PHE C 120 2012 2036 1981 46 -3 -11 C ATOM 4636 CD1 PHE C 120 -2.340 26.963 60.839 1.00 16.14 C ANISOU 4636 CD1 PHE C 120 2095 2005 2033 16 -16 0 C ATOM 4637 CD2 PHE C 120 -2.749 28.498 59.056 1.00 15.99 C ANISOU 4637 CD2 PHE C 120 2039 2048 1987 12 33 -13 C ATOM 4638 CE1 PHE C 120 -1.583 26.178 59.993 1.00 16.34 C ANISOU 4638 CE1 PHE C 120 2094 2103 2012 16 -21 -19 C ATOM 4639 CE2 PHE C 120 -1.997 27.708 58.206 1.00 15.66 C ANISOU 4639 CE2 PHE C 120 1993 1958 2000 -21 4 -31 C ATOM 4640 CZ PHE C 120 -1.413 26.551 58.675 1.00 16.16 C ANISOU 4640 CZ PHE C 120 2095 2016 2028 1 -8 -2 C ATOM 4641 N GLN C 121 -3.902 31.158 63.837 1.00 14.44 N ANISOU 4641 N GLN C 121 1880 1813 1793 26 -16 11 N ATOM 4642 CA GLN C 121 -4.380 32.370 64.503 1.00 14.72 C ANISOU 4642 CA GLN C 121 1913 1844 1835 4 15 -21 C ATOM 4643 C GLN C 121 -3.310 33.453 64.504 1.00 14.67 C ANISOU 4643 C GLN C 121 1916 1843 1813 6 1 -33 C ATOM 4644 O GLN C 121 -3.568 34.600 64.132 1.00 14.60 O ANISOU 4644 O GLN C 121 1980 1826 1740 -3 -31 -57 O ATOM 4645 CB GLN C 121 -4.838 32.040 65.924 1.00 14.55 C ANISOU 4645 CB GLN C 121 1910 1788 1829 15 -4 15 C ATOM 4646 CG GLN C 121 -6.147 31.274 65.962 1.00 15.59 C ANISOU 4646 CG GLN C 121 1948 1920 2055 -2 -33 -52 C ATOM 4647 CD GLN C 121 -6.567 30.813 67.338 1.00 18.40 C ANISOU 4647 CD GLN C 121 2415 2347 2227 34 58 32 C ATOM 4648 OE1 GLN C 121 -7.730 30.474 67.561 1.00 19.88 O ANISOU 4648 OE1 GLN C 121 2519 2555 2481 -33 18 49 O ATOM 4649 NE2 GLN C 121 -5.631 30.778 68.278 1.00 19.89 N ANISOU 4649 NE2 GLN C 121 2566 2584 2409 0 -55 -22 N ATOM 4650 N GLN C 122 -2.082 33.091 64.863 1.00 14.97 N ANISOU 4650 N GLN C 122 1945 1902 1842 1 -24 -41 N ATOM 4651 CA GLN C 122 -0.970 34.032 64.863 1.00 15.41 C ANISOU 4651 CA GLN C 122 1992 1958 1905 -50 38 -49 C ATOM 4652 C GLN C 122 -0.613 34.519 63.467 1.00 15.18 C ANISOU 4652 C GLN C 122 1971 1902 1894 -10 2 -40 C ATOM 4653 O GLN C 122 -0.378 35.717 63.281 1.00 15.30 O ANISOU 4653 O GLN C 122 1985 1914 1915 -32 -33 -43 O ATOM 4654 CB GLN C 122 0.246 33.424 65.568 1.00 17.94 C ANISOU 4654 CB GLN C 122 2316 2275 2225 140 -67 32 C ATOM 4655 CG GLN C 122 1.422 34.379 65.699 1.00 21.70 C ANISOU 4655 CG GLN C 122 2631 2791 2822 -113 -38 76 C ATOM 4656 CD GLN C 122 1.103 35.609 66.524 1.00 25.42 C ANISOU 4656 CD GLN C 122 3323 3124 3210 35 -46 -91 C ATOM 4657 OE1 GLN C 122 0.247 35.580 67.408 1.00 27.66 O ANISOU 4657 OE1 GLN C 122 3471 3560 3478 -1 54 -34 O ATOM 4658 NE2 GLN C 122 1.785 36.715 66.248 1.00 26.08 N ANISOU 4658 NE2 GLN C 122 3352 3261 3297 -21 -21 6 N ATOM 4659 N ILE C 123 -0.622 33.646 62.454 1.00 14.81 N ANISOU 4659 N ILE C 123 1914 1880 1835 14 -33 -22 N ATOM 4660 CA ILE C 123 -0.378 34.105 61.085 1.00 14.41 C ANISOU 4660 CA ILE C 123 1869 1780 1826 3 -26 -29 C ATOM 4661 C ILE C 123 -1.391 35.183 60.706 1.00 14.14 C ANISOU 4661 C ILE C 123 1834 1783 1754 -14 -39 -29 C ATOM 4662 O ILE C 123 -1.035 36.248 60.195 1.00 14.10 O ANISOU 4662 O ILE C 123 1854 1792 1713 -52 -53 -48 O ATOM 4663 CB ILE C 123 -0.440 32.959 60.059 1.00 14.65 C ANISOU 4663 CB ILE C 123 1971 1784 1812 39 -45 -24 C ATOM 4664 CG1 ILE C 123 0.740 31.998 60.233 1.00 14.65 C ANISOU 4664 CG1 ILE C 123 1835 1863 1866 -11 -17 -41 C ATOM 4665 CG2 ILE C 123 -0.461 33.497 58.632 1.00 14.40 C ANISOU 4665 CG2 ILE C 123 1872 1806 1793 -21 -2 -39 C ATOM 4666 CD1 ILE C 123 0.555 30.675 59.514 1.00 15.28 C ANISOU 4666 CD1 ILE C 123 1975 1835 1996 8 -27 -26 C ATOM 4667 N ALA C 124 -2.671 34.905 60.939 1.00 14.53 N ANISOU 4667 N ALA C 124 1863 1853 1804 -12 -2 -48 N ATOM 4668 CA ALA C 124 -3.730 35.853 60.617 1.00 14.99 C ANISOU 4668 CA ALA C 124 1929 1850 1919 8 -6 -14 C ATOM 4669 C ALA C 124 -3.550 37.179 61.353 1.00 15.17 C ANISOU 4669 C ALA C 124 1963 1871 1931 -11 11 -28 C ATOM 4670 O ALA C 124 -3.701 38.231 60.730 1.00 15.15 O ANISOU 4670 O ALA C 124 2005 1844 1910 30 -27 -69 O ATOM 4671 CB ALA C 124 -5.104 35.276 60.923 1.00 15.72 C ANISOU 4671 CB ALA C 124 1949 2024 2000 -20 -15 -8 C ATOM 4672 N ARG C 125 -3.232 37.145 62.640 1.00 15.64 N ANISOU 4672 N ARG C 125 2001 1957 1986 -20 -38 8 N ATOM 4673 CA ARG C 125 -2.991 38.376 63.388 1.00 16.32 C ANISOU 4673 CA ARG C 125 2126 1990 2084 -2 -5 -31 C ATOM 4674 C ARG C 125 -1.850 39.189 62.786 1.00 16.45 C ANISOU 4674 C ARG C 125 2103 2054 2092 0 -7 -30 C ATOM 4675 O ARG C 125 -1.983 40.403 62.589 1.00 16.74 O ANISOU 4675 O ARG C 125 2186 2063 2111 1 -12 -5 O ATOM 4676 CB AARG C 125 -2.702 38.071 64.859 0.50 16.57 C ANISOU 4676 CB AARG C 125 2125 2049 2121 -13 -3 -11 C ATOM 4677 CB BARG C 125 -2.683 38.088 64.858 0.50 17.66 C ANISOU 4677 CB BARG C 125 2325 2226 2160 22 -53 -11 C ATOM 4678 CG AARG C 125 -3.914 37.620 65.658 0.50 16.60 C ANISOU 4678 CG AARG C 125 2117 2102 2088 6 -6 -14 C ATOM 4679 CG BARG C 125 -3.780 37.367 65.617 0.50 19.36 C ANISOU 4679 CG BARG C 125 2428 2452 2476 -26 33 9 C ATOM 4680 CD AARG C 125 -3.631 37.655 67.152 0.50 16.35 C ANISOU 4680 CD AARG C 125 2098 2046 2068 30 -8 14 C ATOM 4681 CD BARG C 125 -3.582 37.490 67.123 0.50 20.43 C ANISOU 4681 CD BARG C 125 2631 2595 2538 4 -6 -5 C ATOM 4682 NE AARG C 125 -2.651 36.669 67.577 0.50 15.38 N ANISOU 4682 NE AARG C 125 1986 1965 1893 -21 -11 -19 N ATOM 4683 NE BARG C 125 -4.308 36.455 67.846 0.50 20.56 N ANISOU 4683 NE BARG C 125 2622 2600 2590 -7 -7 -8 N ATOM 4684 CZ AARG C 125 -2.897 35.423 67.954 0.50 15.57 C ANISOU 4684 CZ AARG C 125 2003 1972 1941 -6 -3 -15 C ATOM 4685 CZ BARG C 125 -3.843 35.247 68.141 0.50 20.73 C ANISOU 4685 CZ BARG C 125 2651 2616 2609 5 -15 -11 C ATOM 4686 NH1AARG C 125 -4.132 34.942 67.985 0.50 15.82 N ANISOU 4686 NH1AARG C 125 2033 1992 1988 -26 -3 -8 N ATOM 4687 NH1BARG C 125 -2.618 34.881 67.792 0.50 20.71 N ANISOU 4687 NH1BARG C 125 2662 2600 2606 18 -15 1 N ATOM 4688 NH2AARG C 125 -1.891 34.638 68.320 0.50 15.98 N ANISOU 4688 NH2AARG C 125 2057 1992 2023 14 -25 -24 N ATOM 4689 NH2BARG C 125 -4.618 34.396 68.803 0.50 21.14 N ANISOU 4689 NH2BARG C 125 2714 2657 2663 -12 -3 13 N ATOM 4690 N GLU C 126 -0.726 38.542 62.482 1.00 16.01 N ANISOU 4690 N GLU C 126 2090 1997 1997 -5 -20 -39 N ATOM 4691 CA GLU C 126 0.412 39.240 61.898 1.00 16.47 C ANISOU 4691 CA GLU C 126 2117 2073 2068 -39 -22 -33 C ATOM 4692 C GLU C 126 0.115 39.808 60.520 1.00 16.42 C ANISOU 4692 C GLU C 126 2111 2061 2068 -33 -32 -34 C ATOM 4693 O GLU C 126 0.543 40.921 60.203 1.00 17.21 O ANISOU 4693 O GLU C 126 2236 2114 2190 -61 -2 -21 O ATOM 4694 CB GLU C 126 1.640 38.326 61.853 1.00 17.52 C ANISOU 4694 CB GLU C 126 2197 2138 2321 1 16 -48 C ATOM 4695 CG GLU C 126 2.059 37.851 63.235 1.00 19.83 C ANISOU 4695 CG GLU C 126 2636 2466 2432 -67 -13 15 C ATOM 4696 CD GLU C 126 3.404 37.167 63.282 1.00 22.98 C ANISOU 4696 CD GLU C 126 2818 2915 3001 26 1 -24 C ATOM 4697 OE1 GLU C 126 4.187 37.272 62.317 1.00 23.13 O ANISOU 4697 OE1 GLU C 126 2963 2945 2879 6 -27 -8 O ATOM 4698 OE2 GLU C 126 3.694 36.512 64.307 1.00 24.76 O ANISOU 4698 OE2 GLU C 126 3156 3103 3149 12 -32 66 O ATOM 4699 N VAL C 127 -0.615 39.071 59.685 1.00 15.56 N ANISOU 4699 N VAL C 127 2008 1910 1993 0 -4 -4 N ATOM 4700 CA VAL C 127 -1.103 39.607 58.422 1.00 15.14 C ANISOU 4700 CA VAL C 127 1939 1842 1971 -8 -25 -46 C ATOM 4701 C VAL C 127 -1.941 40.859 58.661 1.00 14.63 C ANISOU 4701 C VAL C 127 1891 1813 1854 -26 -35 -34 C ATOM 4702 O VAL C 127 -1.687 41.888 58.040 1.00 13.93 O ANISOU 4702 O VAL C 127 1801 1725 1765 -49 -79 -112 O ATOM 4703 CB VAL C 127 -1.918 38.556 57.646 1.00 14.78 C ANISOU 4703 CB VAL C 127 1850 1888 1876 -28 -24 -21 C ATOM 4704 CG1 VAL C 127 -2.585 39.151 56.418 1.00 14.85 C ANISOU 4704 CG1 VAL C 127 1916 1833 1893 3 5 4 C ATOM 4705 CG2 VAL C 127 -1.010 37.398 57.250 1.00 15.82 C ANISOU 4705 CG2 VAL C 127 2047 1928 2035 26 9 -6 C ATOM 4706 N GLY C 128 -2.935 40.760 59.534 1.00 15.07 N ANISOU 4706 N GLY C 128 1911 1887 1928 -28 -16 -33 N ATOM 4707 CA GLY C 128 -3.775 41.900 59.877 1.00 15.46 C ANISOU 4707 CA GLY C 128 1966 1925 1984 8 -7 -32 C ATOM 4708 C GLY C 128 -4.922 42.069 58.888 1.00 15.88 C ANISOU 4708 C GLY C 128 2020 2011 2004 -1 -24 -14 C ATOM 4709 O GLY C 128 -4.876 41.536 57.779 1.00 15.93 O ANISOU 4709 O GLY C 128 2040 1977 2035 -1 -19 -43 O ATOM 4710 N GLU C 129 -5.916 42.872 59.254 1.00 16.08 N ANISOU 4710 N GLU C 129 2067 2030 2014 15 -26 -50 N ATOM 4711 CA GLU C 129 -7.171 42.946 58.520 1.00 16.53 C ANISOU 4711 CA GLU C 129 2089 2115 2077 -8 -32 14 C ATOM 4712 C GLU C 129 -7.037 43.567 57.138 1.00 16.20 C ANISOU 4712 C GLU C 129 2071 2017 2067 -6 -26 0 C ATOM 4713 O GLU C 129 -7.703 43.123 56.198 1.00 16.12 O ANISOU 4713 O GLU C 129 2114 1978 2033 13 -38 13 O ATOM 4714 CB GLU C 129 -8.213 43.719 59.339 1.00 17.66 C ANISOU 4714 CB GLU C 129 2168 2279 2262 50 -6 -35 C ATOM 4715 N VAL C 130 -6.207 44.594 56.993 1.00 15.97 N ANISOU 4715 N VAL C 130 2082 2005 1983 -3 -1 -11 N ATOM 4716 CA VAL C 130 -6.097 45.289 55.711 1.00 15.55 C ANISOU 4716 CA VAL C 130 2008 1941 1960 26 20 -19 C ATOM 4717 C VAL C 130 -5.480 44.384 54.652 1.00 14.87 C ANISOU 4717 C VAL C 130 1924 1826 1901 -6 -9 12 C ATOM 4718 O VAL C 130 -6.064 44.195 53.583 1.00 15.11 O ANISOU 4718 O VAL C 130 2007 1827 1906 -55 -3 4 O ATOM 4719 CB VAL C 130 -5.301 46.596 55.846 1.00 16.62 C ANISOU 4719 CB VAL C 130 2124 2064 2127 -55 1 -1 C ATOM 4720 CG1 VAL C 130 -5.109 47.268 54.495 1.00 16.55 C ANISOU 4720 CG1 VAL C 130 2106 2061 2121 6 -9 9 C ATOM 4721 CG2 VAL C 130 -6.041 47.523 56.802 1.00 17.55 C ANISOU 4721 CG2 VAL C 130 2217 2201 2252 8 22 -45 C ATOM 4722 N ARG C 131 -4.329 43.794 54.963 1.00 14.66 N ANISOU 4722 N ARG C 131 1897 1786 1887 -12 19 -33 N ATOM 4723 CA ARG C 131 -3.685 42.884 54.018 1.00 14.47 C ANISOU 4723 CA ARG C 131 1835 1806 1857 9 -6 -31 C ATOM 4724 C ARG C 131 -4.538 41.646 53.777 1.00 14.55 C ANISOU 4724 C ARG C 131 1850 1834 1846 -28 -5 1 C ATOM 4725 O ARG C 131 -4.673 41.199 52.632 1.00 14.66 O ANISOU 4725 O ARG C 131 1925 1783 1860 -40 5 -8 O ATOM 4726 CB ARG C 131 -2.287 42.495 54.506 1.00 14.12 C ANISOU 4726 CB ARG C 131 1808 1792 1767 -34 -24 -9 C ATOM 4727 CG ARG C 131 -1.364 43.705 54.599 1.00 14.34 C ANISOU 4727 CG ARG C 131 1855 1706 1888 0 28 -11 C ATOM 4728 CD ARG C 131 0.090 43.322 54.793 1.00 15.54 C ANISOU 4728 CD ARG C 131 1921 1971 2011 10 -21 -29 C ATOM 4729 NE ARG C 131 0.351 42.737 56.098 1.00 15.93 N ANISOU 4729 NE ARG C 131 2062 1950 2042 43 -24 -41 N ATOM 4730 CZ ARG C 131 1.559 42.491 56.591 1.00 15.26 C ANISOU 4730 CZ ARG C 131 2000 1833 1965 7 -3 -55 C ATOM 4731 NH1 ARG C 131 2.647 42.773 55.885 1.00 16.17 N ANISOU 4731 NH1 ARG C 131 2092 1941 2111 -50 45 -70 N ATOM 4732 NH2 ARG C 131 1.673 41.958 57.799 1.00 15.58 N ANISOU 4732 NH2 ARG C 131 2025 1891 2003 -17 -45 -32 N ATOM 4733 N MET C 132 -5.134 41.091 54.827 1.00 14.53 N ANISOU 4733 N MET C 132 1840 1841 1839 -17 -28 10 N ATOM 4734 CA MET C 132 -6.000 39.923 54.673 1.00 14.31 C ANISOU 4734 CA MET C 132 1838 1788 1812 4 -8 -3 C ATOM 4735 C MET C 132 -7.148 40.216 53.716 1.00 14.45 C ANISOU 4735 C MET C 132 1877 1789 1826 5 -25 -1 C ATOM 4736 O MET C 132 -7.401 39.471 52.767 1.00 14.53 O ANISOU 4736 O MET C 132 1912 1787 1821 30 -18 -19 O ATOM 4737 CB MET C 132 -6.527 39.462 56.029 1.00 14.43 C ANISOU 4737 CB MET C 132 1872 1791 1820 -16 6 -3 C ATOM 4738 CG MET C 132 -7.304 38.154 56.000 1.00 14.08 C ANISOU 4738 CG MET C 132 1741 1721 1887 71 17 -31 C ATOM 4739 SD MET C 132 -6.240 36.743 55.649 1.00 12.57 S ANISOU 4739 SD MET C 132 1952 1443 1380 -25 6 -120 S ATOM 4740 CE MET C 132 -5.396 36.524 57.211 1.00 14.06 C ANISOU 4740 CE MET C 132 1760 1903 1679 6 -115 14 C ATOM 4741 N GLN C 133 -7.848 41.329 53.917 1.00 14.50 N ANISOU 4741 N GLN C 133 1871 1831 1807 28 5 -17 N ATOM 4742 CA GLN C 133 -8.922 41.747 53.036 1.00 14.65 C ANISOU 4742 CA GLN C 133 1888 1832 1845 47 -7 -14 C ATOM 4743 C GLN C 133 -8.460 41.910 51.588 1.00 14.83 C ANISOU 4743 C GLN C 133 1950 1829 1856 38 0 -10 C ATOM 4744 O GLN C 133 -9.150 41.451 50.669 1.00 14.76 O ANISOU 4744 O GLN C 133 1915 1842 1850 46 -16 25 O ATOM 4745 CB GLN C 133 -9.516 43.087 53.492 1.00 14.28 C ANISOU 4745 CB GLN C 133 1804 1846 1775 20 27 -59 C ATOM 4746 CG GLN C 133 -10.704 43.527 52.647 1.00 14.45 C ANISOU 4746 CG GLN C 133 1985 1829 1677 29 -39 -21 C ATOM 4747 CD GLN C 133 -11.935 42.677 52.886 1.00 16.61 C ANISOU 4747 CD GLN C 133 2080 2065 2166 -21 -11 33 C ATOM 4748 OE1 GLN C 133 -12.750 42.980 53.757 1.00 17.67 O ANISOU 4748 OE1 GLN C 133 2250 2229 2234 -66 68 4 O ATOM 4749 NE2 GLN C 133 -12.092 41.606 52.117 1.00 18.07 N ANISOU 4749 NE2 GLN C 133 2364 2187 2316 -44 -59 -36 N ATOM 4750 N LYS C 134 -7.317 42.559 51.395 1.00 15.32 N ANISOU 4750 N LYS C 134 2020 1841 1959 21 -24 -21 N ATOM 4751 CA LYS C 134 -6.803 42.791 50.051 1.00 16.51 C ANISOU 4751 CA LYS C 134 2238 2019 2017 89 32 -1 C ATOM 4752 C LYS C 134 -6.569 41.475 49.311 1.00 16.10 C ANISOU 4752 C LYS C 134 2139 1993 1986 40 -17 -5 C ATOM 4753 O LYS C 134 -7.044 41.322 48.185 1.00 15.90 O ANISOU 4753 O LYS C 134 2092 1967 1983 32 -21 27 O ATOM 4754 CB LYS C 134 -5.509 43.612 50.060 1.00 21.83 C ANISOU 4754 CB LYS C 134 2576 2646 3073 -120 -95 -63 C ATOM 4755 CG LYS C 134 -5.005 43.909 48.656 1.00 29.42 C ANISOU 4755 CG LYS C 134 3848 3862 3468 74 78 35 C ATOM 4756 CD LYS C 134 -3.974 45.024 48.613 1.00 34.59 C ANISOU 4756 CD LYS C 134 4309 4261 4573 -95 -9 -32 C ATOM 4757 CE LYS C 134 -3.759 45.482 47.176 1.00 38.42 C ANISOU 4757 CE LYS C 134 4927 4907 4765 33 17 17 C ATOM 4758 NZ LYS C 134 -2.850 46.656 47.087 1.00 39.90 N ANISOU 4758 NZ LYS C 134 5067 5021 5071 -16 11 12 N ATOM 4759 N TYR C 135 -5.866 40.539 49.947 1.00 15.54 N ANISOU 4759 N TYR C 135 2032 1939 1933 6 -4 -34 N ATOM 4760 CA TYR C 135 -5.593 39.260 49.295 1.00 15.25 C ANISOU 4760 CA TYR C 135 1987 1910 1897 -10 5 -14 C ATOM 4761 C TYR C 135 -6.856 38.458 49.038 1.00 14.55 C ANISOU 4761 C TYR C 135 1908 1822 1799 33 14 20 C ATOM 4762 O TYR C 135 -6.975 37.852 47.964 1.00 14.28 O ANISOU 4762 O TYR C 135 1881 1735 1809 -5 -13 20 O ATOM 4763 CB TYR C 135 -4.572 38.432 50.077 1.00 16.32 C ANISOU 4763 CB TYR C 135 2099 2054 2047 63 -37 0 C ATOM 4764 CG TYR C 135 -3.153 38.931 49.898 1.00 17.58 C ANISOU 4764 CG TYR C 135 2219 2188 2271 -1 -2 43 C ATOM 4765 CD1 TYR C 135 -2.415 38.600 48.769 1.00 18.38 C ANISOU 4765 CD1 TYR C 135 2355 2298 2331 38 10 6 C ATOM 4766 CD2 TYR C 135 -2.561 39.739 50.859 1.00 18.27 C ANISOU 4766 CD2 TYR C 135 2337 2266 2341 8 -31 -7 C ATOM 4767 CE1 TYR C 135 -1.120 39.061 48.613 1.00 19.27 C ANISOU 4767 CE1 TYR C 135 2434 2425 2463 -2 40 25 C ATOM 4768 CE2 TYR C 135 -1.270 40.205 50.709 1.00 18.94 C ANISOU 4768 CE2 TYR C 135 2395 2344 2458 2 -11 22 C ATOM 4769 CZ TYR C 135 -0.556 39.863 49.582 1.00 19.65 C ANISOU 4769 CZ TYR C 135 2514 2460 2493 22 7 -2 C ATOM 4770 OH TYR C 135 0.732 40.316 49.410 1.00 20.83 O ANISOU 4770 OH TYR C 135 2601 2604 2709 -18 34 -3 O ATOM 4771 N LEU C 136 -7.815 38.444 49.969 1.00 14.27 N ANISOU 4771 N LEU C 136 1813 1792 1819 21 -19 10 N ATOM 4772 CA LEU C 136 -9.045 37.695 49.709 1.00 14.38 C ANISOU 4772 CA LEU C 136 1840 1797 1826 2 -27 6 C ATOM 4773 C LEU C 136 -9.840 38.316 48.568 1.00 14.24 C ANISOU 4773 C LEU C 136 1829 1786 1794 -5 -4 12 C ATOM 4774 O LEU C 136 -10.434 37.575 47.787 1.00 14.25 O ANISOU 4774 O LEU C 136 1861 1737 1815 6 -29 26 O ATOM 4775 CB LEU C 136 -9.894 37.513 50.963 1.00 15.03 C ANISOU 4775 CB LEU C 136 1929 1871 1912 0 39 -4 C ATOM 4776 CG LEU C 136 -9.250 36.718 52.105 1.00 15.33 C ANISOU 4776 CG LEU C 136 2013 1909 1904 0 18 -4 C ATOM 4777 CD1 LEU C 136 -10.260 36.450 53.214 1.00 15.00 C ANISOU 4777 CD1 LEU C 136 1938 1820 1941 1 30 -37 C ATOM 4778 CD2 LEU C 136 -8.656 35.403 51.617 1.00 14.78 C ANISOU 4778 CD2 LEU C 136 1878 1891 1846 -3 10 4 C ATOM 4779 N LYS C 137 -9.844 39.638 48.431 1.00 14.58 N ANISOU 4779 N LYS C 137 1908 1805 1827 13 8 -15 N ATOM 4780 CA LYS C 137 -10.375 40.268 47.225 1.00 15.17 C ANISOU 4780 CA LYS C 137 1951 1941 1872 28 -8 17 C ATOM 4781 C LYS C 137 -9.654 39.798 45.969 1.00 14.89 C ANISOU 4781 C LYS C 137 1908 1861 1889 4 -16 -1 C ATOM 4782 O LYS C 137 -10.291 39.344 45.014 1.00 14.93 O ANISOU 4782 O LYS C 137 1941 1816 1915 25 -16 -27 O ATOM 4783 CB LYS C 137 -10.307 41.796 47.348 1.00 18.15 C ANISOU 4783 CB LYS C 137 2411 2085 2401 -68 25 -103 C ATOM 4784 CG LYS C 137 -10.975 42.518 46.187 1.00 22.50 C ANISOU 4784 CG LYS C 137 2851 2955 2744 52 -85 115 C ATOM 4785 CD LYS C 137 -10.944 44.027 46.374 1.00 27.28 C ANISOU 4785 CD LYS C 137 3532 3265 3570 -31 47 -86 C ATOM 4786 CE LYS C 137 -11.615 44.726 45.200 1.00 30.99 C ANISOU 4786 CE LYS C 137 3963 3984 3828 48 -51 68 C ATOM 4787 NZ LYS C 137 -11.525 46.206 45.320 1.00 33.50 N ANISOU 4787 NZ LYS C 137 4307 4151 4271 -1 3 -9 N ATOM 4788 N LYS C 138 -8.326 39.844 45.946 1.00 14.78 N ANISOU 4788 N LYS C 138 1922 1796 1899 -14 3 -7 N ATOM 4789 CA LYS C 138 -7.531 39.408 44.811 1.00 15.33 C ANISOU 4789 CA LYS C 138 2066 1847 1912 5 29 -5 C ATOM 4790 C LYS C 138 -7.812 37.952 44.446 1.00 14.74 C ANISOU 4790 C LYS C 138 1980 1807 1815 14 23 13 C ATOM 4791 O LYS C 138 -7.869 37.602 43.266 1.00 14.80 O ANISOU 4791 O LYS C 138 2001 1815 1806 4 -12 45 O ATOM 4792 CB LYS C 138 -6.032 39.554 45.068 1.00 19.37 C ANISOU 4792 CB LYS C 138 2231 2632 2496 39 -23 28 C ATOM 4793 CG LYS C 138 -5.513 40.971 45.232 1.00 24.43 C ANISOU 4793 CG LYS C 138 3273 2866 3142 -54 -9 -34 C ATOM 4794 CD LYS C 138 -4.000 40.946 45.420 1.00 28.98 C ANISOU 4794 CD LYS C 138 3541 3768 3703 38 -5 28 C ATOM 4795 CE LYS C 138 -3.453 42.295 45.845 1.00 31.68 C ANISOU 4795 CE LYS C 138 4092 3919 4025 -40 6 -26 C ATOM 4796 NZ LYS C 138 -2.028 42.202 46.276 1.00 33.02 N ANISOU 4796 NZ LYS C 138 4179 4168 4200 10 -15 2 N ATOM 4797 N PHE C 139 -7.985 37.103 45.458 1.00 14.03 N ANISOU 4797 N PHE C 139 1868 1670 1794 7 7 -33 N ATOM 4798 CA PHE C 139 -8.265 35.694 45.242 1.00 13.08 C ANISOU 4798 CA PHE C 139 1683 1637 1650 11 -28 -4 C ATOM 4799 C PHE C 139 -9.721 35.386 44.928 1.00 12.62 C ANISOU 4799 C PHE C 139 1640 1583 1572 28 -5 13 C ATOM 4800 O PHE C 139 -10.033 34.216 44.685 1.00 13.28 O ANISOU 4800 O PHE C 139 1702 1636 1708 8 -39 -30 O ATOM 4801 CB PHE C 139 -7.862 34.857 46.458 1.00 12.81 C ANISOU 4801 CB PHE C 139 1671 1571 1624 20 -16 -26 C ATOM 4802 CG PHE C 139 -6.426 34.876 46.875 1.00 13.31 C ANISOU 4802 CG PHE C 139 1698 1677 1683 -2 -11 -34 C ATOM 4803 CD1 PHE C 139 -5.415 35.359 46.062 1.00 13.56 C ANISOU 4803 CD1 PHE C 139 1720 1681 1749 12 31 -25 C ATOM 4804 CD2 PHE C 139 -6.080 34.400 48.133 1.00 13.20 C ANISOU 4804 CD2 PHE C 139 1713 1592 1711 28 -15 -13 C ATOM 4805 CE1 PHE C 139 -4.101 35.361 46.479 1.00 13.93 C ANISOU 4805 CE1 PHE C 139 1793 1754 1745 -1 -49 -36 C ATOM 4806 CE2 PHE C 139 -4.768 34.399 48.559 1.00 13.25 C ANISOU 4806 CE2 PHE C 139 1695 1559 1779 0 1 -7 C ATOM 4807 CZ PHE C 139 -3.774 34.876 47.727 1.00 13.32 C ANISOU 4807 CZ PHE C 139 1765 1593 1705 -7 24 -25 C ATOM 4808 N SER C 140 -10.616 36.362 44.972 1.00 11.98 N ANISOU 4808 N SER C 140 1561 1504 1489 -26 -1 -1 N ATOM 4809 CA SER C 140 -12.043 36.155 44.800 1.00 11.93 C ANISOU 4809 CA SER C 140 1556 1487 1491 2 17 64 C ATOM 4810 C SER C 140 -12.546 35.056 45.735 1.00 11.27 C ANISOU 4810 C SER C 140 1468 1385 1429 -17 -17 5 C ATOM 4811 O SER C 140 -13.249 34.130 45.342 1.00 11.36 O ANISOU 4811 O SER C 140 1507 1398 1410 -9 -61 6 O ATOM 4812 CB ASER C 140 -12.368 35.816 43.345 0.50 14.17 C ANISOU 4812 CB ASER C 140 1948 1808 1627 -20 -40 -46 C ATOM 4813 CB BSER C 140 -12.381 35.811 43.349 0.50 11.44 C ANISOU 4813 CB BSER C 140 1471 1344 1531 -3 -4 72 C ATOM 4814 OG ASER C 140 -13.746 36.022 43.083 0.50 16.88 O ANISOU 4814 OG ASER C 140 2087 2175 2153 3 -32 -17 O ATOM 4815 OG BSER C 140 -12.230 36.942 42.508 0.50 9.90 O ANISOU 4815 OG BSER C 140 1313 1242 1208 -15 -21 -35 O ATOM 4816 N TYR C 141 -12.219 35.205 47.016 1.00 11.18 N ANISOU 4816 N TYR C 141 1509 1340 1399 -39 20 4 N ATOM 4817 CA TYR C 141 -12.402 34.125 47.977 1.00 10.72 C ANISOU 4817 CA TYR C 141 1420 1308 1346 3 -36 -5 C ATOM 4818 C TYR C 141 -13.728 34.260 48.708 1.00 11.00 C ANISOU 4818 C TYR C 141 1467 1373 1340 14 0 11 C ATOM 4819 O TYR C 141 -13.838 34.966 49.716 1.00 11.01 O ANISOU 4819 O TYR C 141 1474 1341 1367 15 -55 -20 O ATOM 4820 CB TYR C 141 -11.235 34.080 48.965 1.00 10.71 C ANISOU 4820 CB TYR C 141 1402 1315 1353 -3 -22 -15 C ATOM 4821 CG TYR C 141 -11.219 32.790 49.761 1.00 10.88 C ANISOU 4821 CG TYR C 141 1440 1318 1374 -19 -1 -6 C ATOM 4822 CD1 TYR C 141 -10.534 31.685 49.268 1.00 11.18 C ANISOU 4822 CD1 TYR C 141 1484 1370 1395 14 -6 -19 C ATOM 4823 CD2 TYR C 141 -11.876 32.678 50.973 1.00 10.42 C ANISOU 4823 CD2 TYR C 141 1375 1263 1320 -18 -38 -22 C ATOM 4824 CE1 TYR C 141 -10.508 30.497 49.979 1.00 11.01 C ANISOU 4824 CE1 TYR C 141 1426 1372 1385 -3 -15 -18 C ATOM 4825 CE2 TYR C 141 -11.852 31.494 51.691 1.00 10.39 C ANISOU 4825 CE2 TYR C 141 1347 1289 1311 -5 -47 -6 C ATOM 4826 CZ TYR C 141 -11.167 30.410 51.182 1.00 10.65 C ANISOU 4826 CZ TYR C 141 1410 1308 1328 0 -37 -20 C ATOM 4827 OH TYR C 141 -11.147 29.234 51.897 1.00 11.39 O ANISOU 4827 OH TYR C 141 1618 1353 1357 46 -67 4 O ATOM 4828 N GLY C 142 -14.755 33.602 48.183 1.00 11.84 N ANISOU 4828 N GLY C 142 1538 1499 1462 -31 -33 4 N ATOM 4829 CA GLY C 142 -16.057 33.546 48.832 1.00 12.54 C ANISOU 4829 CA GLY C 142 1591 1624 1548 13 3 -15 C ATOM 4830 C GLY C 142 -16.717 34.915 48.888 1.00 13.08 C ANISOU 4830 C GLY C 142 1709 1633 1629 23 -1 -24 C ATOM 4831 O GLY C 142 -16.559 35.764 48.008 1.00 13.66 O ANISOU 4831 O GLY C 142 1861 1648 1681 25 -18 -12 O ATOM 4832 N ASN C 143 -17.417 35.174 49.993 1.00 13.19 N ANISOU 4832 N ASN C 143 1749 1659 1604 40 -11 -10 N ATOM 4833 CA ASN C 143 -18.062 36.468 50.200 1.00 13.11 C ANISOU 4833 CA ASN C 143 1716 1639 1626 25 -9 19 C ATOM 4834 C ASN C 143 -17.076 37.545 50.617 1.00 13.54 C ANISOU 4834 C ASN C 143 1728 1714 1702 1 -31 5 C ATOM 4835 O ASN C 143 -17.441 38.708 50.817 1.00 14.31 O ANISOU 4835 O ASN C 143 1829 1753 1858 16 -69 -36 O ATOM 4836 CB ASN C 143 -19.213 36.351 51.194 1.00 12.94 C ANISOU 4836 CB ASN C 143 1683 1628 1605 11 -33 31 C ATOM 4837 CG ASN C 143 -18.820 35.986 52.608 1.00 12.45 C ANISOU 4837 CG ASN C 143 1600 1581 1551 -20 17 13 C ATOM 4838 OD1 ASN C 143 -17.640 35.920 52.944 1.00 12.87 O ANISOU 4838 OD1 ASN C 143 1659 1668 1564 46 -42 13 O ATOM 4839 ND2 ASN C 143 -19.821 35.747 53.450 1.00 11.69 N ANISOU 4839 ND2 ASN C 143 1487 1485 1469 27 -50 -20 N ATOM 4840 N GLN C 144 -15.815 37.206 50.856 1.00 13.23 N ANISOU 4840 N GLN C 144 1734 1672 1622 0 -37 19 N ATOM 4841 CA GLN C 144 -14.733 38.120 51.156 1.00 13.77 C ANISOU 4841 CA GLN C 144 1747 1728 1756 -6 -6 -17 C ATOM 4842 C GLN C 144 -14.970 38.885 52.454 1.00 13.89 C ANISOU 4842 C GLN C 144 1787 1751 1739 -26 3 -7 C ATOM 4843 O GLN C 144 -14.395 39.951 52.677 1.00 14.71 O ANISOU 4843 O GLN C 144 1938 1793 1857 -61 8 -51 O ATOM 4844 CB GLN C 144 -14.493 39.097 49.998 1.00 15.10 C ANISOU 4844 CB GLN C 144 1982 1826 1929 -33 -4 76 C ATOM 4845 CG GLN C 144 -13.943 38.445 48.739 1.00 17.59 C ANISOU 4845 CG GLN C 144 2221 2275 2189 27 47 -122 C ATOM 4846 CD GLN C 144 -13.855 39.401 47.567 1.00 20.13 C ANISOU 4846 CD GLN C 144 2564 2560 2525 2 20 98 C ATOM 4847 OE1 GLN C 144 -13.998 38.985 46.417 1.00 21.71 O ANISOU 4847 OE1 GLN C 144 2788 2835 2624 48 -18 20 O ATOM 4848 NE2 GLN C 144 -13.618 40.678 47.836 1.00 21.82 N ANISOU 4848 NE2 GLN C 144 2836 2657 2796 -15 30 43 N ATOM 4849 N ASN C 145 -15.772 38.320 53.344 1.00 13.22 N ANISOU 4849 N ASN C 145 1691 1681 1651 2 -29 -40 N ATOM 4850 CA ASN C 145 -16.201 39.005 54.555 1.00 13.23 C ANISOU 4850 CA ASN C 145 1699 1656 1673 3 -5 -26 C ATOM 4851 C ASN C 145 -15.365 38.467 55.713 1.00 13.56 C ANISOU 4851 C ASN C 145 1741 1714 1697 -3 -28 -16 C ATOM 4852 O ASN C 145 -15.572 37.342 56.159 1.00 13.88 O ANISOU 4852 O ASN C 145 1814 1733 1727 23 -56 4 O ATOM 4853 CB ASN C 145 -17.691 38.796 54.793 1.00 13.28 C ANISOU 4853 CB ASN C 145 1713 1617 1716 -20 -2 -1 C ATOM 4854 CG ASN C 145 -18.262 39.626 55.921 1.00 14.17 C ANISOU 4854 CG ASN C 145 1894 1761 1729 -11 -46 -69 C ATOM 4855 OD1 ASN C 145 -19.484 39.804 56.007 1.00 16.89 O ANISOU 4855 OD1 ASN C 145 2035 2149 2236 17 28 8 O ATOM 4856 ND2 ASN C 145 -17.417 40.137 56.804 1.00 11.88 N ANISOU 4856 ND2 ASN C 145 1584 1324 1605 82 31 26 N ATOM 4857 N ILE C 146 -14.457 39.313 56.202 1.00 13.67 N ANISOU 4857 N ILE C 146 1715 1761 1717 10 -33 -37 N ATOM 4858 CA ILE C 146 -13.541 38.845 57.240 1.00 13.50 C ANISOU 4858 CA ILE C 146 1744 1707 1677 9 -17 -29 C ATOM 4859 C ILE C 146 -13.957 39.390 58.602 1.00 13.38 C ANISOU 4859 C ILE C 146 1741 1674 1667 0 -9 -24 C ATOM 4860 O ILE C 146 -13.158 39.322 59.531 1.00 13.01 O ANISOU 4860 O ILE C 146 1713 1576 1654 22 11 -61 O ATOM 4861 CB ILE C 146 -12.079 39.191 56.935 1.00 13.59 C ANISOU 4861 CB ILE C 146 1756 1687 1720 18 12 2 C ATOM 4862 CG1 ILE C 146 -11.865 40.705 56.840 1.00 12.99 C ANISOU 4862 CG1 ILE C 146 1713 1654 1568 8 11 10 C ATOM 4863 CG2 ILE C 146 -11.626 38.520 55.641 1.00 13.88 C ANISOU 4863 CG2 ILE C 146 1829 1701 1746 46 -12 -25 C ATOM 4864 CD1 ILE C 146 -10.401 41.099 56.769 1.00 14.61 C ANISOU 4864 CD1 ILE C 146 1821 1782 1950 -40 -17 -11 C ATOM 4865 N SER C 147 -15.190 39.865 58.732 1.00 13.83 N ANISOU 4865 N SER C 147 1781 1703 1772 26 -23 -16 N ATOM 4866 CA SER C 147 -15.708 40.269 60.033 1.00 14.74 C ANISOU 4866 CA SER C 147 1896 1875 1831 29 18 -31 C ATOM 4867 C SER C 147 -15.773 39.089 61.002 1.00 15.83 C ANISOU 4867 C SER C 147 2083 1961 1971 -4 8 29 C ATOM 4868 O SER C 147 -15.906 37.937 60.593 1.00 16.20 O ANISOU 4868 O SER C 147 2112 1997 2048 -20 15 -5 O ATOM 4869 CB ASER C 147 -17.088 40.916 59.911 0.50 14.76 C ANISOU 4869 CB ASER C 147 1888 1864 1858 10 18 9 C ATOM 4870 CB BSER C 147 -17.104 40.882 59.902 0.50 14.88 C ANISOU 4870 CB BSER C 147 1891 1894 1869 17 20 -6 C ATOM 4871 OG ASER C 147 -17.471 41.491 61.149 0.50 14.79 O ANISOU 4871 OG ASER C 147 1876 1868 1875 -15 0 -27 O ATOM 4872 OG BSER C 147 -17.053 42.112 59.203 0.50 15.63 O ANISOU 4872 OG BSER C 147 2040 1899 2000 -8 0 -5 O ATOM 4873 N GLY C 148 -15.652 39.404 62.289 1.00 16.05 N ANISOU 4873 N GLY C 148 2104 1996 1998 -14 -2 -6 N ATOM 4874 CA GLY C 148 -15.828 38.410 63.335 1.00 15.74 C ANISOU 4874 CA GLY C 148 2014 1988 1977 -11 0 -14 C ATOM 4875 C GLY C 148 -14.601 38.214 64.209 1.00 15.80 C ANISOU 4875 C GLY C 148 2011 2008 1987 -20 0 -20 C ATOM 4876 O GLY C 148 -14.643 37.422 65.153 1.00 16.35 O ANISOU 4876 O GLY C 148 2149 2039 2026 -18 -18 -3 O ATOM 4877 N GLY C 149 -13.520 38.922 63.914 1.00 15.45 N ANISOU 4877 N GLY C 149 1958 1972 1942 4 -16 -40 N ATOM 4878 CA GLY C 149 -12.271 38.777 64.660 1.00 15.00 C ANISOU 4878 CA GLY C 149 1931 1886 1883 15 4 -42 C ATOM 4879 C GLY C 149 -11.162 38.292 63.737 1.00 14.76 C ANISOU 4879 C GLY C 149 1897 1856 1854 -5 -17 -32 C ATOM 4880 O GLY C 149 -11.338 37.322 62.997 1.00 14.47 O ANISOU 4880 O GLY C 149 1867 1828 1801 7 -36 -34 O ATOM 4881 N ILE C 150 -10.018 38.973 63.740 1.00 14.75 N ANISOU 4881 N ILE C 150 1902 1867 1836 -13 -26 -48 N ATOM 4882 CA ILE C 150 -8.957 38.723 62.774 1.00 15.27 C ANISOU 4882 CA ILE C 150 1966 1950 1886 16 5 -14 C ATOM 4883 C ILE C 150 -8.384 37.317 62.877 1.00 15.49 C ANISOU 4883 C ILE C 150 1970 1966 1950 14 -1 -14 C ATOM 4884 O ILE C 150 -7.914 36.767 61.874 1.00 15.56 O ANISOU 4884 O ILE C 150 2012 1971 1931 -4 -18 -31 O ATOM 4885 CB ILE C 150 -7.828 39.768 62.876 1.00 16.58 C ANISOU 4885 CB ILE C 150 2059 2084 2158 -35 -37 8 C ATOM 4886 CG1 ILE C 150 -6.821 39.614 61.735 1.00 17.00 C ANISOU 4886 CG1 ILE C 150 2134 2104 2221 4 11 18 C ATOM 4887 CG2 ILE C 150 -7.126 39.678 64.222 1.00 16.80 C ANISOU 4887 CG2 ILE C 150 2135 2132 2118 9 -11 -24 C ATOM 4888 CD1 ILE C 150 -7.425 39.754 60.354 1.00 18.73 C ANISOU 4888 CD1 ILE C 150 2432 2425 2262 -25 -5 -14 C ATOM 4889 N ASP C 151 -8.431 36.706 64.058 1.00 15.81 N ANISOU 4889 N ASP C 151 2042 1993 1971 -25 -9 -7 N ATOM 4890 CA ASP C 151 -7.939 35.353 64.239 1.00 16.44 C ANISOU 4890 CA ASP C 151 2114 2014 2120 -8 33 -15 C ATOM 4891 C ASP C 151 -9.043 34.311 64.349 1.00 15.85 C ANISOU 4891 C ASP C 151 2044 1982 1995 14 -19 5 C ATOM 4892 O ASP C 151 -8.746 33.214 64.835 1.00 15.83 O ANISOU 4892 O ASP C 151 2099 1936 1979 7 -45 -57 O ATOM 4893 CB ASP C 151 -7.014 35.276 65.458 1.00 19.08 C ANISOU 4893 CB ASP C 151 2402 2439 2409 -2 -155 21 C ATOM 4894 CG ASP C 151 -7.668 35.717 66.749 1.00 21.95 C ANISOU 4894 CG ASP C 151 2809 2793 2737 27 107 -23 C ATOM 4895 OD1 ASP C 151 -8.902 35.892 66.797 1.00 21.43 O ANISOU 4895 OD1 ASP C 151 2782 2715 2645 5 3 -61 O ATOM 4896 OD2 ASP C 151 -6.930 35.891 67.746 1.00 24.60 O ANISOU 4896 OD2 ASP C 151 3176 3151 3021 -14 -111 -29 O ATOM 4897 N LYS C 152 -10.240 34.572 63.827 1.00 15.48 N ANISOU 4897 N LYS C 152 2000 1924 1959 -13 -9 19 N ATOM 4898 CA LYS C 152 -11.298 33.573 63.869 1.00 15.45 C ANISOU 4898 CA LYS C 152 1952 1916 2001 15 -93 6 C ATOM 4899 C LYS C 152 -12.370 33.745 62.809 1.00 14.10 C ANISOU 4899 C LYS C 152 1835 1730 1792 -6 18 18 C ATOM 4900 O LYS C 152 -13.355 32.999 62.819 1.00 13.70 O ANISOU 4900 O LYS C 152 1787 1768 1650 8 -40 -11 O ATOM 4901 CB LYS C 152 -11.944 33.586 65.267 1.00 19.65 C ANISOU 4901 CB LYS C 152 2483 2706 2278 -64 96 42 C ATOM 4902 CG LYS C 152 -12.623 34.904 65.594 1.00 24.87 C ANISOU 4902 CG LYS C 152 3141 2963 3344 76 15 -12 C ATOM 4903 CD LYS C 152 -12.733 35.158 67.084 1.00 29.64 C ANISOU 4903 CD LYS C 152 3848 3806 3606 52 -38 -53 C ATOM 4904 CE LYS C 152 -13.733 34.253 67.773 1.00 32.02 C ANISOU 4904 CE LYS C 152 4021 4035 4108 -47 9 30 C ATOM 4905 NZ LYS C 152 -13.974 34.675 69.183 1.00 33.10 N ANISOU 4905 NZ LYS C 152 4218 4190 4170 -3 12 -1 N ATOM 4906 N PHE C 153 -12.199 34.650 61.843 1.00 13.47 N ANISOU 4906 N PHE C 153 1726 1708 1683 36 -41 2 N ATOM 4907 CA PHE C 153 -13.300 34.977 60.939 1.00 12.38 C ANISOU 4907 CA PHE C 153 1620 1515 1569 0 17 -6 C ATOM 4908 C PHE C 153 -13.681 33.829 60.014 1.00 12.18 C ANISOU 4908 C PHE C 153 1568 1507 1555 -9 1 9 C ATOM 4909 O PHE C 153 -14.825 33.773 59.563 1.00 12.61 O ANISOU 4909 O PHE C 153 1605 1551 1634 -11 -42 -10 O ATOM 4910 CB PHE C 153 -12.993 36.214 60.100 1.00 11.81 C ANISOU 4910 CB PHE C 153 1502 1490 1498 9 -9 -22 C ATOM 4911 CG PHE C 153 -11.766 36.124 59.245 1.00 11.96 C ANISOU 4911 CG PHE C 153 1516 1505 1524 11 -1 -5 C ATOM 4912 CD1 PHE C 153 -11.810 35.531 57.989 1.00 12.74 C ANISOU 4912 CD1 PHE C 153 1647 1645 1548 17 -19 -15 C ATOM 4913 CD2 PHE C 153 -10.559 36.626 59.700 1.00 11.30 C ANISOU 4913 CD2 PHE C 153 1540 1316 1436 4 -21 24 C ATOM 4914 CE1 PHE C 153 -10.667 35.450 57.220 1.00 13.00 C ANISOU 4914 CE1 PHE C 153 1666 1623 1649 4 24 13 C ATOM 4915 CE2 PHE C 153 -9.417 36.553 58.932 1.00 12.42 C ANISOU 4915 CE2 PHE C 153 1612 1532 1574 26 27 -6 C ATOM 4916 CZ PHE C 153 -9.472 35.959 57.683 1.00 12.96 C ANISOU 4916 CZ PHE C 153 1743 1579 1600 -5 -46 -14 C ATOM 4917 N TRP C 154 -12.743 32.946 59.710 1.00 11.91 N ANISOU 4917 N TRP C 154 1587 1458 1481 -22 10 -10 N ATOM 4918 CA TRP C 154 -12.979 31.792 58.857 1.00 11.71 C ANISOU 4918 CA TRP C 154 1523 1475 1452 3 -16 -22 C ATOM 4919 C TRP C 154 -13.668 30.642 59.578 1.00 12.16 C ANISOU 4919 C TRP C 154 1586 1518 1518 -28 -21 -11 C ATOM 4920 O TRP C 154 -14.094 29.671 58.942 1.00 11.98 O ANISOU 4920 O TRP C 154 1610 1491 1453 -38 -15 0 O ATOM 4921 CB TRP C 154 -11.623 31.295 58.319 1.00 12.30 C ANISOU 4921 CB TRP C 154 1559 1550 1564 46 8 28 C ATOM 4922 CG TRP C 154 -10.678 30.938 59.432 1.00 12.31 C ANISOU 4922 CG TRP C 154 1607 1524 1546 11 -43 -58 C ATOM 4923 CD1 TRP C 154 -10.618 29.761 60.121 1.00 12.87 C ANISOU 4923 CD1 TRP C 154 1657 1620 1614 14 3 19 C ATOM 4924 CD2 TRP C 154 -9.666 31.784 59.989 1.00 11.90 C ANISOU 4924 CD2 TRP C 154 1496 1497 1528 24 17 -25 C ATOM 4925 NE1 TRP C 154 -9.633 29.824 61.075 1.00 13.39 N ANISOU 4925 NE1 TRP C 154 1674 1641 1773 -17 -57 20 N ATOM 4926 CE2 TRP C 154 -9.035 31.057 61.016 1.00 12.52 C ANISOU 4926 CE2 TRP C 154 1608 1566 1581 42 -12 -4 C ATOM 4927 CE3 TRP C 154 -9.241 33.089 59.728 1.00 12.37 C ANISOU 4927 CE3 TRP C 154 1536 1561 1602 -26 -10 20 C ATOM 4928 CZ2 TRP C 154 -7.989 31.583 61.768 1.00 12.72 C ANISOU 4928 CZ2 TRP C 154 1625 1606 1604 -47 30 0 C ATOM 4929 CZ3 TRP C 154 -8.204 33.615 60.477 1.00 12.02 C ANISOU 4929 CZ3 TRP C 154 1593 1506 1469 -30 0 -4 C ATOM 4930 CH2 TRP C 154 -7.579 32.856 61.477 1.00 12.83 C ANISOU 4930 CH2 TRP C 154 1715 1555 1605 21 -42 33 C ATOM 4931 N LEU C 155 -13.733 30.704 60.906 1.00 12.37 N ANISOU 4931 N LEU C 155 1607 1566 1526 -2 -12 -37 N ATOM 4932 CA LEU C 155 -14.211 29.588 61.710 1.00 12.87 C ANISOU 4932 CA LEU C 155 1682 1615 1593 -29 -32 -10 C ATOM 4933 C LEU C 155 -15.459 29.944 62.501 1.00 13.65 C ANISOU 4933 C LEU C 155 1724 1747 1715 3 -11 -3 C ATOM 4934 O LEU C 155 -16.380 29.125 62.593 1.00 13.77 O ANISOU 4934 O LEU C 155 1782 1741 1710 -22 -42 -30 O ATOM 4935 CB LEU C 155 -13.099 29.108 62.647 1.00 13.08 C ANISOU 4935 CB LEU C 155 1664 1650 1657 9 -28 -7 C ATOM 4936 CG LEU C 155 -13.438 27.969 63.608 1.00 13.68 C ANISOU 4936 CG LEU C 155 1785 1663 1748 -5 24 -1 C ATOM 4937 CD1 LEU C 155 -13.704 26.673 62.852 1.00 13.68 C ANISOU 4937 CD1 LEU C 155 1782 1711 1705 -29 -12 -21 C ATOM 4938 CD2 LEU C 155 -12.315 27.775 64.618 1.00 15.09 C ANISOU 4938 CD2 LEU C 155 1914 1941 1880 -26 -50 14 C ATOM 4939 N GLU C 156 -15.494 31.140 63.093 1.00 14.34 N ANISOU 4939 N GLU C 156 1841 1748 1861 15 -65 -4 N ATOM 4940 CA GLU C 156 -16.724 31.574 63.758 1.00 15.82 C ANISOU 4940 CA GLU C 156 1963 1947 2102 41 39 -4 C ATOM 4941 C GLU C 156 -17.162 32.966 63.325 1.00 15.37 C ANISOU 4941 C GLU C 156 1966 1921 1951 -2 33 22 C ATOM 4942 O GLU C 156 -18.063 33.540 63.943 1.00 16.11 O ANISOU 4942 O GLU C 156 2035 2063 2023 70 49 61 O ATOM 4943 CB GLU C 156 -16.638 31.463 65.275 1.00 20.73 C ANISOU 4943 CB GLU C 156 2776 2770 2330 24 32 5 C ATOM 4944 CG GLU C 156 -15.282 31.587 65.914 1.00 23.07 C ANISOU 4944 CG GLU C 156 2858 3040 2866 -7 -11 -43 C ATOM 4945 CD GLU C 156 -15.228 31.127 67.358 1.00 22.50 C ANISOU 4945 CD GLU C 156 2802 2858 2889 27 -33 29 C ATOM 4946 OE1 GLU C 156 -16.275 31.038 68.033 1.00 22.38 O ANISOU 4946 OE1 GLU C 156 2846 2869 2788 5 -20 12 O ATOM 4947 OE2 GLU C 156 -14.102 30.857 67.829 1.00 20.15 O ANISOU 4947 OE2 GLU C 156 2692 2510 2454 -10 21 2 O ATOM 4948 N GLY C 157 -16.555 33.501 62.274 1.00 14.30 N ANISOU 4948 N GLY C 157 1897 1757 1778 23 -33 -41 N ATOM 4949 CA GLY C 157 -16.885 34.830 61.786 1.00 13.42 C ANISOU 4949 CA GLY C 157 1755 1708 1635 -9 -29 -53 C ATOM 4950 C GLY C 157 -17.858 34.799 60.611 1.00 12.98 C ANISOU 4950 C GLY C 157 1697 1625 1611 -16 -8 -8 C ATOM 4951 O GLY C 157 -18.668 33.886 60.491 1.00 12.71 O ANISOU 4951 O GLY C 157 1681 1630 1517 -14 -37 -44 O ATOM 4952 N GLN C 158 -17.741 35.787 59.728 1.00 12.62 N ANISOU 4952 N GLN C 158 1670 1624 1500 20 1 -38 N ATOM 4953 CA GLN C 158 -18.707 36.002 58.668 1.00 12.51 C ANISOU 4953 CA GLN C 158 1638 1590 1527 22 2 -18 C ATOM 4954 C GLN C 158 -18.248 35.463 57.316 1.00 12.17 C ANISOU 4954 C GLN C 158 1561 1548 1515 27 -2 -15 C ATOM 4955 O GLN C 158 -19.003 35.600 56.349 1.00 12.07 O ANISOU 4955 O GLN C 158 1569 1540 1476 35 8 -34 O ATOM 4956 CB GLN C 158 -18.981 37.502 58.493 1.00 12.93 C ANISOU 4956 CB GLN C 158 1683 1612 1616 35 -53 -1 C ATOM 4957 CG GLN C 158 -19.588 38.188 59.704 1.00 13.94 C ANISOU 4957 CG GLN C 158 1859 1733 1705 38 10 -29 C ATOM 4958 CD GLN C 158 -20.914 37.557 60.078 1.00 15.14 C ANISOU 4958 CD GLN C 158 1967 1896 1889 -41 59 -47 C ATOM 4959 OE1 GLN C 158 -21.907 37.761 59.383 1.00 17.89 O ANISOU 4959 OE1 GLN C 158 2174 2321 2301 73 -94 5 O ATOM 4960 NE2 GLN C 158 -20.904 36.785 61.157 1.00 15.42 N ANISOU 4960 NE2 GLN C 158 2067 1818 1974 -17 17 -21 N ATOM 4961 N LEU C 159 -17.046 34.907 57.251 1.00 11.91 N ANISOU 4961 N LEU C 159 1544 1523 1458 16 15 -36 N ATOM 4962 CA LEU C 159 -16.515 34.438 55.972 1.00 11.27 C ANISOU 4962 CA LEU C 159 1437 1406 1438 5 10 -17 C ATOM 4963 C LEU C 159 -17.243 33.188 55.505 1.00 11.22 C ANISOU 4963 C LEU C 159 1465 1407 1392 -5 -10 -8 C ATOM 4964 O LEU C 159 -17.495 32.259 56.273 1.00 11.33 O ANISOU 4964 O LEU C 159 1580 1375 1351 8 -24 -30 O ATOM 4965 CB LEU C 159 -15.012 34.179 56.064 1.00 10.91 C ANISOU 4965 CB LEU C 159 1417 1372 1356 12 2 -5 C ATOM 4966 CG LEU C 159 -14.308 33.769 54.768 1.00 10.70 C ANISOU 4966 CG LEU C 159 1366 1364 1335 -1 -22 -24 C ATOM 4967 CD1 LEU C 159 -14.511 34.820 53.685 1.00 11.44 C ANISOU 4967 CD1 LEU C 159 1487 1419 1440 41 -9 32 C ATOM 4968 CD2 LEU C 159 -12.819 33.536 54.996 1.00 10.67 C ANISOU 4968 CD2 LEU C 159 1360 1370 1323 -1 8 34 C ATOM 4969 N ARG C 160 -17.648 33.180 54.239 1.00 11.05 N ANISOU 4969 N ARG C 160 1437 1345 1416 21 -51 1 N ATOM 4970 CA ARG C 160 -18.376 32.064 53.647 1.00 10.92 C ANISOU 4970 CA ARG C 160 1410 1372 1368 3 -10 -16 C ATOM 4971 C ARG C 160 -17.842 31.816 52.234 1.00 10.90 C ANISOU 4971 C ARG C 160 1464 1325 1352 -13 -12 -11 C ATOM 4972 O ARG C 160 -17.512 32.778 51.542 1.00 10.78 O ANISOU 4972 O ARG C 160 1555 1340 1202 11 7 -36 O ATOM 4973 CB ARG C 160 -19.875 32.354 53.567 1.00 12.01 C ANISOU 4973 CB ARG C 160 1454 1581 1528 59 30 -32 C ATOM 4974 CG ARG C 160 -20.634 32.628 54.847 1.00 11.28 C ANISOU 4974 CG ARG C 160 1468 1410 1408 13 11 38 C ATOM 4975 CD ARG C 160 -20.721 31.400 55.744 1.00 11.64 C ANISOU 4975 CD ARG C 160 1499 1425 1499 23 3 60 C ATOM 4976 NE ARG C 160 -21.510 31.648 56.945 1.00 12.29 N ANISOU 4976 NE ARG C 160 1621 1553 1498 34 -7 7 N ATOM 4977 CZ ARG C 160 -21.035 32.204 58.058 1.00 12.04 C ANISOU 4977 CZ ARG C 160 1497 1485 1593 -6 -23 -37 C ATOM 4978 NH1 ARG C 160 -19.762 32.557 58.139 1.00 10.15 N ANISOU 4978 NH1 ARG C 160 1418 1149 1290 58 -12 -96 N ATOM 4979 NH2 ARG C 160 -21.842 32.395 59.096 1.00 13.31 N ANISOU 4979 NH2 ARG C 160 1804 1660 1592 15 54 4 N ATOM 4980 N ILE C 161 -17.761 30.559 51.818 1.00 10.64 N ANISOU 4980 N ILE C 161 1407 1329 1307 33 -30 -23 N ATOM 4981 CA ILE C 161 -17.310 30.225 50.469 1.00 10.49 C ANISOU 4981 CA ILE C 161 1355 1332 1297 -5 -31 -3 C ATOM 4982 C ILE C 161 -18.066 28.997 49.969 1.00 10.53 C ANISOU 4982 C ILE C 161 1397 1306 1297 -3 -6 -9 C ATOM 4983 O ILE C 161 -18.396 28.104 50.750 1.00 10.39 O ANISOU 4983 O ILE C 161 1472 1251 1226 29 -8 -53 O ATOM 4984 CB ILE C 161 -15.792 30.007 50.397 1.00 9.94 C ANISOU 4984 CB ILE C 161 1349 1248 1179 59 -10 -16 C ATOM 4985 CG1 ILE C 161 -15.315 29.855 48.949 1.00 9.47 C ANISOU 4985 CG1 ILE C 161 1228 1178 1191 11 16 16 C ATOM 4986 CG2 ILE C 161 -15.376 28.801 51.240 1.00 10.32 C ANISOU 4986 CG2 ILE C 161 1413 1235 1273 26 -70 -7 C ATOM 4987 CD1 ILE C 161 -13.816 29.867 48.772 1.00 10.01 C ANISOU 4987 CD1 ILE C 161 1260 1305 1237 -2 -15 -14 C ATOM 4988 N SER C 162 -18.379 28.974 48.672 1.00 10.60 N ANISOU 4988 N SER C 162 1403 1307 1317 18 -39 -32 N ATOM 4989 CA SER C 162 -19.099 27.843 48.100 1.00 10.54 C ANISOU 4989 CA SER C 162 1363 1312 1330 22 -43 -7 C ATOM 4990 C SER C 162 -18.140 26.772 47.583 1.00 10.15 C ANISOU 4990 C SER C 162 1328 1299 1229 -1 -29 -10 C ATOM 4991 O SER C 162 -16.955 27.010 47.363 1.00 9.58 O ANISOU 4991 O SER C 162 1297 1176 1166 25 -58 -49 O ATOM 4992 CB SER C 162 -19.979 28.298 46.931 1.00 10.60 C ANISOU 4992 CB SER C 162 1338 1397 1291 4 -31 -23 C ATOM 4993 OG SER C 162 -19.189 28.570 45.786 1.00 10.31 O ANISOU 4993 OG SER C 162 1353 1294 1271 -15 -58 9 O ATOM 4994 N ALA C 163 -18.702 25.591 47.335 1.00 10.19 N ANISOU 4994 N ALA C 163 1338 1283 1250 19 -43 -3 N ATOM 4995 CA ALA C 163 -17.968 24.496 46.713 1.00 10.06 C ANISOU 4995 CA ALA C 163 1289 1319 1215 23 -27 -6 C ATOM 4996 C ALA C 163 -17.488 24.873 45.314 1.00 10.49 C ANISOU 4996 C ALA C 163 1340 1384 1263 19 -2 22 C ATOM 4997 O ALA C 163 -16.339 24.615 44.962 1.00 10.15 O ANISOU 4997 O ALA C 163 1336 1361 1159 -3 -14 -35 O ATOM 4998 CB ALA C 163 -18.831 23.249 46.648 1.00 10.16 C ANISOU 4998 CB ALA C 163 1318 1308 1236 22 -55 17 C ATOM 4999 N VAL C 164 -18.362 25.495 44.519 1.00 10.48 N ANISOU 4999 N VAL C 164 1355 1330 1297 33 -10 7 N ATOM 5000 CA VAL C 164 -17.932 26.047 43.235 1.00 10.65 C ANISOU 5000 CA VAL C 164 1405 1324 1319 -11 7 -11 C ATOM 5001 C VAL C 164 -16.769 27.014 43.376 1.00 10.38 C ANISOU 5001 C VAL C 164 1354 1298 1293 22 -1 -18 C ATOM 5002 O VAL C 164 -15.782 26.927 42.637 1.00 10.42 O ANISOU 5002 O VAL C 164 1327 1295 1338 -7 -4 -49 O ATOM 5003 CB VAL C 164 -19.106 26.730 42.506 1.00 12.15 C ANISOU 5003 CB VAL C 164 1464 1607 1548 51 -64 -10 C ATOM 5004 CG1 VAL C 164 -18.639 27.457 41.254 1.00 14.02 C ANISOU 5004 CG1 VAL C 164 1834 1772 1721 -35 -14 61 C ATOM 5005 CG2 VAL C 164 -20.169 25.702 42.143 1.00 13.17 C ANISOU 5005 CG2 VAL C 164 1691 1647 1667 -70 -22 6 C ATOM 5006 N ASN C 165 -16.834 27.956 44.318 1.00 10.17 N ANISOU 5006 N ASN C 165 1339 1285 1242 27 -36 16 N ATOM 5007 CA ASN C 165 -15.763 28.931 44.482 1.00 10.23 C ANISOU 5007 CA ASN C 165 1335 1309 1244 13 -31 18 C ATOM 5008 C ASN C 165 -14.473 28.259 44.932 1.00 9.79 C ANISOU 5008 C ASN C 165 1312 1216 1193 1 -19 -7 C ATOM 5009 O ASN C 165 -13.384 28.643 44.501 1.00 10.38 O ANISOU 5009 O ASN C 165 1368 1343 1235 -20 12 22 O ATOM 5010 CB ASN C 165 -16.180 30.026 45.454 1.00 11.47 C ANISOU 5010 CB ASN C 165 1484 1427 1448 47 37 -74 C ATOM 5011 CG ASN C 165 -15.357 31.286 45.430 1.00 12.11 C ANISOU 5011 CG ASN C 165 1476 1540 1586 -16 -18 33 C ATOM 5012 OD1 ASN C 165 -15.860 32.305 45.930 1.00 13.68 O ANISOU 5012 OD1 ASN C 165 1779 1716 1702 24 26 -93 O ATOM 5013 ND2 ASN C 165 -14.145 31.324 44.903 1.00 11.76 N ANISOU 5013 ND2 ASN C 165 1504 1554 1409 13 39 33 N ATOM 5014 N GLN C 166 -14.557 27.233 45.777 1.00 9.54 N ANISOU 5014 N GLN C 166 1304 1206 1113 10 -16 -32 N ATOM 5015 CA GLN C 166 -13.367 26.469 46.144 1.00 9.62 C ANISOU 5015 CA GLN C 166 1285 1182 1187 0 0 17 C ATOM 5016 C GLN C 166 -12.697 25.862 44.918 1.00 9.92 C ANISOU 5016 C GLN C 166 1327 1203 1239 35 7 8 C ATOM 5017 O GLN C 166 -11.479 25.974 44.776 1.00 10.73 O ANISOU 5017 O GLN C 166 1383 1376 1317 14 39 -45 O ATOM 5018 CB GLN C 166 -13.716 25.379 47.159 1.00 9.72 C ANISOU 5018 CB GLN C 166 1315 1231 1148 -16 -11 35 C ATOM 5019 CG GLN C 166 -14.146 25.905 48.518 1.00 10.81 C ANISOU 5019 CG GLN C 166 1405 1428 1272 41 18 -49 C ATOM 5020 CD GLN C 166 -13.037 25.921 49.548 1.00 10.72 C ANISOU 5020 CD GLN C 166 1326 1337 1410 5 5 -10 C ATOM 5021 OE1 GLN C 166 -11.853 26.046 49.245 1.00 9.62 O ANISOU 5021 OE1 GLN C 166 1259 1225 1172 33 -83 -97 O ATOM 5022 NE2 GLN C 166 -13.442 25.790 50.812 1.00 12.45 N ANISOU 5022 NE2 GLN C 166 1727 1603 1401 50 -60 -14 N ATOM 5023 N VAL C 167 -13.458 25.257 44.010 1.00 10.38 N ANISOU 5023 N VAL C 167 1407 1239 1298 18 -27 26 N ATOM 5024 CA VAL C 167 -12.878 24.727 42.775 1.00 11.00 C ANISOU 5024 CA VAL C 167 1471 1370 1338 48 16 34 C ATOM 5025 C VAL C 167 -12.220 25.817 41.945 1.00 11.02 C ANISOU 5025 C VAL C 167 1440 1376 1371 6 3 -1 C ATOM 5026 O VAL C 167 -11.127 25.585 41.413 1.00 11.46 O ANISOU 5026 O VAL C 167 1388 1447 1520 6 -30 9 O ATOM 5027 CB VAL C 167 -13.927 23.951 41.958 1.00 13.30 C ANISOU 5027 CB VAL C 167 1711 1639 1705 -98 -47 -64 C ATOM 5028 CG1 VAL C 167 -13.434 23.617 40.558 1.00 15.35 C ANISOU 5028 CG1 VAL C 167 1985 2010 1838 -20 44 -44 C ATOM 5029 CG2 VAL C 167 -14.294 22.675 42.708 1.00 14.33 C ANISOU 5029 CG2 VAL C 167 1897 1702 1848 -39 -9 -2 C ATOM 5030 N GLU C 168 -12.848 26.986 41.805 1.00 10.92 N ANISOU 5030 N GLU C 168 1419 1410 1319 21 -36 11 N ATOM 5031 CA GLU C 168 -12.235 28.062 41.026 1.00 10.99 C ANISOU 5031 CA GLU C 168 1425 1427 1324 -25 -29 -4 C ATOM 5032 C GLU C 168 -10.920 28.531 41.629 1.00 10.65 C ANISOU 5032 C GLU C 168 1384 1349 1315 0 7 -17 C ATOM 5033 O GLU C 168 -9.915 28.714 40.943 1.00 10.41 O ANISOU 5033 O GLU C 168 1367 1309 1280 38 -14 -16 O ATOM 5034 CB GLU C 168 -13.212 29.234 40.884 1.00 13.06 C ANISOU 5034 CB GLU C 168 1694 1550 1718 88 0 30 C ATOM 5035 CG GLU C 168 -14.474 28.834 40.128 1.00 15.11 C ANISOU 5035 CG GLU C 168 1938 1982 1820 -97 -76 1 C ATOM 5036 CD GLU C 168 -15.592 29.850 40.243 1.00 19.01 C ANISOU 5036 CD GLU C 168 2367 2346 2510 127 9 14 C ATOM 5037 OE1 GLU C 168 -15.569 30.680 41.177 1.00 20.63 O ANISOU 5037 OE1 GLU C 168 2707 2510 2620 28 -44 -46 O ATOM 5038 OE2 GLU C 168 -16.511 29.807 39.396 1.00 20.22 O ANISOU 5038 OE2 GLU C 168 2556 2556 2572 25 -69 13 O ATOM 5039 N PHE C 169 -10.927 28.745 42.943 1.00 10.42 N ANISOU 5039 N PHE C 169 1368 1313 1279 -4 -11 21 N ATOM 5040 CA PHE C 169 -9.735 29.120 43.692 1.00 10.46 C ANISOU 5040 CA PHE C 169 1351 1330 1292 -10 13 -1 C ATOM 5041 C PHE C 169 -8.625 28.088 43.567 1.00 10.67 C ANISOU 5041 C PHE C 169 1374 1345 1337 -2 6 -2 C ATOM 5042 O PHE C 169 -7.462 28.433 43.322 1.00 10.53 O ANISOU 5042 O PHE C 169 1406 1300 1295 -30 20 8 O ATOM 5043 CB PHE C 169 -10.126 29.354 45.157 1.00 10.30 C ANISOU 5043 CB PHE C 169 1310 1326 1277 14 -16 -21 C ATOM 5044 CG PHE C 169 -8.958 29.598 46.073 1.00 10.56 C ANISOU 5044 CG PHE C 169 1339 1334 1338 18 -44 -20 C ATOM 5045 CD1 PHE C 169 -8.278 30.802 46.054 1.00 10.90 C ANISOU 5045 CD1 PHE C 169 1370 1386 1387 -16 28 -6 C ATOM 5046 CD2 PHE C 169 -8.550 28.606 46.951 1.00 10.96 C ANISOU 5046 CD2 PHE C 169 1457 1376 1329 17 -10 13 C ATOM 5047 CE1 PHE C 169 -7.200 31.017 46.894 1.00 11.48 C ANISOU 5047 CE1 PHE C 169 1494 1427 1441 -2 -53 -45 C ATOM 5048 CE2 PHE C 169 -7.477 28.820 47.796 1.00 11.57 C ANISOU 5048 CE2 PHE C 169 1458 1453 1483 12 -47 23 C ATOM 5049 CZ PHE C 169 -6.803 30.023 47.767 1.00 12.05 C ANISOU 5049 CZ PHE C 169 1581 1466 1530 -12 -40 -2 C ATOM 5050 N LEU C 170 -8.955 26.805 43.710 1.00 10.56 N ANISOU 5050 N LEU C 170 1415 1347 1250 -9 4 18 N ATOM 5051 CA LEU C 170 -7.973 25.734 43.615 1.00 10.89 C ANISOU 5051 CA LEU C 170 1409 1372 1355 -12 -10 4 C ATOM 5052 C LEU C 170 -7.417 25.580 42.205 1.00 10.99 C ANISOU 5052 C LEU C 170 1419 1373 1384 -17 6 -12 C ATOM 5053 O LEU C 170 -6.218 25.368 42.015 1.00 10.67 O ANISOU 5053 O LEU C 170 1429 1309 1316 10 14 3 O ATOM 5054 CB LEU C 170 -8.561 24.406 44.102 1.00 10.81 C ANISOU 5054 CB LEU C 170 1362 1372 1375 -4 -5 5 C ATOM 5055 CG LEU C 170 -8.909 24.353 45.595 1.00 11.69 C ANISOU 5055 CG LEU C 170 1469 1550 1425 -22 19 19 C ATOM 5056 CD1 LEU C 170 -9.756 23.123 45.881 1.00 11.49 C ANISOU 5056 CD1 LEU C 170 1508 1477 1381 -2 20 -4 C ATOM 5057 CD2 LEU C 170 -7.648 24.358 46.444 1.00 12.19 C ANISOU 5057 CD2 LEU C 170 1494 1653 1484 -11 5 15 C ATOM 5058 N GLU C 171 -8.286 25.718 41.204 1.00 11.53 N ANISOU 5058 N GLU C 171 1549 1418 1415 -33 -43 6 N ATOM 5059 CA GLU C 171 -7.819 25.741 39.819 1.00 11.98 C ANISOU 5059 CA GLU C 171 1544 1529 1478 -19 16 5 C ATOM 5060 C GLU C 171 -6.823 26.868 39.587 1.00 11.65 C ANISOU 5060 C GLU C 171 1505 1459 1463 25 -3 4 C ATOM 5061 O GLU C 171 -5.776 26.655 38.968 1.00 11.51 O ANISOU 5061 O GLU C 171 1500 1421 1452 16 2 -3 O ATOM 5062 CB GLU C 171 -9.016 25.842 38.876 1.00 12.97 C ANISOU 5062 CB GLU C 171 1576 1694 1660 37 -44 9 C ATOM 5063 CG GLU C 171 -8.631 26.066 37.419 1.00 14.86 C ANISOU 5063 CG GLU C 171 2004 1878 1766 -28 40 26 C ATOM 5064 CD GLU C 171 -9.871 26.233 36.557 1.00 17.02 C ANISOU 5064 CD GLU C 171 2092 2226 2147 -34 -61 57 C ATOM 5065 OE1 GLU C 171 -10.737 27.044 36.938 1.00 18.65 O ANISOU 5065 OE1 GLU C 171 2411 2322 2353 48 -16 -50 O ATOM 5066 OE2 GLU C 171 -9.971 25.548 35.524 1.00 18.80 O ANISOU 5066 OE2 GLU C 171 2509 2360 2275 -37 3 -24 O ATOM 5067 N SER C 172 -7.115 28.076 40.072 1.00 11.55 N ANISOU 5067 N SER C 172 1505 1479 1406 7 -39 -32 N ATOM 5068 CA SER C 172 -6.165 29.178 39.981 1.00 11.76 C ANISOU 5068 CA SER C 172 1496 1502 1470 13 -29 11 C ATOM 5069 C SER C 172 -4.838 28.819 40.637 1.00 11.49 C ANISOU 5069 C SER C 172 1470 1459 1438 -4 -17 -9 C ATOM 5070 O SER C 172 -3.782 29.012 40.038 1.00 11.60 O ANISOU 5070 O SER C 172 1482 1495 1433 24 -3 -18 O ATOM 5071 CB SER C 172 -6.738 30.452 40.602 1.00 12.83 C ANISOU 5071 CB SER C 172 1663 1606 1606 11 24 -88 C ATOM 5072 OG SER C 172 -7.847 30.905 39.847 1.00 13.92 O ANISOU 5072 OG SER C 172 1803 1704 1783 66 -16 38 O ATOM 5073 N LEU C 173 -4.885 28.272 41.848 1.00 11.26 N ANISOU 5073 N LEU C 173 1455 1385 1437 18 -2 -22 N ATOM 5074 CA LEU C 173 -3.669 27.812 42.515 1.00 11.34 C ANISOU 5074 CA LEU C 173 1479 1414 1415 -5 -42 -17 C ATOM 5075 C LEU C 173 -2.906 26.796 41.680 1.00 11.63 C ANISOU 5075 C LEU C 173 1493 1474 1451 -1 1 1 C ATOM 5076 O LEU C 173 -1.690 26.897 41.495 1.00 11.88 O ANISOU 5076 O LEU C 173 1507 1537 1470 7 -2 -18 O ATOM 5077 CB LEU C 173 -4.025 27.234 43.886 1.00 12.34 C ANISOU 5077 CB LEU C 173 1665 1535 1490 -9 6 17 C ATOM 5078 CG LEU C 173 -2.863 26.672 44.710 1.00 13.04 C ANISOU 5078 CG LEU C 173 1595 1695 1664 -4 7 20 C ATOM 5079 CD1 LEU C 173 -1.803 27.731 44.964 1.00 11.93 C ANISOU 5079 CD1 LEU C 173 1584 1465 1483 82 30 -41 C ATOM 5080 CD2 LEU C 173 -3.390 26.095 46.019 1.00 13.18 C ANISOU 5080 CD2 LEU C 173 1713 1672 1622 6 11 -7 C ATOM 5081 N TYR C 174 -3.614 25.815 41.127 1.00 11.84 N ANISOU 5081 N TYR C 174 1565 1507 1425 -33 -2 -2 N ATOM 5082 CA TYR C 174 -3.023 24.801 40.263 1.00 12.45 C ANISOU 5082 CA TYR C 174 1610 1569 1552 22 21 -12 C ATOM 5083 C TYR C 174 -2.265 25.433 39.103 1.00 12.64 C ANISOU 5083 C TYR C 174 1636 1628 1537 4 8 -18 C ATOM 5084 O TYR C 174 -1.122 25.084 38.815 1.00 12.38 O ANISOU 5084 O TYR C 174 1609 1651 1446 -35 -5 -30 O ATOM 5085 CB TYR C 174 -4.128 23.875 39.751 1.00 13.42 C ANISOU 5085 CB TYR C 174 1702 1707 1689 -43 -12 -10 C ATOM 5086 CG TYR C 174 -3.659 22.759 38.845 1.00 14.60 C ANISOU 5086 CG TYR C 174 1881 1797 1868 -5 16 -57 C ATOM 5087 CD1 TYR C 174 -3.069 21.617 39.363 1.00 15.19 C ANISOU 5087 CD1 TYR C 174 1943 1903 1924 20 -18 6 C ATOM 5088 CD2 TYR C 174 -3.817 22.852 37.469 1.00 15.69 C ANISOU 5088 CD2 TYR C 174 2049 1976 1936 -8 -9 -9 C ATOM 5089 CE1 TYR C 174 -2.643 20.594 38.535 1.00 15.94 C ANISOU 5089 CE1 TYR C 174 2049 1971 2036 34 -1 -29 C ATOM 5090 CE2 TYR C 174 -3.392 21.834 36.630 1.00 16.31 C ANISOU 5090 CE2 TYR C 174 2129 2051 2018 32 11 -32 C ATOM 5091 CZ TYR C 174 -2.813 20.707 37.172 1.00 16.61 C ANISOU 5091 CZ TYR C 174 2157 2082 2073 23 -6 -2 C ATOM 5092 OH TYR C 174 -2.380 19.691 36.348 1.00 17.17 O ANISOU 5092 OH TYR C 174 2224 2173 2126 -8 -10 -74 O ATOM 5093 N LEU C 175 -2.886 26.408 38.446 1.00 13.23 N ANISOU 5093 N LEU C 175 1745 1648 1633 -4 -33 2 N ATOM 5094 CA LEU C 175 -2.312 27.079 37.288 1.00 13.68 C ANISOU 5094 CA LEU C 175 1764 1765 1668 -18 -3 21 C ATOM 5095 C LEU C 175 -1.349 28.204 37.614 1.00 14.32 C ANISOU 5095 C LEU C 175 1884 1749 1807 -27 22 -5 C ATOM 5096 O LEU C 175 -0.765 28.845 36.731 1.00 14.65 O ANISOU 5096 O LEU C 175 1978 1767 1822 -37 41 20 O ATOM 5097 CB LEU C 175 -3.473 27.621 36.433 1.00 13.49 C ANISOU 5097 CB LEU C 175 1753 1697 1675 65 55 12 C ATOM 5098 CG LEU C 175 -4.411 26.545 35.875 1.00 14.96 C ANISOU 5098 CG LEU C 175 1916 1853 1914 -24 7 -21 C ATOM 5099 CD1 LEU C 175 -5.614 27.182 35.195 1.00 16.07 C ANISOU 5099 CD1 LEU C 175 2023 2071 2011 27 -40 14 C ATOM 5100 CD2 LEU C 175 -3.666 25.633 34.910 1.00 14.81 C ANISOU 5100 CD2 LEU C 175 1921 1866 1838 10 -21 -1 C ATOM 5101 N ASN C 176 -1.136 28.486 38.890 1.00 14.48 N ANISOU 5101 N ASN C 176 1922 1772 1806 5 4 20 N ATOM 5102 CA ASN C 176 -0.279 29.548 39.383 1.00 15.11 C ANISOU 5102 CA ASN C 176 1964 1885 1891 -36 -30 -2 C ATOM 5103 C ASN C 176 -0.822 30.929 39.027 1.00 15.37 C ANISOU 5103 C ASN C 176 1987 1917 1937 -1 6 2 C ATOM 5104 O ASN C 176 -0.056 31.887 38.889 1.00 15.74 O ANISOU 5104 O ASN C 176 1976 1983 2022 -32 3 -9 O ATOM 5105 CB ASN C 176 1.158 29.404 38.877 1.00 16.31 C ANISOU 5105 CB ASN C 176 2031 2095 2069 -22 16 -55 C ATOM 5106 CG ASN C 176 1.785 28.074 39.251 1.00 18.06 C ANISOU 5106 CG ASN C 176 2327 2220 2316 30 -19 26 C ATOM 5107 OD1 ASN C 176 1.938 27.753 40.425 1.00 17.61 O ANISOU 5107 OD1 ASN C 176 2237 2178 2275 9 -26 -25 O ATOM 5108 ND2 ASN C 176 2.110 27.296 38.223 1.00 18.61 N ANISOU 5108 ND2 ASN C 176 2379 2373 2320 33 22 -3 N ATOM 5109 N LYS C 177 -2.141 31.061 38.976 1.00 15.46 N ANISOU 5109 N LYS C 177 1988 1966 1922 -19 1 4 N ATOM 5110 CA LYS C 177 -2.791 32.271 38.512 1.00 16.19 C ANISOU 5110 CA LYS C 177 2094 2004 2055 33 31 4 C ATOM 5111 C LYS C 177 -3.292 33.137 39.661 1.00 16.07 C ANISOU 5111 C LYS C 177 2090 2010 2007 9 6 3 C ATOM 5112 O LYS C 177 -3.839 34.210 39.402 1.00 16.44 O ANISOU 5112 O LYS C 177 2144 2068 2036 51 -9 24 O ATOM 5113 CB LYS C 177 -3.972 31.936 37.589 1.00 18.15 C ANISOU 5113 CB LYS C 177 2231 2260 2406 -41 -119 37 C ATOM 5114 CG LYS C 177 -3.544 31.445 36.215 1.00 22.42 C ANISOU 5114 CG LYS C 177 2978 2788 2751 15 143 -44 C ATOM 5115 CD LYS C 177 -4.749 31.258 35.304 1.00 26.72 C ANISOU 5115 CD LYS C 177 3281 3410 3460 -42 -126 21 C ATOM 5116 CE LYS C 177 -4.312 30.808 33.918 1.00 30.24 C ANISOU 5116 CE LYS C 177 3900 3841 3750 27 73 -39 C ATOM 5117 NZ LYS C 177 -5.479 30.553 33.028 1.00 31.61 N ANISOU 5117 NZ LYS C 177 3999 4016 3994 5 -24 -3 N ATOM 5118 N LEU C 178 -3.145 32.672 40.899 1.00 15.74 N ANISOU 5118 N LEU C 178 2033 1966 1982 11 8 -1 N ATOM 5119 CA LEU C 178 -3.461 33.542 42.032 1.00 15.60 C ANISOU 5119 CA LEU C 178 2047 1933 1948 4 -2 33 C ATOM 5120 C LEU C 178 -2.536 34.753 42.020 1.00 15.71 C ANISOU 5120 C LEU C 178 2011 1975 1984 -2 10 24 C ATOM 5121 O LEU C 178 -1.409 34.702 41.519 1.00 14.93 O ANISOU 5121 O LEU C 178 2006 1780 1887 25 18 -4 O ATOM 5122 CB LEU C 178 -3.337 32.812 43.365 1.00 14.68 C ANISOU 5122 CB LEU C 178 1847 1848 1882 -42 -1 -3 C ATOM 5123 CG LEU C 178 -4.333 31.680 43.621 1.00 13.51 C ANISOU 5123 CG LEU C 178 1692 1743 1699 42 -23 19 C ATOM 5124 CD1 LEU C 178 -4.026 31.007 44.954 1.00 13.47 C ANISOU 5124 CD1 LEU C 178 1794 1672 1652 2 7 9 C ATOM 5125 CD2 LEU C 178 -5.765 32.184 43.601 1.00 11.49 C ANISOU 5125 CD2 LEU C 178 1614 1319 1433 -5 -12 -9 C ATOM 5126 N SER C 179 -2.991 35.839 42.634 1.00 16.26 N ANISOU 5126 N SER C 179 2125 2035 2019 35 -2 3 N ATOM 5127 CA SER C 179 -2.198 37.053 42.771 1.00 17.14 C ANISOU 5127 CA SER C 179 2180 2168 2163 -42 -20 -8 C ATOM 5128 C SER C 179 -1.184 36.903 43.900 1.00 17.07 C ANISOU 5128 C SER C 179 2162 2160 2163 25 -4 9 C ATOM 5129 O SER C 179 -1.290 37.443 44.997 1.00 17.56 O ANISOU 5129 O SER C 179 2293 2150 2228 25 39 -22 O ATOM 5130 CB ASER C 179 -3.107 38.257 43.020 0.50 17.97 C ANISOU 5130 CB ASER C 179 2285 2239 2302 -5 -12 -8 C ATOM 5131 CB BSER C 179 -3.111 38.257 43.006 0.50 18.92 C ANISOU 5131 CB BSER C 179 2396 2355 2439 80 1 -25 C ATOM 5132 OG ASER C 179 -3.930 38.522 41.900 0.50 17.94 O ANISOU 5132 OG ASER C 179 2306 2201 2310 -3 -26 -4 O ATOM 5133 OG BSER C 179 -2.385 39.471 42.929 0.50 20.33 O ANISOU 5133 OG BSER C 179 2613 2497 2614 -23 3 23 O ATOM 5134 N ALA C 180 -0.144 36.139 43.613 1.00 16.25 N ANISOU 5134 N ALA C 180 2126 2047 2000 0 -16 -18 N ATOM 5135 CA ALA C 180 0.886 35.716 44.539 1.00 15.71 C ANISOU 5135 CA ALA C 180 2037 1936 1997 0 16 -5 C ATOM 5136 C ALA C 180 2.039 35.149 43.709 1.00 15.27 C ANISOU 5136 C ALA C 180 1982 1859 1961 -18 -12 14 C ATOM 5137 O ALA C 180 1.785 34.729 42.578 1.00 15.68 O ANISOU 5137 O ALA C 180 2080 1899 1980 -11 13 -9 O ATOM 5138 CB ALA C 180 0.354 34.671 45.506 1.00 15.60 C ANISOU 5138 CB ALA C 180 1990 1960 1978 -25 28 -28 C ATOM 5139 N SER C 181 3.253 35.156 44.238 1.00 14.86 N ANISOU 5139 N SER C 181 1920 1780 1945 7 32 18 N ATOM 5140 CA SER C 181 4.386 34.653 43.465 1.00 14.73 C ANISOU 5140 CA SER C 181 1893 1812 1894 -5 10 19 C ATOM 5141 C SER C 181 4.122 33.195 43.097 1.00 14.68 C ANISOU 5141 C SER C 181 1875 1831 1873 -8 12 -8 C ATOM 5142 O SER C 181 3.485 32.477 43.870 1.00 14.56 O ANISOU 5142 O SER C 181 1889 1747 1895 -5 -4 2 O ATOM 5143 CB SER C 181 5.694 34.777 44.234 1.00 14.93 C ANISOU 5143 CB SER C 181 1925 1878 1869 15 -10 13 C ATOM 5144 OG SER C 181 5.762 33.903 45.348 1.00 14.39 O ANISOU 5144 OG SER C 181 1944 1648 1874 14 49 -40 O ATOM 5145 N LYS C 182 4.640 32.774 41.948 1.00 14.79 N ANISOU 5145 N LYS C 182 1885 1841 1892 -26 6 -49 N ATOM 5146 CA LYS C 182 4.577 31.356 41.589 1.00 15.10 C ANISOU 5146 CA LYS C 182 1959 1822 1956 21 2 12 C ATOM 5147 C LYS C 182 5.294 30.515 42.640 1.00 14.75 C ANISOU 5147 C LYS C 182 1890 1848 1865 4 15 -13 C ATOM 5148 O LYS C 182 4.803 29.460 43.030 1.00 15.11 O ANISOU 5148 O LYS C 182 1988 1825 1927 9 18 -10 O ATOM 5149 CB LYS C 182 5.184 31.100 40.210 1.00 16.38 C ANISOU 5149 CB LYS C 182 2116 2102 2004 -2 23 -4 C ATOM 5150 CG LYS C 182 5.211 29.621 39.843 1.00 18.32 C ANISOU 5150 CG LYS C 182 2406 2179 2375 22 -7 -11 C ATOM 5151 CD LYS C 182 5.309 29.429 38.340 1.00 20.69 C ANISOU 5151 CD LYS C 182 2712 2640 2510 1 25 -10 C ATOM 5152 CE LYS C 182 5.378 27.952 37.981 1.00 21.48 C ANISOU 5152 CE LYS C 182 2770 2672 2719 -2 23 4 C ATOM 5153 NZ LYS C 182 5.150 27.765 36.521 1.00 21.83 N ANISOU 5153 NZ LYS C 182 2750 2802 2744 -9 -5 -22 N ATOM 5154 N GLU C 183 6.462 30.968 43.078 1.00 14.52 N ANISOU 5154 N GLU C 183 1914 1786 1816 13 6 -26 N ATOM 5155 CA GLU C 183 7.197 30.360 44.172 1.00 14.91 C ANISOU 5155 CA GLU C 183 1990 1869 1807 77 50 11 C ATOM 5156 C GLU C 183 6.331 30.026 45.376 1.00 13.84 C ANISOU 5156 C GLU C 183 1819 1697 1741 37 -20 -20 C ATOM 5157 O GLU C 183 6.343 28.886 45.849 1.00 13.25 O ANISOU 5157 O GLU C 183 1751 1644 1640 1 -48 -53 O ATOM 5158 CB GLU C 183 8.329 31.308 44.585 1.00 19.40 C ANISOU 5158 CB GLU C 183 2401 2373 2599 -224 62 -95 C ATOM 5159 CG GLU C 183 9.276 30.762 45.640 1.00 25.28 C ANISOU 5159 CG GLU C 183 3246 3286 3073 176 -89 106 C ATOM 5160 CD GLU C 183 10.408 31.738 45.916 1.00 30.74 C ANISOU 5160 CD GLU C 183 3771 3815 4094 -110 5 -32 C ATOM 5161 OE1 GLU C 183 10.908 32.351 44.950 1.00 31.32 O ANISOU 5161 OE1 GLU C 183 3950 3903 4049 -23 -18 11 O ATOM 5162 OE2 GLU C 183 10.801 31.887 47.091 1.00 34.26 O ANISOU 5162 OE2 GLU C 183 4347 4398 4274 -39 -55 -14 O ATOM 5163 N ASN C 184 5.593 31.004 45.908 1.00 13.23 N ANISOU 5163 N ASN C 184 1690 1680 1657 4 -9 6 N ATOM 5164 CA ASN C 184 4.737 30.753 47.063 1.00 12.92 C ANISOU 5164 CA ASN C 184 1640 1617 1650 -2 -12 -10 C ATOM 5165 C ASN C 184 3.563 29.839 46.759 1.00 12.52 C ANISOU 5165 C ASN C 184 1630 1574 1551 -1 10 -14 C ATOM 5166 O ASN C 184 3.188 29.020 47.605 1.00 12.73 O ANISOU 5166 O ASN C 184 1733 1570 1534 -1 -3 -13 O ATOM 5167 CB ASN C 184 4.254 32.082 47.660 1.00 13.00 C ANISOU 5167 CB ASN C 184 1681 1618 1638 -26 -29 -37 C ATOM 5168 CG ASN C 184 5.400 32.786 48.366 1.00 12.37 C ANISOU 5168 CG ASN C 184 1586 1611 1505 -3 21 -12 C ATOM 5169 OD1 ASN C 184 6.347 32.135 48.802 1.00 12.32 O ANISOU 5169 OD1 ASN C 184 1686 1395 1600 -34 -32 -56 O ATOM 5170 ND2 ASN C 184 5.301 34.104 48.482 1.00 13.81 N ANISOU 5170 ND2 ASN C 184 1887 1667 1692 -33 6 -2 N ATOM 5171 N GLN C 185 2.974 29.930 45.569 1.00 12.28 N ANISOU 5171 N GLN C 185 1582 1516 1568 -19 5 26 N ATOM 5172 CA GLN C 185 1.939 28.974 45.177 1.00 12.27 C ANISOU 5172 CA GLN C 185 1592 1538 1533 -1 -17 -26 C ATOM 5173 C GLN C 185 2.479 27.553 45.108 1.00 11.77 C ANISOU 5173 C GLN C 185 1515 1506 1452 -14 -28 4 C ATOM 5174 O GLN C 185 1.824 26.614 45.572 1.00 11.80 O ANISOU 5174 O GLN C 185 1520 1488 1476 14 -20 10 O ATOM 5175 CB GLN C 185 1.310 29.419 43.850 1.00 12.65 C ANISOU 5175 CB GLN C 185 1657 1589 1558 -20 -19 12 C ATOM 5176 CG GLN C 185 0.646 30.789 43.991 1.00 13.78 C ANISOU 5176 CG GLN C 185 1746 1703 1786 53 15 45 C ATOM 5177 CD GLN C 185 0.071 31.269 42.673 1.00 14.35 C ANISOU 5177 CD GLN C 185 1735 1882 1834 -22 -106 -27 C ATOM 5178 OE1 GLN C 185 0.649 32.148 42.026 1.00 16.77 O ANISOU 5178 OE1 GLN C 185 2231 2064 2076 -74 60 60 O ATOM 5179 NE2 GLN C 185 -1.057 30.681 42.306 1.00 10.79 N ANISOU 5179 NE2 GLN C 185 1536 1287 1277 86 12 76 N ATOM 5180 N LEU C 186 3.670 27.364 44.548 1.00 11.87 N ANISOU 5180 N LEU C 186 1535 1511 1464 9 -31 -36 N ATOM 5181 CA LEU C 186 4.326 26.064 44.521 1.00 12.24 C ANISOU 5181 CA LEU C 186 1600 1505 1547 1 -19 -1 C ATOM 5182 C LEU C 186 4.655 25.536 45.911 1.00 12.52 C ANISOU 5182 C LEU C 186 1635 1561 1563 -10 -44 2 C ATOM 5183 O LEU C 186 4.447 24.351 46.174 1.00 12.50 O ANISOU 5183 O LEU C 186 1633 1546 1572 -16 -61 -28 O ATOM 5184 CB LEU C 186 5.605 26.107 43.676 1.00 12.93 C ANISOU 5184 CB LEU C 186 1689 1595 1630 -9 40 -29 C ATOM 5185 CG LEU C 186 5.401 26.359 42.179 1.00 13.32 C ANISOU 5185 CG LEU C 186 1720 1663 1679 2 -31 17 C ATOM 5186 CD1 LEU C 186 6.729 26.657 41.502 1.00 13.83 C ANISOU 5186 CD1 LEU C 186 1785 1725 1743 -31 12 -17 C ATOM 5187 CD2 LEU C 186 4.731 25.151 41.534 1.00 13.89 C ANISOU 5187 CD2 LEU C 186 1878 1702 1699 3 -32 -31 C ATOM 5188 N ILE C 187 5.140 26.396 46.806 1.00 12.63 N ANISOU 5188 N ILE C 187 1649 1564 1586 -30 -32 -3 N ATOM 5189 CA ILE C 187 5.412 25.981 48.182 1.00 12.54 C ANISOU 5189 CA ILE C 187 1631 1573 1561 -12 -7 -9 C ATOM 5190 C ILE C 187 4.167 25.417 48.846 1.00 12.35 C ANISOU 5190 C ILE C 187 1611 1544 1535 4 -19 -26 C ATOM 5191 O ILE C 187 4.175 24.323 49.423 1.00 12.80 O ANISOU 5191 O ILE C 187 1707 1547 1608 20 -41 -21 O ATOM 5192 CB ILE C 187 5.986 27.152 48.998 1.00 13.01 C ANISOU 5192 CB ILE C 187 1694 1595 1655 -45 12 -34 C ATOM 5193 CG1 ILE C 187 7.430 27.447 48.573 1.00 13.22 C ANISOU 5193 CG1 ILE C 187 1687 1690 1644 -13 15 -29 C ATOM 5194 CG2 ILE C 187 5.919 26.896 50.498 1.00 14.71 C ANISOU 5194 CG2 ILE C 187 1985 1861 1742 -32 -22 23 C ATOM 5195 CD1 ILE C 187 7.939 28.786 49.078 1.00 13.95 C ANISOU 5195 CD1 ILE C 187 1810 1746 1744 -31 -41 -55 C ATOM 5196 N VAL C 188 3.059 26.152 48.772 1.00 12.23 N ANISOU 5196 N VAL C 188 1596 1547 1504 -2 -3 -12 N ATOM 5197 CA VAL C 188 1.810 25.739 49.400 1.00 12.42 C ANISOU 5197 CA VAL C 188 1628 1558 1534 -46 -7 -8 C ATOM 5198 C VAL C 188 1.265 24.493 48.716 1.00 12.20 C ANISOU 5198 C VAL C 188 1610 1547 1479 -30 -8 -9 C ATOM 5199 O VAL C 188 0.756 23.603 49.395 1.00 12.01 O ANISOU 5199 O VAL C 188 1637 1549 1378 -60 -18 -54 O ATOM 5200 CB VAL C 188 0.763 26.860 49.433 1.00 13.73 C ANISOU 5200 CB VAL C 188 1712 1724 1780 38 28 26 C ATOM 5201 CG1 VAL C 188 -0.570 26.394 49.993 1.00 12.94 C ANISOU 5201 CG1 VAL C 188 1685 1586 1644 22 13 -58 C ATOM 5202 CG2 VAL C 188 1.276 28.031 50.274 1.00 15.75 C ANISOU 5202 CG2 VAL C 188 2050 1941 1995 -49 -46 -65 C ATOM 5203 N LYS C 189 1.415 24.400 47.392 1.00 11.92 N ANISOU 5203 N LYS C 189 1586 1474 1469 -33 -3 7 N ATOM 5204 CA LYS C 189 1.002 23.179 46.707 1.00 12.07 C ANISOU 5204 CA LYS C 189 1627 1472 1488 -6 -19 -2 C ATOM 5205 C LYS C 189 1.751 21.954 47.199 1.00 11.98 C ANISOU 5205 C LYS C 189 1558 1513 1481 8 -5 2 C ATOM 5206 O LYS C 189 1.079 20.955 47.496 1.00 12.21 O ANISOU 5206 O LYS C 189 1624 1512 1503 -10 -7 -1 O ATOM 5207 CB LYS C 189 1.084 23.343 45.188 1.00 12.07 C ANISOU 5207 CB LYS C 189 1571 1530 1484 35 11 -7 C ATOM 5208 CG LYS C 189 -0.151 24.072 44.661 1.00 12.49 C ANISOU 5208 CG LYS C 189 1569 1547 1628 24 -16 -11 C ATOM 5209 CD LYS C 189 -0.154 24.206 43.153 1.00 13.98 C ANISOU 5209 CD LYS C 189 1830 1785 1699 22 12 -15 C ATOM 5210 CE LYS C 189 0.821 25.261 42.665 1.00 15.22 C ANISOU 5210 CE LYS C 189 1879 1925 1977 -30 21 24 C ATOM 5211 NZ LYS C 189 0.748 25.428 41.186 1.00 17.04 N ANISOU 5211 NZ LYS C 189 2283 2130 2060 -8 -22 5 N ATOM 5212 N GLU C 190 3.072 21.980 47.381 1.00 12.25 N ANISOU 5212 N GLU C 190 1590 1544 1518 14 -33 2 N ATOM 5213 CA GLU C 190 3.724 20.757 47.853 1.00 12.46 C ANISOU 5213 CA GLU C 190 1660 1538 1538 30 -22 -7 C ATOM 5214 C GLU C 190 3.280 20.410 49.267 1.00 12.36 C ANISOU 5214 C GLU C 190 1634 1522 1540 -2 -25 -18 C ATOM 5215 O GLU C 190 3.134 19.229 49.595 1.00 12.53 O ANISOU 5215 O GLU C 190 1682 1566 1514 -32 -60 22 O ATOM 5216 CB GLU C 190 5.247 20.789 47.754 1.00 14.67 C ANISOU 5216 CB GLU C 190 1752 1959 1861 -41 -36 5 C ATOM 5217 CG GLU C 190 5.794 19.373 47.964 1.00 17.55 C ANISOU 5217 CG GLU C 190 2376 2072 2219 43 -3 -14 C ATOM 5218 CD GLU C 190 7.301 19.303 47.977 1.00 21.08 C ANISOU 5218 CD GLU C 190 2563 2671 2775 -3 15 13 C ATOM 5219 OE1 GLU C 190 7.900 19.603 49.033 1.00 22.95 O ANISOU 5219 OE1 GLU C 190 2926 2976 2818 28 -38 -17 O ATOM 5220 OE2 GLU C 190 7.875 18.947 46.927 1.00 21.83 O ANISOU 5220 OE2 GLU C 190 2714 2820 2761 23 -21 -35 O ATOM 5221 N ALA C 191 2.991 21.408 50.107 1.00 11.91 N ANISOU 5221 N ALA C 191 1521 1524 1481 13 -1 -3 N ATOM 5222 CA ALA C 191 2.430 21.161 51.426 1.00 11.94 C ANISOU 5222 CA ALA C 191 1557 1498 1483 -14 3 -21 C ATOM 5223 C ALA C 191 1.053 20.520 51.413 1.00 11.82 C ANISOU 5223 C ALA C 191 1536 1510 1444 -5 -34 -15 C ATOM 5224 O ALA C 191 0.651 19.961 52.439 1.00 12.46 O ANISOU 5224 O ALA C 191 1671 1515 1549 -30 -5 42 O ATOM 5225 CB ALA C 191 2.393 22.455 52.236 1.00 12.06 C ANISOU 5225 CB ALA C 191 1595 1493 1493 6 -35 -31 C ATOM 5226 N LEU C 192 0.307 20.573 50.317 1.00 11.32 N ANISOU 5226 N LEU C 192 1465 1401 1434 -2 -26 -34 N ATOM 5227 CA LEU C 192 -0.999 19.960 50.199 1.00 10.68 C ANISOU 5227 CA LEU C 192 1395 1334 1329 45 -4 -5 C ATOM 5228 C LEU C 192 -0.976 18.566 49.584 1.00 10.60 C ANISOU 5228 C LEU C 192 1377 1346 1305 5 -11 -7 C ATOM 5229 O LEU C 192 -2.029 17.932 49.454 1.00 10.33 O ANISOU 5229 O LEU C 192 1360 1367 1198 0 -25 -3 O ATOM 5230 CB LEU C 192 -1.898 20.875 49.349 1.00 10.73 C ANISOU 5230 CB LEU C 192 1451 1252 1374 18 -62 -23 C ATOM 5231 CG LEU C 192 -2.212 22.243 49.965 1.00 10.61 C ANISOU 5231 CG LEU C 192 1350 1272 1410 18 -27 -53 C ATOM 5232 CD1 LEU C 192 -2.900 23.146 48.950 1.00 11.79 C ANISOU 5232 CD1 LEU C 192 1599 1490 1389 19 -66 -2 C ATOM 5233 CD2 LEU C 192 -3.097 22.087 51.193 1.00 12.54 C ANISOU 5233 CD2 LEU C 192 1650 1645 1468 -3 17 8 C ATOM 5234 N VAL C 193 0.196 18.064 49.201 1.00 10.75 N ANISOU 5234 N VAL C 193 1405 1340 1339 38 1 -4 N ATOM 5235 CA VAL C 193 0.256 16.706 48.652 1.00 10.71 C ANISOU 5235 CA VAL C 193 1394 1312 1365 -9 -2 -7 C ATOM 5236 C VAL C 193 -0.135 15.700 49.732 1.00 10.71 C ANISOU 5236 C VAL C 193 1412 1299 1357 23 19 -15 C ATOM 5237 O VAL C 193 0.461 15.690 50.805 1.00 11.33 O ANISOU 5237 O VAL C 193 1556 1351 1397 -6 -18 29 O ATOM 5238 CB VAL C 193 1.628 16.344 48.073 1.00 10.84 C ANISOU 5238 CB VAL C 193 1385 1299 1436 -20 10 -4 C ATOM 5239 CG1 VAL C 193 1.690 14.869 47.682 1.00 11.09 C ANISOU 5239 CG1 VAL C 193 1458 1333 1423 -3 -14 -45 C ATOM 5240 CG2 VAL C 193 1.938 17.209 46.856 1.00 11.37 C ANISOU 5240 CG2 VAL C 193 1447 1472 1401 -8 -6 19 C ATOM 5241 N THR C 194 -1.108 14.843 49.434 1.00 11.03 N ANISOU 5241 N THR C 194 1389 1387 1414 1 12 6 N ATOM 5242 CA THR C 194 -1.590 13.883 50.421 1.00 11.57 C ANISOU 5242 CA THR C 194 1518 1414 1465 9 27 33 C ATOM 5243 C THR C 194 -1.525 12.446 49.921 1.00 12.31 C ANISOU 5243 C THR C 194 1660 1476 1540 17 15 -12 C ATOM 5244 O THR C 194 -1.607 11.506 50.721 1.00 12.61 O ANISOU 5244 O THR C 194 1780 1458 1554 6 35 -18 O ATOM 5245 CB THR C 194 -3.032 14.160 50.885 1.00 11.64 C ANISOU 5245 CB THR C 194 1466 1422 1533 -7 -28 15 C ATOM 5246 OG1 THR C 194 -3.907 14.194 49.747 1.00 12.92 O ANISOU 5246 OG1 THR C 194 1741 1699 1469 3 -56 -66 O ATOM 5247 CG2 THR C 194 -3.147 15.473 51.641 1.00 11.51 C ANISOU 5247 CG2 THR C 194 1507 1518 1349 14 -9 -12 C ATOM 5248 N GLU C 195 -1.436 12.249 48.616 1.00 12.61 N ANISOU 5248 N GLU C 195 1723 1534 1535 43 -9 21 N ATOM 5249 CA GLU C 195 -1.266 10.906 48.055 1.00 13.40 C ANISOU 5249 CA GLU C 195 1865 1622 1606 100 49 -15 C ATOM 5250 C GLU C 195 -0.327 11.000 46.858 1.00 12.61 C ANISOU 5250 C GLU C 195 1729 1527 1535 16 -35 -34 C ATOM 5251 O GLU C 195 -0.425 11.954 46.089 1.00 12.46 O ANISOU 5251 O GLU C 195 1730 1524 1481 -26 -35 -43 O ATOM 5252 CB GLU C 195 -2.599 10.279 47.658 1.00 19.61 C ANISOU 5252 CB GLU C 195 2283 2463 2705 -67 -225 -180 C ATOM 5253 CG GLU C 195 -3.300 9.537 48.785 1.00 27.47 C ANISOU 5253 CG GLU C 195 3702 3439 3295 -23 210 120 C ATOM 5254 CD GLU C 195 -4.715 9.126 48.435 1.00 34.31 C ANISOU 5254 CD GLU C 195 4154 4494 4390 -77 -35 -75 C ATOM 5255 OE1 GLU C 195 -5.453 9.959 47.871 1.00 35.94 O ANISOU 5255 OE1 GLU C 195 4540 4552 4565 12 -24 36 O ATOM 5256 OE2 GLU C 195 -5.090 7.973 48.730 1.00 36.67 O ANISOU 5256 OE2 GLU C 195 4664 4621 4649 -46 11 24 O ATOM 5257 N ALA C 196 0.579 10.039 46.728 1.00 12.66 N ANISOU 5257 N ALA C 196 1622 1622 1567 20 -47 12 N ATOM 5258 CA ALA C 196 1.559 10.084 45.651 1.00 13.05 C ANISOU 5258 CA ALA C 196 1669 1660 1630 18 -9 -6 C ATOM 5259 C ALA C 196 1.816 8.687 45.089 1.00 14.00 C ANISOU 5259 C ALA C 196 1869 1715 1735 42 -7 -41 C ATOM 5260 O ALA C 196 2.105 7.743 45.816 1.00 14.75 O ANISOU 5260 O ALA C 196 2019 1721 1866 91 -2 -25 O ATOM 5261 CB ALA C 196 2.854 10.714 46.131 1.00 12.69 C ANISOU 5261 CB ALA C 196 1665 1522 1636 14 20 -16 C ATOM 5262 N ALA C 197 1.627 8.577 43.789 1.00 13.61 N ANISOU 5262 N ALA C 197 1778 1675 1719 20 10 -54 N ATOM 5263 CA ALA C 197 1.993 7.403 43.008 1.00 12.86 C ANISOU 5263 CA ALA C 197 1674 1568 1646 -29 -2 13 C ATOM 5264 C ALA C 197 2.611 7.930 41.718 1.00 12.82 C ANISOU 5264 C ALA C 197 1628 1634 1609 -14 -5 -24 C ATOM 5265 O ALA C 197 2.512 9.124 41.437 1.00 13.00 O ANISOU 5265 O ALA C 197 1690 1660 1588 30 -55 -32 O ATOM 5266 CB ALA C 197 0.755 6.577 42.708 1.00 12.64 C ANISOU 5266 CB ALA C 197 1594 1598 1609 18 -25 2 C ATOM 5267 N PRO C 198 3.217 7.055 40.927 1.00 12.96 N ANISOU 5267 N PRO C 198 1630 1649 1647 -5 -1 -27 N ATOM 5268 CA PRO C 198 3.937 7.500 39.742 1.00 12.92 C ANISOU 5268 CA PRO C 198 1645 1633 1631 -10 -17 -24 C ATOM 5269 C PRO C 198 3.060 8.305 38.807 1.00 13.08 C ANISOU 5269 C PRO C 198 1673 1660 1638 1 -15 -15 C ATOM 5270 O PRO C 198 3.505 9.341 38.310 1.00 13.70 O ANISOU 5270 O PRO C 198 1827 1715 1663 -19 -30 19 O ATOM 5271 CB PRO C 198 4.457 6.201 39.146 1.00 13.11 C ANISOU 5271 CB PRO C 198 1675 1650 1656 19 5 -14 C ATOM 5272 CG PRO C 198 4.700 5.339 40.342 1.00 13.26 C ANISOU 5272 CG PRO C 198 1706 1694 1637 -1 -3 -13 C ATOM 5273 CD PRO C 198 3.622 5.687 41.337 1.00 13.28 C ANISOU 5273 CD PRO C 198 1672 1683 1690 15 -3 -10 C ATOM 5274 N GLU C 199 1.827 7.865 38.555 1.00 12.77 N ANISOU 5274 N GLU C 199 1651 1617 1583 4 -19 -23 N ATOM 5275 CA GLU C 199 0.916 8.610 37.692 1.00 13.26 C ANISOU 5275 CA GLU C 199 1667 1672 1700 26 -37 -13 C ATOM 5276 C GLU C 199 -0.381 8.962 38.408 1.00 13.41 C ANISOU 5276 C GLU C 199 1717 1711 1669 33 -14 -32 C ATOM 5277 O GLU C 199 -1.462 9.015 37.809 1.00 13.97 O ANISOU 5277 O GLU C 199 1781 1802 1723 43 -65 -59 O ATOM 5278 CB GLU C 199 0.583 7.804 36.438 1.00 14.09 C ANISOU 5278 CB GLU C 199 1883 1784 1687 -8 -51 -5 C ATOM 5279 CG GLU C 199 1.768 7.538 35.517 1.00 15.72 C ANISOU 5279 CG GLU C 199 1909 2016 2048 10 33 12 C ATOM 5280 CD GLU C 199 1.358 6.515 34.465 1.00 17.87 C ANISOU 5280 CD GLU C 199 2337 2219 2234 -8 -12 -91 C ATOM 5281 OE1 GLU C 199 0.749 6.935 33.468 1.00 18.49 O ANISOU 5281 OE1 GLU C 199 2503 2280 2242 -21 -59 -103 O ATOM 5282 OE2 GLU C 199 1.635 5.327 34.696 1.00 18.99 O ANISOU 5282 OE2 GLU C 199 2529 2271 2417 -3 -4 -53 O ATOM 5283 N TYR C 200 -0.281 9.214 39.709 1.00 12.88 N ANISOU 5283 N TYR C 200 1671 1588 1635 35 -28 9 N ATOM 5284 CA TYR C 200 -1.456 9.620 40.476 1.00 12.98 C ANISOU 5284 CA TYR C 200 1704 1624 1604 13 -25 -41 C ATOM 5285 C TYR C 200 -0.985 10.511 41.621 1.00 12.72 C ANISOU 5285 C TYR C 200 1707 1550 1577 48 -6 -41 C ATOM 5286 O TYR C 200 -0.197 10.060 42.443 1.00 13.45 O ANISOU 5286 O TYR C 200 1792 1688 1630 87 -81 -130 O ATOM 5287 CB TYR C 200 -2.210 8.405 40.990 1.00 13.67 C ANISOU 5287 CB TYR C 200 1804 1688 1702 -13 -31 13 C ATOM 5288 CG TYR C 200 -3.616 8.655 41.475 1.00 14.74 C ANISOU 5288 CG TYR C 200 1886 1821 1892 8 23 19 C ATOM 5289 CD1 TYR C 200 -3.866 8.988 42.799 1.00 15.13 C ANISOU 5289 CD1 TYR C 200 1984 1852 1912 4 21 22 C ATOM 5290 CD2 TYR C 200 -4.697 8.555 40.607 1.00 15.60 C ANISOU 5290 CD2 TYR C 200 1989 1975 1964 8 -36 -7 C ATOM 5291 CE1 TYR C 200 -5.155 9.208 43.245 1.00 15.69 C ANISOU 5291 CE1 TYR C 200 2031 1918 2012 11 40 2 C ATOM 5292 CE2 TYR C 200 -5.990 8.776 41.047 1.00 16.32 C ANISOU 5292 CE2 TYR C 200 2039 2106 2055 9 -15 36 C ATOM 5293 CZ TYR C 200 -6.210 9.108 42.367 1.00 16.35 C ANISOU 5293 CZ TYR C 200 2113 2017 2084 2 -10 12 C ATOM 5294 OH TYR C 200 -7.494 9.330 42.810 1.00 17.37 O ANISOU 5294 OH TYR C 200 2212 2111 2276 32 61 57 O ATOM 5295 N LEU C 201 -1.439 11.757 41.619 1.00 11.67 N ANISOU 5295 N LEU C 201 1610 1459 1367 -25 -12 -19 N ATOM 5296 CA LEU C 201 -0.991 12.686 42.656 1.00 10.83 C ANISOU 5296 CA LEU C 201 1427 1314 1373 -19 4 21 C ATOM 5297 C LEU C 201 -2.194 13.458 43.175 1.00 10.99 C ANISOU 5297 C LEU C 201 1442 1364 1369 2 2 -14 C ATOM 5298 O LEU C 201 -2.963 13.999 42.378 1.00 11.31 O ANISOU 5298 O LEU C 201 1485 1427 1384 82 -4 -61 O ATOM 5299 CB LEU C 201 0.075 13.629 42.106 1.00 10.25 C ANISOU 5299 CB LEU C 201 1297 1319 1279 -2 -10 -35 C ATOM 5300 CG LEU C 201 0.720 14.572 43.133 1.00 10.36 C ANISOU 5300 CG LEU C 201 1430 1291 1217 7 2 -37 C ATOM 5301 CD1 LEU C 201 1.553 13.782 44.134 1.00 11.62 C ANISOU 5301 CD1 LEU C 201 1476 1427 1514 77 -80 -8 C ATOM 5302 CD2 LEU C 201 1.556 15.621 42.416 1.00 12.03 C ANISOU 5302 CD2 LEU C 201 1546 1468 1558 -91 48 -2 C ATOM 5303 N VAL C 202 -2.358 13.489 44.493 1.00 11.00 N ANISOU 5303 N VAL C 202 1439 1364 1379 -7 26 -11 N ATOM 5304 CA VAL C 202 -3.504 14.164 45.085 1.00 10.78 C ANISOU 5304 CA VAL C 202 1386 1335 1376 -43 5 -28 C ATOM 5305 C VAL C 202 -3.018 15.340 45.936 1.00 10.79 C ANISOU 5305 C VAL C 202 1419 1341 1340 10 -18 -48 C ATOM 5306 O VAL C 202 -2.156 15.161 46.785 1.00 11.04 O ANISOU 5306 O VAL C 202 1451 1412 1331 10 -31 -84 O ATOM 5307 CB VAL C 202 -4.367 13.240 45.956 1.00 10.22 C ANISOU 5307 CB VAL C 202 1343 1296 1242 10 -23 -8 C ATOM 5308 CG1 VAL C 202 -5.498 14.026 46.615 1.00 10.61 C ANISOU 5308 CG1 VAL C 202 1325 1416 1290 0 13 -3 C ATOM 5309 CG2 VAL C 202 -4.950 12.107 45.124 1.00 10.62 C ANISOU 5309 CG2 VAL C 202 1347 1332 1355 -23 6 -55 C ATOM 5310 N HIS C 203 -3.550 16.512 45.633 1.00 10.91 N ANISOU 5310 N HIS C 203 1448 1315 1382 -20 -33 -44 N ATOM 5311 CA HIS C 203 -3.417 17.657 46.534 1.00 10.69 C ANISOU 5311 CA HIS C 203 1434 1310 1317 -6 -10 -15 C ATOM 5312 C HIS C 203 -4.777 17.870 47.196 1.00 11.61 C ANISOU 5312 C HIS C 203 1471 1513 1429 16 12 -2 C ATOM 5313 O HIS C 203 -5.770 17.969 46.470 1.00 12.16 O ANISOU 5313 O HIS C 203 1435 1608 1578 43 -10 -13 O ATOM 5314 CB HIS C 203 -3.056 18.902 45.737 1.00 9.83 C ANISOU 5314 CB HIS C 203 1301 1268 1166 -56 -37 -83 C ATOM 5315 CG HIS C 203 -1.688 18.906 45.144 1.00 9.71 C ANISOU 5315 CG HIS C 203 1301 1146 1243 34 2 38 C ATOM 5316 ND1 HIS C 203 -1.308 18.119 44.080 1.00 10.56 N ANISOU 5316 ND1 HIS C 203 1463 1259 1289 30 49 10 N ATOM 5317 CD2 HIS C 203 -0.601 19.643 45.461 1.00 11.05 C ANISOU 5317 CD2 HIS C 203 1407 1389 1403 -17 -95 21 C ATOM 5318 CE1 HIS C 203 -0.044 18.361 43.783 1.00 12.64 C ANISOU 5318 CE1 HIS C 203 1531 1610 1661 -14 -9 -18 C ATOM 5319 NE2 HIS C 203 0.410 19.292 44.606 1.00 12.42 N ANISOU 5319 NE2 HIS C 203 1570 1569 1582 19 12 2 N ATOM 5320 N SER C 204 -4.826 17.911 48.520 1.00 11.53 N ANISOU 5320 N SER C 204 1469 1494 1418 21 4 -24 N ATOM 5321 CA SER C 204 -6.141 17.971 49.158 1.00 11.35 C ANISOU 5321 CA SER C 204 1481 1476 1354 8 7 -34 C ATOM 5322 C SER C 204 -6.037 18.654 50.517 1.00 10.49 C ANISOU 5322 C SER C 204 1333 1336 1316 10 0 -1 C ATOM 5323 O SER C 204 -4.949 18.825 51.053 1.00 10.14 O ANISOU 5323 O SER C 204 1372 1260 1222 18 -29 -9 O ATOM 5324 CB SER C 204 -6.766 16.587 49.289 1.00 12.51 C ANISOU 5324 CB SER C 204 1642 1525 1587 -30 39 -27 C ATOM 5325 OG SER C 204 -6.061 15.802 50.232 1.00 14.22 O ANISOU 5325 OG SER C 204 1816 1793 1794 62 -66 28 O ATOM 5326 N LYS C 205 -7.202 19.069 50.990 1.00 9.82 N ANISOU 5326 N LYS C 205 1330 1223 1178 22 2 -13 N ATOM 5327 CA LYS C 205 -7.292 19.759 52.270 1.00 9.92 C ANISOU 5327 CA LYS C 205 1308 1281 1181 12 -23 -35 C ATOM 5328 C LYS C 205 -8.645 19.499 52.910 1.00 9.81 C ANISOU 5328 C LYS C 205 1299 1250 1180 14 -24 -68 C ATOM 5329 O LYS C 205 -9.688 19.780 52.325 1.00 9.67 O ANISOU 5329 O LYS C 205 1336 1265 1072 71 -11 -58 O ATOM 5330 CB LYS C 205 -7.098 21.267 52.093 1.00 11.13 C ANISOU 5330 CB LYS C 205 1435 1331 1463 -21 1 -12 C ATOM 5331 CG LYS C 205 -7.062 22.010 53.429 1.00 12.66 C ANISOU 5331 CG LYS C 205 1678 1621 1511 6 -27 -56 C ATOM 5332 CD LYS C 205 -5.733 21.734 54.129 1.00 13.30 C ANISOU 5332 CD LYS C 205 1685 1691 1678 13 -26 20 C ATOM 5333 CE LYS C 205 -5.816 22.058 55.609 1.00 13.76 C ANISOU 5333 CE LYS C 205 1772 1726 1732 4 16 -26 C ATOM 5334 NZ LYS C 205 -6.676 21.094 56.345 1.00 13.43 N ANISOU 5334 NZ LYS C 205 1730 1709 1665 17 -39 -7 N ATOM 5335 N THR C 206 -8.621 18.983 54.135 1.00 10.81 N ANISOU 5335 N THR C 206 1419 1389 1299 11 -32 30 N ATOM 5336 CA THR C 206 -9.854 18.837 54.901 1.00 11.41 C ANISOU 5336 CA THR C 206 1440 1501 1395 2 0 -39 C ATOM 5337 C THR C 206 -10.247 20.146 55.571 1.00 11.40 C ANISOU 5337 C THR C 206 1475 1459 1397 21 -13 22 C ATOM 5338 O THR C 206 -9.419 21.020 55.823 1.00 11.97 O ANISOU 5338 O THR C 206 1617 1526 1403 -26 -15 -60 O ATOM 5339 CB THR C 206 -9.665 17.752 55.982 1.00 13.78 C ANISOU 5339 CB THR C 206 1830 1666 1740 -13 -22 129 C ATOM 5340 OG1 THR C 206 -8.511 18.091 56.763 1.00 15.02 O ANISOU 5340 OG1 THR C 206 1986 1973 1748 -18 -81 75 O ATOM 5341 CG2 THR C 206 -9.461 16.399 55.322 1.00 15.35 C ANISOU 5341 CG2 THR C 206 2041 1863 1930 56 27 -13 C ATOM 5342 N GLY C 207 -11.527 20.257 55.898 1.00 11.19 N ANISOU 5342 N GLY C 207 1473 1416 1361 36 -4 44 N ATOM 5343 CA GLY C 207 -12.021 21.359 56.720 1.00 11.47 C ANISOU 5343 CA GLY C 207 1494 1448 1415 12 -14 -11 C ATOM 5344 C GLY C 207 -13.103 20.851 57.669 1.00 11.64 C ANISOU 5344 C GLY C 207 1517 1457 1447 15 -6 19 C ATOM 5345 O GLY C 207 -13.772 19.858 57.396 1.00 11.78 O ANISOU 5345 O GLY C 207 1550 1488 1438 14 -22 -8 O ATOM 5346 N PHE C 208 -13.250 21.534 58.800 1.00 11.92 N ANISOU 5346 N PHE C 208 1531 1549 1449 9 -73 -11 N ATOM 5347 CA PHE C 208 -14.211 21.114 59.817 1.00 12.70 C ANISOU 5347 CA PHE C 208 1596 1675 1553 -18 -13 -17 C ATOM 5348 C PHE C 208 -14.420 22.259 60.798 1.00 13.39 C ANISOU 5348 C PHE C 208 1746 1690 1651 -18 -16 -24 C ATOM 5349 O PHE C 208 -13.427 22.762 61.324 1.00 13.45 O ANISOU 5349 O PHE C 208 1831 1707 1574 -23 -58 -63 O ATOM 5350 CB PHE C 208 -13.671 19.873 60.513 1.00 15.16 C ANISOU 5350 CB PHE C 208 2052 1753 1955 89 -39 21 C ATOM 5351 CG PHE C 208 -14.466 19.279 61.630 1.00 16.99 C ANISOU 5351 CG PHE C 208 2220 2094 2141 -51 78 -8 C ATOM 5352 CD1 PHE C 208 -15.820 19.038 61.513 1.00 17.78 C ANISOU 5352 CD1 PHE C 208 2250 2188 2317 9 -3 -53 C ATOM 5353 CD2 PHE C 208 -13.829 18.920 62.814 1.00 19.31 C ANISOU 5353 CD2 PHE C 208 2529 2444 2365 9 -67 40 C ATOM 5354 CE1 PHE C 208 -16.532 18.463 62.546 1.00 19.28 C ANISOU 5354 CE1 PHE C 208 2487 2446 2393 -31 31 12 C ATOM 5355 CE2 PHE C 208 -14.539 18.358 63.856 1.00 19.43 C ANISOU 5355 CE2 PHE C 208 2498 2450 2434 -18 -12 4 C ATOM 5356 CZ PHE C 208 -15.893 18.128 63.724 1.00 19.35 C ANISOU 5356 CZ PHE C 208 2491 2421 2441 -3 -5 23 C ATOM 5357 N SER C 209 -15.661 22.686 60.991 1.00 14.40 N ANISOU 5357 N SER C 209 1807 1848 1815 22 -11 2 N ATOM 5358 CA SER C 209 -15.921 23.826 61.869 1.00 15.63 C ANISOU 5358 CA SER C 209 2026 1933 1979 33 -4 -55 C ATOM 5359 C SER C 209 -16.276 23.371 63.279 1.00 16.81 C ANISOU 5359 C SER C 209 2211 2124 2052 17 5 -3 C ATOM 5360 O SER C 209 -16.330 24.189 64.198 1.00 17.07 O ANISOU 5360 O SER C 209 2298 2124 2063 -13 -22 -13 O ATOM 5361 CB SER C 209 -17.059 24.688 61.324 1.00 15.89 C ANISOU 5361 CB SER C 209 2018 1961 2057 7 -13 -7 C ATOM 5362 OG SER C 209 -18.287 23.984 61.352 1.00 15.12 O ANISOU 5362 OG SER C 209 1981 1949 1814 13 -8 -12 O ATOM 5363 N GLY C 210 -16.525 22.078 63.435 1.00 17.63 N ANISOU 5363 N GLY C 210 2312 2184 2202 -35 -22 -7 N ATOM 5364 CA GLY C 210 -16.973 21.535 64.712 1.00 18.21 C ANISOU 5364 CA GLY C 210 2375 2307 2239 -3 9 8 C ATOM 5365 C GLY C 210 -18.305 20.813 64.543 1.00 19.05 C ANISOU 5365 C GLY C 210 2427 2420 2389 -18 -14 -9 C ATOM 5366 O GLY C 210 -19.004 20.976 63.540 1.00 19.27 O ANISOU 5366 O GLY C 210 2516 2453 2354 -6 -6 23 O ATOM 5367 N VAL C 211 -18.603 19.928 65.487 1.00 19.52 N ANISOU 5367 N VAL C 211 2557 2460 2400 8 -10 7 N ATOM 5368 CA VAL C 211 -19.867 19.207 65.491 1.00 20.76 C ANISOU 5368 CA VAL C 211 2662 2622 2602 -60 -20 13 C ATOM 5369 C VAL C 211 -20.992 20.114 65.974 1.00 22.01 C ANISOU 5369 C VAL C 211 2795 2786 2780 4 35 -5 C ATOM 5370 O VAL C 211 -20.913 20.693 67.057 1.00 22.80 O ANISOU 5370 O VAL C 211 2948 2922 2791 -19 42 -20 O ATOM 5371 CB VAL C 211 -19.807 17.950 66.377 1.00 20.82 C ANISOU 5371 CB VAL C 211 2679 2613 2619 8 -18 5 C ATOM 5372 CG1 VAL C 211 -21.125 17.192 66.335 1.00 21.29 C ANISOU 5372 CG1 VAL C 211 2706 2727 2656 -22 17 35 C ATOM 5373 CG2 VAL C 211 -18.653 17.062 65.944 1.00 20.90 C ANISOU 5373 CG2 VAL C 211 2670 2657 2612 2 -3 -20 C ATOM 5374 N GLY C 212 -22.023 20.243 65.150 1.00 22.76 N ANISOU 5374 N GLY C 212 2904 2911 2834 -25 -23 24 N ATOM 5375 CA GLY C 212 -23.173 21.067 65.512 1.00 23.94 C ANISOU 5375 CA GLY C 212 3057 3034 3006 52 0 -10 C ATOM 5376 C GLY C 212 -24.334 20.157 65.901 1.00 25.07 C ANISOU 5376 C GLY C 212 3214 3162 3152 -31 30 7 C ATOM 5377 O GLY C 212 -24.145 18.996 66.261 1.00 25.65 O ANISOU 5377 O GLY C 212 3298 3198 3251 4 51 25 O ATOM 5378 N THR C 213 -25.534 20.703 65.824 1.00 26.00 N ANISOU 5378 N THR C 213 3313 3295 3269 46 3 -8 N ATOM 5379 CA THR C 213 -26.756 19.951 66.092 1.00 27.30 C ANISOU 5379 CA THR C 213 3451 3422 3500 -29 24 24 C ATOM 5380 C THR C 213 -27.532 19.780 64.799 1.00 28.03 C ANISOU 5380 C THR C 213 3561 3546 3545 18 1 3 C ATOM 5381 O THR C 213 -27.063 20.266 63.763 1.00 27.74 O ANISOU 5381 O THR C 213 3496 3504 3539 -1 1 1 O ATOM 5382 CB THR C 213 -27.610 20.695 67.132 1.00 28.44 C ANISOU 5382 CB THR C 213 3618 3580 3608 38 51 -30 C ATOM 5383 OG1 THR C 213 -27.778 22.055 66.702 1.00 28.67 O ANISOU 5383 OG1 THR C 213 3701 3599 3591 14 55 -11 O ATOM 5384 CG2 THR C 213 -26.949 20.678 68.498 1.00 29.23 C ANISOU 5384 CG2 THR C 213 3724 3688 3694 5 -5 4 C ATOM 5385 N GLU C 214 -28.669 19.089 64.804 1.00 28.96 N ANISOU 5385 N GLU C 214 3651 3632 3720 -23 38 2 N ATOM 5386 CA GLU C 214 -29.437 18.948 63.566 1.00 29.74 C ANISOU 5386 CA GLU C 214 3760 3762 3778 20 -4 -10 C ATOM 5387 C GLU C 214 -29.917 20.316 63.090 1.00 29.82 C ANISOU 5387 C GLU C 214 3777 3747 3808 -1 8 -8 C ATOM 5388 O GLU C 214 -29.795 20.656 61.917 1.00 30.05 O ANISOU 5388 O GLU C 214 3800 3800 3819 -10 0 -13 O ATOM 5389 CB GLU C 214 -30.609 17.988 63.729 1.00 30.97 C ANISOU 5389 CB GLU C 214 3893 3867 4009 -42 22 13 C ATOM 5390 N SER C 215 -30.426 21.118 64.020 1.00 29.65 N ANISOU 5390 N SER C 215 3748 3697 3821 -8 18 10 N ATOM 5391 CA SER C 215 -30.871 22.473 63.755 1.00 29.01 C ANISOU 5391 CA SER C 215 3630 3661 3731 -48 3 23 C ATOM 5392 C SER C 215 -29.750 23.395 63.299 1.00 27.59 C ANISOU 5392 C SER C 215 3461 3521 3502 30 -34 -4 C ATOM 5393 O SER C 215 -29.945 24.234 62.419 1.00 27.84 O ANISOU 5393 O SER C 215 3514 3540 3522 15 6 16 O ATOM 5394 CB SER C 215 -31.487 23.072 65.031 1.00 30.59 C ANISOU 5394 CB SER C 215 3883 3890 3851 63 18 -51 C ATOM 5395 OG SER C 215 -32.272 22.106 65.705 1.00 32.43 O ANISOU 5395 OG SER C 215 4098 4064 4161 -18 40 28 O ATOM 5396 N ASN C 216 -28.583 23.295 63.925 1.00 26.09 N ANISOU 5396 N ASN C 216 3290 3267 3355 -16 67 9 N ATOM 5397 CA ASN C 216 -27.448 24.163 63.655 1.00 24.52 C ANISOU 5397 CA ASN C 216 3062 3114 3141 117 37 63 C ATOM 5398 C ASN C 216 -26.168 23.357 63.451 1.00 21.80 C ANISOU 5398 C ASN C 216 2837 2776 2668 -33 -6 -26 C ATOM 5399 O ASN C 216 -25.288 23.314 64.310 1.00 21.15 O ANISOU 5399 O ASN C 216 2756 2680 2601 -10 42 -19 O ATOM 5400 CB ASN C 216 -27.207 25.138 64.813 1.00 28.57 C ANISOU 5400 CB ASN C 216 3799 3608 3450 -122 -45 -91 C ATOM 5401 CG ASN C 216 -28.283 26.166 65.050 1.00 33.46 C ANISOU 5401 CG ASN C 216 4174 4144 4396 97 23 -42 C ATOM 5402 OD1 ASN C 216 -28.803 26.770 64.110 1.00 34.59 O ANISOU 5402 OD1 ASN C 216 4397 4364 4382 24 -4 14 O ATOM 5403 ND2 ASN C 216 -28.632 26.375 66.316 1.00 35.44 N ANISOU 5403 ND2 ASN C 216 4497 4480 4489 17 32 -7 N ATOM 5404 N PRO C 217 -26.072 22.674 62.313 1.00 20.09 N ANISOU 5404 N PRO C 217 2497 2560 2578 21 4 24 N ATOM 5405 CA PRO C 217 -24.953 21.796 62.028 1.00 18.72 C ANISOU 5405 CA PRO C 217 2363 2387 2365 -60 -14 24 C ATOM 5406 C PRO C 217 -23.651 22.555 61.845 1.00 17.21 C ANISOU 5406 C PRO C 217 2201 2194 2143 52 -31 -2 C ATOM 5407 O PRO C 217 -23.653 23.743 61.513 1.00 17.31 O ANISOU 5407 O PRO C 217 2200 2201 2176 28 -44 12 O ATOM 5408 CB PRO C 217 -25.367 21.088 60.742 1.00 19.05 C ANISOU 5408 CB PRO C 217 2424 2424 2391 -12 -16 -14 C ATOM 5409 CG PRO C 217 -26.230 22.087 60.044 1.00 19.53 C ANISOU 5409 CG PRO C 217 2495 2461 2466 27 -2 8 C ATOM 5410 CD PRO C 217 -26.963 22.820 61.137 1.00 19.82 C ANISOU 5410 CD PRO C 217 2509 2506 2516 21 29 3 C ATOM 5411 N GLY C 218 -22.534 21.879 62.094 1.00 15.57 N ANISOU 5411 N GLY C 218 2028 1985 1901 -56 29 -35 N ATOM 5412 CA GLY C 218 -21.238 22.402 61.654 1.00 14.44 C ANISOU 5412 CA GLY C 218 1923 1841 1721 1 0 -43 C ATOM 5413 C GLY C 218 -21.084 22.063 60.166 1.00 13.27 C ANISOU 5413 C GLY C 218 1698 1684 1662 -10 -1 -13 C ATOM 5414 O GLY C 218 -21.980 21.459 59.575 1.00 12.62 O ANISOU 5414 O GLY C 218 1684 1587 1524 23 38 -38 O ATOM 5415 N VAL C 219 -19.957 22.461 59.598 1.00 12.86 N ANISOU 5415 N VAL C 219 1670 1678 1539 2 -11 -50 N ATOM 5416 CA VAL C 219 -19.650 22.073 58.217 1.00 12.08 C ANISOU 5416 CA VAL C 219 1528 1561 1502 -6 4 -25 C ATOM 5417 C VAL C 219 -18.345 21.296 58.186 1.00 11.58 C ANISOU 5417 C VAL C 219 1532 1439 1428 -21 -21 -25 C ATOM 5418 O VAL C 219 -17.427 21.548 58.976 1.00 11.34 O ANISOU 5418 O VAL C 219 1588 1417 1305 33 -29 -30 O ATOM 5419 CB VAL C 219 -19.611 23.312 57.308 1.00 13.30 C ANISOU 5419 CB VAL C 219 1755 1641 1657 21 14 26 C ATOM 5420 CG1 VAL C 219 -18.470 24.233 57.704 1.00 13.87 C ANISOU 5420 CG1 VAL C 219 1817 1725 1727 -18 20 -27 C ATOM 5421 CG2 VAL C 219 -19.520 22.916 55.841 1.00 13.66 C ANISOU 5421 CG2 VAL C 219 1852 1689 1651 -2 9 25 C ATOM 5422 N ALA C 220 -18.262 20.307 57.302 1.00 10.89 N ANISOU 5422 N ALA C 220 1436 1389 1314 8 -23 26 N ATOM 5423 CA ALA C 220 -17.016 19.601 57.045 1.00 11.07 C ANISOU 5423 CA ALA C 220 1420 1453 1333 -4 -10 23 C ATOM 5424 C ALA C 220 -16.737 19.627 55.539 1.00 10.98 C ANISOU 5424 C ALA C 220 1412 1425 1336 -12 0 -4 C ATOM 5425 O ALA C 220 -17.685 19.588 54.761 1.00 11.11 O ANISOU 5425 O ALA C 220 1525 1441 1255 -11 -32 -11 O ATOM 5426 CB ALA C 220 -17.055 18.171 57.543 1.00 11.93 C ANISOU 5426 CB ALA C 220 1581 1414 1538 -9 12 -34 C ATOM 5427 N TRP C 221 -15.470 19.730 55.191 1.00 10.81 N ANISOU 5427 N TRP C 221 1403 1400 1306 24 3 -28 N ATOM 5428 CA TRP C 221 -15.057 19.922 53.814 1.00 10.66 C ANISOU 5428 CA TRP C 221 1372 1367 1312 7 3 15 C ATOM 5429 C TRP C 221 -13.992 18.897 53.411 1.00 10.64 C ANISOU 5429 C TRP C 221 1412 1353 1277 24 -17 -14 C ATOM 5430 O TRP C 221 -13.188 18.471 54.239 1.00 10.96 O ANISOU 5430 O TRP C 221 1406 1390 1369 36 -72 -44 O ATOM 5431 CB TRP C 221 -14.398 21.275 53.608 1.00 11.60 C ANISOU 5431 CB TRP C 221 1555 1385 1469 -32 -54 -9 C ATOM 5432 CG TRP C 221 -15.173 22.539 53.659 1.00 11.76 C ANISOU 5432 CG TRP C 221 1575 1436 1458 25 -28 4 C ATOM 5433 CD1 TRP C 221 -15.424 23.310 54.762 1.00 12.30 C ANISOU 5433 CD1 TRP C 221 1621 1566 1486 55 -14 -28 C ATOM 5434 CD2 TRP C 221 -15.767 23.233 52.552 1.00 11.56 C ANISOU 5434 CD2 TRP C 221 1556 1460 1376 24 -34 -35 C ATOM 5435 NE1 TRP C 221 -16.143 24.426 54.413 1.00 12.18 N ANISOU 5435 NE1 TRP C 221 1680 1513 1434 28 -31 -13 N ATOM 5436 CE2 TRP C 221 -16.367 24.400 53.058 1.00 11.89 C ANISOU 5436 CE2 TRP C 221 1565 1522 1430 69 -43 -50 C ATOM 5437 CE3 TRP C 221 -15.859 22.966 51.180 1.00 10.96 C ANISOU 5437 CE3 TRP C 221 1469 1362 1333 93 -46 20 C ATOM 5438 CZ2 TRP C 221 -17.047 25.308 52.249 1.00 11.91 C ANISOU 5438 CZ2 TRP C 221 1650 1498 1376 32 6 -9 C ATOM 5439 CZ3 TRP C 221 -16.532 23.872 50.377 1.00 9.68 C ANISOU 5439 CZ3 TRP C 221 1271 1225 1182 -4 -19 -16 C ATOM 5440 CH2 TRP C 221 -17.118 25.024 50.916 1.00 10.32 C ANISOU 5440 CH2 TRP C 221 1308 1307 1305 67 -18 4 C ATOM 5441 N TRP C 222 -13.957 18.573 52.121 1.00 9.99 N ANISOU 5441 N TRP C 222 1273 1270 1253 30 -14 -19 N ATOM 5442 CA TRP C 222 -12.737 18.001 51.539 1.00 9.70 C ANISOU 5442 CA TRP C 222 1283 1212 1190 19 -6 14 C ATOM 5443 C TRP C 222 -12.581 18.607 50.150 1.00 9.48 C ANISOU 5443 C TRP C 222 1242 1209 1150 20 12 -30 C ATOM 5444 O TRP C 222 -13.526 18.540 49.362 1.00 9.99 O ANISOU 5444 O TRP C 222 1342 1311 1141 52 -43 -53 O ATOM 5445 CB TRP C 222 -12.781 16.479 51.524 1.00 10.11 C ANISOU 5445 CB TRP C 222 1381 1222 1239 -35 -51 -59 C ATOM 5446 CG TRP C 222 -11.439 15.849 51.290 1.00 12.30 C ANISOU 5446 CG TRP C 222 1497 1581 1596 53 27 -5 C ATOM 5447 CD1 TRP C 222 -10.248 16.240 51.832 1.00 12.88 C ANISOU 5447 CD1 TRP C 222 1627 1690 1575 -35 -45 -48 C ATOM 5448 CD2 TRP C 222 -11.141 14.716 50.465 1.00 12.69 C ANISOU 5448 CD2 TRP C 222 1722 1541 1558 14 21 20 C ATOM 5449 NE1 TRP C 222 -9.232 15.428 51.397 1.00 13.79 N ANISOU 5449 NE1 TRP C 222 1753 1707 1781 32 -33 10 N ATOM 5450 CE2 TRP C 222 -9.757 14.484 50.554 1.00 14.19 C ANISOU 5450 CE2 TRP C 222 1791 1802 1797 -41 -49 4 C ATOM 5451 CE3 TRP C 222 -11.921 13.876 49.663 1.00 13.88 C ANISOU 5451 CE3 TRP C 222 1786 1788 1698 -90 -53 30 C ATOM 5452 CZ2 TRP C 222 -9.123 13.446 49.869 1.00 16.25 C ANISOU 5452 CZ2 TRP C 222 2056 2017 2100 86 30 -57 C ATOM 5453 CZ3 TRP C 222 -11.293 12.849 48.983 1.00 16.82 C ANISOU 5453 CZ3 TRP C 222 2158 2087 2146 82 41 -55 C ATOM 5454 CH2 TRP C 222 -9.911 12.644 49.092 1.00 17.19 C ANISOU 5454 CH2 TRP C 222 2156 2178 2196 -7 -24 -38 C ATOM 5455 N VAL C 223 -11.498 19.339 49.929 1.00 9.60 N ANISOU 5455 N VAL C 223 1292 1207 1150 0 -2 -3 N ATOM 5456 CA VAL C 223 -11.291 20.036 48.658 1.00 9.51 C ANISOU 5456 CA VAL C 223 1268 1190 1157 -26 -9 4 C ATOM 5457 C VAL C 223 -9.904 19.715 48.117 1.00 9.96 C ANISOU 5457 C VAL C 223 1281 1313 1192 11 -25 23 C ATOM 5458 O VAL C 223 -8.991 19.354 48.868 1.00 9.85 O ANISOU 5458 O VAL C 223 1308 1357 1076 7 -31 21 O ATOM 5459 CB VAL C 223 -11.467 21.562 48.753 1.00 9.90 C ANISOU 5459 CB VAL C 223 1226 1209 1328 36 -50 22 C ATOM 5460 CG1 VAL C 223 -12.815 21.971 49.335 1.00 9.93 C ANISOU 5460 CG1 VAL C 223 1293 1278 1204 10 -6 -44 C ATOM 5461 CG2 VAL C 223 -10.347 22.207 49.569 1.00 9.96 C ANISOU 5461 CG2 VAL C 223 1361 1180 1244 -21 -54 31 C ATOM 5462 N GLY C 224 -9.719 19.809 46.802 1.00 9.96 N ANISOU 5462 N GLY C 224 1273 1337 1174 -7 -63 -23 N ATOM 5463 CA GLY C 224 -8.387 19.654 46.229 1.00 10.21 C ANISOU 5463 CA GLY C 224 1313 1337 1228 17 -26 0 C ATOM 5464 C GLY C 224 -8.451 19.289 44.752 1.00 10.50 C ANISOU 5464 C GLY C 224 1354 1371 1266 22 -24 -32 C ATOM 5465 O GLY C 224 -9.412 19.633 44.069 1.00 10.71 O ANISOU 5465 O GLY C 224 1373 1406 1289 100 -27 -68 O ATOM 5466 N TRP C 225 -7.416 18.599 44.285 1.00 10.31 N ANISOU 5466 N TRP C 225 1421 1252 1245 17 -5 -11 N ATOM 5467 CA TRP C 225 -7.437 18.100 42.916 1.00 10.61 C ANISOU 5467 CA TRP C 225 1453 1320 1257 -11 -19 -9 C ATOM 5468 C TRP C 225 -6.672 16.787 42.825 1.00 11.21 C ANISOU 5468 C TRP C 225 1481 1389 1390 35 -43 -21 C ATOM 5469 O TRP C 225 -5.775 16.481 43.612 1.00 10.98 O ANISOU 5469 O TRP C 225 1515 1300 1357 66 -56 -82 O ATOM 5470 CB TRP C 225 -6.914 19.120 41.910 1.00 10.59 C ANISOU 5470 CB TRP C 225 1405 1306 1315 -12 -18 13 C ATOM 5471 CG TRP C 225 -5.493 19.546 42.106 1.00 11.21 C ANISOU 5471 CG TRP C 225 1423 1443 1395 -28 -18 73 C ATOM 5472 CD1 TRP C 225 -4.366 18.926 41.651 1.00 12.59 C ANISOU 5472 CD1 TRP C 225 1552 1594 1638 45 5 19 C ATOM 5473 CD2 TRP C 225 -5.048 20.711 42.808 1.00 12.47 C ANISOU 5473 CD2 TRP C 225 1598 1562 1579 -55 -45 -14 C ATOM 5474 NE1 TRP C 225 -3.247 19.623 42.035 1.00 12.81 N ANISOU 5474 NE1 TRP C 225 1697 1534 1636 -28 -21 18 N ATOM 5475 CE2 TRP C 225 -3.642 20.725 42.750 1.00 12.35 C ANISOU 5475 CE2 TRP C 225 1593 1554 1544 28 9 47 C ATOM 5476 CE3 TRP C 225 -5.712 21.742 43.484 1.00 13.50 C ANISOU 5476 CE3 TRP C 225 1691 1746 1691 75 4 -32 C ATOM 5477 CZ2 TRP C 225 -2.879 21.736 43.336 1.00 13.59 C ANISOU 5477 CZ2 TRP C 225 1743 1717 1705 -33 -45 -8 C ATOM 5478 CZ3 TRP C 225 -4.954 22.740 44.067 1.00 15.02 C ANISOU 5478 CZ3 TRP C 225 1879 1890 1937 -56 -10 -45 C ATOM 5479 CH2 TRP C 225 -3.553 22.724 43.993 1.00 14.66 C ANISOU 5479 CH2 TRP C 225 1866 1796 1909 18 21 -24 C ATOM 5480 N VAL C 226 -7.107 15.986 41.858 1.00 11.42 N ANISOU 5480 N VAL C 226 1524 1418 1397 -3 -41 -22 N ATOM 5481 CA VAL C 226 -6.468 14.713 41.557 1.00 11.76 C ANISOU 5481 CA VAL C 226 1527 1470 1469 37 -5 1 C ATOM 5482 C VAL C 226 -5.801 14.807 40.187 1.00 11.70 C ANISOU 5482 C VAL C 226 1540 1453 1451 35 -19 -36 C ATOM 5483 O VAL C 226 -6.477 15.166 39.224 1.00 11.98 O ANISOU 5483 O VAL C 226 1707 1437 1409 24 -54 -62 O ATOM 5484 CB VAL C 226 -7.481 13.553 41.542 1.00 12.67 C ANISOU 5484 CB VAL C 226 1586 1589 1638 -30 6 2 C ATOM 5485 CG1 VAL C 226 -6.798 12.241 41.170 1.00 13.62 C ANISOU 5485 CG1 VAL C 226 1800 1671 1703 41 -4 -24 C ATOM 5486 CG2 VAL C 226 -8.176 13.424 42.890 1.00 13.42 C ANISOU 5486 CG2 VAL C 226 1763 1712 1624 0 -6 25 C ATOM 5487 N GLU C 227 -4.505 14.532 40.127 1.00 11.89 N ANISOU 5487 N GLU C 227 1525 1516 1476 4 -16 -2 N ATOM 5488 CA GLU C 227 -3.864 14.336 38.827 1.00 12.23 C ANISOU 5488 CA GLU C 227 1595 1546 1507 37 -5 -10 C ATOM 5489 C GLU C 227 -3.749 12.840 38.555 1.00 12.66 C ANISOU 5489 C GLU C 227 1666 1563 1582 35 -39 -21 C ATOM 5490 O GLU C 227 -3.089 12.120 39.301 1.00 12.69 O ANISOU 5490 O GLU C 227 1729 1523 1569 64 -26 -24 O ATOM 5491 CB GLU C 227 -2.508 15.023 38.779 1.00 13.56 C ANISOU 5491 CB GLU C 227 1677 1791 1686 -31 9 -17 C ATOM 5492 CG GLU C 227 -2.588 16.546 38.810 1.00 15.56 C ANISOU 5492 CG GLU C 227 2086 1894 1933 9 15 29 C ATOM 5493 CD GLU C 227 -1.194 17.147 38.885 1.00 17.27 C ANISOU 5493 CD GLU C 227 2169 2161 2231 -39 -14 -10 C ATOM 5494 OE1 GLU C 227 -0.498 16.893 39.891 1.00 18.10 O ANISOU 5494 OE1 GLU C 227 2385 2275 2216 -41 -31 30 O ATOM 5495 OE2 GLU C 227 -0.798 17.855 37.939 1.00 17.92 O ANISOU 5495 OE2 GLU C 227 2320 2290 2197 -65 10 -20 O ATOM 5496 N LYS C 228 -4.431 12.385 37.510 1.00 12.65 N ANISOU 5496 N LYS C 228 1647 1579 1582 5 -35 -8 N ATOM 5497 CA LYS C 228 -4.368 10.980 37.118 1.00 13.00 C ANISOU 5497 CA LYS C 228 1696 1610 1633 18 -9 -11 C ATOM 5498 C LYS C 228 -3.833 10.915 35.689 1.00 13.09 C ANISOU 5498 C LYS C 228 1718 1609 1646 4 3 -24 C ATOM 5499 O LYS C 228 -4.489 11.447 34.794 1.00 13.52 O ANISOU 5499 O LYS C 228 1811 1683 1643 14 5 -10 O ATOM 5500 CB LYS C 228 -5.742 10.318 37.207 1.00 13.64 C ANISOU 5500 CB LYS C 228 1705 1778 1698 -6 -6 20 C ATOM 5501 CG LYS C 228 -5.729 8.842 36.844 1.00 16.31 C ANISOU 5501 CG LYS C 228 2239 1921 2037 24 -21 -43 C ATOM 5502 CD LYS C 228 -7.093 8.193 37.008 1.00 19.47 C ANISOU 5502 CD LYS C 228 2376 2523 2497 -38 3 36 C ATOM 5503 CE LYS C 228 -7.022 6.734 36.570 1.00 22.17 C ANISOU 5503 CE LYS C 228 2916 2699 2809 27 -6 -62 C ATOM 5504 NZ LYS C 228 -8.275 5.995 36.872 1.00 24.38 N ANISOU 5504 NZ LYS C 228 3036 3064 3164 -43 12 3 N ATOM 5505 N GLU C 229 -2.680 10.288 35.516 1.00 13.32 N ANISOU 5505 N GLU C 229 1674 1666 1720 -26 4 -10 N ATOM 5506 CA GLU C 229 -2.022 10.287 34.204 1.00 14.22 C ANISOU 5506 CA GLU C 229 1832 1803 1768 21 43 53 C ATOM 5507 C GLU C 229 -1.853 11.728 33.753 1.00 14.04 C ANISOU 5507 C GLU C 229 1816 1774 1746 -24 -21 -5 C ATOM 5508 O GLU C 229 -1.197 12.493 34.485 1.00 13.56 O ANISOU 5508 O GLU C 229 1833 1703 1618 0 -13 6 O ATOM 5509 CB GLU C 229 -2.783 9.379 33.235 1.00 17.14 C ANISOU 5509 CB GLU C 229 2186 2212 2114 -82 -52 -127 C ATOM 5510 CG GLU C 229 -2.813 7.929 33.699 1.00 20.23 C ANISOU 5510 CG GLU C 229 2680 2474 2531 76 42 97 C ATOM 5511 CD GLU C 229 -3.737 7.016 32.926 1.00 23.67 C ANISOU 5511 CD GLU C 229 3023 2936 3036 -109 -38 -69 C ATOM 5512 OE1 GLU C 229 -4.732 7.478 32.331 1.00 25.61 O ANISOU 5512 OE1 GLU C 229 3215 3231 3284 17 -68 15 O ATOM 5513 OE2 GLU C 229 -3.482 5.792 32.914 1.00 24.14 O ANISOU 5513 OE2 GLU C 229 3101 2982 3087 -23 -35 -43 O ATOM 5514 N THR C 230 -2.435 12.148 32.638 1.00 13.84 N ANISOU 5514 N THR C 230 1805 1722 1730 -2 -1 -20 N ATOM 5515 CA THR C 230 -2.270 13.528 32.191 1.00 13.70 C ANISOU 5515 CA THR C 230 1753 1721 1732 3 2 -16 C ATOM 5516 C THR C 230 -3.562 14.326 32.323 1.00 13.53 C ANISOU 5516 C THR C 230 1736 1706 1697 -12 4 -18 C ATOM 5517 O THR C 230 -3.692 15.395 31.728 1.00 14.33 O ANISOU 5517 O THR C 230 1900 1794 1752 31 19 24 O ATOM 5518 CB THR C 230 -1.767 13.639 30.739 1.00 14.53 C ANISOU 5518 CB THR C 230 1804 1918 1798 -23 36 -13 C ATOM 5519 OG1 THR C 230 -2.693 12.991 29.859 1.00 14.77 O ANISOU 5519 OG1 THR C 230 1932 1984 1695 18 -22 -16 O ATOM 5520 CG2 THR C 230 -0.391 13.015 30.626 1.00 13.61 C ANISOU 5520 CG2 THR C 230 1835 1727 1610 28 -26 -12 C ATOM 5521 N GLU C 231 -4.501 13.809 33.105 1.00 12.76 N ANISOU 5521 N GLU C 231 1694 1621 1532 15 -25 -54 N ATOM 5522 CA GLU C 231 -5.731 14.529 33.392 1.00 13.41 C ANISOU 5522 CA GLU C 231 1731 1743 1620 54 1 -24 C ATOM 5523 C GLU C 231 -5.675 15.155 34.785 1.00 13.28 C ANISOU 5523 C GLU C 231 1726 1695 1625 38 -1 -16 C ATOM 5524 O GLU C 231 -4.949 14.660 35.642 1.00 13.41 O ANISOU 5524 O GLU C 231 1730 1722 1644 27 -37 -49 O ATOM 5525 CB GLU C 231 -6.945 13.604 33.294 1.00 15.35 C ANISOU 5525 CB GLU C 231 2011 1887 1933 -116 -7 -31 C ATOM 5526 CG GLU C 231 -8.279 14.334 33.256 1.00 18.64 C ANISOU 5526 CG GLU C 231 2246 2404 2431 62 -3 -63 C ATOM 5527 CD GLU C 231 -8.320 15.409 32.185 1.00 21.16 C ANISOU 5527 CD GLU C 231 2730 2534 2775 -15 9 74 C ATOM 5528 OE1 GLU C 231 -8.667 15.083 31.030 1.00 24.51 O ANISOU 5528 OE1 GLU C 231 3250 3101 2962 -29 -58 -35 O ATOM 5529 OE2 GLU C 231 -7.987 16.573 32.497 1.00 18.98 O ANISOU 5529 OE2 GLU C 231 2428 2483 2302 74 -54 -39 O ATOM 5530 N VAL C 232 -6.433 16.225 34.982 1.00 13.12 N ANISOU 5530 N VAL C 232 1702 1684 1598 28 26 6 N ATOM 5531 CA VAL C 232 -6.600 16.789 36.321 1.00 12.96 C ANISOU 5531 CA VAL C 232 1666 1667 1593 27 -20 1 C ATOM 5532 C VAL C 232 -8.081 16.925 36.639 1.00 12.83 C ANISOU 5532 C VAL C 232 1663 1651 1560 2 -8 11 C ATOM 5533 O VAL C 232 -8.904 17.311 35.804 1.00 12.76 O ANISOU 5533 O VAL C 232 1716 1601 1532 16 -32 9 O ATOM 5534 CB VAL C 232 -5.862 18.125 36.477 1.00 13.99 C ANISOU 5534 CB VAL C 232 1802 1742 1771 -30 -39 -28 C ATOM 5535 CG1 VAL C 232 -6.345 19.150 35.458 1.00 15.07 C ANISOU 5535 CG1 VAL C 232 1990 1821 1914 15 -9 48 C ATOM 5536 CG2 VAL C 232 -6.008 18.678 37.888 1.00 14.06 C ANISOU 5536 CG2 VAL C 232 1835 1759 1749 17 3 16 C ATOM 5537 N TYR C 233 -8.457 16.539 37.854 1.00 12.28 N ANISOU 5537 N TYR C 233 1585 1543 1537 -14 -16 -7 N ATOM 5538 CA TYR C 233 -9.824 16.675 38.329 1.00 12.02 C ANISOU 5538 CA TYR C 233 1590 1490 1487 -10 8 -27 C ATOM 5539 C TYR C 233 -9.857 17.585 39.559 1.00 11.91 C ANISOU 5539 C TYR C 233 1563 1479 1485 22 4 -34 C ATOM 5540 O TYR C 233 -9.187 17.261 40.534 1.00 12.98 O ANISOU 5540 O TYR C 233 1750 1644 1539 68 -30 -13 O ATOM 5541 CB TYR C 233 -10.409 15.311 38.710 1.00 12.44 C ANISOU 5541 CB TYR C 233 1647 1526 1555 -21 15 27 C ATOM 5542 CG TYR C 233 -10.464 14.346 37.544 1.00 13.18 C ANISOU 5542 CG TYR C 233 1748 1614 1647 -38 -8 -13 C ATOM 5543 CD1 TYR C 233 -11.571 14.316 36.705 1.00 14.04 C ANISOU 5543 CD1 TYR C 233 1803 1769 1762 -1 -43 42 C ATOM 5544 CD2 TYR C 233 -9.405 13.490 37.282 1.00 13.73 C ANISOU 5544 CD2 TYR C 233 1759 1739 1720 -6 6 16 C ATOM 5545 CE1 TYR C 233 -11.619 13.437 35.639 1.00 14.80 C ANISOU 5545 CE1 TYR C 233 1927 1848 1850 -25 -36 4 C ATOM 5546 CE2 TYR C 233 -9.447 12.609 36.214 1.00 14.63 C ANISOU 5546 CE2 TYR C 233 1928 1767 1863 -9 20 -24 C ATOM 5547 CZ TYR C 233 -10.559 12.594 35.400 1.00 15.60 C ANISOU 5547 CZ TYR C 233 1989 1954 1985 11 -19 -9 C ATOM 5548 OH TYR C 233 -10.623 11.723 34.331 1.00 17.23 O ANISOU 5548 OH TYR C 233 2304 2109 2133 2 13 -91 O ATOM 5549 N PHE C 234 -10.599 18.675 39.489 1.00 10.95 N ANISOU 5549 N PHE C 234 1468 1401 1290 -22 -7 -28 N ATOM 5550 CA PHE C 234 -10.764 19.546 40.656 1.00 10.63 C ANISOU 5550 CA PHE C 234 1395 1343 1299 27 -1 -6 C ATOM 5551 C PHE C 234 -12.005 19.125 41.425 1.00 10.71 C ANISOU 5551 C PHE C 234 1411 1374 1283 -2 -10 -9 C ATOM 5552 O PHE C 234 -13.026 18.774 40.828 1.00 10.64 O ANISOU 5552 O PHE C 234 1476 1412 1154 -48 12 -56 O ATOM 5553 CB PHE C 234 -10.843 21.012 40.214 1.00 11.00 C ANISOU 5553 CB PHE C 234 1523 1335 1322 13 -14 -39 C ATOM 5554 CG PHE C 234 -9.617 21.434 39.448 1.00 12.71 C ANISOU 5554 CG PHE C 234 1589 1577 1663 -43 24 44 C ATOM 5555 CD1 PHE C 234 -8.459 21.801 40.114 1.00 12.68 C ANISOU 5555 CD1 PHE C 234 1656 1515 1648 10 -45 -5 C ATOM 5556 CD2 PHE C 234 -9.624 21.444 38.065 1.00 13.64 C ANISOU 5556 CD2 PHE C 234 1764 1713 1705 -5 7 -28 C ATOM 5557 CE1 PHE C 234 -7.331 22.181 39.411 1.00 13.48 C ANISOU 5557 CE1 PHE C 234 1685 1703 1735 20 -10 -1 C ATOM 5558 CE2 PHE C 234 -8.498 21.822 37.356 1.00 13.85 C ANISOU 5558 CE2 PHE C 234 1796 1743 1723 -24 12 13 C ATOM 5559 CZ PHE C 234 -7.350 22.190 38.029 1.00 13.94 C ANISOU 5559 CZ PHE C 234 1743 1805 1747 -11 27 35 C ATOM 5560 N PHE C 235 -11.927 19.132 42.760 1.00 10.65 N ANISOU 5560 N PHE C 235 1433 1339 1274 -16 5 -12 N ATOM 5561 CA PHE C 235 -13.089 18.729 43.539 1.00 10.77 C ANISOU 5561 CA PHE C 235 1410 1333 1350 -17 14 -34 C ATOM 5562 C PHE C 235 -13.276 19.585 44.788 1.00 10.38 C ANISOU 5562 C PHE C 235 1346 1303 1294 -16 16 6 C ATOM 5563 O PHE C 235 -12.340 20.116 45.368 1.00 10.70 O ANISOU 5563 O PHE C 235 1392 1321 1354 -32 -19 35 O ATOM 5564 CB PHE C 235 -13.050 17.250 43.915 1.00 10.83 C ANISOU 5564 CB PHE C 235 1439 1349 1327 26 16 14 C ATOM 5565 CG PHE C 235 -12.005 16.841 44.910 1.00 11.99 C ANISOU 5565 CG PHE C 235 1502 1575 1480 12 -64 -17 C ATOM 5566 CD1 PHE C 235 -12.276 16.894 46.272 1.00 12.37 C ANISOU 5566 CD1 PHE C 235 1631 1568 1501 37 -22 3 C ATOM 5567 CD2 PHE C 235 -10.765 16.399 44.490 1.00 11.29 C ANISOU 5567 CD2 PHE C 235 1513 1336 1441 -30 -7 -51 C ATOM 5568 CE1 PHE C 235 -11.313 16.512 47.191 1.00 12.27 C ANISOU 5568 CE1 PHE C 235 1604 1556 1500 24 -30 -16 C ATOM 5569 CE2 PHE C 235 -9.799 16.016 45.403 1.00 12.81 C ANISOU 5569 CE2 PHE C 235 1635 1638 1596 43 -56 10 C ATOM 5570 CZ PHE C 235 -10.077 16.078 46.754 1.00 13.06 C ANISOU 5570 CZ PHE C 235 1626 1706 1628 7 0 -12 C ATOM 5571 N ALA C 236 -14.538 19.670 45.195 1.00 10.41 N ANISOU 5571 N ALA C 236 1363 1334 1257 19 24 -17 N ATOM 5572 CA ALA C 236 -14.888 20.284 46.470 1.00 9.75 C ANISOU 5572 CA ALA C 236 1271 1228 1207 5 -6 14 C ATOM 5573 C ALA C 236 -16.121 19.586 47.037 1.00 10.01 C ANISOU 5573 C ALA C 236 1281 1301 1221 -23 -16 15 C ATOM 5574 O ALA C 236 -17.150 19.430 46.380 1.00 9.86 O ANISOU 5574 O ALA C 236 1331 1314 1102 3 -40 0 O ATOM 5575 CB ALA C 236 -15.115 21.777 46.309 1.00 9.85 C ANISOU 5575 CB ALA C 236 1327 1189 1225 -47 -24 -25 C ATOM 5576 N PHE C 237 -15.979 19.133 48.277 1.00 9.80 N ANISOU 5576 N PHE C 237 1251 1249 1223 -23 -45 20 N ATOM 5577 CA PHE C 237 -17.059 18.504 49.017 1.00 9.75 C ANISOU 5577 CA PHE C 237 1288 1233 1183 1 -7 7 C ATOM 5578 C PHE C 237 -17.357 19.289 50.295 1.00 9.62 C ANISOU 5578 C PHE C 237 1279 1192 1183 0 -23 25 C ATOM 5579 O PHE C 237 -16.410 19.692 50.978 1.00 9.82 O ANISOU 5579 O PHE C 237 1347 1218 1167 -43 -43 25 O ATOM 5580 CB PHE C 237 -16.658 17.076 49.398 1.00 10.92 C ANISOU 5580 CB PHE C 237 1494 1282 1373 57 -28 -6 C ATOM 5581 CG PHE C 237 -17.643 16.347 50.263 1.00 12.53 C ANISOU 5581 CG PHE C 237 1562 1561 1636 -13 51 52 C ATOM 5582 CD1 PHE C 237 -17.572 16.412 51.645 1.00 14.28 C ANISOU 5582 CD1 PHE C 237 1813 1885 1729 23 4 -27 C ATOM 5583 CD2 PHE C 237 -18.645 15.578 49.691 1.00 13.63 C ANISOU 5583 CD2 PHE C 237 1761 1657 1760 -31 -32 -51 C ATOM 5584 CE1 PHE C 237 -18.479 15.741 52.441 1.00 14.58 C ANISOU 5584 CE1 PHE C 237 1877 1827 1834 -11 -26 46 C ATOM 5585 CE2 PHE C 237 -19.543 14.892 50.487 1.00 14.60 C ANISOU 5585 CE2 PHE C 237 1820 1848 1878 -45 26 -7 C ATOM 5586 CZ PHE C 237 -19.469 14.974 51.862 1.00 15.00 C ANISOU 5586 CZ PHE C 237 1915 1870 1914 -8 -20 -12 C ATOM 5587 N ASN C 238 -18.632 19.484 50.604 1.00 9.62 N ANISOU 5587 N ASN C 238 1282 1180 1193 5 -22 54 N ATOM 5588 CA ASN C 238 -18.986 19.863 51.973 1.00 10.57 C ANISOU 5588 CA ASN C 238 1376 1347 1291 12 12 -12 C ATOM 5589 C ASN C 238 -20.241 19.124 52.426 1.00 11.16 C ANISOU 5589 C ASN C 238 1445 1424 1371 -55 -25 32 C ATOM 5590 O ASN C 238 -21.023 18.617 51.624 1.00 10.97 O ANISOU 5590 O ASN C 238 1492 1411 1265 -17 -30 24 O ATOM 5591 CB ASN C 238 -19.133 21.364 52.155 1.00 10.49 C ANISOU 5591 CB ASN C 238 1374 1335 1276 31 -29 0 C ATOM 5592 CG ASN C 238 -20.247 22.018 51.371 1.00 10.41 C ANISOU 5592 CG ASN C 238 1288 1360 1307 8 1 -1 C ATOM 5593 OD1 ASN C 238 -21.427 21.728 51.564 1.00 9.75 O ANISOU 5593 OD1 ASN C 238 1231 1344 1128 32 -108 -6 O ATOM 5594 ND2 ASN C 238 -19.854 22.933 50.494 1.00 11.33 N ANISOU 5594 ND2 ASN C 238 1561 1427 1315 23 -35 58 N ATOM 5595 N MET C 239 -20.401 19.034 53.744 1.00 11.36 N ANISOU 5595 N MET C 239 1426 1513 1378 -23 -13 -18 N ATOM 5596 CA MET C 239 -21.600 18.440 54.318 1.00 11.59 C ANISOU 5596 CA MET C 239 1475 1483 1444 -31 3 7 C ATOM 5597 C MET C 239 -21.920 19.111 55.651 1.00 12.10 C ANISOU 5597 C MET C 239 1575 1543 1480 2 -11 -6 C ATOM 5598 O MET C 239 -21.027 19.651 56.298 1.00 11.93 O ANISOU 5598 O MET C 239 1596 1504 1434 5 2 -26 O ATOM 5599 CB MET C 239 -21.427 16.938 54.552 1.00 13.07 C ANISOU 5599 CB MET C 239 1715 1555 1694 22 -10 22 C ATOM 5600 CG MET C 239 -20.268 16.623 55.492 1.00 14.07 C ANISOU 5600 CG MET C 239 1829 1744 1773 62 -69 17 C ATOM 5601 SD MET C 239 -20.079 14.854 55.753 1.00 15.77 S ANISOU 5601 SD MET C 239 2475 1759 1760 37 -159 12 S ATOM 5602 CE MET C 239 -21.244 14.568 57.081 1.00 19.57 C ANISOU 5602 CE MET C 239 2441 2510 2486 -42 80 52 C ATOM 5603 N ASP C 240 -23.186 19.042 56.026 1.00 13.12 N ANISOU 5603 N ASP C 240 1630 1728 1628 14 22 5 N ATOM 5604 CA ASP C 240 -23.580 19.438 57.382 1.00 13.67 C ANISOU 5604 CA ASP C 240 1775 1796 1622 11 -14 -11 C ATOM 5605 C ASP C 240 -23.189 18.309 58.330 1.00 14.11 C ANISOU 5605 C ASP C 240 1860 1762 1738 -8 -5 14 C ATOM 5606 O ASP C 240 -23.401 17.143 57.997 1.00 14.36 O ANISOU 5606 O ASP C 240 1917 1816 1725 -6 -56 -38 O ATOM 5607 CB ASP C 240 -25.075 19.705 57.452 1.00 14.88 C ANISOU 5607 CB ASP C 240 1833 1929 1892 12 11 3 C ATOM 5608 CG ASP C 240 -25.543 20.801 56.514 1.00 15.78 C ANISOU 5608 CG ASP C 240 2134 1954 1908 2 -5 4 C ATOM 5609 OD1 ASP C 240 -24.723 21.640 56.099 1.00 15.94 O ANISOU 5609 OD1 ASP C 240 2120 2002 1935 4 -18 19 O ATOM 5610 OD2 ASP C 240 -26.750 20.816 56.190 1.00 18.72 O ANISOU 5610 OD2 ASP C 240 2271 2421 2420 39 -42 -56 O ATOM 5611 N ILE C 241 -22.574 18.644 59.461 1.00 14.30 N ANISOU 5611 N ILE C 241 1889 1776 1770 -14 -28 -15 N ATOM 5612 CA ILE C 241 -22.203 17.595 60.414 1.00 14.87 C ANISOU 5612 CA ILE C 241 1981 1829 1841 26 -15 13 C ATOM 5613 C ILE C 241 -22.825 17.854 61.779 1.00 15.26 C ANISOU 5613 C ILE C 241 2007 1917 1875 15 -8 3 C ATOM 5614 O ILE C 241 -22.643 18.906 62.383 1.00 14.93 O ANISOU 5614 O ILE C 241 1972 1885 1816 -9 3 42 O ATOM 5615 CB ILE C 241 -20.685 17.400 60.489 1.00 16.46 C ANISOU 5615 CB ILE C 241 2049 2155 2050 33 -29 10 C ATOM 5616 CG1 ILE C 241 -20.310 16.366 61.563 1.00 17.10 C ANISOU 5616 CG1 ILE C 241 2228 2161 2107 22 -13 39 C ATOM 5617 CG2 ILE C 241 -19.949 18.700 60.742 1.00 18.07 C ANISOU 5617 CG2 ILE C 241 2314 2239 2313 -36 -15 27 C ATOM 5618 CD1 ILE C 241 -18.906 15.824 61.379 1.00 18.16 C ANISOU 5618 CD1 ILE C 241 2277 2336 2287 21 3 13 C ATOM 5619 N ASP C 242 -23.569 16.859 62.254 1.00 16.04 N ANISOU 5619 N ASP C 242 2088 2015 1991 -40 -26 31 N ATOM 5620 CA ASP C 242 -24.262 16.951 63.536 1.00 17.26 C ANISOU 5620 CA ASP C 242 2294 2165 2098 -10 51 -22 C ATOM 5621 C ASP C 242 -23.995 15.692 64.358 1.00 17.74 C ANISOU 5621 C ASP C 242 2311 2204 2226 24 9 3 C ATOM 5622 O ASP C 242 -24.687 15.392 65.328 1.00 18.92 O ANISOU 5622 O ASP C 242 2458 2371 2357 3 63 39 O ATOM 5623 CB ASP C 242 -25.757 17.122 63.311 1.00 21.21 C ANISOU 5623 CB ASP C 242 2499 2801 2761 84 34 67 C ATOM 5624 CG ASP C 242 -26.376 16.108 62.377 1.00 24.68 C ANISOU 5624 CG ASP C 242 3145 3111 3120 -96 -26 -71 C ATOM 5625 OD1 ASP C 242 -25.904 14.954 62.331 1.00 26.15 O ANISOU 5625 OD1 ASP C 242 3303 3240 3391 9 -29 6 O ATOM 5626 OD2 ASP C 242 -27.347 16.469 61.674 1.00 25.82 O ANISOU 5626 OD2 ASP C 242 3266 3284 3261 21 -18 28 O ATOM 5627 N ASN C 243 -22.994 14.943 63.917 1.00 17.06 N ANISOU 5627 N ASN C 243 2243 2107 2132 -9 -31 -6 N ATOM 5628 CA ASN C 243 -22.589 13.718 64.598 1.00 17.14 C ANISOU 5628 CA ASN C 243 2216 2147 2147 -2 -16 18 C ATOM 5629 C ASN C 243 -21.098 13.505 64.388 1.00 17.32 C ANISOU 5629 C ASN C 243 2230 2178 2173 1 2 20 C ATOM 5630 O ASN C 243 -20.619 13.334 63.266 1.00 17.53 O ANISOU 5630 O ASN C 243 2275 2233 2151 0 -15 13 O ATOM 5631 CB ASN C 243 -23.391 12.525 64.081 1.00 17.33 C ANISOU 5631 CB ASN C 243 2216 2201 2167 -32 19 -20 C ATOM 5632 CG ASN C 243 -23.176 11.249 64.866 1.00 18.75 C ANISOU 5632 CG ASN C 243 2414 2311 2400 33 -1 49 C ATOM 5633 OD1 ASN C 243 -22.078 10.946 65.333 1.00 18.92 O ANISOU 5633 OD1 ASN C 243 2410 2438 2340 -3 -4 13 O ATOM 5634 ND2 ASN C 243 -24.246 10.472 65.016 1.00 19.97 N ANISOU 5634 ND2 ASN C 243 2483 2474 2630 -25 -3 23 N ATOM 5635 N GLU C 244 -20.342 13.452 65.481 1.00 17.42 N ANISOU 5635 N GLU C 244 2238 2189 2193 -25 -6 -5 N ATOM 5636 CA GLU C 244 -18.902 13.262 65.435 1.00 18.13 C ANISOU 5636 CA GLU C 244 2284 2238 2368 9 44 -9 C ATOM 5637 C GLU C 244 -18.472 12.065 64.600 1.00 17.67 C ANISOU 5637 C GLU C 244 2263 2227 2225 12 -6 25 C ATOM 5638 O GLU C 244 -17.459 12.116 63.895 1.00 17.86 O ANISOU 5638 O GLU C 244 2284 2275 2225 22 -6 41 O ATOM 5639 CB GLU C 244 -18.357 13.101 66.860 1.00 22.36 C ANISOU 5639 CB GLU C 244 3041 2902 2553 17 -71 -7 C ATOM 5640 CG GLU C 244 -16.840 13.029 66.929 1.00 27.76 C ANISOU 5640 CG GLU C 244 3343 3522 3682 8 45 1 C ATOM 5641 CD GLU C 244 -16.345 13.112 68.363 1.00 31.70 C ANISOU 5641 CD GLU C 244 4035 4093 3917 12 -72 -21 C ATOM 5642 OE1 GLU C 244 -16.449 12.097 69.079 1.00 32.87 O ANISOU 5642 OE1 GLU C 244 4224 4148 4117 -25 -32 24 O ATOM 5643 OE2 GLU C 244 -15.869 14.198 68.751 1.00 32.46 O ANISOU 5643 OE2 GLU C 244 4137 4091 4104 -3 -43 14 O ATOM 5644 N SER C 245 -19.227 10.978 64.645 1.00 17.58 N ANISOU 5644 N SER C 245 2281 2221 2179 8 -23 -6 N ATOM 5645 CA SER C 245 -18.932 9.739 63.953 1.00 17.74 C ANISOU 5645 CA SER C 245 2318 2225 2198 18 -1 -4 C ATOM 5646 C SER C 245 -18.995 9.859 62.433 1.00 17.53 C ANISOU 5646 C SER C 245 2272 2199 2191 24 -19 12 C ATOM 5647 O SER C 245 -18.417 9.020 61.745 1.00 17.81 O ANISOU 5647 O SER C 245 2324 2234 2211 43 3 12 O ATOM 5648 CB ASER C 245 -19.900 8.635 64.400 0.50 18.66 C ANISOU 5648 CB ASER C 245 2383 2327 2381 -28 10 9 C ATOM 5649 CB BSER C 245 -19.915 8.646 64.396 0.50 18.33 C ANISOU 5649 CB BSER C 245 2334 2309 2321 -9 -6 4 C ATOM 5650 OG ASER C 245 -21.183 8.832 63.833 0.50 18.93 O ANISOU 5650 OG ASER C 245 2401 2357 2435 15 5 -22 O ATOM 5651 OG BSER C 245 -19.887 8.478 65.800 0.50 18.33 O ANISOU 5651 OG BSER C 245 2349 2299 2314 7 11 -7 O ATOM 5652 N LYS C 246 -19.686 10.857 61.902 1.00 16.86 N ANISOU 5652 N LYS C 246 2221 2122 2062 -33 1 10 N ATOM 5653 CA LYS C 246 -19.850 11.019 60.467 1.00 16.10 C ANISOU 5653 CA LYS C 246 2084 2015 2021 -77 0 -15 C ATOM 5654 C LYS C 246 -18.749 11.816 59.793 1.00 15.26 C ANISOU 5654 C LYS C 246 1968 1937 1895 -25 -46 -14 C ATOM 5655 O LYS C 246 -18.737 11.938 58.560 1.00 15.19 O ANISOU 5655 O LYS C 246 1982 1899 1891 -34 -37 -28 O ATOM 5656 CB LYS C 246 -21.216 11.663 60.182 1.00 17.56 C ANISOU 5656 CB LYS C 246 2269 2196 2209 88 -41 -61 C ATOM 5657 CG LYS C 246 -22.363 10.773 60.647 1.00 20.69 C ANISOU 5657 CG LYS C 246 2619 2601 2642 -94 95 29 C ATOM 5658 CD LYS C 246 -23.668 11.165 59.976 1.00 23.18 C ANISOU 5658 CD LYS C 246 2928 2984 2897 60 -75 7 C ATOM 5659 CE LYS C 246 -24.785 10.211 60.355 1.00 24.98 C ANISOU 5659 CE LYS C 246 3193 3138 3162 -59 36 0 C ATOM 5660 NZ LYS C 246 -26.073 10.608 59.719 1.00 26.41 N ANISOU 5660 NZ LYS C 246 3331 3358 3347 23 -33 6 N ATOM 5661 N LEU C 247 -17.750 12.289 60.545 1.00 14.42 N ANISOU 5661 N LEU C 247 1874 1806 1799 -8 -4 23 N ATOM 5662 CA LEU C 247 -16.693 13.103 59.965 1.00 14.55 C ANISOU 5662 CA LEU C 247 1834 1872 1823 -22 -31 17 C ATOM 5663 C LEU C 247 -15.959 12.457 58.808 1.00 14.92 C ANISOU 5663 C LEU C 247 1898 1904 1868 -11 -13 -5 C ATOM 5664 O LEU C 247 -15.719 13.129 57.797 1.00 14.96 O ANISOU 5664 O LEU C 247 1972 1860 1850 -11 -65 0 O ATOM 5665 CB LEU C 247 -15.704 13.606 61.025 1.00 14.36 C ANISOU 5665 CB LEU C 247 1878 1791 1787 -26 -8 -22 C ATOM 5666 CG LEU C 247 -14.705 14.662 60.544 1.00 14.43 C ANISOU 5666 CG LEU C 247 1822 1807 1853 6 -34 17 C ATOM 5667 CD1 LEU C 247 -15.424 15.883 59.985 1.00 13.45 C ANISOU 5667 CD1 LEU C 247 1759 1679 1672 -61 -44 -35 C ATOM 5668 CD2 LEU C 247 -13.759 15.071 61.667 1.00 14.97 C ANISOU 5668 CD2 LEU C 247 1918 1929 1840 -32 -31 -8 C ATOM 5669 N PRO C 248 -15.617 11.170 58.860 1.00 15.50 N ANISOU 5669 N PRO C 248 1987 1947 1957 23 -17 -4 N ATOM 5670 CA PRO C 248 -14.876 10.502 57.807 1.00 15.37 C ANISOU 5670 CA PRO C 248 1975 1962 1903 15 -37 4 C ATOM 5671 C PRO C 248 -15.571 10.398 56.463 1.00 14.60 C ANISOU 5671 C PRO C 248 1852 1850 1846 0 9 6 C ATOM 5672 O PRO C 248 -14.928 10.189 55.427 1.00 14.28 O ANISOU 5672 O PRO C 248 1873 1816 1737 8 -58 -14 O ATOM 5673 CB PRO C 248 -14.622 9.096 58.356 1.00 16.15 C ANISOU 5673 CB PRO C 248 2093 1999 2045 28 -11 31 C ATOM 5674 CG PRO C 248 -14.608 9.270 59.829 1.00 16.38 C ANISOU 5674 CG PRO C 248 2113 2052 2060 24 -12 -2 C ATOM 5675 CD PRO C 248 -15.530 10.414 60.143 1.00 16.13 C ANISOU 5675 CD PRO C 248 2096 2019 2013 22 -6 35 C ATOM 5676 N LEU C 249 -16.879 10.602 56.426 1.00 13.97 N ANISOU 5676 N LEU C 249 1819 1775 1715 -17 -44 39 N ATOM 5677 CA LEU C 249 -17.677 10.689 55.218 1.00 13.51 C ANISOU 5677 CA LEU C 249 1714 1692 1727 -22 -43 18 C ATOM 5678 C LEU C 249 -17.243 11.808 54.284 1.00 13.61 C ANISOU 5678 C LEU C 249 1772 1708 1693 -35 -28 4 C ATOM 5679 O LEU C 249 -17.425 11.744 53.066 1.00 13.74 O ANISOU 5679 O LEU C 249 1807 1705 1710 -32 -98 4 O ATOM 5680 CB LEU C 249 -19.151 10.913 55.589 1.00 13.14 C ANISOU 5680 CB LEU C 249 1728 1667 1598 -6 -3 -42 C ATOM 5681 CG LEU C 249 -19.830 9.761 56.337 1.00 14.12 C ANISOU 5681 CG LEU C 249 1864 1739 1761 -36 0 24 C ATOM 5682 CD1 LEU C 249 -21.259 10.119 56.706 1.00 15.89 C ANISOU 5682 CD1 LEU C 249 1963 2093 1980 3 1 -45 C ATOM 5683 CD2 LEU C 249 -19.794 8.490 55.495 1.00 14.64 C ANISOU 5683 CD2 LEU C 249 1902 1786 1872 -46 15 -33 C ATOM 5684 N ARG C 250 -16.618 12.853 54.823 1.00 13.39 N ANISOU 5684 N ARG C 250 1728 1665 1695 -12 -40 16 N ATOM 5685 CA ARG C 250 -15.996 13.916 54.051 1.00 13.59 C ANISOU 5685 CA ARG C 250 1726 1745 1694 11 0 51 C ATOM 5686 C ARG C 250 -14.993 13.387 53.032 1.00 13.71 C ANISOU 5686 C ARG C 250 1745 1743 1721 0 -8 11 C ATOM 5687 O ARG C 250 -14.794 14.026 51.992 1.00 14.12 O ANISOU 5687 O ARG C 250 1835 1823 1706 -30 -24 6 O ATOM 5688 CB ARG C 250 -15.337 14.938 54.995 1.00 15.59 C ANISOU 5688 CB ARG C 250 2094 1847 1981 -65 35 -103 C ATOM 5689 CG ARG C 250 -13.909 14.610 55.373 1.00 19.13 C ANISOU 5689 CG ARG C 250 2285 2357 2625 29 -5 53 C ATOM 5690 CD ARG C 250 -13.479 14.758 56.805 1.00 24.09 C ANISOU 5690 CD ARG C 250 3153 3126 2874 5 -19 -32 C ATOM 5691 NE ARG C 250 -13.071 16.052 57.262 1.00 25.28 N ANISOU 5691 NE ARG C 250 3223 3223 3158 -107 -14 -41 N ATOM 5692 CZ ARG C 250 -12.153 16.399 58.149 1.00 23.21 C ANISOU 5692 CZ ARG C 250 2973 2905 2942 13 25 69 C ATOM 5693 NH1 ARG C 250 -11.372 15.547 58.799 1.00 22.58 N ANISOU 5693 NH1 ARG C 250 2947 2781 2853 -3 34 -3 N ATOM 5694 NH2 ARG C 250 -12.015 17.699 58.371 1.00 22.56 N ANISOU 5694 NH2 ARG C 250 2926 2884 2762 32 -9 12 N ATOM 5695 N LYS C 251 -14.307 12.276 53.291 1.00 13.47 N ANISOU 5695 N LYS C 251 1722 1731 1667 -9 -9 13 N ATOM 5696 CA LYS C 251 -13.437 11.650 52.315 1.00 13.88 C ANISOU 5696 CA LYS C 251 1796 1721 1756 5 19 -19 C ATOM 5697 C LYS C 251 -14.101 10.466 51.615 1.00 14.10 C ANISOU 5697 C LYS C 251 1813 1753 1793 -5 -19 -12 C ATOM 5698 O LYS C 251 -13.857 10.269 50.422 1.00 14.72 O ANISOU 5698 O LYS C 251 1932 1831 1830 28 -8 -4 O ATOM 5699 CB LYS C 251 -12.115 11.196 52.936 1.00 15.40 C ANISOU 5699 CB LYS C 251 1908 1997 1949 39 -55 24 C ATOM 5700 CG LYS C 251 -11.238 12.338 53.429 1.00 16.61 C ANISOU 5700 CG LYS C 251 2222 2053 2037 -68 18 -38 C ATOM 5701 CD LYS C 251 -9.906 11.797 53.932 1.00 20.12 C ANISOU 5701 CD LYS C 251 2485 2586 2575 109 -47 33 C ATOM 5702 CE LYS C 251 -9.024 12.907 54.477 1.00 22.66 C ANISOU 5702 CE LYS C 251 2861 2807 2942 -81 -13 -28 C ATOM 5703 NZ LYS C 251 -7.801 12.351 55.119 1.00 23.67 N ANISOU 5703 NZ LYS C 251 2981 3040 2972 9 -31 5 N ATOM 5704 N SER C 252 -14.923 9.702 52.333 1.00 14.11 N ANISOU 5704 N SER C 252 1787 1771 1805 -24 -44 -29 N ATOM 5705 CA SER C 252 -15.455 8.470 51.750 1.00 14.42 C ANISOU 5705 CA SER C 252 1857 1782 1841 -27 -41 -20 C ATOM 5706 C SER C 252 -16.548 8.744 50.725 1.00 14.08 C ANISOU 5706 C SER C 252 1817 1747 1787 -6 -10 0 C ATOM 5707 O SER C 252 -16.643 7.984 49.755 1.00 14.37 O ANISOU 5707 O SER C 252 1885 1834 1742 13 -40 0 O ATOM 5708 CB SER C 252 -15.936 7.500 52.822 1.00 15.02 C ANISOU 5708 CB SER C 252 1949 1816 1941 -1 -4 28 C ATOM 5709 OG SER C 252 -17.107 7.932 53.480 1.00 15.33 O ANISOU 5709 OG SER C 252 2020 1939 1867 -18 40 0 O ATOM 5710 N ILE C 253 -17.353 9.788 50.900 1.00 13.88 N ANISOU 5710 N ILE C 253 1773 1769 1733 -1 -40 -15 N ATOM 5711 CA ILE C 253 -18.374 10.096 49.893 1.00 13.29 C ANISOU 5711 CA ILE C 253 1694 1689 1667 13 15 -16 C ATOM 5712 C ILE C 253 -17.741 10.531 48.583 1.00 13.10 C ANISOU 5712 C ILE C 253 1693 1655 1627 13 -18 -7 C ATOM 5713 O ILE C 253 -18.033 9.939 47.537 1.00 13.05 O ANISOU 5713 O ILE C 253 1720 1665 1573 29 -13 1 O ATOM 5714 CB ILE C 253 -19.447 11.069 50.396 1.00 12.47 C ANISOU 5714 CB ILE C 253 1634 1566 1539 -59 32 2 C ATOM 5715 CG1 ILE C 253 -20.281 10.367 51.476 1.00 11.16 C ANISOU 5715 CG1 ILE C 253 1370 1381 1488 -24 -52 -5 C ATOM 5716 CG2 ILE C 253 -20.348 11.545 49.262 1.00 13.55 C ANISOU 5716 CG2 ILE C 253 1748 1674 1725 29 -52 20 C ATOM 5717 CD1 ILE C 253 -21.252 11.266 52.208 1.00 12.65 C ANISOU 5717 CD1 ILE C 253 1595 1643 1569 48 40 -58 C ATOM 5718 N PRO C 254 -16.822 11.485 48.618 1.00 13.28 N ANISOU 5718 N PRO C 254 1734 1655 1656 5 -17 -11 N ATOM 5719 CA PRO C 254 -16.060 11.876 47.443 1.00 13.50 C ANISOU 5719 CA PRO C 254 1728 1694 1707 -15 -7 17 C ATOM 5720 C PRO C 254 -15.324 10.724 46.788 1.00 13.87 C ANISOU 5720 C PRO C 254 1793 1749 1728 12 -22 -12 C ATOM 5721 O PRO C 254 -15.361 10.552 45.567 1.00 14.14 O ANISOU 5721 O PRO C 254 1832 1821 1718 -13 21 24 O ATOM 5722 CB PRO C 254 -15.089 12.924 47.976 1.00 13.54 C ANISOU 5722 CB PRO C 254 1716 1717 1713 -7 -1 -5 C ATOM 5723 CG PRO C 254 -15.827 13.558 49.099 1.00 13.25 C ANISOU 5723 CG PRO C 254 1674 1670 1690 4 -1 0 C ATOM 5724 CD PRO C 254 -16.674 12.474 49.719 1.00 13.29 C ANISOU 5724 CD PRO C 254 1735 1617 1698 0 -21 -9 C ATOM 5725 N THR C 255 -14.659 9.895 47.594 1.00 13.86 N ANISOU 5725 N THR C 255 1801 1736 1729 7 -53 -30 N ATOM 5726 CA THR C 255 -13.938 8.736 47.087 1.00 14.31 C ANISOU 5726 CA THR C 255 1848 1752 1838 -35 5 -81 C ATOM 5727 C THR C 255 -14.866 7.785 46.344 1.00 13.67 C ANISOU 5727 C THR C 255 1766 1703 1724 4 -9 -15 C ATOM 5728 O THR C 255 -14.510 7.347 45.248 1.00 13.27 O ANISOU 5728 O THR C 255 1722 1615 1706 3 1 6 O ATOM 5729 CB THR C 255 -13.187 8.006 48.216 1.00 17.81 C ANISOU 5729 CB THR C 255 2297 2272 2197 72 -131 109 C ATOM 5730 OG1 THR C 255 -12.215 8.917 48.751 1.00 19.33 O ANISOU 5730 OG1 THR C 255 2445 2478 2420 -5 -65 -51 O ATOM 5731 CG2 THR C 255 -12.466 6.773 47.696 1.00 20.31 C ANISOU 5731 CG2 THR C 255 2608 2496 2614 81 6 -51 C ATOM 5732 N LYS C 256 -16.034 7.489 46.902 1.00 13.56 N ANISOU 5732 N LYS C 256 1766 1659 1726 8 -32 7 N ATOM 5733 CA LYS C 256 -16.992 6.616 46.227 1.00 14.44 C ANISOU 5733 CA LYS C 256 1875 1767 1846 -23 -107 -6 C ATOM 5734 C LYS C 256 -17.481 7.186 44.905 1.00 14.36 C ANISOU 5734 C LYS C 256 1894 1771 1790 4 -24 -9 C ATOM 5735 O LYS C 256 -17.529 6.460 43.904 1.00 14.16 O ANISOU 5735 O LYS C 256 1852 1736 1793 -28 -101 -12 O ATOM 5736 CB LYS C 256 -18.163 6.310 47.174 1.00 17.38 C ANISOU 5736 CB LYS C 256 2146 2273 2186 -64 108 -98 C ATOM 5737 CG LYS C 256 -17.710 5.329 48.246 1.00 21.75 C ANISOU 5737 CG LYS C 256 2879 2627 2756 56 -136 75 C ATOM 5738 CD LYS C 256 -18.715 5.120 49.361 1.00 25.50 C ANISOU 5738 CD LYS C 256 3185 3264 3240 -43 116 -48 C ATOM 5739 CE LYS C 256 -18.128 4.176 50.404 1.00 28.33 C ANISOU 5739 CE LYS C 256 3611 3524 3629 33 -85 53 C ATOM 5740 NZ LYS C 256 -18.989 4.067 51.611 1.00 30.32 N ANISOU 5740 NZ LYS C 256 3888 3820 3813 6 39 2 N ATOM 5741 N ILE C 257 -17.810 8.475 44.885 1.00 13.90 N ANISOU 5741 N ILE C 257 1801 1750 1729 10 -13 26 N ATOM 5742 CA ILE C 257 -18.165 9.148 43.637 1.00 13.44 C ANISOU 5742 CA ILE C 257 1720 1662 1726 37 -14 -2 C ATOM 5743 C ILE C 257 -17.025 9.131 42.634 1.00 13.54 C ANISOU 5743 C ILE C 257 1730 1698 1716 5 -18 9 C ATOM 5744 O ILE C 257 -17.241 8.814 41.458 1.00 13.80 O ANISOU 5744 O ILE C 257 1783 1736 1725 -10 -28 -1 O ATOM 5745 CB ILE C 257 -18.648 10.587 43.896 1.00 12.25 C ANISOU 5745 CB ILE C 257 1556 1586 1514 -18 14 36 C ATOM 5746 CG1 ILE C 257 -19.930 10.551 44.732 1.00 11.82 C ANISOU 5746 CG1 ILE C 257 1482 1505 1504 -16 -14 -49 C ATOM 5747 CG2 ILE C 257 -18.887 11.326 42.590 1.00 11.61 C ANISOU 5747 CG2 ILE C 257 1505 1455 1450 4 25 -17 C ATOM 5748 CD1 ILE C 257 -20.387 11.893 45.263 1.00 12.57 C ANISOU 5748 CD1 ILE C 257 1599 1548 1629 38 4 -30 C ATOM 5749 N MET C 258 -15.796 9.420 43.062 1.00 13.55 N ANISOU 5749 N MET C 258 1729 1676 1744 -24 -12 -23 N ATOM 5750 CA MET C 258 -14.658 9.357 42.144 1.00 14.17 C ANISOU 5750 CA MET C 258 1794 1808 1783 -13 15 -10 C ATOM 5751 C MET C 258 -14.382 7.939 41.663 1.00 14.98 C ANISOU 5751 C MET C 258 1896 1885 1910 6 -14 -73 C ATOM 5752 O MET C 258 -13.967 7.772 40.512 1.00 15.13 O ANISOU 5752 O MET C 258 1945 1888 1916 2 -26 -71 O ATOM 5753 CB MET C 258 -13.429 10.037 42.762 1.00 14.50 C ANISOU 5753 CB MET C 258 1837 1881 1792 -25 -41 34 C ATOM 5754 CG MET C 258 -13.642 11.549 42.788 1.00 15.68 C ANISOU 5754 CG MET C 258 2010 1944 2002 41 -22 -21 C ATOM 5755 SD MET C 258 -12.240 12.528 43.329 1.00 17.38 S ANISOU 5755 SD MET C 258 2262 2252 2088 -135 -32 -175 S ATOM 5756 CE MET C 258 -12.016 11.928 44.996 1.00 18.79 C ANISOU 5756 CE MET C 258 2428 2393 2320 7 -52 63 C ATOM 5757 N GLU C 259 -14.625 6.930 42.488 1.00 16.08 N ANISOU 5757 N GLU C 259 2055 2028 2026 -10 -38 5 N ATOM 5758 CA GLU C 259 -14.583 5.539 42.054 1.00 18.10 C ANISOU 5758 CA GLU C 259 2314 2183 2380 17 -26 -131 C ATOM 5759 C GLU C 259 -15.584 5.284 40.929 1.00 18.51 C ANISOU 5759 C GLU C 259 2372 2307 2356 3 -31 -41 C ATOM 5760 O GLU C 259 -15.238 4.779 39.860 1.00 18.66 O ANISOU 5760 O GLU C 259 2399 2327 2365 -5 -21 -56 O ATOM 5761 CB GLU C 259 -14.920 4.587 43.197 1.00 22.43 C ANISOU 5761 CB GLU C 259 3023 2627 2873 -62 180 106 C ATOM 5762 CG GLU C 259 -13.906 4.455 44.312 1.00 28.66 C ANISOU 5762 CG GLU C 259 3563 3683 3643 55 -211 -67 C ATOM 5763 CD GLU C 259 -14.451 3.700 45.511 1.00 33.09 C ANISOU 5763 CD GLU C 259 4289 4138 4144 -8 110 88 C ATOM 5764 OE1 GLU C 259 -15.548 3.106 45.418 1.00 34.12 O ANISOU 5764 OE1 GLU C 259 4346 4272 4344 -4 -20 26 O ATOM 5765 OE2 GLU C 259 -13.778 3.697 46.563 1.00 34.62 O ANISOU 5765 OE2 GLU C 259 4445 4366 4341 -1 -28 21 O ATOM 5766 N SER C 260 -16.837 5.666 41.161 1.00 18.76 N ANISOU 5766 N SER C 260 2412 2332 2383 13 0 -21 N ATOM 5767 CA SER C 260 -17.899 5.501 40.176 1.00 19.69 C ANISOU 5767 CA SER C 260 2547 2461 2475 -36 -71 -10 C ATOM 5768 C SER C 260 -17.604 6.201 38.857 1.00 19.67 C ANISOU 5768 C SER C 260 2521 2462 2491 -13 -23 -9 C ATOM 5769 O SER C 260 -17.983 5.717 37.784 1.00 19.73 O ANISOU 5769 O SER C 260 2501 2473 2521 -21 -43 -27 O ATOM 5770 CB SER C 260 -19.232 6.010 40.735 1.00 22.64 C ANISOU 5770 CB SER C 260 2725 2935 2942 71 -4 -78 C ATOM 5771 OG SER C 260 -19.718 5.167 41.764 1.00 25.60 O ANISOU 5771 OG SER C 260 3251 3224 3252 -18 38 58 O ATOM 5772 N GLU C 261 -16.913 7.336 38.897 1.00 19.47 N ANISOU 5772 N GLU C 261 2448 2468 2481 -2 -20 -15 N ATOM 5773 CA GLU C 261 -16.526 8.075 37.710 1.00 19.75 C ANISOU 5773 CA GLU C 261 2488 2542 2474 1 -22 -2 C ATOM 5774 C GLU C 261 -15.269 7.555 37.031 1.00 19.54 C ANISOU 5774 C GLU C 261 2479 2478 2469 7 -41 -3 C ATOM 5775 O GLU C 261 -14.865 8.091 35.994 1.00 20.26 O ANISOU 5775 O GLU C 261 2615 2565 2516 -18 -17 2 O ATOM 5776 CB GLU C 261 -16.329 9.557 38.067 1.00 21.62 C ANISOU 5776 CB GLU C 261 2857 2633 2723 -54 -51 -17 C ATOM 5777 CG GLU C 261 -17.631 10.296 38.343 1.00 24.34 C ANISOU 5777 CG GLU C 261 3047 3027 3174 32 72 -36 C ATOM 5778 CD GLU C 261 -18.439 10.490 37.071 1.00 27.11 C ANISOU 5778 CD GLU C 261 3466 3436 3398 52 -90 10 C ATOM 5779 OE1 GLU C 261 -17.865 10.990 36.083 1.00 28.63 O ANISOU 5779 OE1 GLU C 261 3685 3676 3519 15 21 11 O ATOM 5780 OE2 GLU C 261 -19.632 10.137 37.063 1.00 28.35 O ANISOU 5780 OE2 GLU C 261 3566 3566 3639 -7 -52 26 O ATOM 5781 N GLY C 262 -14.594 6.564 37.599 1.00 18.94 N ANISOU 5781 N GLY C 262 2418 2378 2399 -9 -13 -46 N ATOM 5782 CA GLY C 262 -13.451 5.934 36.964 1.00 18.58 C ANISOU 5782 CA GLY C 262 2375 2348 2336 -18 -29 -12 C ATOM 5783 C GLY C 262 -12.130 6.601 37.304 1.00 17.90 C ANISOU 5783 C GLY C 262 2330 2244 2226 13 -10 -20 C ATOM 5784 O GLY C 262 -11.090 6.241 36.747 1.00 18.18 O ANISOU 5784 O GLY C 262 2379 2319 2211 47 -14 -41 O ATOM 5785 N ILE C 263 -12.150 7.572 38.215 1.00 17.04 N ANISOU 5785 N ILE C 263 2197 2172 2107 0 -5 20 N ATOM 5786 CA ILE C 263 -10.931 8.261 38.618 1.00 16.69 C ANISOU 5786 CA ILE C 263 2147 2110 2084 27 27 -16 C ATOM 5787 C ILE C 263 -10.116 7.361 39.542 1.00 17.09 C ANISOU 5787 C ILE C 263 2196 2127 2171 27 -4 2 C ATOM 5788 O ILE C 263 -8.907 7.240 39.381 1.00 17.30 O ANISOU 5788 O ILE C 263 2221 2145 2206 70 0 37 O ATOM 5789 CB ILE C 263 -11.220 9.599 39.315 1.00 15.45 C ANISOU 5789 CB ILE C 263 1936 2001 1934 10 -44 43 C ATOM 5790 CG1 ILE C 263 -11.936 10.555 38.349 1.00 14.86 C ANISOU 5790 CG1 ILE C 263 1929 1831 1887 3 -16 -8 C ATOM 5791 CG2 ILE C 263 -9.945 10.248 39.836 1.00 15.49 C ANISOU 5791 CG2 ILE C 263 1945 1982 1956 -9 -9 23 C ATOM 5792 CD1 ILE C 263 -12.537 11.764 39.037 1.00 15.10 C ANISOU 5792 CD1 ILE C 263 1948 1890 1898 36 12 -2 C ATOM 5793 N ILE C 264 -10.798 6.773 40.518 1.00 17.60 N ANISOU 5793 N ILE C 264 2253 2224 2211 -21 15 4 N ATOM 5794 CA ILE C 264 -10.141 5.851 41.443 1.00 18.63 C ANISOU 5794 CA ILE C 264 2382 2354 2342 9 -20 57 C ATOM 5795 C ILE C 264 -10.236 4.432 40.895 1.00 19.84 C ANISOU 5795 C ILE C 264 2584 2443 2514 -32 -12 11 C ATOM 5796 O ILE C 264 -11.327 3.940 40.612 1.00 19.83 O ANISOU 5796 O ILE C 264 2579 2434 2521 -24 -3 19 O ATOM 5797 CB ILE C 264 -10.735 5.969 42.853 1.00 18.54 C ANISOU 5797 CB ILE C 264 2391 2296 2358 13 -1 26 C ATOM 5798 CG1 ILE C 264 -10.303 7.309 43.462 1.00 18.80 C ANISOU 5798 CG1 ILE C 264 2422 2329 2394 6 -8 2 C ATOM 5799 CG2 ILE C 264 -10.304 4.816 43.745 1.00 18.13 C ANISOU 5799 CG2 ILE C 264 2303 2286 2298 8 -12 9 C ATOM 5800 CD1 ILE C 264 -11.068 7.732 44.690 1.00 19.27 C ANISOU 5800 CD1 ILE C 264 2427 2473 2420 21 -11 -5 C ATOM 5801 N GLY C 265 -9.081 3.799 40.722 1.00 21.40 N ANISOU 5801 N GLY C 265 2675 2697 2757 35 16 46 N ATOM 5802 CA GLY C 265 -9.023 2.453 40.167 1.00 22.97 C ANISOU 5802 CA GLY C 265 2949 2813 2967 18 -7 -26 C ATOM 5803 C GLY C 265 -8.854 2.474 38.653 1.00 24.56 C ANISOU 5803 C GLY C 265 3171 3104 3057 -1 18 12 C ATOM 5804 O GLY C 265 -9.028 3.505 38.004 1.00 25.13 O ANISOU 5804 O GLY C 265 3253 3136 3160 27 11 33 O ATOM 5805 N GLY C 266 -8.512 1.317 38.091 1.00 25.32 N ANISOU 5805 N GLY C 266 3257 3129 3233 18 2 4 N ATOM 5806 CA GLY C 266 -8.345 1.182 36.651 1.00 26.15 C ANISOU 5806 CA GLY C 266 3355 3283 3297 21 24 5 C ATOM 5807 C GLY C 266 -9.470 0.345 36.048 1.00 27.04 C ANISOU 5807 C GLY C 266 3417 3375 3483 -13 -25 28 C ATOM 5808 O GLY C 266 -10.504 0.166 36.725 1.00 27.24 O ANISOU 5808 O GLY C 266 3442 3401 3508 -10 -18 42 O ATOM 5809 OXT GLY C 266 -9.316 -0.123 34.900 1.00 29.28 O ANISOU 5809 OXT GLY C 266 3850 3665 3610 -6 -12 -46 O TER 5810 GLY C 266 ATOM 5811 N ILE D 22 20.383 3.866 -12.390 1.00 19.75 N ANISOU 5811 N ILE D 22 2536 2488 2478 9 13 -42 N ATOM 5812 CA ILE D 22 20.210 4.987 -11.414 1.00 19.14 C ANISOU 5812 CA ILE D 22 2445 2397 2430 -8 -5 1 C ATOM 5813 C ILE D 22 21.492 5.797 -11.315 1.00 19.09 C ANISOU 5813 C ILE D 22 2423 2417 2415 8 -3 -7 C ATOM 5814 O ILE D 22 22.596 5.248 -11.284 1.00 19.55 O ANISOU 5814 O ILE D 22 2473 2488 2465 59 -21 -17 O ATOM 5815 CB ILE D 22 19.730 4.464 -10.051 1.00 19.44 C ANISOU 5815 CB ILE D 22 2495 2473 2419 22 17 -11 C ATOM 5816 CG1 ILE D 22 19.576 5.602 -9.036 1.00 19.89 C ANISOU 5816 CG1 ILE D 22 2569 2519 2469 11 -10 -42 C ATOM 5817 CG2 ILE D 22 20.662 3.383 -9.519 1.00 19.56 C ANISOU 5817 CG2 ILE D 22 2529 2497 2405 23 12 -4 C ATOM 5818 CD1 ILE D 22 18.886 5.184 -7.754 1.00 20.07 C ANISOU 5818 CD1 ILE D 22 2544 2525 2556 -28 5 6 C ATOM 5819 N THR D 23 21.354 7.118 -11.323 1.00 18.58 N ANISOU 5819 N THR D 23 2340 2393 2328 -1 -6 1 N ATOM 5820 CA THR D 23 22.490 8.026 -11.315 1.00 18.99 C ANISOU 5820 CA THR D 23 2385 2414 2415 -17 -4 -67 C ATOM 5821 C THR D 23 22.498 8.849 -10.027 1.00 18.64 C ANISOU 5821 C THR D 23 2320 2401 2361 -2 10 -28 C ATOM 5822 O THR D 23 21.441 9.105 -9.451 1.00 17.88 O ANISOU 5822 O THR D 23 2261 2364 2170 -29 -28 -27 O ATOM 5823 CB THR D 23 22.489 9.001 -12.508 1.00 21.79 C ANISOU 5823 CB THR D 23 2869 2724 2686 -24 -12 101 C ATOM 5824 OG1 THR D 23 21.373 9.893 -12.394 1.00 23.20 O ANISOU 5824 OG1 THR D 23 2938 2939 2936 19 -28 -7 O ATOM 5825 CG2 THR D 23 22.400 8.263 -13.834 1.00 22.42 C ANISOU 5825 CG2 THR D 23 2873 2839 2805 -20 -2 -11 C ATOM 5826 N GLU D 24 23.686 9.263 -9.604 1.00 18.42 N ANISOU 5826 N GLU D 24 2318 2358 2323 -16 22 -28 N ATOM 5827 CA GLU D 24 23.795 10.108 -8.420 1.00 18.35 C ANISOU 5827 CA GLU D 24 2345 2303 2324 -4 40 -15 C ATOM 5828 C GLU D 24 23.720 11.580 -8.807 1.00 18.04 C ANISOU 5828 C GLU D 24 2302 2282 2271 -4 30 -28 C ATOM 5829 O GLU D 24 24.359 12.050 -9.745 1.00 18.48 O ANISOU 5829 O GLU D 24 2374 2340 2309 -48 59 -40 O ATOM 5830 CB GLU D 24 25.076 9.820 -7.637 1.00 20.03 C ANISOU 5830 CB GLU D 24 2449 2558 2603 23 -47 37 C ATOM 5831 CG GLU D 24 25.028 10.379 -6.220 1.00 22.64 C ANISOU 5831 CG GLU D 24 2925 2883 2796 -17 36 -77 C ATOM 5832 CD GLU D 24 26.163 9.881 -5.347 1.00 24.61 C ANISOU 5832 CD GLU D 24 3128 3112 3111 60 -59 21 C ATOM 5833 OE1 GLU D 24 26.030 8.805 -4.726 1.00 24.27 O ANISOU 5833 OE1 GLU D 24 3057 3133 3032 -14 -2 -4 O ATOM 5834 OE2 GLU D 24 27.191 10.589 -5.288 1.00 26.46 O ANISOU 5834 OE2 GLU D 24 3257 3352 3445 -32 -39 9 O ATOM 5835 N ASN D 25 22.894 12.313 -8.073 1.00 17.49 N ANISOU 5835 N ASN D 25 2242 2225 2180 -15 13 9 N ATOM 5836 CA ASN D 25 22.790 13.760 -8.194 1.00 17.29 C ANISOU 5836 CA ASN D 25 2219 2210 2139 -43 32 -9 C ATOM 5837 C ASN D 25 23.335 14.380 -6.910 1.00 17.18 C ANISOU 5837 C ASN D 25 2177 2204 2148 -28 12 -6 C ATOM 5838 O ASN D 25 22.656 14.389 -5.881 1.00 16.67 O ANISOU 5838 O ASN D 25 2071 2148 2115 -60 -15 -6 O ATOM 5839 CB ASN D 25 21.340 14.161 -8.441 1.00 18.78 C ANISOU 5839 CB ASN D 25 2330 2488 2316 26 -36 -14 C ATOM 5840 CG ASN D 25 21.113 15.633 -8.685 1.00 21.19 C ANISOU 5840 CG ASN D 25 2721 2620 2710 43 18 66 C ATOM 5841 OD1 ASN D 25 21.720 16.492 -8.043 1.00 23.37 O ANISOU 5841 OD1 ASN D 25 2981 2916 2982 -59 -55 -59 O ATOM 5842 ND2 ASN D 25 20.221 15.963 -9.613 1.00 20.80 N ANISOU 5842 ND2 ASN D 25 2662 2631 2608 -27 37 2 N ATOM 5843 N THR D 26 24.567 14.880 -6.960 1.00 17.27 N ANISOU 5843 N THR D 26 2189 2201 2171 -34 10 23 N ATOM 5844 CA THR D 26 25.226 15.407 -5.771 1.00 17.51 C ANISOU 5844 CA THR D 26 2263 2210 2179 -12 -5 5 C ATOM 5845 C THR D 26 24.543 16.634 -5.197 1.00 17.52 C ANISOU 5845 C THR D 26 2213 2233 2210 -5 6 11 C ATOM 5846 O THR D 26 24.513 16.820 -3.977 1.00 17.79 O ANISOU 5846 O THR D 26 2246 2297 2217 -21 24 18 O ATOM 5847 CB THR D 26 26.702 15.778 -6.037 1.00 19.01 C ANISOU 5847 CB THR D 26 2313 2420 2490 -27 -9 -27 C ATOM 5848 OG1 THR D 26 26.751 16.739 -7.097 1.00 20.95 O ANISOU 5848 OG1 THR D 26 2718 2650 2592 -18 35 25 O ATOM 5849 CG2 THR D 26 27.496 14.534 -6.385 1.00 19.59 C ANISOU 5849 CG2 THR D 26 2418 2481 2544 -3 36 -40 C ATOM 5850 N SER D 27 23.960 17.476 -6.043 1.00 17.59 N ANISOU 5850 N SER D 27 2231 2230 2223 -3 14 18 N ATOM 5851 CA SER D 27 23.276 18.685 -5.622 1.00 17.50 C ANISOU 5851 CA SER D 27 2181 2228 2240 -35 46 -10 C ATOM 5852 C SER D 27 22.109 18.408 -4.686 1.00 16.63 C ANISOU 5852 C SER D 27 2120 2078 2122 -38 -5 -4 C ATOM 5853 O SER D 27 21.816 19.233 -3.819 1.00 16.63 O ANISOU 5853 O SER D 27 2113 2097 2110 -29 13 10 O ATOM 5854 CB SER D 27 22.789 19.495 -6.828 1.00 19.44 C ANISOU 5854 CB SER D 27 2512 2486 2388 -7 -38 71 C ATOM 5855 OG SER D 27 21.626 18.931 -7.405 1.00 19.79 O ANISOU 5855 OG SER D 27 2539 2563 2416 -41 -16 47 O ATOM 5856 N TRP D 28 21.470 17.244 -4.784 1.00 15.62 N ANISOU 5856 N TRP D 28 1975 2039 1923 -13 10 -2 N ATOM 5857 CA TRP D 28 20.380 16.871 -3.907 1.00 14.85 C ANISOU 5857 CA TRP D 28 1908 1915 1818 -21 -41 7 C ATOM 5858 C TRP D 28 20.782 16.550 -2.474 1.00 14.32 C ANISOU 5858 C TRP D 28 1789 1858 1795 -7 -21 5 C ATOM 5859 O TRP D 28 19.888 16.327 -1.651 1.00 14.44 O ANISOU 5859 O TRP D 28 1789 1880 1817 -8 -10 27 O ATOM 5860 CB TRP D 28 19.610 15.669 -4.463 1.00 14.76 C ANISOU 5860 CB TRP D 28 1888 1853 1868 -12 -31 38 C ATOM 5861 CG TRP D 28 18.876 15.928 -5.742 1.00 14.60 C ANISOU 5861 CG TRP D 28 1892 1854 1803 6 -9 -23 C ATOM 5862 CD1 TRP D 28 18.751 17.106 -6.420 1.00 15.23 C ANISOU 5862 CD1 TRP D 28 1982 1891 1913 -17 -18 1 C ATOM 5863 CD2 TRP D 28 18.116 14.961 -6.480 1.00 14.73 C ANISOU 5863 CD2 TRP D 28 1871 1878 1847 -20 12 -25 C ATOM 5864 NE1 TRP D 28 17.979 16.933 -7.540 1.00 15.44 N ANISOU 5864 NE1 TRP D 28 2040 1963 1863 -3 -9 31 N ATOM 5865 CE2 TRP D 28 17.578 15.624 -7.602 1.00 15.84 C ANISOU 5865 CE2 TRP D 28 2021 1976 2022 12 -56 45 C ATOM 5866 CE3 TRP D 28 17.848 13.599 -6.311 1.00 15.05 C ANISOU 5866 CE3 TRP D 28 1915 1902 1901 -3 6 12 C ATOM 5867 CZ2 TRP D 28 16.790 14.973 -8.549 1.00 16.17 C ANISOU 5867 CZ2 TRP D 28 2088 2033 2024 -40 -9 -20 C ATOM 5868 CZ3 TRP D 28 17.062 12.958 -7.249 1.00 15.52 C ANISOU 5868 CZ3 TRP D 28 1942 1982 1974 -22 -10 -22 C ATOM 5869 CH2 TRP D 28 16.545 13.643 -8.357 1.00 16.08 C ANISOU 5869 CH2 TRP D 28 2044 2011 2056 34 -9 17 C ATOM 5870 N ASN D 29 22.065 16.563 -2.131 1.00 13.68 N ANISOU 5870 N ASN D 29 1755 1727 1715 13 0 0 N ATOM 5871 CA ASN D 29 22.481 16.468 -0.740 1.00 13.71 C ANISOU 5871 CA ASN D 29 1741 1740 1730 9 -19 18 C ATOM 5872 C ASN D 29 22.336 17.771 0.029 1.00 14.09 C ANISOU 5872 C ASN D 29 1795 1790 1767 0 10 -14 C ATOM 5873 O ASN D 29 22.497 17.797 1.252 1.00 14.05 O ANISOU 5873 O ASN D 29 1796 1786 1756 -11 33 1 O ATOM 5874 CB ASN D 29 23.938 15.982 -0.678 1.00 13.82 C ANISOU 5874 CB ASN D 29 1721 1726 1804 -11 49 8 C ATOM 5875 CG ASN D 29 24.009 14.527 -1.109 1.00 14.32 C ANISOU 5875 CG ASN D 29 1864 1762 1813 -33 1 -16 C ATOM 5876 OD1 ASN D 29 23.681 13.648 -0.311 1.00 14.11 O ANISOU 5876 OD1 ASN D 29 1874 1751 1735 -34 -28 -34 O ATOM 5877 ND2 ASN D 29 24.418 14.298 -2.349 1.00 14.67 N ANISOU 5877 ND2 ASN D 29 1790 1929 1856 -10 33 16 N ATOM 5878 N LYS D 30 22.047 18.870 -0.656 1.00 14.37 N ANISOU 5878 N LYS D 30 1801 1832 1826 -13 54 35 N ATOM 5879 CA LYS D 30 21.972 20.194 -0.074 1.00 15.71 C ANISOU 5879 CA LYS D 30 1978 1967 2025 -38 53 -87 C ATOM 5880 C LYS D 30 21.141 20.264 1.200 1.00 15.46 C ANISOU 5880 C LYS D 30 1958 1943 1973 -17 19 1 C ATOM 5881 O LYS D 30 21.633 20.768 2.211 1.00 15.63 O ANISOU 5881 O LYS D 30 1974 1985 1980 -11 29 -15 O ATOM 5882 CB LYS D 30 21.399 21.191 -1.090 1.00 19.30 C ANISOU 5882 CB LYS D 30 2457 2527 2350 45 -61 166 C ATOM 5883 CG LYS D 30 21.282 22.616 -0.570 1.00 24.20 C ANISOU 5883 CG LYS D 30 3110 2907 3179 -33 53 -151 C ATOM 5884 CD LYS D 30 20.757 23.542 -1.659 1.00 28.32 C ANISOU 5884 CD LYS D 30 3608 3662 3490 50 -50 120 C ATOM 5885 CE LYS D 30 20.824 25.001 -1.236 1.00 32.00 C ANISOU 5885 CE LYS D 30 4102 3931 4125 -21 15 -74 C ATOM 5886 NZ LYS D 30 20.331 25.898 -2.322 1.00 33.58 N ANISOU 5886 NZ LYS D 30 4301 4196 4261 18 -11 25 N ATOM 5887 N GLU D 31 19.894 19.793 1.160 1.00 15.56 N ANISOU 5887 N GLU D 31 1960 1960 1993 8 -14 10 N ATOM 5888 CA GLU D 31 19.028 19.959 2.330 1.00 16.02 C ANISOU 5888 CA GLU D 31 2084 1984 2019 -3 40 10 C ATOM 5889 C GLU D 31 19.373 18.968 3.431 1.00 15.97 C ANISOU 5889 C GLU D 31 2065 1976 2028 15 4 -13 C ATOM 5890 O GLU D 31 19.267 19.291 4.619 1.00 16.35 O ANISOU 5890 O GLU D 31 2104 2040 2066 10 73 -27 O ATOM 5891 CB GLU D 31 17.557 19.895 1.928 1.00 18.66 C ANISOU 5891 CB GLU D 31 2213 2452 2427 -39 -20 -45 C ATOM 5892 CG GLU D 31 17.128 20.951 0.929 1.00 20.97 C ANISOU 5892 CG GLU D 31 2628 2714 2628 48 -17 79 C ATOM 5893 CD GLU D 31 17.275 22.387 1.374 1.00 23.50 C ANISOU 5893 CD GLU D 31 2970 2896 3064 -19 -19 -62 C ATOM 5894 OE1 GLU D 31 17.462 22.675 2.573 1.00 23.99 O ANISOU 5894 OE1 GLU D 31 3109 2951 3056 -4 2 9 O ATOM 5895 OE2 GLU D 31 17.198 23.276 0.495 1.00 25.50 O ANISOU 5895 OE2 GLU D 31 3317 3145 3225 -15 -5 63 O ATOM 5896 N PHE D 32 19.853 17.781 3.067 1.00 15.11 N ANISOU 5896 N PHE D 32 1932 1903 1904 -31 -3 -14 N ATOM 5897 CA PHE D 32 20.379 16.836 4.046 1.00 15.15 C ANISOU 5897 CA PHE D 32 1926 1903 1926 4 0 -28 C ATOM 5898 C PHE D 32 21.514 17.464 4.851 1.00 15.45 C ANISOU 5898 C PHE D 32 1949 1986 1934 -24 -8 -9 C ATOM 5899 O PHE D 32 21.535 17.431 6.081 1.00 15.49 O ANISOU 5899 O PHE D 32 1920 2033 1931 -26 -20 -5 O ATOM 5900 CB PHE D 32 20.888 15.560 3.370 1.00 14.74 C ANISOU 5900 CB PHE D 32 1849 1876 1875 -47 6 -38 C ATOM 5901 CG PHE D 32 19.805 14.784 2.675 1.00 14.09 C ANISOU 5901 CG PHE D 32 1718 1848 1789 -6 37 -2 C ATOM 5902 CD1 PHE D 32 19.021 13.894 3.390 1.00 13.68 C ANISOU 5902 CD1 PHE D 32 1727 1731 1741 1 -25 -3 C ATOM 5903 CD2 PHE D 32 19.574 14.941 1.320 1.00 15.25 C ANISOU 5903 CD2 PHE D 32 1908 2017 1870 -51 -32 21 C ATOM 5904 CE1 PHE D 32 18.019 13.182 2.762 1.00 14.07 C ANISOU 5904 CE1 PHE D 32 1746 1814 1784 -28 -39 12 C ATOM 5905 CE2 PHE D 32 18.578 14.218 0.686 1.00 14.90 C ANISOU 5905 CE2 PHE D 32 1924 1891 1847 -46 -1 11 C ATOM 5906 CZ PHE D 32 17.802 13.338 1.408 1.00 14.28 C ANISOU 5906 CZ PHE D 32 1856 1804 1767 -15 2 -45 C ATOM 5907 N SER D 33 22.460 18.070 4.137 1.00 15.47 N ANISOU 5907 N SER D 33 1939 1999 1940 -14 17 -29 N ATOM 5908 CA SER D 33 23.603 18.710 4.767 1.00 15.83 C ANISOU 5908 CA SER D 33 2000 2023 1992 -48 -9 -19 C ATOM 5909 C SER D 33 23.197 19.895 5.629 1.00 16.11 C ANISOU 5909 C SER D 33 2050 2040 2030 -24 19 -10 C ATOM 5910 O SER D 33 23.710 20.076 6.738 1.00 16.38 O ANISOU 5910 O SER D 33 2097 2077 2052 -17 4 -23 O ATOM 5911 CB SER D 33 24.606 19.154 3.691 1.00 16.73 C ANISOU 5911 CB SER D 33 2127 2163 2066 -13 57 64 C ATOM 5912 OG SER D 33 25.763 19.666 4.336 1.00 18.88 O ANISOU 5912 OG SER D 33 2370 2459 2346 -110 -39 -24 O ATOM 5913 N ALA D 34 22.251 20.701 5.161 1.00 16.83 N ANISOU 5913 N ALA D 34 2125 2128 2141 10 0 3 N ATOM 5914 CA ALA D 34 21.809 21.895 5.873 1.00 17.75 C ANISOU 5914 CA ALA D 34 2285 2201 2258 28 -8 -43 C ATOM 5915 C ALA D 34 21.107 21.565 7.183 1.00 18.75 C ANISOU 5915 C ALA D 34 2393 2379 2352 -7 38 -19 C ATOM 5916 O ALA D 34 21.174 22.329 8.153 1.00 19.15 O ANISOU 5916 O ALA D 34 2447 2449 2380 -25 8 -50 O ATOM 5917 CB ALA D 34 20.886 22.712 4.977 1.00 17.90 C ANISOU 5917 CB ALA D 34 2242 2273 2288 34 15 -18 C ATOM 5918 N GLU D 35 20.425 20.427 7.235 1.00 19.25 N ANISOU 5918 N GLU D 35 2479 2387 2449 -12 9 -25 N ATOM 5919 CA GLU D 35 19.712 19.984 8.424 1.00 19.81 C ANISOU 5919 CA GLU D 35 2578 2480 2470 9 28 0 C ATOM 5920 C GLU D 35 20.512 18.959 9.217 1.00 19.71 C ANISOU 5920 C GLU D 35 2530 2473 2486 -3 5 -22 C ATOM 5921 O GLU D 35 20.044 18.421 10.224 1.00 20.22 O ANISOU 5921 O GLU D 35 2623 2566 2492 -23 27 -42 O ATOM 5922 CB GLU D 35 18.360 19.382 8.029 1.00 21.63 C ANISOU 5922 CB GLU D 35 2690 2769 2759 -91 42 -79 C ATOM 5923 CG GLU D 35 17.473 20.280 7.193 1.00 24.72 C ANISOU 5923 CG GLU D 35 3100 3151 3143 -2 -80 101 C ATOM 5924 CD GLU D 35 16.894 21.468 7.930 1.00 27.50 C ANISOU 5924 CD GLU D 35 3480 3407 3563 30 38 -66 C ATOM 5925 OE1 GLU D 35 17.016 21.547 9.169 1.00 29.37 O ANISOU 5925 OE1 GLU D 35 3721 3786 3654 10 20 -11 O ATOM 5926 OE2 GLU D 35 16.296 22.348 7.271 1.00 28.18 O ANISOU 5926 OE2 GLU D 35 3597 3528 3583 30 11 8 O ATOM 5927 N ALA D 36 21.716 18.647 8.756 1.00 19.48 N ANISOU 5927 N ALA D 36 2500 2457 2446 -5 -17 -6 N ATOM 5928 CA ALA D 36 22.587 17.665 9.384 1.00 19.41 C ANISOU 5928 CA ALA D 36 2490 2421 2465 -7 -3 -11 C ATOM 5929 C ALA D 36 21.874 16.336 9.590 1.00 19.03 C ANISOU 5929 C ALA D 36 2442 2429 2360 -24 -20 -20 C ATOM 5930 O ALA D 36 21.790 15.788 10.691 1.00 19.47 O ANISOU 5930 O ALA D 36 2536 2473 2388 -29 -52 13 O ATOM 5931 CB ALA D 36 23.136 18.206 10.699 1.00 20.44 C ANISOU 5931 CB ALA D 36 2649 2613 2504 -17 -49 -11 C ATOM 5932 N VAL D 37 21.314 15.798 8.505 1.00 17.95 N ANISOU 5932 N VAL D 37 2273 2254 2293 -29 13 21 N ATOM 5933 CA VAL D 37 20.619 14.522 8.559 1.00 17.21 C ANISOU 5933 CA VAL D 37 2222 2153 2166 31 11 -28 C ATOM 5934 C VAL D 37 21.172 13.562 7.508 1.00 16.09 C ANISOU 5934 C VAL D 37 2051 2040 2023 -13 -39 16 C ATOM 5935 O VAL D 37 21.637 13.970 6.446 1.00 16.39 O ANISOU 5935 O VAL D 37 2048 2120 2059 -26 -20 9 O ATOM 5936 CB VAL D 37 19.098 14.644 8.407 1.00 18.38 C ANISOU 5936 CB VAL D 37 2264 2311 2410 -16 -1 -14 C ATOM 5937 CG1 VAL D 37 18.467 15.242 9.662 1.00 19.72 C ANISOU 5937 CG1 VAL D 37 2539 2489 2466 0 52 -25 C ATOM 5938 CG2 VAL D 37 18.720 15.474 7.191 1.00 19.58 C ANISOU 5938 CG2 VAL D 37 2504 2498 2436 6 -5 8 C ATOM 5939 N ASN D 38 21.154 12.284 7.858 1.00 15.08 N ANISOU 5939 N ASN D 38 1922 1968 1841 -29 -32 -59 N ATOM 5940 CA ASN D 38 21.544 11.225 6.933 1.00 14.93 C ANISOU 5940 CA ASN D 38 1858 1961 1854 -62 -23 -70 C ATOM 5941 C ASN D 38 20.283 10.629 6.315 1.00 13.87 C ANISOU 5941 C ASN D 38 1777 1839 1654 -30 -1 -14 C ATOM 5942 O ASN D 38 19.373 10.223 7.037 1.00 13.51 O ANISOU 5942 O ASN D 38 1680 1902 1553 -20 -78 -18 O ATOM 5943 CB ASN D 38 22.353 10.146 7.653 1.00 17.91 C ANISOU 5943 CB ASN D 38 2349 2169 2287 127 -33 46 C ATOM 5944 CG ASN D 38 23.737 10.646 8.027 1.00 21.57 C ANISOU 5944 CG ASN D 38 2598 2755 2843 -41 -63 -39 C ATOM 5945 OD1 ASN D 38 24.425 11.247 7.200 1.00 22.93 O ANISOU 5945 OD1 ASN D 38 2826 2950 2935 -37 -8 43 O ATOM 5946 ND2 ASN D 38 24.150 10.403 9.260 1.00 23.36 N ANISOU 5946 ND2 ASN D 38 2979 2986 2911 -7 -24 17 N ATOM 5947 N GLY D 39 20.231 10.607 4.984 1.00 13.00 N ANISOU 5947 N GLY D 39 1636 1690 1615 -38 -20 7 N ATOM 5948 CA GLY D 39 19.071 9.990 4.340 1.00 12.27 C ANISOU 5948 CA GLY D 39 1589 1597 1476 -20 13 3 C ATOM 5949 C GLY D 39 19.277 9.912 2.832 1.00 11.87 C ANISOU 5949 C GLY D 39 1494 1562 1455 -25 -13 0 C ATOM 5950 O GLY D 39 20.327 10.291 2.319 1.00 11.51 O ANISOU 5950 O GLY D 39 1457 1556 1359 -6 -31 -1 O ATOM 5951 N VAL D 40 18.221 9.457 2.162 1.00 11.69 N ANISOU 5951 N VAL D 40 1481 1524 1438 22 -11 -34 N ATOM 5952 CA VAL D 40 18.281 9.314 0.712 1.00 10.74 C ANISOU 5952 CA VAL D 40 1314 1386 1380 32 -24 7 C ATOM 5953 C VAL D 40 16.949 9.702 0.083 1.00 10.08 C ANISOU 5953 C VAL D 40 1266 1294 1272 -7 10 9 C ATOM 5954 O VAL D 40 15.890 9.500 0.675 1.00 9.37 O ANISOU 5954 O VAL D 40 1214 1262 1083 -37 -43 -7 O ATOM 5955 CB VAL D 40 18.677 7.880 0.326 1.00 10.69 C ANISOU 5955 CB VAL D 40 1332 1345 1385 -42 -27 -20 C ATOM 5956 CG1 VAL D 40 17.625 6.872 0.767 1.00 9.69 C ANISOU 5956 CG1 VAL D 40 1295 1246 1139 37 5 10 C ATOM 5957 CG2 VAL D 40 18.947 7.769 -1.165 1.00 11.93 C ANISOU 5957 CG2 VAL D 40 1554 1543 1437 -39 11 8 C ATOM 5958 N PHE D 41 17.041 10.316 -1.087 1.00 9.78 N ANISOU 5958 N PHE D 41 1257 1276 1185 1 -27 -44 N ATOM 5959 CA PHE D 41 15.868 10.545 -1.932 1.00 9.67 C ANISOU 5959 CA PHE D 41 1242 1230 1201 32 -12 -3 C ATOM 5960 C PHE D 41 16.111 9.859 -3.272 1.00 9.53 C ANISOU 5960 C PHE D 41 1218 1239 1163 -15 -25 17 C ATOM 5961 O PHE D 41 17.190 10.019 -3.848 1.00 9.75 O ANISOU 5961 O PHE D 41 1220 1377 1107 2 -47 -35 O ATOM 5962 CB PHE D 41 15.637 12.041 -2.122 1.00 10.29 C ANISOU 5962 CB PHE D 41 1334 1249 1325 0 -42 28 C ATOM 5963 CG PHE D 41 14.375 12.405 -2.852 1.00 10.40 C ANISOU 5963 CG PHE D 41 1304 1308 1340 9 -40 -40 C ATOM 5964 CD1 PHE D 41 13.143 12.008 -2.359 1.00 11.15 C ANISOU 5964 CD1 PHE D 41 1378 1501 1357 -9 4 -20 C ATOM 5965 CD2 PHE D 41 14.418 13.149 -4.018 1.00 11.85 C ANISOU 5965 CD2 PHE D 41 1574 1474 1456 -22 -24 17 C ATOM 5966 CE1 PHE D 41 11.969 12.335 -3.011 1.00 11.04 C ANISOU 5966 CE1 PHE D 41 1389 1434 1373 37 -13 -73 C ATOM 5967 CE2 PHE D 41 13.247 13.486 -4.676 1.00 13.10 C ANISOU 5967 CE2 PHE D 41 1601 1682 1696 40 -31 6 C ATOM 5968 CZ PHE D 41 12.030 13.082 -4.172 1.00 12.72 C ANISOU 5968 CZ PHE D 41 1703 1566 1563 -27 16 26 C ATOM 5969 N VAL D 42 15.136 9.086 -3.733 1.00 9.38 N ANISOU 5969 N VAL D 42 1259 1155 1150 -10 -23 20 N ATOM 5970 CA VAL D 42 15.198 8.480 -5.060 1.00 10.14 C ANISOU 5970 CA VAL D 42 1355 1294 1203 3 -19 -7 C ATOM 5971 C VAL D 42 14.024 9.036 -5.866 1.00 10.39 C ANISOU 5971 C VAL D 42 1317 1342 1289 -23 -40 -26 C ATOM 5972 O VAL D 42 12.899 9.080 -5.367 1.00 10.47 O ANISOU 5972 O VAL D 42 1362 1405 1213 -13 -28 -17 O ATOM 5973 CB VAL D 42 15.129 6.948 -5.026 1.00 11.33 C ANISOU 5973 CB VAL D 42 1469 1334 1500 37 16 -32 C ATOM 5974 CG1 VAL D 42 15.144 6.366 -6.436 1.00 12.18 C ANISOU 5974 CG1 VAL D 42 1591 1559 1479 12 -45 -3 C ATOM 5975 CG2 VAL D 42 16.273 6.337 -4.226 1.00 11.68 C ANISOU 5975 CG2 VAL D 42 1540 1512 1388 22 -10 -1 C ATOM 5976 N LEU D 43 14.305 9.499 -7.072 1.00 10.94 N ANISOU 5976 N LEU D 43 1417 1419 1319 1 -25 0 N ATOM 5977 CA LEU D 43 13.272 10.119 -7.908 1.00 11.53 C ANISOU 5977 CA LEU D 43 1453 1481 1447 28 -49 8 C ATOM 5978 C LEU D 43 13.388 9.556 -9.319 1.00 12.12 C ANISOU 5978 C LEU D 43 1559 1583 1462 7 -19 19 C ATOM 5979 O LEU D 43 14.494 9.541 -9.860 1.00 12.77 O ANISOU 5979 O LEU D 43 1587 1756 1510 18 -13 -1 O ATOM 5980 CB LEU D 43 13.453 11.635 -7.927 1.00 12.07 C ANISOU 5980 CB LEU D 43 1561 1507 1520 25 21 42 C ATOM 5981 CG LEU D 43 12.450 12.437 -8.761 1.00 12.47 C ANISOU 5981 CG LEU D 43 1550 1665 1524 44 -20 23 C ATOM 5982 CD1 LEU D 43 11.043 12.280 -8.207 1.00 12.02 C ANISOU 5982 CD1 LEU D 43 1506 1566 1496 -15 -53 -14 C ATOM 5983 CD2 LEU D 43 12.855 13.905 -8.800 1.00 15.19 C ANISOU 5983 CD2 LEU D 43 1958 1832 1982 -41 -16 8 C ATOM 5984 N CYS D 44 12.290 9.061 -9.873 1.00 12.28 N ANISOU 5984 N CYS D 44 1573 1574 1518 9 -39 29 N ATOM 5985 CA CYS D 44 12.323 8.442 -11.193 1.00 12.95 C ANISOU 5985 CA CYS D 44 1647 1723 1552 11 -28 1 C ATOM 5986 C CYS D 44 11.265 9.089 -12.083 1.00 13.23 C ANISOU 5986 C CYS D 44 1671 1727 1628 21 -33 26 C ATOM 5987 O CYS D 44 10.100 9.129 -11.693 1.00 13.62 O ANISOU 5987 O CYS D 44 1726 1858 1590 35 7 61 O ATOM 5988 CB CYS D 44 12.074 6.936 -11.122 1.00 15.24 C ANISOU 5988 CB CYS D 44 2072 1798 1922 26 -11 -46 C ATOM 5989 SG CYS D 44 13.033 6.086 -9.847 1.00 17.23 S ANISOU 5989 SG CYS D 44 2377 2179 1990 32 -135 58 S ATOM 5990 N LYS D 45 11.682 9.607 -13.231 1.00 13.12 N ANISOU 5990 N LYS D 45 1660 1715 1609 19 -9 -24 N ATOM 5991 CA LYS D 45 10.731 10.212 -14.163 1.00 13.17 C ANISOU 5991 CA LYS D 45 1684 1670 1651 29 -17 -18 C ATOM 5992 C LYS D 45 10.234 9.155 -15.139 1.00 13.00 C ANISOU 5992 C LYS D 45 1679 1660 1601 23 -6 4 C ATOM 5993 O LYS D 45 11.042 8.466 -15.767 1.00 12.76 O ANISOU 5993 O LYS D 45 1683 1579 1588 36 -35 12 O ATOM 5994 CB LYS D 45 11.397 11.364 -14.916 1.00 14.62 C ANISOU 5994 CB LYS D 45 1876 1801 1877 -60 61 16 C ATOM 5995 CG LYS D 45 10.521 12.003 -15.985 1.00 16.88 C ANISOU 5995 CG LYS D 45 2134 2209 2072 125 -56 -13 C ATOM 5996 CD LYS D 45 11.262 13.151 -16.660 1.00 20.46 C ANISOU 5996 CD LYS D 45 2628 2501 2645 -98 80 14 C ATOM 5997 CE LYS D 45 10.373 13.872 -17.658 1.00 23.28 C ANISOU 5997 CE LYS D 45 2946 2973 2926 65 -72 25 C ATOM 5998 NZ LYS D 45 11.106 14.967 -18.358 1.00 25.05 N ANISOU 5998 NZ LYS D 45 3225 3092 3200 -33 22 20 N ATOM 5999 N SER D 46 8.928 8.972 -15.245 1.00 13.45 N ANISOU 5999 N SER D 46 1709 1690 1712 -4 -17 37 N ATOM 6000 CA SER D 46 8.284 8.088 -16.195 1.00 14.26 C ANISOU 6000 CA SER D 46 1825 1787 1806 -24 -47 -17 C ATOM 6001 C SER D 46 8.247 6.624 -15.769 1.00 14.81 C ANISOU 6001 C SER D 46 1938 1823 1864 -15 -14 -16 C ATOM 6002 O SER D 46 7.190 5.994 -15.819 1.00 15.38 O ANISOU 6002 O SER D 46 1953 1934 1957 -36 24 14 O ATOM 6003 CB SER D 46 8.916 8.174 -17.592 1.00 16.45 C ANISOU 6003 CB SER D 46 2134 2169 1945 10 58 -29 C ATOM 6004 OG SER D 46 8.745 9.477 -18.117 1.00 18.62 O ANISOU 6004 OG SER D 46 2445 2297 2333 -16 -1 66 O ATOM 6005 N SER D 47 9.393 6.067 -15.419 1.00 15.20 N ANISOU 6005 N SER D 47 1968 1900 1910 4 -27 -40 N ATOM 6006 CA SER D 47 9.514 4.687 -14.991 1.00 15.80 C ANISOU 6006 CA SER D 47 2069 1956 1980 11 9 -3 C ATOM 6007 C SER D 47 10.743 4.530 -14.103 1.00 16.50 C ANISOU 6007 C SER D 47 2110 2114 2044 -2 -9 -40 C ATOM 6008 O SER D 47 11.581 5.430 -14.023 1.00 16.27 O ANISOU 6008 O SER D 47 2141 2058 1982 6 -44 -17 O ATOM 6009 CB SER D 47 9.662 3.755 -16.199 1.00 15.43 C ANISOU 6009 CB SER D 47 1901 1973 1988 -18 1 -37 C ATOM 6010 OG SER D 47 10.969 3.856 -16.754 1.00 14.52 O ANISOU 6010 OG SER D 47 1899 1873 1746 -11 -6 -20 O ATOM 6011 N SER D 48 10.927 3.331 -13.560 1.00 17.71 N ANISOU 6011 N SER D 48 2330 2180 2218 -12 39 13 N ATOM 6012 CA SER D 48 12.094 3.011 -12.749 1.00 19.36 C ANISOU 6012 CA SER D 48 2463 2432 2459 -13 -67 28 C ATOM 6013 C SER D 48 13.363 2.745 -13.543 1.00 20.81 C ANISOU 6013 C SER D 48 2608 2605 2694 18 28 -11 C ATOM 6014 O SER D 48 14.408 2.432 -12.958 1.00 21.18 O ANISOU 6014 O SER D 48 2663 2650 2733 20 -14 -2 O ATOM 6015 CB SER D 48 11.787 1.794 -11.863 1.00 19.13 C ANISOU 6015 CB SER D 48 2439 2418 2413 23 -33 16 C ATOM 6016 OG SER D 48 11.455 0.674 -12.666 1.00 19.65 O ANISOU 6016 OG SER D 48 2504 2435 2527 24 -24 -9 O ATOM 6017 N LYS D 49 13.349 2.901 -14.858 1.00 22.15 N ANISOU 6017 N LYS D 49 2863 2766 2787 -3 -7 25 N ATOM 6018 CA LYS D 49 14.545 2.857 -15.682 1.00 23.44 C ANISOU 6018 CA LYS D 49 2916 2934 3056 19 64 48 C ATOM 6019 C LYS D 49 15.253 4.207 -15.737 1.00 23.26 C ANISOU 6019 C LYS D 49 2928 2912 2996 20 12 -8 C ATOM 6020 O LYS D 49 16.357 4.325 -16.270 1.00 23.49 O ANISOU 6020 O LYS D 49 2939 2987 2999 -2 -2 -2 O ATOM 6021 CB LYS D 49 14.189 2.405 -17.102 1.00 27.82 C ANISOU 6021 CB LYS D 49 3622 3665 3281 75 -30 -64 C ATOM 6022 CG LYS D 49 13.323 1.164 -17.196 1.00 32.38 C ANISOU 6022 CG LYS D 49 4064 4072 4167 -143 35 -84 C ATOM 6023 CD LYS D 49 13.878 -0.021 -16.427 1.00 36.16 C ANISOU 6023 CD LYS D 49 4709 4448 4582 12 -75 77 C ATOM 6024 CE LYS D 49 15.173 -0.545 -17.021 1.00 39.11 C ANISOU 6024 CE LYS D 49 4891 4971 4999 0 51 -43 C ATOM 6025 NZ LYS D 49 15.765 -1.625 -16.183 1.00 40.49 N ANISOU 6025 NZ LYS D 49 5154 5078 5151 11 -12 16 N ATOM 6026 N SER D 50 14.623 5.241 -15.197 1.00 22.69 N ANISOU 6026 N SER D 50 2885 2862 2876 -30 1 -16 N ATOM 6027 CA SER D 50 15.142 6.599 -15.246 1.00 21.98 C ANISOU 6027 CA SER D 50 2803 2827 2723 -28 21 -70 C ATOM 6028 C SER D 50 15.153 7.223 -13.855 1.00 20.73 C ANISOU 6028 C SER D 50 2601 2672 2603 31 -31 11 C ATOM 6029 O SER D 50 14.330 8.089 -13.554 1.00 20.85 O ANISOU 6029 O SER D 50 2631 2706 2583 48 -29 3 O ATOM 6030 CB SER D 50 14.288 7.431 -16.207 1.00 24.53 C ANISOU 6030 CB SER D 50 3124 3155 3040 96 -60 53 C ATOM 6031 OG SER D 50 14.824 8.733 -16.365 1.00 27.79 O ANISOU 6031 OG SER D 50 3607 3389 3562 -55 -2 1 O ATOM 6032 N CYS D 51 16.084 6.780 -13.007 1.00 19.33 N ANISOU 6032 N CYS D 51 2461 2508 2376 -8 38 -71 N ATOM 6033 CA CYS D 51 16.117 7.247 -11.627 1.00 17.33 C ANISOU 6033 CA CYS D 51 2111 2204 2270 -51 -12 -29 C ATOM 6034 C CYS D 51 17.390 8.024 -11.298 1.00 15.48 C ANISOU 6034 C CYS D 51 1987 1979 1917 26 28 -52 C ATOM 6035 O CYS D 51 18.449 7.843 -11.887 1.00 15.22 O ANISOU 6035 O CYS D 51 1928 2006 1848 -7 -9 -38 O ATOM 6036 CB CYS D 51 15.985 6.088 -10.635 1.00 18.62 C ANISOU 6036 CB CYS D 51 2355 2353 2367 3 -3 52 C ATOM 6037 SG CYS D 51 14.500 5.085 -10.829 1.00 19.12 S ANISOU 6037 SG CYS D 51 2433 2346 2486 -2 -63 -147 S ATOM 6038 N ALA D 52 17.255 8.896 -10.308 1.00 13.78 N ANISOU 6038 N ALA D 52 1702 1772 1762 -41 -2 19 N ATOM 6039 CA ALA D 52 18.382 9.638 -9.757 1.00 13.05 C ANISOU 6039 CA ALA D 52 1653 1730 1574 1 -3 -2 C ATOM 6040 C ALA D 52 18.263 9.653 -8.234 1.00 12.25 C ANISOU 6040 C ALA D 52 1520 1599 1537 -22 14 0 C ATOM 6041 O ALA D 52 17.175 9.440 -7.702 1.00 11.35 O ANISOU 6041 O ALA D 52 1438 1510 1365 1 -41 -48 O ATOM 6042 CB ALA D 52 18.431 11.055 -10.296 1.00 14.16 C ANISOU 6042 CB ALA D 52 1829 1771 1781 -1 -23 13 C ATOM 6043 N THR D 53 19.387 9.895 -7.567 1.00 12.15 N ANISOU 6043 N THR D 53 1570 1569 1478 -60 -1 -20 N ATOM 6044 CA THR D 53 19.380 9.887 -6.104 1.00 12.27 C ANISOU 6044 CA THR D 53 1609 1564 1487 -43 -17 3 C ATOM 6045 C THR D 53 20.516 10.748 -5.574 1.00 12.43 C ANISOU 6045 C THR D 53 1626 1580 1517 -50 -5 -34 C ATOM 6046 O THR D 53 21.529 10.909 -6.258 1.00 12.96 O ANISOU 6046 O THR D 53 1677 1685 1561 -66 25 -56 O ATOM 6047 CB THR D 53 19.517 8.447 -5.575 1.00 12.00 C ANISOU 6047 CB THR D 53 1546 1570 1443 26 7 4 C ATOM 6048 OG1 THR D 53 19.513 8.450 -4.143 1.00 11.89 O ANISOU 6048 OG1 THR D 53 1561 1525 1430 34 -8 -9 O ATOM 6049 CG2 THR D 53 20.797 7.795 -6.073 1.00 11.81 C ANISOU 6049 CG2 THR D 53 1511 1489 1489 18 -24 32 C ATOM 6050 N ASN D 54 20.382 11.252 -4.350 1.00 11.79 N ANISOU 6050 N ASN D 54 1555 1477 1447 -46 -9 19 N ATOM 6051 CA ASN D 54 21.501 11.957 -3.725 1.00 12.00 C ANISOU 6051 CA ASN D 54 1558 1487 1513 -41 -3 -18 C ATOM 6052 C ASN D 54 22.608 11.021 -3.260 1.00 12.59 C ANISOU 6052 C ASN D 54 1584 1592 1608 -4 10 6 C ATOM 6053 O ASN D 54 23.737 11.466 -3.047 1.00 12.85 O ANISOU 6053 O ASN D 54 1635 1608 1641 -38 -22 -8 O ATOM 6054 CB ASN D 54 21.009 12.782 -2.528 1.00 11.84 C ANISOU 6054 CB ASN D 54 1464 1533 1502 -24 18 -18 C ATOM 6055 CG ASN D 54 20.509 11.897 -1.402 1.00 12.81 C ANISOU 6055 CG ASN D 54 1655 1663 1548 -41 -14 36 C ATOM 6056 OD1 ASN D 54 19.587 11.108 -1.605 1.00 13.39 O ANISOU 6056 OD1 ASN D 54 1703 1724 1661 -83 24 -18 O ATOM 6057 ND2 ASN D 54 21.127 12.023 -0.234 1.00 12.15 N ANISOU 6057 ND2 ASN D 54 1547 1590 1477 -29 34 25 N ATOM 6058 N ASP D 55 22.291 9.748 -3.034 1.00 12.79 N ANISOU 6058 N ASP D 55 1658 1576 1625 -7 22 -36 N ATOM 6059 CA ASP D 55 23.260 8.811 -2.483 1.00 13.87 C ANISOU 6059 CA ASP D 55 1736 1717 1815 29 -13 1 C ATOM 6060 C ASP D 55 23.003 7.404 -3.004 1.00 13.79 C ANISOU 6060 C ASP D 55 1736 1711 1793 9 -2 23 C ATOM 6061 O ASP D 55 22.064 6.720 -2.605 1.00 12.73 O ANISOU 6061 O ASP D 55 1676 1559 1603 56 0 -28 O ATOM 6062 CB ASP D 55 23.224 8.846 -0.953 1.00 16.75 C ANISOU 6062 CB ASP D 55 2242 2185 1939 -42 24 -21 C ATOM 6063 CG ASP D 55 24.432 8.158 -0.344 1.00 19.36 C ANISOU 6063 CG ASP D 55 2478 2394 2486 124 -13 49 C ATOM 6064 OD1 ASP D 55 24.501 6.914 -0.382 1.00 17.79 O ANISOU 6064 OD1 ASP D 55 2191 2321 2248 7 -79 50 O ATOM 6065 OD2 ASP D 55 25.316 8.884 0.154 1.00 22.56 O ANISOU 6065 OD2 ASP D 55 2787 2847 2939 -48 -123 -34 O ATOM 6066 N LEU D 56 23.859 6.971 -3.928 1.00 14.50 N ANISOU 6066 N LEU D 56 1840 1849 1821 26 30 9 N ATOM 6067 CA LEU D 56 23.735 5.667 -4.558 1.00 15.08 C ANISOU 6067 CA LEU D 56 1942 1875 1912 -5 -42 1 C ATOM 6068 C LEU D 56 23.761 4.519 -3.560 1.00 14.82 C ANISOU 6068 C LEU D 56 1892 1882 1857 7 -13 -5 C ATOM 6069 O LEU D 56 22.929 3.610 -3.624 1.00 15.33 O ANISOU 6069 O LEU D 56 1946 1966 1914 -29 -48 -21 O ATOM 6070 CB LEU D 56 24.872 5.473 -5.575 1.00 17.41 C ANISOU 6070 CB LEU D 56 2149 2240 2225 1 115 -81 C ATOM 6071 CG LEU D 56 24.727 6.276 -6.870 1.00 20.56 C ANISOU 6071 CG LEU D 56 2699 2608 2505 17 -41 64 C ATOM 6072 CD1 LEU D 56 26.006 6.188 -7.689 1.00 22.71 C ANISOU 6072 CD1 LEU D 56 2807 2949 2874 -18 48 7 C ATOM 6073 CD2 LEU D 56 23.537 5.772 -7.677 1.00 21.08 C ANISOU 6073 CD2 LEU D 56 2674 2694 2643 -26 10 -18 C ATOM 6074 N ALA D 57 24.707 4.551 -2.621 1.00 14.40 N ANISOU 6074 N ALA D 57 1818 1836 1818 29 27 5 N ATOM 6075 CA ALA D 57 24.808 3.484 -1.631 1.00 14.29 C ANISOU 6075 CA ALA D 57 1809 1817 1804 8 25 -2 C ATOM 6076 C ALA D 57 23.542 3.385 -0.790 1.00 13.62 C ANISOU 6076 C ALA D 57 1732 1705 1737 14 -23 -16 C ATOM 6077 O ALA D 57 22.998 2.291 -0.599 1.00 13.87 O ANISOU 6077 O ALA D 57 1783 1719 1769 -2 -45 -9 O ATOM 6078 CB ALA D 57 26.026 3.698 -0.745 1.00 14.96 C ANISOU 6078 CB ALA D 57 1855 1942 1887 -21 -21 8 C ATOM 6079 N ARG D 58 23.042 4.523 -0.297 1.00 12.73 N ANISOU 6079 N ARG D 58 1594 1697 1544 -31 -11 -30 N ATOM 6080 CA ARG D 58 21.882 4.474 0.586 1.00 11.97 C ANISOU 6080 CA ARG D 58 1520 1532 1497 -10 -34 -58 C ATOM 6081 C ARG D 58 20.593 4.176 -0.164 1.00 12.22 C ANISOU 6081 C ARG D 58 1522 1604 1518 -16 -34 3 C ATOM 6082 O ARG D 58 19.667 3.600 0.413 1.00 11.94 O ANISOU 6082 O ARG D 58 1497 1553 1486 -41 -93 9 O ATOM 6083 CB ARG D 58 21.733 5.744 1.429 1.00 10.67 C ANISOU 6083 CB ARG D 58 1275 1412 1368 20 18 39 C ATOM 6084 CG ARG D 58 20.643 5.566 2.475 1.00 9.80 C ANISOU 6084 CG ARG D 58 1254 1248 1221 64 -18 23 C ATOM 6085 CD ARG D 58 20.644 6.663 3.529 1.00 10.58 C ANISOU 6085 CD ARG D 58 1380 1302 1341 14 -66 -35 C ATOM 6086 NE ARG D 58 19.457 6.498 4.370 1.00 12.40 N ANISOU 6086 NE ARG D 58 1455 1659 1597 -28 7 -38 N ATOM 6087 CZ ARG D 58 19.410 6.589 5.689 1.00 13.38 C ANISOU 6087 CZ ARG D 58 1641 1811 1630 7 27 6 C ATOM 6088 NH1 ARG D 58 20.514 6.840 6.382 1.00 13.19 N ANISOU 6088 NH1 ARG D 58 1731 1725 1557 -24 -20 -73 N ATOM 6089 NH2 ARG D 58 18.255 6.396 6.315 1.00 11.93 N ANISOU 6089 NH2 ARG D 58 1513 1575 1444 -22 -71 -36 N ATOM 6090 N ALA D 59 20.522 4.481 -1.455 1.00 12.31 N ANISOU 6090 N ALA D 59 1562 1594 1522 -36 -6 -6 N ATOM 6091 CA ALA D 59 19.349 4.158 -2.259 1.00 12.26 C ANISOU 6091 CA ALA D 59 1554 1580 1525 -1 -21 17 C ATOM 6092 C ALA D 59 19.002 2.675 -2.241 1.00 12.39 C ANISOU 6092 C ALA D 59 1584 1592 1531 -8 -8 -12 C ATOM 6093 O ALA D 59 17.816 2.326 -2.301 1.00 12.46 O ANISOU 6093 O ALA D 59 1590 1601 1544 -15 -9 -28 O ATOM 6094 CB ALA D 59 19.569 4.625 -3.695 1.00 13.00 C ANISOU 6094 CB ALA D 59 1664 1721 1555 -25 14 27 C ATOM 6095 N SER D 60 20.001 1.795 -2.184 1.00 12.46 N ANISOU 6095 N SER D 60 1643 1594 1497 21 -18 -1 N ATOM 6096 CA SER D 60 19.754 0.362 -2.124 1.00 13.01 C ANISOU 6096 CA SER D 60 1679 1628 1636 4 -23 25 C ATOM 6097 C SER D 60 19.860 -0.217 -0.718 1.00 12.70 C ANISOU 6097 C SER D 60 1616 1598 1612 15 -6 12 C ATOM 6098 O SER D 60 19.626 -1.423 -0.568 1.00 12.19 O ANISOU 6098 O SER D 60 1557 1581 1494 33 -48 28 O ATOM 6099 CB ASER D 60 20.696 -0.383 -3.073 0.50 13.42 C ANISOU 6099 CB ASER D 60 1690 1703 1707 -1 -15 -9 C ATOM 6100 CB BSER D 60 20.739 -0.368 -3.047 0.50 14.43 C ANISOU 6100 CB BSER D 60 1824 1814 1846 40 42 -60 C ATOM 6101 OG ASER D 60 22.050 -0.114 -2.763 0.50 13.23 O ANISOU 6101 OG ASER D 60 1644 1635 1745 26 24 -25 O ATOM 6102 OG BSER D 60 20.659 0.152 -4.361 0.50 16.10 O ANISOU 6102 OG BSER D 60 2096 2047 1974 15 7 26 O ATOM 6103 N LYS D 61 20.143 0.589 0.300 1.00 13.08 N ANISOU 6103 N LYS D 61 1690 1634 1645 28 -6 -2 N ATOM 6104 CA LYS D 61 20.160 0.056 1.664 1.00 13.45 C ANISOU 6104 CA LYS D 61 1691 1733 1687 42 57 59 C ATOM 6105 C LYS D 61 18.745 -0.207 2.162 1.00 12.31 C ANISOU 6105 C LYS D 61 1640 1548 1490 14 -4 -5 C ATOM 6106 O LYS D 61 17.823 0.555 1.887 1.00 12.40 O ANISOU 6106 O LYS D 61 1623 1645 1443 10 -59 20 O ATOM 6107 CB LYS D 61 20.901 1.002 2.614 1.00 17.51 C ANISOU 6107 CB LYS D 61 2169 2069 2416 -122 -90 -199 C ATOM 6108 CG LYS D 61 21.001 0.451 4.029 1.00 24.83 C ANISOU 6108 CG LYS D 61 3331 3162 2940 64 63 164 C ATOM 6109 CD LYS D 61 22.134 1.089 4.815 1.00 29.94 C ANISOU 6109 CD LYS D 61 3702 3785 3888 -89 -80 -123 C ATOM 6110 CE LYS D 61 22.359 0.336 6.120 1.00 33.50 C ANISOU 6110 CE LYS D 61 4347 4202 4180 38 15 61 C ATOM 6111 NZ LYS D 61 23.596 0.798 6.805 1.00 35.34 N ANISOU 6111 NZ LYS D 61 4460 4479 4489 -14 -21 -10 N ATOM 6112 N GLU D 62 18.557 -1.295 2.908 1.00 11.87 N ANISOU 6112 N GLU D 62 1541 1542 1428 -18 8 -22 N ATOM 6113 CA GLU D 62 17.207 -1.718 3.276 1.00 11.74 C ANISOU 6113 CA GLU D 62 1513 1528 1419 11 -5 2 C ATOM 6114 C GLU D 62 16.883 -1.401 4.727 1.00 11.85 C ANISOU 6114 C GLU D 62 1506 1550 1446 39 2 -39 C ATOM 6115 O GLU D 62 17.666 -1.688 5.631 1.00 12.40 O ANISOU 6115 O GLU D 62 1592 1644 1476 49 -15 6 O ATOM 6116 CB GLU D 62 17.026 -3.207 2.972 1.00 12.39 C ANISOU 6116 CB GLU D 62 1608 1542 1558 -3 -2 -1 C ATOM 6117 CG GLU D 62 17.363 -3.525 1.518 1.00 13.37 C ANISOU 6117 CG GLU D 62 1657 1838 1584 21 8 8 C ATOM 6118 CD GLU D 62 17.123 -4.964 1.126 1.00 16.70 C ANISOU 6118 CD GLU D 62 2175 1999 2171 -16 48 -37 C ATOM 6119 OE1 GLU D 62 17.077 -5.823 2.027 1.00 17.08 O ANISOU 6119 OE1 GLU D 62 2256 2071 2162 52 -11 -13 O ATOM 6120 OE2 GLU D 62 16.985 -5.228 -0.089 1.00 18.54 O ANISOU 6120 OE2 GLU D 62 2462 2316 2266 26 -85 -36 O ATOM 6121 N TYR D 63 15.736 -0.772 4.940 1.00 11.06 N ANISOU 6121 N TYR D 63 1463 1407 1333 11 0 2 N ATOM 6122 CA TYR D 63 15.280 -0.352 6.253 1.00 10.88 C ANISOU 6122 CA TYR D 63 1406 1377 1352 9 8 5 C ATOM 6123 C TYR D 63 13.909 -0.928 6.591 1.00 10.40 C ANISOU 6123 C TYR D 63 1364 1326 1263 12 -1 10 C ATOM 6124 O TYR D 63 13.142 -1.343 5.717 1.00 10.38 O ANISOU 6124 O TYR D 63 1319 1343 1281 3 21 12 O ATOM 6125 CB TYR D 63 15.197 1.182 6.331 1.00 11.30 C ANISOU 6125 CB TYR D 63 1497 1383 1412 -2 -18 -15 C ATOM 6126 CG TYR D 63 16.531 1.861 6.112 1.00 12.25 C ANISOU 6126 CG TYR D 63 1552 1532 1569 -24 7 -1 C ATOM 6127 CD1 TYR D 63 17.417 2.050 7.163 1.00 13.00 C ANISOU 6127 CD1 TYR D 63 1652 1663 1624 -2 -32 -17 C ATOM 6128 CD2 TYR D 63 16.914 2.284 4.846 1.00 12.98 C ANISOU 6128 CD2 TYR D 63 1679 1667 1586 -11 11 2 C ATOM 6129 CE1 TYR D 63 18.638 2.659 6.960 1.00 13.28 C ANISOU 6129 CE1 TYR D 63 1670 1723 1651 -20 -46 -13 C ATOM 6130 CE2 TYR D 63 18.137 2.891 4.631 1.00 13.25 C ANISOU 6130 CE2 TYR D 63 1722 1658 1656 -23 4 25 C ATOM 6131 CZ TYR D 63 18.994 3.076 5.695 1.00 13.90 C ANISOU 6131 CZ TYR D 63 1787 1774 1721 -20 -38 40 C ATOM 6132 OH TYR D 63 20.215 3.673 5.495 1.00 14.84 O ANISOU 6132 OH TYR D 63 1867 1852 1921 -37 10 84 O ATOM 6133 N LEU D 64 13.582 -0.948 7.886 1.00 10.22 N ANISOU 6133 N LEU D 64 1285 1351 1249 16 -27 45 N ATOM 6134 CA LEU D 64 12.209 -1.251 8.294 1.00 9.78 C ANISOU 6134 CA LEU D 64 1266 1306 1145 41 -12 29 C ATOM 6135 C LEU D 64 11.243 -0.367 7.518 1.00 9.44 C ANISOU 6135 C LEU D 64 1210 1255 1123 -7 -33 17 C ATOM 6136 O LEU D 64 11.448 0.843 7.445 1.00 10.26 O ANISOU 6136 O LEU D 64 1403 1285 1212 -40 -124 -6 O ATOM 6137 CB LEU D 64 12.040 -0.933 9.784 1.00 9.84 C ANISOU 6137 CB LEU D 64 1245 1342 1152 41 0 -30 C ATOM 6138 CG LEU D 64 12.647 -1.941 10.761 1.00 11.00 C ANISOU 6138 CG LEU D 64 1465 1301 1412 37 -15 37 C ATOM 6139 CD1 LEU D 64 12.845 -1.284 12.120 1.00 12.42 C ANISOU 6139 CD1 LEU D 64 1675 1581 1463 12 -52 -11 C ATOM 6140 CD2 LEU D 64 11.742 -3.158 10.866 1.00 10.37 C ANISOU 6140 CD2 LEU D 64 1395 1329 1214 16 -3 47 C ATOM 6141 N PRO D 65 10.180 -0.949 6.981 1.00 9.11 N ANISOU 6141 N PRO D 65 1220 1165 1078 -10 -6 -1 N ATOM 6142 CA PRO D 65 9.204 -0.178 6.229 1.00 9.17 C ANISOU 6142 CA PRO D 65 1182 1157 1146 4 -12 -7 C ATOM 6143 C PRO D 65 8.320 0.670 7.131 1.00 9.41 C ANISOU 6143 C PRO D 65 1217 1209 1151 13 -3 -3 C ATOM 6144 O PRO D 65 7.803 1.707 6.711 1.00 9.29 O ANISOU 6144 O PRO D 65 1280 1164 1084 -16 -26 -24 O ATOM 6145 CB PRO D 65 8.420 -1.212 5.434 1.00 9.37 C ANISOU 6145 CB PRO D 65 1236 1153 1171 -15 -32 15 C ATOM 6146 CG PRO D 65 8.671 -2.511 6.114 1.00 9.34 C ANISOU 6146 CG PRO D 65 1229 1153 1168 -14 -20 20 C ATOM 6147 CD PRO D 65 10.034 -2.404 6.744 1.00 9.32 C ANISOU 6147 CD PRO D 65 1231 1157 1154 -8 -28 28 C ATOM 6148 N ALA D 66 8.143 0.227 8.374 1.00 9.27 N ANISOU 6148 N ALA D 66 1138 1247 1138 -5 -4 10 N ATOM 6149 CA ALA D 66 7.258 0.920 9.307 1.00 9.53 C ANISOU 6149 CA ALA D 66 1249 1234 1140 2 9 -6 C ATOM 6150 C ALA D 66 5.926 1.197 8.627 1.00 9.97 C ANISOU 6150 C ALA D 66 1292 1294 1203 -1 -18 22 C ATOM 6151 O ALA D 66 5.411 0.301 7.950 1.00 10.48 O ANISOU 6151 O ALA D 66 1411 1337 1235 -15 -64 15 O ATOM 6152 CB ALA D 66 7.934 2.172 9.827 1.00 9.91 C ANISOU 6152 CB ALA D 66 1331 1215 1219 -30 -3 37 C ATOM 6153 N SER D 67 5.383 2.403 8.716 1.00 10.42 N ANISOU 6153 N SER D 67 1382 1344 1232 36 13 53 N ATOM 6154 CA SER D 67 4.031 2.684 8.262 1.00 10.80 C ANISOU 6154 CA SER D 67 1348 1385 1372 -34 17 41 C ATOM 6155 C SER D 67 3.889 2.769 6.752 1.00 10.95 C ANISOU 6155 C SER D 67 1383 1400 1378 24 7 4 C ATOM 6156 O SER D 67 2.754 2.749 6.259 1.00 11.55 O ANISOU 6156 O SER D 67 1406 1515 1466 32 -12 -2 O ATOM 6157 CB SER D 67 3.458 3.938 8.932 1.00 13.16 C ANISOU 6157 CB SER D 67 1760 1563 1677 93 71 -39 C ATOM 6158 OG SER D 67 4.464 4.739 9.518 1.00 16.06 O ANISOU 6158 OG SER D 67 1872 2114 2115 -99 19 -48 O ATOM 6159 N THR D 68 4.980 2.725 5.984 1.00 10.77 N ANISOU 6159 N THR D 68 1401 1376 1314 -4 11 41 N ATOM 6160 CA THR D 68 4.863 2.467 4.552 1.00 10.46 C ANISOU 6160 CA THR D 68 1330 1347 1296 -2 2 17 C ATOM 6161 C THR D 68 4.392 1.051 4.252 1.00 10.89 C ANISOU 6161 C THR D 68 1422 1346 1372 -4 -1 26 C ATOM 6162 O THR D 68 3.890 0.791 3.154 1.00 11.41 O ANISOU 6162 O THR D 68 1491 1387 1458 3 -109 75 O ATOM 6163 CB THR D 68 6.153 2.714 3.748 1.00 9.89 C ANISOU 6163 CB THR D 68 1244 1196 1316 -32 -45 -1 C ATOM 6164 OG1 THR D 68 7.132 1.718 4.070 1.00 9.82 O ANISOU 6164 OG1 THR D 68 1322 1214 1196 -11 -68 28 O ATOM 6165 CG2 THR D 68 6.702 4.106 4.012 1.00 9.17 C ANISOU 6165 CG2 THR D 68 1180 1155 1150 -19 -18 0 C ATOM 6166 N PHE D 69 4.484 0.109 5.191 1.00 10.46 N ANISOU 6166 N PHE D 69 1333 1344 1299 4 -27 -2 N ATOM 6167 CA PHE D 69 3.921 -1.218 5.046 1.00 11.04 C ANISOU 6167 CA PHE D 69 1400 1363 1432 -4 -12 32 C ATOM 6168 C PHE D 69 2.401 -1.240 5.003 1.00 11.11 C ANISOU 6168 C PHE D 69 1414 1421 1388 -7 8 20 C ATOM 6169 O PHE D 69 1.803 -2.220 4.533 1.00 11.62 O ANISOU 6169 O PHE D 69 1509 1499 1407 -51 -27 28 O ATOM 6170 CB PHE D 69 4.419 -2.135 6.185 1.00 11.71 C ANISOU 6170 CB PHE D 69 1557 1360 1532 -1 -27 64 C ATOM 6171 CG PHE D 69 4.130 -3.579 5.864 1.00 9.59 C ANISOU 6171 CG PHE D 69 1191 1295 1158 18 -62 35 C ATOM 6172 CD1 PHE D 69 4.884 -4.243 4.914 1.00 9.99 C ANISOU 6172 CD1 PHE D 69 1217 1287 1292 34 -64 -22 C ATOM 6173 CD2 PHE D 69 3.098 -4.251 6.499 1.00 10.05 C ANISOU 6173 CD2 PHE D 69 1291 1273 1253 -3 -4 23 C ATOM 6174 CE1 PHE D 69 4.623 -5.566 4.605 1.00 10.49 C ANISOU 6174 CE1 PHE D 69 1355 1280 1353 -7 -67 40 C ATOM 6175 CE2 PHE D 69 2.828 -5.570 6.188 1.00 10.13 C ANISOU 6175 CE2 PHE D 69 1300 1252 1296 44 -58 33 C ATOM 6176 CZ PHE D 69 3.591 -6.226 5.243 1.00 11.09 C ANISOU 6176 CZ PHE D 69 1380 1479 1355 27 31 21 C ATOM 6177 N LYS D 70 1.714 -0.161 5.370 1.00 10.68 N ANISOU 6177 N LYS D 70 1396 1374 1288 -17 2 89 N ATOM 6178 CA LYS D 70 0.271 -0.062 5.192 1.00 11.67 C ANISOU 6178 CA LYS D 70 1435 1542 1457 -16 5 51 C ATOM 6179 C LYS D 70 -0.155 -0.264 3.747 1.00 11.57 C ANISOU 6179 C LYS D 70 1470 1487 1441 -16 -11 47 C ATOM 6180 O LYS D 70 -1.267 -0.747 3.510 1.00 11.64 O ANISOU 6180 O LYS D 70 1470 1470 1482 -26 26 82 O ATOM 6181 CB LYS D 70 -0.248 1.267 5.757 1.00 13.72 C ANISOU 6181 CB LYS D 70 1717 1633 1861 47 0 -16 C ATOM 6182 CG LYS D 70 0.021 1.376 7.247 1.00 15.98 C ANISOU 6182 CG LYS D 70 2025 2084 1962 10 0 4 C ATOM 6183 CD LYS D 70 -0.158 2.762 7.823 1.00 17.93 C ANISOU 6183 CD LYS D 70 2279 2190 2344 26 43 -44 C ATOM 6184 CE LYS D 70 -1.621 3.135 7.956 1.00 17.12 C ANISOU 6184 CE LYS D 70 2211 2074 2222 -8 -23 -2 C ATOM 6185 NZ LYS D 70 -1.815 4.263 8.909 1.00 16.13 N ANISOU 6185 NZ LYS D 70 2082 2045 2003 15 43 72 N ATOM 6186 N ILE D 71 0.682 0.087 2.771 1.00 11.27 N ANISOU 6186 N ILE D 71 1452 1447 1384 0 -20 7 N ATOM 6187 CA ILE D 71 0.347 -0.137 1.371 1.00 10.85 C ANISOU 6187 CA ILE D 71 1423 1365 1336 -22 -3 39 C ATOM 6188 C ILE D 71 0.151 -1.602 1.032 1.00 11.02 C ANISOU 6188 C ILE D 71 1402 1382 1403 0 -14 1 C ATOM 6189 O ILE D 71 -0.966 -2.010 0.688 1.00 11.15 O ANISOU 6189 O ILE D 71 1413 1447 1375 -23 -46 59 O ATOM 6190 CB ILE D 71 1.330 0.565 0.419 1.00 10.39 C ANISOU 6190 CB ILE D 71 1336 1348 1266 -56 -48 -34 C ATOM 6191 CG1 ILE D 71 1.380 2.056 0.749 1.00 10.70 C ANISOU 6191 CG1 ILE D 71 1381 1339 1347 22 11 12 C ATOM 6192 CG2 ILE D 71 0.882 0.348 -1.021 1.00 9.96 C ANISOU 6192 CG2 ILE D 71 1326 1283 1174 -10 2 44 C ATOM 6193 CD1 ILE D 71 2.359 2.871 -0.070 1.00 11.05 C ANISOU 6193 CD1 ILE D 71 1411 1420 1366 -4 -3 58 C ATOM 6194 N PRO D 72 1.164 -2.444 1.165 1.00 11.00 N ANISOU 6194 N PRO D 72 1436 1361 1383 3 -56 26 N ATOM 6195 CA PRO D 72 1.022 -3.869 0.904 1.00 11.06 C ANISOU 6195 CA PRO D 72 1431 1370 1402 0 -43 17 C ATOM 6196 C PRO D 72 0.026 -4.517 1.850 1.00 11.60 C ANISOU 6196 C PRO D 72 1481 1466 1462 -25 -12 32 C ATOM 6197 O PRO D 72 -0.776 -5.356 1.432 1.00 11.98 O ANISOU 6197 O PRO D 72 1549 1474 1530 -28 -58 14 O ATOM 6198 CB PRO D 72 2.423 -4.437 1.065 1.00 11.20 C ANISOU 6198 CB PRO D 72 1420 1390 1445 -17 -42 34 C ATOM 6199 CG PRO D 72 3.161 -3.415 1.859 1.00 11.21 C ANISOU 6199 CG PRO D 72 1474 1371 1416 11 -74 21 C ATOM 6200 CD PRO D 72 2.577 -2.082 1.432 1.00 11.15 C ANISOU 6200 CD PRO D 72 1419 1349 1467 18 -10 31 C ATOM 6201 N ASN D 73 0.032 -4.116 3.122 1.00 12.12 N ANISOU 6201 N ASN D 73 1530 1585 1492 -6 3 10 N ATOM 6202 CA ASN D 73 -0.881 -4.685 4.108 1.00 12.03 C ANISOU 6202 CA ASN D 73 1500 1544 1525 -13 -14 31 C ATOM 6203 C ASN D 73 -2.334 -4.451 3.702 1.00 12.11 C ANISOU 6203 C ASN D 73 1511 1539 1551 -5 -18 42 C ATOM 6204 O ASN D 73 -3.124 -5.396 3.727 1.00 12.08 O ANISOU 6204 O ASN D 73 1543 1536 1511 -18 -60 43 O ATOM 6205 CB ASN D 73 -0.594 -4.141 5.506 1.00 12.33 C ANISOU 6205 CB ASN D 73 1602 1582 1499 8 9 43 C ATOM 6206 CG ASN D 73 -0.990 -5.104 6.613 1.00 12.22 C ANISOU 6206 CG ASN D 73 1596 1496 1552 -1 1 31 C ATOM 6207 OD1 ASN D 73 -1.255 -6.279 6.371 1.00 12.02 O ANISOU 6207 OD1 ASN D 73 1542 1511 1512 -37 -38 59 O ATOM 6208 ND2 ASN D 73 -1.032 -4.606 7.843 1.00 12.56 N ANISOU 6208 ND2 ASN D 73 1717 1510 1545 30 -34 66 N ATOM 6209 N ALA D 74 -2.676 -3.241 3.266 1.00 12.12 N ANISOU 6209 N ALA D 74 1540 1507 1557 -3 -9 10 N ATOM 6210 CA ALA D 74 -4.022 -2.951 2.788 1.00 12.25 C ANISOU 6210 CA ALA D 74 1549 1538 1569 -5 -3 29 C ATOM 6211 C ALA D 74 -4.375 -3.738 1.530 1.00 12.64 C ANISOU 6211 C ALA D 74 1611 1600 1593 1 -6 16 C ATOM 6212 O ALA D 74 -5.497 -4.245 1.427 1.00 13.33 O ANISOU 6212 O ALA D 74 1674 1668 1722 -58 -27 72 O ATOM 6213 CB ALA D 74 -4.197 -1.460 2.527 1.00 13.01 C ANISOU 6213 CB ALA D 74 1684 1558 1700 12 -34 8 C ATOM 6214 N ILE D 75 -3.448 -3.841 0.583 1.00 11.98 N ANISOU 6214 N ILE D 75 1584 1484 1484 36 -45 42 N ATOM 6215 CA ILE D 75 -3.680 -4.623 -0.629 1.00 12.20 C ANISOU 6215 CA ILE D 75 1588 1519 1528 23 -26 12 C ATOM 6216 C ILE D 75 -3.928 -6.090 -0.299 1.00 12.53 C ANISOU 6216 C ILE D 75 1618 1554 1587 -19 -48 31 C ATOM 6217 O ILE D 75 -4.881 -6.700 -0.779 1.00 12.49 O ANISOU 6217 O ILE D 75 1670 1503 1573 -43 -80 81 O ATOM 6218 CB ILE D 75 -2.502 -4.501 -1.611 1.00 12.34 C ANISOU 6218 CB ILE D 75 1531 1592 1565 -6 -46 3 C ATOM 6219 CG1 ILE D 75 -2.353 -3.048 -2.077 1.00 12.96 C ANISOU 6219 CG1 ILE D 75 1634 1622 1669 -16 -30 13 C ATOM 6220 CG2 ILE D 75 -2.681 -5.426 -2.807 1.00 12.76 C ANISOU 6220 CG2 ILE D 75 1703 1574 1570 -8 8 17 C ATOM 6221 CD1 ILE D 75 -1.025 -2.755 -2.741 1.00 13.59 C ANISOU 6221 CD1 ILE D 75 1682 1743 1738 -16 -2 49 C ATOM 6222 N ILE D 76 -3.065 -6.655 0.542 1.00 12.62 N ANISOU 6222 N ILE D 76 1615 1552 1628 25 -48 28 N ATOM 6223 CA ILE D 76 -3.192 -8.055 0.951 1.00 12.90 C ANISOU 6223 CA ILE D 76 1646 1599 1656 -5 -56 54 C ATOM 6224 C ILE D 76 -4.475 -8.281 1.734 1.00 13.26 C ANISOU 6224 C ILE D 76 1647 1678 1712 25 -40 16 C ATOM 6225 O ILE D 76 -5.168 -9.281 1.520 1.00 14.00 O ANISOU 6225 O ILE D 76 1712 1732 1874 -6 -84 39 O ATOM 6226 CB ILE D 76 -1.954 -8.476 1.762 1.00 12.44 C ANISOU 6226 CB ILE D 76 1587 1551 1590 2 -28 7 C ATOM 6227 CG1 ILE D 76 -0.705 -8.431 0.874 1.00 12.70 C ANISOU 6227 CG1 ILE D 76 1620 1595 1609 -15 -18 -8 C ATOM 6228 CG2 ILE D 76 -2.124 -9.871 2.356 1.00 13.30 C ANISOU 6228 CG2 ILE D 76 1757 1633 1666 -22 -30 61 C ATOM 6229 CD1 ILE D 76 0.594 -8.410 1.657 1.00 14.01 C ANISOU 6229 CD1 ILE D 76 1683 1779 1859 42 -83 24 C ATOM 6230 N GLY D 77 -4.827 -7.367 2.630 1.00 13.31 N ANISOU 6230 N GLY D 77 1682 1725 1651 42 -61 15 N ATOM 6231 CA GLY D 77 -6.099 -7.391 3.332 1.00 14.03 C ANISOU 6231 CA GLY D 77 1776 1780 1775 4 13 43 C ATOM 6232 C GLY D 77 -7.290 -7.455 2.387 1.00 14.83 C ANISOU 6232 C GLY D 77 1859 1900 1876 -7 -42 41 C ATOM 6233 O GLY D 77 -8.203 -8.262 2.586 1.00 15.33 O ANISOU 6233 O GLY D 77 1906 1981 1938 -34 -18 86 O ATOM 6234 N LEU D 78 -7.303 -6.608 1.358 1.00 14.93 N ANISOU 6234 N LEU D 78 1892 1880 1900 -19 -2 54 N ATOM 6235 CA LEU D 78 -8.359 -6.676 0.349 1.00 15.41 C ANISOU 6235 CA LEU D 78 1982 1942 1929 -14 -39 69 C ATOM 6236 C LEU D 78 -8.313 -7.975 -0.439 1.00 16.29 C ANISOU 6236 C LEU D 78 2129 2017 2043 -10 -30 26 C ATOM 6237 O LEU D 78 -9.341 -8.638 -0.624 1.00 16.90 O ANISOU 6237 O LEU D 78 2158 2074 2188 -16 -58 24 O ATOM 6238 CB LEU D 78 -8.261 -5.469 -0.591 1.00 14.42 C ANISOU 6238 CB LEU D 78 1777 1845 1859 -12 -34 19 C ATOM 6239 CG LEU D 78 -8.690 -4.129 0.011 1.00 14.97 C ANISOU 6239 CG LEU D 78 1925 1896 1867 6 -19 -7 C ATOM 6240 CD1 LEU D 78 -8.154 -2.971 -0.817 1.00 15.88 C ANISOU 6240 CD1 LEU D 78 2016 1966 2050 -13 22 51 C ATOM 6241 CD2 LEU D 78 -10.209 -4.055 0.102 1.00 16.39 C ANISOU 6241 CD2 LEU D 78 2001 2062 2163 4 27 32 C ATOM 6242 N GLU D 79 -7.131 -8.387 -0.883 1.00 17.10 N ANISOU 6242 N GLU D 79 2169 2184 2145 9 -17 70 N ATOM 6243 CA GLU D 79 -6.967 -9.592 -1.677 1.00 18.85 C ANISOU 6243 CA GLU D 79 2452 2334 2377 19 -34 -37 C ATOM 6244 C GLU D 79 -7.465 -10.849 -0.969 1.00 20.03 C ANISOU 6244 C GLU D 79 2596 2438 2579 -11 -20 30 C ATOM 6245 O GLU D 79 -8.074 -11.717 -1.593 1.00 20.30 O ANISOU 6245 O GLU D 79 2610 2445 2657 -20 -49 35 O ATOM 6246 CB GLU D 79 -5.499 -9.804 -2.061 1.00 21.48 C ANISOU 6246 CB GLU D 79 2577 2748 2838 22 23 -45 C ATOM 6247 CG GLU D 79 -5.053 -9.091 -3.317 1.00 23.27 C ANISOU 6247 CG GLU D 79 2944 2942 2954 -2 1 60 C ATOM 6248 CD GLU D 79 -5.842 -9.490 -4.551 1.00 24.12 C ANISOU 6248 CD GLU D 79 3011 3125 3028 7 -43 37 C ATOM 6249 OE1 GLU D 79 -5.675 -10.621 -5.050 1.00 26.88 O ANISOU 6249 OE1 GLU D 79 3521 3246 3447 19 48 -3 O ATOM 6250 OE2 GLU D 79 -6.633 -8.653 -5.028 1.00 22.66 O ANISOU 6250 OE2 GLU D 79 2901 2904 2807 -71 16 2 O ATOM 6251 N THR D 80 -7.189 -10.950 0.325 1.00 20.95 N ANISOU 6251 N THR D 80 2692 2640 2626 -3 -30 24 N ATOM 6252 CA THR D 80 -7.522 -12.144 1.089 1.00 21.55 C ANISOU 6252 CA THR D 80 2767 2701 2719 -19 -21 51 C ATOM 6253 C THR D 80 -8.980 -12.171 1.518 1.00 22.21 C ANISOU 6253 C THR D 80 2800 2795 2844 1 -1 12 C ATOM 6254 O THR D 80 -9.508 -13.232 1.850 1.00 22.82 O ANISOU 6254 O THR D 80 2881 2822 2966 -15 -15 38 O ATOM 6255 CB THR D 80 -6.631 -12.254 2.342 1.00 21.25 C ANISOU 6255 CB THR D 80 2732 2668 2675 -8 7 17 C ATOM 6256 OG1 THR D 80 -6.729 -11.048 3.107 1.00 20.75 O ANISOU 6256 OG1 THR D 80 2631 2570 2682 -4 -30 66 O ATOM 6257 CG2 THR D 80 -5.186 -12.495 1.943 1.00 21.57 C ANISOU 6257 CG2 THR D 80 2747 2716 2734 -13 9 24 C ATOM 6258 N GLY D 81 -9.622 -11.010 1.563 1.00 22.17 N ANISOU 6258 N GLY D 81 2803 2767 2853 -20 -7 19 N ATOM 6259 CA GLY D 81 -11.011 -10.904 1.983 1.00 22.03 C ANISOU 6259 CA GLY D 81 2811 2740 2819 -5 -3 10 C ATOM 6260 C GLY D 81 -11.110 -10.443 3.430 1.00 21.88 C ANISOU 6260 C GLY D 81 2784 2723 2806 -9 -14 15 C ATOM 6261 O GLY D 81 -12.200 -10.243 3.960 1.00 22.39 O ANISOU 6261 O GLY D 81 2792 2803 2913 -10 -6 30 O ATOM 6262 N VAL D 82 -9.961 -10.230 4.064 1.00 21.43 N ANISOU 6262 N VAL D 82 2753 2649 2741 -12 2 25 N ATOM 6263 CA VAL D 82 -9.885 -9.691 5.416 1.00 21.31 C ANISOU 6263 CA VAL D 82 2679 2691 2727 -16 4 29 C ATOM 6264 C VAL D 82 -10.503 -8.301 5.476 1.00 21.67 C ANISOU 6264 C VAL D 82 2730 2718 2788 -3 8 1 C ATOM 6265 O VAL D 82 -11.239 -7.969 6.404 1.00 21.53 O ANISOU 6265 O VAL D 82 2732 2684 2766 -15 12 45 O ATOM 6266 CB VAL D 82 -8.427 -9.677 5.904 1.00 20.10 C ANISOU 6266 CB VAL D 82 2632 2471 2535 -5 11 18 C ATOM 6267 CG1 VAL D 82 -8.240 -8.869 7.177 1.00 19.94 C ANISOU 6267 CG1 VAL D 82 2555 2516 2506 -31 25 16 C ATOM 6268 CG2 VAL D 82 -7.954 -11.113 6.121 1.00 19.21 C ANISOU 6268 CG2 VAL D 82 2419 2416 2463 -23 -9 -7 C ATOM 6269 N ILE D 83 -10.181 -7.473 4.488 1.00 22.16 N ANISOU 6269 N ILE D 83 2797 2793 2829 -24 24 38 N ATOM 6270 CA ILE D 83 -10.911 -6.233 4.243 1.00 22.85 C ANISOU 6270 CA ILE D 83 2901 2829 2950 -13 15 40 C ATOM 6271 C ILE D 83 -11.960 -6.488 3.161 1.00 23.73 C ANISOU 6271 C ILE D 83 3063 2959 2995 -28 -34 12 C ATOM 6272 O ILE D 83 -11.614 -6.901 2.058 1.00 22.99 O ANISOU 6272 O ILE D 83 2905 2858 2970 -43 -38 29 O ATOM 6273 CB ILE D 83 -9.959 -5.108 3.805 1.00 21.72 C ANISOU 6273 CB ILE D 83 2725 2768 2760 15 -86 23 C ATOM 6274 CG1 ILE D 83 -8.816 -4.956 4.813 1.00 19.94 C ANISOU 6274 CG1 ILE D 83 2509 2480 2587 -51 34 42 C ATOM 6275 CG2 ILE D 83 -10.722 -3.797 3.656 1.00 21.93 C ANISOU 6275 CG2 ILE D 83 2778 2747 2810 13 1 2 C ATOM 6276 CD1 ILE D 83 -7.702 -4.033 4.366 1.00 18.73 C ANISOU 6276 CD1 ILE D 83 2354 2363 2402 13 -23 9 C ATOM 6277 N LYS D 84 -13.229 -6.274 3.485 1.00 25.50 N ANISOU 6277 N LYS D 84 3187 3211 3290 26 40 19 N ATOM 6278 CA LYS D 84 -14.329 -6.674 2.618 1.00 27.03 C ANISOU 6278 CA LYS D 84 3377 3429 3464 -26 -46 -40 C ATOM 6279 C LYS D 84 -14.352 -5.908 1.304 1.00 28.03 C ANISOU 6279 C LYS D 84 3540 3554 3557 -2 -13 17 C ATOM 6280 O LYS D 84 -14.461 -6.504 0.229 1.00 28.66 O ANISOU 6280 O LYS D 84 3626 3645 3618 7 -17 -32 O ATOM 6281 CB LYS D 84 -15.674 -6.491 3.334 1.00 28.02 C ANISOU 6281 CB LYS D 84 3483 3570 3592 -6 33 -21 C ATOM 6282 N ASN D 85 -14.295 -4.581 1.383 1.00 28.42 N ANISOU 6282 N ASN D 85 3592 3572 3635 1 3 -13 N ATOM 6283 CA ASN D 85 -14.209 -3.768 0.178 1.00 28.86 C ANISOU 6283 CA ASN D 85 3696 3600 3668 -2 38 -3 C ATOM 6284 C ASN D 85 -13.745 -2.352 0.481 1.00 28.34 C ANISOU 6284 C ASN D 85 3606 3572 3591 17 10 12 C ATOM 6285 O ASN D 85 -13.330 -1.984 1.573 1.00 28.32 O ANISOU 6285 O ASN D 85 3597 3578 3587 25 2 16 O ATOM 6286 CB ASN D 85 -15.555 -3.737 -0.551 1.00 31.04 C ANISOU 6286 CB ASN D 85 3898 3963 3935 1 -103 21 C ATOM 6287 CG ASN D 85 -16.688 -3.143 0.253 1.00 32.53 C ANISOU 6287 CG ASN D 85 4126 4118 4116 46 27 -6 C ATOM 6288 OD1 ASN D 85 -16.545 -2.171 0.994 1.00 32.40 O ANISOU 6288 OD1 ASN D 85 4072 4106 4133 11 1 -8 O ATOM 6289 ND2 ASN D 85 -17.869 -3.739 0.106 1.00 33.45 N ANISOU 6289 ND2 ASN D 85 4224 4225 4262 -16 -14 7 N ATOM 6290 N GLU D 86 -13.895 -1.507 -0.522 1.00 27.84 N ANISOU 6290 N GLU D 86 3512 3512 3553 8 4 -22 N ATOM 6291 CA GLU D 86 -13.600 -0.088 -0.516 1.00 27.47 C ANISOU 6291 CA GLU D 86 3440 3486 3510 23 36 -36 C ATOM 6292 C GLU D 86 -14.275 0.676 0.608 1.00 26.47 C ANISOU 6292 C GLU D 86 3320 3354 3384 -16 -4 23 C ATOM 6293 O GLU D 86 -13.680 1.598 1.174 1.00 26.27 O ANISOU 6293 O GLU D 86 3284 3383 3315 -9 -6 25 O ATOM 6294 CB GLU D 86 -14.024 0.405 -1.899 1.00 29.45 C ANISOU 6294 CB GLU D 86 3763 3796 3631 27 -5 44 C ATOM 6295 CG GLU D 86 -14.234 1.863 -2.202 1.00 30.54 C ANISOU 6295 CG GLU D 86 3882 3819 3905 2 8 -7 C ATOM 6296 CD GLU D 86 -14.841 2.043 -3.589 1.00 31.11 C ANISOU 6296 CD GLU D 86 3970 3918 3932 -5 -13 -27 C ATOM 6297 OE1 GLU D 86 -15.367 1.044 -4.129 1.00 30.16 O ANISOU 6297 OE1 GLU D 86 3799 3848 3812 3 3 23 O ATOM 6298 OE2 GLU D 86 -14.799 3.161 -4.140 1.00 31.34 O ANISOU 6298 OE2 GLU D 86 4022 3929 3955 -31 28 -23 O ATOM 6299 N HIS D 87 -15.510 0.330 0.963 1.00 25.60 N ANISOU 6299 N HIS D 87 3280 3220 3226 22 5 8 N ATOM 6300 CA HIS D 87 -16.295 1.122 1.896 1.00 25.08 C ANISOU 6300 CA HIS D 87 3205 3168 3158 -9 -4 22 C ATOM 6301 C HIS D 87 -16.435 0.486 3.273 1.00 24.80 C ANISOU 6301 C HIS D 87 3146 3142 3135 -1 6 -1 C ATOM 6302 O HIS D 87 -17.286 0.913 4.060 1.00 24.41 O ANISOU 6302 O HIS D 87 3089 3122 3065 -12 -18 37 O ATOM 6303 CB HIS D 87 -17.685 1.411 1.306 1.00 25.71 C ANISOU 6303 CB HIS D 87 3224 3275 3270 26 -8 -14 C ATOM 6304 CG HIS D 87 -17.622 2.162 0.008 1.00 26.47 C ANISOU 6304 CG HIS D 87 3369 3348 3342 7 1 19 C ATOM 6305 ND1 HIS D 87 -16.906 3.331 -0.131 1.00 26.74 N ANISOU 6305 ND1 HIS D 87 3422 3358 3382 -6 14 9 N ATOM 6306 CD2 HIS D 87 -18.176 1.914 -1.202 1.00 26.35 C ANISOU 6306 CD2 HIS D 87 3338 3353 3322 -9 10 19 C ATOM 6307 CE1 HIS D 87 -17.018 3.767 -1.371 1.00 26.16 C ANISOU 6307 CE1 HIS D 87 3315 3282 3341 5 1 -10 C ATOM 6308 NE2 HIS D 87 -17.791 2.932 -2.040 1.00 26.02 N ANISOU 6308 NE2 HIS D 87 3292 3277 3316 11 0 -3 N ATOM 6309 N GLN D 88 -15.602 -0.503 3.588 1.00 25.01 N ANISOU 6309 N GLN D 88 3176 3173 3154 -10 -9 25 N ATOM 6310 CA GLN D 88 -15.641 -1.079 4.931 1.00 25.29 C ANISOU 6310 CA GLN D 88 3224 3247 3137 -59 -8 -3 C ATOM 6311 C GLN D 88 -15.216 -0.040 5.964 1.00 24.55 C ANISOU 6311 C GLN D 88 3096 3135 3096 -5 2 28 C ATOM 6312 O GLN D 88 -14.269 0.714 5.751 1.00 23.97 O ANISOU 6312 O GLN D 88 3027 3106 2974 19 -24 25 O ATOM 6313 CB GLN D 88 -14.765 -2.326 5.065 1.00 28.56 C ANISOU 6313 CB GLN D 88 3599 3482 3770 98 -20 -47 C ATOM 6314 CG GLN D 88 -14.962 -2.996 6.421 1.00 32.30 C ANISOU 6314 CG GLN D 88 4164 4139 3967 -65 24 39 C ATOM 6315 CD GLN D 88 -14.069 -4.188 6.661 1.00 35.01 C ANISOU 6315 CD GLN D 88 4396 4370 4539 43 -6 36 C ATOM 6316 OE1 GLN D 88 -13.661 -4.885 5.735 1.00 35.76 O ANISOU 6316 OE1 GLN D 88 4561 4506 4521 -5 -11 -4 O ATOM 6317 NE2 GLN D 88 -13.760 -4.434 7.932 1.00 36.33 N ANISOU 6317 NE2 GLN D 88 4634 4583 4588 -10 -8 6 N ATOM 6318 N VAL D 89 -15.937 0.007 7.080 1.00 24.34 N ANISOU 6318 N VAL D 89 3082 3080 3087 -11 -4 21 N ATOM 6319 CA VAL D 89 -15.588 0.898 8.181 1.00 24.48 C ANISOU 6319 CA VAL D 89 3100 3097 3106 5 17 -5 C ATOM 6320 C VAL D 89 -14.948 0.094 9.309 1.00 25.15 C ANISOU 6320 C VAL D 89 3204 3171 3181 13 -7 30 C ATOM 6321 O VAL D 89 -15.491 -0.933 9.720 1.00 25.40 O ANISOU 6321 O VAL D 89 3241 3187 3221 -9 -23 34 O ATOM 6322 CB VAL D 89 -16.817 1.656 8.704 1.00 23.80 C ANISOU 6322 CB VAL D 89 3045 2985 3011 -25 -15 3 C ATOM 6323 CG1 VAL D 89 -16.491 2.509 9.920 1.00 23.20 C ANISOU 6323 CG1 VAL D 89 2932 2944 2940 14 0 26 C ATOM 6324 CG2 VAL D 89 -17.411 2.530 7.606 1.00 23.96 C ANISOU 6324 CG2 VAL D 89 3007 3043 3053 19 -9 22 C ATOM 6325 N PHE D 90 -13.801 0.556 9.792 1.00 25.65 N ANISOU 6325 N PHE D 90 3226 3243 3278 -22 9 1 N ATOM 6326 CA PHE D 90 -13.169 -0.079 10.950 1.00 26.68 C ANISOU 6326 CA PHE D 90 3357 3380 3401 -1 -47 43 C ATOM 6327 C PHE D 90 -13.674 0.604 12.218 1.00 28.11 C ANISOU 6327 C PHE D 90 3586 3549 3545 42 -39 -47 C ATOM 6328 O PHE D 90 -13.380 1.768 12.478 1.00 27.54 O ANISOU 6328 O PHE D 90 3505 3505 3456 24 -16 34 O ATOM 6329 CB PHE D 90 -11.650 -0.030 10.843 1.00 25.66 C ANISOU 6329 CB PHE D 90 3314 3214 3222 19 -12 35 C ATOM 6330 CG PHE D 90 -11.102 -0.651 9.589 1.00 25.89 C ANISOU 6330 CG PHE D 90 3288 3272 3278 5 2 -10 C ATOM 6331 CD1 PHE D 90 -10.800 -2.002 9.537 1.00 26.18 C ANISOU 6331 CD1 PHE D 90 3331 3292 3326 14 -4 18 C ATOM 6332 CD2 PHE D 90 -10.886 0.116 8.457 1.00 26.18 C ANISOU 6332 CD2 PHE D 90 3331 3283 3333 22 9 24 C ATOM 6333 CE1 PHE D 90 -10.294 -2.573 8.387 1.00 26.55 C ANISOU 6333 CE1 PHE D 90 3402 3336 3351 17 -1 -6 C ATOM 6334 CE2 PHE D 90 -10.386 -0.449 7.301 1.00 26.48 C ANISOU 6334 CE2 PHE D 90 3388 3341 3330 -6 6 8 C ATOM 6335 CZ PHE D 90 -10.087 -1.796 7.262 1.00 26.75 C ANISOU 6335 CZ PHE D 90 3421 3357 3386 4 6 13 C ATOM 6336 N LYS D 91 -14.469 -0.124 12.992 1.00 30.21 N ANISOU 6336 N LYS D 91 3829 3789 3861 -43 -4 92 N ATOM 6337 CA LYS D 91 -15.155 0.426 14.151 1.00 32.87 C ANISOU 6337 CA LYS D 91 4224 4150 4115 72 76 -31 C ATOM 6338 C LYS D 91 -14.272 0.388 15.395 1.00 34.37 C ANISOU 6338 C LYS D 91 4343 4401 4317 18 -21 44 C ATOM 6339 O LYS D 91 -13.591 -0.614 15.624 1.00 34.22 O ANISOU 6339 O LYS D 91 4355 4357 4289 -4 3 34 O ATOM 6340 CB LYS D 91 -16.425 -0.383 14.436 1.00 35.72 C ANISOU 6340 CB LYS D 91 4476 4450 4645 -77 109 25 C ATOM 6341 CG LYS D 91 -17.426 -0.448 13.301 1.00 39.31 C ANISOU 6341 CG LYS D 91 4992 5043 4902 -75 -86 3 C ATOM 6342 CD LYS D 91 -18.514 0.606 13.437 1.00 42.28 C ANISOU 6342 CD LYS D 91 5380 5262 5421 73 57 10 C ATOM 6343 CE LYS D 91 -19.647 0.337 12.458 1.00 44.40 C ANISOU 6343 CE LYS D 91 5642 5614 5613 -39 -51 -1 C ATOM 6344 NZ LYS D 91 -20.874 1.108 12.798 1.00 45.39 N ANISOU 6344 NZ LYS D 91 5763 5725 5758 20 9 -2 N ATOM 6345 N TRP D 92 -14.294 1.457 16.185 1.00 36.31 N ANISOU 6345 N TRP D 92 4627 4541 4629 3 52 -53 N ATOM 6346 CA TRP D 92 -13.615 1.416 17.481 1.00 38.57 C ANISOU 6346 CA TRP D 92 4878 4957 4821 12 -52 -2 C ATOM 6347 C TRP D 92 -14.234 0.316 18.343 1.00 39.96 C ANISOU 6347 C TRP D 92 5082 5069 5031 -44 19 17 C ATOM 6348 O TRP D 92 -15.435 0.330 18.606 1.00 39.95 O ANISOU 6348 O TRP D 92 5082 5055 5042 -21 13 14 O ATOM 6349 CB TRP D 92 -13.663 2.759 18.198 1.00 40.94 C ANISOU 6349 CB TRP D 92 5229 5028 5298 -3 56 -57 C ATOM 6350 CG TRP D 92 -13.061 2.746 19.572 1.00 43.77 C ANISOU 6350 CG TRP D 92 5590 5546 5497 -33 -67 25 C ATOM 6351 CD1 TRP D 92 -11.913 2.115 19.959 1.00 44.44 C ANISOU 6351 CD1 TRP D 92 5605 5599 5681 14 -8 9 C ATOM 6352 CD2 TRP D 92 -13.559 3.417 20.735 1.00 44.93 C ANISOU 6352 CD2 TRP D 92 5745 5672 5655 -11 42 -35 C ATOM 6353 NE1 TRP D 92 -11.675 2.337 21.292 1.00 45.39 N ANISOU 6353 NE1 TRP D 92 5777 5733 5735 -10 -10 1 N ATOM 6354 CE2 TRP D 92 -12.670 3.136 21.791 1.00 45.76 C ANISOU 6354 CE2 TRP D 92 5785 5780 5823 16 -15 11 C ATOM 6355 CE3 TRP D 92 -14.673 4.224 20.989 1.00 45.49 C ANISOU 6355 CE3 TRP D 92 5761 5714 5809 14 0 9 C ATOM 6356 CZ2 TRP D 92 -12.859 3.632 23.080 1.00 46.41 C ANISOU 6356 CZ2 TRP D 92 5911 5862 5860 -2 0 -5 C ATOM 6357 CZ3 TRP D 92 -14.858 4.715 22.268 1.00 46.25 C ANISOU 6357 CZ3 TRP D 92 5886 5832 5856 1 18 -10 C ATOM 6358 CH2 TRP D 92 -13.956 4.417 23.297 1.00 46.61 C ANISOU 6358 CH2 TRP D 92 5916 5886 5910 3 -6 -2 C ATOM 6359 N PRO D 93 -13.404 -0.630 18.769 1.00 41.20 N ANISOU 6359 N PRO D 93 5218 5200 5234 43 -22 -5 N ATOM 6360 CA PRO D 93 -13.867 -1.769 19.539 1.00 42.30 C ANISOU 6360 CA PRO D 93 5374 5303 5396 -12 16 27 C ATOM 6361 C PRO D 93 -13.103 -1.948 20.839 1.00 42.87 C ANISOU 6361 C PRO D 93 5451 5391 5445 2 -17 15 C ATOM 6362 O PRO D 93 -13.691 -1.906 21.921 1.00 43.21 O ANISOU 6362 O PRO D 93 5503 5442 5475 -1 1 7 O ATOM 6363 CB PRO D 93 -13.664 -2.962 18.615 1.00 42.60 C ANISOU 6363 CB PRO D 93 5414 5349 5422 -2 7 2 C ATOM 6364 N ARG D 97 -5.424 2.214 24.055 1.00 38.14 N ANISOU 6364 N ARG D 97 4871 4770 4851 -1 -33 1 N ATOM 6365 CA ARG D 97 -6.262 3.399 24.195 1.00 38.19 C ANISOU 6365 CA ARG D 97 4871 4770 4868 -2 -58 -19 C ATOM 6366 C ARG D 97 -5.432 4.602 24.628 1.00 37.57 C ANISOU 6366 C ARG D 97 4753 4742 4780 15 -11 -9 C ATOM 6367 O ARG D 97 -5.960 5.620 25.073 1.00 37.57 O ANISOU 6367 O ARG D 97 4748 4743 4783 10 -17 -11 O ATOM 6368 CB ARG D 97 -7.390 3.145 25.197 1.00 40.79 C ANISOU 6368 CB ARG D 97 5115 5277 5107 26 75 11 C ATOM 6369 CG ARG D 97 -7.940 1.730 25.141 1.00 44.34 C ANISOU 6369 CG ARG D 97 5739 5468 5641 -41 -33 -13 C ATOM 6370 CD ARG D 97 -9.392 1.666 25.584 1.00 47.43 C ANISOU 6370 CD ARG D 97 5933 6074 6014 30 37 28 C ATOM 6371 NE ARG D 97 -9.993 0.400 25.173 1.00 49.69 N ANISOU 6371 NE ARG D 97 6399 6173 6309 -23 0 -10 N ATOM 6372 CZ ARG D 97 -11.284 0.196 24.954 1.00 51.41 C ANISOU 6372 CZ ARG D 97 6479 6525 6531 -21 -5 14 C ATOM 6373 NH1 ARG D 97 -12.162 1.180 25.095 1.00 51.98 N ANISOU 6373 NH1 ARG D 97 6606 6543 6601 17 12 1 N ATOM 6374 NH2 ARG D 97 -11.712 -1.004 24.579 1.00 51.91 N ANISOU 6374 NH2 ARG D 97 6598 6538 6588 -6 3 -2 N ATOM 6375 N ALA D 98 -4.118 4.498 24.443 1.00 36.94 N ANISOU 6375 N ALA D 98 4714 4640 4680 -17 -12 -6 N ATOM 6376 CA ALA D 98 -3.187 5.541 24.849 1.00 36.35 C ANISOU 6376 CA ALA D 98 4639 4581 4590 8 7 14 C ATOM 6377 C ALA D 98 -3.017 6.606 23.772 1.00 35.86 C ANISOU 6377 C ALA D 98 4564 4525 4537 6 -8 -18 C ATOM 6378 O ALA D 98 -2.339 7.615 23.972 1.00 35.85 O ANISOU 6378 O ALA D 98 4554 4525 4543 7 -15 -6 O ATOM 6379 CB ALA D 98 -1.839 4.928 25.207 1.00 36.73 C ANISOU 6379 CB ALA D 98 4645 4627 4684 11 2 1 C ATOM 6380 N MET D 99 -3.593 6.369 22.600 1.00 35.34 N ANISOU 6380 N MET D 99 4492 4443 4492 8 14 5 N ATOM 6381 CA MET D 99 -3.741 7.388 21.574 1.00 34.94 C ANISOU 6381 CA MET D 99 4433 4425 4417 7 22 -25 C ATOM 6382 C MET D 99 -5.226 7.696 21.389 1.00 34.97 C ANISOU 6382 C MET D 99 4438 4412 4435 9 -2 -4 C ATOM 6383 O MET D 99 -6.044 6.775 21.357 1.00 35.09 O ANISOU 6383 O MET D 99 4418 4444 4469 3 -9 0 O ATOM 6384 CB MET D 99 -3.139 6.924 20.249 1.00 33.50 C ANISOU 6384 CB MET D 99 4155 4236 4338 26 -45 7 C ATOM 6385 CG MET D 99 -1.688 6.481 20.324 1.00 30.84 C ANISOU 6385 CG MET D 99 3974 3808 3938 -77 -32 -51 C ATOM 6386 SD MET D 99 -0.563 7.806 20.790 1.00 28.11 S ANISOU 6386 SD MET D 99 3563 3600 3519 59 20 58 S ATOM 6387 CE MET D 99 -0.579 8.781 19.283 1.00 27.75 C ANISOU 6387 CE MET D 99 3558 3477 3507 -4 -22 26 C ATOM 6388 N LYS D 100 -5.561 8.973 21.249 1.00 34.79 N ANISOU 6388 N LYS D 100 4408 4405 4406 8 -14 -7 N ATOM 6389 CA LYS D 100 -6.932 9.375 20.947 1.00 34.44 C ANISOU 6389 CA LYS D 100 4380 4359 4348 -2 4 -4 C ATOM 6390 C LYS D 100 -7.332 8.912 19.553 1.00 33.95 C ANISOU 6390 C LYS D 100 4301 4283 4316 5 20 8 C ATOM 6391 O LYS D 100 -8.455 8.474 19.306 1.00 34.08 O ANISOU 6391 O LYS D 100 4317 4301 4333 3 -3 5 O ATOM 6392 CB LYS D 100 -7.087 10.893 21.066 1.00 34.91 C ANISOU 6392 CB LYS D 100 4427 4386 4451 11 13 -7 C ATOM 6393 N GLN D 101 -6.389 8.955 18.619 1.00 33.20 N ANISOU 6393 N GLN D 101 4249 4161 4206 7 -34 -12 N ATOM 6394 CA GLN D 101 -6.518 8.416 17.284 1.00 32.28 C ANISOU 6394 CA GLN D 101 4124 3997 4146 -10 -16 29 C ATOM 6395 C GLN D 101 -7.103 7.016 17.203 1.00 31.10 C ANISOU 6395 C GLN D 101 3956 3922 3939 25 -28 43 C ATOM 6396 O GLN D 101 -7.899 6.748 16.296 1.00 30.97 O ANISOU 6396 O GLN D 101 3953 3913 3903 0 -11 35 O ATOM 6397 CB GLN D 101 -5.141 8.399 16.594 1.00 33.34 C ANISOU 6397 CB GLN D 101 4189 4204 4277 9 25 2 C ATOM 6398 N TRP D 102 -6.757 6.105 18.110 1.00 29.75 N ANISOU 6398 N TRP D 102 3749 3726 3827 -13 -13 -33 N ATOM 6399 CA TRP D 102 -7.170 4.714 18.001 1.00 28.42 C ANISOU 6399 CA TRP D 102 3547 3619 3634 73 -37 46 C ATOM 6400 C TRP D 102 -8.535 4.442 18.617 1.00 28.32 C ANISOU 6400 C TRP D 102 3584 3589 3589 13 -14 16 C ATOM 6401 O TRP D 102 -8.968 3.289 18.685 1.00 28.29 O ANISOU 6401 O TRP D 102 3596 3593 3561 1 1 20 O ATOM 6402 CB TRP D 102 -6.120 3.774 18.597 1.00 25.16 C ANISOU 6402 CB TRP D 102 3126 3277 3157 -101 116 -31 C ATOM 6403 CG TRP D 102 -4.711 3.993 18.141 1.00 22.12 C ANISOU 6403 CG TRP D 102 2895 2784 2727 26 -51 40 C ATOM 6404 CD1 TRP D 102 -4.295 4.612 16.996 1.00 21.14 C ANISOU 6404 CD1 TRP D 102 2643 2692 2699 8 -20 -8 C ATOM 6405 CD2 TRP D 102 -3.515 3.564 18.806 1.00 21.06 C ANISOU 6405 CD2 TRP D 102 2712 2631 2658 -31 47 -28 C ATOM 6406 NE1 TRP D 102 -2.929 4.615 16.917 1.00 20.02 N ANISOU 6406 NE1 TRP D 102 2583 2499 2525 14 2 15 N ATOM 6407 CE2 TRP D 102 -2.423 3.972 18.018 1.00 20.01 C ANISOU 6407 CE2 TRP D 102 2595 2513 2496 18 -25 -23 C ATOM 6408 CE3 TRP D 102 -3.263 2.879 20.002 1.00 22.42 C ANISOU 6408 CE3 TRP D 102 2861 2857 2801 12 -19 47 C ATOM 6409 CZ2 TRP D 102 -1.101 3.725 18.378 1.00 20.74 C ANISOU 6409 CZ2 TRP D 102 2604 2627 2649 -9 -7 -31 C ATOM 6410 CZ3 TRP D 102 -1.949 2.632 20.358 1.00 22.27 C ANISOU 6410 CZ3 TRP D 102 2835 2805 2823 1 17 15 C ATOM 6411 CH2 TRP D 102 -0.885 3.051 19.547 1.00 21.85 C ANISOU 6411 CH2 TRP D 102 2792 2768 2744 4 -25 23 C ATOM 6412 N GLU D 103 -9.245 5.476 19.052 1.00 28.48 N ANISOU 6412 N GLU D 103 3596 3600 3626 23 -30 20 N ATOM 6413 CA GLU D 103 -10.605 5.363 19.546 1.00 28.86 C ANISOU 6413 CA GLU D 103 3611 3650 3703 10 -18 49 C ATOM 6414 C GLU D 103 -11.612 5.978 18.576 1.00 28.44 C ANISOU 6414 C GLU D 103 3596 3614 3596 16 7 3 C ATOM 6415 O GLU D 103 -12.672 6.460 18.978 1.00 28.26 O ANISOU 6415 O GLU D 103 3576 3604 3557 16 -26 -5 O ATOM 6416 CB GLU D 103 -10.735 6.034 20.917 1.00 31.83 C ANISOU 6416 CB GLU D 103 4137 4026 3930 -5 62 -94 C ATOM 6417 CG GLU D 103 -9.664 5.631 21.915 1.00 34.15 C ANISOU 6417 CG GLU D 103 4274 4327 4376 29 -62 45 C ATOM 6418 CD GLU D 103 -10.000 6.021 23.339 1.00 36.18 C ANISOU 6418 CD GLU D 103 4611 4613 4522 -6 11 -30 C ATOM 6419 OE1 GLU D 103 -10.452 7.162 23.564 1.00 36.93 O ANISOU 6419 OE1 GLU D 103 4714 4651 4669 15 2 -16 O ATOM 6420 OE2 GLU D 103 -9.806 5.169 24.233 1.00 36.61 O ANISOU 6420 OE2 GLU D 103 4661 4627 4623 9 6 12 O ATOM 6421 N ARG D 104 -11.297 5.939 17.289 1.00 28.18 N ANISOU 6421 N ARG D 104 3579 3574 3552 37 -45 -14 N ATOM 6422 CA ARG D 104 -12.150 6.499 16.250 1.00 27.73 C ANISOU 6422 CA ARG D 104 3527 3525 3486 44 -68 -106 C ATOM 6423 C ARG D 104 -12.639 5.422 15.286 1.00 25.85 C ANISOU 6423 C ARG D 104 3236 3333 3255 50 -26 22 C ATOM 6424 O ARG D 104 -11.962 4.410 15.095 1.00 25.83 O ANISOU 6424 O ARG D 104 3256 3328 3231 48 -15 15 O ATOM 6425 CB ARG D 104 -11.362 7.549 15.463 1.00 31.68 C ANISOU 6425 CB ARG D 104 3939 4090 4007 -66 69 201 C ATOM 6426 CG ARG D 104 -11.216 8.897 16.145 1.00 37.95 C ANISOU 6426 CG ARG D 104 5030 4593 4796 52 -61 -118 C ATOM 6427 CD ARG D 104 -9.878 9.540 15.808 1.00 43.27 C ANISOU 6427 CD ARG D 104 5333 5419 5687 -74 -13 57 C ATOM 6428 NE ARG D 104 -9.458 9.248 14.447 1.00 47.65 N ANISOU 6428 NE ARG D 104 6196 6004 5906 22 -8 -50 N ATOM 6429 CZ ARG D 104 -8.254 9.445 13.933 1.00 50.29 C ANISOU 6429 CZ ARG D 104 6307 6351 6449 0 50 24 C ATOM 6430 NH1 ARG D 104 -7.263 9.960 14.644 1.00 50.64 N ANISOU 6430 NH1 ARG D 104 6414 6399 6427 -4 2 -7 N ATOM 6431 NH2 ARG D 104 -8.041 9.118 12.666 1.00 51.39 N ANISOU 6431 NH2 ARG D 104 6533 6493 6502 0 5 -1 N ATOM 6432 N ASP D 105 -13.810 5.629 14.685 1.00 24.07 N ANISOU 6432 N ASP D 105 3127 3067 2950 -8 45 -25 N ATOM 6433 CA ASP D 105 -14.201 4.814 13.535 1.00 22.37 C ANISOU 6433 CA ASP D 105 2887 2825 2789 -10 84 75 C ATOM 6434 C ASP D 105 -13.468 5.345 12.305 1.00 20.31 C ANISOU 6434 C ASP D 105 2581 2557 2581 38 -11 -34 C ATOM 6435 O ASP D 105 -13.361 6.564 12.163 1.00 19.46 O ANISOU 6435 O ASP D 105 2447 2541 2405 6 18 18 O ATOM 6436 CB ASP D 105 -15.703 4.856 13.283 1.00 24.92 C ANISOU 6436 CB ASP D 105 3033 3206 3229 23 -72 -6 C ATOM 6437 CG ASP D 105 -16.532 4.231 14.385 1.00 27.51 C ANISOU 6437 CG ASP D 105 3493 3528 3430 -31 78 59 C ATOM 6438 OD1 ASP D 105 -15.945 3.739 15.371 1.00 27.89 O ANISOU 6438 OD1 ASP D 105 3519 3587 3489 19 9 21 O ATOM 6439 OD2 ASP D 105 -17.776 4.231 14.258 1.00 28.48 O ANISOU 6439 OD2 ASP D 105 3559 3664 3599 -3 0 35 O ATOM 6440 N LEU D 106 -12.972 4.455 11.453 1.00 19.01 N ANISOU 6440 N LEU D 106 2379 2473 2371 -2 -16 54 N ATOM 6441 CA LEU D 106 -12.193 4.894 10.299 1.00 18.15 C ANISOU 6441 CA LEU D 106 2290 2337 2268 8 -52 9 C ATOM 6442 C LEU D 106 -12.616 4.168 9.027 1.00 17.40 C ANISOU 6442 C LEU D 106 2205 2217 2191 0 -5 52 C ATOM 6443 O LEU D 106 -12.942 2.987 9.048 1.00 17.38 O ANISOU 6443 O LEU D 106 2209 2215 2181 9 -1 78 O ATOM 6444 CB LEU D 106 -10.697 4.658 10.513 1.00 17.81 C ANISOU 6444 CB LEU D 106 2250 2275 2244 7 16 22 C ATOM 6445 CG LEU D 106 -9.966 5.492 11.563 1.00 18.07 C ANISOU 6445 CG LEU D 106 2271 2308 2287 0 -2 -2 C ATOM 6446 CD1 LEU D 106 -8.562 4.943 11.793 1.00 18.85 C ANISOU 6446 CD1 LEU D 106 2306 2425 2431 21 9 22 C ATOM 6447 CD2 LEU D 106 -9.909 6.960 11.168 1.00 19.44 C ANISOU 6447 CD2 LEU D 106 2455 2401 2530 -11 3 41 C ATOM 6448 N THR D 107 -12.582 4.885 7.901 1.00 16.72 N ANISOU 6448 N THR D 107 2108 2135 2110 23 -18 7 N ATOM 6449 CA THR D 107 -12.670 4.215 6.604 1.00 16.31 C ANISOU 6449 CA THR D 107 2044 2082 2070 13 -1 30 C ATOM 6450 C THR D 107 -11.326 3.577 6.278 1.00 15.72 C ANISOU 6450 C THR D 107 2027 1978 1967 -5 -15 18 C ATOM 6451 O THR D 107 -10.347 3.793 6.998 1.00 15.27 O ANISOU 6451 O THR D 107 1966 1912 1925 11 4 50 O ATOM 6452 CB THR D 107 -13.045 5.212 5.493 1.00 16.73 C ANISOU 6452 CB THR D 107 2130 2063 2165 13 -30 46 C ATOM 6453 OG1 THR D 107 -11.969 6.138 5.303 1.00 16.18 O ANISOU 6453 OG1 THR D 107 2063 2083 2000 29 -22 54 O ATOM 6454 CG2 THR D 107 -14.301 5.977 5.881 1.00 17.18 C ANISOU 6454 CG2 THR D 107 2160 2244 2124 28 29 8 C ATOM 6455 N LEU D 108 -11.260 2.825 5.183 1.00 15.60 N ANISOU 6455 N LEU D 108 2025 1946 1955 1 10 45 N ATOM 6456 CA LEU D 108 -9.974 2.292 4.731 1.00 15.72 C ANISOU 6456 CA LEU D 108 2015 1969 1990 13 9 56 C ATOM 6457 C LEU D 108 -8.993 3.416 4.432 1.00 15.30 C ANISOU 6457 C LEU D 108 1964 1934 1914 23 -8 31 C ATOM 6458 O LEU D 108 -7.854 3.410 4.911 1.00 15.30 O ANISOU 6458 O LEU D 108 1965 1918 1928 45 6 50 O ATOM 6459 CB LEU D 108 -10.172 1.387 3.521 1.00 17.30 C ANISOU 6459 CB LEU D 108 2277 2147 2150 -89 -69 -27 C ATOM 6460 CG LEU D 108 -8.927 0.774 2.880 1.00 20.24 C ANISOU 6460 CG LEU D 108 2506 2589 2594 52 42 -7 C ATOM 6461 CD1 LEU D 108 -8.156 -0.092 3.865 1.00 20.37 C ANISOU 6461 CD1 LEU D 108 2628 2555 2558 37 25 -1 C ATOM 6462 CD2 LEU D 108 -9.324 -0.041 1.655 1.00 21.42 C ANISOU 6462 CD2 LEU D 108 2760 2691 2688 -13 -24 -9 C ATOM 6463 N ARG D 109 -9.432 4.426 3.674 1.00 15.10 N ANISOU 6463 N ARG D 109 1933 1915 1890 14 1 17 N ATOM 6464 CA ARG D 109 -8.593 5.586 3.414 1.00 14.84 C ANISOU 6464 CA ARG D 109 1895 1884 1859 16 -3 -22 C ATOM 6465 C ARG D 109 -8.188 6.300 4.698 1.00 14.13 C ANISOU 6465 C ARG D 109 1787 1772 1811 20 6 27 C ATOM 6466 O ARG D 109 -7.017 6.644 4.867 1.00 13.87 O ANISOU 6466 O ARG D 109 1755 1765 1749 17 45 53 O ATOM 6467 CB AARG D 109 -9.316 6.566 2.479 0.50 14.41 C ANISOU 6467 CB AARG D 109 1809 1798 1866 -55 32 1 C ATOM 6468 CB BARG D 109 -9.276 6.561 2.448 0.50 16.89 C ANISOU 6468 CB BARG D 109 2171 2172 2073 133 -78 74 C ATOM 6469 CG AARG D 109 -8.537 7.845 2.249 0.50 12.66 C ANISOU 6469 CG AARG D 109 1587 1627 1597 68 -41 30 C ATOM 6470 CG BARG D 109 -8.388 7.733 2.067 0.50 20.24 C ANISOU 6470 CG BARG D 109 2527 2495 2671 -72 39 -6 C ATOM 6471 CD AARG D 109 -9.326 8.876 1.447 0.50 11.07 C ANISOU 6471 CD AARG D 109 1411 1367 1428 -52 10 -22 C ATOM 6472 CD BARG D 109 -8.886 8.466 0.832 0.50 22.72 C ANISOU 6472 CD BARG D 109 2915 2921 2797 69 -44 21 C ATOM 6473 NE AARG D 109 -8.641 10.156 1.535 0.50 9.21 N ANISOU 6473 NE AARG D 109 1186 1228 1085 36 -20 20 N ATOM 6474 NE BARG D 109 -8.010 9.584 0.487 0.50 24.74 N ANISOU 6474 NE BARG D 109 3084 3139 3176 -26 11 62 N ATOM 6475 CZ AARG D 109 -7.622 10.575 0.797 0.50 9.33 C ANISOU 6475 CZ AARG D 109 1176 1165 1206 34 7 28 C ATOM 6476 CZ BARG D 109 -7.912 10.703 1.196 0.50 26.23 C ANISOU 6476 CZ BARG D 109 3372 3275 3319 33 -34 -33 C ATOM 6477 NH1AARG D 109 -7.106 9.851 -0.183 0.50 9.31 N ANISOU 6477 NH1AARG D 109 1140 1210 1187 8 -2 8 N ATOM 6478 NH1BARG D 109 -8.647 10.863 2.290 0.50 26.76 N ANISOU 6478 NH1BARG D 109 3404 3406 3360 10 -9 2 N ATOM 6479 NH2AARG D 109 -7.154 11.784 1.087 0.50 9.55 N ANISOU 6479 NH2AARG D 109 1182 1231 1214 28 -46 -12 N ATOM 6480 NH2BARG D 109 -7.093 11.676 0.826 0.50 27.29 N ANISOU 6480 NH2BARG D 109 3433 3428 3507 -12 0 7 N ATOM 6481 N GLY D 110 -9.133 6.515 5.608 1.00 14.00 N ANISOU 6481 N GLY D 110 1806 1733 1781 31 6 19 N ATOM 6482 CA GLY D 110 -8.835 7.137 6.892 1.00 14.20 C ANISOU 6482 CA GLY D 110 1820 1792 1781 15 -15 27 C ATOM 6483 C GLY D 110 -7.783 6.341 7.659 1.00 14.17 C ANISOU 6483 C GLY D 110 1810 1791 1784 9 -9 29 C ATOM 6484 O GLY D 110 -6.787 6.901 8.123 1.00 14.32 O ANISOU 6484 O GLY D 110 1826 1806 1808 -8 5 42 O ATOM 6485 N ALA D 111 -7.985 5.030 7.769 1.00 13.96 N ANISOU 6485 N ALA D 111 1808 1778 1716 22 -2 27 N ATOM 6486 CA ALA D 111 -7.028 4.169 8.457 1.00 14.14 C ANISOU 6486 CA ALA D 111 1780 1815 1776 18 -6 31 C ATOM 6487 C ALA D 111 -5.651 4.180 7.806 1.00 14.26 C ANISOU 6487 C ALA D 111 1800 1841 1776 9 5 4 C ATOM 6488 O ALA D 111 -4.641 4.123 8.512 1.00 14.24 O ANISOU 6488 O ALA D 111 1791 1860 1760 34 18 14 O ATOM 6489 CB ALA D 111 -7.563 2.747 8.532 1.00 14.92 C ANISOU 6489 CB ALA D 111 1931 1847 1889 -14 -46 4 C ATOM 6490 N ILE D 112 -5.576 4.239 6.480 1.00 14.22 N ANISOU 6490 N ILE D 112 1817 1811 1774 0 -17 9 N ATOM 6491 CA ILE D 112 -4.283 4.360 5.807 1.00 14.66 C ANISOU 6491 CA ILE D 112 1861 1865 1844 4 16 17 C ATOM 6492 C ILE D 112 -3.610 5.682 6.137 1.00 14.90 C ANISOU 6492 C ILE D 112 1911 1893 1857 -13 7 15 C ATOM 6493 O ILE D 112 -2.398 5.710 6.376 1.00 15.37 O ANISOU 6493 O ILE D 112 1937 1975 1929 12 -14 25 O ATOM 6494 CB ILE D 112 -4.440 4.153 4.290 1.00 15.54 C ANISOU 6494 CB ILE D 112 1996 2016 1891 0 -2 12 C ATOM 6495 CG1 ILE D 112 -4.743 2.671 4.034 1.00 16.52 C ANISOU 6495 CG1 ILE D 112 2123 2062 2092 -2 14 -6 C ATOM 6496 CG2 ILE D 112 -3.204 4.582 3.518 1.00 15.41 C ANISOU 6496 CG2 ILE D 112 1991 1965 1898 11 -2 30 C ATOM 6497 CD1 ILE D 112 -5.195 2.351 2.627 1.00 17.09 C ANISOU 6497 CD1 ILE D 112 2218 2150 2126 -20 -32 2 C ATOM 6498 N GLN D 113 -4.364 6.777 6.190 1.00 15.18 N ANISOU 6498 N GLN D 113 1957 1928 1882 14 23 13 N ATOM 6499 CA GLN D 113 -3.759 8.095 6.308 1.00 15.82 C ANISOU 6499 CA GLN D 113 2022 1975 2015 -17 17 1 C ATOM 6500 C GLN D 113 -3.542 8.586 7.725 1.00 16.29 C ANISOU 6500 C GLN D 113 2092 2064 2035 -13 6 7 C ATOM 6501 O GLN D 113 -2.823 9.577 7.901 1.00 16.72 O ANISOU 6501 O GLN D 113 2174 2095 2084 -43 -39 17 O ATOM 6502 CB GLN D 113 -4.612 9.114 5.532 1.00 16.93 C ANISOU 6502 CB GLN D 113 2190 2066 2177 34 -24 55 C ATOM 6503 CG GLN D 113 -4.747 8.702 4.074 1.00 18.74 C ANISOU 6503 CG GLN D 113 2484 2358 2279 -31 9 12 C ATOM 6504 CD GLN D 113 -4.426 9.815 3.103 1.00 17.85 C ANISOU 6504 CD GLN D 113 2329 2096 2356 -32 -1 -71 C ATOM 6505 OE1 GLN D 113 -4.383 9.573 1.894 1.00 19.86 O ANISOU 6505 OE1 GLN D 113 2612 2525 2411 -5 -37 -44 O ATOM 6506 NE2 GLN D 113 -4.188 11.016 3.618 1.00 13.37 N ANISOU 6506 NE2 GLN D 113 1696 1880 1503 32 10 74 N ATOM 6507 N VAL D 114 -4.148 7.944 8.719 1.00 16.08 N ANISOU 6507 N VAL D 114 2056 2039 2014 16 -15 36 N ATOM 6508 CA VAL D 114 -3.967 8.373 10.103 1.00 16.33 C ANISOU 6508 CA VAL D 114 2118 2057 2031 6 -30 23 C ATOM 6509 C VAL D 114 -3.308 7.254 10.913 1.00 16.19 C ANISOU 6509 C VAL D 114 2090 2050 2011 12 -12 13 C ATOM 6510 O VAL D 114 -3.237 6.128 10.435 1.00 16.48 O ANISOU 6510 O VAL D 114 2159 2122 1980 13 6 -33 O ATOM 6511 CB VAL D 114 -5.285 8.741 10.805 1.00 17.63 C ANISOU 6511 CB VAL D 114 2197 2227 2275 52 16 -6 C ATOM 6512 CG1 VAL D 114 -6.045 9.823 10.054 1.00 17.54 C ANISOU 6512 CG1 VAL D 114 2224 2214 2228 18 -30 -12 C ATOM 6513 CG2 VAL D 114 -6.159 7.504 10.981 1.00 18.34 C ANISOU 6513 CG2 VAL D 114 2332 2310 2325 -3 26 53 C ATOM 6514 N SER D 115 -2.915 7.560 12.146 1.00 16.03 N ANISOU 6514 N SER D 115 2061 2027 2001 11 -5 9 N ATOM 6515 CA SER D 115 -2.404 6.511 13.029 1.00 16.36 C ANISOU 6515 CA SER D 115 2079 2051 2086 22 12 48 C ATOM 6516 C SER D 115 -3.535 5.570 13.436 1.00 16.22 C ANISOU 6516 C SER D 115 2064 2051 2046 13 -2 27 C ATOM 6517 O SER D 115 -4.519 5.993 14.047 1.00 16.38 O ANISOU 6517 O SER D 115 2047 2140 2037 21 3 67 O ATOM 6518 CB SER D 115 -1.731 7.104 14.263 1.00 17.73 C ANISOU 6518 CB SER D 115 2316 2226 2194 -12 -25 -25 C ATOM 6519 OG SER D 115 -1.372 6.075 15.176 1.00 18.35 O ANISOU 6519 OG SER D 115 2344 2332 2296 24 -31 49 O ATOM 6520 N ALA D 116 -3.400 4.297 13.095 1.00 16.16 N ANISOU 6520 N ALA D 116 2055 2061 2025 4 12 15 N ATOM 6521 CA ALA D 116 -4.450 3.313 13.338 1.00 16.02 C ANISOU 6521 CA ALA D 116 2065 2008 2014 3 2 -5 C ATOM 6522 C ALA D 116 -3.835 1.951 13.637 1.00 15.92 C ANISOU 6522 C ALA D 116 2073 2001 1975 -10 14 -3 C ATOM 6523 O ALA D 116 -4.144 0.936 13.014 1.00 15.28 O ANISOU 6523 O ALA D 116 1990 1959 1856 -33 31 49 O ATOM 6524 CB ALA D 116 -5.386 3.229 12.140 1.00 16.97 C ANISOU 6524 CB ALA D 116 2141 2237 2071 14 -37 15 C ATOM 6525 N VAL D 117 -2.979 1.924 14.660 1.00 16.34 N ANISOU 6525 N VAL D 117 2102 2097 2009 0 -3 -24 N ATOM 6526 CA VAL D 117 -2.178 0.746 14.969 1.00 17.07 C ANISOU 6526 CA VAL D 117 2194 2166 2127 29 -43 -1 C ATOM 6527 C VAL D 117 -3.002 -0.507 15.177 1.00 17.86 C ANISOU 6527 C VAL D 117 2304 2232 2248 -13 -9 17 C ATOM 6528 O VAL D 117 -2.705 -1.548 14.582 1.00 17.51 O ANISOU 6528 O VAL D 117 2209 2227 2216 10 11 27 O ATOM 6529 CB VAL D 117 -1.203 1.009 16.129 1.00 16.21 C ANISOU 6529 CB VAL D 117 2104 1994 2060 7 17 -5 C ATOM 6530 CG1 VAL D 117 -0.566 -0.270 16.642 1.00 16.07 C ANISOU 6530 CG1 VAL D 117 2067 2055 1985 30 14 25 C ATOM 6531 CG2 VAL D 117 -0.110 1.967 15.660 1.00 16.11 C ANISOU 6531 CG2 VAL D 117 1993 2121 2008 12 -23 22 C ATOM 6532 N PRO D 118 -4.058 -0.450 15.984 1.00 18.65 N ANISOU 6532 N PRO D 118 2351 2375 2362 -5 28 19 N ATOM 6533 CA PRO D 118 -4.913 -1.601 16.216 1.00 18.67 C ANISOU 6533 CA PRO D 118 2363 2361 2372 -11 -9 5 C ATOM 6534 C PRO D 118 -5.464 -2.208 14.940 1.00 18.15 C ANISOU 6534 C PRO D 118 2312 2288 2295 23 26 29 C ATOM 6535 O PRO D 118 -5.527 -3.432 14.798 1.00 18.19 O ANISOU 6535 O PRO D 118 2354 2281 2275 3 36 40 O ATOM 6536 CB PRO D 118 -6.014 -1.058 17.120 1.00 19.22 C ANISOU 6536 CB PRO D 118 2430 2427 2443 -9 35 -6 C ATOM 6537 CG PRO D 118 -5.390 0.076 17.852 1.00 19.44 C ANISOU 6537 CG PRO D 118 2467 2449 2472 -12 27 -16 C ATOM 6538 CD PRO D 118 -4.330 0.645 16.946 1.00 19.18 C ANISOU 6538 CD PRO D 118 2458 2402 2429 9 23 0 C ATOM 6539 N VAL D 119 -5.874 -1.379 13.981 1.00 17.58 N ANISOU 6539 N VAL D 119 2212 2258 2210 8 33 -8 N ATOM 6540 CA VAL D 119 -6.424 -1.861 12.724 1.00 17.10 C ANISOU 6540 CA VAL D 119 2147 2170 2182 -2 40 13 C ATOM 6541 C VAL D 119 -5.412 -2.687 11.945 1.00 16.35 C ANISOU 6541 C VAL D 119 2079 2069 2062 -30 2 43 C ATOM 6542 O VAL D 119 -5.740 -3.787 11.496 1.00 16.53 O ANISOU 6542 O VAL D 119 2137 2040 2105 -27 18 64 O ATOM 6543 CB VAL D 119 -6.922 -0.692 11.851 1.00 18.00 C ANISOU 6543 CB VAL D 119 2283 2265 2292 28 -44 44 C ATOM 6544 CG1 VAL D 119 -7.364 -1.162 10.474 1.00 17.96 C ANISOU 6544 CG1 VAL D 119 2252 2268 2306 10 12 -19 C ATOM 6545 CG2 VAL D 119 -8.066 0.024 12.560 1.00 18.79 C ANISOU 6545 CG2 VAL D 119 2408 2379 2351 22 44 1 C ATOM 6546 N PHE D 120 -4.199 -2.157 11.763 1.00 15.57 N ANISOU 6546 N PHE D 120 1998 1958 1961 28 -27 44 N ATOM 6547 CA PHE D 120 -3.236 -2.843 10.905 1.00 15.23 C ANISOU 6547 CA PHE D 120 1917 1927 1941 -9 -22 48 C ATOM 6548 C PHE D 120 -2.611 -4.046 11.588 1.00 15.17 C ANISOU 6548 C PHE D 120 1915 1917 1935 11 -3 24 C ATOM 6549 O PHE D 120 -2.306 -5.023 10.901 1.00 15.32 O ANISOU 6549 O PHE D 120 1978 1903 1941 61 -4 58 O ATOM 6550 CB PHE D 120 -2.187 -1.862 10.356 1.00 15.07 C ANISOU 6550 CB PHE D 120 1934 1923 1870 -20 -22 33 C ATOM 6551 CG PHE D 120 -2.861 -0.989 9.321 1.00 15.16 C ANISOU 6551 CG PHE D 120 1969 1947 1843 21 23 27 C ATOM 6552 CD1 PHE D 120 -3.486 0.181 9.699 1.00 15.32 C ANISOU 6552 CD1 PHE D 120 2008 1927 1887 -12 13 -14 C ATOM 6553 CD2 PHE D 120 -2.887 -1.380 7.992 1.00 14.00 C ANISOU 6553 CD2 PHE D 120 1735 1776 1809 -46 -44 4 C ATOM 6554 CE1 PHE D 120 -4.124 0.970 8.762 1.00 15.77 C ANISOU 6554 CE1 PHE D 120 1978 2033 1981 2 6 34 C ATOM 6555 CE2 PHE D 120 -3.524 -0.589 7.052 1.00 14.29 C ANISOU 6555 CE2 PHE D 120 1844 1785 1801 -55 34 96 C ATOM 6556 CZ PHE D 120 -4.141 0.584 7.438 1.00 15.99 C ANISOU 6556 CZ PHE D 120 2083 1960 2033 -1 43 -38 C ATOM 6557 N GLN D 121 -2.488 -4.026 12.912 1.00 15.45 N ANISOU 6557 N GLN D 121 1946 1981 1944 5 20 17 N ATOM 6558 CA GLN D 121 -2.080 -5.240 13.624 1.00 16.32 C ANISOU 6558 CA GLN D 121 2127 2029 2044 32 2 36 C ATOM 6559 C GLN D 121 -3.123 -6.336 13.454 1.00 16.68 C ANISOU 6559 C GLN D 121 2168 2089 2082 -2 17 40 C ATOM 6560 O GLN D 121 -2.792 -7.479 13.135 1.00 16.35 O ANISOU 6560 O GLN D 121 2177 2064 1972 -9 10 67 O ATOM 6561 CB GLN D 121 -1.798 -4.936 15.093 1.00 16.87 C ANISOU 6561 CB GLN D 121 2226 2100 2082 16 -16 0 C ATOM 6562 CG GLN D 121 -0.526 -4.143 15.322 1.00 18.06 C ANISOU 6562 CG GLN D 121 2260 2252 2349 -14 10 68 C ATOM 6563 CD GLN D 121 -0.319 -3.698 16.751 1.00 20.70 C ANISOU 6563 CD GLN D 121 2715 2652 2496 12 36 -24 C ATOM 6564 OE1 GLN D 121 0.804 -3.370 17.148 1.00 23.39 O ANISOU 6564 OE1 GLN D 121 2884 3065 2937 -24 -64 -23 O ATOM 6565 NE2 GLN D 121 -1.380 -3.664 17.546 1.00 20.49 N ANISOU 6565 NE2 GLN D 121 2653 2629 2504 10 5 17 N ATOM 6566 N GLN D 122 -4.401 -5.991 13.596 1.00 17.31 N ANISOU 6566 N GLN D 122 2209 2223 2145 13 5 68 N ATOM 6567 CA GLN D 122 -5.486 -6.941 13.380 1.00 18.34 C ANISOU 6567 CA GLN D 122 2427 2281 2260 -84 -53 51 C ATOM 6568 C GLN D 122 -5.514 -7.459 11.952 1.00 17.79 C ANISOU 6568 C GLN D 122 2297 2222 2238 -24 -5 54 C ATOM 6569 O GLN D 122 -5.621 -8.667 11.730 1.00 18.19 O ANISOU 6569 O GLN D 122 2352 2228 2333 -30 20 85 O ATOM 6570 CB GLN D 122 -6.825 -6.305 13.760 1.00 22.81 C ANISOU 6570 CB GLN D 122 2830 2951 2887 239 57 -24 C ATOM 6571 CG GLN D 122 -8.013 -7.248 13.742 1.00 28.73 C ANISOU 6571 CG GLN D 122 3447 3635 3836 -136 12 -119 C ATOM 6572 CD GLN D 122 -7.977 -8.283 14.846 1.00 33.72 C ANISOU 6572 CD GLN D 122 4337 4212 4262 30 53 144 C ATOM 6573 OE1 GLN D 122 -7.467 -8.030 15.938 1.00 35.63 O ANISOU 6573 OE1 GLN D 122 4561 4509 4467 -36 -39 -10 O ATOM 6574 NE2 GLN D 122 -8.524 -9.464 14.572 1.00 34.72 N ANISOU 6574 NE2 GLN D 122 4425 4343 4425 -10 2 1 N ATOM 6575 N ILE D 123 -5.382 -6.584 10.953 1.00 17.11 N ANISOU 6575 N ILE D 123 2159 2173 2170 -23 7 24 N ATOM 6576 CA ILE D 123 -5.326 -7.039 9.564 1.00 16.73 C ANISOU 6576 CA ILE D 123 2132 2068 2156 -11 30 29 C ATOM 6577 C ILE D 123 -4.239 -8.087 9.360 1.00 16.38 C ANISOU 6577 C ILE D 123 2108 2042 2074 -22 10 52 C ATOM 6578 O ILE D 123 -4.479 -9.131 8.751 1.00 16.44 O ANISOU 6578 O ILE D 123 2133 2060 2053 -32 17 41 O ATOM 6579 CB ILE D 123 -5.114 -5.861 8.593 1.00 16.83 C ANISOU 6579 CB ILE D 123 2144 2121 2129 10 24 59 C ATOM 6580 CG1 ILE D 123 -6.368 -4.979 8.579 1.00 17.12 C ANISOU 6580 CG1 ILE D 123 2154 2103 2250 -12 -31 7 C ATOM 6581 CG2 ILE D 123 -4.786 -6.350 7.190 1.00 17.45 C ANISOU 6581 CG2 ILE D 123 2241 2194 2195 -31 18 -12 C ATOM 6582 CD1 ILE D 123 -6.166 -3.632 7.918 1.00 16.69 C ANISOU 6582 CD1 ILE D 123 2127 2136 2078 13 -39 31 C ATOM 6583 N ALA D 124 -3.027 -7.810 9.828 1.00 16.53 N ANISOU 6583 N ALA D 124 2120 2066 2094 -18 -9 34 N ATOM 6584 CA ALA D 124 -1.911 -8.734 9.665 1.00 16.84 C ANISOU 6584 CA ALA D 124 2110 2135 2154 -4 -4 27 C ATOM 6585 C ALA D 124 -2.180 -10.079 10.329 1.00 17.11 C ANISOU 6585 C ALA D 124 2167 2140 2194 6 -18 26 C ATOM 6586 O ALA D 124 -1.916 -11.122 9.725 1.00 16.94 O ANISOU 6586 O ALA D 124 2172 2106 2158 -22 -7 46 O ATOM 6587 CB ALA D 124 -0.638 -8.116 10.216 1.00 16.59 C ANISOU 6587 CB ALA D 124 2147 2047 2108 -11 -21 21 C ATOM 6588 N ARG D 125 -2.724 -10.077 11.545 1.00 17.71 N ANISOU 6588 N ARG D 125 2215 2266 2247 11 0 -10 N ATOM 6589 CA ARG D 125 -3.027 -11.339 12.216 1.00 18.83 C ANISOU 6589 CA ARG D 125 2381 2322 2452 -7 -18 48 C ATOM 6590 C ARG D 125 -4.056 -12.150 11.438 1.00 18.98 C ANISOU 6590 C ARG D 125 2379 2381 2453 -10 -8 33 C ATOM 6591 O ARG D 125 -3.908 -13.365 11.288 1.00 19.28 O ANISOU 6591 O ARG D 125 2426 2401 2497 3 -20 28 O ATOM 6592 CB ARG D 125 -3.505 -11.131 13.651 1.00 21.87 C ANISOU 6592 CB ARG D 125 2846 2836 2628 69 116 64 C ATOM 6593 CG ARG D 125 -2.587 -10.286 14.512 1.00 25.64 C ANISOU 6593 CG ARG D 125 3209 3188 3346 -61 -75 -85 C ATOM 6594 CD ARG D 125 -2.845 -10.503 15.997 1.00 29.83 C ANISOU 6594 CD ARG D 125 3798 3902 3633 -15 13 94 C ATOM 6595 NE ARG D 125 -3.013 -9.213 16.675 1.00 33.50 N ANISOU 6595 NE ARG D 125 4389 4164 4177 -39 16 -71 N ATOM 6596 CZ ARG D 125 -4.194 -8.608 16.766 1.00 35.92 C ANISOU 6596 CZ ARG D 125 4519 4586 4543 69 19 34 C ATOM 6597 NH1 ARG D 125 -5.273 -9.186 16.255 1.00 36.78 N ANISOU 6597 NH1 ARG D 125 4678 4646 4651 -39 -7 8 N ATOM 6598 NH2 ARG D 125 -4.303 -7.440 17.381 1.00 37.20 N ANISOU 6598 NH2 ARG D 125 4775 4640 4718 -8 -2 2 N ATOM 6599 N GLU D 126 -5.101 -11.498 10.934 1.00 18.81 N ANISOU 6599 N GLU D 126 2395 2378 2375 -25 6 75 N ATOM 6600 CA GLU D 126 -6.117 -12.180 10.143 1.00 18.93 C ANISOU 6600 CA GLU D 126 2442 2382 2368 -47 28 18 C ATOM 6601 C GLU D 126 -5.585 -12.703 8.820 1.00 18.21 C ANISOU 6601 C GLU D 126 2303 2287 2328 -21 2 52 C ATOM 6602 O GLU D 126 -5.979 -13.792 8.396 1.00 18.77 O ANISOU 6602 O GLU D 126 2375 2321 2435 -40 -9 40 O ATOM 6603 CB GLU D 126 -7.328 -11.256 9.942 1.00 21.54 C ANISOU 6603 CB GLU D 126 2658 2626 2899 55 -72 47 C ATOM 6604 CG GLU D 126 -8.091 -11.047 11.241 1.00 24.98 C ANISOU 6604 CG GLU D 126 3253 3174 3065 -61 65 -4 C ATOM 6605 CD GLU D 126 -9.304 -10.156 11.143 1.00 27.93 C ANISOU 6605 CD GLU D 126 3459 3515 3638 47 4 26 C ATOM 6606 OE1 GLU D 126 -9.939 -10.089 10.071 1.00 29.15 O ANISOU 6606 OE1 GLU D 126 3673 3741 3663 7 -20 31 O ATOM 6607 OE2 GLU D 126 -9.655 -9.507 12.154 1.00 29.06 O ANISOU 6607 OE2 GLU D 126 3691 3643 3709 5 -10 -34 O ATOM 6608 N VAL D 127 -4.693 -11.972 8.153 1.00 17.15 N ANISOU 6608 N VAL D 127 2169 2141 2208 42 -25 28 N ATOM 6609 CA VAL D 127 -4.031 -12.481 6.959 1.00 16.92 C ANISOU 6609 CA VAL D 127 2162 2086 2181 -22 -13 38 C ATOM 6610 C VAL D 127 -3.237 -13.741 7.296 1.00 16.92 C ANISOU 6610 C VAL D 127 2154 2107 2170 0 1 30 C ATOM 6611 O VAL D 127 -3.373 -14.757 6.622 1.00 16.67 O ANISOU 6611 O VAL D 127 2128 2048 2159 -10 -2 82 O ATOM 6612 CB VAL D 127 -3.102 -11.436 6.320 1.00 15.97 C ANISOU 6612 CB VAL D 127 2028 2051 1990 10 -21 -6 C ATOM 6613 CG1 VAL D 127 -2.235 -12.028 5.220 1.00 15.84 C ANISOU 6613 CG1 VAL D 127 2022 1963 2033 19 -8 16 C ATOM 6614 CG2 VAL D 127 -3.940 -10.286 5.768 1.00 16.58 C ANISOU 6614 CG2 VAL D 127 2095 2106 2099 5 -55 54 C ATOM 6615 N GLY D 128 -2.384 -13.641 8.311 1.00 17.65 N ANISOU 6615 N GLY D 128 2231 2228 2247 -23 -38 28 N ATOM 6616 CA GLY D 128 -1.649 -14.801 8.793 1.00 17.77 C ANISOU 6616 CA GLY D 128 2252 2238 2261 13 -4 19 C ATOM 6617 C GLY D 128 -0.309 -14.969 8.090 1.00 17.77 C ANISOU 6617 C GLY D 128 2255 2260 2238 -18 -4 9 C ATOM 6618 O GLY D 128 -0.066 -14.417 7.019 1.00 17.39 O ANISOU 6618 O GLY D 128 2178 2180 2248 -40 -34 32 O ATOM 6619 N GLU D 129 0.552 -15.796 8.679 1.00 18.14 N ANISOU 6619 N GLU D 129 2319 2273 2300 5 -21 -7 N ATOM 6620 CA GLU D 129 1.914 -15.983 8.219 1.00 18.89 C ANISOU 6620 CA GLU D 129 2387 2426 2365 -71 74 -102 C ATOM 6621 C GLU D 129 2.017 -16.453 6.775 1.00 17.54 C ANISOU 6621 C GLU D 129 2218 2190 2258 -31 13 -2 C ATOM 6622 O GLU D 129 2.781 -15.878 5.999 1.00 17.06 O ANISOU 6622 O GLU D 129 2175 2127 2180 -11 -5 -18 O ATOM 6623 CB GLU D 129 2.640 -17.015 9.093 1.00 24.16 C ANISOU 6623 CB GLU D 129 2983 2930 3268 173 -34 216 C ATOM 6624 CG GLU D 129 2.993 -16.546 10.486 1.00 31.80 C ANISOU 6624 CG GLU D 129 4097 4151 3835 -98 -3 -198 C ATOM 6625 CD GLU D 129 3.737 -17.587 11.299 1.00 36.79 C ANISOU 6625 CD GLU D 129 4683 4641 4656 128 -17 130 C ATOM 6626 OE1 GLU D 129 3.462 -18.800 11.178 1.00 38.25 O ANISOU 6626 OE1 GLU D 129 4860 4804 4869 -16 -3 -53 O ATOM 6627 OE2 GLU D 129 4.621 -17.174 12.081 1.00 38.56 O ANISOU 6627 OE2 GLU D 129 4912 4874 4864 -13 -35 -18 O ATOM 6628 N VAL D 130 1.291 -17.513 6.430 1.00 16.84 N ANISOU 6628 N VAL D 130 2162 2123 2114 -13 11 43 N ATOM 6629 CA VAL D 130 1.430 -18.127 5.114 1.00 16.69 C ANISOU 6629 CA VAL D 130 2162 2050 2129 -15 -21 25 C ATOM 6630 C VAL D 130 1.001 -17.176 4.003 1.00 16.55 C ANISOU 6630 C VAL D 130 2125 2073 2093 -15 -29 10 C ATOM 6631 O VAL D 130 1.751 -16.984 3.047 1.00 16.79 O ANISOU 6631 O VAL D 130 2149 2171 2058 -20 -54 -16 O ATOM 6632 CB VAL D 130 0.643 -19.446 5.022 1.00 16.34 C ANISOU 6632 CB VAL D 130 2079 2043 2087 -6 -34 -2 C ATOM 6633 CG1 VAL D 130 0.637 -19.997 3.608 1.00 16.24 C ANISOU 6633 CG1 VAL D 130 2092 1989 2090 18 -9 16 C ATOM 6634 CG2 VAL D 130 1.268 -20.456 5.983 1.00 17.28 C ANISOU 6634 CG2 VAL D 130 2235 2134 2195 25 -45 60 C ATOM 6635 N ARG D 131 -0.176 -16.580 4.145 1.00 16.48 N ANISOU 6635 N ARG D 131 2119 2054 2091 -26 -48 10 N ATOM 6636 CA ARG D 131 -0.672 -15.653 3.129 1.00 16.60 C ANISOU 6636 CA ARG D 131 2157 2062 2089 -18 -27 15 C ATOM 6637 C ARG D 131 0.186 -14.399 3.061 1.00 16.56 C ANISOU 6637 C ARG D 131 2146 2081 2065 -36 -27 -16 C ATOM 6638 O ARG D 131 0.513 -13.932 1.963 1.00 16.93 O ANISOU 6638 O ARG D 131 2203 2096 2132 -66 6 27 O ATOM 6639 CB ARG D 131 -2.143 -15.313 3.377 1.00 17.25 C ANISOU 6639 CB ARG D 131 2176 2175 2203 -14 -21 28 C ATOM 6640 CG ARG D 131 -3.055 -16.521 3.194 1.00 17.57 C ANISOU 6640 CG ARG D 131 2189 2189 2298 -15 -17 23 C ATOM 6641 CD ARG D 131 -4.521 -16.145 3.161 1.00 16.09 C ANISOU 6641 CD ARG D 131 2111 1949 2054 -47 -29 54 C ATOM 6642 NE ARG D 131 -5.011 -15.586 4.410 1.00 16.26 N ANISOU 6642 NE ARG D 131 2110 1992 2078 -26 -18 50 N ATOM 6643 CZ ARG D 131 -6.279 -15.305 4.684 1.00 17.67 C ANISOU 6643 CZ ARG D 131 2215 2148 2352 22 36 42 C ATOM 6644 NH1 ARG D 131 -7.220 -15.528 3.776 1.00 19.50 N ANISOU 6644 NH1 ARG D 131 2441 2417 2550 -58 -88 40 N ATOM 6645 NH2 ARG D 131 -6.616 -14.797 5.859 1.00 18.68 N ANISOU 6645 NH2 ARG D 131 2384 2341 2374 -5 15 33 N ATOM 6646 N MET D 132 0.582 -13.859 4.212 1.00 15.65 N ANISOU 6646 N MET D 132 2000 1952 1995 -33 -21 48 N ATOM 6647 CA MET D 132 1.457 -12.688 4.216 1.00 14.63 C ANISOU 6647 CA MET D 132 1889 1855 1815 19 -30 7 C ATOM 6648 C MET D 132 2.751 -12.946 3.459 1.00 14.18 C ANISOU 6648 C MET D 132 1860 1763 1766 -5 -32 17 C ATOM 6649 O MET D 132 3.164 -12.169 2.596 1.00 13.57 O ANISOU 6649 O MET D 132 1755 1646 1756 8 -87 20 O ATOM 6650 CB MET D 132 1.771 -12.247 5.647 1.00 13.71 C ANISOU 6650 CB MET D 132 1792 1642 1773 1 -6 10 C ATOM 6651 CG MET D 132 2.505 -10.918 5.728 1.00 12.64 C ANISOU 6651 CG MET D 132 1579 1580 1646 54 -38 36 C ATOM 6652 SD MET D 132 1.477 -9.521 5.232 1.00 12.37 S ANISOU 6652 SD MET D 132 1683 1579 1439 -36 -180 206 S ATOM 6653 CE MET D 132 0.413 -9.323 6.657 1.00 14.53 C ANISOU 6653 CE MET D 132 1855 1873 1794 27 22 16 C ATOM 6654 N GLN D 133 3.424 -14.057 3.758 1.00 14.35 N ANISOU 6654 N GLN D 133 1852 1803 1797 8 -44 41 N ATOM 6655 CA GLN D 133 4.652 -14.440 3.087 1.00 14.69 C ANISOU 6655 CA GLN D 133 1889 1839 1852 -2 -16 -6 C ATOM 6656 C GLN D 133 4.480 -14.607 1.581 1.00 14.63 C ANISOU 6656 C GLN D 133 1892 1819 1849 0 5 7 C ATOM 6657 O GLN D 133 5.310 -14.142 0.799 1.00 14.71 O ANISOU 6657 O GLN D 133 1895 1868 1827 -15 -6 8 O ATOM 6658 CB GLN D 133 5.172 -15.768 3.663 1.00 15.95 C ANISOU 6658 CB GLN D 133 2064 1957 2041 47 -53 73 C ATOM 6659 CG GLN D 133 6.497 -16.199 3.046 1.00 17.20 C ANISOU 6659 CG GLN D 133 2187 2218 2132 49 29 39 C ATOM 6660 CD GLN D 133 7.623 -15.282 3.487 1.00 18.72 C ANISOU 6660 CD GLN D 133 2351 2394 2370 16 -69 -56 C ATOM 6661 OE1 GLN D 133 7.894 -14.267 2.845 1.00 21.69 O ANISOU 6661 OE1 GLN D 133 2832 2609 2801 -63 77 65 O ATOM 6662 NE2 GLN D 133 8.258 -15.647 4.588 1.00 16.65 N ANISOU 6662 NE2 GLN D 133 2116 1963 2249 -54 7 -35 N ATOM 6663 N LYS D 134 3.407 -15.283 1.182 1.00 14.48 N ANISOU 6663 N LYS D 134 1882 1759 1861 16 -4 29 N ATOM 6664 CA LYS D 134 3.104 -15.497 -0.224 1.00 15.71 C ANISOU 6664 CA LYS D 134 2108 1936 1923 49 -31 26 C ATOM 6665 C LYS D 134 3.026 -14.174 -0.984 1.00 15.12 C ANISOU 6665 C LYS D 134 1943 1910 1894 2 -37 17 C ATOM 6666 O LYS D 134 3.665 -14.041 -2.025 1.00 15.27 O ANISOU 6666 O LYS D 134 1918 1953 1931 22 -32 7 O ATOM 6667 CB LYS D 134 1.790 -16.259 -0.393 1.00 19.86 C ANISOU 6667 CB LYS D 134 2375 2429 2742 -129 -1 35 C ATOM 6668 CG LYS D 134 1.352 -16.449 -1.836 1.00 24.61 C ANISOU 6668 CG LYS D 134 3278 3123 2951 57 -46 0 C ATOM 6669 CD LYS D 134 0.018 -17.171 -1.936 1.00 28.41 C ANISOU 6669 CD LYS D 134 3561 3589 3643 -113 -35 16 C ATOM 6670 CE LYS D 134 -1.132 -16.314 -1.435 1.00 30.48 C ANISOU 6670 CE LYS D 134 3865 3845 3873 77 16 -18 C ATOM 6671 NZ LYS D 134 -2.404 -17.084 -1.348 1.00 31.81 N ANISOU 6671 NZ LYS D 134 4013 4001 4072 -23 -12 4 N ATOM 6672 N TYR D 135 2.253 -13.223 -0.467 1.00 15.23 N ANISOU 6672 N TYR D 135 1953 1902 1930 -29 -2 8 N ATOM 6673 CA TYR D 135 2.084 -11.951 -1.159 1.00 15.69 C ANISOU 6673 CA TYR D 135 2019 1943 2000 -21 -37 34 C ATOM 6674 C TYR D 135 3.341 -11.099 -1.171 1.00 15.25 C ANISOU 6674 C TYR D 135 1970 1906 1920 1 -33 11 C ATOM 6675 O TYR D 135 3.632 -10.477 -2.197 1.00 15.24 O ANISOU 6675 O TYR D 135 1996 1888 1906 -41 -20 -6 O ATOM 6676 CB TYR D 135 0.921 -11.147 -0.571 1.00 16.97 C ANISOU 6676 CB TYR D 135 2162 2128 2158 51 23 -3 C ATOM 6677 CG TYR D 135 -0.413 -11.668 -1.071 1.00 18.68 C ANISOU 6677 CG TYR D 135 2307 2361 2429 -19 -28 -30 C ATOM 6678 CD1 TYR D 135 -0.879 -11.333 -2.333 1.00 19.66 C ANISOU 6678 CD1 TYR D 135 2503 2492 2474 8 -14 7 C ATOM 6679 CD2 TYR D 135 -1.183 -12.502 -0.274 1.00 19.58 C ANISOU 6679 CD2 TYR D 135 2479 2456 2506 -16 27 33 C ATOM 6680 CE1 TYR D 135 -2.094 -11.811 -2.789 1.00 20.35 C ANISOU 6680 CE1 TYR D 135 2592 2576 2563 -5 -62 -14 C ATOM 6681 CE2 TYR D 135 -2.399 -12.982 -0.725 1.00 20.55 C ANISOU 6681 CE2 TYR D 135 2591 2581 2637 -46 -11 1 C ATOM 6682 CZ TYR D 135 -2.846 -12.634 -1.980 1.00 21.14 C ANISOU 6682 CZ TYR D 135 2696 2669 2667 -12 -5 22 C ATOM 6683 OH TYR D 135 -4.059 -13.117 -2.420 1.00 22.57 O ANISOU 6683 OH TYR D 135 2802 2853 2922 -49 -43 -20 O ATOM 6684 N LEU D 136 4.107 -11.076 -0.078 1.00 15.04 N ANISOU 6684 N LEU D 136 1931 1871 1913 -4 -24 6 N ATOM 6685 CA LEU D 136 5.349 -10.296 -0.099 1.00 14.76 C ANISOU 6685 CA LEU D 136 1895 1878 1834 2 -16 -6 C ATOM 6686 C LEU D 136 6.347 -10.870 -1.093 1.00 14.64 C ANISOU 6686 C LEU D 136 1886 1863 1815 -27 -8 7 C ATOM 6687 O LEU D 136 7.100 -10.126 -1.725 1.00 14.09 O ANISOU 6687 O LEU D 136 1884 1753 1715 -66 -77 -26 O ATOM 6688 CB LEU D 136 5.939 -10.163 1.304 1.00 14.61 C ANISOU 6688 CB LEU D 136 1832 1867 1852 -9 -39 8 C ATOM 6689 CG LEU D 136 5.109 -9.382 2.325 1.00 14.97 C ANISOU 6689 CG LEU D 136 1916 1817 1957 11 11 10 C ATOM 6690 CD1 LEU D 136 5.944 -9.076 3.561 1.00 17.16 C ANISOU 6690 CD1 LEU D 136 2252 2198 2069 0 -84 -15 C ATOM 6691 CD2 LEU D 136 4.562 -8.081 1.755 1.00 14.31 C ANISOU 6691 CD2 LEU D 136 1823 1812 1801 -11 -28 4 C ATOM 6692 N LYS D 137 6.360 -12.190 -1.273 1.00 15.10 N ANISOU 6692 N LYS D 137 1932 1883 1923 -8 -33 10 N ATOM 6693 CA LYS D 137 7.124 -12.823 -2.338 1.00 15.97 C ANISOU 6693 CA LYS D 137 2045 2067 1954 8 0 -18 C ATOM 6694 C LYS D 137 6.631 -12.392 -3.715 1.00 15.80 C ANISOU 6694 C LYS D 137 2014 2010 1981 10 -5 10 C ATOM 6695 O LYS D 137 7.430 -12.009 -4.572 1.00 15.61 O ANISOU 6695 O LYS D 137 1994 1958 1981 41 -12 26 O ATOM 6696 CB LYS D 137 7.062 -14.348 -2.197 1.00 19.26 C ANISOU 6696 CB LYS D 137 2510 2226 2581 -50 -37 80 C ATOM 6697 CG LYS D 137 7.889 -15.105 -3.223 1.00 22.70 C ANISOU 6697 CG LYS D 137 2839 3003 2782 43 52 -92 C ATOM 6698 CD LYS D 137 7.837 -16.604 -2.974 1.00 27.60 C ANISOU 6698 CD LYS D 137 3601 3313 3574 -45 -50 61 C ATOM 6699 CE LYS D 137 8.830 -17.351 -3.849 1.00 30.30 C ANISOU 6699 CE LYS D 137 3813 3794 3905 24 74 -36 C ATOM 6700 NZ LYS D 137 8.535 -17.186 -5.296 1.00 31.96 N ANISOU 6700 NZ LYS D 137 4048 4068 4027 1 -4 7 N ATOM 6701 N LYS D 138 5.317 -12.409 -3.927 1.00 15.49 N ANISOU 6701 N LYS D 138 2030 1914 1941 26 -18 -1 N ATOM 6702 CA LYS D 138 4.730 -11.985 -5.193 1.00 15.63 C ANISOU 6702 CA LYS D 138 2119 1883 1937 30 -14 1 C ATOM 6703 C LYS D 138 5.030 -10.521 -5.488 1.00 14.80 C ANISOU 6703 C LYS D 138 1964 1841 1818 18 -20 -28 C ATOM 6704 O LYS D 138 5.279 -10.149 -6.636 1.00 15.35 O ANISOU 6704 O LYS D 138 2047 1943 1841 -13 -8 -29 O ATOM 6705 CB LYS D 138 3.215 -12.211 -5.199 1.00 19.91 C ANISOU 6705 CB LYS D 138 2313 2678 2574 -22 -19 31 C ATOM 6706 CG LYS D 138 2.807 -13.669 -5.353 1.00 24.10 C ANISOU 6706 CG LYS D 138 3222 2857 3080 -36 -10 -13 C ATOM 6707 CD LYS D 138 1.292 -13.814 -5.369 1.00 28.07 C ANISOU 6707 CD LYS D 138 3440 3653 3571 21 -9 37 C ATOM 6708 CE LYS D 138 0.883 -15.241 -5.700 1.00 31.00 C ANISOU 6708 CE LYS D 138 4014 3825 3939 -36 -17 -9 C ATOM 6709 NZ LYS D 138 -0.596 -15.383 -5.794 1.00 32.50 N ANISOU 6709 NZ LYS D 138 4093 4103 4153 -5 -3 9 N ATOM 6710 N PHE D 139 5.045 -9.677 -4.459 1.00 13.60 N ANISOU 6710 N PHE D 139 1767 1672 1730 20 -27 49 N ATOM 6711 CA PHE D 139 5.302 -8.255 -4.612 1.00 12.64 C ANISOU 6711 CA PHE D 139 1582 1628 1592 20 -1 5 C ATOM 6712 C PHE D 139 6.782 -7.906 -4.671 1.00 12.26 C ANISOU 6712 C PHE D 139 1573 1523 1564 23 -25 7 C ATOM 6713 O PHE D 139 7.136 -6.732 -4.816 1.00 12.37 O ANISOU 6713 O PHE D 139 1640 1510 1551 24 -44 36 O ATOM 6714 CB PHE D 139 4.660 -7.464 -3.468 1.00 12.33 C ANISOU 6714 CB PHE D 139 1637 1521 1529 -15 -15 36 C ATOM 6715 CG PHE D 139 3.171 -7.535 -3.328 1.00 13.20 C ANISOU 6715 CG PHE D 139 1662 1693 1662 -1 -47 20 C ATOM 6716 CD1 PHE D 139 2.348 -8.071 -4.307 1.00 12.51 C ANISOU 6716 CD1 PHE D 139 1623 1471 1658 -12 -10 7 C ATOM 6717 CD2 PHE D 139 2.576 -7.049 -2.171 1.00 14.11 C ANISOU 6717 CD2 PHE D 139 1813 1764 1785 1 53 2 C ATOM 6718 CE1 PHE D 139 0.981 -8.122 -4.134 1.00 12.81 C ANISOU 6718 CE1 PHE D 139 1643 1573 1652 33 -13 43 C ATOM 6719 CE2 PHE D 139 1.205 -7.087 -1.996 1.00 14.16 C ANISOU 6719 CE2 PHE D 139 1793 1728 1858 -8 -40 -26 C ATOM 6720 CZ PHE D 139 0.403 -7.626 -2.984 1.00 13.41 C ANISOU 6720 CZ PHE D 139 1808 1651 1638 20 6 43 C ATOM 6721 N SER D 140 7.658 -8.889 -4.495 1.00 11.43 N ANISOU 6721 N SER D 140 1497 1429 1415 -8 -30 -17 N ATOM 6722 CA SER D 140 9.092 -8.655 -4.405 1.00 11.60 C ANISOU 6722 CA SER D 140 1494 1422 1490 8 -51 -62 C ATOM 6723 C SER D 140 9.369 -7.553 -3.380 1.00 10.92 C ANISOU 6723 C SER D 140 1414 1381 1355 1 -19 -2 C ATOM 6724 O SER D 140 10.087 -6.595 -3.652 1.00 11.16 O ANISOU 6724 O SER D 140 1404 1473 1363 -50 -36 -17 O ATOM 6725 CB SER D 140 9.697 -8.298 -5.759 1.00 14.47 C ANISOU 6725 CB SER D 140 1909 1870 1719 -62 64 83 C ATOM 6726 OG SER D 140 9.613 -9.388 -6.663 1.00 16.81 O ANISOU 6726 OG SER D 140 2311 2070 2005 -7 -14 -66 O ATOM 6727 N TYR D 141 8.806 -7.727 -2.189 1.00 10.49 N ANISOU 6727 N TYR D 141 1394 1287 1306 -6 -41 14 N ATOM 6728 CA TYR D 141 8.799 -6.647 -1.207 1.00 10.49 C ANISOU 6728 CA TYR D 141 1371 1276 1337 3 -10 5 C ATOM 6729 C TYR D 141 10.004 -6.775 -0.281 1.00 10.65 C ANISOU 6729 C TYR D 141 1399 1316 1331 31 -19 1 C ATOM 6730 O TYR D 141 9.956 -7.505 0.707 1.00 10.73 O ANISOU 6730 O TYR D 141 1390 1349 1337 20 31 10 O ATOM 6731 CB TYR D 141 7.486 -6.645 -0.427 1.00 10.50 C ANISOU 6731 CB TYR D 141 1373 1285 1332 -10 -17 16 C ATOM 6732 CG TYR D 141 7.273 -5.355 0.337 1.00 10.45 C ANISOU 6732 CG TYR D 141 1334 1317 1318 20 -14 5 C ATOM 6733 CD1 TYR D 141 6.675 -4.257 -0.265 1.00 10.00 C ANISOU 6733 CD1 TYR D 141 1267 1284 1250 -34 -43 9 C ATOM 6734 CD2 TYR D 141 7.703 -5.245 1.651 1.00 10.52 C ANISOU 6734 CD2 TYR D 141 1353 1340 1304 -11 5 -8 C ATOM 6735 CE1 TYR D 141 6.484 -3.079 0.432 1.00 10.56 C ANISOU 6735 CE1 TYR D 141 1349 1341 1323 6 -18 -12 C ATOM 6736 CE2 TYR D 141 7.524 -4.070 2.357 1.00 10.78 C ANISOU 6736 CE2 TYR D 141 1401 1322 1374 3 -3 -5 C ATOM 6737 CZ TYR D 141 6.919 -2.994 1.742 1.00 10.87 C ANISOU 6737 CZ TYR D 141 1419 1386 1325 15 -38 15 C ATOM 6738 OH TYR D 141 6.742 -1.830 2.441 1.00 11.28 O ANISOU 6738 OH TYR D 141 1511 1496 1279 25 -52 -35 O ATOM 6739 N GLY D 142 11.085 -6.090 -0.629 1.00 11.24 N ANISOU 6739 N GLY D 142 1440 1450 1382 -9 -18 9 N ATOM 6740 CA GLY D 142 12.277 -6.031 0.207 1.00 11.27 C ANISOU 6740 CA GLY D 142 1424 1441 1417 -9 -16 16 C ATOM 6741 C GLY D 142 12.901 -7.404 0.383 1.00 11.74 C ANISOU 6741 C GLY D 142 1557 1466 1436 23 -24 4 C ATOM 6742 O GLY D 142 12.889 -8.264 -0.502 1.00 11.87 O ANISOU 6742 O GLY D 142 1680 1434 1395 25 -54 37 O ATOM 6743 N ASN D 143 13.402 -7.654 1.595 1.00 11.70 N ANISOU 6743 N ASN D 143 1585 1477 1382 25 11 -10 N ATOM 6744 CA ASN D 143 14.024 -8.934 1.911 1.00 12.10 C ANISOU 6744 CA ASN D 143 1585 1507 1506 20 -40 -13 C ATOM 6745 C ASN D 143 12.993 -10.017 2.168 1.00 12.42 C ANISOU 6745 C ASN D 143 1603 1581 1535 -6 -11 -6 C ATOM 6746 O ASN D 143 13.323 -11.186 2.372 1.00 12.96 O ANISOU 6746 O ASN D 143 1721 1602 1600 -18 -30 23 O ATOM 6747 CB ASN D 143 14.984 -8.791 3.092 1.00 12.18 C ANISOU 6747 CB ASN D 143 1600 1575 1454 4 -13 6 C ATOM 6748 CG ASN D 143 14.316 -8.516 4.420 1.00 11.38 C ANISOU 6748 CG ASN D 143 1362 1495 1465 7 -38 -6 C ATOM 6749 OD1 ASN D 143 13.098 -8.404 4.531 1.00 9.49 O ANISOU 6749 OD1 ASN D 143 1303 1172 1129 40 -50 22 O ATOM 6750 ND2 ASN D 143 15.143 -8.410 5.461 1.00 10.73 N ANISOU 6750 ND2 ASN D 143 1477 1367 1232 23 23 -37 N ATOM 6751 N GLN D 144 11.709 -9.676 2.227 1.00 12.61 N ANISOU 6751 N GLN D 144 1623 1581 1589 6 10 -4 N ATOM 6752 CA GLN D 144 10.612 -10.624 2.311 1.00 13.22 C ANISOU 6752 CA GLN D 144 1658 1687 1679 -23 -21 30 C ATOM 6753 C GLN D 144 10.648 -11.407 3.619 1.00 13.47 C ANISOU 6753 C GLN D 144 1747 1693 1679 -18 -32 14 C ATOM 6754 O GLN D 144 10.092 -12.499 3.717 1.00 14.57 O ANISOU 6754 O GLN D 144 1930 1763 1841 -86 -26 34 O ATOM 6755 CB GLN D 144 10.611 -11.568 1.104 1.00 14.54 C ANISOU 6755 CB GLN D 144 1946 1718 1862 5 1 -49 C ATOM 6756 CG GLN D 144 10.347 -10.886 -0.234 1.00 16.32 C ANISOU 6756 CG GLN D 144 2117 2064 2022 5 -57 96 C ATOM 6757 CD GLN D 144 10.475 -11.844 -1.404 1.00 18.80 C ANISOU 6757 CD GLN D 144 2437 2406 2301 18 -2 -95 C ATOM 6758 OE1 GLN D 144 10.195 -13.036 -1.271 1.00 20.81 O ANISOU 6758 OE1 GLN D 144 2742 2511 2654 -7 -78 -27 O ATOM 6759 NE2 GLN D 144 10.901 -11.344 -2.556 1.00 19.05 N ANISOU 6759 NE2 GLN D 144 2502 2362 2375 23 -26 -14 N ATOM 6760 N ASN D 145 11.267 -10.834 4.644 1.00 12.75 N ANISOU 6760 N ASN D 145 1648 1595 1600 -3 -7 57 N ATOM 6761 CA ASN D 145 11.458 -11.526 5.912 1.00 12.41 C ANISOU 6761 CA ASN D 145 1579 1567 1571 -10 -18 24 C ATOM 6762 C ASN D 145 10.404 -11.028 6.892 1.00 12.63 C ANISOU 6762 C ASN D 145 1601 1592 1605 -1 -13 7 C ATOM 6763 O ASN D 145 10.460 -9.876 7.330 1.00 12.98 O ANISOU 6763 O ASN D 145 1683 1600 1649 14 -7 -11 O ATOM 6764 CB ASN D 145 12.874 -11.281 6.428 1.00 12.15 C ANISOU 6764 CB ASN D 145 1598 1591 1429 -19 -19 0 C ATOM 6765 CG ASN D 145 13.219 -12.177 7.601 1.00 11.95 C ANISOU 6765 CG ASN D 145 1593 1452 1494 15 -36 -17 C ATOM 6766 OD1 ASN D 145 12.330 -12.576 8.351 1.00 13.14 O ANISOU 6766 OD1 ASN D 145 1735 1595 1663 27 56 61 O ATOM 6767 ND2 ASN D 145 14.497 -12.487 7.748 1.00 13.11 N ANISOU 6767 ND2 ASN D 145 1633 1682 1665 12 -11 -74 N ATOM 6768 N ILE D 146 9.436 -11.890 7.205 1.00 12.57 N ANISOU 6768 N ILE D 146 1613 1580 1583 16 -23 70 N ATOM 6769 CA ILE D 146 8.345 -11.471 8.079 1.00 12.93 C ANISOU 6769 CA ILE D 146 1650 1626 1636 -4 9 24 C ATOM 6770 C ILE D 146 8.507 -12.021 9.492 1.00 13.40 C ANISOU 6770 C ILE D 146 1755 1683 1655 -12 -1 22 C ATOM 6771 O ILE D 146 7.548 -11.990 10.266 1.00 13.45 O ANISOU 6771 O ILE D 146 1756 1682 1670 6 -12 74 O ATOM 6772 CB ILE D 146 6.962 -11.837 7.514 1.00 13.26 C ANISOU 6772 CB ILE D 146 1694 1680 1664 -2 -44 15 C ATOM 6773 CG1 ILE D 146 6.755 -13.351 7.446 1.00 13.52 C ANISOU 6773 CG1 ILE D 146 1720 1678 1741 8 -50 23 C ATOM 6774 CG2 ILE D 146 6.786 -11.222 6.129 1.00 13.48 C ANISOU 6774 CG2 ILE D 146 1717 1728 1676 37 -8 27 C ATOM 6775 CD1 ILE D 146 5.323 -13.749 7.129 1.00 13.88 C ANISOU 6775 CD1 ILE D 146 1738 1628 1908 -16 5 -7 C ATOM 6776 N SER D 147 9.709 -12.452 9.853 1.00 14.48 N ANISOU 6776 N SER D 147 1843 1798 1861 37 -22 1 N ATOM 6777 CA SER D 147 10.014 -12.812 11.229 1.00 15.71 C ANISOU 6777 CA SER D 147 2069 1982 1917 -7 -19 37 C ATOM 6778 C SER D 147 9.896 -11.615 12.171 1.00 15.93 C ANISOU 6778 C SER D 147 2042 1987 2026 15 -12 5 C ATOM 6779 O SER D 147 10.092 -10.461 11.786 1.00 16.02 O ANISOU 6779 O SER D 147 2021 1999 2066 -2 -58 13 O ATOM 6780 CB SER D 147 11.433 -13.380 11.353 1.00 18.48 C ANISOU 6780 CB SER D 147 2194 2451 2378 58 -33 59 C ATOM 6781 OG SER D 147 11.593 -14.578 10.626 1.00 21.82 O ANISOU 6781 OG SER D 147 2843 2681 2768 28 26 -69 O ATOM 6782 N GLY D 148 9.589 -11.911 13.428 1.00 16.31 N ANISOU 6782 N GLY D 148 2101 2055 2042 35 -26 5 N ATOM 6783 CA GLY D 148 9.558 -10.900 14.476 1.00 16.37 C ANISOU 6783 CA GLY D 148 2107 2079 2035 27 -21 1 C ATOM 6784 C GLY D 148 8.174 -10.760 15.088 1.00 16.25 C ANISOU 6784 C GLY D 148 2108 2047 2019 -17 -5 23 C ATOM 6785 O GLY D 148 7.974 -9.949 15.993 1.00 16.51 O ANISOU 6785 O GLY D 148 2168 2097 2008 -4 -22 13 O ATOM 6786 N GLY D 149 7.220 -11.546 14.602 1.00 16.26 N ANISOU 6786 N GLY D 149 2078 2108 1993 -6 -17 19 N ATOM 6787 CA GLY D 149 5.852 -11.497 15.112 1.00 15.94 C ANISOU 6787 CA GLY D 149 2063 2045 1948 14 -15 16 C ATOM 6788 C GLY D 149 4.912 -11.010 14.015 1.00 15.63 C ANISOU 6788 C GLY D 149 2007 1965 1965 14 -1 19 C ATOM 6789 O GLY D 149 5.162 -9.980 13.388 1.00 15.30 O ANISOU 6789 O GLY D 149 1916 1978 1918 8 -11 42 O ATOM 6790 N ILE D 150 3.825 -11.737 13.786 1.00 16.03 N ANISOU 6790 N ILE D 150 2022 2061 2007 -15 18 41 N ATOM 6791 CA ILE D 150 2.933 -11.476 12.663 1.00 16.60 C ANISOU 6791 CA ILE D 150 2128 2138 2041 32 -19 23 C ATOM 6792 C ILE D 150 2.315 -10.088 12.682 1.00 16.64 C ANISOU 6792 C ILE D 150 2113 2123 2085 2 -4 11 C ATOM 6793 O ILE D 150 2.006 -9.539 11.617 1.00 16.71 O ANISOU 6793 O ILE D 150 2120 2125 2103 -13 18 57 O ATOM 6794 CB ILE D 150 1.828 -12.547 12.567 1.00 18.45 C ANISOU 6794 CB ILE D 150 2315 2295 2399 -57 -15 -2 C ATOM 6795 CG1 ILE D 150 1.012 -12.390 11.277 1.00 19.16 C ANISOU 6795 CG1 ILE D 150 2443 2401 2435 7 -32 -7 C ATOM 6796 CG2 ILE D 150 0.912 -12.502 13.783 1.00 19.57 C ANISOU 6796 CG2 ILE D 150 2474 2480 2482 -8 44 24 C ATOM 6797 CD1 ILE D 150 1.829 -12.540 10.014 1.00 19.59 C ANISOU 6797 CD1 ILE D 150 2539 2450 2455 -31 8 43 C ATOM 6798 N ASP D 151 2.118 -9.500 13.857 1.00 16.49 N ANISOU 6798 N ASP D 151 2107 2068 2092 -15 -19 9 N ATOM 6799 CA ASP D 151 1.559 -8.163 13.962 1.00 17.03 C ANISOU 6799 CA ASP D 151 2193 2074 2201 -11 -78 11 C ATOM 6800 C ASP D 151 2.596 -7.089 14.255 1.00 15.86 C ANISOU 6800 C ASP D 151 2030 1992 2005 46 0 18 C ATOM 6801 O ASP D 151 2.184 -5.988 14.645 1.00 15.91 O ANISOU 6801 O ASP D 151 2067 1956 2021 19 11 44 O ATOM 6802 CB ASP D 151 0.454 -8.142 15.023 1.00 20.72 C ANISOU 6802 CB ASP D 151 2499 2674 2698 14 168 -19 C ATOM 6803 CG ASP D 151 0.940 -8.477 16.416 1.00 24.18 C ANISOU 6803 CG ASP D 151 3125 3052 3010 17 -121 35 C ATOM 6804 OD1 ASP D 151 2.157 -8.671 16.616 1.00 23.32 O ANISOU 6804 OD1 ASP D 151 3065 2934 2861 47 28 32 O ATOM 6805 OD2 ASP D 151 0.102 -8.540 17.342 1.00 27.17 O ANISOU 6805 OD2 ASP D 151 3406 3483 3434 -13 115 18 O ATOM 6806 N LYS D 152 3.882 -7.331 14.005 1.00 14.80 N ANISOU 6806 N LYS D 152 1950 1824 1849 0 -14 37 N ATOM 6807 CA LYS D 152 4.858 -6.260 14.168 1.00 14.71 C ANISOU 6807 CA LYS D 152 1836 1864 1888 26 40 18 C ATOM 6808 C LYS D 152 6.120 -6.409 13.342 1.00 13.44 C ANISOU 6808 C LYS D 152 1742 1679 1686 18 -37 -8 C ATOM 6809 O LYS D 152 7.044 -5.611 13.532 1.00 13.46 O ANISOU 6809 O LYS D 152 1740 1679 1695 8 3 39 O ATOM 6810 CB LYS D 152 5.213 -6.105 15.651 1.00 17.47 C ANISOU 6810 CB LYS D 152 2268 2327 2045 -34 -33 -54 C ATOM 6811 CG LYS D 152 5.831 -7.338 16.288 1.00 20.61 C ANISOU 6811 CG LYS D 152 2611 2517 2703 74 4 85 C ATOM 6812 CD LYS D 152 6.129 -7.040 17.753 1.00 24.19 C ANISOU 6812 CD LYS D 152 3138 3111 2941 -40 -25 -67 C ATOM 6813 CE LYS D 152 6.808 -8.211 18.443 1.00 26.92 C ANISOU 6813 CE LYS D 152 3439 3341 3450 61 -23 70 C ATOM 6814 NZ LYS D 152 7.121 -7.870 19.862 1.00 28.11 N ANISOU 6814 NZ LYS D 152 3585 3557 3537 -13 -14 7 N ATOM 6815 N PHE D 153 6.175 -7.321 12.374 1.00 12.35 N ANISOU 6815 N PHE D 153 1551 1590 1550 29 8 56 N ATOM 6816 CA PHE D 153 7.425 -7.596 11.672 1.00 11.47 C ANISOU 6816 CA PHE D 153 1536 1422 1401 -20 9 22 C ATOM 6817 C PHE D 153 7.922 -6.420 10.842 1.00 10.89 C ANISOU 6817 C PHE D 153 1414 1380 1342 12 -22 18 C ATOM 6818 O PHE D 153 9.126 -6.256 10.633 1.00 10.95 O ANISOU 6818 O PHE D 153 1421 1436 1304 54 22 76 O ATOM 6819 CB PHE D 153 7.296 -8.840 10.793 1.00 10.86 C ANISOU 6819 CB PHE D 153 1410 1319 1397 -5 18 64 C ATOM 6820 CG PHE D 153 6.231 -8.777 9.739 1.00 11.90 C ANISOU 6820 CG PHE D 153 1491 1565 1466 -7 -16 31 C ATOM 6821 CD1 PHE D 153 6.460 -8.122 8.537 1.00 11.59 C ANISOU 6821 CD1 PHE D 153 1475 1503 1426 9 -57 21 C ATOM 6822 CD2 PHE D 153 5.004 -9.382 9.948 1.00 12.00 C ANISOU 6822 CD2 PHE D 153 1496 1537 1526 -18 -28 -1 C ATOM 6823 CE1 PHE D 153 5.472 -8.069 7.571 1.00 10.96 C ANISOU 6823 CE1 PHE D 153 1377 1425 1361 46 9 13 C ATOM 6824 CE2 PHE D 153 4.014 -9.333 8.983 1.00 11.66 C ANISOU 6824 CE2 PHE D 153 1518 1484 1429 16 -1 26 C ATOM 6825 CZ PHE D 153 4.256 -8.674 7.794 1.00 10.98 C ANISOU 6825 CZ PHE D 153 1432 1308 1434 19 -3 7 C ATOM 6826 N TRP D 154 7.015 -5.574 10.367 1.00 10.53 N ANISOU 6826 N TRP D 154 1417 1288 1296 -15 -6 17 N ATOM 6827 CA TRP D 154 7.362 -4.408 9.570 1.00 10.37 C ANISOU 6827 CA TRP D 154 1363 1295 1281 -10 -27 34 C ATOM 6828 C TRP D 154 7.881 -3.239 10.397 1.00 10.63 C ANISOU 6828 C TRP D 154 1401 1317 1320 -46 -14 18 C ATOM 6829 O TRP D 154 8.372 -2.252 9.841 1.00 10.36 O ANISOU 6829 O TRP D 154 1469 1276 1191 -23 -45 25 O ATOM 6830 CB TRP D 154 6.101 -3.949 8.812 1.00 10.24 C ANISOU 6830 CB TRP D 154 1329 1306 1256 13 -4 29 C ATOM 6831 CG TRP D 154 4.966 -3.669 9.757 1.00 10.52 C ANISOU 6831 CG TRP D 154 1323 1330 1346 61 5 33 C ATOM 6832 CD1 TRP D 154 4.758 -2.522 10.468 1.00 11.15 C ANISOU 6832 CD1 TRP D 154 1423 1429 1386 16 -17 -49 C ATOM 6833 CD2 TRP D 154 3.901 -4.560 10.109 1.00 10.99 C ANISOU 6833 CD2 TRP D 154 1369 1434 1373 20 4 46 C ATOM 6834 NE1 TRP D 154 3.632 -2.646 11.237 1.00 12.07 N ANISOU 6834 NE1 TRP D 154 1417 1538 1631 1 17 -17 N ATOM 6835 CE2 TRP D 154 3.078 -3.880 11.030 1.00 11.18 C ANISOU 6835 CE2 TRP D 154 1424 1438 1387 68 -19 27 C ATOM 6836 CE3 TRP D 154 3.556 -5.856 9.724 1.00 12.68 C ANISOU 6836 CE3 TRP D 154 1649 1534 1634 -57 -11 14 C ATOM 6837 CZ2 TRP D 154 1.935 -4.460 11.575 1.00 12.22 C ANISOU 6837 CZ2 TRP D 154 1496 1572 1574 9 7 3 C ATOM 6838 CZ3 TRP D 154 2.420 -6.433 10.266 1.00 12.63 C ANISOU 6838 CZ3 TRP D 154 1553 1612 1631 53 30 27 C ATOM 6839 CH2 TRP D 154 1.620 -5.725 11.177 1.00 12.59 C ANISOU 6839 CH2 TRP D 154 1654 1582 1547 -2 25 -3 C ATOM 6840 N LEU D 155 7.749 -3.308 11.716 1.00 11.08 N ANISOU 6840 N LEU D 155 1496 1370 1344 -40 9 25 N ATOM 6841 CA LEU D 155 8.041 -2.197 12.606 1.00 11.38 C ANISOU 6841 CA LEU D 155 1508 1427 1388 -15 16 -18 C ATOM 6842 C LEU D 155 9.149 -2.531 13.598 1.00 12.11 C ANISOU 6842 C LEU D 155 1573 1564 1465 -4 -18 -12 C ATOM 6843 O LEU D 155 10.022 -1.713 13.894 1.00 12.59 O ANISOU 6843 O LEU D 155 1665 1624 1494 -41 -44 5 O ATOM 6844 CB LEU D 155 6.767 -1.821 13.372 1.00 11.37 C ANISOU 6844 CB LEU D 155 1442 1429 1450 -17 -20 -17 C ATOM 6845 CG LEU D 155 6.849 -0.627 14.325 1.00 11.58 C ANISOU 6845 CG LEU D 155 1514 1451 1434 -11 24 -33 C ATOM 6846 CD1 LEU D 155 7.256 0.640 13.589 1.00 12.22 C ANISOU 6846 CD1 LEU D 155 1633 1539 1473 -15 22 23 C ATOM 6847 CD2 LEU D 155 5.517 -0.432 15.038 1.00 12.37 C ANISOU 6847 CD2 LEU D 155 1541 1615 1544 45 21 -10 C ATOM 6848 N GLU D 156 9.079 -3.734 14.157 1.00 12.63 N ANISOU 6848 N GLU D 156 1673 1602 1523 30 1 9 N ATOM 6849 CA GLU D 156 10.050 -4.193 15.140 1.00 13.53 C ANISOU 6849 CA GLU D 156 1739 1759 1645 36 -51 22 C ATOM 6850 C GLU D 156 10.770 -5.466 14.719 1.00 14.35 C ANISOU 6850 C GLU D 156 1879 1807 1767 44 -27 -39 C ATOM 6851 O GLU D 156 11.627 -5.960 15.462 1.00 15.81 O ANISOU 6851 O GLU D 156 2063 2040 1906 122 -110 -24 O ATOM 6852 CB GLU D 156 9.335 -4.462 16.472 1.00 14.38 C ANISOU 6852 CB GLU D 156 1882 1858 1725 17 11 50 C ATOM 6853 CG GLU D 156 8.731 -3.219 17.106 1.00 15.73 C ANISOU 6853 CG GLU D 156 2003 1938 2034 50 -13 -28 C ATOM 6854 CD GLU D 156 8.157 -3.524 18.477 1.00 17.15 C ANISOU 6854 CD GLU D 156 2170 2184 2160 -22 78 -1 C ATOM 6855 OE1 GLU D 156 8.960 -3.661 19.424 1.00 19.33 O ANISOU 6855 OE1 GLU D 156 2439 2558 2349 26 -58 43 O ATOM 6856 OE2 GLU D 156 6.922 -3.630 18.579 1.00 16.29 O ANISOU 6856 OE2 GLU D 156 2125 2091 1974 20 -30 -2 O ATOM 6857 N GLY D 157 10.419 -6.022 13.571 1.00 13.32 N ANISOU 6857 N GLY D 157 1741 1653 1667 27 21 31 N ATOM 6858 CA GLY D 157 10.885 -7.336 13.161 1.00 12.59 C ANISOU 6858 CA GLY D 157 1607 1638 1537 11 11 29 C ATOM 6859 C GLY D 157 12.015 -7.276 12.144 1.00 11.62 C ANISOU 6859 C GLY D 157 1522 1492 1402 11 -57 40 C ATOM 6860 O GLY D 157 12.831 -6.357 12.139 1.00 11.27 O ANISOU 6860 O GLY D 157 1547 1455 1279 21 -80 80 O ATOM 6861 N GLN D 158 12.053 -8.268 11.258 1.00 11.75 N ANISOU 6861 N GLN D 158 1548 1529 1389 20 -58 41 N ATOM 6862 CA GLN D 158 13.178 -8.480 10.366 1.00 12.55 C ANISOU 6862 CA GLN D 158 1554 1724 1490 -32 -16 30 C ATOM 6863 C GLN D 158 12.939 -7.981 8.944 1.00 11.70 C ANISOU 6863 C GLN D 158 1455 1524 1469 11 -31 -2 C ATOM 6864 O GLN D 158 13.856 -8.106 8.124 1.00 11.80 O ANISOU 6864 O GLN D 158 1502 1488 1494 29 -15 -45 O ATOM 6865 CB GLN D 158 13.513 -9.973 10.261 1.00 17.42 C ANISOU 6865 CB GLN D 158 2187 1973 2460 85 7 -152 C ATOM 6866 CG GLN D 158 13.493 -10.746 11.554 1.00 24.50 C ANISOU 6866 CG GLN D 158 3384 3012 2914 26 128 155 C ATOM 6867 CD GLN D 158 14.792 -10.765 12.317 1.00 30.95 C ANISOU 6867 CD GLN D 158 3749 4109 3902 5 -97 -25 C ATOM 6868 OE1 GLN D 158 15.212 -11.828 12.787 1.00 33.37 O ANISOU 6868 OE1 GLN D 158 4245 4187 4247 50 -11 21 O ATOM 6869 NE2 GLN D 158 15.424 -9.610 12.455 1.00 33.18 N ANISOU 6869 NE2 GLN D 158 4261 4123 4222 -16 -12 22 N ATOM 6870 N LEU D 159 11.764 -7.430 8.661 1.00 11.00 N ANISOU 6870 N LEU D 159 1438 1399 1342 2 -47 -7 N ATOM 6871 CA LEU D 159 11.498 -6.938 7.305 1.00 10.45 C ANISOU 6871 CA LEU D 159 1326 1321 1323 14 -6 -1 C ATOM 6872 C LEU D 159 12.310 -5.695 6.985 1.00 10.63 C ANISOU 6872 C LEU D 159 1373 1332 1332 17 -15 11 C ATOM 6873 O LEU D 159 12.468 -4.783 7.804 1.00 10.90 O ANISOU 6873 O LEU D 159 1449 1298 1394 4 -82 20 O ATOM 6874 CB LEU D 159 10.001 -6.689 7.129 1.00 10.10 C ANISOU 6874 CB LEU D 159 1324 1316 1199 11 -83 13 C ATOM 6875 CG LEU D 159 9.514 -6.273 5.737 1.00 9.26 C ANISOU 6875 CG LEU D 159 1246 1144 1128 42 17 25 C ATOM 6876 CD1 LEU D 159 9.913 -7.302 4.689 1.00 9.52 C ANISOU 6876 CD1 LEU D 159 1312 1156 1149 38 0 8 C ATOM 6877 CD2 LEU D 159 8.001 -6.095 5.746 1.00 10.32 C ANISOU 6877 CD2 LEU D 159 1287 1305 1329 -3 -11 -7 C ATOM 6878 N ARG D 160 12.895 -5.663 5.790 1.00 10.37 N ANISOU 6878 N ARG D 160 1241 1354 1345 25 -16 34 N ATOM 6879 CA ARG D 160 13.693 -4.533 5.333 1.00 10.60 C ANISOU 6879 CA ARG D 160 1410 1333 1284 -2 3 24 C ATOM 6880 C ARG D 160 13.397 -4.264 3.852 1.00 10.45 C ANISOU 6880 C ARG D 160 1399 1301 1270 11 -15 5 C ATOM 6881 O ARG D 160 13.239 -5.218 3.089 1.00 10.72 O ANISOU 6881 O ARG D 160 1473 1344 1257 -30 -18 -6 O ATOM 6882 CB ARG D 160 15.191 -4.765 5.478 1.00 12.21 C ANISOU 6882 CB ARG D 160 1492 1671 1478 73 -26 37 C ATOM 6883 CG ARG D 160 15.753 -5.158 6.824 1.00 11.91 C ANISOU 6883 CG ARG D 160 1566 1540 1418 -4 -44 -18 C ATOM 6884 CD ARG D 160 15.773 -3.998 7.818 1.00 12.08 C ANISOU 6884 CD ARG D 160 1613 1496 1480 68 -18 -6 C ATOM 6885 NE ARG D 160 16.349 -4.481 9.081 1.00 11.70 N ANISOU 6885 NE ARG D 160 1444 1584 1417 -10 20 -9 N ATOM 6886 CZ ARG D 160 15.652 -5.002 10.083 1.00 10.68 C ANISOU 6886 CZ ARG D 160 1370 1313 1374 -22 -39 -18 C ATOM 6887 NH1 ARG D 160 14.331 -5.084 10.030 1.00 9.96 N ANISOU 6887 NH1 ARG D 160 1339 1269 1175 22 0 15 N ATOM 6888 NH2 ARG D 160 16.286 -5.429 11.171 1.00 11.19 N ANISOU 6888 NH2 ARG D 160 1476 1365 1411 -6 -95 -51 N ATOM 6889 N ILE D 161 13.350 -2.999 3.473 1.00 10.02 N ANISOU 6889 N ILE D 161 1345 1275 1188 -20 3 -15 N ATOM 6890 CA ILE D 161 13.124 -2.630 2.074 1.00 9.65 C ANISOU 6890 CA ILE D 161 1245 1214 1208 7 -7 25 C ATOM 6891 C ILE D 161 13.884 -1.353 1.744 1.00 9.29 C ANISOU 6891 C ILE D 161 1196 1187 1148 19 -7 -5 C ATOM 6892 O ILE D 161 14.018 -0.483 2.605 1.00 8.83 O ANISOU 6892 O ILE D 161 1188 1122 1045 -3 -24 60 O ATOM 6893 CB ILE D 161 11.629 -2.480 1.748 1.00 9.62 C ANISOU 6893 CB ILE D 161 1225 1229 1201 38 26 -50 C ATOM 6894 CG1 ILE D 161 11.417 -2.335 0.238 1.00 10.26 C ANISOU 6894 CG1 ILE D 161 1298 1354 1248 -21 -3 36 C ATOM 6895 CG2 ILE D 161 11.008 -1.303 2.492 1.00 8.41 C ANISOU 6895 CG2 ILE D 161 1081 1099 1014 24 -101 14 C ATOM 6896 CD1 ILE D 161 9.980 -2.428 -0.225 1.00 10.66 C ANISOU 6896 CD1 ILE D 161 1286 1387 1376 -4 21 20 C ATOM 6897 N SER D 162 14.390 -1.232 0.518 1.00 9.45 N ANISOU 6897 N SER D 162 1234 1213 1145 4 -13 39 N ATOM 6898 CA SER D 162 15.140 -0.050 0.117 1.00 9.33 C ANISOU 6898 CA SER D 162 1183 1167 1195 8 -18 -12 C ATOM 6899 C SER D 162 14.254 0.997 -0.554 1.00 9.40 C ANISOU 6899 C SER D 162 1219 1184 1170 -9 -25 22 C ATOM 6900 O SER D 162 13.134 0.714 -0.984 1.00 9.30 O ANISOU 6900 O SER D 162 1202 1138 1194 30 -31 27 O ATOM 6901 CB SER D 162 16.262 -0.415 -0.861 1.00 9.84 C ANISOU 6901 CB SER D 162 1363 1217 1158 -13 51 -4 C ATOM 6902 OG SER D 162 15.718 -0.819 -2.108 1.00 10.08 O ANISOU 6902 OG SER D 162 1271 1359 1200 -30 -25 32 O ATOM 6903 N ALA D 163 14.805 2.202 -0.695 1.00 9.64 N ANISOU 6903 N ALA D 163 1240 1177 1245 10 -21 25 N ATOM 6904 CA ALA D 163 14.127 3.261 -1.444 1.00 9.57 C ANISOU 6904 CA ALA D 163 1239 1218 1180 9 -34 28 C ATOM 6905 C ALA D 163 13.906 2.850 -2.898 1.00 9.88 C ANISOU 6905 C ALA D 163 1262 1293 1198 30 -20 -3 C ATOM 6906 O ALA D 163 12.810 3.054 -3.427 1.00 9.46 O ANISOU 6906 O ALA D 163 1282 1235 1076 -10 -49 41 O ATOM 6907 CB ALA D 163 14.912 4.561 -1.374 1.00 10.04 C ANISOU 6907 CB ALA D 163 1292 1259 1262 -24 20 -41 C ATOM 6908 N VAL D 164 14.921 2.258 -3.524 1.00 9.80 N ANISOU 6908 N VAL D 164 1294 1245 1185 30 -11 9 N ATOM 6909 CA VAL D 164 14.755 1.721 -4.876 1.00 9.89 C ANISOU 6909 CA VAL D 164 1317 1248 1195 -10 -15 5 C ATOM 6910 C VAL D 164 13.644 0.688 -4.954 1.00 9.68 C ANISOU 6910 C VAL D 164 1305 1219 1156 -1 -20 -9 C ATOM 6911 O VAL D 164 12.789 0.766 -5.844 1.00 9.68 O ANISOU 6911 O VAL D 164 1242 1224 1213 -7 -26 -6 O ATOM 6912 CB VAL D 164 16.077 1.155 -5.422 1.00 11.63 C ANISOU 6912 CB VAL D 164 1348 1579 1493 20 21 -11 C ATOM 6913 CG1 VAL D 164 15.877 0.388 -6.723 1.00 13.11 C ANISOU 6913 CG1 VAL D 164 1712 1681 1587 23 22 -56 C ATOM 6914 CG2 VAL D 164 17.064 2.298 -5.636 1.00 12.61 C ANISOU 6914 CG2 VAL D 164 1605 1585 1602 -44 16 21 C ATOM 6915 N ASN D 165 13.585 -0.263 -4.027 1.00 9.77 N ANISOU 6915 N ASN D 165 1295 1218 1199 -20 -25 -8 N ATOM 6916 CA ASN D 165 12.528 -1.271 -4.027 1.00 9.41 C ANISOU 6916 CA ASN D 165 1256 1167 1154 6 6 -17 C ATOM 6917 C ASN D 165 11.159 -0.651 -3.791 1.00 9.35 C ANISOU 6917 C ASN D 165 1227 1171 1154 -7 -2 -2 C ATOM 6918 O ASN D 165 10.174 -1.056 -4.413 1.00 9.54 O ANISOU 6918 O ASN D 165 1246 1167 1212 -22 -2 -31 O ATOM 6919 CB ASN D 165 12.838 -2.334 -2.978 1.00 10.42 C ANISOU 6919 CB ASN D 165 1409 1262 1290 -6 -79 53 C ATOM 6920 CG ASN D 165 12.126 -3.653 -3.163 1.00 10.49 C ANISOU 6920 CG ASN D 165 1426 1197 1361 38 -3 37 C ATOM 6921 OD1 ASN D 165 11.084 -3.779 -3.808 1.00 12.30 O ANISOU 6921 OD1 ASN D 165 1581 1485 1606 -29 -101 -17 O ATOM 6922 ND2 ASN D 165 12.706 -4.687 -2.559 1.00 9.30 N ANISOU 6922 ND2 ASN D 165 1324 1093 1117 -41 -36 -32 N ATOM 6923 N GLN D 166 11.069 0.369 -2.931 1.00 9.25 N ANISOU 6923 N GLN D 166 1207 1190 1119 21 -20 -10 N ATOM 6924 CA GLN D 166 9.808 1.095 -2.767 1.00 9.37 C ANISOU 6924 CA GLN D 166 1227 1186 1145 31 -7 -3 C ATOM 6925 C GLN D 166 9.338 1.687 -4.093 1.00 9.31 C ANISOU 6925 C GLN D 166 1239 1151 1147 -4 -29 -11 C ATOM 6926 O GLN D 166 8.168 1.524 -4.443 1.00 9.41 O ANISOU 6926 O GLN D 166 1236 1205 1134 26 -18 87 O ATOM 6927 CB GLN D 166 9.922 2.196 -1.715 1.00 9.27 C ANISOU 6927 CB GLN D 166 1205 1103 1212 -24 -6 2 C ATOM 6928 CG GLN D 166 10.181 1.708 -0.305 1.00 10.68 C ANISOU 6928 CG GLN D 166 1357 1411 1291 16 -43 51 C ATOM 6929 CD GLN D 166 8.976 1.595 0.595 1.00 11.15 C ANISOU 6929 CD GLN D 166 1300 1462 1477 -23 -49 4 C ATOM 6930 OE1 GLN D 166 9.111 1.626 1.828 1.00 12.91 O ANISOU 6930 OE1 GLN D 166 1616 1771 1518 44 35 13 O ATOM 6931 NE2 GLN D 166 7.782 1.459 0.034 1.00 8.08 N ANISOU 6931 NE2 GLN D 166 1156 1004 912 -10 61 103 N ATOM 6932 N VAL D 167 10.237 2.334 -4.836 1.00 9.62 N ANISOU 6932 N VAL D 167 1261 1204 1189 -19 -3 -48 N ATOM 6933 CA VAL D 167 9.863 2.889 -6.136 1.00 10.63 C ANISOU 6933 CA VAL D 167 1403 1340 1294 22 -32 20 C ATOM 6934 C VAL D 167 9.403 1.789 -7.085 1.00 11.21 C ANISOU 6934 C VAL D 167 1471 1411 1378 -10 -17 -28 C ATOM 6935 O VAL D 167 8.391 1.972 -7.774 1.00 11.74 O ANISOU 6935 O VAL D 167 1510 1451 1500 7 -58 -27 O ATOM 6936 CB VAL D 167 10.992 3.724 -6.759 1.00 12.10 C ANISOU 6936 CB VAL D 167 1532 1461 1605 -71 -7 42 C ATOM 6937 CG1 VAL D 167 10.739 4.017 -8.232 1.00 14.56 C ANISOU 6937 CG1 VAL D 167 1915 1907 1709 -58 -11 40 C ATOM 6938 CG2 VAL D 167 11.142 5.033 -5.986 1.00 12.70 C ANISOU 6938 CG2 VAL D 167 1680 1562 1583 -7 -14 -22 C ATOM 6939 N GLU D 168 10.104 0.659 -7.121 1.00 11.51 N ANISOU 6939 N GLU D 168 1532 1431 1410 -4 -8 -3 N ATOM 6940 CA GLU D 168 9.707 -0.441 -8.000 1.00 11.64 C ANISOU 6940 CA GLU D 168 1513 1458 1452 -20 -29 -9 C ATOM 6941 C GLU D 168 8.327 -0.973 -7.658 1.00 11.22 C ANISOU 6941 C GLU D 168 1514 1382 1367 -19 -21 36 C ATOM 6942 O GLU D 168 7.482 -1.216 -8.527 1.00 11.32 O ANISOU 6942 O GLU D 168 1557 1403 1341 -56 -29 49 O ATOM 6943 CB GLU D 168 10.745 -1.566 -7.950 1.00 12.67 C ANISOU 6943 CB GLU D 168 1594 1581 1640 50 -37 -24 C ATOM 6944 CG GLU D 168 12.099 -1.161 -8.515 1.00 13.66 C ANISOU 6944 CG GLU D 168 1796 1810 1586 -89 73 -42 C ATOM 6945 CD GLU D 168 13.190 -2.167 -8.209 1.00 17.58 C ANISOU 6945 CD GLU D 168 2215 2180 2283 112 -59 27 C ATOM 6946 OE1 GLU D 168 13.034 -2.951 -7.251 1.00 18.19 O ANISOU 6946 OE1 GLU D 168 2322 2222 2367 15 15 28 O ATOM 6947 OE2 GLU D 168 14.215 -2.177 -8.925 1.00 19.87 O ANISOU 6947 OE2 GLU D 168 2431 2599 2520 59 80 10 O ATOM 6948 N PHE D 169 8.069 -1.172 -6.371 1.00 10.84 N ANISOU 6948 N PHE D 169 1450 1337 1330 -30 -5 -14 N ATOM 6949 CA PHE D 169 6.781 -1.634 -5.872 1.00 10.59 C ANISOU 6949 CA PHE D 169 1388 1388 1250 13 -31 -7 C ATOM 6950 C PHE D 169 5.666 -0.649 -6.185 1.00 10.51 C ANISOU 6950 C PHE D 169 1390 1340 1263 -1 -13 -3 C ATOM 6951 O PHE D 169 4.595 -1.037 -6.664 1.00 10.95 O ANISOU 6951 O PHE D 169 1425 1419 1318 -17 -33 -11 O ATOM 6952 CB PHE D 169 6.901 -1.876 -4.359 1.00 9.79 C ANISOU 6952 CB PHE D 169 1308 1206 1204 6 6 11 C ATOM 6953 CG PHE D 169 5.595 -2.144 -3.670 1.00 9.42 C ANISOU 6953 CG PHE D 169 1248 1161 1170 11 -40 36 C ATOM 6954 CD1 PHE D 169 4.973 -3.377 -3.807 1.00 9.74 C ANISOU 6954 CD1 PHE D 169 1276 1224 1201 -33 -78 32 C ATOM 6955 CD2 PHE D 169 4.986 -1.174 -2.888 1.00 9.84 C ANISOU 6955 CD2 PHE D 169 1266 1347 1125 22 -23 -22 C ATOM 6956 CE1 PHE D 169 3.771 -3.633 -3.177 1.00 10.90 C ANISOU 6956 CE1 PHE D 169 1358 1441 1341 40 17 -1 C ATOM 6957 CE2 PHE D 169 3.781 -1.428 -2.258 1.00 10.21 C ANISOU 6957 CE2 PHE D 169 1326 1346 1207 -46 -21 52 C ATOM 6958 CZ PHE D 169 3.173 -2.660 -2.403 1.00 10.09 C ANISOU 6958 CZ PHE D 169 1321 1294 1217 12 -72 36 C ATOM 6959 N LEU D 170 5.908 0.642 -5.973 1.00 10.22 N ANISOU 6959 N LEU D 170 1365 1340 1180 -6 -64 -28 N ATOM 6960 CA LEU D 170 4.913 1.670 -6.244 1.00 10.71 C ANISOU 6960 CA LEU D 170 1439 1319 1313 25 -9 -39 C ATOM 6961 C LEU D 170 4.634 1.813 -7.735 1.00 11.19 C ANISOU 6961 C LEU D 170 1465 1426 1362 -5 -17 13 C ATOM 6962 O LEU D 170 3.490 2.031 -8.135 1.00 11.79 O ANISOU 6962 O LEU D 170 1480 1513 1487 6 -7 7 O ATOM 6963 CB LEU D 170 5.371 3.021 -5.680 1.00 10.88 C ANISOU 6963 CB LEU D 170 1396 1347 1392 -46 -57 -2 C ATOM 6964 CG LEU D 170 5.397 3.085 -4.148 1.00 12.30 C ANISOU 6964 CG LEU D 170 1583 1646 1445 6 -15 13 C ATOM 6965 CD1 LEU D 170 6.129 4.344 -3.708 1.00 14.12 C ANISOU 6965 CD1 LEU D 170 1864 1740 1762 -68 -33 -29 C ATOM 6966 CD2 LEU D 170 3.997 3.039 -3.563 1.00 13.04 C ANISOU 6966 CD2 LEU D 170 1610 1724 1622 -31 -8 6 C ATOM 6967 N GLU D 171 5.687 1.691 -8.546 1.00 11.25 N ANISOU 6967 N GLU D 171 1497 1405 1374 2 7 -8 N ATOM 6968 CA GLU D 171 5.498 1.687 -9.996 1.00 11.83 C ANISOU 6968 CA GLU D 171 1574 1500 1420 -20 -30 1 C ATOM 6969 C GLU D 171 4.595 0.535 -10.414 1.00 12.03 C ANISOU 6969 C GLU D 171 1565 1488 1517 -14 -29 11 C ATOM 6970 O GLU D 171 3.651 0.730 -11.189 1.00 12.26 O ANISOU 6970 O GLU D 171 1658 1547 1454 -31 -67 -3 O ATOM 6971 CB GLU D 171 6.839 1.622 -10.714 1.00 12.85 C ANISOU 6971 CB GLU D 171 1585 1670 1628 21 -4 20 C ATOM 6972 CG GLU D 171 6.730 1.432 -12.225 1.00 14.60 C ANISOU 6972 CG GLU D 171 1948 1870 1728 -28 -38 -26 C ATOM 6973 CD GLU D 171 8.105 1.306 -12.853 1.00 16.56 C ANISOU 6973 CD GLU D 171 2050 2126 2116 -11 39 -57 C ATOM 6974 OE1 GLU D 171 8.906 0.482 -12.366 1.00 17.97 O ANISOU 6974 OE1 GLU D 171 2271 2265 2293 57 -16 9 O ATOM 6975 OE2 GLU D 171 8.380 2.036 -13.821 1.00 18.05 O ANISOU 6975 OE2 GLU D 171 2328 2311 2218 -44 -3 22 O ATOM 6976 N SER D 172 4.843 -0.662 -9.881 1.00 11.86 N ANISOU 6976 N SER D 172 1553 1488 1464 -14 -21 5 N ATOM 6977 CA SER D 172 3.963 -1.796 -10.166 1.00 12.03 C ANISOU 6977 CA SER D 172 1584 1479 1509 -13 -4 -24 C ATOM 6978 C SER D 172 2.523 -1.507 -9.772 1.00 12.08 C ANISOU 6978 C SER D 172 1580 1491 1519 -16 -4 10 C ATOM 6979 O SER D 172 1.601 -1.803 -10.533 1.00 12.82 O ANISOU 6979 O SER D 172 1680 1565 1626 -43 -77 7 O ATOM 6980 CB SER D 172 4.464 -3.056 -9.460 1.00 12.67 C ANISOU 6980 CB SER D 172 1672 1562 1579 7 -49 19 C ATOM 6981 OG SER D 172 5.717 -3.453 -9.974 1.00 13.79 O ANISOU 6981 OG SER D 172 1764 1765 1710 19 23 17 O ATOM 6982 N LEU D 173 2.310 -0.912 -8.603 1.00 11.88 N ANISOU 6982 N LEU D 173 1531 1503 1478 -10 -6 23 N ATOM 6983 CA LEU D 173 0.986 -0.525 -8.144 1.00 11.82 C ANISOU 6983 CA LEU D 173 1541 1494 1454 18 -14 0 C ATOM 6984 C LEU D 173 0.341 0.489 -9.082 1.00 11.91 C ANISOU 6984 C LEU D 173 1504 1527 1495 24 -22 8 C ATOM 6985 O LEU D 173 -0.828 0.362 -9.443 1.00 11.75 O ANISOU 6985 O LEU D 173 1512 1526 1426 -13 -34 6 O ATOM 6986 CB LEU D 173 1.051 0.048 -6.725 1.00 11.53 C ANISOU 6986 CB LEU D 173 1473 1478 1430 0 -7 10 C ATOM 6987 CG LEU D 173 -0.249 0.613 -6.145 1.00 12.15 C ANISOU 6987 CG LEU D 173 1482 1561 1574 -25 11 -22 C ATOM 6988 CD1 LEU D 173 -1.342 -0.445 -6.087 1.00 11.07 C ANISOU 6988 CD1 LEU D 173 1430 1402 1372 32 -41 25 C ATOM 6989 CD2 LEU D 173 -0.003 1.199 -4.758 1.00 13.22 C ANISOU 6989 CD2 LEU D 173 1675 1754 1594 0 -6 -25 C ATOM 6990 N TYR D 174 1.108 1.493 -9.489 1.00 12.42 N ANISOU 6990 N TYR D 174 1581 1548 1588 -3 -22 16 N ATOM 6991 CA TYR D 174 0.653 2.511 -10.429 1.00 12.97 C ANISOU 6991 CA TYR D 174 1669 1635 1625 13 -24 38 C ATOM 6992 C TYR D 174 0.121 1.889 -11.712 1.00 13.57 C ANISOU 6992 C TYR D 174 1743 1748 1666 -17 -33 19 C ATOM 6993 O TYR D 174 -0.955 2.222 -12.203 1.00 13.71 O ANISOU 6993 O TYR D 174 1787 1758 1663 18 -53 -1 O ATOM 6994 CB TYR D 174 1.820 3.449 -10.747 1.00 13.42 C ANISOU 6994 CB TYR D 174 1730 1692 1675 -42 -24 -10 C ATOM 6995 CG TYR D 174 1.476 4.569 -11.704 1.00 14.32 C ANISOU 6995 CG TYR D 174 1848 1775 1818 -14 -36 39 C ATOM 6996 CD1 TYR D 174 0.697 5.641 -11.298 1.00 14.99 C ANISOU 6996 CD1 TYR D 174 1936 1851 1907 11 -42 -25 C ATOM 6997 CD2 TYR D 174 1.938 4.540 -13.012 1.00 15.04 C ANISOU 6997 CD2 TYR D 174 1947 1911 1857 -10 -22 3 C ATOM 6998 CE1 TYR D 174 0.391 6.667 -12.175 1.00 15.34 C ANISOU 6998 CE1 TYR D 174 1985 1862 1981 -2 -29 4 C ATOM 6999 CE2 TYR D 174 1.635 5.560 -13.898 1.00 15.34 C ANISOU 6999 CE2 TYR D 174 1981 1936 1912 -11 -29 22 C ATOM 7000 CZ TYR D 174 0.863 6.617 -13.467 1.00 15.99 C ANISOU 7000 CZ TYR D 174 2049 1996 2029 9 3 -7 C ATOM 7001 OH TYR D 174 0.557 7.629 -14.351 1.00 17.19 O ANISOU 7001 OH TYR D 174 2213 2136 2181 46 -54 72 O ATOM 7002 N LEU D 175 0.875 0.950 -12.257 1.00 14.49 N ANISOU 7002 N LEU D 175 1887 1806 1811 28 -1 20 N ATOM 7003 CA LEU D 175 0.584 0.257 -13.499 1.00 15.69 C ANISOU 7003 CA LEU D 175 2081 1985 1897 -20 -62 -14 C ATOM 7004 C LEU D 175 -0.381 -0.905 -13.358 1.00 16.27 C ANISOU 7004 C LEU D 175 2117 2043 2020 -26 -8 13 C ATOM 7005 O LEU D 175 -0.737 -1.566 -14.339 1.00 16.64 O ANISOU 7005 O LEU D 175 2177 2109 2036 -42 -50 15 O ATOM 7006 CB LEU D 175 1.912 -0.232 -14.081 1.00 17.74 C ANISOU 7006 CB LEU D 175 2219 2327 2193 93 -35 -75 C ATOM 7007 CG LEU D 175 2.647 0.528 -15.172 1.00 20.58 C ANISOU 7007 CG LEU D 175 2577 2590 2651 -51 90 59 C ATOM 7008 CD1 LEU D 175 2.237 1.979 -15.323 1.00 20.70 C ANISOU 7008 CD1 LEU D 175 2645 2594 2626 -15 20 -4 C ATOM 7009 CD2 LEU D 175 4.158 0.445 -14.944 1.00 19.73 C ANISOU 7009 CD2 LEU D 175 2576 2505 2416 -20 -33 -2 C ATOM 7010 N ASN D 176 -0.841 -1.209 -12.150 1.00 16.09 N ANISOU 7010 N ASN D 176 2071 2038 2004 4 -24 28 N ATOM 7011 CA ASN D 176 -1.725 -2.318 -11.843 1.00 16.46 C ANISOU 7011 CA ASN D 176 2105 2069 2079 -12 -14 13 C ATOM 7012 C ASN D 176 -1.069 -3.669 -12.115 1.00 16.65 C ANISOU 7012 C ASN D 176 2121 2091 2116 8 -21 11 C ATOM 7013 O ASN D 176 -1.742 -4.652 -12.438 1.00 17.29 O ANISOU 7013 O ASN D 176 2221 2126 2222 -17 -72 21 O ATOM 7014 CB ASN D 176 -3.059 -2.215 -12.592 1.00 17.18 C ANISOU 7014 CB ASN D 176 2122 2186 2220 2 -28 6 C ATOM 7015 CG ASN D 176 -3.769 -0.900 -12.337 1.00 16.95 C ANISOU 7015 CG ASN D 176 2137 2172 2131 -19 24 -34 C ATOM 7016 OD1 ASN D 176 -4.102 -0.557 -11.206 1.00 15.33 O ANISOU 7016 OD1 ASN D 176 1942 1903 1981 -24 -68 75 O ATOM 7017 ND2 ASN D 176 -3.975 -0.146 -13.415 1.00 18.41 N ANISOU 7017 ND2 ASN D 176 2428 2312 2254 -1 -83 26 N ATOM 7018 N LYS D 177 0.242 -3.748 -11.905 1.00 16.20 N ANISOU 7018 N LYS D 177 2103 2034 2017 6 -39 -2 N ATOM 7019 CA LYS D 177 1.012 -4.928 -12.253 1.00 16.44 C ANISOU 7019 CA LYS D 177 2134 2068 2046 23 -29 -16 C ATOM 7020 C LYS D 177 1.300 -5.799 -11.033 1.00 16.48 C ANISOU 7020 C LYS D 177 2146 2062 2055 21 0 -2 C ATOM 7021 O LYS D 177 1.908 -6.858 -11.194 1.00 16.66 O ANISOU 7021 O LYS D 177 2162 2071 2098 46 -56 23 O ATOM 7022 CB LYS D 177 2.330 -4.555 -12.931 1.00 17.59 C ANISOU 7022 CB LYS D 177 2199 2181 2304 -39 26 -24 C ATOM 7023 CG LYS D 177 2.191 -4.119 -14.381 1.00 20.40 C ANISOU 7023 CG LYS D 177 2737 2550 2465 18 -67 25 C ATOM 7024 CD LYS D 177 3.560 -3.866 -14.994 1.00 24.34 C ANISOU 7024 CD LYS D 177 2943 3093 3211 -25 63 -40 C ATOM 7025 CE LYS D 177 3.448 -3.310 -16.403 1.00 28.55 C ANISOU 7025 CE LYS D 177 3735 3618 3494 20 -24 54 C ATOM 7026 NZ LYS D 177 4.784 -2.930 -16.947 1.00 30.55 N ANISOU 7026 NZ LYS D 177 3829 3882 3897 -12 26 3 N ATOM 7027 N LEU D 178 0.883 -5.359 -9.848 1.00 16.11 N ANISOU 7027 N LEU D 178 2103 1987 2028 -18 -28 -24 N ATOM 7028 CA LEU D 178 1.026 -6.231 -8.683 1.00 16.17 C ANISOU 7028 CA LEU D 178 2093 2026 2025 0 -1 -27 C ATOM 7029 C LEU D 178 0.175 -7.480 -8.866 1.00 16.38 C ANISOU 7029 C LEU D 178 2098 2048 2078 -11 -23 -15 C ATOM 7030 O LEU D 178 -0.833 -7.470 -9.578 1.00 16.36 O ANISOU 7030 O LEU D 178 2118 2001 2098 14 -48 15 O ATOM 7031 CB LEU D 178 0.654 -5.515 -7.385 1.00 15.29 C ANISOU 7031 CB LEU D 178 1882 1973 1952 -32 -25 -1 C ATOM 7032 CG LEU D 178 1.610 -4.390 -6.964 1.00 14.59 C ANISOU 7032 CG LEU D 178 1859 1819 1865 51 -27 -14 C ATOM 7033 CD1 LEU D 178 1.103 -3.724 -5.692 1.00 14.93 C ANISOU 7033 CD1 LEU D 178 1956 1874 1841 21 -5 -10 C ATOM 7034 CD2 LEU D 178 3.024 -4.914 -6.779 1.00 13.81 C ANISOU 7034 CD2 LEU D 178 1787 1724 1737 2 17 -15 C ATOM 7035 N SER D 179 0.532 -8.543 -8.159 1.00 16.64 N ANISOU 7035 N SER D 179 2120 2069 2131 4 -45 -6 N ATOM 7036 CA SER D 179 -0.252 -9.771 -8.127 1.00 17.01 C ANISOU 7036 CA SER D 179 2138 2118 2208 -17 -15 0 C ATOM 7037 C SER D 179 -1.460 -9.643 -7.208 1.00 16.85 C ANISOU 7037 C SER D 179 2145 2096 2159 17 -25 -11 C ATOM 7038 O SER D 179 -1.566 -10.222 -6.129 1.00 17.74 O ANISOU 7038 O SER D 179 2328 2186 2225 -18 -25 18 O ATOM 7039 CB ASER D 179 0.627 -10.945 -7.689 0.50 16.86 C ANISOU 7039 CB ASER D 179 2152 2112 2141 -17 -9 10 C ATOM 7040 CB BSER D 179 0.632 -10.943 -7.693 0.50 17.16 C ANISOU 7040 CB BSER D 179 2181 2168 2171 21 -5 20 C ATOM 7041 OG ASER D 179 1.679 -11.170 -8.610 0.50 17.41 O ANISOU 7041 OG ASER D 179 2216 2194 2206 14 14 -11 O ATOM 7042 OG BSER D 179 -0.061 -12.171 -7.822 0.50 18.22 O ANISOU 7042 OG BSER D 179 2355 2238 2329 -22 -6 -13 O ATOM 7043 N ALA D 180 -2.440 -8.875 -7.657 1.00 16.20 N ANISOU 7043 N ALA D 180 2085 2022 2050 -26 -6 16 N ATOM 7044 CA ALA D 180 -3.647 -8.524 -6.941 1.00 15.97 C ANISOU 7044 CA ALA D 180 2067 1978 2022 13 -39 14 C ATOM 7045 C ALA D 180 -4.652 -8.021 -7.980 1.00 15.65 C ANISOU 7045 C ALA D 180 2010 1938 2000 -1 -21 -6 C ATOM 7046 O ALA D 180 -4.194 -7.607 -9.047 1.00 15.79 O ANISOU 7046 O ALA D 180 2051 1935 2012 11 -39 24 O ATOM 7047 CB ALA D 180 -3.376 -7.440 -5.911 1.00 16.21 C ANISOU 7047 CB ALA D 180 2141 1969 2049 35 -43 9 C ATOM 7048 N SER D 181 -5.941 -8.074 -7.684 1.00 15.73 N ANISOU 7048 N SER D 181 2014 1933 2028 -2 -22 -10 N ATOM 7049 CA SER D 181 -6.908 -7.598 -8.678 1.00 16.13 C ANISOU 7049 CA SER D 181 2064 2020 2044 2 -44 0 C ATOM 7050 C SER D 181 -6.623 -6.139 -9.009 1.00 16.40 C ANISOU 7050 C SER D 181 2141 2044 2048 -18 -40 15 C ATOM 7051 O SER D 181 -6.133 -5.390 -8.156 1.00 16.31 O ANISOU 7051 O SER D 181 2142 1977 2080 -39 -44 24 O ATOM 7052 CB SER D 181 -8.336 -7.761 -8.177 1.00 16.92 C ANISOU 7052 CB SER D 181 2119 2139 2172 0 2 29 C ATOM 7053 OG SER D 181 -8.614 -6.868 -7.115 1.00 17.25 O ANISOU 7053 OG SER D 181 2270 2081 2205 -12 -41 24 O ATOM 7054 N LYS D 182 -6.989 -5.709 -10.220 1.00 16.25 N ANISOU 7054 N LYS D 182 2086 2018 2070 -10 -59 15 N ATOM 7055 CA LYS D 182 -6.863 -4.287 -10.545 1.00 15.95 C ANISOU 7055 CA LYS D 182 2046 1993 2022 9 -12 -11 C ATOM 7056 C LYS D 182 -7.779 -3.465 -9.644 1.00 15.30 C ANISOU 7056 C LYS D 182 1968 1916 1929 -10 -48 21 C ATOM 7057 O LYS D 182 -7.408 -2.386 -9.182 1.00 15.11 O ANISOU 7057 O LYS D 182 1978 1865 1898 -25 -33 50 O ATOM 7058 CB LYS D 182 -7.155 -3.999 -12.019 1.00 17.60 C ANISOU 7058 CB LYS D 182 2338 2250 2099 -8 -50 19 C ATOM 7059 CG LYS D 182 -7.061 -2.518 -12.358 1.00 18.37 C ANISOU 7059 CG LYS D 182 2380 2272 2326 12 -13 8 C ATOM 7060 CD LYS D 182 -6.963 -2.251 -13.851 1.00 19.07 C ANISOU 7060 CD LYS D 182 2448 2426 2373 3 -5 26 C ATOM 7061 CE LYS D 182 -7.051 -0.753 -14.123 1.00 19.42 C ANISOU 7061 CE LYS D 182 2473 2425 2479 -14 -15 -17 C ATOM 7062 NZ LYS D 182 -6.682 -0.417 -15.525 1.00 20.26 N ANISOU 7062 NZ LYS D 182 2654 2494 2550 -34 8 33 N ATOM 7063 N GLU D 183 -8.972 -3.978 -9.368 1.00 15.11 N ANISOU 7063 N GLU D 183 1948 1919 1871 10 -50 5 N ATOM 7064 CA GLU D 183 -9.895 -3.374 -8.421 1.00 15.61 C ANISOU 7064 CA GLU D 183 2082 1981 1868 66 -49 -24 C ATOM 7065 C GLU D 183 -9.231 -3.020 -7.097 1.00 14.73 C ANISOU 7065 C GLU D 183 1942 1817 1837 34 -33 14 C ATOM 7066 O GLU D 183 -9.336 -1.881 -6.639 1.00 13.65 O ANISOU 7066 O GLU D 183 1816 1728 1644 -13 -75 74 O ATOM 7067 CB GLU D 183 -11.069 -4.326 -8.178 1.00 19.83 C ANISOU 7067 CB GLU D 183 2511 2365 2661 -198 -116 99 C ATOM 7068 CG GLU D 183 -12.135 -3.803 -7.235 1.00 25.91 C ANISOU 7068 CG GLU D 183 3319 3364 3162 194 86 -77 C ATOM 7069 CD GLU D 183 -13.293 -4.774 -7.083 1.00 31.75 C ANISOU 7069 CD GLU D 183 3905 3939 4221 -127 -34 42 C ATOM 7070 OE1 GLU D 183 -13.576 -5.519 -8.044 1.00 32.65 O ANISOU 7070 OE1 GLU D 183 4090 4068 4248 -36 -3 -21 O ATOM 7071 OE2 GLU D 183 -13.918 -4.772 -6.003 1.00 34.95 O ANISOU 7071 OE2 GLU D 183 4403 4485 4391 -16 59 8 O ATOM 7072 N ASN D 184 -8.576 -3.986 -6.451 1.00 14.36 N ANISOU 7072 N ASN D 184 1834 1794 1828 5 -23 5 N ATOM 7073 CA ASN D 184 -7.955 -3.718 -5.154 1.00 14.07 C ANISOU 7073 CA ASN D 184 1776 1774 1798 -48 5 16 C ATOM 7074 C ASN D 184 -6.780 -2.758 -5.241 1.00 13.16 C ANISOU 7074 C ASN D 184 1697 1649 1653 15 3 7 C ATOM 7075 O ASN D 184 -6.581 -1.921 -4.351 1.00 13.02 O ANISOU 7075 O ASN D 184 1703 1628 1616 -19 -53 57 O ATOM 7076 CB ASN D 184 -7.553 -5.048 -4.497 1.00 15.47 C ANISOU 7076 CB ASN D 184 1955 1854 2069 21 -39 53 C ATOM 7077 CG ASN D 184 -8.794 -5.813 -4.060 1.00 15.80 C ANISOU 7077 CG ASN D 184 1994 2027 1984 -26 30 -31 C ATOM 7078 OD1 ASN D 184 -9.834 -5.209 -3.800 1.00 15.65 O ANISOU 7078 OD1 ASN D 184 1952 1917 2077 -24 -53 117 O ATOM 7079 ND2 ASN D 184 -8.695 -7.133 -3.976 1.00 17.25 N ANISOU 7079 ND2 ASN D 184 2185 2119 2249 -19 -45 58 N ATOM 7080 N GLN D 185 -6.002 -2.832 -6.316 1.00 12.50 N ANISOU 7080 N GLN D 185 1582 1551 1617 -4 -42 44 N ATOM 7081 CA GLN D 185 -4.940 -1.853 -6.548 1.00 12.13 C ANISOU 7081 CA GLN D 185 1532 1517 1559 19 -19 24 C ATOM 7082 C GLN D 185 -5.508 -0.454 -6.711 1.00 11.85 C ANISOU 7082 C GLN D 185 1508 1484 1512 -10 -48 20 C ATOM 7083 O GLN D 185 -4.993 0.501 -6.121 1.00 11.75 O ANISOU 7083 O GLN D 185 1513 1492 1461 -6 -66 26 O ATOM 7084 CB GLN D 185 -4.083 -2.281 -7.741 1.00 12.03 C ANISOU 7084 CB GLN D 185 1527 1501 1544 -27 -31 -30 C ATOM 7085 CG GLN D 185 -3.429 -3.639 -7.495 1.00 13.49 C ANISOU 7085 CG GLN D 185 1679 1647 1800 45 -35 49 C ATOM 7086 CD GLN D 185 -2.591 -4.113 -8.658 1.00 14.67 C ANISOU 7086 CD GLN D 185 1759 1945 1869 -4 44 61 C ATOM 7087 OE1 GLN D 185 -2.969 -5.043 -9.380 1.00 17.89 O ANISOU 7087 OE1 GLN D 185 2401 2198 2198 -80 -71 -86 O ATOM 7088 NE2 GLN D 185 -1.440 -3.483 -8.837 1.00 12.10 N ANISOU 7088 NE2 GLN D 185 1674 1435 1487 34 -110 43 N ATOM 7089 N LEU D 186 -6.607 -0.312 -7.460 1.00 11.54 N ANISOU 7089 N LEU D 186 1460 1448 1478 -20 -26 -12 N ATOM 7090 CA LEU D 186 -7.248 0.992 -7.614 1.00 11.57 C ANISOU 7090 CA LEU D 186 1455 1473 1467 2 -10 22 C ATOM 7091 C LEU D 186 -7.824 1.514 -6.307 1.00 11.51 C ANISOU 7091 C LEU D 186 1455 1446 1475 -1 -7 19 C ATOM 7092 O LEU D 186 -7.733 2.709 -6.003 1.00 11.54 O ANISOU 7092 O LEU D 186 1449 1469 1469 -28 -16 -15 O ATOM 7093 CB LEU D 186 -8.333 0.902 -8.699 1.00 12.52 C ANISOU 7093 CB LEU D 186 1578 1603 1576 -22 -85 8 C ATOM 7094 CG LEU D 186 -7.811 0.714 -10.128 1.00 13.36 C ANISOU 7094 CG LEU D 186 1700 1724 1652 -37 -22 10 C ATOM 7095 CD1 LEU D 186 -8.931 0.225 -11.034 1.00 13.65 C ANISOU 7095 CD1 LEU D 186 1758 1714 1714 -56 -65 11 C ATOM 7096 CD2 LEU D 186 -7.232 2.022 -10.648 1.00 13.49 C ANISOU 7096 CD2 LEU D 186 1746 1722 1657 -18 -32 27 C ATOM 7097 N ILE D 187 -8.402 0.632 -5.492 1.00 11.38 N ANISOU 7097 N ILE D 187 1435 1447 1443 -4 2 3 N ATOM 7098 CA ILE D 187 -8.937 1.010 -4.190 1.00 11.03 C ANISOU 7098 CA ILE D 187 1402 1398 1389 -6 -24 27 C ATOM 7099 C ILE D 187 -7.837 1.594 -3.311 1.00 10.87 C ANISOU 7099 C ILE D 187 1407 1368 1358 -21 -14 49 C ATOM 7100 O ILE D 187 -8.006 2.659 -2.721 1.00 11.13 O ANISOU 7100 O ILE D 187 1420 1411 1400 32 -62 43 O ATOM 7101 CB ILE D 187 -9.611 -0.169 -3.465 1.00 11.68 C ANISOU 7101 CB ILE D 187 1560 1407 1472 -82 -15 2 C ATOM 7102 CG1 ILE D 187 -10.925 -0.539 -4.164 1.00 12.35 C ANISOU 7102 CG1 ILE D 187 1479 1610 1602 8 -9 34 C ATOM 7103 CG2 ILE D 187 -9.887 0.143 -1.999 1.00 12.72 C ANISOU 7103 CG2 ILE D 187 1674 1615 1544 -44 14 -34 C ATOM 7104 CD1 ILE D 187 -11.504 -1.871 -3.733 1.00 13.41 C ANISOU 7104 CD1 ILE D 187 1667 1644 1784 -25 -28 31 C ATOM 7105 N VAL D 188 -6.710 0.890 -3.222 1.00 11.27 N ANISOU 7105 N VAL D 188 1421 1400 1462 -22 -26 30 N ATOM 7106 CA VAL D 188 -5.617 1.363 -2.366 1.00 11.73 C ANISOU 7106 CA VAL D 188 1459 1487 1512 -46 -50 22 C ATOM 7107 C VAL D 188 -5.027 2.653 -2.918 1.00 12.04 C ANISOU 7107 C VAL D 188 1555 1495 1526 -35 -25 24 C ATOM 7108 O VAL D 188 -4.687 3.550 -2.139 1.00 12.25 O ANISOU 7108 O VAL D 188 1650 1444 1561 -49 -47 48 O ATOM 7109 CB VAL D 188 -4.553 0.279 -2.149 1.00 12.42 C ANISOU 7109 CB VAL D 188 1543 1512 1665 2 14 7 C ATOM 7110 CG1 VAL D 188 -3.339 0.818 -1.404 1.00 13.40 C ANISOU 7110 CG1 VAL D 188 1657 1701 1735 -35 -46 2 C ATOM 7111 CG2 VAL D 188 -5.150 -0.885 -1.361 1.00 12.30 C ANISOU 7111 CG2 VAL D 188 1581 1570 1522 0 -9 21 C ATOM 7112 N LYS D 189 -4.931 2.770 -4.240 1.00 12.28 N ANISOU 7112 N LYS D 189 1561 1556 1548 -27 -13 26 N ATOM 7113 CA LYS D 189 -4.450 4.012 -4.839 1.00 12.43 C ANISOU 7113 CA LYS D 189 1608 1560 1557 -24 -6 17 C ATOM 7114 C LYS D 189 -5.319 5.201 -4.483 1.00 12.86 C ANISOU 7114 C LYS D 189 1641 1631 1613 3 -4 -16 C ATOM 7115 O LYS D 189 -4.754 6.218 -4.052 1.00 12.97 O ANISOU 7115 O LYS D 189 1746 1596 1585 -14 -4 2 O ATOM 7116 CB LYS D 189 -4.284 3.856 -6.355 1.00 12.29 C ANISOU 7116 CB LYS D 189 1531 1600 1537 -4 -47 11 C ATOM 7117 CG LYS D 189 -3.018 3.067 -6.675 1.00 13.03 C ANISOU 7117 CG LYS D 189 1564 1698 1691 -3 10 -24 C ATOM 7118 CD LYS D 189 -2.721 3.008 -8.158 1.00 15.01 C ANISOU 7118 CD LYS D 189 1995 1941 1768 -3 -13 -8 C ATOM 7119 CE LYS D 189 -3.617 2.002 -8.864 1.00 15.67 C ANISOU 7119 CE LYS D 189 1933 2045 1976 -59 -22 -11 C ATOM 7120 NZ LYS D 189 -3.202 1.823 -10.285 1.00 16.73 N ANISOU 7120 NZ LYS D 189 2151 2177 2030 0 22 7 N ATOM 7121 N GLU D 190 -6.650 5.126 -4.569 1.00 12.88 N ANISOU 7121 N GLU D 190 1653 1638 1604 -5 -22 6 N ATOM 7122 CA GLU D 190 -7.429 6.300 -4.165 1.00 13.38 C ANISOU 7122 CA GLU D 190 1767 1662 1657 16 5 -25 C ATOM 7123 C GLU D 190 -7.219 6.640 -2.695 1.00 12.88 C ANISOU 7123 C GLU D 190 1682 1584 1628 -5 -14 12 C ATOM 7124 O GLU D 190 -7.150 7.817 -2.330 1.00 12.42 O ANISOU 7124 O GLU D 190 1560 1576 1583 -1 -39 -6 O ATOM 7125 CB GLU D 190 -8.922 6.196 -4.474 1.00 16.09 C ANISOU 7125 CB GLU D 190 1894 2130 2089 -33 -43 -1 C ATOM 7126 CG GLU D 190 -9.566 7.576 -4.306 1.00 18.63 C ANISOU 7126 CG GLU D 190 2423 2261 2393 65 -18 -15 C ATOM 7127 CD GLU D 190 -11.046 7.578 -4.610 1.00 20.32 C ANISOU 7127 CD GLU D 190 2524 2615 2582 8 -46 17 C ATOM 7128 OE1 GLU D 190 -11.835 7.269 -3.695 1.00 21.29 O ANISOU 7128 OE1 GLU D 190 2657 2814 2617 39 17 38 O ATOM 7129 OE2 GLU D 190 -11.391 7.895 -5.768 1.00 19.52 O ANISOU 7129 OE2 GLU D 190 2378 2537 2502 -11 -12 -17 O ATOM 7130 N ALA D 191 -7.045 5.646 -1.827 1.00 12.60 N ANISOU 7130 N ALA D 191 1619 1571 1597 -16 -53 0 N ATOM 7131 CA ALA D 191 -6.737 5.866 -0.424 1.00 12.41 C ANISOU 7131 CA ALA D 191 1596 1560 1559 -26 -13 33 C ATOM 7132 C ALA D 191 -5.405 6.560 -0.175 1.00 11.97 C ANISOU 7132 C ALA D 191 1544 1524 1480 -11 35 19 C ATOM 7133 O ALA D 191 -5.188 7.115 0.910 1.00 12.13 O ANISOU 7133 O ALA D 191 1584 1548 1478 22 -10 35 O ATOM 7134 CB ALA D 191 -6.742 4.534 0.326 1.00 12.11 C ANISOU 7134 CB ALA D 191 1532 1516 1554 -47 -7 22 C ATOM 7135 N LEU D 192 -4.497 6.550 -1.142 1.00 11.15 N ANISOU 7135 N LEU D 192 1421 1389 1425 8 -25 35 N ATOM 7136 CA LEU D 192 -3.201 7.191 -1.014 1.00 10.59 C ANISOU 7136 CA LEU D 192 1401 1320 1302 -6 -16 26 C ATOM 7137 C LEU D 192 -3.163 8.598 -1.590 1.00 10.25 C ANISOU 7137 C LEU D 192 1325 1328 1243 -10 -25 38 C ATOM 7138 O LEU D 192 -2.119 9.248 -1.504 1.00 10.18 O ANISOU 7138 O LEU D 192 1325 1368 1177 -19 -51 65 O ATOM 7139 CB LEU D 192 -2.135 6.318 -1.691 1.00 11.72 C ANISOU 7139 CB LEU D 192 1510 1429 1515 48 14 -24 C ATOM 7140 CG LEU D 192 -1.940 4.935 -1.055 1.00 12.49 C ANISOU 7140 CG LEU D 192 1685 1555 1504 11 -25 82 C ATOM 7141 CD1 LEU D 192 -1.049 4.066 -1.928 1.00 13.68 C ANISOU 7141 CD1 LEU D 192 1810 1699 1689 29 20 -9 C ATOM 7142 CD2 LEU D 192 -1.344 5.077 0.340 1.00 12.17 C ANISOU 7142 CD2 LEU D 192 1520 1582 1523 -5 -18 -8 C ATOM 7143 N VAL D 193 -4.263 9.081 -2.168 1.00 10.33 N ANISOU 7143 N VAL D 193 1324 1313 1287 1 -28 27 N ATOM 7144 CA VAL D 193 -4.266 10.446 -2.694 1.00 10.21 C ANISOU 7144 CA VAL D 193 1292 1274 1313 6 -40 0 C ATOM 7145 C VAL D 193 -4.111 11.437 -1.542 1.00 10.46 C ANISOU 7145 C VAL D 193 1357 1306 1314 17 -45 -2 C ATOM 7146 O VAL D 193 -4.892 11.386 -0.590 1.00 11.58 O ANISOU 7146 O VAL D 193 1474 1503 1422 -34 0 10 O ATOM 7147 CB VAL D 193 -5.538 10.783 -3.483 1.00 10.02 C ANISOU 7147 CB VAL D 193 1302 1215 1291 47 -30 16 C ATOM 7148 CG1 VAL D 193 -5.536 12.258 -3.893 1.00 10.53 C ANISOU 7148 CG1 VAL D 193 1422 1231 1348 -22 -31 10 C ATOM 7149 CG2 VAL D 193 -5.651 9.905 -4.721 1.00 10.76 C ANISOU 7149 CG2 VAL D 193 1371 1385 1333 8 -24 -31 C ATOM 7150 N THR D 194 -3.112 12.310 -1.635 1.00 10.24 N ANISOU 7150 N THR D 194 1329 1284 1278 33 -53 6 N ATOM 7151 CA THR D 194 -2.887 13.304 -0.592 1.00 10.92 C ANISOU 7151 CA THR D 194 1439 1374 1336 8 -41 -33 C ATOM 7152 C THR D 194 -2.940 14.734 -1.099 1.00 11.67 C ANISOU 7152 C THR D 194 1557 1429 1449 30 -13 7 C ATOM 7153 O THR D 194 -3.066 15.665 -0.293 1.00 12.28 O ANISOU 7153 O THR D 194 1746 1445 1474 35 -40 0 O ATOM 7154 CB THR D 194 -1.531 13.101 0.116 1.00 11.59 C ANISOU 7154 CB THR D 194 1399 1493 1512 9 -17 17 C ATOM 7155 OG1 THR D 194 -0.476 13.054 -0.850 1.00 11.76 O ANISOU 7155 OG1 THR D 194 1538 1597 1332 -35 -24 -19 O ATOM 7156 CG2 THR D 194 -1.529 11.820 0.931 1.00 12.29 C ANISOU 7156 CG2 THR D 194 1626 1544 1501 -21 20 26 C ATOM 7157 N GLU D 195 -2.760 14.951 -2.395 1.00 11.77 N ANISOU 7157 N GLU D 195 1544 1477 1451 26 -18 6 N ATOM 7158 CA GLU D 195 -2.853 16.286 -2.978 1.00 12.46 C ANISOU 7158 CA GLU D 195 1704 1520 1508 40 -45 15 C ATOM 7159 C GLU D 195 -3.614 16.185 -4.305 1.00 12.32 C ANISOU 7159 C GLU D 195 1645 1536 1502 14 -23 8 C ATOM 7160 O GLU D 195 -3.408 15.212 -5.033 1.00 11.87 O ANISOU 7160 O GLU D 195 1552 1542 1415 12 -61 23 O ATOM 7161 CB GLU D 195 -1.498 16.922 -3.246 1.00 16.34 C ANISOU 7161 CB GLU D 195 1910 2093 2207 -67 131 62 C ATOM 7162 CG GLU D 195 -0.554 17.186 -2.105 1.00 20.18 C ANISOU 7162 CG GLU D 195 2497 2656 2516 -61 -147 50 C ATOM 7163 CD GLU D 195 -1.096 18.008 -0.960 1.00 23.34 C ANISOU 7163 CD GLU D 195 3000 2937 2933 7 71 -82 C ATOM 7164 OE1 GLU D 195 -2.075 18.762 -1.134 1.00 23.84 O ANISOU 7164 OE1 GLU D 195 3039 3017 3001 -1 -32 11 O ATOM 7165 OE2 GLU D 195 -0.535 17.899 0.157 1.00 24.87 O ANISOU 7165 OE2 GLU D 195 3164 3181 3105 -6 -63 19 O ATOM 7166 N ALA D 196 -4.437 17.181 -4.606 1.00 12.64 N ANISOU 7166 N ALA D 196 1617 1609 1577 22 -14 20 N ATOM 7167 CA ALA D 196 -5.239 17.119 -5.824 1.00 12.78 C ANISOU 7167 CA ALA D 196 1664 1642 1549 9 2 33 C ATOM 7168 C ALA D 196 -5.484 18.511 -6.398 1.00 13.19 C ANISOU 7168 C ALA D 196 1752 1643 1616 27 13 31 C ATOM 7169 O ALA D 196 -5.980 19.429 -5.751 1.00 13.95 O ANISOU 7169 O ALA D 196 1894 1690 1715 92 32 28 O ATOM 7170 CB ALA D 196 -6.547 16.389 -5.567 1.00 13.23 C ANISOU 7170 CB ALA D 196 1677 1716 1636 -19 -31 -52 C ATOM 7171 N ALA D 197 -5.072 18.666 -7.643 1.00 12.72 N ANISOU 7171 N ALA D 197 1681 1566 1586 8 -12 30 N ATOM 7172 CA ALA D 197 -5.372 19.831 -8.472 1.00 12.17 C ANISOU 7172 CA ALA D 197 1609 1464 1550 -18 -9 -26 C ATOM 7173 C ALA D 197 -5.688 19.299 -9.867 1.00 12.47 C ANISOU 7173 C ALA D 197 1618 1572 1548 -11 -30 -9 C ATOM 7174 O ALA D 197 -5.407 18.140 -10.164 1.00 12.28 O ANISOU 7174 O ALA D 197 1580 1547 1538 -2 -10 42 O ATOM 7175 CB ALA D 197 -4.157 20.741 -8.535 1.00 11.78 C ANISOU 7175 CB ALA D 197 1534 1499 1442 11 7 26 C ATOM 7176 N PRO D 198 -6.197 20.142 -10.754 1.00 13.03 N ANISOU 7176 N PRO D 198 1679 1655 1618 21 -42 21 N ATOM 7177 CA PRO D 198 -6.652 19.676 -12.056 1.00 13.00 C ANISOU 7177 CA PRO D 198 1677 1652 1612 18 -38 18 C ATOM 7178 C PRO D 198 -5.600 18.901 -12.816 1.00 13.23 C ANISOU 7178 C PRO D 198 1685 1702 1639 12 -7 35 C ATOM 7179 O PRO D 198 -5.916 17.859 -13.400 1.00 14.12 O ANISOU 7179 O PRO D 198 1845 1791 1731 -24 6 -6 O ATOM 7180 CB PRO D 198 -7.089 20.959 -12.753 1.00 12.95 C ANISOU 7180 CB PRO D 198 1675 1643 1603 33 -28 5 C ATOM 7181 CG PRO D 198 -7.596 21.803 -11.625 1.00 13.31 C ANISOU 7181 CG PRO D 198 1727 1693 1638 25 -31 -33 C ATOM 7182 CD PRO D 198 -6.672 21.513 -10.466 1.00 13.32 C ANISOU 7182 CD PRO D 198 1721 1677 1664 24 -32 4 C ATOM 7183 N GLU D 199 -4.352 19.375 -12.831 1.00 13.22 N ANISOU 7183 N GLU D 199 1683 1695 1647 12 -1 60 N ATOM 7184 CA GLU D 199 -3.277 18.671 -13.511 1.00 13.36 C ANISOU 7184 CA GLU D 199 1663 1700 1713 18 -11 38 C ATOM 7185 C GLU D 199 -2.139 18.319 -12.557 1.00 13.22 C ANISOU 7185 C GLU D 199 1665 1678 1681 21 2 39 C ATOM 7186 O GLU D 199 -0.977 18.253 -12.955 1.00 12.84 O ANISOU 7186 O GLU D 199 1660 1633 1585 55 1 122 O ATOM 7187 CB GLU D 199 -2.735 19.495 -14.678 1.00 14.02 C ANISOU 7187 CB GLU D 199 1867 1730 1732 -7 27 27 C ATOM 7188 CG GLU D 199 -3.738 19.758 -15.791 1.00 15.02 C ANISOU 7188 CG GLU D 199 1850 1931 1927 32 -33 -5 C ATOM 7189 CD GLU D 199 -3.199 20.784 -16.771 1.00 16.36 C ANISOU 7189 CD GLU D 199 2054 2041 2120 -39 -18 70 C ATOM 7190 OE1 GLU D 199 -2.400 20.404 -17.645 1.00 18.04 O ANISOU 7190 OE1 GLU D 199 2363 2334 2157 -21 50 9 O ATOM 7191 OE2 GLU D 199 -3.580 21.960 -16.643 1.00 17.06 O ANISOU 7191 OE2 GLU D 199 2246 2089 2148 -19 -20 28 O ATOM 7192 N TYR D 200 -2.480 18.069 -11.297 1.00 13.54 N ANISOU 7192 N TYR D 200 1753 1700 1691 18 6 42 N ATOM 7193 CA TYR D 200 -1.462 17.680 -10.318 1.00 13.94 C ANISOU 7193 CA TYR D 200 1796 1747 1755 19 -11 61 C ATOM 7194 C TYR D 200 -2.093 16.737 -9.299 1.00 13.97 C ANISOU 7194 C TYR D 200 1840 1713 1757 43 7 62 C ATOM 7195 O TYR D 200 -3.013 17.144 -8.591 1.00 14.98 O ANISOU 7195 O TYR D 200 1940 1855 1898 96 64 81 O ATOM 7196 CB TYR D 200 -0.888 18.908 -9.621 1.00 14.88 C ANISOU 7196 CB TYR D 200 1964 1811 1878 8 7 -10 C ATOM 7197 CG TYR D 200 0.439 18.692 -8.929 1.00 16.27 C ANISOU 7197 CG TYR D 200 2067 2035 2078 14 -54 -18 C ATOM 7198 CD1 TYR D 200 1.629 18.871 -9.622 1.00 17.34 C ANISOU 7198 CD1 TYR D 200 2182 2215 2191 6 24 3 C ATOM 7199 CD2 TYR D 200 0.501 18.323 -7.591 1.00 17.00 C ANISOU 7199 CD2 TYR D 200 2235 2090 2136 9 -19 -5 C ATOM 7200 CE1 TYR D 200 2.854 18.681 -9.008 1.00 18.11 C ANISOU 7200 CE1 TYR D 200 2258 2320 2303 8 -16 -24 C ATOM 7201 CE2 TYR D 200 1.723 18.135 -6.968 1.00 17.69 C ANISOU 7201 CE2 TYR D 200 2289 2182 2249 1 -50 6 C ATOM 7202 CZ TYR D 200 2.888 18.313 -7.678 1.00 18.41 C ANISOU 7202 CZ TYR D 200 2346 2315 2334 8 4 3 C ATOM 7203 OH TYR D 200 4.108 18.124 -7.065 1.00 19.42 O ANISOU 7203 OH TYR D 200 2418 2494 2466 -2 -45 -34 O ATOM 7204 N LEU D 201 -1.613 15.499 -9.252 1.00 12.75 N ANISOU 7204 N LEU D 201 1704 1620 1521 -29 15 45 N ATOM 7205 CA LEU D 201 -2.181 14.543 -8.300 1.00 11.42 C ANISOU 7205 CA LEU D 201 1442 1438 1458 -4 -41 -17 C ATOM 7206 C LEU D 201 -1.060 13.832 -7.559 1.00 11.03 C ANISOU 7206 C LEU D 201 1436 1416 1337 11 -3 5 C ATOM 7207 O LEU D 201 -0.152 13.308 -8.206 1.00 10.50 O ANISOU 7207 O LEU D 201 1393 1422 1174 25 -34 107 O ATOM 7208 CB LEU D 201 -3.072 13.543 -9.036 1.00 11.01 C ANISOU 7208 CB LEU D 201 1398 1369 1418 -25 -31 56 C ATOM 7209 CG LEU D 201 -3.908 12.605 -8.161 1.00 10.12 C ANISOU 7209 CG LEU D 201 1364 1324 1156 25 -42 16 C ATOM 7210 CD1 LEU D 201 -4.950 13.362 -7.356 1.00 10.82 C ANISOU 7210 CD1 LEU D 201 1372 1414 1324 75 -14 58 C ATOM 7211 CD2 LEU D 201 -4.561 11.533 -9.026 1.00 11.31 C ANISOU 7211 CD2 LEU D 201 1498 1366 1435 -57 -60 -21 C ATOM 7212 N VAL D 202 -1.116 13.830 -6.226 1.00 10.85 N ANISOU 7212 N VAL D 202 1381 1400 1341 22 -21 46 N ATOM 7213 CA VAL D 202 -0.072 13.170 -5.448 1.00 10.20 C ANISOU 7213 CA VAL D 202 1335 1291 1248 -35 -17 26 C ATOM 7214 C VAL D 202 -0.641 11.943 -4.736 1.00 9.48 C ANISOU 7214 C VAL D 202 1210 1251 1142 5 -31 15 C ATOM 7215 O VAL D 202 -1.636 12.049 -4.030 1.00 9.12 O ANISOU 7215 O VAL D 202 1266 1194 1007 28 -40 14 O ATOM 7216 CB VAL D 202 0.564 14.107 -4.410 1.00 9.86 C ANISOU 7216 CB VAL D 202 1220 1260 1267 15 -77 31 C ATOM 7217 CG1 VAL D 202 1.619 13.367 -3.588 1.00 9.19 C ANISOU 7217 CG1 VAL D 202 1199 1179 1115 14 -22 25 C ATOM 7218 CG2 VAL D 202 1.198 15.324 -5.068 1.00 11.37 C ANISOU 7218 CG2 VAL D 202 1433 1406 1481 -49 17 77 C ATOM 7219 N HIS D 203 -0.023 10.793 -4.961 1.00 9.68 N ANISOU 7219 N HIS D 203 1288 1219 1173 -18 7 12 N ATOM 7220 CA HIS D 203 -0.249 9.608 -4.139 1.00 9.82 C ANISOU 7220 CA HIS D 203 1289 1251 1194 9 -17 31 C ATOM 7221 C HIS D 203 0.956 9.438 -3.212 1.00 10.36 C ANISOU 7221 C HIS D 203 1293 1375 1269 36 -29 24 C ATOM 7222 O HIS D 203 2.081 9.372 -3.716 1.00 10.45 O ANISOU 7222 O HIS D 203 1271 1462 1236 51 -58 15 O ATOM 7223 CB HIS D 203 -0.397 8.366 -5.012 1.00 9.75 C ANISOU 7223 CB HIS D 203 1281 1206 1217 -38 4 61 C ATOM 7224 CG HIS D 203 -1.651 8.328 -5.827 1.00 10.79 C ANISOU 7224 CG HIS D 203 1332 1405 1363 33 -45 -30 C ATOM 7225 ND1 HIS D 203 -1.879 9.130 -6.919 1.00 12.26 N ANISOU 7225 ND1 HIS D 203 1582 1570 1506 32 -13 76 N ATOM 7226 CD2 HIS D 203 -2.746 7.549 -5.700 1.00 11.84 C ANISOU 7226 CD2 HIS D 203 1446 1529 1525 -25 31 5 C ATOM 7227 CE1 HIS D 203 -3.071 8.855 -7.421 1.00 13.35 C ANISOU 7227 CE1 HIS D 203 1675 1678 1720 -7 -61 28 C ATOM 7228 NE2 HIS D 203 -3.626 7.899 -6.699 1.00 13.50 N ANISOU 7228 NE2 HIS D 203 1697 1837 1597 -22 -46 49 N ATOM 7229 N SER D 204 0.745 9.385 -1.900 1.00 10.38 N ANISOU 7229 N SER D 204 1293 1380 1269 56 -20 2 N ATOM 7230 CA SER D 204 1.928 9.326 -1.031 1.00 10.32 C ANISOU 7230 CA SER D 204 1322 1351 1249 -31 -30 13 C ATOM 7231 C SER D 204 1.618 8.606 0.273 1.00 10.46 C ANISOU 7231 C SER D 204 1346 1349 1279 1 -18 48 C ATOM 7232 O SER D 204 0.461 8.431 0.636 1.00 10.72 O ANISOU 7232 O SER D 204 1383 1364 1328 -4 -5 97 O ATOM 7233 CB SER D 204 2.463 10.730 -0.755 1.00 10.49 C ANISOU 7233 CB SER D 204 1347 1314 1325 -23 -24 56 C ATOM 7234 OG SER D 204 1.578 11.473 0.058 1.00 11.84 O ANISOU 7234 OG SER D 204 1530 1508 1462 42 8 -5 O ATOM 7235 N LYS D 205 2.691 8.230 0.961 1.00 10.42 N ANISOU 7235 N LYS D 205 1395 1348 1216 1 -28 62 N ATOM 7236 CA LYS D 205 2.543 7.500 2.219 1.00 9.63 C ANISOU 7236 CA LYS D 205 1240 1252 1168 -57 -35 22 C ATOM 7237 C LYS D 205 3.749 7.775 3.112 1.00 9.19 C ANISOU 7237 C LYS D 205 1154 1185 1153 14 -13 39 C ATOM 7238 O LYS D 205 4.892 7.599 2.685 1.00 8.41 O ANISOU 7238 O LYS D 205 1125 1132 938 -30 -30 49 O ATOM 7239 CB LYS D 205 2.411 5.998 1.967 1.00 10.07 C ANISOU 7239 CB LYS D 205 1314 1249 1265 54 -31 21 C ATOM 7240 CG LYS D 205 2.118 5.216 3.245 1.00 10.88 C ANISOU 7240 CG LYS D 205 1439 1360 1335 -51 16 50 C ATOM 7241 CD LYS D 205 0.706 5.475 3.751 1.00 12.32 C ANISOU 7241 CD LYS D 205 1540 1631 1508 24 39 11 C ATOM 7242 CE LYS D 205 0.598 5.160 5.239 1.00 11.37 C ANISOU 7242 CE LYS D 205 1394 1444 1483 12 -11 53 C ATOM 7243 NZ LYS D 205 1.352 6.156 6.054 1.00 12.35 N ANISOU 7243 NZ LYS D 205 1663 1505 1524 -13 -53 14 N ATOM 7244 N THR D 206 3.480 8.235 4.328 1.00 9.95 N ANISOU 7244 N THR D 206 1273 1294 1215 24 -13 4 N ATOM 7245 CA THR D 206 4.562 8.410 5.295 1.00 10.44 C ANISOU 7245 CA THR D 206 1351 1322 1293 -3 -68 18 C ATOM 7246 C THR D 206 4.893 7.086 5.972 1.00 10.03 C ANISOU 7246 C THR D 206 1306 1262 1244 -4 -13 -33 C ATOM 7247 O THR D 206 4.064 6.180 6.057 1.00 10.08 O ANISOU 7247 O THR D 206 1294 1355 1181 -37 -12 37 O ATOM 7248 CB THR D 206 4.160 9.429 6.379 1.00 12.34 C ANISOU 7248 CB THR D 206 1657 1533 1499 8 3 -105 C ATOM 7249 OG1 THR D 206 2.926 8.996 6.964 1.00 13.68 O ANISOU 7249 OG1 THR D 206 1759 1753 1685 5 50 10 O ATOM 7250 CG2 THR D 206 3.968 10.801 5.753 1.00 14.06 C ANISOU 7250 CG2 THR D 206 1887 1671 1782 40 -54 7 C ATOM 7251 N GLY D 207 6.106 7.007 6.512 1.00 10.07 N ANISOU 7251 N GLY D 207 1323 1269 1235 21 -31 -36 N ATOM 7252 CA GLY D 207 6.461 5.903 7.409 1.00 11.12 C ANISOU 7252 CA GLY D 207 1486 1358 1380 -5 -40 46 C ATOM 7253 C GLY D 207 7.358 6.441 8.522 1.00 11.39 C ANISOU 7253 C GLY D 207 1477 1436 1413 6 -48 20 C ATOM 7254 O GLY D 207 8.038 7.450 8.342 1.00 11.91 O ANISOU 7254 O GLY D 207 1519 1525 1482 -33 -62 60 O ATOM 7255 N PHE D 208 7.310 5.797 9.683 1.00 11.71 N ANISOU 7255 N PHE D 208 1524 1501 1424 11 -18 21 N ATOM 7256 CA PHE D 208 8.088 6.258 10.829 1.00 11.56 C ANISOU 7256 CA PHE D 208 1503 1466 1423 -19 -27 50 C ATOM 7257 C PHE D 208 8.170 5.144 11.866 1.00 11.28 C ANISOU 7257 C PHE D 208 1469 1423 1395 -4 -2 14 C ATOM 7258 O PHE D 208 7.118 4.625 12.236 1.00 11.66 O ANISOU 7258 O PHE D 208 1498 1476 1455 8 29 43 O ATOM 7259 CB PHE D 208 7.429 7.487 11.441 1.00 13.41 C ANISOU 7259 CB PHE D 208 1760 1592 1742 61 59 6 C ATOM 7260 CG PHE D 208 8.105 8.093 12.637 1.00 15.88 C ANISOU 7260 CG PHE D 208 2104 1985 1946 -39 -87 -15 C ATOM 7261 CD1 PHE D 208 9.468 8.299 12.674 1.00 17.02 C ANISOU 7261 CD1 PHE D 208 2148 2163 2156 -11 -4 59 C ATOM 7262 CD2 PHE D 208 7.335 8.488 13.724 1.00 17.86 C ANISOU 7262 CD2 PHE D 208 2321 2282 2181 53 57 -23 C ATOM 7263 CE1 PHE D 208 10.066 8.881 13.777 1.00 18.65 C ANISOU 7263 CE1 PHE D 208 2448 2345 2295 -53 -19 -46 C ATOM 7264 CE2 PHE D 208 7.925 9.064 14.831 1.00 18.73 C ANISOU 7264 CE2 PHE D 208 2388 2376 2352 -24 -31 -35 C ATOM 7265 CZ PHE D 208 9.289 9.263 14.854 1.00 18.57 C ANISOU 7265 CZ PHE D 208 2367 2361 2327 -9 -3 -10 C ATOM 7266 N SER D 209 9.373 4.773 12.280 1.00 11.34 N ANISOU 7266 N SER D 209 1475 1455 1378 -8 -6 6 N ATOM 7267 CA SER D 209 9.497 3.652 13.212 1.00 12.26 C ANISOU 7267 CA SER D 209 1632 1487 1540 26 3 50 C ATOM 7268 C SER D 209 9.592 4.131 14.656 1.00 13.29 C ANISOU 7268 C SER D 209 1773 1678 1599 18 3 0 C ATOM 7269 O SER D 209 9.475 3.307 15.568 1.00 13.96 O ANISOU 7269 O SER D 209 1866 1750 1688 12 -25 67 O ATOM 7270 CB SER D 209 10.722 2.798 12.887 1.00 12.32 C ANISOU 7270 CB SER D 209 1510 1635 1535 -8 -12 30 C ATOM 7271 OG SER D 209 11.911 3.529 13.132 1.00 11.88 O ANISOU 7271 OG SER D 209 1544 1551 1418 -5 -66 8 O ATOM 7272 N GLY D 210 9.810 5.424 14.847 1.00 13.68 N ANISOU 7272 N GLY D 210 1779 1717 1702 -23 -20 -3 N ATOM 7273 CA GLY D 210 10.038 5.960 16.190 1.00 14.52 C ANISOU 7273 CA GLY D 210 1926 1845 1745 4 -12 -28 C ATOM 7274 C GLY D 210 11.372 6.697 16.245 1.00 15.28 C ANISOU 7274 C GLY D 210 1949 1962 1894 -6 -6 -8 C ATOM 7275 O GLY D 210 12.219 6.557 15.361 1.00 15.81 O ANISOU 7275 O GLY D 210 2077 2055 1877 17 23 6 O ATOM 7276 N VAL D 211 11.530 7.567 17.238 1.00 15.60 N ANISOU 7276 N VAL D 211 2043 1977 1908 14 9 -19 N ATOM 7277 CA VAL D 211 12.767 8.310 17.435 1.00 16.17 C ANISOU 7277 CA VAL D 211 2104 2054 1986 -19 13 -37 C ATOM 7278 C VAL D 211 13.812 7.403 18.078 1.00 17.14 C ANISOU 7278 C VAL D 211 2223 2170 2118 6 -47 -2 C ATOM 7279 O VAL D 211 13.526 6.765 19.094 1.00 17.70 O ANISOU 7279 O VAL D 211 2334 2236 2154 -24 -13 11 O ATOM 7280 CB VAL D 211 12.542 9.555 18.312 1.00 15.78 C ANISOU 7280 CB VAL D 211 2002 1998 1994 5 -1 -7 C ATOM 7281 CG1 VAL D 211 13.820 10.365 18.465 1.00 15.20 C ANISOU 7281 CG1 VAL D 211 1980 1863 1932 40 -33 6 C ATOM 7282 CG2 VAL D 211 11.430 10.424 17.740 1.00 15.66 C ANISOU 7282 CG2 VAL D 211 2034 1966 1948 25 -4 -34 C ATOM 7283 N GLY D 212 14.999 7.335 17.492 1.00 17.97 N ANISOU 7283 N GLY D 212 2327 2312 2188 0 25 -37 N ATOM 7284 CA GLY D 212 16.084 6.552 18.078 1.00 19.37 C ANISOU 7284 CA GLY D 212 2481 2461 2418 81 6 12 C ATOM 7285 C GLY D 212 17.222 7.446 18.549 1.00 20.91 C ANISOU 7285 C GLY D 212 2690 2637 2617 -25 -37 -21 C ATOM 7286 O GLY D 212 17.066 8.656 18.714 1.00 21.43 O ANISOU 7286 O GLY D 212 2804 2668 2672 26 -75 -23 O ATOM 7287 N THR D 213 18.381 6.841 18.774 1.00 22.00 N ANISOU 7287 N THR D 213 2806 2766 2786 69 -16 9 N ATOM 7288 CA THR D 213 19.591 7.557 19.160 1.00 23.17 C ANISOU 7288 CA THR D 213 2933 2888 2983 5 -51 -19 C ATOM 7289 C THR D 213 20.491 7.788 17.960 1.00 24.18 C ANISOU 7289 C THR D 213 3083 3059 3044 35 -6 14 C ATOM 7290 O THR D 213 20.183 7.296 16.868 1.00 24.25 O ANISOU 7290 O THR D 213 3059 3094 3061 16 -42 8 O ATOM 7291 CB THR D 213 20.382 6.749 20.210 1.00 23.66 C ANISOU 7291 CB THR D 213 3045 2981 2965 24 -49 3 C ATOM 7292 OG1 THR D 213 20.787 5.507 19.617 1.00 23.96 O ANISOU 7292 OG1 THR D 213 3116 2992 2994 82 -64 27 O ATOM 7293 CG2 THR D 213 19.522 6.466 21.427 1.00 24.10 C ANISOU 7293 CG2 THR D 213 3065 3007 3085 14 14 -4 C ATOM 7294 N GLU D 214 21.591 8.528 18.102 1.00 25.14 N ANISOU 7294 N GLU D 214 3187 3164 3202 4 -62 1 N ATOM 7295 CA GLU D 214 22.490 8.747 16.973 1.00 26.56 C ANISOU 7295 CA GLU D 214 3412 3390 3291 110 36 37 C ATOM 7296 C GLU D 214 23.088 7.430 16.486 1.00 26.17 C ANISOU 7296 C GLU D 214 3323 3325 3296 31 -5 19 C ATOM 7297 O GLU D 214 23.186 7.202 15.280 1.00 26.08 O ANISOU 7297 O GLU D 214 3279 3324 3306 44 -26 6 O ATOM 7298 CB GLU D 214 23.596 9.744 17.308 1.00 31.97 C ANISOU 7298 CB GLU D 214 3989 3881 4276 -123 -191 -95 C ATOM 7299 CG GLU D 214 24.538 10.060 16.159 1.00 38.26 C ANISOU 7299 CG GLU D 214 4872 4957 4709 82 158 76 C ATOM 7300 CD GLU D 214 25.582 11.098 16.520 1.00 43.17 C ANISOU 7300 CD GLU D 214 5388 5403 5610 -94 -10 -88 C ATOM 7301 OE1 GLU D 214 26.196 10.983 17.602 1.00 44.63 O ANISOU 7301 OE1 GLU D 214 5664 5638 5654 -8 -12 1 O ATOM 7302 OE2 GLU D 214 25.789 12.030 15.715 1.00 44.94 O ANISOU 7302 OE2 GLU D 214 5714 5643 5717 -4 0 44 O ATOM 7303 N SER D 215 23.475 6.564 17.416 1.00 25.68 N ANISOU 7303 N SER D 215 3252 3224 3281 21 -28 -33 N ATOM 7304 CA SER D 215 24.044 5.267 17.096 1.00 25.10 C ANISOU 7304 CA SER D 215 3154 3163 3219 -40 -20 -30 C ATOM 7305 C SER D 215 22.993 4.272 16.622 1.00 24.05 C ANISOU 7305 C SER D 215 2989 3077 3071 20 9 -3 C ATOM 7306 O SER D 215 23.310 3.391 15.818 1.00 24.38 O ANISOU 7306 O SER D 215 3038 3093 3133 17 -8 -30 O ATOM 7307 CB ASER D 215 24.812 4.684 18.284 0.50 25.58 C ANISOU 7307 CB ASER D 215 3240 3214 3267 -3 -19 -3 C ATOM 7308 CB BSER D 215 24.761 4.689 18.323 0.50 26.02 C ANISOU 7308 CB BSER D 215 3304 3289 3292 22 -21 26 C ATOM 7309 OG ASER D 215 23.961 4.377 19.370 0.50 26.03 O ANISOU 7309 OG ASER D 215 3318 3278 3294 2 14 -1 O ATOM 7310 OG BSER D 215 25.620 5.654 18.907 0.50 26.83 O ANISOU 7310 OG BSER D 215 3409 3373 3413 -20 -31 -13 O ATOM 7311 N ASN D 216 21.756 4.380 17.101 1.00 22.68 N ANISOU 7311 N ASN D 216 2880 2839 2898 -26 -59 -20 N ATOM 7312 CA ASN D 216 20.681 3.487 16.691 1.00 21.18 C ANISOU 7312 CA ASN D 216 2644 2681 2721 95 -31 -9 C ATOM 7313 C ASN D 216 19.407 4.246 16.325 1.00 19.06 C ANISOU 7313 C ASN D 216 2470 2401 2371 -26 20 15 C ATOM 7314 O ASN D 216 18.406 4.220 17.039 1.00 18.57 O ANISOU 7314 O ASN D 216 2406 2330 2321 11 -21 4 O ATOM 7315 CB ASN D 216 20.342 2.486 17.799 1.00 23.22 C ANISOU 7315 CB ASN D 216 3012 2978 2833 -62 27 43 C ATOM 7316 CG ASN D 216 21.335 1.354 17.937 1.00 25.96 C ANISOU 7316 CG ASN D 216 3315 3199 3350 73 28 26 C ATOM 7317 OD1 ASN D 216 21.437 0.491 17.067 1.00 25.95 O ANISOU 7317 OD1 ASN D 216 3376 3217 3268 -26 -34 33 O ATOM 7318 ND2 ASN D 216 22.082 1.365 19.037 1.00 27.79 N ANISOU 7318 ND2 ASN D 216 3556 3523 3481 10 -52 -12 N ATOM 7319 N PRO D 217 19.452 4.959 15.205 1.00 17.76 N ANISOU 7319 N PRO D 217 2217 2254 2276 35 -21 -32 N ATOM 7320 CA PRO D 217 18.366 5.823 14.784 1.00 16.52 C ANISOU 7320 CA PRO D 217 2088 2103 2087 -48 -20 -37 C ATOM 7321 C PRO D 217 17.127 5.065 14.339 1.00 15.24 C ANISOU 7321 C PRO D 217 1951 1930 1909 43 2 -2 C ATOM 7322 O PRO D 217 17.202 3.919 13.894 1.00 15.42 O ANISOU 7322 O PRO D 217 2011 1944 1903 30 -40 -18 O ATOM 7323 CB PRO D 217 18.978 6.615 13.630 1.00 16.77 C ANISOU 7323 CB PRO D 217 2114 2129 2129 -21 -4 -4 C ATOM 7324 CG PRO D 217 19.958 5.677 13.015 1.00 17.27 C ANISOU 7324 CG PRO D 217 2185 2179 2197 26 -14 -12 C ATOM 7325 CD PRO D 217 20.482 4.830 14.144 1.00 17.59 C ANISOU 7325 CD PRO D 217 2218 2242 2222 18 -28 10 C ATOM 7326 N GLY D 218 15.970 5.700 14.488 1.00 13.93 N ANISOU 7326 N GLY D 218 1805 1795 1695 -55 -49 -16 N ATOM 7327 CA GLY D 218 14.749 5.200 13.850 1.00 12.75 C ANISOU 7327 CA GLY D 218 1671 1643 1531 16 4 9 C ATOM 7328 C GLY D 218 14.817 5.574 12.369 1.00 11.56 C ANISOU 7328 C GLY D 218 1458 1466 1468 -13 5 -33 C ATOM 7329 O GLY D 218 15.749 6.257 11.942 1.00 10.89 O ANISOU 7329 O GLY D 218 1461 1324 1355 -23 -69 -58 O ATOM 7330 N VAL D 219 13.810 5.146 11.614 1.00 11.19 N ANISOU 7330 N VAL D 219 1425 1493 1333 -10 6 23 N ATOM 7331 CA VAL D 219 13.746 5.536 10.203 1.00 10.88 C ANISOU 7331 CA VAL D 219 1386 1420 1327 20 -10 10 C ATOM 7332 C VAL D 219 12.430 6.253 9.937 1.00 10.37 C ANISOU 7332 C VAL D 219 1346 1331 1262 -17 -6 -4 C ATOM 7333 O VAL D 219 11.396 5.928 10.519 1.00 9.92 O ANISOU 7333 O VAL D 219 1298 1313 1158 10 -45 -16 O ATOM 7334 CB VAL D 219 13.923 4.325 9.276 1.00 10.96 C ANISOU 7334 CB VAL D 219 1432 1387 1346 -1 8 23 C ATOM 7335 CG1 VAL D 219 12.814 3.308 9.496 1.00 10.85 C ANISOU 7335 CG1 VAL D 219 1418 1328 1376 15 -5 -44 C ATOM 7336 CG2 VAL D 219 13.992 4.767 7.820 1.00 11.23 C ANISOU 7336 CG2 VAL D 219 1463 1473 1331 45 -41 19 C ATOM 7337 N ALA D 220 12.489 7.269 9.085 1.00 10.34 N ANISOU 7337 N ALA D 220 1350 1309 1268 2 -6 -9 N ATOM 7338 CA ALA D 220 11.286 7.966 8.643 1.00 10.65 C ANISOU 7338 CA ALA D 220 1349 1421 1277 4 -42 -29 C ATOM 7339 C ALA D 220 11.262 7.918 7.114 1.00 10.59 C ANISOU 7339 C ALA D 220 1347 1410 1268 -13 -32 -9 C ATOM 7340 O ALA D 220 12.316 8.056 6.501 1.00 10.83 O ANISOU 7340 O ALA D 220 1383 1590 1142 -4 -51 -43 O ATOM 7341 CB ALA D 220 11.259 9.399 9.127 1.00 11.48 C ANISOU 7341 CB ALA D 220 1479 1382 1500 26 30 48 C ATOM 7342 N TRP D 221 10.078 7.729 6.557 1.00 10.02 N ANISOU 7342 N TRP D 221 1324 1263 1219 -11 -21 12 N ATOM 7343 CA TRP D 221 9.942 7.554 5.122 1.00 9.79 C ANISOU 7343 CA TRP D 221 1287 1200 1231 18 -38 -10 C ATOM 7344 C TRP D 221 8.910 8.536 4.551 1.00 9.68 C ANISOU 7344 C TRP D 221 1224 1267 1188 23 -10 14 C ATOM 7345 O TRP D 221 7.957 8.904 5.227 1.00 9.44 O ANISOU 7345 O TRP D 221 1191 1280 1118 66 -44 47 O ATOM 7346 CB TRP D 221 9.393 6.183 4.793 1.00 9.55 C ANISOU 7346 CB TRP D 221 1155 1204 1270 24 -48 -17 C ATOM 7347 CG TRP D 221 10.164 4.933 4.974 1.00 9.31 C ANISOU 7347 CG TRP D 221 1266 1128 1145 21 9 -4 C ATOM 7348 CD1 TRP D 221 10.196 4.134 6.086 1.00 9.99 C ANISOU 7348 CD1 TRP D 221 1323 1313 1160 64 -30 36 C ATOM 7349 CD2 TRP D 221 10.972 4.273 3.991 1.00 8.79 C ANISOU 7349 CD2 TRP D 221 1089 1206 1046 20 -37 38 C ATOM 7350 NE1 TRP D 221 10.993 3.040 5.859 1.00 9.32 N ANISOU 7350 NE1 TRP D 221 1313 1147 1082 -14 -30 16 N ATOM 7351 CE2 TRP D 221 11.481 3.099 4.577 1.00 8.97 C ANISOU 7351 CE2 TRP D 221 1143 1145 1121 2 2 25 C ATOM 7352 CE3 TRP D 221 11.323 4.575 2.669 1.00 8.50 C ANISOU 7352 CE3 TRP D 221 1116 1036 1078 -11 32 17 C ATOM 7353 CZ2 TRP D 221 12.317 2.221 3.890 1.00 9.45 C ANISOU 7353 CZ2 TRP D 221 1209 1239 1143 31 -14 -23 C ATOM 7354 CZ3 TRP D 221 12.156 3.706 1.992 1.00 8.15 C ANISOU 7354 CZ3 TRP D 221 1041 1044 1012 -32 0 -13 C ATOM 7355 CH2 TRP D 221 12.647 2.543 2.602 1.00 9.14 C ANISOU 7355 CH2 TRP D 221 1223 1131 1118 1 -93 2 C ATOM 7356 N TRP D 222 9.089 8.871 3.279 1.00 9.87 N ANISOU 7356 N TRP D 222 1250 1309 1191 24 -22 16 N ATOM 7357 CA TRP D 222 7.974 9.421 2.498 1.00 9.60 C ANISOU 7357 CA TRP D 222 1260 1240 1147 16 -29 -12 C ATOM 7358 C TRP D 222 8.096 8.823 1.103 1.00 9.36 C ANISOU 7358 C TRP D 222 1204 1222 1131 -13 -33 -4 C ATOM 7359 O TRP D 222 9.170 8.910 0.502 1.00 10.07 O ANISOU 7359 O TRP D 222 1243 1405 1178 3 -21 -6 O ATOM 7360 CB TRP D 222 7.993 10.942 2.477 1.00 10.81 C ANISOU 7360 CB TRP D 222 1388 1288 1432 -35 -1 -2 C ATOM 7361 CG TRP D 222 6.685 11.548 2.058 1.00 11.83 C ANISOU 7361 CG TRP D 222 1499 1546 1452 65 -52 -14 C ATOM 7362 CD1 TRP D 222 5.438 11.124 2.407 1.00 12.99 C ANISOU 7362 CD1 TRP D 222 1615 1665 1655 -13 17 27 C ATOM 7363 CD2 TRP D 222 6.502 12.707 1.234 1.00 12.87 C ANISOU 7363 CD2 TRP D 222 1716 1564 1610 54 -33 20 C ATOM 7364 NE1 TRP D 222 4.483 11.933 1.837 1.00 14.18 N ANISOU 7364 NE1 TRP D 222 1719 1836 1834 58 -13 51 N ATOM 7365 CE2 TRP D 222 5.114 12.913 1.116 1.00 14.21 C ANISOU 7365 CE2 TRP D 222 1757 1845 1796 -9 -2 12 C ATOM 7366 CE3 TRP D 222 7.378 13.580 0.587 1.00 14.44 C ANISOU 7366 CE3 TRP D 222 1851 1807 1828 -46 42 38 C ATOM 7367 CZ2 TRP D 222 4.579 13.966 0.372 1.00 15.66 C ANISOU 7367 CZ2 TRP D 222 1985 1938 2028 75 -21 54 C ATOM 7368 CZ3 TRP D 222 6.846 14.621 -0.156 1.00 15.41 C ANISOU 7368 CZ3 TRP D 222 1992 1905 1959 37 -34 30 C ATOM 7369 CH2 TRP D 222 5.459 14.799 -0.253 1.00 16.43 C ANISOU 7369 CH2 TRP D 222 2033 2040 2169 -4 1 26 C ATOM 7370 N VAL D 223 7.073 8.093 0.667 1.00 9.14 N ANISOU 7370 N VAL D 223 1192 1160 1121 7 -7 -13 N ATOM 7371 CA VAL D 223 7.140 7.393 -0.615 1.00 8.84 C ANISOU 7371 CA VAL D 223 1122 1171 1067 7 -18 17 C ATOM 7372 C VAL D 223 5.874 7.699 -1.415 1.00 8.99 C ANISOU 7372 C VAL D 223 1134 1204 1078 29 -9 21 C ATOM 7373 O VAL D 223 4.857 8.051 -0.824 1.00 8.80 O ANISOU 7373 O VAL D 223 1135 1203 1004 47 -16 81 O ATOM 7374 CB VAL D 223 7.297 5.872 -0.485 1.00 9.35 C ANISOU 7374 CB VAL D 223 1116 1180 1257 -12 7 -24 C ATOM 7375 CG1 VAL D 223 8.534 5.470 0.318 1.00 10.54 C ANISOU 7375 CG1 VAL D 223 1265 1410 1329 68 -50 15 C ATOM 7376 CG2 VAL D 223 6.071 5.228 0.154 1.00 8.91 C ANISOU 7376 CG2 VAL D 223 1109 1145 1133 -8 -52 55 C ATOM 7377 N GLY D 224 5.952 7.610 -2.738 1.00 9.01 N ANISOU 7377 N GLY D 224 1149 1212 1064 9 -11 57 N ATOM 7378 CA GLY D 224 4.721 7.687 -3.533 1.00 9.37 C ANISOU 7378 CA GLY D 224 1172 1266 1122 4 -37 14 C ATOM 7379 C GLY D 224 5.034 8.092 -4.969 1.00 9.63 C ANISOU 7379 C GLY D 224 1199 1300 1161 -5 3 32 C ATOM 7380 O GLY D 224 6.118 7.802 -5.476 1.00 9.75 O ANISOU 7380 O GLY D 224 1194 1383 1126 31 -40 -2 O ATOM 7381 N TRP D 225 4.073 8.758 -5.610 1.00 9.78 N ANISOU 7381 N TRP D 225 1306 1229 1181 -6 -36 45 N ATOM 7382 CA TRP D 225 4.332 9.308 -6.940 1.00 9.80 C ANISOU 7382 CA TRP D 225 1305 1222 1196 11 4 30 C ATOM 7383 C TRP D 225 3.552 10.602 -7.152 1.00 9.65 C ANISOU 7383 C TRP D 225 1230 1252 1183 23 -23 24 C ATOM 7384 O TRP D 225 2.526 10.863 -6.528 1.00 9.65 O ANISOU 7384 O TRP D 225 1276 1242 1148 92 -19 84 O ATOM 7385 CB TRP D 225 4.009 8.304 -8.041 1.00 10.23 C ANISOU 7385 CB TRP D 225 1362 1272 1253 15 28 -17 C ATOM 7386 CG TRP D 225 2.598 7.817 -8.111 1.00 11.32 C ANISOU 7386 CG TRP D 225 1412 1451 1436 -8 -29 -38 C ATOM 7387 CD1 TRP D 225 1.550 8.393 -8.772 1.00 11.84 C ANISOU 7387 CD1 TRP D 225 1465 1497 1535 48 -35 -12 C ATOM 7388 CD2 TRP D 225 2.075 6.628 -7.508 1.00 12.06 C ANISOU 7388 CD2 TRP D 225 1562 1493 1527 -49 55 -39 C ATOM 7389 NE1 TRP D 225 0.408 7.644 -8.605 1.00 12.44 N ANISOU 7389 NE1 TRP D 225 1578 1526 1624 -9 -3 -26 N ATOM 7390 CE2 TRP D 225 0.709 6.548 -7.839 1.00 12.69 C ANISOU 7390 CE2 TRP D 225 1627 1658 1535 65 -45 -3 C ATOM 7391 CE3 TRP D 225 2.639 5.615 -6.722 1.00 14.37 C ANISOU 7391 CE3 TRP D 225 1886 1804 1769 59 -78 66 C ATOM 7392 CZ2 TRP D 225 -0.107 5.505 -7.405 1.00 15.30 C ANISOU 7392 CZ2 TRP D 225 1931 1889 1994 -88 1 39 C ATOM 7393 CZ3 TRP D 225 1.828 4.581 -6.297 1.00 15.83 C ANISOU 7393 CZ3 TRP D 225 2026 1976 2013 -56 2 39 C ATOM 7394 CH2 TRP D 225 0.469 4.532 -6.639 1.00 16.39 C ANISOU 7394 CH2 TRP D 225 2053 2067 2109 33 -32 57 C ATOM 7395 N VAL D 226 4.099 11.434 -8.034 1.00 9.89 N ANISOU 7395 N VAL D 226 1307 1231 1219 11 -28 31 N ATOM 7396 CA VAL D 226 3.456 12.681 -8.434 1.00 10.39 C ANISOU 7396 CA VAL D 226 1360 1305 1281 55 -31 35 C ATOM 7397 C VAL D 226 3.068 12.587 -9.910 1.00 10.32 C ANISOU 7397 C VAL D 226 1343 1302 1275 -3 -16 21 C ATOM 7398 O VAL D 226 3.938 12.301 -10.734 1.00 10.39 O ANISOU 7398 O VAL D 226 1419 1351 1177 1 -37 21 O ATOM 7399 CB VAL D 226 4.399 13.887 -8.262 1.00 12.02 C ANISOU 7399 CB VAL D 226 1539 1447 1581 -45 -2 -14 C ATOM 7400 CG1 VAL D 226 3.717 15.176 -8.709 1.00 13.36 C ANISOU 7400 CG1 VAL D 226 1746 1583 1748 26 -28 57 C ATOM 7401 CG2 VAL D 226 4.875 14.006 -6.820 1.00 14.18 C ANISOU 7401 CG2 VAL D 226 1839 1854 1693 -19 -57 -10 C ATOM 7402 N GLU D 227 1.798 12.812 -10.211 1.00 10.65 N ANISOU 7402 N GLU D 227 1349 1366 1333 -7 2 36 N ATOM 7403 CA GLU D 227 1.396 13.004 -11.606 1.00 11.33 C ANISOU 7403 CA GLU D 227 1476 1465 1364 20 -12 28 C ATOM 7404 C GLU D 227 1.272 14.504 -11.862 1.00 11.63 C ANISOU 7404 C GLU D 227 1507 1484 1430 34 -14 30 C ATOM 7405 O GLU D 227 0.490 15.193 -11.207 1.00 11.85 O ANISOU 7405 O GLU D 227 1662 1502 1338 74 10 53 O ATOM 7406 CB GLU D 227 0.095 12.280 -11.924 1.00 12.52 C ANISOU 7406 CB GLU D 227 1516 1703 1538 -23 0 -24 C ATOM 7407 CG GLU D 227 0.219 10.759 -11.904 1.00 15.91 C ANISOU 7407 CG GLU D 227 2178 1875 1992 42 -11 5 C ATOM 7408 CD GLU D 227 -1.138 10.091 -12.012 1.00 18.68 C ANISOU 7408 CD GLU D 227 2312 2328 2456 -44 -14 32 C ATOM 7409 OE1 GLU D 227 -1.980 10.322 -11.122 1.00 20.02 O ANISOU 7409 OE1 GLU D 227 2558 2537 2512 -18 62 -42 O ATOM 7410 OE2 GLU D 227 -1.370 9.345 -12.981 1.00 20.27 O ANISOU 7410 OE2 GLU D 227 2658 2536 2505 -33 -38 -17 O ATOM 7411 N LYS D 228 2.086 14.995 -12.789 1.00 11.57 N ANISOU 7411 N LYS D 228 1474 1522 1401 6 -58 28 N ATOM 7412 CA LYS D 228 2.068 16.401 -13.155 1.00 12.64 C ANISOU 7412 CA LYS D 228 1683 1559 1560 31 -19 6 C ATOM 7413 C LYS D 228 1.820 16.495 -14.663 1.00 12.64 C ANISOU 7413 C LYS D 228 1678 1574 1550 6 17 28 C ATOM 7414 O LYS D 228 2.645 15.986 -15.422 1.00 12.35 O ANISOU 7414 O LYS D 228 1704 1522 1468 12 -19 14 O ATOM 7415 CB LYS D 228 3.380 17.111 -12.817 1.00 14.53 C ANISOU 7415 CB LYS D 228 1780 1908 1835 -58 -18 -37 C ATOM 7416 CG LYS D 228 3.313 18.594 -13.166 1.00 17.66 C ANISOU 7416 CG LYS D 228 2375 2091 2242 16 -23 44 C ATOM 7417 CD LYS D 228 4.646 19.283 -12.934 1.00 20.00 C ANISOU 7417 CD LYS D 228 2475 2569 2554 -60 -38 11 C ATOM 7418 CE LYS D 228 4.500 20.778 -13.192 1.00 21.89 C ANISOU 7418 CE LYS D 228 2834 2666 2816 18 -25 4 C ATOM 7419 NZ LYS D 228 5.700 21.527 -12.743 1.00 22.42 N ANISOU 7419 NZ LYS D 228 2813 2780 2925 2 -25 46 N ATOM 7420 N GLU D 229 0.722 17.136 -15.037 1.00 13.22 N ANISOU 7420 N GLU D 229 1696 1648 1678 -2 -24 16 N ATOM 7421 CA GLU D 229 0.318 17.114 -16.452 1.00 13.94 C ANISOU 7421 CA GLU D 229 1814 1767 1717 3 -59 -38 C ATOM 7422 C GLU D 229 0.314 15.675 -16.930 1.00 13.57 C ANISOU 7422 C GLU D 229 1734 1730 1691 6 -2 17 C ATOM 7423 O GLU D 229 -0.387 14.877 -16.281 1.00 13.33 O ANISOU 7423 O GLU D 229 1664 1716 1686 -28 -40 9 O ATOM 7424 CB GLU D 229 1.188 18.086 -17.249 1.00 16.24 C ANISOU 7424 CB GLU D 229 2089 2097 1982 -58 47 114 C ATOM 7425 CG GLU D 229 1.059 19.512 -16.722 1.00 19.36 C ANISOU 7425 CG GLU D 229 2581 2360 2416 93 -64 -90 C ATOM 7426 CD GLU D 229 2.078 20.492 -17.255 1.00 23.43 C ANISOU 7426 CD GLU D 229 2992 2892 3020 -132 45 55 C ATOM 7427 OE1 GLU D 229 3.190 20.097 -17.657 1.00 25.56 O ANISOU 7427 OE1 GLU D 229 3159 3266 3287 22 49 6 O ATOM 7428 OE2 GLU D 229 1.772 21.706 -17.265 1.00 24.04 O ANISOU 7428 OE2 GLU D 229 3077 2963 3094 -13 -5 60 O ATOM 7429 N THR D 230 1.045 15.289 -17.968 1.00 13.17 N ANISOU 7429 N THR D 230 1695 1679 1631 16 -40 21 N ATOM 7430 CA THR D 230 1.024 13.894 -18.400 1.00 13.30 C ANISOU 7430 CA THR D 230 1677 1683 1692 8 -27 14 C ATOM 7431 C THR D 230 2.283 13.128 -18.015 1.00 12.80 C ANISOU 7431 C THR D 230 1646 1611 1605 -5 -6 18 C ATOM 7432 O THR D 230 2.564 12.066 -18.580 1.00 13.13 O ANISOU 7432 O THR D 230 1695 1679 1615 36 -50 2 O ATOM 7433 CB THR D 230 0.814 13.749 -19.919 1.00 14.30 C ANISOU 7433 CB THR D 230 1839 1854 1741 -5 -23 -7 C ATOM 7434 OG1 THR D 230 1.871 14.427 -20.601 1.00 14.44 O ANISOU 7434 OG1 THR D 230 1863 2013 1613 -31 -62 39 O ATOM 7435 CG2 THR D 230 -0.530 14.327 -20.315 1.00 14.93 C ANISOU 7435 CG2 THR D 230 1871 1924 1877 12 -18 10 C ATOM 7436 N GLU D 231 3.052 13.669 -17.078 1.00 12.52 N ANISOU 7436 N GLU D 231 1636 1606 1514 18 2 62 N ATOM 7437 CA GLU D 231 4.258 12.994 -16.616 1.00 12.86 C ANISOU 7437 CA GLU D 231 1685 1642 1560 75 5 48 C ATOM 7438 C GLU D 231 4.007 12.360 -15.248 1.00 12.46 C ANISOU 7438 C GLU D 231 1608 1581 1545 39 15 26 C ATOM 7439 O GLU D 231 3.122 12.799 -14.524 1.00 12.28 O ANISOU 7439 O GLU D 231 1623 1576 1466 61 -19 43 O ATOM 7440 CB GLU D 231 5.455 13.937 -16.554 1.00 15.72 C ANISOU 7440 CB GLU D 231 1986 1969 2020 -128 -45 -8 C ATOM 7441 CG GLU D 231 6.797 13.243 -16.370 1.00 18.08 C ANISOU 7441 CG GLU D 231 2221 2308 2339 53 -29 51 C ATOM 7442 CD GLU D 231 7.047 12.154 -17.397 1.00 19.73 C ANISOU 7442 CD GLU D 231 2537 2386 2573 0 -17 -51 C ATOM 7443 OE1 GLU D 231 7.590 12.480 -18.473 1.00 22.62 O ANISOU 7443 OE1 GLU D 231 2962 2906 2727 -26 73 24 O ATOM 7444 OE2 GLU D 231 6.690 10.984 -17.142 1.00 17.74 O ANISOU 7444 OE2 GLU D 231 2338 2309 2093 70 -6 15 O ATOM 7445 N VAL D 232 4.788 11.335 -14.930 1.00 12.10 N ANISOU 7445 N VAL D 232 1537 1588 1474 6 -32 24 N ATOM 7446 CA VAL D 232 4.684 10.698 -13.618 1.00 12.28 C ANISOU 7446 CA VAL D 232 1552 1643 1472 -12 -26 11 C ATOM 7447 C VAL D 232 6.083 10.584 -13.027 1.00 12.19 C ANISOU 7447 C VAL D 232 1547 1627 1458 36 -18 1 C ATOM 7448 O VAL D 232 7.048 10.291 -13.731 1.00 11.99 O ANISOU 7448 O VAL D 232 1556 1621 1379 19 -32 1 O ATOM 7449 CB VAL D 232 3.977 9.341 -13.676 1.00 13.50 C ANISOU 7449 CB VAL D 232 1747 1622 1762 11 32 6 C ATOM 7450 CG1 VAL D 232 4.743 8.319 -14.502 1.00 13.15 C ANISOU 7450 CG1 VAL D 232 1730 1646 1620 29 -31 11 C ATOM 7451 CG2 VAL D 232 3.733 8.815 -12.266 1.00 14.50 C ANISOU 7451 CG2 VAL D 232 1860 1852 1798 -11 16 38 C ATOM 7452 N TYR D 233 6.201 10.922 -11.745 1.00 12.06 N ANISOU 7452 N TYR D 233 1523 1615 1445 24 -13 8 N ATOM 7453 CA TYR D 233 7.471 10.849 -11.035 1.00 11.62 C ANISOU 7453 CA TYR D 233 1491 1507 1418 -4 12 8 C ATOM 7454 C TYR D 233 7.298 9.927 -9.825 1.00 11.72 C ANISOU 7454 C TYR D 233 1508 1500 1444 14 -15 29 C ATOM 7455 O TYR D 233 6.439 10.235 -8.998 1.00 12.46 O ANISOU 7455 O TYR D 233 1606 1629 1502 30 40 20 O ATOM 7456 CB TYR D 233 7.916 12.227 -10.542 1.00 12.28 C ANISOU 7456 CB TYR D 233 1611 1542 1511 -16 -10 -18 C ATOM 7457 CG TYR D 233 8.161 13.221 -11.661 1.00 12.87 C ANISOU 7457 CG TYR D 233 1698 1587 1605 -42 -8 11 C ATOM 7458 CD1 TYR D 233 7.134 14.019 -12.143 1.00 13.29 C ANISOU 7458 CD1 TYR D 233 1771 1633 1644 -5 -27 -19 C ATOM 7459 CD2 TYR D 233 9.421 13.330 -12.231 1.00 13.59 C ANISOU 7459 CD2 TYR D 233 1732 1754 1679 -26 -1 -29 C ATOM 7460 CE1 TYR D 233 7.364 14.918 -13.173 1.00 13.73 C ANISOU 7460 CE1 TYR D 233 1829 1661 1728 -14 -24 5 C ATOM 7461 CE2 TYR D 233 9.660 14.229 -13.255 1.00 14.17 C ANISOU 7461 CE2 TYR D 233 1830 1770 1785 -32 3 2 C ATOM 7462 CZ TYR D 233 8.625 15.014 -13.716 1.00 14.67 C ANISOU 7462 CZ TYR D 233 1878 1828 1868 8 3 -8 C ATOM 7463 OH TYR D 233 8.868 15.903 -14.738 1.00 16.25 O ANISOU 7463 OH TYR D 233 2167 2029 1980 -20 11 82 O ATOM 7464 N PHE D 234 8.055 8.846 -9.769 1.00 11.27 N ANISOU 7464 N PHE D 234 1466 1456 1359 -17 -19 57 N ATOM 7465 CA PHE D 234 8.016 7.974 -8.592 1.00 10.66 C ANISOU 7465 CA PHE D 234 1378 1366 1305 -22 -42 11 C ATOM 7466 C PHE D 234 9.086 8.424 -7.604 1.00 10.09 C ANISOU 7466 C PHE D 234 1306 1330 1197 9 5 11 C ATOM 7467 O PHE D 234 10.191 8.775 -8.021 1.00 10.08 O ANISOU 7467 O PHE D 234 1355 1361 1112 -61 -23 20 O ATOM 7468 CB PHE D 234 8.234 6.514 -8.999 1.00 11.24 C ANISOU 7468 CB PHE D 234 1479 1396 1394 9 43 19 C ATOM 7469 CG PHE D 234 7.189 6.057 -9.986 1.00 12.98 C ANISOU 7469 CG PHE D 234 1638 1624 1669 -17 -91 -32 C ATOM 7470 CD1 PHE D 234 5.925 5.692 -9.558 1.00 13.54 C ANISOU 7470 CD1 PHE D 234 1729 1685 1732 -4 24 -16 C ATOM 7471 CD2 PHE D 234 7.486 6.021 -11.336 1.00 14.32 C ANISOU 7471 CD2 PHE D 234 1851 1832 1757 -13 2 -21 C ATOM 7472 CE1 PHE D 234 4.965 5.285 -10.468 1.00 14.18 C ANISOU 7472 CE1 PHE D 234 1777 1825 1786 18 -28 -16 C ATOM 7473 CE2 PHE D 234 6.528 5.616 -12.253 1.00 14.54 C ANISOU 7473 CE2 PHE D 234 1856 1874 1796 -29 -28 15 C ATOM 7474 CZ PHE D 234 5.273 5.249 -11.814 1.00 14.17 C ANISOU 7474 CZ PHE D 234 1778 1836 1768 12 -56 -5 C ATOM 7475 N PHE D 235 8.760 8.421 -6.309 1.00 9.49 N ANISOU 7475 N PHE D 235 1246 1214 1144 -40 -38 18 N ATOM 7476 CA PHE D 235 9.763 8.866 -5.343 1.00 9.22 C ANISOU 7476 CA PHE D 235 1206 1181 1115 -32 -21 29 C ATOM 7477 C PHE D 235 9.760 8.018 -4.077 1.00 8.93 C ANISOU 7477 C PHE D 235 1156 1179 1058 -17 -31 6 C ATOM 7478 O PHE D 235 8.737 7.484 -3.672 1.00 8.95 O ANISOU 7478 O PHE D 235 1149 1234 1017 2 -14 -13 O ATOM 7479 CB PHE D 235 9.594 10.332 -4.971 1.00 9.20 C ANISOU 7479 CB PHE D 235 1170 1155 1173 18 -31 66 C ATOM 7480 CG PHE D 235 8.386 10.684 -4.155 1.00 10.18 C ANISOU 7480 CG PHE D 235 1226 1335 1305 -7 24 -14 C ATOM 7481 CD1 PHE D 235 8.415 10.615 -2.772 1.00 11.75 C ANISOU 7481 CD1 PHE D 235 1522 1570 1374 32 2 2 C ATOM 7482 CD2 PHE D 235 7.215 11.097 -4.768 1.00 10.42 C ANISOU 7482 CD2 PHE D 235 1357 1295 1307 87 -13 10 C ATOM 7483 CE1 PHE D 235 7.308 10.952 -2.016 1.00 11.78 C ANISOU 7483 CE1 PHE D 235 1459 1581 1437 29 -17 19 C ATOM 7484 CE2 PHE D 235 6.104 11.433 -4.020 1.00 10.52 C ANISOU 7484 CE2 PHE D 235 1250 1398 1349 9 -24 31 C ATOM 7485 CZ PHE D 235 6.142 11.357 -2.642 1.00 11.57 C ANISOU 7485 CZ PHE D 235 1448 1552 1394 29 5 10 C ATOM 7486 N ALA D 236 10.937 7.958 -3.460 1.00 9.14 N ANISOU 7486 N ALA D 236 1155 1239 1079 -1 -24 20 N ATOM 7487 CA ALA D 236 11.066 7.291 -2.166 1.00 8.95 C ANISOU 7487 CA ALA D 236 1190 1141 1068 -36 -27 2 C ATOM 7488 C ALA D 236 12.160 8.002 -1.366 1.00 9.14 C ANISOU 7488 C ALA D 236 1138 1245 1090 -17 -28 -8 C ATOM 7489 O ALA D 236 13.272 8.218 -1.845 1.00 8.99 O ANISOU 7489 O ALA D 236 1177 1265 975 -30 -9 8 O ATOM 7490 CB ALA D 236 11.380 5.815 -2.334 1.00 10.07 C ANISOU 7490 CB ALA D 236 1326 1218 1281 63 -18 -15 C ATOM 7491 N PHE D 237 11.790 8.406 -0.162 1.00 8.97 N ANISOU 7491 N PHE D 237 1124 1200 1084 25 -34 -7 N ATOM 7492 CA PHE D 237 12.694 9.082 0.755 1.00 8.84 C ANISOU 7492 CA PHE D 237 1113 1150 1097 -21 -21 23 C ATOM 7493 C PHE D 237 12.777 8.301 2.067 1.00 8.64 C ANISOU 7493 C PHE D 237 1089 1147 1046 -12 6 -13 C ATOM 7494 O PHE D 237 11.749 7.839 2.562 1.00 8.38 O ANISOU 7494 O PHE D 237 1109 1138 938 -52 -3 -58 O ATOM 7495 CB PHE D 237 12.196 10.498 1.034 1.00 9.77 C ANISOU 7495 CB PHE D 237 1302 1184 1226 -12 11 5 C ATOM 7496 CG PHE D 237 12.909 11.243 2.123 1.00 10.36 C ANISOU 7496 CG PHE D 237 1362 1280 1292 15 -65 -15 C ATOM 7497 CD1 PHE D 237 12.508 11.092 3.440 1.00 10.62 C ANISOU 7497 CD1 PHE D 237 1274 1417 1345 19 11 9 C ATOM 7498 CD2 PHE D 237 13.957 12.102 1.839 1.00 11.62 C ANISOU 7498 CD2 PHE D 237 1427 1503 1484 -38 -6 27 C ATOM 7499 CE1 PHE D 237 13.147 11.770 4.462 1.00 11.94 C ANISOU 7499 CE1 PHE D 237 1552 1523 1462 -41 -31 -39 C ATOM 7500 CE2 PHE D 237 14.595 12.790 2.860 1.00 12.24 C ANISOU 7500 CE2 PHE D 237 1571 1552 1529 -36 -22 -35 C ATOM 7501 CZ PHE D 237 14.190 12.621 4.166 1.00 12.11 C ANISOU 7501 CZ PHE D 237 1513 1535 1554 -1 -13 2 C ATOM 7502 N ASN D 238 13.977 8.193 2.628 1.00 8.49 N ANISOU 7502 N ASN D 238 1086 1147 991 2 7 -50 N ATOM 7503 CA ASN D 238 14.068 7.755 4.024 1.00 9.08 C ANISOU 7503 CA ASN D 238 1175 1197 1078 10 -8 6 C ATOM 7504 C ASN D 238 15.202 8.535 4.682 1.00 9.65 C ANISOU 7504 C ASN D 238 1212 1272 1184 -41 -4 -15 C ATOM 7505 O ASN D 238 16.079 9.076 4.003 1.00 9.71 O ANISOU 7505 O ASN D 238 1210 1354 1127 -34 -9 -1 O ATOM 7506 CB ASN D 238 14.224 6.256 4.178 1.00 9.53 C ANISOU 7506 CB ASN D 238 1218 1205 1198 4 40 2 C ATOM 7507 CG ASN D 238 15.500 5.679 3.615 1.00 9.21 C ANISOU 7507 CG ASN D 238 1165 1194 1141 14 -6 33 C ATOM 7508 OD1 ASN D 238 16.602 6.042 4.026 1.00 8.99 O ANISOU 7508 OD1 ASN D 238 1203 1138 1075 -30 27 -11 O ATOM 7509 ND2 ASN D 238 15.363 4.759 2.665 1.00 10.64 N ANISOU 7509 ND2 ASN D 238 1455 1218 1369 16 -27 -54 N ATOM 7510 N MET D 239 15.123 8.644 6.000 1.00 9.98 N ANISOU 7510 N MET D 239 1282 1316 1194 -28 6 34 N ATOM 7511 CA MET D 239 16.180 9.304 6.756 1.00 10.60 C ANISOU 7511 CA MET D 239 1334 1389 1305 -40 -22 0 C ATOM 7512 C MET D 239 16.305 8.657 8.132 1.00 11.03 C ANISOU 7512 C MET D 239 1416 1430 1347 -14 -1 21 C ATOM 7513 O MET D 239 15.363 8.042 8.624 1.00 10.24 O ANISOU 7513 O MET D 239 1363 1337 1190 -2 -72 11 O ATOM 7514 CB MET D 239 15.898 10.797 6.910 1.00 12.24 C ANISOU 7514 CB MET D 239 1549 1492 1608 46 5 -31 C ATOM 7515 CG MET D 239 14.662 11.081 7.755 1.00 12.50 C ANISOU 7515 CG MET D 239 1546 1701 1503 18 -17 -8 C ATOM 7516 SD MET D 239 14.272 12.828 7.881 1.00 14.30 S ANISOU 7516 SD MET D 239 2119 1723 1593 -14 34 -71 S ATOM 7517 CE MET D 239 15.849 13.558 8.262 1.00 17.47 C ANISOU 7517 CE MET D 239 2159 2215 2263 -30 -61 -11 C ATOM 7518 N ASP D 240 17.482 8.836 8.721 1.00 12.13 N ANISOU 7518 N ASP D 240 1478 1596 1535 6 -60 10 N ATOM 7519 CA ASP D 240 17.679 8.403 10.104 1.00 12.82 C ANISOU 7519 CA ASP D 240 1674 1677 1520 -7 7 1 C ATOM 7520 C ASP D 240 17.107 9.480 11.021 1.00 13.16 C ANISOU 7520 C ASP D 240 1735 1653 1611 -13 -47 -36 C ATOM 7521 O ASP D 240 17.359 10.659 10.777 1.00 13.12 O ANISOU 7521 O ASP D 240 1782 1656 1547 -5 -28 -29 O ATOM 7522 CB ASP D 240 19.155 8.178 10.407 1.00 15.20 C ANISOU 7522 CB ASP D 240 1793 1998 1985 20 -50 -13 C ATOM 7523 CG ASP D 240 19.779 7.070 9.583 1.00 16.47 C ANISOU 7523 CG ASP D 240 2217 1987 2054 -18 18 -35 C ATOM 7524 OD1 ASP D 240 19.046 6.183 9.108 1.00 15.13 O ANISOU 7524 OD1 ASP D 240 1997 1995 1755 75 -20 -19 O ATOM 7525 OD2 ASP D 240 21.015 7.091 9.416 1.00 20.02 O ANISOU 7525 OD2 ASP D 240 2379 2660 2566 45 -20 0 O ATOM 7526 N ILE D 241 16.335 9.064 12.016 1.00 13.94 N ANISOU 7526 N ILE D 241 1802 1791 1705 -31 -11 0 N ATOM 7527 CA ILE D 241 15.778 10.058 12.939 1.00 15.04 C ANISOU 7527 CA ILE D 241 2020 1868 1825 19 26 -36 C ATOM 7528 C ILE D 241 16.218 9.746 14.364 1.00 15.48 C ANISOU 7528 C ILE D 241 2049 1941 1892 12 -5 14 C ATOM 7529 O ILE D 241 15.911 8.698 14.919 1.00 14.90 O ANISOU 7529 O ILE D 241 1998 1919 1745 9 -41 -22 O ATOM 7530 CB ILE D 241 14.263 10.206 12.792 1.00 18.35 C ANISOU 7530 CB ILE D 241 2163 2396 2413 52 22 34 C ATOM 7531 CG1 ILE D 241 13.694 11.161 13.851 1.00 19.66 C ANISOU 7531 CG1 ILE D 241 2558 2513 2399 7 31 -27 C ATOM 7532 CG2 ILE D 241 13.535 8.876 12.844 1.00 20.50 C ANISOU 7532 CG2 ILE D 241 2600 2511 2678 -35 17 -14 C ATOM 7533 CD1 ILE D 241 12.316 11.681 13.482 1.00 21.67 C ANISOU 7533 CD1 ILE D 241 2672 2792 2768 31 -21 -16 C ATOM 7534 N ASP D 242 16.968 10.694 14.915 1.00 16.22 N ANISOU 7534 N ASP D 242 2146 2008 2007 -8 -9 -42 N ATOM 7535 CA ASP D 242 17.507 10.570 16.266 1.00 17.23 C ANISOU 7535 CA ASP D 242 2308 2155 2084 15 -43 -11 C ATOM 7536 C ASP D 242 17.095 11.787 17.090 1.00 17.38 C ANISOU 7536 C ASP D 242 2282 2169 2154 49 -26 -12 C ATOM 7537 O ASP D 242 17.600 12.029 18.183 1.00 18.46 O ANISOU 7537 O ASP D 242 2423 2351 2241 37 -81 -35 O ATOM 7538 CB ASP D 242 19.018 10.438 16.231 1.00 20.57 C ANISOU 7538 CB ASP D 242 2475 2701 2639 77 -65 -45 C ATOM 7539 CG ASP D 242 19.797 11.497 15.498 1.00 23.41 C ANISOU 7539 CG ASP D 242 2995 2933 2968 -104 -12 40 C ATOM 7540 OD1 ASP D 242 19.340 12.654 15.420 1.00 24.43 O ANISOU 7540 OD1 ASP D 242 3107 3036 3139 1 -19 -24 O ATOM 7541 OD2 ASP D 242 20.895 11.176 14.986 1.00 25.16 O ANISOU 7541 OD2 ASP D 242 3150 3233 3175 31 7 -19 O ATOM 7542 N ASN D 243 16.185 12.565 16.526 1.00 16.59 N ANISOU 7542 N ASN D 243 2175 2116 2012 15 -18 -52 N ATOM 7543 CA ASN D 243 15.661 13.759 17.183 1.00 16.56 C ANISOU 7543 CA ASN D 243 2131 2099 2061 21 -23 -33 C ATOM 7544 C ASN D 243 14.232 13.966 16.702 1.00 16.52 C ANISOU 7544 C ASN D 243 2141 2069 2067 28 -20 -7 C ATOM 7545 O ASN D 243 13.988 14.072 15.499 1.00 16.72 O ANISOU 7545 O ASN D 243 2195 2102 2057 12 -28 -26 O ATOM 7546 CB ASN D 243 16.522 14.976 16.852 1.00 17.84 C ANISOU 7546 CB ASN D 243 2284 2252 2243 -65 16 39 C ATOM 7547 CG ASN D 243 16.168 16.220 17.637 1.00 19.41 C ANISOU 7547 CG ASN D 243 2521 2401 2453 42 8 -34 C ATOM 7548 OD1 ASN D 243 15.005 16.505 17.917 1.00 19.81 O ANISOU 7548 OD1 ASN D 243 2559 2511 2458 17 54 -43 O ATOM 7549 ND2 ASN D 243 17.184 16.997 18.004 1.00 20.81 N ANISOU 7549 ND2 ASN D 243 2663 2593 2652 -60 -18 0 N ATOM 7550 N GLU D 244 13.288 14.049 17.623 1.00 16.81 N ANISOU 7550 N GLU D 244 2186 2085 2117 6 7 -6 N ATOM 7551 CA GLU D 244 11.880 14.221 17.303 1.00 18.22 C ANISOU 7551 CA GLU D 244 2280 2267 2377 9 -84 -7 C ATOM 7552 C GLU D 244 11.599 15.425 16.422 1.00 18.38 C ANISOU 7552 C GLU D 244 2342 2316 2327 31 -15 -6 C ATOM 7553 O GLU D 244 10.722 15.377 15.555 1.00 18.42 O ANISOU 7553 O GLU D 244 2377 2327 2295 42 -16 -17 O ATOM 7554 CB GLU D 244 11.088 14.326 18.610 1.00 22.40 C ANISOU 7554 CB GLU D 244 3037 2850 2624 28 157 -11 C ATOM 7555 CG GLU D 244 9.582 14.354 18.450 1.00 28.46 C ANISOU 7555 CG GLU D 244 3423 3618 3771 -19 -117 30 C ATOM 7556 CD GLU D 244 8.869 14.633 19.762 1.00 32.81 C ANISOU 7556 CD GLU D 244 4205 4199 4061 -34 106 -47 C ATOM 7557 OE1 GLU D 244 9.365 14.187 20.816 1.00 33.72 O ANISOU 7557 OE1 GLU D 244 4289 4312 4213 -4 6 10 O ATOM 7558 OE2 GLU D 244 7.814 15.300 19.735 1.00 34.52 O ANISOU 7558 OE2 GLU D 244 4360 4363 4392 31 15 0 O ATOM 7559 N SER D 245 12.332 16.515 16.580 1.00 19.02 N ANISOU 7559 N SER D 245 2441 2392 2392 -20 24 -13 N ATOM 7560 CA SER D 245 12.155 17.759 15.861 1.00 19.66 C ANISOU 7560 CA SER D 245 2548 2453 2471 33 2 21 C ATOM 7561 C SER D 245 12.497 17.676 14.376 1.00 19.86 C ANISOU 7561 C SER D 245 2587 2479 2479 26 9 -14 C ATOM 7562 O SER D 245 12.104 18.567 13.618 1.00 20.61 O ANISOU 7562 O SER D 245 2753 2509 2571 35 -23 8 O ATOM 7563 CB ASER D 245 13.042 18.852 16.481 0.50 20.71 C ANISOU 7563 CB ASER D 245 2615 2588 2666 -20 -11 -11 C ATOM 7564 CB BSER D 245 12.995 18.874 16.499 0.50 20.60 C ANISOU 7564 CB BSER D 245 2640 2576 2610 -17 -9 -12 C ATOM 7565 OG ASER D 245 12.812 18.989 17.868 0.50 21.74 O ANISOU 7565 OG ASER D 245 2811 2729 2719 3 5 8 O ATOM 7566 OG BSER D 245 14.368 18.714 16.192 0.50 20.92 O ANISOU 7566 OG BSER D 245 2662 2613 2672 -1 -17 -2 O ATOM 7567 N LYS D 246 13.211 16.650 13.943 1.00 19.04 N ANISOU 7567 N LYS D 246 2470 2428 2338 -18 8 13 N ATOM 7568 CA LYS D 246 13.599 16.477 12.554 1.00 18.45 C ANISOU 7568 CA LYS D 246 2399 2302 2310 -67 -17 -18 C ATOM 7569 C LYS D 246 12.550 15.758 11.718 1.00 17.53 C ANISOU 7569 C LYS D 246 2259 2193 2207 -9 28 13 C ATOM 7570 O LYS D 246 12.698 15.671 10.495 1.00 17.19 O ANISOU 7570 O LYS D 246 2266 2080 2183 -18 -28 -7 O ATOM 7571 CB LYS D 246 14.922 15.706 12.481 1.00 20.43 C ANISOU 7571 CB LYS D 246 2585 2563 2616 83 71 51 C ATOM 7572 CG LYS D 246 16.111 16.382 13.139 1.00 23.56 C ANISOU 7572 CG LYS D 246 2960 3029 2963 -26 -103 -106 C ATOM 7573 CD LYS D 246 16.611 17.560 12.321 1.00 27.12 C ANISOU 7573 CD LYS D 246 3587 3328 3391 -7 80 73 C ATOM 7574 CE LYS D 246 17.895 18.147 12.879 1.00 30.46 C ANISOU 7574 CE LYS D 246 3842 3888 3842 -90 -54 -11 C ATOM 7575 NZ LYS D 246 19.069 17.265 12.628 1.00 32.30 N ANISOU 7575 NZ LYS D 246 4083 4075 4116 41 15 4 N ATOM 7576 N LEU D 247 11.458 15.291 12.321 1.00 17.05 N ANISOU 7576 N LEU D 247 2175 2142 2161 -1 -15 -20 N ATOM 7577 CA LEU D 247 10.485 14.469 11.618 1.00 16.84 C ANISOU 7577 CA LEU D 247 2121 2148 2128 -21 29 -5 C ATOM 7578 C LEU D 247 9.876 15.126 10.391 1.00 17.34 C ANISOU 7578 C LEU D 247 2197 2226 2166 -8 0 7 C ATOM 7579 O LEU D 247 9.772 14.485 9.338 1.00 16.71 O ANISOU 7579 O LEU D 247 2152 2111 2087 1 7 69 O ATOM 7580 CB LEU D 247 9.382 13.958 12.549 1.00 15.79 C ANISOU 7580 CB LEU D 247 2095 1946 1959 -9 -29 -6 C ATOM 7581 CG LEU D 247 8.404 12.948 11.938 1.00 15.62 C ANISOU 7581 CG LEU D 247 1970 1992 1975 13 -4 -9 C ATOM 7582 CD1 LEU D 247 9.135 11.714 11.432 1.00 15.58 C ANISOU 7582 CD1 LEU D 247 1999 1973 1948 -8 -13 -23 C ATOM 7583 CD2 LEU D 247 7.337 12.551 12.949 1.00 16.27 C ANISOU 7583 CD2 LEU D 247 2073 2078 2032 -21 26 34 C ATOM 7584 N PRO D 248 9.536 16.412 10.455 1.00 18.38 N ANISOU 7584 N PRO D 248 2357 2287 2341 16 5 20 N ATOM 7585 CA PRO D 248 8.961 17.128 9.330 1.00 18.46 C ANISOU 7585 CA PRO D 248 2361 2334 2321 17 24 24 C ATOM 7586 C PRO D 248 9.818 17.205 8.084 1.00 17.71 C ANISOU 7586 C PRO D 248 2217 2245 2265 20 -16 8 C ATOM 7587 O PRO D 248 9.301 17.398 6.974 1.00 17.82 O ANISOU 7587 O PRO D 248 2255 2262 2254 27 10 48 O ATOM 7588 CB PRO D 248 8.696 18.524 9.891 1.00 19.20 C ANISOU 7588 CB PRO D 248 2485 2382 2430 34 12 -11 C ATOM 7589 CG PRO D 248 8.424 18.300 11.336 1.00 19.46 C ANISOU 7589 CG PRO D 248 2519 2424 2449 27 11 12 C ATOM 7590 CD PRO D 248 9.260 17.116 11.739 1.00 19.18 C ANISOU 7590 CD PRO D 248 2482 2402 2403 28 15 -20 C ATOM 7591 N LEU D 249 11.125 16.995 8.187 1.00 16.55 N ANISOU 7591 N LEU D 249 2147 2079 2063 -14 45 13 N ATOM 7592 CA LEU D 249 12.036 16.908 7.062 1.00 15.35 C ANISOU 7592 CA LEU D 249 1968 1880 1984 4 -29 -17 C ATOM 7593 C LEU D 249 11.725 15.770 6.106 1.00 14.75 C ANISOU 7593 C LEU D 249 1871 1857 1875 2 -4 17 C ATOM 7594 O LEU D 249 12.082 15.858 4.930 1.00 14.19 O ANISOU 7594 O LEU D 249 1818 1731 1843 -27 -21 17 O ATOM 7595 CB LEU D 249 13.484 16.786 7.567 1.00 14.76 C ANISOU 7595 CB LEU D 249 1926 1790 1894 -11 -3 -5 C ATOM 7596 CG LEU D 249 13.969 17.948 8.443 1.00 14.39 C ANISOU 7596 CG LEU D 249 1835 1839 1793 -17 -3 -15 C ATOM 7597 CD1 LEU D 249 15.352 17.678 9.008 1.00 14.82 C ANISOU 7597 CD1 LEU D 249 1868 1888 1875 11 1 54 C ATOM 7598 CD2 LEU D 249 13.980 19.249 7.648 1.00 16.07 C ANISOU 7598 CD2 LEU D 249 2109 1913 2084 13 -24 52 C ATOM 7599 N ARG D 250 11.030 14.722 6.539 1.00 14.75 N ANISOU 7599 N ARG D 250 1868 1826 1909 25 -21 37 N ATOM 7600 CA ARG D 250 10.595 13.631 5.686 1.00 15.26 C ANISOU 7600 CA ARG D 250 1941 1933 1925 57 -47 -35 C ATOM 7601 C ARG D 250 9.757 14.116 4.504 1.00 15.12 C ANISOU 7601 C ARG D 250 1920 1917 1908 17 -23 -12 C ATOM 7602 O ARG D 250 9.765 13.472 3.457 1.00 14.96 O ANISOU 7602 O ARG D 250 1913 1863 1910 30 22 8 O ATOM 7603 CB ARG D 250 9.801 12.593 6.500 1.00 18.63 C ANISOU 7603 CB ARG D 250 2506 2289 2284 -84 83 132 C ATOM 7604 CG ARG D 250 8.308 12.582 6.239 1.00 23.01 C ANISOU 7604 CG ARG D 250 2777 2951 3014 -13 -70 15 C ATOM 7605 CD ARG D 250 7.429 12.582 7.459 1.00 24.67 C ANISOU 7605 CD ARG D 250 3132 3177 3063 11 5 -66 C ATOM 7606 NE ARG D 250 7.250 11.278 8.056 1.00 26.10 N ANISOU 7606 NE ARG D 250 3374 3324 3220 -39 -44 33 N ATOM 7607 CZ ARG D 250 6.304 10.941 8.923 1.00 26.14 C ANISOU 7607 CZ ARG D 250 3269 3339 3324 15 -14 -11 C ATOM 7608 NH1 ARG D 250 5.389 11.802 9.336 1.00 25.34 N ANISOU 7608 NH1 ARG D 250 3307 3145 3177 -22 -51 -32 N ATOM 7609 NH2 ARG D 250 6.280 9.694 9.379 1.00 26.59 N ANISOU 7609 NH2 ARG D 250 3383 3356 3363 7 2 0 N ATOM 7610 N LYS D 251 8.951 15.160 4.694 1.00 15.30 N ANISOU 7610 N LYS D 251 1947 1902 1965 16 -11 10 N ATOM 7611 CA LYS D 251 8.241 15.772 3.583 1.00 15.41 C ANISOU 7611 CA LYS D 251 1999 1925 1931 -22 -27 17 C ATOM 7612 C LYS D 251 8.971 16.993 3.035 1.00 15.32 C ANISOU 7612 C LYS D 251 1968 1907 1947 -14 -21 -1 C ATOM 7613 O LYS D 251 8.945 17.177 1.815 1.00 15.49 O ANISOU 7613 O LYS D 251 1979 1946 1962 -3 4 17 O ATOM 7614 CB LYS D 251 6.811 16.158 3.967 1.00 17.70 C ANISOU 7614 CB LYS D 251 2140 2291 2293 63 27 -16 C ATOM 7615 CG LYS D 251 5.958 14.971 4.392 1.00 19.58 C ANISOU 7615 CG LYS D 251 2560 2383 2496 -58 39 37 C ATOM 7616 CD LYS D 251 4.501 15.388 4.548 1.00 22.31 C ANISOU 7616 CD LYS D 251 2731 2891 2856 62 -4 -9 C ATOM 7617 CE LYS D 251 3.666 14.253 5.114 1.00 24.15 C ANISOU 7617 CE LYS D 251 3077 2999 3101 -60 5 19 C ATOM 7618 NZ LYS D 251 2.254 14.674 5.355 1.00 25.63 N ANISOU 7618 NZ LYS D 251 3190 3261 3289 30 17 5 N ATOM 7619 N SER D 252 9.625 17.786 3.889 1.00 14.79 N ANISOU 7619 N SER D 252 1881 1846 1894 19 -9 25 N ATOM 7620 CA SER D 252 10.152 19.060 3.393 1.00 14.74 C ANISOU 7620 CA SER D 252 1856 1848 1895 11 -2 18 C ATOM 7621 C SER D 252 11.374 18.868 2.505 1.00 14.62 C ANISOU 7621 C SER D 252 1876 1832 1848 24 -5 24 C ATOM 7622 O SER D 252 11.531 19.618 1.535 1.00 14.99 O ANISOU 7622 O SER D 252 1954 1954 1788 0 -30 31 O ATOM 7623 CB SER D 252 10.426 20.051 4.516 1.00 15.70 C ANISOU 7623 CB SER D 252 2056 1927 1983 5 -16 -36 C ATOM 7624 OG SER D 252 11.449 19.640 5.398 1.00 16.55 O ANISOU 7624 OG SER D 252 2103 2038 2146 -43 -73 27 O ATOM 7625 N ILE D 253 12.233 17.894 2.799 1.00 13.93 N ANISOU 7625 N ILE D 253 1772 1804 1716 10 1 -16 N ATOM 7626 CA ILE D 253 13.395 17.660 1.938 1.00 13.61 C ANISOU 7626 CA ILE D 253 1762 1740 1668 5 -15 -9 C ATOM 7627 C ILE D 253 12.973 17.205 0.553 1.00 12.85 C ANISOU 7627 C ILE D 253 1671 1587 1626 5 3 7 C ATOM 7628 O ILE D 253 13.372 17.815 -0.448 1.00 12.59 O ANISOU 7628 O ILE D 253 1686 1496 1603 -12 33 -45 O ATOM 7629 CB ILE D 253 14.436 16.746 2.603 1.00 13.84 C ANISOU 7629 CB ILE D 253 1771 1780 1708 41 11 -4 C ATOM 7630 CG1 ILE D 253 15.045 17.502 3.789 1.00 13.69 C ANISOU 7630 CG1 ILE D 253 1726 1709 1768 -30 14 1 C ATOM 7631 CG2 ILE D 253 15.525 16.321 1.626 1.00 13.43 C ANISOU 7631 CG2 ILE D 253 1701 1727 1674 8 -10 7 C ATOM 7632 CD1 ILE D 253 16.098 16.767 4.580 1.00 14.61 C ANISOU 7632 CD1 ILE D 253 1847 1906 1800 8 -40 23 C ATOM 7633 N PRO D 254 12.120 16.194 0.455 1.00 12.73 N ANISOU 7633 N PRO D 254 1620 1605 1610 7 -11 38 N ATOM 7634 CA PRO D 254 11.613 15.738 -0.834 1.00 13.07 C ANISOU 7634 CA PRO D 254 1675 1642 1650 -24 1 -20 C ATOM 7635 C PRO D 254 10.914 16.837 -1.609 1.00 13.61 C ANISOU 7635 C PRO D 254 1748 1710 1712 -19 -22 13 C ATOM 7636 O PRO D 254 11.135 17.018 -2.810 1.00 14.00 O ANISOU 7636 O PRO D 254 1809 1790 1720 -23 -12 7 O ATOM 7637 CB PRO D 254 10.663 14.605 -0.467 1.00 12.95 C ANISOU 7637 CB PRO D 254 1697 1595 1629 -7 3 -22 C ATOM 7638 CG PRO D 254 11.265 14.024 0.762 1.00 13.11 C ANISOU 7638 CG PRO D 254 1682 1633 1665 -12 -44 -18 C ATOM 7639 CD PRO D 254 11.869 15.186 1.521 1.00 12.79 C ANISOU 7639 CD PRO D 254 1655 1577 1629 -32 -10 15 C ATOM 7640 N THR D 255 10.076 17.606 -0.922 1.00 14.34 N ANISOU 7640 N THR D 255 1815 1802 1831 5 23 -3 N ATOM 7641 CA THR D 255 9.386 18.741 -1.524 1.00 14.95 C ANISOU 7641 CA THR D 255 1938 1842 1902 -9 -60 22 C ATOM 7642 C THR D 255 10.369 19.744 -2.108 1.00 14.95 C ANISOU 7642 C THR D 255 1938 1858 1882 13 -7 4 C ATOM 7643 O THR D 255 10.222 20.147 -3.263 1.00 14.69 O ANISOU 7643 O THR D 255 1896 1817 1867 41 -28 -19 O ATOM 7644 CB THR D 255 8.443 19.407 -0.504 1.00 17.52 C ANISOU 7644 CB THR D 255 2177 2268 2210 38 103 -48 C ATOM 7645 OG1 THR D 255 7.441 18.452 -0.116 1.00 17.94 O ANISOU 7645 OG1 THR D 255 2296 2258 2264 -11 2 14 O ATOM 7646 CG2 THR D 255 7.760 20.630 -1.095 1.00 19.40 C ANISOU 7646 CG2 THR D 255 2463 2411 2498 66 -30 18 C ATOM 7647 N LYS D 256 11.398 20.123 -1.351 1.00 15.24 N ANISOU 7647 N LYS D 256 1912 1884 1993 21 -19 16 N ATOM 7648 CA LYS D 256 12.392 21.073 -1.832 1.00 15.98 C ANISOU 7648 CA LYS D 256 2010 1964 2098 2 45 35 C ATOM 7649 C LYS D 256 13.170 20.556 -3.031 1.00 15.77 C ANISOU 7649 C LYS D 256 2007 1944 2040 2 -11 9 C ATOM 7650 O LYS D 256 13.454 21.316 -3.961 1.00 16.40 O ANISOU 7650 O LYS D 256 2108 2002 2120 -37 10 43 O ATOM 7651 CB LYS D 256 13.354 21.465 -0.703 1.00 18.63 C ANISOU 7651 CB LYS D 256 2377 2368 2335 -95 -157 63 C ATOM 7652 CG LYS D 256 12.716 22.374 0.335 1.00 22.96 C ANISOU 7652 CG LYS D 256 2969 2848 2907 72 136 -58 C ATOM 7653 CD LYS D 256 13.714 22.796 1.402 1.00 26.18 C ANISOU 7653 CD LYS D 256 3269 3339 3339 -73 -111 42 C ATOM 7654 CE LYS D 256 13.065 23.715 2.425 1.00 29.19 C ANISOU 7654 CE LYS D 256 3744 3636 3710 43 83 -30 C ATOM 7655 NZ LYS D 256 14.052 24.208 3.426 1.00 30.94 N ANISOU 7655 NZ LYS D 256 3922 3919 3916 -13 -30 -20 N ATOM 7656 N ILE D 257 13.524 19.273 -3.044 1.00 15.15 N ANISOU 7656 N ILE D 257 1913 1909 1935 -13 -5 -9 N ATOM 7657 CA ILE D 257 14.160 18.671 -4.211 1.00 14.69 C ANISOU 7657 CA ILE D 257 1869 1825 1890 10 -26 21 C ATOM 7658 C ILE D 257 13.221 18.699 -5.412 1.00 14.93 C ANISOU 7658 C ILE D 257 1918 1885 1869 -2 -17 5 C ATOM 7659 O ILE D 257 13.636 19.093 -6.511 1.00 14.63 O ANISOU 7659 O ILE D 257 1860 1833 1865 -43 -57 30 O ATOM 7660 CB ILE D 257 14.646 17.241 -3.928 1.00 13.14 C ANISOU 7660 CB ILE D 257 1665 1733 1595 -27 -15 -42 C ATOM 7661 CG1 ILE D 257 15.758 17.275 -2.873 1.00 12.44 C ANISOU 7661 CG1 ILE D 257 1587 1554 1584 6 -6 21 C ATOM 7662 CG2 ILE D 257 15.150 16.571 -5.202 1.00 12.29 C ANISOU 7662 CG2 ILE D 257 1623 1498 1547 -14 -18 18 C ATOM 7663 CD1 ILE D 257 16.169 15.922 -2.339 1.00 11.84 C ANISOU 7663 CD1 ILE D 257 1494 1491 1512 -42 -25 -22 C ATOM 7664 N MET D 258 11.963 18.313 -5.211 1.00 15.35 N ANISOU 7664 N MET D 258 1960 1921 1950 -32 23 40 N ATOM 7665 CA MET D 258 11.003 18.314 -6.316 1.00 16.69 C ANISOU 7665 CA MET D 258 2052 2167 2124 -67 -45 15 C ATOM 7666 C MET D 258 10.657 19.729 -6.754 1.00 18.57 C ANISOU 7666 C MET D 258 2360 2293 2403 -4 -18 80 C ATOM 7667 O MET D 258 10.422 19.945 -7.947 1.00 19.07 O ANISOU 7667 O MET D 258 2443 2363 2439 -46 -79 46 O ATOM 7668 CB MET D 258 9.769 17.472 -5.974 1.00 14.95 C ANISOU 7668 CB MET D 258 1928 1897 1857 56 -37 -3 C ATOM 7669 CG MET D 258 10.118 15.988 -5.935 1.00 14.81 C ANISOU 7669 CG MET D 258 1866 1844 1916 -33 -35 -18 C ATOM 7670 SD MET D 258 8.730 14.887 -5.657 1.00 15.14 S ANISOU 7670 SD MET D 258 1988 1949 1814 -126 -96 130 S ATOM 7671 CE MET D 258 8.305 15.238 -3.958 1.00 16.60 C ANISOU 7671 CE MET D 258 2159 2120 2027 -18 69 -60 C ATOM 7672 N GLU D 259 10.667 20.698 -5.846 1.00 20.07 N ANISOU 7672 N GLU D 259 2579 2516 2530 -26 -33 -25 N ATOM 7673 CA GLU D 259 10.591 22.110 -6.217 1.00 21.64 C ANISOU 7673 CA GLU D 259 2766 2637 2819 14 -34 73 C ATOM 7674 C GLU D 259 11.777 22.519 -7.078 1.00 22.39 C ANISOU 7674 C GLU D 259 2848 2792 2868 -10 2 41 C ATOM 7675 O GLU D 259 11.620 23.157 -8.126 1.00 22.51 O ANISOU 7675 O GLU D 259 2847 2846 2859 -12 -25 49 O ATOM 7676 CB GLU D 259 10.505 22.988 -4.965 1.00 24.70 C ANISOU 7676 CB GLU D 259 3298 3027 3061 16 -65 -93 C ATOM 7677 CG GLU D 259 9.181 22.906 -4.229 1.00 28.58 C ANISOU 7677 CG GLU D 259 3517 3613 3731 2 72 64 C ATOM 7678 CD GLU D 259 9.165 23.550 -2.860 1.00 31.78 C ANISOU 7678 CD GLU D 259 4143 3977 3954 -2 -2 -40 C ATOM 7679 OE1 GLU D 259 10.237 23.807 -2.273 1.00 32.57 O ANISOU 7679 OE1 GLU D 259 4163 4072 4140 5 -32 -5 O ATOM 7680 OE2 GLU D 259 8.053 23.805 -2.339 1.00 33.10 O ANISOU 7680 OE2 GLU D 259 4200 4177 4200 31 26 -4 O ATOM 7681 N SER D 260 12.988 22.114 -6.694 1.00 22.65 N ANISOU 7681 N SER D 260 2885 2836 2885 4 -33 14 N ATOM 7682 CA SER D 260 14.199 22.464 -7.419 1.00 23.59 C ANISOU 7682 CA SER D 260 2984 2976 3004 -19 27 6 C ATOM 7683 C SER D 260 14.243 21.876 -8.823 1.00 23.82 C ANISOU 7683 C SER D 260 3021 3013 3015 -16 -3 -1 C ATOM 7684 O SER D 260 14.823 22.473 -9.735 1.00 24.21 O ANISOU 7684 O SER D 260 3077 3044 3078 -32 -11 47 O ATOM 7685 CB SER D 260 15.450 22.015 -6.652 1.00 24.87 C ANISOU 7685 CB SER D 260 3078 3206 3167 2 -47 13 C ATOM 7686 OG SER D 260 15.698 20.636 -6.865 1.00 26.47 O ANISOU 7686 OG SER D 260 3357 3303 3396 10 -19 4 O ATOM 7687 N GLU D 261 13.635 20.712 -9.022 1.00 23.62 N ANISOU 7687 N GLU D 261 2991 2987 2995 8 -9 8 N ATOM 7688 CA GLU D 261 13.550 20.054 -10.310 1.00 23.59 C ANISOU 7688 CA GLU D 261 2955 3019 2989 26 -13 3 C ATOM 7689 C GLU D 261 12.408 20.559 -11.183 1.00 23.07 C ANISOU 7689 C GLU D 261 2925 2910 2928 6 11 4 C ATOM 7690 O GLU D 261 12.272 20.126 -12.330 1.00 23.59 O ANISOU 7690 O GLU D 261 3037 2999 2928 7 7 36 O ATOM 7691 CB GLU D 261 13.369 18.541 -10.106 1.00 25.72 C ANISOU 7691 CB GLU D 261 3332 3131 3311 -52 22 10 C ATOM 7692 CG GLU D 261 14.576 17.848 -9.499 1.00 27.50 C ANISOU 7692 CG GLU D 261 3513 3429 3507 35 -79 23 C ATOM 7693 CD GLU D 261 15.777 17.838 -10.428 1.00 29.71 C ANISOU 7693 CD GLU D 261 3782 3763 3745 19 87 5 C ATOM 7694 OE1 GLU D 261 15.624 17.405 -11.587 1.00 29.68 O ANISOU 7694 OE1 GLU D 261 3736 3815 3725 18 18 33 O ATOM 7695 OE2 GLU D 261 16.868 18.259 -9.992 1.00 31.70 O ANISOU 7695 OE2 GLU D 261 3915 4037 4090 -38 -9 33 O ATOM 7696 N GLY D 262 11.539 21.398 -10.641 1.00 22.30 N ANISOU 7696 N GLY D 262 2832 2802 2839 -24 -23 41 N ATOM 7697 CA GLY D 262 10.467 22.019 -11.402 1.00 22.09 C ANISOU 7697 CA GLY D 262 2818 2773 2801 -20 -14 19 C ATOM 7698 C GLY D 262 9.198 21.179 -11.413 1.00 21.81 C ANISOU 7698 C GLY D 262 2785 2751 2751 5 -11 19 C ATOM 7699 O GLY D 262 8.257 21.487 -12.145 1.00 21.91 O ANISOU 7699 O GLY D 262 2825 2759 2741 25 -29 14 O ATOM 7700 N ILE D 263 9.161 20.124 -10.604 1.00 21.39 N ANISOU 7700 N ILE D 263 2751 2669 2707 14 -11 -17 N ATOM 7701 CA ILE D 263 7.966 19.297 -10.489 1.00 21.72 C ANISOU 7701 CA ILE D 263 2799 2689 2765 -9 -31 42 C ATOM 7702 C ILE D 263 6.902 20.041 -9.688 1.00 23.04 C ANISOU 7702 C ILE D 263 2897 2889 2969 37 25 12 C ATOM 7703 O ILE D 263 5.769 20.188 -10.141 1.00 22.59 O ANISOU 7703 O ILE D 263 2898 2802 2882 19 -3 -33 O ATOM 7704 CB ILE D 263 8.278 17.941 -9.835 1.00 19.53 C ANISOU 7704 CB ILE D 263 2413 2569 2440 13 38 -42 C ATOM 7705 CG1 ILE D 263 9.256 17.148 -10.713 1.00 18.23 C ANISOU 7705 CG1 ILE D 263 2355 2313 2258 6 -33 18 C ATOM 7706 CG2 ILE D 263 7.011 17.131 -9.603 1.00 19.31 C ANISOU 7706 CG2 ILE D 263 2447 2458 2432 -4 -22 -45 C ATOM 7707 CD1 ILE D 263 9.934 16.005 -9.986 1.00 18.08 C ANISOU 7707 CD1 ILE D 263 2299 2265 2307 35 10 -22 C ATOM 7708 N ILE D 264 7.274 20.466 -8.483 1.00 24.81 N ANISOU 7708 N ILE D 264 3155 3163 3108 -48 -54 -35 N ATOM 7709 CA ILE D 264 6.408 21.346 -7.700 1.00 26.69 C ANISOU 7709 CA ILE D 264 3360 3393 3390 33 38 -74 C ATOM 7710 C ILE D 264 6.608 22.779 -8.185 1.00 28.33 C ANISOU 7710 C ILE D 264 3635 3510 3617 -22 21 -11 C ATOM 7711 O ILE D 264 7.736 23.271 -8.249 1.00 28.31 O ANISOU 7711 O ILE D 264 3626 3510 3620 -4 -6 -10 O ATOM 7712 CB ILE D 264 6.682 21.242 -6.193 1.00 27.71 C ANISOU 7712 CB ILE D 264 3526 3542 3462 13 -14 -12 C ATOM 7713 CG1 ILE D 264 6.366 19.826 -5.706 1.00 28.82 C ANISOU 7713 CG1 ILE D 264 3682 3607 3660 -9 6 5 C ATOM 7714 CG2 ILE D 264 5.866 22.268 -5.416 1.00 28.12 C ANISOU 7714 CG2 ILE D 264 3577 3533 3575 20 2 -16 C ATOM 7715 CD1 ILE D 264 6.797 19.525 -4.289 1.00 29.23 C ANISOU 7715 CD1 ILE D 264 3718 3706 3683 7 -8 -1 C ATOM 7716 N GLY D 265 5.503 23.419 -8.553 1.00 29.84 N ANISOU 7716 N GLY D 265 3719 3775 3843 42 -16 -29 N ATOM 7717 CA GLY D 265 5.574 24.761 -9.126 1.00 31.30 C ANISOU 7717 CA GLY D 265 3956 3886 4049 4 -6 26 C ATOM 7718 C GLY D 265 5.715 24.676 -10.642 1.00 32.75 C ANISOU 7718 C GLY D 265 4150 4159 4136 -4 7 -24 C ATOM 7719 O GLY D 265 5.974 23.606 -11.190 1.00 32.99 O ANISOU 7719 O GLY D 265 4178 4153 4204 -5 -4 -20 O ATOM 7720 N GLY D 266 5.545 25.811 -11.311 1.00 33.89 N ANISOU 7720 N GLY D 266 4319 4218 4340 11 -4 16 N ATOM 7721 CA GLY D 266 5.604 25.856 -12.767 1.00 35.08 C ANISOU 7721 CA GLY D 266 4499 4419 4411 24 -5 -8 C ATOM 7722 C GLY D 266 6.769 26.711 -13.249 1.00 36.10 C ANISOU 7722 C GLY D 266 4571 4543 4603 -20 27 -21 C ATOM 7723 O GLY D 266 7.783 26.800 -12.522 1.00 36.52 O ANISOU 7723 O GLY D 266 4621 4614 4640 -4 3 -17 O ATOM 7724 OXT GLY D 266 6.674 27.288 -14.355 1.00 37.46 O ANISOU 7724 OXT GLY D 266 4810 4713 4710 9 -16 32 O TER 7725 GLY D 266 HETATM 7726 AU AUC A 301 18.165 9.000 32.204 1.00 18.63 AU ANISOU 7726 AU AUC A 301 2623 2503 1952 -103 -288 -221 AU HETATM 7727 C1 AUC A 301 18.176 7.270 32.227 1.00 18.96 C ANISOU 7727 C1 AUC A 301 2465 2466 2274 -4 -85 -32 C HETATM 7728 N1 AUC A 301 18.461 6.159 32.357 1.00 18.50 N ANISOU 7728 N1 AUC A 301 2440 2454 2133 -21 -93 -58 N HETATM 7729 C2 AUC A 301 17.790 10.677 31.921 1.00 19.14 C ANISOU 7729 C2 AUC A 301 2501 2486 2284 -53 -87 -59 C HETATM 7730 N2 AUC A 301 17.861 11.833 32.025 1.00 18.40 N ANISOU 7730 N2 AUC A 301 2432 2459 2101 -64 -85 -89 N HETATM 7731 S SO4 A 302 14.766 2.848 37.157 1.00 22.29 S ANISOU 7731 S SO4 A 302 2858 2855 2757 -15 -24 22 S HETATM 7732 O1 SO4 A 302 15.113 3.172 35.735 1.00 22.51 O ANISOU 7732 O1 SO4 A 302 2866 2912 2776 -2 -27 20 O HETATM 7733 O2 SO4 A 302 13.763 3.817 37.687 1.00 23.20 O ANISOU 7733 O2 SO4 A 302 2960 2974 2881 36 6 18 O HETATM 7734 O3 SO4 A 302 14.236 1.445 37.233 1.00 23.37 O ANISOU 7734 O3 SO4 A 302 3012 2936 2933 -55 -13 46 O HETATM 7735 O4 SO4 A 302 15.999 2.924 37.997 1.00 22.08 O ANISOU 7735 O4 SO4 A 302 2804 2810 2774 -28 20 38 O HETATM 7736 S SO4 A 303 20.217 29.057 28.714 1.00 45.18 S ANISOU 7736 S SO4 A 303 5731 5690 5746 2 -2 -5 S HETATM 7737 O1 SO4 A 303 19.412 28.625 27.525 1.00 45.14 O ANISOU 7737 O1 SO4 A 303 5735 5679 5736 1 3 -4 O HETATM 7738 O2 SO4 A 303 21.026 30.267 28.349 1.00 45.34 O ANISOU 7738 O2 SO4 A 303 5746 5709 5770 -6 -2 3 O HETATM 7739 O3 SO4 A 303 19.287 29.404 29.839 1.00 45.29 O ANISOU 7739 O3 SO4 A 303 5747 5719 5742 1 -3 -7 O HETATM 7740 O4 SO4 A 303 21.131 27.952 29.151 1.00 45.06 O ANISOU 7740 O4 SO4 A 303 5722 5677 5721 -6 -1 -1 O HETATM 7741 S SO4 A 304 34.686 3.240 34.978 1.00 56.81 S ANISOU 7741 S SO4 A 304 7217 7152 7216 2 1 2 S HETATM 7742 O1 SO4 A 304 34.819 4.007 33.695 1.00 56.81 O ANISOU 7742 O1 SO4 A 304 7218 7156 7210 4 4 -1 O HETATM 7743 O2 SO4 A 304 34.343 4.182 36.094 1.00 56.83 O ANISOU 7743 O2 SO4 A 304 7218 7163 7209 4 0 2 O HETATM 7744 O3 SO4 A 304 33.597 2.218 34.834 1.00 56.77 O ANISOU 7744 O3 SO4 A 304 7211 7150 7209 1 1 -2 O HETATM 7745 O4 SO4 A 304 35.984 2.551 35.284 1.00 56.84 O ANISOU 7745 O4 SO4 A 304 7216 7162 7217 4 -1 3 O HETATM 7746 S SO4 A 305 35.310 12.827 53.071 1.00 39.35 S ANISOU 7746 S SO4 A 305 4990 4949 5011 -9 1 -1 S HETATM 7747 O1 SO4 A 305 36.258 13.227 51.982 1.00 39.64 O ANISOU 7747 O1 SO4 A 305 5032 5004 5027 -9 7 -4 O HETATM 7748 O2 SO4 A 305 35.246 13.898 54.118 1.00 39.74 O ANISOU 7748 O2 SO4 A 305 5057 4997 5044 -16 -2 -14 O HETATM 7749 O3 SO4 A 305 33.943 12.617 52.488 1.00 39.55 O ANISOU 7749 O3 SO4 A 305 5012 4974 5039 -2 -8 4 O HETATM 7750 O4 SO4 A 305 35.780 11.551 53.703 1.00 39.72 O ANISOU 7750 O4 SO4 A 305 5048 4998 5046 15 -3 6 O HETATM 7751 S SO4 A 306 25.039 22.310 21.015 1.00 56.49 S ANISOU 7751 S SO4 A 306 7170 7114 7179 -1 7 1 S HETATM 7752 O1 SO4 A 306 23.603 22.010 20.706 1.00 56.49 O ANISOU 7752 O1 SO4 A 306 7174 7123 7169 -2 0 3 O HETATM 7753 O2 SO4 A 306 25.668 23.000 19.839 1.00 56.53 O ANISOU 7753 O2 SO4 A 306 7184 7129 7165 3 3 3 O HETATM 7754 O3 SO4 A 306 25.126 23.203 22.214 1.00 56.49 O ANISOU 7754 O3 SO4 A 306 7173 7121 7168 2 2 2 O HETATM 7755 O4 SO4 A 306 25.767 21.029 21.294 1.00 56.60 O ANISOU 7755 O4 SO4 A 306 7184 7125 7196 5 11 7 O HETATM 7756 S SO4 A 307 0.877 12.752 37.509 1.00 51.95 S ANISOU 7756 S SO4 A 307 6611 6547 6581 9 6 0 S HETATM 7757 O1 SO4 A 307 -0.396 12.854 38.293 1.00 52.09 O ANISOU 7757 O1 SO4 A 307 6605 6577 6611 4 2 -1 O HETATM 7758 O2 SO4 A 307 0.653 11.863 36.322 1.00 51.59 O ANISOU 7758 O2 SO4 A 307 6546 6499 6555 1 0 17 O HETATM 7759 O3 SO4 A 307 1.309 14.116 37.059 1.00 51.89 O ANISOU 7759 O3 SO4 A 307 6606 6535 6575 9 2 -6 O HETATM 7760 O4 SO4 A 307 1.944 12.164 38.387 1.00 51.84 O ANISOU 7760 O4 SO4 A 307 6591 6531 6575 -1 7 -3 O HETATM 7761 C1 EDO A 308 7.167 18.047 56.364 1.00 28.25 C ANISOU 7761 C1 EDO A 308 3600 3587 3545 28 -7 -3 C HETATM 7762 O1 EDO A 308 8.060 19.277 56.188 1.00 29.22 O ANISOU 7762 O1 EDO A 308 3708 3670 3725 -12 -8 -7 O HETATM 7763 C2 EDO A 308 7.716 16.957 57.304 1.00 27.76 C ANISOU 7763 C2 EDO A 308 3527 3526 3494 10 8 -25 C HETATM 7764 O2 EDO A 308 7.048 17.166 58.707 1.00 26.93 O ANISOU 7764 O2 EDO A 308 3408 3384 3440 -7 -8 16 O HETATM 7765 C1 EDO A 309 27.156 -7.767 41.338 1.00 31.88 C ANISOU 7765 C1 EDO A 309 4047 4014 4051 -1 10 -12 C HETATM 7766 O1 EDO A 309 28.626 -7.378 41.158 1.00 31.67 O ANISOU 7766 O1 EDO A 309 4026 3983 4025 6 -15 -17 O HETATM 7767 C2 EDO A 309 26.906 -8.990 42.236 1.00 32.13 C ANISOU 7767 C2 EDO A 309 4092 4038 4077 3 3 2 C HETATM 7768 O2 EDO A 309 27.534 -8.708 43.643 1.00 32.34 O ANISOU 7768 O2 EDO A 309 4108 4079 4100 4 -7 -4 O HETATM 7769 AU AUC B 301 -19.106 17.886 -22.052 1.00 18.75 AU ANISOU 7769 AU AUC B 301 2626 2555 1942 -99 -338 281 AU HETATM 7770 C1 AUC B 301 -18.901 16.183 -22.189 1.00 18.77 C ANISOU 7770 C1 AUC B 301 2391 2519 2223 -28 -93 57 C HETATM 7771 N1 AUC B 301 -18.725 15.049 -22.141 1.00 18.29 N ANISOU 7771 N1 AUC B 301 2369 2491 2089 -37 -114 92 N HETATM 7772 C2 AUC B 301 -19.091 19.617 -22.049 1.00 19.23 C ANISOU 7772 C2 AUC B 301 2484 2514 2309 1 -72 50 C HETATM 7773 N2 AUC B 301 -19.365 20.727 -21.873 1.00 18.89 N ANISOU 7773 N2 AUC B 301 2474 2501 2204 -20 -73 84 N HETATM 7774 S SO4 B 302 -16.847 23.944 -16.444 1.00 21.36 S ANISOU 7774 S SO4 B 302 2751 2756 2610 -16 -3 19 S HETATM 7775 O1 SO4 B 302 -18.230 24.173 -15.935 1.00 21.20 O ANISOU 7775 O1 SO4 B 302 2709 2715 2631 -3 -67 9 O HETATM 7776 O2 SO4 B 302 -16.013 25.129 -16.078 1.00 22.48 O ANISOU 7776 O2 SO4 B 302 2926 2843 2772 -65 -10 -20 O HETATM 7777 O3 SO4 B 302 -16.330 22.705 -15.773 1.00 22.22 O ANISOU 7777 O3 SO4 B 302 2902 2785 2755 34 -27 6 O HETATM 7778 O4 SO4 B 302 -16.858 23.739 -17.926 1.00 21.72 O ANISOU 7778 O4 SO4 B 302 2807 2794 2653 -26 2 -6 O HETATM 7779 S SO4 B 303 -7.910 30.577 -21.300 1.00 31.69 S ANISOU 7779 S SO4 B 303 4047 3975 4021 -1 -1 -12 S HETATM 7780 O1 SO4 B 303 -9.081 31.159 -20.567 1.00 31.60 O ANISOU 7780 O1 SO4 B 303 4029 3956 4022 -3 4 4 O HETATM 7781 O2 SO4 B 303 -6.643 31.221 -20.817 1.00 31.67 O ANISOU 7781 O2 SO4 B 303 4036 3981 4017 3 2 4 O HETATM 7782 O3 SO4 B 303 -7.849 29.099 -21.048 1.00 31.42 O ANISOU 7782 O3 SO4 B 303 3993 3964 3979 13 5 -8 O HETATM 7783 O4 SO4 B 303 -8.058 30.835 -22.771 1.00 31.44 O ANISOU 7783 O4 SO4 B 303 4007 3931 4008 -4 4 4 O HETATM 7784 S SO4 B 304 -20.268 37.347 -8.331 1.00 33.27 S ANISOU 7784 S SO4 B 304 4280 4174 4187 -15 3 9 S HETATM 7785 O1 SO4 B 304 -20.729 38.236 -7.212 1.00 34.10 O ANISOU 7785 O1 SO4 B 304 4351 4300 4304 13 47 -25 O HETATM 7786 O2 SO4 B 304 -19.219 38.069 -9.130 1.00 33.65 O ANISOU 7786 O2 SO4 B 304 4281 4247 4258 -16 18 8 O HETATM 7787 O3 SO4 B 304 -19.633 36.125 -7.758 1.00 33.64 O ANISOU 7787 O3 SO4 B 304 4301 4213 4268 5 -1 5 O HETATM 7788 O4 SO4 B 304 -21.430 36.990 -9.192 1.00 34.06 O ANISOU 7788 O4 SO4 B 304 4314 4306 4320 -19 -13 6 O HETATM 7789 S SO4 B 305 -12.336 9.666 4.188 1.00 42.87 S ANISOU 7789 S SO4 B 305 5438 5419 5430 -13 -10 10 S HETATM 7790 O1 SO4 B 305 -13.113 10.793 3.584 1.00 43.04 O ANISOU 7790 O1 SO4 B 305 5458 5412 5481 -3 -1 1 O HETATM 7791 O2 SO4 B 305 -10.872 9.898 3.930 1.00 42.79 O ANISOU 7791 O2 SO4 B 305 5436 5405 5416 2 11 3 O HETATM 7792 O3 SO4 B 305 -12.583 9.613 5.668 1.00 42.53 O ANISOU 7792 O3 SO4 B 305 5379 5365 5413 -3 5 -10 O HETATM 7793 O4 SO4 B 305 -12.740 8.366 3.560 1.00 42.79 O ANISOU 7793 O4 SO4 B 305 5436 5414 5409 -9 -5 8 O HETATM 7794 C1 EDO B 306 -33.288 29.761 -4.478 1.00 22.87 C ANISOU 7794 C1 EDO B 306 2905 2892 2894 -9 -16 2 C HETATM 7795 O1 EDO B 306 -33.045 30.256 -5.907 1.00 22.38 O ANISOU 7795 O1 EDO B 306 2829 2783 2890 -20 19 3 O HETATM 7796 C2 EDO B 306 -33.684 30.862 -3.478 1.00 23.21 C ANISOU 7796 C2 EDO B 306 2952 2922 2946 -1 -1 -16 C HETATM 7797 O2 EDO B 306 -35.056 31.465 -3.937 1.00 23.63 O ANISOU 7797 O2 EDO B 306 2978 3010 2991 14 -1 6 O HETATM 7798 C1 EDO B 307 -29.108 17.168 5.390 1.00 35.54 C ANISOU 7798 C1 EDO B 307 4519 4472 4513 3 7 -2 C HETATM 7799 O1 EDO B 307 -28.135 16.065 5.840 1.00 35.85 O ANISOU 7799 O1 EDO B 307 4575 4490 4558 27 7 1 O HETATM 7800 C2 EDO B 307 -29.073 18.430 6.277 1.00 35.29 C ANISOU 7800 C2 EDO B 307 4492 4457 4462 -2 16 13 C HETATM 7801 O2 EDO B 307 -27.641 18.510 6.910 1.00 35.62 O ANISOU 7801 O2 EDO B 307 4524 4526 4483 -13 8 3 O HETATM 7802 C1 EDO B 308 -19.336 -2.365 -27.326 1.00 35.26 C ANISOU 7802 C1 EDO B 308 4478 4435 4485 5 0 16 C HETATM 7803 O1 EDO B 308 -18.195 -1.406 -26.961 1.00 35.40 O ANISOU 7803 O1 EDO B 308 4513 4444 4495 -2 -15 10 O HETATM 7804 C2 EDO B 308 -20.346 -2.608 -26.191 1.00 35.23 C ANISOU 7804 C2 EDO B 308 4485 4431 4468 8 0 7 C HETATM 7805 O2 EDO B 308 -20.564 -1.253 -25.436 1.00 35.18 O ANISOU 7805 O2 EDO B 308 4490 4406 4470 -21 -15 14 O HETATM 7806 C1 EDO B 309 -16.900 21.142 0.451 1.00 24.30 C ANISOU 7806 C1 EDO B 309 3082 3062 3090 0 16 -8 C HETATM 7807 O1 EDO B 309 -15.601 20.540 1.004 1.00 24.63 O ANISOU 7807 O1 EDO B 309 3114 3100 3144 16 -7 3 O HETATM 7808 C2 EDO B 309 -18.108 21.033 1.403 1.00 24.01 C ANISOU 7808 C2 EDO B 309 3053 3020 3051 15 -3 -8 C HETATM 7809 O2 EDO B 309 -17.894 22.046 2.579 1.00 23.66 O ANISOU 7809 O2 EDO B 309 2984 2987 3018 -9 1 12 O HETATM 7810 C1 EDO B 310 -30.010 35.280 -13.550 1.00 29.08 C ANISOU 7810 C1 EDO B 310 3704 3654 3688 10 4 16 C HETATM 7811 O1 EDO B 310 -30.721 35.087 -12.202 1.00 29.04 O ANISOU 7811 O1 EDO B 310 3692 3667 3675 22 -7 9 O HETATM 7812 C2 EDO B 310 -30.102 34.102 -14.530 1.00 29.07 C ANISOU 7812 C2 EDO B 310 3713 3649 3684 3 10 19 C HETATM 7813 O2 EDO B 310 -31.596 33.837 -14.888 1.00 29.12 O ANISOU 7813 O2 EDO B 310 3723 3656 3684 12 -14 25 O HETATM 7814 C1 EDO B 311 -37.367 14.605 -24.107 1.00 36.98 C ANISOU 7814 C1 EDO B 311 4684 4668 4697 -4 1 -4 C HETATM 7815 O1 EDO B 311 -37.416 13.117 -24.484 1.00 37.16 O ANISOU 7815 O1 EDO B 311 4710 4679 4728 21 5 -1 O HETATM 7816 C2 EDO B 311 -38.333 15.026 -22.983 1.00 36.92 C ANISOU 7816 C2 EDO B 311 4689 4658 4682 -8 -2 -6 C HETATM 7817 O2 EDO B 311 -37.537 15.917 -21.966 1.00 36.79 O ANISOU 7817 O2 EDO B 311 4680 4643 4654 8 -8 4 O HETATM 7818 AU AUC C 301 -6.677 26.695 62.756 1.00 17.05 AU ANISOU 7818 AU AUC C 301 2627 2176 1674 109 -342 -157 AU HETATM 7819 C1 AUC C 301 -5.602 25.458 62.214 1.00 17.35 C ANISOU 7819 C1 AUC C 301 2373 2229 1990 50 -89 -26 C HETATM 7820 N1 AUC C 301 -4.960 24.504 62.092 1.00 17.17 N ANISOU 7820 N1 AUC C 301 2384 2218 1923 48 -106 -57 N HETATM 7821 C2 AUC C 301 -7.667 27.894 63.516 1.00 16.72 C ANISOU 7821 C2 AUC C 301 2297 2169 1888 25 -102 -24 C HETATM 7822 N2 AUC C 301 -8.474 28.697 63.723 1.00 16.33 N ANISOU 7822 N2 AUC C 301 2245 2162 1800 24 -161 -6 N HETATM 7823 AU AUC C 302 -8.180 27.373 60.039 1.00 14.96 AU ANISOU 7823 AU AUC C 302 2400 1866 1417 -1 -271 -199 AU HETATM 7824 C1 AUC C 302 -9.319 26.415 60.915 1.00 15.42 C ANISOU 7824 C1 AUC C 302 2128 1954 1776 38 -92 -137 C HETATM 7825 N1 AUC C 302 -10.270 25.835 61.244 1.00 15.35 N ANISOU 7825 N1 AUC C 302 2122 1952 1758 19 -142 -128 N HETATM 7826 C2 AUC C 302 -7.138 28.450 59.188 1.00 14.56 C ANISOU 7826 C2 AUC C 302 2020 1885 1628 54 -139 -165 C HETATM 7827 N2 AUC C 302 -6.302 29.158 58.824 1.00 14.96 N ANISOU 7827 N2 AUC C 302 2062 1921 1702 30 -140 -137 N HETATM 7828 AU AUC C 303 -10.688 45.370 56.217 1.00 28.90 AU ANISOU 7828 AU AUC C 303 4167 3349 3465 18 -171 -220 AU HETATM 7829 C1 AUC C 303 -11.443 44.579 57.549 1.00 28.48 C ANISOU 7829 C1 AUC C 303 3760 3465 3599 15 -90 -122 C HETATM 7830 N1 AUC C 303 -12.008 44.143 58.443 1.00 28.38 N ANISOU 7830 N1 AUC C 303 3761 3434 3587 24 -104 -135 N HETATM 7831 C2 AUC C 303 -9.820 46.239 55.006 1.00 28.80 C ANISOU 7831 C2 AUC C 303 3818 3518 3606 25 -93 -115 C HETATM 7832 N2 AUC C 303 -9.390 46.766 54.085 1.00 28.87 N ANISOU 7832 N2 AUC C 303 3820 3523 3626 16 -93 -106 N HETATM 7833 S SO4 C 304 -9.663 19.249 60.051 1.00 30.77 S ANISOU 7833 S SO4 C 304 3944 3833 3915 9 -29 -2 S HETATM 7834 O1 SO4 C 304 -8.237 18.940 59.712 1.00 31.47 O ANISOU 7834 O1 SO4 C 304 3977 3961 4021 -2 0 -2 O HETATM 7835 O2 SO4 C 304 -10.376 19.637 58.797 1.00 30.45 O ANISOU 7835 O2 SO4 C 304 3921 3785 3866 14 3 -26 O HETATM 7836 O3 SO4 C 304 -10.324 18.043 60.650 1.00 30.91 O ANISOU 7836 O3 SO4 C 304 3959 3897 3888 -15 -16 3 O HETATM 7837 O4 SO4 C 304 -9.718 20.381 61.033 1.00 30.93 O ANISOU 7837 O4 SO4 C 304 3960 3892 3899 8 -2 -12 O HETATM 7838 S SO4 C 305 6.105 35.752 40.103 1.00 43.35 S ANISOU 7838 S SO4 C 305 5505 5467 5499 3 6 -2 S HETATM 7839 O1 SO4 C 305 7.305 35.768 41.003 1.00 43.30 O ANISOU 7839 O1 SO4 C 305 5501 5459 5490 -4 9 6 O HETATM 7840 O2 SO4 C 305 5.096 36.742 40.612 1.00 43.37 O ANISOU 7840 O2 SO4 C 305 5514 5456 5506 9 6 13 O HETATM 7841 O3 SO4 C 305 6.520 36.137 38.714 1.00 43.39 O ANISOU 7841 O3 SO4 C 305 5520 5457 5510 2 7 10 O HETATM 7842 O4 SO4 C 305 5.503 34.382 40.087 1.00 43.16 O ANISOU 7842 O4 SO4 C 305 5473 5450 5474 12 2 1 O HETATM 7843 C1 EDO C 306 -7.420 8.456 46.116 1.00 23.70 C ANISOU 7843 C1 EDO C 306 3009 2998 2996 -20 10 6 C HETATM 7844 O1 EDO C 306 -7.999 9.766 45.550 1.00 24.08 O ANISOU 7844 O1 EDO C 306 3068 2988 3095 -43 29 18 O HETATM 7845 C2 EDO C 306 -7.917 8.147 47.546 1.00 23.40 C ANISOU 7845 C2 EDO C 306 2994 2935 2962 -5 -5 -24 C HETATM 7846 O2 EDO C 306 -7.973 9.504 48.325 1.00 22.21 O ANISOU 7846 O2 EDO C 306 2798 2834 2806 -29 -31 24 O HETATM 7847 C1 EDO C 307 -27.313 15.578 49.344 1.00 28.76 C ANISOU 7847 C1 EDO C 307 3647 3624 3658 -4 4 0 C HETATM 7848 O1 EDO C 307 -27.813 16.081 50.701 1.00 28.79 O ANISOU 7848 O1 EDO C 307 3658 3638 3644 -15 -5 -1 O HETATM 7849 C2 EDO C 307 -28.061 14.372 48.761 1.00 28.57 C ANISOU 7849 C2 EDO C 307 3637 3608 3610 8 -4 3 C HETATM 7850 O2 EDO C 307 -29.556 14.409 49.206 1.00 28.22 O ANISOU 7850 O2 EDO C 307 3620 3568 3533 -12 -9 -2 O HETATM 7851 C1 EDO C 308 -11.444 42.378 61.434 1.00 33.77 C ANISOU 7851 C1 EDO C 308 4309 4247 4275 10 -15 -4 C HETATM 7852 O1 EDO C 308 -12.652 43.286 61.140 1.00 33.94 O ANISOU 7852 O1 EDO C 308 4321 4269 4306 29 3 -13 O HETATM 7853 C2 EDO C 308 -11.834 40.900 61.569 1.00 33.59 C ANISOU 7853 C2 EDO C 308 4290 4241 4232 10 -22 -4 C HETATM 7854 O2 EDO C 308 -13.219 40.818 62.288 1.00 34.10 O ANISOU 7854 O2 EDO C 308 4317 4326 4314 -18 -20 9 O HETATM 7855 AU AUC D 301 2.290 -0.162 9.920 1.00 14.64 AU ANISOU 7855 AU AUC D 301 2123 1964 1477 47 -84 316 AU HETATM 7856 C1 AUC D 301 1.394 -1.255 8.935 1.00 14.14 C ANISOU 7856 C1 AUC D 301 1941 1822 1608 13 43 189 C HETATM 7857 N1 AUC D 301 0.670 -1.939 8.360 1.00 14.37 N ANISOU 7857 N1 AUC D 301 1895 1879 1687 31 30 147 N HETATM 7858 C2 AUC D 301 3.207 0.795 11.024 1.00 14.52 C ANISOU 7858 C2 AUC D 301 1993 1824 1699 -16 8 170 C HETATM 7859 N2 AUC D 301 4.058 1.352 11.581 1.00 15.10 N ANISOU 7859 N2 AUC D 301 2026 1962 1749 0 -17 111 N HETATM 7860 AU AUC D 302 0.346 0.494 12.350 1.00 16.22 AU ANISOU 7860 AU AUC D 302 2226 2290 1647 108 -27 308 AU HETATM 7861 C1 AUC D 302 1.150 -0.762 13.234 1.00 15.44 C ANISOU 7861 C1 AUC D 302 2095 2009 1764 57 -11 96 C HETATM 7862 N1 AUC D 302 1.890 -1.596 13.544 1.00 15.29 N ANISOU 7862 N1 AUC D 302 2025 2024 1760 44 34 81 N HETATM 7863 C2 AUC D 302 -0.563 1.787 11.649 1.00 16.12 C ANISOU 7863 C2 AUC D 302 2144 2082 1901 70 -36 108 C HETATM 7864 N2 AUC D 302 -1.224 2.726 11.490 1.00 16.06 N ANISOU 7864 N2 AUC D 302 2115 2103 1885 71 2 101 N HETATM 7865 AU AUC D 303 5.769 -18.084 6.627 1.00 34.64 AU ANISOU 7865 AU AUC D 303 4772 3951 4440 39 0 282 AU HETATM 7866 C1 AUC D 303 6.410 -17.347 8.046 1.00 34.04 C ANISOU 7866 C1 AUC D 303 4435 4097 4402 28 45 157 C HETATM 7867 N1 AUC D 303 6.940 -16.870 8.941 1.00 34.16 N ANISOU 7867 N1 AUC D 303 4455 4109 4413 28 51 154 N HETATM 7868 C2 AUC D 303 5.152 -18.993 5.297 1.00 34.77 C ANISOU 7868 C2 AUC D 303 4531 4227 4452 28 22 113 C HETATM 7869 N2 AUC D 303 4.877 -19.566 4.344 1.00 34.78 N ANISOU 7869 N2 AUC D 303 4524 4225 4464 28 19 111 N HETATM 7870 S SO4 D 304 3.722 8.078 10.379 1.00 27.46 S ANISOU 7870 S SO4 D 304 3513 3424 3498 43 2 2 S HETATM 7871 O1 SO4 D 304 4.517 7.820 9.144 1.00 27.27 O ANISOU 7871 O1 SO4 D 304 3524 3379 3459 25 -4 41 O HETATM 7872 O2 SO4 D 304 2.289 8.310 10.006 1.00 28.22 O ANISOU 7872 O2 SO4 D 304 3550 3557 3616 0 -39 18 O HETATM 7873 O3 SO4 D 304 3.805 6.894 11.295 1.00 27.76 O ANISOU 7873 O3 SO4 D 304 3573 3485 3489 14 -10 19 O HETATM 7874 O4 SO4 D 304 4.259 9.295 11.071 1.00 27.50 O ANISOU 7874 O4 SO4 D 304 3493 3450 3505 13 -17 16 O HETATM 7875 S SO4 D 305 -7.976 -8.654 -12.382 1.00 49.77 S ANISOU 7875 S SO4 D 305 6318 6275 6319 -3 -7 5 S HETATM 7876 O1 SO4 D 305 -6.925 -9.631 -11.944 1.00 49.81 O ANISOU 7876 O1 SO4 D 305 6323 6270 6332 2 -5 -9 O HETATM 7877 O2 SO4 D 305 -7.447 -7.257 -12.259 1.00 49.81 O ANISOU 7877 O2 SO4 D 305 6331 6275 6321 -1 -6 3 O HETATM 7878 O3 SO4 D 305 -8.339 -8.930 -13.812 1.00 49.87 O ANISOU 7878 O3 SO4 D 305 6328 6293 6326 -2 -4 -4 O HETATM 7879 O4 SO4 D 305 -9.193 -8.806 -11.519 1.00 49.77 O ANISOU 7879 O4 SO4 D 305 6329 6272 6310 -2 -3 -3 O HETATM 7880 S SO4 D 306 20.326 2.520 21.797 1.00 49.48 S ANISOU 7880 S SO4 D 306 6294 6232 6274 9 1 -2 S HETATM 7881 O1 SO4 D 306 20.911 1.159 22.038 1.00 49.59 O ANISOU 7881 O1 SO4 D 306 6311 6239 6291 9 6 1 O HETATM 7882 O2 SO4 D 306 20.067 3.185 23.117 1.00 49.54 O ANISOU 7882 O2 SO4 D 306 6310 6243 6272 10 -3 3 O HETATM 7883 O3 SO4 D 306 21.293 3.348 21.004 1.00 49.38 O ANISOU 7883 O3 SO4 D 306 6285 6215 6260 13 -1 -6 O HETATM 7884 O4 SO4 D 306 19.035 2.381 21.048 1.00 49.58 O ANISOU 7884 O4 SO4 D 306 6297 6251 6291 3 -1 -3 O HETATM 7885 C1 EDO D 307 -2.668 14.427 -14.381 1.00 27.72 C ANISOU 7885 C1 EDO D 307 3496 3493 3542 -1 -8 7 C HETATM 7886 O1 EDO D 307 -2.498 15.832 -14.968 1.00 26.70 O ANISOU 7886 O1 EDO D 307 3354 3421 3368 4 -19 -35 O HETATM 7887 C2 EDO D 307 -2.880 14.398 -12.859 1.00 28.23 C ANISOU 7887 C2 EDO D 307 3578 3582 3568 -3 -8 -4 C HETATM 7888 O2 EDO D 307 -4.358 14.842 -12.576 1.00 28.66 O ANISOU 7888 O2 EDO D 307 3588 3655 3645 -12 -2 -3 O HETATM 7889 O HOH A 401 20.030 9.732 33.258 1.00 47.84 O ANISOU 7889 O HOH A 401 6055 6034 6088 -2 -15 2 O HETATM 7890 O HOH A 402 23.339 23.678 24.051 1.00 19.56 O ANISOU 7890 O HOH A 402 2569 2474 2389 -2 -21 -7 O HETATM 7891 O HOH A 403 3.810 17.989 33.487 1.00 23.33 O ANISOU 7891 O HOH A 403 3026 2902 2936 26 -22 -29 O HETATM 7892 O HOH A 404 11.090 15.072 51.989 1.00 26.26 O ANISOU 7892 O HOH A 404 3356 3375 3246 -27 -45 11 O HETATM 7893 O HOH A 405 23.402 9.473 20.278 1.00 34.57 O ANISOU 7893 O HOH A 405 4354 4387 4395 18 -2 -15 O HETATM 7894 O HOH A 406 3.533 1.740 16.668 1.00 19.40 O ANISOU 7894 O HOH A 406 2418 2498 2456 -16 -43 -23 O HETATM 7895 O HOH A 407 15.896 -10.227 50.236 1.00 18.54 O ANISOU 7895 O HOH A 407 2360 2317 2366 -79 -27 12 O HETATM 7896 O HOH A 408 6.486 17.846 63.066 1.00 18.68 O ANISOU 7896 O HOH A 408 2418 2379 2299 29 -59 -59 O HETATM 7897 O HOH A 409 29.453 -9.499 39.686 1.00 28.50 O ANISOU 7897 O HOH A 409 3604 3604 3620 10 1 -17 O HETATM 7898 O HOH A 410 36.261 9.291 43.586 1.00 18.30 O ANISOU 7898 O HOH A 410 2344 2374 2235 -57 10 -34 O HETATM 7899 O HOH A 411 14.564 3.495 33.122 1.00 23.38 O ANISOU 7899 O HOH A 411 2975 2995 2912 -4 -11 -10 O HETATM 7900 O HOH A 412 32.306 12.568 45.905 1.00 21.59 O ANISOU 7900 O HOH A 412 2750 2768 2686 -46 -48 -13 O HETATM 7901 O HOH A 413 30.457 -6.528 42.957 1.00 23.49 O ANISOU 7901 O HOH A 413 3003 2908 3013 11 -10 -43 O HETATM 7902 O HOH A 414 30.862 12.472 42.255 1.00 16.27 O ANISOU 7902 O HOH A 414 2139 2039 2005 -42 3 7 O HETATM 7903 O HOH A 415 3.540 2.275 35.599 1.00 27.11 O ANISOU 7903 O HOH A 415 3444 3465 3390 18 -11 -19 O HETATM 7904 O HOH A 416 10.648 5.898 54.021 1.00 26.76 O ANISOU 7904 O HOH A 416 3461 3338 3370 11 3 33 O HETATM 7905 O HOH A 417 -2.547 13.888 27.280 1.00 22.18 O ANISOU 7905 O HOH A 417 2828 2854 2744 24 8 -3 O HETATM 7906 O HOH A 418 9.408 6.245 48.590 1.00 25.76 O ANISOU 7906 O HOH A 418 3240 3297 3251 12 -10 47 O HETATM 7907 O HOH A 419 1.070 -0.068 24.452 1.00 33.34 O ANISOU 7907 O HOH A 419 4238 4169 4260 -5 15 -22 O HETATM 7908 O HOH A 420 25.720 21.214 45.115 1.00 26.28 O ANISOU 7908 O HOH A 420 3322 3304 3361 -10 2 -24 O HETATM 7909 O HOH A 421 31.904 17.950 40.423 1.00 32.68 O ANISOU 7909 O HOH A 421 4166 4085 4165 4 -8 -8 O HETATM 7910 O HOH A 422 9.520 7.548 19.192 1.00 22.53 O ANISOU 7910 O HOH A 422 2898 2895 2766 -37 27 26 O HETATM 7911 O HOH A 423 21.044 12.970 40.299 1.00 13.06 O ANISOU 7911 O HOH A 423 1628 1721 1612 -117 -56 -24 O HETATM 7912 O HOH A 424 25.221 20.766 49.250 1.00 25.67 O ANISOU 7912 O HOH A 424 3269 3239 3246 -30 -59 -24 O HETATM 7913 O HOH A 425 7.973 33.133 41.859 1.00 21.26 O ANISOU 7913 O HOH A 425 2676 2666 2736 -17 -28 6 O HETATM 7914 O HOH A 426 25.420 0.819 30.809 1.00 39.13 O ANISOU 7914 O HOH A 426 5000 4912 4957 0 7 10 O HETATM 7915 O HOH A 427 -2.115 13.615 23.275 1.00 35.20 O ANISOU 7915 O HOH A 427 4480 4482 4413 12 -27 3 O HETATM 7916 O HOH A 428 6.906 11.896 24.738 1.00 18.65 O ANISOU 7916 O HOH A 428 2385 2394 2307 27 -58 -19 O HETATM 7917 O HOH A 429 -1.135 10.423 22.651 1.00 33.26 O ANISOU 7917 O HOH A 429 4268 4197 4171 12 -16 -18 O HETATM 7918 O HOH A 430 7.805 6.754 21.380 1.00 26.52 O ANISOU 7918 O HOH A 430 3352 3343 3379 37 7 -14 O HETATM 7919 O HOH A 431 30.888 -1.880 49.529 1.00 27.89 O ANISOU 7919 O HOH A 431 3525 3501 3572 -14 -16 8 O HETATM 7920 O HOH A 432 10.961 9.282 41.474 1.00 31.51 O ANISOU 7920 O HOH A 432 3948 4065 3961 -10 -34 -5 O HETATM 7921 O HOH A 433 9.901 3.488 55.893 1.00 29.44 O ANISOU 7921 O HOH A 433 3716 3748 3723 -10 6 8 O HETATM 7922 O HOH A 434 26.585 -6.306 44.579 1.00 24.75 O ANISOU 7922 O HOH A 434 3204 3110 3089 -24 -37 -23 O HETATM 7923 O HOH A 435 29.350 6.146 45.600 1.00 14.36 O ANISOU 7923 O HOH A 435 1855 1899 1703 -16 -29 -22 O HETATM 7924 O HOH A 436 6.640 33.262 37.519 1.00 36.51 O ANISOU 7924 O HOH A 436 4654 4593 4624 -17 9 11 O HETATM 7925 O HOH A 437 12.855 -2.722 58.926 1.00 40.56 O ANISOU 7925 O HOH A 437 5121 5115 5174 -4 5 -1 O HETATM 7926 O HOH A 438 21.561 18.029 20.501 1.00 24.12 O ANISOU 7926 O HOH A 438 3072 3096 2998 4 33 -3 O HETATM 7927 O HOH A 439 31.455 15.352 45.726 1.00 28.91 O ANISOU 7927 O HOH A 439 3644 3671 3669 -4 -11 -38 O HETATM 7928 O HOH A 440 8.078 11.358 17.898 1.00 25.48 O ANISOU 7928 O HOH A 440 3244 3177 3259 3 15 -12 O HETATM 7929 O HOH A 441 35.396 8.652 38.094 1.00 51.26 O ANISOU 7929 O HOH A 441 6491 6483 6503 -13 -1 5 O HETATM 7930 O HOH A 442 29.162 18.692 45.039 1.00 22.31 O ANISOU 7930 O HOH A 442 2875 2795 2807 -42 -13 -12 O HETATM 7931 O HOH A 443 4.310 22.318 44.138 1.00 18.30 O ANISOU 7931 O HOH A 443 2422 2216 2314 -25 15 -36 O HETATM 7932 O HOH A 444 2.085 18.660 24.830 1.00 40.99 O ANISOU 7932 O HOH A 444 5244 5140 5189 -1 -3 -4 O HETATM 7933 O HOH A 445 2.358 23.479 29.799 1.00 33.36 O ANISOU 7933 O HOH A 445 4274 4147 4253 9 -1 -1 O HETATM 7934 O HOH A 446 -0.217 1.893 25.729 1.00 28.77 O ANISOU 7934 O HOH A 446 3694 3547 3691 -11 12 -36 O HETATM 7935 O HOH A 447 7.879 19.339 53.431 1.00 26.04 O ANISOU 7935 O HOH A 447 3294 3316 3283 -18 -51 -60 O HETATM 7936 O HOH A 448 13.885 -6.539 38.697 1.00 24.25 O ANISOU 7936 O HOH A 448 3110 3027 3078 -15 -41 -42 O HETATM 7937 O HOH A 449 11.745 2.140 63.257 1.00 43.59 O ANISOU 7937 O HOH A 449 5543 5494 5526 -1 8 10 O HETATM 7938 O HOH A 450 33.241 -0.407 42.600 1.00 24.26 O ANISOU 7938 O HOH A 450 3048 3089 3078 16 -25 -17 O HETATM 7939 O HOH A 451 5.088 8.234 43.809 1.00 21.98 O ANISOU 7939 O HOH A 451 2777 2774 2799 -16 -56 13 O HETATM 7940 O HOH A 452 32.235 16.474 28.990 1.00 26.88 O ANISOU 7940 O HOH A 452 3404 3407 3401 -2 10 5 O HETATM 7941 O HOH A 453 16.951 -11.069 47.712 1.00 51.78 O ANISOU 7941 O HOH A 453 6578 6514 6581 -7 -5 -10 O HETATM 7942 O HOH A 454 21.093 21.156 54.911 1.00 26.59 O ANISOU 7942 O HOH A 454 3443 3311 3349 -18 -24 2 O HETATM 7943 O HOH A 455 31.361 19.545 26.253 1.00 34.53 O ANISOU 7943 O HOH A 455 4373 4376 4370 -1 0 -12 O HETATM 7944 O HOH A 456 6.889 -2.106 23.325 1.00 27.93 O ANISOU 7944 O HOH A 456 3547 3498 3566 11 -14 -1 O HETATM 7945 O HOH A 457 4.036 17.324 40.634 1.00 19.76 O ANISOU 7945 O HOH A 457 2659 2472 2376 -32 -2 -2 O HETATM 7946 O HOH A 458 24.210 -11.274 41.907 1.00 31.65 O ANISOU 7946 O HOH A 458 4043 3948 4036 -25 -1 15 O HETATM 7947 O HOH A 459 5.421 10.045 26.900 1.00 14.75 O ANISOU 7947 O HOH A 459 1871 1804 1928 21 3 -40 O HETATM 7948 O HOH A 460 1.926 20.905 41.018 1.00 47.66 O ANISOU 7948 O HOH A 460 6049 5989 6071 -7 -11 1 O HETATM 7949 O HOH A 461 5.517 18.369 24.943 1.00 30.78 O ANISOU 7949 O HOH A 461 3949 3877 3870 -26 15 -9 O HETATM 7950 O HOH A 462 10.532 26.703 31.654 1.00 19.90 O ANISOU 7950 O HOH A 462 2579 2449 2532 11 -19 10 O HETATM 7951 O HOH A 463 10.164 21.443 23.232 1.00 43.26 O ANISOU 7951 O HOH A 463 5499 5444 5492 10 2 2 O HETATM 7952 O HOH A 464 17.759 30.721 42.458 1.00 39.78 O ANISOU 7952 O HOH A 464 5062 5013 5041 -1 -7 -7 O HETATM 7953 O HOH A 465 1.221 13.106 61.982 1.00 28.66 O ANISOU 7953 O HOH A 465 3657 3642 3591 -4 6 1 O HETATM 7954 O HOH A 466 6.065 19.011 39.476 1.00 21.20 O ANISOU 7954 O HOH A 466 2591 2735 2729 -4 -25 92 O HETATM 7955 O HOH A 467 17.806 0.529 32.926 1.00 44.71 O ANISOU 7955 O HOH A 467 5686 5622 5679 -4 -21 -8 O HETATM 7956 O HOH A 468 33.909 12.232 43.690 1.00 23.74 O ANISOU 7956 O HOH A 468 3002 3073 2947 -18 0 -3 O HETATM 7957 O HOH A 469 17.861 3.844 35.372 1.00 12.09 O ANISOU 7957 O HOH A 469 1588 1434 1572 20 -55 -50 O HETATM 7958 O HOH A 470 16.793 30.120 45.056 1.00 38.37 O ANISOU 7958 O HOH A 470 4889 4809 4879 -3 -4 7 O HETATM 7959 O HOH A 471 23.937 -10.198 57.803 1.00 39.59 O ANISOU 7959 O HOH A 471 5027 4995 5018 6 -18 10 O HETATM 7960 O HOH A 472 6.813 0.586 37.631 1.00 33.50 O ANISOU 7960 O HOH A 472 4287 4210 4231 -21 -10 -20 O HETATM 7961 O HOH A 473 13.348 9.992 22.405 1.00 21.23 O ANISOU 7961 O HOH A 473 2736 2741 2589 -13 -32 -20 O HETATM 7962 O HOH A 474 32.815 -1.549 55.178 1.00 40.42 O ANISOU 7962 O HOH A 474 5143 5079 5135 9 -1 11 O HETATM 7963 O HOH A 475 4.664 21.189 40.467 1.00 34.84 O ANISOU 7963 O HOH A 475 4421 4411 4407 -8 -7 25 O HETATM 7964 O HOH A 476 9.946 19.602 25.713 1.00 36.41 O ANISOU 7964 O HOH A 476 4617 4563 4655 9 7 -5 O HETATM 7965 O HOH A 477 28.988 -3.878 50.479 1.00 24.50 O ANISOU 7965 O HOH A 477 3107 3048 3152 11 -19 23 O HETATM 7966 O HOH A 478 24.301 24.924 41.502 1.00 21.75 O ANISOU 7966 O HOH A 478 2729 2726 2808 -35 2 -26 O HETATM 7967 O HOH A 479 25.941 -0.795 33.146 1.00 26.01 O ANISOU 7967 O HOH A 479 3354 3304 3225 18 2 -25 O HETATM 7968 O HOH A 480 28.921 -1.079 39.378 1.00 24.08 O ANISOU 7968 O HOH A 480 3000 3031 3120 23 -48 6 O HETATM 7969 O HOH A 481 16.900 -5.758 52.122 1.00 28.34 O ANISOU 7969 O HOH A 481 3629 3525 3615 7 -1 7 O HETATM 7970 O HOH A 482 11.246 18.148 58.174 1.00 20.46 O ANISOU 7970 O HOH A 482 2631 2613 2529 4 13 -41 O HETATM 7971 O HOH A 483 26.670 18.964 43.785 1.00 15.35 O ANISOU 7971 O HOH A 483 2021 1886 1923 -37 -91 28 O HETATM 7972 O HOH A 484 29.390 24.937 27.893 1.00 26.37 O ANISOU 7972 O HOH A 484 3344 3303 3373 -30 -32 15 O HETATM 7973 O HOH A 485 4.087 7.170 55.010 1.00 44.95 O ANISOU 7973 O HOH A 485 5691 5671 5718 -4 7 -1 O HETATM 7974 O HOH A 486 15.400 -2.266 60.151 1.00 35.53 O ANISOU 7974 O HOH A 486 4515 4484 4498 -11 -9 -5 O HETATM 7975 O HOH A 487 27.979 13.841 24.109 1.00 30.24 O ANISOU 7975 O HOH A 487 3852 3858 3781 -2 -49 -47 O HETATM 7976 O HOH A 488 11.699 30.059 36.362 1.00 20.05 O ANISOU 7976 O HOH A 488 2655 2458 2504 38 -52 26 O HETATM 7977 O HOH A 489 11.830 6.237 44.192 1.00 16.17 O ANISOU 7977 O HOH A 489 1964 2151 2028 -13 -51 -48 O HETATM 7978 O HOH A 490 31.659 -4.672 49.881 1.00 40.39 O ANISOU 7978 O HOH A 490 5119 5077 5149 10 -2 5 O HETATM 7979 O HOH A 491 36.023 14.499 34.092 1.00 36.34 O ANISOU 7979 O HOH A 491 4570 4625 4611 -6 18 30 O HETATM 7980 O HOH A 492 11.168 6.777 65.288 1.00 42.68 O ANISOU 7980 O HOH A 492 5426 5374 5418 6 3 -10 O HETATM 7981 O HOH A 493 23.089 -6.749 43.336 1.00 24.56 O ANISOU 7981 O HOH A 493 3139 3079 3115 -29 28 -55 O HETATM 7982 O HOH A 494 12.176 -2.807 47.264 1.00 16.26 O ANISOU 7982 O HOH A 494 2053 1973 2150 -58 -10 -33 O HETATM 7983 O HOH A 495 9.608 4.950 46.064 1.00 49.18 O ANISOU 7983 O HOH A 495 6232 6177 6279 -4 1 -7 O HETATM 7984 O HOH A 496 9.213 26.720 34.402 1.00 24.30 O ANISOU 7984 O HOH A 496 3172 3053 3009 37 -24 -6 O HETATM 7985 O HOH A 497 7.421 4.878 56.192 1.00 41.50 O ANISOU 7985 O HOH A 497 5274 5218 5277 -4 6 -6 O HETATM 7986 O HOH A 498 14.612 -0.559 35.240 1.00 33.62 O ANISOU 7986 O HOH A 498 4288 4227 4258 18 6 -9 O HETATM 7987 O HOH A 499 15.832 25.444 23.286 1.00 41.85 O ANISOU 7987 O HOH A 499 5317 5280 5305 3 -2 1 O HETATM 7988 O HOH A 500 10.686 3.887 37.653 1.00 43.99 O ANISOU 7988 O HOH A 500 5587 5549 5576 4 -2 9 O HETATM 7989 O HOH A 501 19.653 6.866 27.159 1.00 28.50 O ANISOU 7989 O HOH A 501 3596 3602 3631 3 3 -16 O HETATM 7990 O HOH A 502 11.386 2.990 40.423 1.00 34.11 O ANISOU 7990 O HOH A 502 4326 4316 4317 10 -4 -6 O HETATM 7991 O HOH A 503 28.673 -7.734 51.148 1.00 40.93 O ANISOU 7991 O HOH A 503 5210 5138 5203 -2 -5 2 O HETATM 7992 O HOH A 504 36.282 11.951 32.951 1.00 37.25 O ANISOU 7992 O HOH A 504 4681 4742 4729 0 5 -4 O HETATM 7993 O HOH A 505 14.782 29.522 49.647 1.00 36.21 O ANISOU 7993 O HOH A 505 4599 4593 4566 13 6 -12 O HETATM 7994 O HOH A 506 14.684 5.291 23.088 1.00 39.94 O ANISOU 7994 O HOH A 506 5081 5037 5057 -4 12 -1 O HETATM 7995 O HOH A 507 5.254 17.902 36.779 1.00 26.04 O ANISOU 7995 O HOH A 507 3377 3358 3158 61 28 6 O HETATM 7996 O HOH A 508 2.054 11.226 33.903 1.00 12.48 O ANISOU 7996 O HOH A 508 1587 1598 1558 68 -23 -91 O HETATM 7997 O HOH A 509 24.697 -2.838 31.638 1.00 32.60 O ANISOU 7997 O HOH A 509 4184 4072 4129 19 11 15 O HETATM 7998 O HOH A 510 11.631 16.719 64.542 1.00 32.07 O ANISOU 7998 O HOH A 510 4091 4022 4072 -25 -23 12 O HETATM 7999 O HOH A 511 8.668 5.985 41.797 1.00 39.63 O ANISOU 7999 O HOH A 511 5038 4976 5042 -3 -24 -8 O HETATM 8000 O HOH A 512 21.888 29.312 36.039 1.00 34.13 O ANISOU 8000 O HOH A 512 4370 4275 4321 6 -6 14 O HETATM 8001 O HOH A 513 -1.594 8.951 29.736 1.00 26.56 O ANISOU 8001 O HOH A 513 3363 3408 3319 3 -1 -44 O HETATM 8002 O HOH A 514 10.637 14.979 25.405 1.00 16.88 O ANISOU 8002 O HOH A 514 2239 2138 2035 -6 11 -34 O HETATM 8003 O HOH A 515 10.918 2.881 51.242 1.00 30.43 O ANISOU 8003 O HOH A 515 3861 3835 3867 -4 -5 5 O HETATM 8004 O HOH A 516 25.868 13.594 20.855 1.00 20.86 O ANISOU 8004 O HOH A 516 2647 2712 2568 -19 -24 -15 O HETATM 8005 O HOH A 517 35.525 7.317 41.827 1.00 25.59 O ANISOU 8005 O HOH A 517 3187 3284 3251 19 24 47 O HETATM 8006 O HOH A 518 24.130 18.620 21.389 1.00 24.82 O ANISOU 8006 O HOH A 518 3166 3182 3083 2 15 12 O HETATM 8007 O HOH A 519 1.142 18.555 35.600 1.00 27.24 O ANISOU 8007 O HOH A 519 3493 3382 3476 -31 4 13 O HETATM 8008 O HOH A 520 6.045 19.033 60.686 1.00 15.47 O ANISOU 8008 O HOH A 520 1993 1994 1889 -57 -44 -59 O HETATM 8009 O HOH A 521 1.032 2.099 28.977 1.00 27.64 O ANISOU 8009 O HOH A 521 3486 3483 3533 1 1 -15 O HETATM 8010 O HOH A 522 20.045 29.615 43.969 1.00 31.49 O ANISOU 8010 O HOH A 522 4034 3953 3977 4 -8 -17 O HETATM 8011 O HOH A 523 17.518 20.294 60.397 1.00 36.29 O ANISOU 8011 O HOH A 523 4615 4553 4623 4 10 -20 O HETATM 8012 O HOH A 524 31.870 -2.284 46.797 1.00 23.81 O ANISOU 8012 O HOH A 524 3012 2968 3067 38 -78 -14 O HETATM 8013 O HOH A 525 8.114 22.932 25.496 1.00 50.03 O ANISOU 8013 O HOH A 525 6350 6309 6350 4 5 1 O HETATM 8014 O HOH A 526 25.480 25.765 20.861 1.00 38.25 O ANISOU 8014 O HOH A 526 4866 4859 4808 -13 -13 20 O HETATM 8015 O HOH A 527 25.431 -9.597 34.251 1.00 30.19 O ANISOU 8015 O HOH A 527 3837 3816 3817 27 -13 14 O HETATM 8016 O HOH A 528 9.615 27.748 27.041 1.00 39.15 O ANISOU 8016 O HOH A 528 4973 4932 4969 9 -1 2 O HETATM 8017 O HOH A 529 -0.495 9.262 54.471 1.00 29.27 O ANISOU 8017 O HOH A 529 3760 3656 3707 -33 -22 0 O HETATM 8018 O HOH A 530 12.314 4.769 56.012 1.00 25.93 O ANISOU 8018 O HOH A 530 3240 3271 3341 -11 -44 -10 O HETATM 8019 O HOH A 531 6.507 10.399 21.417 1.00 21.70 O ANISOU 8019 O HOH A 531 2748 2833 2666 -16 9 -14 O HETATM 8020 O HOH A 532 2.296 8.062 50.527 1.00 28.59 O ANISOU 8020 O HOH A 532 3628 3597 3639 -33 -2 -31 O HETATM 8021 O HOH A 533 19.478 -10.325 34.896 1.00 28.66 O ANISOU 8021 O HOH A 533 3666 3628 3596 3 -11 -11 O HETATM 8022 O HOH A 534 27.673 27.187 40.663 1.00 41.92 O ANISOU 8022 O HOH A 534 5331 5282 5315 -6 2 2 O HETATM 8023 O HOH A 535 11.805 31.468 40.960 1.00 25.95 O ANISOU 8023 O HOH A 535 3345 3184 3332 19 -30 1 O HETATM 8024 O HOH A 536 23.421 -8.610 41.330 1.00 22.82 O ANISOU 8024 O HOH A 536 2897 2871 2904 17 -16 -8 O HETATM 8025 O HOH A 537 6.204 22.449 42.280 1.00 35.64 O ANISOU 8025 O HOH A 537 4546 4493 4502 3 -7 -5 O HETATM 8026 O HOH A 538 29.291 2.958 36.556 1.00 21.84 O ANISOU 8026 O HOH A 538 2778 2789 2731 21 -25 -16 O HETATM 8027 O HOH A 539 1.788 20.383 27.053 1.00 23.96 O ANISOU 8027 O HOH A 539 3095 2972 3038 10 -25 15 O HETATM 8028 O HOH A 540 31.375 17.406 43.217 1.00 33.60 O ANISOU 8028 O HOH A 540 4234 4218 4316 -8 -12 -1 O HETATM 8029 O HOH A 541 6.460 11.515 61.359 1.00 24.83 O ANISOU 8029 O HOH A 541 3148 3149 3135 24 -14 -6 O HETATM 8030 O HOH A 542 31.979 3.150 37.746 1.00 32.41 O ANISOU 8030 O HOH A 542 4119 4086 4110 11 -1 3 O HETATM 8031 O HOH A 543 28.997 26.864 34.227 1.00 27.80 O ANISOU 8031 O HOH A 543 3563 3489 3511 -32 -6 19 O HETATM 8032 O HOH A 544 34.500 8.288 32.889 1.00 43.46 O ANISOU 8032 O HOH A 544 5510 5487 5514 5 1 0 O HETATM 8033 O HOH A 545 5.221 16.068 23.317 1.00 22.56 O ANISOU 8033 O HOH A 545 3010 2825 2738 5 -12 16 O HETATM 8034 O HOH A 546 35.950 10.012 35.587 1.00 33.10 O ANISOU 8034 O HOH A 546 4173 4193 4210 -8 3 0 O HETATM 8035 O HOH A 547 4.309 -0.811 21.020 1.00 37.83 O ANISOU 8035 O HOH A 547 4841 4749 4783 -8 2 -2 O HETATM 8036 O HOH A 548 9.596 1.752 34.763 1.00 41.84 O ANISOU 8036 O HOH A 548 5336 5256 5304 -6 9 -3 O HETATM 8037 O HOH A 549 11.444 17.564 24.779 1.00 30.38 O ANISOU 8037 O HOH A 549 3890 3846 3806 -11 12 5 O HETATM 8038 O HOH A 550 9.324 9.367 21.746 1.00 32.49 O ANISOU 8038 O HOH A 550 4150 4095 4100 -11 9 -20 O HETATM 8039 O HOH A 551 2.445 11.839 59.795 1.00 16.69 O ANISOU 8039 O HOH A 551 2237 2078 2026 -9 -36 56 O HETATM 8040 O HOH A 552 12.269 28.942 33.635 1.00 25.38 O ANISOU 8040 O HOH A 552 3299 3127 3216 -1 -20 14 O HETATM 8041 O HOH A 553 2.864 16.642 36.634 1.00 31.87 O ANISOU 8041 O HOH A 553 4158 3980 3973 18 -17 -25 O HETATM 8042 O HOH A 554 25.345 6.325 62.179 1.00 41.65 O ANISOU 8042 O HOH A 554 5310 5252 5262 -6 3 -6 O HETATM 8043 O HOH A 555 12.183 3.558 24.545 1.00 13.70 O ANISOU 8043 O HOH A 555 1762 1687 1757 -8 -35 -79 O HETATM 8044 O HOH A 556 36.032 1.548 53.455 1.00 40.01 O ANISOU 8044 O HOH A 556 5071 5058 5073 -2 -13 2 O HETATM 8045 O HOH A 557 4.682 29.097 31.381 1.00 36.55 O ANISOU 8045 O HOH A 557 4639 4590 4656 9 -3 20 O HETATM 8046 O HOH A 558 17.458 3.307 32.303 1.00 23.88 O ANISOU 8046 O HOH A 558 3018 3086 2971 -19 -37 -1 O HETATM 8047 O HOH A 559 11.407 19.095 50.136 1.00 43.92 O ANISOU 8047 O HOH A 559 5577 5529 5583 -12 7 -23 O HETATM 8048 O HOH A 560 21.206 -4.959 31.116 1.00 38.47 O ANISOU 8048 O HOH A 560 4917 4821 4879 -3 -11 -5 O HETATM 8049 O HOH A 561 18.350 29.453 48.336 1.00 35.01 O ANISOU 8049 O HOH A 561 4455 4392 4456 -4 -10 -11 O HETATM 8050 O HOH A 562 34.729 6.491 61.033 1.00 40.80 O ANISOU 8050 O HOH A 562 5193 5142 5168 -6 -21 9 O HETATM 8051 O HOH A 563 12.216 6.916 40.705 1.00 31.63 O ANISOU 8051 O HOH A 563 3998 3952 4069 -23 -14 17 O HETATM 8052 O HOH A 564 25.467 27.869 27.464 1.00 31.78 O ANISOU 8052 O HOH A 564 4051 4045 3980 -18 -18 10 O HETATM 8053 O HOH A 565 7.818 -3.747 28.666 1.00 42.61 O ANISOU 8053 O HOH A 565 5411 5340 5438 -20 -27 20 O HETATM 8054 O HOH A 566 16.376 -9.730 45.421 1.00 32.00 O ANISOU 8054 O HOH A 566 4091 4009 4058 -16 8 15 O HETATM 8055 O HOH A 567 22.684 16.912 62.531 1.00 41.51 O ANISOU 8055 O HOH A 567 5258 5250 5263 -18 -17 4 O HETATM 8056 O HOH A 568 5.316 5.844 45.178 1.00 32.28 O ANISOU 8056 O HOH A 568 4097 4073 4096 -3 -26 3 O HETATM 8057 O HOH A 569 32.400 22.667 38.897 1.00 44.31 O ANISOU 8057 O HOH A 569 5630 5573 5633 -8 -5 -1 O HETATM 8058 O HOH A 570 32.293 -2.373 40.792 1.00 43.88 O ANISOU 8058 O HOH A 570 5558 5516 5596 -6 10 -1 O HETATM 8059 O HOH A 571 36.013 0.475 42.510 1.00 48.60 O ANISOU 8059 O HOH A 571 6158 6132 6177 -6 0 0 O HETATM 8060 O HOH A 572 31.153 12.167 22.684 1.00 44.50 O ANISOU 8060 O HOH A 572 5672 5620 5617 -4 -6 12 O HETATM 8061 O HOH A 573 10.032 24.492 24.142 1.00 46.87 O ANISOU 8061 O HOH A 573 5966 5899 5945 -4 0 -9 O HETATM 8062 O HOH A 574 23.816 23.473 49.602 1.00 31.94 O ANISOU 8062 O HOH A 574 4051 3997 4087 -14 -8 -3 O HETATM 8063 O HOH A 575 22.838 -13.758 41.648 1.00 33.71 O ANISOU 8063 O HOH A 575 4259 4265 4286 5 1 -3 O HETATM 8064 O HOH A 576 1.101 0.936 32.548 1.00 42.04 O ANISOU 8064 O HOH A 576 5337 5294 5340 3 -13 -7 O HETATM 8065 O HOH A 577 23.686 10.250 60.044 1.00 48.03 O ANISOU 8065 O HOH A 577 6099 6067 6085 9 -6 -1 O HETATM 8066 O HOH A 578 33.110 17.773 47.872 1.00 48.78 O ANISOU 8066 O HOH A 578 6207 6142 6184 1 3 0 O HETATM 8067 O HOH A 579 20.408 23.012 21.101 1.00 45.70 O ANISOU 8067 O HOH A 579 5815 5783 5765 -2 -7 5 O HETATM 8068 O HOH A 580 24.223 31.372 31.752 1.00 40.86 O ANISOU 8068 O HOH A 580 5191 5133 5201 1 5 8 O HETATM 8069 O HOH A 581 28.895 0.716 64.606 1.00 41.17 O ANISOU 8069 O HOH A 581 5235 5198 5210 -1 -5 3 O HETATM 8070 O HOH A 582 15.261 32.501 41.634 1.00 28.81 O ANISOU 8070 O HOH A 582 3675 3618 3652 26 -10 -52 O HETATM 8071 O HOH A 583 34.301 18.731 32.410 1.00 50.27 O ANISOU 8071 O HOH A 583 6370 6338 6391 -6 2 7 O HETATM 8072 O HOH A 584 18.118 -13.969 47.962 1.00 45.05 O ANISOU 8072 O HOH A 584 5722 5661 5735 11 2 -5 O HETATM 8073 O HOH A 585 28.309 5.971 62.555 1.00 40.86 O ANISOU 8073 O HOH A 585 5194 5148 5184 4 -20 -10 O HETATM 8074 O HOH A 586 34.646 3.779 40.399 1.00 37.06 O ANISOU 8074 O HOH A 586 4724 4638 4720 -1 10 3 O HETATM 8075 O HOH A 587 30.524 24.855 30.450 1.00 26.21 O ANISOU 8075 O HOH A 587 3296 3323 3341 -25 -1 18 O HETATM 8076 O HOH A 588 6.539 -3.205 30.947 1.00 24.74 O ANISOU 8076 O HOH A 588 3211 3164 3025 15 -6 18 O HETATM 8077 O HOH A 589 9.073 2.941 53.276 1.00 33.02 O ANISOU 8077 O HOH A 589 4168 4173 4205 12 -8 3 O HETATM 8078 O HOH A 590 24.789 24.107 52.430 1.00 44.65 O ANISOU 8078 O HOH A 590 5667 5620 5676 -20 -11 -8 O HETATM 8079 O HOH A 591 13.582 26.741 24.328 1.00 48.81 O ANISOU 8079 O HOH A 591 6196 6159 6190 0 4 11 O HETATM 8080 O HOH A 592 20.074 27.603 53.458 1.00 34.99 O ANISOU 8080 O HOH A 592 4463 4380 4451 1 3 -3 O HETATM 8081 O HOH A 593 5.339 23.239 25.414 1.00 47.19 O ANISOU 8081 O HOH A 593 6000 5947 5984 0 -4 2 O HETATM 8082 O HOH A 594 11.571 -0.210 21.612 1.00 35.26 O ANISOU 8082 O HOH A 594 4493 4457 4448 10 13 -31 O HETATM 8083 O HOH A 595 16.426 -4.882 59.611 1.00 38.07 O ANISOU 8083 O HOH A 595 4840 4805 4818 -4 3 11 O HETATM 8084 O HOH A 596 23.371 26.301 22.966 1.00 30.52 O ANISOU 8084 O HOH A 596 3899 3834 3864 -23 -8 12 O HETATM 8085 O HOH A 597 34.665 16.432 30.541 1.00 42.04 O ANISOU 8085 O HOH A 597 5311 5320 5345 -9 9 -1 O HETATM 8086 O HOH A 598 30.482 27.179 31.871 1.00 32.67 O ANISOU 8086 O HOH A 598 4165 4101 4147 -15 22 6 O HETATM 8087 O HOH A 599 22.867 8.002 61.481 1.00 26.65 O ANISOU 8087 O HOH A 599 3433 3354 3339 -1 -42 -5 O HETATM 8088 O HOH A 600 4.901 20.946 23.853 1.00 39.10 O ANISOU 8088 O HOH A 600 4986 4938 4934 -6 -9 15 O HETATM 8089 O HOH A 601 30.021 27.273 37.143 1.00 43.25 O ANISOU 8089 O HOH A 601 5482 5432 5519 -11 -2 -7 O HETATM 8090 O HOH A 602 30.298 21.792 25.078 1.00 33.14 O ANISOU 8090 O HOH A 602 4189 4184 4219 -5 6 17 O HETATM 8091 O HOH A 603 14.828 3.806 25.540 1.00 35.09 O ANISOU 8091 O HOH A 603 4444 4463 4423 -6 -12 -10 O HETATM 8092 O HOH A 604 28.044 20.580 48.837 1.00 45.43 O ANISOU 8092 O HOH A 604 5765 5737 5761 -13 -6 -1 O HETATM 8093 O HOH A 605 28.293 27.775 27.800 1.00 28.84 O ANISOU 8093 O HOH A 605 3677 3660 3621 -15 1 4 O HETATM 8094 O HOH A 606 3.216 22.864 27.185 1.00 33.92 O ANISOU 8094 O HOH A 606 4320 4279 4290 -6 -9 4 O HETATM 8095 O HOH A 607 4.561 9.976 60.096 1.00 50.42 O ANISOU 8095 O HOH A 607 6414 6340 6402 1 9 2 O HETATM 8096 O HOH A 608 5.952 12.620 16.547 1.00 28.29 O ANISOU 8096 O HOH A 608 3664 3528 3556 9 9 -10 O HETATM 8097 O HOH A 609 25.517 16.377 20.524 1.00 36.69 O ANISOU 8097 O HOH A 609 4667 4635 4640 8 3 11 O HETATM 8098 O HOH A 610 21.266 10.294 61.574 1.00 41.02 O ANISOU 8098 O HOH A 610 5223 5158 5205 6 -17 11 O HETATM 8099 O HOH A 611 -3.036 19.776 29.614 1.00 36.51 O ANISOU 8099 O HOH A 611 4648 4602 4623 -2 -14 11 O HETATM 8100 O HOH A 612 -1.744 13.453 61.794 1.00 31.15 O ANISOU 8100 O HOH A 612 3981 3930 3926 1 -3 -1 O HETATM 8101 O HOH A 613 28.233 27.439 21.495 1.00 46.36 O ANISOU 8101 O HOH A 613 5897 5823 5896 -9 4 9 O HETATM 8102 O HOH A 614 16.861 2.685 27.892 1.00 43.46 O ANISOU 8102 O HOH A 614 5538 5459 5516 4 13 -10 O HETATM 8103 O HOH B 401 -19.313 33.802 -7.020 1.00 68.49 O ANISOU 8103 O HOH B 401 8695 8630 8698 4 3 2 O HETATM 8104 O HOH B 402 -33.326 33.114 -13.131 1.00 18.04 O ANISOU 8104 O HOH B 402 2341 2241 2272 23 -67 82 O HETATM 8105 O HOH B 403 -31.856 35.975 -16.372 1.00 22.82 O ANISOU 8105 O HOH B 403 2887 2894 2887 17 -18 37 O HETATM 8106 O HOH B 404 -4.990 9.230 -18.256 1.00 23.27 O ANISOU 8106 O HOH B 404 3017 2881 2945 20 22 -23 O HETATM 8107 O HOH B 405 -20.748 38.534 -3.173 1.00 21.95 O ANISOU 8107 O HOH B 405 2754 2793 2791 -46 -37 -27 O HETATM 8108 O HOH B 406 -1.626 25.793 -34.450 1.00 24.80 O ANISOU 8108 O HOH B 406 3148 3152 3122 10 -1 8 O HETATM 8109 O HOH B 407 -35.456 13.819 -11.224 1.00 23.46 O ANISOU 8109 O HOH B 407 2894 3003 3017 -15 -26 10 O HETATM 8110 O HOH B 408 -23.358 24.054 -32.822 1.00 39.68 O ANISOU 8110 O HOH B 408 5014 5034 5030 3 -4 10 O HETATM 8111 O HOH B 409 -15.366 11.553 -1.334 1.00 22.82 O ANISOU 8111 O HOH B 409 2876 2915 2880 -30 19 0 O HETATM 8112 O HOH B 410 2.348 13.551 -23.116 1.00 25.12 O ANISOU 8112 O HOH B 410 3174 3227 3146 6 -9 32 O HETATM 8113 O HOH B 411 -26.771 38.064 -13.577 1.00 24.16 O ANISOU 8113 O HOH B 411 3123 3029 3029 -29 19 -6 O HETATM 8114 O HOH B 412 -32.495 20.227 -10.938 1.00 13.93 O ANISOU 8114 O HOH B 412 1686 1783 1826 -37 -83 149 O HETATM 8115 O HOH B 413 -33.656 8.327 -16.758 1.00 22.10 O ANISOU 8115 O HOH B 413 2724 2853 2819 -22 -27 46 O HETATM 8116 O HOH B 414 -23.325 13.796 -14.646 1.00 13.11 O ANISOU 8116 O HOH B 414 1662 1682 1637 -109 -46 72 O HETATM 8117 O HOH B 415 -8.146 19.802 -33.278 1.00 25.52 O ANISOU 8117 O HOH B 415 3291 3265 3140 -4 -25 -3 O HETATM 8118 O HOH B 416 -15.463 23.194 2.850 1.00 24.75 O ANISOU 8118 O HOH B 416 3118 3182 3103 0 -26 -13 O HETATM 8119 O HOH B 417 -6.466 16.108 -34.468 1.00 24.13 O ANISOU 8119 O HOH B 417 3041 3022 3106 -33 -44 2 O HETATM 8120 O HOH B 418 -13.762 20.991 -14.243 1.00 37.84 O ANISOU 8120 O HOH B 418 4797 4788 4792 16 -2 5 O HETATM 8121 O HOH B 419 -18.804 28.948 6.433 1.00 38.86 O ANISOU 8121 O HOH B 419 4931 4890 4946 -2 -9 2 O HETATM 8122 O HOH B 420 -27.214 27.433 -22.265 1.00 20.98 O ANISOU 8122 O HOH B 420 2745 2647 2581 36 -21 44 O HETATM 8123 O HOH B 421 -6.303 29.461 -28.760 1.00 28.65 O ANISOU 8123 O HOH B 421 3660 3571 3657 -6 4 10 O HETATM 8124 O HOH B 422 -31.878 37.125 -10.029 1.00 32.21 O ANISOU 8124 O HOH B 422 4126 4032 4082 -7 -22 19 O HETATM 8125 O HOH B 423 -12.869 8.869 10.299 1.00 19.92 O ANISOU 8125 O HOH B 423 2563 2577 2429 7 -27 42 O HETATM 8126 O HOH B 424 -28.483 5.553 -10.685 1.00 26.34 O ANISOU 8126 O HOH B 424 3331 3335 3341 -24 -40 51 O HETATM 8127 O HOH B 425 -36.866 17.687 -19.217 1.00 30.76 O ANISOU 8127 O HOH B 425 3861 3884 3943 -26 -40 26 O HETATM 8128 O HOH B 426 -13.480 20.648 -4.506 1.00 27.25 O ANISOU 8128 O HOH B 426 3427 3426 3500 25 -21 -20 O HETATM 8129 O HOH B 427 -41.303 17.624 -9.082 1.00 26.37 O ANISOU 8129 O HOH B 427 3342 3333 3344 -2 22 11 O HETATM 8130 O HOH B 428 -8.650 22.183 -32.136 1.00 40.40 O ANISOU 8130 O HOH B 428 5137 5095 5118 0 -3 3 O HETATM 8131 O HOH B 429 -0.107 25.540 -25.129 1.00 25.22 O ANISOU 8131 O HOH B 429 3187 3167 3229 -31 -17 -21 O HETATM 8132 O HOH B 430 -19.674 5.126 3.113 1.00 36.58 O ANISOU 8132 O HOH B 430 4624 4596 4679 -12 -6 16 O HETATM 8133 O HOH B 431 -36.015 26.689 -14.189 1.00 23.40 O ANISOU 8133 O HOH B 431 2982 2967 2944 5 -42 21 O HETATM 8134 O HOH B 432 -21.287 39.378 -10.562 1.00 44.19 O ANISOU 8134 O HOH B 432 5617 5567 5608 -10 4 -12 O HETATM 8135 O HOH B 433 -19.634 40.750 -7.307 1.00 34.52 O ANISOU 8135 O HOH B 433 4368 4368 4380 -5 -21 10 O HETATM 8136 O HOH B 434 -31.976 10.183 -28.119 1.00 25.17 O ANISOU 8136 O HOH B 434 3135 3218 3211 -21 -29 -15 O HETATM 8137 O HOH B 435 -5.533 25.161 -15.973 1.00 25.76 O ANISOU 8137 O HOH B 435 3302 3294 3191 -12 10 5 O HETATM 8138 O HOH B 436 -5.192 9.062 -26.905 1.00 35.85 O ANISOU 8138 O HOH B 436 4592 4492 4536 -10 1 -8 O HETATM 8139 O HOH B 437 -13.505 21.844 -6.933 1.00 32.28 O ANISOU 8139 O HOH B 437 4097 4013 4153 -4 5 -15 O HETATM 8140 O HOH B 438 -28.798 1.647 -28.566 1.00 32.79 O ANISOU 8140 O HOH B 438 4148 4153 4158 -12 -13 -9 O HETATM 8141 O HOH B 439 -10.985 0.450 -21.423 1.00 23.57 O ANISOU 8141 O HOH B 439 3016 2934 3007 -5 -41 -3 O HETATM 8142 O HOH B 440 -12.462 17.068 -30.807 1.00 21.79 O ANISOU 8142 O HOH B 440 2870 2802 2606 -14 -5 7 O HETATM 8143 O HOH B 441 -37.416 13.011 -9.566 1.00 28.23 O ANISOU 8143 O HOH B 441 3585 3609 3533 -11 -17 41 O HETATM 8144 O HOH B 442 -6.576 9.721 -11.278 1.00 20.81 O ANISOU 8144 O HOH B 442 2738 2642 2527 -9 -8 11 O HETATM 8145 O HOH B 443 -38.687 26.896 -8.249 1.00 29.93 O ANISOU 8145 O HOH B 443 3768 3788 3814 9 -18 40 O HETATM 8146 O HOH B 444 -28.661 5.568 -6.695 1.00 21.86 O ANISOU 8146 O HOH B 444 2768 2720 2817 -59 10 5 O HETATM 8147 O HOH B 445 -34.877 27.946 -6.865 1.00 17.99 O ANISOU 8147 O HOH B 445 2273 2254 2307 21 21 30 O HETATM 8148 O HOH B 446 -1.469 8.748 -26.316 1.00 29.77 O ANISOU 8148 O HOH B 446 3804 3759 3748 -4 34 -20 O HETATM 8149 O HOH B 447 -28.028 25.131 7.658 1.00 42.78 O ANISOU 8149 O HOH B 447 5433 5413 5408 1 3 7 O HETATM 8150 O HOH B 448 -21.567 32.451 -1.813 1.00 20.63 O ANISOU 8150 O HOH B 448 2656 2595 2586 32 -12 27 O HETATM 8151 O HOH B 449 -19.335 -3.221 -9.794 1.00 29.74 O ANISOU 8151 O HOH B 449 3793 3701 3807 10 11 9 O HETATM 8152 O HOH B 450 -15.716 23.617 -20.445 1.00 31.50 O ANISOU 8152 O HOH B 450 3999 4012 3959 -16 16 17 O HETATM 8153 O HOH B 451 -6.563 15.331 -27.387 1.00 19.16 O ANISOU 8153 O HOH B 451 2435 2474 2371 1 -22 27 O HETATM 8154 O HOH B 452 -26.399 1.613 -14.290 1.00 23.50 O ANISOU 8154 O HOH B 452 2990 2945 2994 -15 -31 53 O HETATM 8155 O HOH B 453 -29.618 32.898 -10.873 1.00 17.76 O ANISOU 8155 O HOH B 453 2295 2240 2212 -31 6 10 O HETATM 8156 O HOH B 454 -14.621 21.260 -2.145 1.00 29.29 O ANISOU 8156 O HOH B 454 3712 3710 3709 2 3 5 O HETATM 8157 O HOH B 455 -30.618 7.043 -30.549 1.00 34.44 O ANISOU 8157 O HOH B 455 4371 4335 4380 3 -25 -7 O HETATM 8158 O HOH B 456 -7.350 4.788 -7.860 1.00 20.48 O ANISOU 8158 O HOH B 456 2678 2523 2581 -20 -35 34 O HETATM 8159 O HOH B 457 -7.729 4.885 -27.152 1.00 54.86 O ANISOU 8159 O HOH B 457 6964 6912 6968 -4 1 -9 O HETATM 8160 O HOH B 458 -33.412 13.906 -14.547 1.00 16.54 O ANISOU 8160 O HOH B 458 2023 2075 2187 -50 -43 80 O HETATM 8161 O HOH B 459 -14.170 25.815 -10.563 1.00 39.71 O ANISOU 8161 O HOH B 459 5034 5007 5049 15 12 13 O HETATM 8162 O HOH B 460 -29.435 -0.158 -22.365 1.00 27.75 O ANISOU 8162 O HOH B 460 3533 3476 3537 -23 -29 17 O HETATM 8163 O HOH B 461 -23.719 38.100 -19.981 1.00 28.31 O ANISOU 8163 O HOH B 461 3634 3564 3558 -11 -18 6 O HETATM 8164 O HOH B 462 -11.308 20.926 -10.832 1.00 36.54 O ANISOU 8164 O HOH B 462 4611 4612 4660 -10 13 6 O HETATM 8165 O HOH B 463 -40.989 20.506 -10.614 1.00 37.02 O ANISOU 8165 O HOH B 463 4693 4661 4713 -13 -16 -14 O HETATM 8166 O HOH B 464 -19.566 22.945 -18.839 1.00 11.70 O ANISOU 8166 O HOH B 464 1511 1464 1469 -40 -55 19 O HETATM 8167 O HOH B 465 -34.769 36.227 -25.682 1.00 47.81 O ANISOU 8167 O HOH B 465 6065 6028 6071 7 -10 2 O HETATM 8168 O HOH B 466 -7.816 -6.384 -14.896 1.00 40.37 O ANISOU 8168 O HOH B 466 5160 5094 5085 -3 -18 -6 O HETATM 8169 O HOH B 467 -27.345 13.231 -31.835 1.00 31.81 O ANISOU 8169 O HOH B 467 4019 4041 4025 -38 -8 21 O HETATM 8170 O HOH B 468 -16.284 29.780 -5.659 1.00 14.87 O ANISOU 8170 O HOH B 468 1844 1817 1989 0 -11 86 O HETATM 8171 O HOH B 469 -34.700 11.521 -0.328 1.00 28.27 O ANISOU 8171 O HOH B 469 3618 3554 3569 -13 -2 18 O HETATM 8172 O HOH B 470 -26.898 35.591 0.902 1.00 26.40 O ANISOU 8172 O HOH B 470 3378 3325 3326 13 -8 0 O HETATM 8173 O HOH B 471 -7.000 5.696 -11.792 1.00 38.20 O ANISOU 8173 O HOH B 471 4865 4805 4844 -12 -11 -11 O HETATM 8174 O HOH B 472 -10.321 0.388 -18.674 1.00 24.71 O ANISOU 8174 O HOH B 472 3165 3156 3065 -2 -25 -33 O HETATM 8175 O HOH B 473 -22.693 -2.974 -11.318 1.00 31.73 O ANISOU 8175 O HOH B 473 4039 3946 4071 -13 7 19 O HETATM 8176 O HOH B 474 -12.319 4.088 -31.455 1.00 39.33 O ANISOU 8176 O HOH B 474 4988 4953 5002 7 -1 -6 O HETATM 8177 O HOH B 475 -14.099 23.971 -12.663 1.00 35.01 O ANISOU 8177 O HOH B 475 4408 4428 4464 -6 6 -4 O HETATM 8178 O HOH B 476 2.454 13.758 -27.239 1.00 34.14 O ANISOU 8178 O HOH B 476 4342 4335 4296 1 9 4 O HETATM 8179 O HOH B 477 -12.639 15.260 8.542 1.00 28.81 O ANISOU 8179 O HOH B 477 3653 3655 3637 12 0 7 O HETATM 8180 O HOH B 478 -19.005 5.037 11.839 1.00 26.46 O ANISOU 8180 O HOH B 478 3316 3378 3361 6 13 32 O HETATM 8181 O HOH B 479 -23.871 31.826 -0.281 1.00 28.18 O ANISOU 8181 O HOH B 479 3586 3574 3549 2 14 3 O HETATM 8182 O HOH B 480 -8.580 18.893 -8.455 1.00 20.61 O ANISOU 8182 O HOH B 480 2618 2539 2674 -59 25 23 O HETATM 8183 O HOH B 481 -41.131 23.521 -3.373 1.00 32.57 O ANISOU 8183 O HOH B 481 4123 4076 4175 0 -20 23 O HETATM 8184 O HOH B 482 -21.727 -1.163 -3.043 1.00 34.14 O ANISOU 8184 O HOH B 482 4349 4285 4336 0 15 33 O HETATM 8185 O HOH B 483 -23.352 33.648 3.147 1.00 44.04 O ANISOU 8185 O HOH B 483 5595 5557 5581 -4 3 -1 O HETATM 8186 O HOH B 484 -21.637 28.501 6.094 1.00 26.40 O ANISOU 8186 O HOH B 484 3354 3368 3309 15 12 -3 O HETATM 8187 O HOH B 485 -22.862 31.145 5.605 1.00 35.38 O ANISOU 8187 O HOH B 485 4505 4479 4458 1 5 -5 O HETATM 8188 O HOH B 486 -17.008 6.237 3.133 1.00 34.69 O ANISOU 8188 O HOH B 486 4377 4368 4435 9 -37 -27 O HETATM 8189 O HOH B 487 -6.777 20.711 -30.686 1.00 26.31 O ANISOU 8189 O HOH B 487 3320 3352 3326 49 4 14 O HETATM 8190 O HOH B 488 -9.391 7.600 -27.320 1.00 39.12 O ANISOU 8190 O HOH B 488 4974 4905 4984 4 -11 -2 O HETATM 8191 O HOH B 489 -13.540 17.519 -11.647 1.00 41.68 O ANISOU 8191 O HOH B 489 5282 5308 5245 -11 -5 8 O HETATM 8192 O HOH B 490 -5.569 17.191 -24.996 1.00 17.88 O ANISOU 8192 O HOH B 490 2369 2220 2206 -8 -82 82 O HETATM 8193 O HOH B 491 -12.901 -3.180 -17.110 1.00 27.09 O ANISOU 8193 O HOH B 491 3454 3416 3423 8 -19 -5 O HETATM 8194 O HOH B 492 -1.736 25.124 -22.237 1.00 30.21 O ANISOU 8194 O HOH B 492 3842 3809 3827 -11 -14 9 O HETATM 8195 O HOH B 493 -15.803 -2.841 -27.377 1.00 38.20 O ANISOU 8195 O HOH B 493 4845 4813 4858 -1 -13 -18 O HETATM 8196 O HOH B 494 -20.095 26.271 -22.051 1.00 35.37 O ANISOU 8196 O HOH B 494 4495 4441 4503 1 -1 6 O HETATM 8197 O HOH B 495 -20.038 -4.122 -12.284 1.00 30.64 O ANISOU 8197 O HOH B 495 3909 3832 3903 -3 -10 9 O HETATM 8198 O HOH B 496 -40.506 26.124 -4.639 1.00 37.70 O ANISOU 8198 O HOH B 496 4747 4779 4797 2 -12 11 O HETATM 8199 O HOH B 497 -37.844 27.280 -1.904 1.00 46.86 O ANISOU 8199 O HOH B 497 5945 5898 5961 9 7 -1 O HETATM 8200 O HOH B 498 0.727 18.181 -20.861 1.00 22.72 O ANISOU 8200 O HOH B 498 2818 2999 2814 -39 -30 39 O HETATM 8201 O HOH B 499 -15.113 3.729 -32.614 1.00 33.57 O ANISOU 8201 O HOH B 499 4291 4228 4235 -1 2 -1 O HETATM 8202 O HOH B 500 -2.649 3.789 -21.638 1.00 31.88 O ANISOU 8202 O HOH B 500 4091 4002 4022 -18 11 -14 O HETATM 8203 O HOH B 501 -8.154 8.007 -12.823 1.00 27.16 O ANISOU 8203 O HOH B 501 3441 3439 3439 9 -19 -40 O HETATM 8204 O HOH B 502 -29.981 7.112 4.223 1.00 31.12 O ANISOU 8204 O HOH B 502 3950 3921 3954 -22 6 8 O HETATM 8205 O HOH B 503 -15.154 7.787 -3.013 1.00 33.00 O ANISOU 8205 O HOH B 503 4178 4147 4213 -11 -7 26 O HETATM 8206 O HOH B 504 -27.090 36.323 -20.890 1.00 18.80 O ANISOU 8206 O HOH B 504 2398 2350 2395 -26 -34 20 O HETATM 8207 O HOH B 505 -15.163 20.583 -9.154 1.00 20.06 O ANISOU 8207 O HOH B 505 2543 2562 2518 32 43 49 O HETATM 8208 O HOH B 506 -29.562 39.689 0.986 1.00 41.93 O ANISOU 8208 O HOH B 506 5317 5289 5324 0 6 -1 O HETATM 8209 O HOH B 507 -16.534 8.437 4.614 1.00 18.48 O ANISOU 8209 O HOH B 507 2284 2443 2293 17 -53 77 O HETATM 8210 O HOH B 508 -29.446 3.990 -1.998 1.00 48.69 O ANISOU 8210 O HOH B 508 6180 6131 6189 -13 -1 12 O HETATM 8211 O HOH B 509 -0.136 6.150 -21.731 1.00 47.49 O ANISOU 8211 O HOH B 509 6021 5987 6036 -3 4 -3 O HETATM 8212 O HOH B 510 -22.340 3.292 -31.297 1.00 21.08 O ANISOU 8212 O HOH B 510 2748 2670 2589 -31 -70 -2 O HETATM 8213 O HOH B 511 -25.884 34.805 -2.794 1.00 21.26 O ANISOU 8213 O HOH B 511 2716 2656 2705 24 -10 28 O HETATM 8214 O HOH B 512 -29.164 7.589 -12.358 1.00 21.21 O ANISOU 8214 O HOH B 512 2658 2686 2716 -39 -40 46 O HETATM 8215 O HOH B 513 -25.495 5.085 -0.563 1.00 27.99 O ANISOU 8215 O HOH B 513 3526 3522 3585 -14 12 39 O HETATM 8216 O HOH B 514 -21.607 20.006 -33.624 1.00 34.50 O ANISOU 8216 O HOH B 514 4388 4349 4369 9 -1 23 O HETATM 8217 O HOH B 515 -0.868 24.934 -36.918 1.00 27.76 O ANISOU 8217 O HOH B 515 3547 3508 3494 13 -48 16 O HETATM 8218 O HOH B 516 -10.196 -6.121 -10.952 1.00 22.73 O ANISOU 8218 O HOH B 516 2882 2880 2874 -40 -40 -12 O HETATM 8219 O HOH B 517 -37.743 19.606 -16.192 1.00 30.78 O ANISOU 8219 O HOH B 517 3900 3929 3863 9 -13 11 O HETATM 8220 O HOH B 518 -20.298 9.076 -34.300 1.00 29.51 O ANISOU 8220 O HOH B 518 3803 3750 3660 2 -9 15 O HETATM 8221 O HOH B 519 -22.926 8.317 -33.877 1.00 34.27 O ANISOU 8221 O HOH B 519 4338 4352 4329 5 -21 3 O HETATM 8222 O HOH B 520 -18.129 32.913 -4.988 1.00 16.96 O ANISOU 8222 O HOH B 520 2141 2137 2168 14 17 -57 O HETATM 8223 O HOH B 521 -37.001 14.749 -13.411 1.00 29.58 O ANISOU 8223 O HOH B 521 3759 3730 3749 -19 -15 -9 O HETATM 8224 O HOH B 522 -31.137 27.529 -16.560 1.00 24.26 O ANISOU 8224 O HOH B 522 3035 3047 3137 2 9 -1 O HETATM 8225 O HOH B 523 -19.210 39.224 -17.658 1.00 33.68 O ANISOU 8225 O HOH B 523 4271 4256 4271 4 8 25 O HETATM 8226 O HOH B 524 -8.988 21.011 -6.908 1.00 28.96 O ANISOU 8226 O HOH B 524 3656 3621 3726 -41 31 -19 O HETATM 8227 O HOH B 525 -23.731 4.908 3.197 1.00 40.82 O ANISOU 8227 O HOH B 525 5166 5160 5184 6 12 1 O HETATM 8228 O HOH B 526 -35.773 21.868 -21.173 1.00 37.14 O ANISOU 8228 O HOH B 526 4703 4699 4710 -5 -1 -6 O HETATM 8229 O HOH B 527 -1.691 6.940 -24.121 1.00 23.71 O ANISOU 8229 O HOH B 527 3069 2908 3030 8 22 -27 O HETATM 8230 O HOH B 528 -15.492 24.017 -1.974 1.00 26.44 O ANISOU 8230 O HOH B 528 3351 3317 3376 -5 -6 1 O HETATM 8231 O HOH B 529 -34.846 4.644 -15.819 1.00 39.30 O ANISOU 8231 O HOH B 529 4976 4959 4997 -11 -11 -4 O HETATM 8232 O HOH B 530 -36.439 11.642 -16.643 1.00 46.72 O ANISOU 8232 O HOH B 530 5918 5891 5942 -5 2 -10 O HETATM 8233 O HOH B 531 -33.574 38.091 -22.954 1.00 34.78 O ANISOU 8233 O HOH B 531 4410 4388 4419 12 -22 -3 O HETATM 8234 O HOH B 532 -36.433 20.414 -18.846 1.00 46.05 O ANISOU 8234 O HOH B 532 5844 5803 5850 0 -3 15 O HETATM 8235 O HOH B 533 -34.981 34.169 -16.957 1.00 49.41 O ANISOU 8235 O HOH B 533 6272 6223 6278 -1 -2 -6 O HETATM 8236 O HOH B 534 -30.993 22.936 -26.480 1.00 39.33 O ANISOU 8236 O HOH B 534 5016 4947 4981 1 4 -1 O HETATM 8237 O HOH B 535 -31.008 19.908 -30.555 1.00 38.10 O ANISOU 8237 O HOH B 535 4842 4802 4833 8 -15 9 O HETATM 8238 O HOH B 536 -13.827 19.294 -31.804 1.00 51.38 O ANISOU 8238 O HOH B 536 6526 6487 6508 -3 -9 -3 O HETATM 8239 O HOH B 537 -34.394 10.748 -11.366 1.00 34.40 O ANISOU 8239 O HOH B 537 4388 4322 4362 -13 -12 5 O HETATM 8240 O HOH B 538 -6.925 9.235 -15.293 1.00 26.37 O ANISOU 8240 O HOH B 538 3399 3416 3204 53 -36 17 O HETATM 8241 O HOH B 539 -24.265 13.362 -34.722 1.00 30.91 O ANISOU 8241 O HOH B 539 3953 3906 3886 -22 1 13 O HETATM 8242 O HOH B 540 -27.956 36.165 -9.990 1.00 25.94 O ANISOU 8242 O HOH B 540 3255 3321 3282 -5 10 -3 O HETATM 8243 O HOH B 541 -7.533 13.873 10.192 1.00 24.46 O ANISOU 8243 O HOH B 541 3080 3165 3048 -16 -22 28 O HETATM 8244 O HOH B 542 -10.339 12.206 -27.414 1.00 18.36 O ANISOU 8244 O HOH B 542 2421 2404 2150 31 -37 57 O HETATM 8245 O HOH B 543 -8.479 15.084 7.842 1.00 21.91 O ANISOU 8245 O HOH B 543 2805 2786 2731 20 41 -5 O HETATM 8246 O HOH B 544 -8.943 6.132 -29.855 1.00 47.16 O ANISOU 8246 O HOH B 544 5997 5941 5981 9 -7 10 O HETATM 8247 O HOH B 545 -33.849 23.319 -18.682 1.00 28.57 O ANISOU 8247 O HOH B 545 3646 3570 3638 21 -18 34 O HETATM 8248 O HOH B 546 -11.794 19.688 8.121 1.00 63.73 O ANISOU 8248 O HOH B 546 8088 8034 8094 -1 4 -5 O HETATM 8249 O HOH B 547 -26.327 35.216 -13.792 1.00 18.33 O ANISOU 8249 O HOH B 547 2368 2289 2306 -11 -58 32 O HETATM 8250 O HOH B 548 -20.987 36.878 -19.425 1.00 21.90 O ANISOU 8250 O HOH B 548 2849 2777 2696 -50 -11 41 O HETATM 8251 O HOH B 549 -33.788 9.016 -13.591 1.00 34.48 O ANISOU 8251 O HOH B 549 4347 4367 4388 -10 -8 7 O HETATM 8252 O HOH B 550 -28.054 20.968 -31.373 1.00 39.94 O ANISOU 8252 O HOH B 550 5080 5051 5043 3 3 -5 O HETATM 8253 O HOH B 551 -24.959 -1.220 -28.210 1.00 36.85 O ANISOU 8253 O HOH B 551 4691 4639 4670 -17 -30 3 O HETATM 8254 O HOH B 552 -13.856 -4.556 -12.644 1.00 26.79 O ANISOU 8254 O HOH B 552 3414 3335 3430 -6 -29 -9 O HETATM 8255 O HOH B 553 -8.807 4.645 -10.094 1.00 37.90 O ANISOU 8255 O HOH B 553 4794 4786 4822 14 -8 -1 O HETATM 8256 O HOH B 554 -30.920 23.579 -19.625 1.00 16.89 O ANISOU 8256 O HOH B 554 2203 2083 2132 22 10 72 O HETATM 8257 O HOH B 555 -19.712 20.119 -27.161 1.00 24.29 O ANISOU 8257 O HOH B 555 3065 3077 3087 -21 -21 28 O HETATM 8258 O HOH B 556 -4.522 11.206 -28.506 1.00 24.44 O ANISOU 8258 O HOH B 556 3155 3123 3009 -9 11 -9 O HETATM 8259 O HOH B 557 -12.983 -1.958 -19.730 1.00 27.50 O ANISOU 8259 O HOH B 557 3538 3413 3497 2 -7 -24 O HETATM 8260 O HOH B 558 -22.688 5.875 5.728 1.00 36.59 O ANISOU 8260 O HOH B 558 4651 4619 4633 2 -25 16 O HETATM 8261 O HOH B 559 -31.880 7.557 -11.637 1.00 19.95 O ANISOU 8261 O HOH B 559 2499 2574 2506 -34 -48 17 O HETATM 8262 O HOH B 560 -12.389 7.608 0.741 1.00 25.36 O ANISOU 8262 O HOH B 560 3169 3238 3227 -7 0 8 O HETATM 8263 O HOH B 561 -6.856 19.152 -1.231 1.00 24.63 O ANISOU 8263 O HOH B 561 3101 3103 3153 -43 -25 56 O HETATM 8264 O HOH B 562 -25.626 29.765 -23.833 1.00 36.05 O ANISOU 8264 O HOH B 562 4597 4522 4580 6 -22 -8 O HETATM 8265 O HOH B 563 -27.003 40.685 -10.098 1.00 45.30 O ANISOU 8265 O HOH B 563 5757 5706 5750 11 2 -8 O HETATM 8266 O HOH B 564 -17.555 19.751 11.606 1.00 43.03 O ANISOU 8266 O HOH B 564 5476 5430 5445 10 3 12 O HETATM 8267 O HOH B 565 -35.838 30.705 -7.053 1.00 27.63 O ANISOU 8267 O HOH B 565 3473 3432 3593 18 -14 10 O HETATM 8268 O HOH B 566 -18.315 -2.984 -4.450 1.00 38.42 O ANISOU 8268 O HOH B 566 4837 4877 4884 0 -23 5 O HETATM 8269 O HOH B 567 -2.664 8.709 -15.829 1.00 23.73 O ANISOU 8269 O HOH B 567 2990 2975 3052 -71 -3 17 O HETATM 8270 O HOH B 568 -35.468 12.743 3.043 1.00 31.31 O ANISOU 8270 O HOH B 568 3975 3916 4006 -15 29 41 O HETATM 8271 O HOH B 569 -18.609 23.591 -21.696 1.00 26.76 O ANISOU 8271 O HOH B 569 3430 3343 3393 -10 6 -2 O HETATM 8272 O HOH B 570 -11.804 23.686 -28.521 1.00 16.40 O ANISOU 8272 O HOH B 570 2130 2125 1975 -30 -3 60 O HETATM 8273 O HOH B 571 -14.825 19.958 -11.998 1.00 32.52 O ANISOU 8273 O HOH B 571 4107 4039 4210 -16 40 -9 O HETATM 8274 O HOH B 572 -2.670 25.919 -18.772 1.00 46.29 O ANISOU 8274 O HOH B 572 5885 5819 5885 2 -1 0 O HETATM 8275 O HOH B 573 -9.065 -0.424 -25.630 1.00 41.34 O ANISOU 8275 O HOH B 573 5257 5207 5244 -5 3 -8 O HETATM 8276 O HOH B 574 -13.070 21.947 3.602 1.00 41.13 O ANISOU 8276 O HOH B 574 5209 5186 5234 -2 -15 -5 O HETATM 8277 O HOH B 575 -5.716 17.015 -30.498 1.00 23.50 O ANISOU 8277 O HOH B 575 2977 3009 2944 -29 -12 39 O HETATM 8278 O HOH B 576 -27.336 2.980 -6.253 1.00 29.21 O ANISOU 8278 O HOH B 576 3717 3678 3702 -17 -2 17 O HETATM 8279 O HOH B 577 -16.404 27.423 -18.036 1.00 37.34 O ANISOU 8279 O HOH B 577 4727 4718 4743 9 13 13 O HETATM 8280 O HOH B 578 -22.369 31.688 -23.603 1.00 31.04 O ANISOU 8280 O HOH B 578 3983 3863 3947 2 14 18 O HETATM 8281 O HOH B 579 -33.600 10.401 -4.167 1.00 27.84 O ANISOU 8281 O HOH B 579 3489 3505 3585 8 -10 27 O HETATM 8282 O HOH B 580 -16.288 27.710 -10.296 1.00 15.62 O ANISOU 8282 O HOH B 580 2037 2048 1850 -102 -54 -60 O HETATM 8283 O HOH B 581 -21.721 -2.834 -6.393 1.00 28.23 O ANISOU 8283 O HOH B 581 3593 3544 3589 -14 0 41 O HETATM 8284 O HOH B 582 -3.038 28.199 -30.213 1.00 48.62 O ANISOU 8284 O HOH B 582 6171 6131 6173 1 -5 7 O HETATM 8285 O HOH B 583 -11.259 28.999 -17.007 1.00 34.61 O ANISOU 8285 O HOH B 583 4392 4383 4375 13 -4 -3 O HETATM 8286 O HOH B 584 -35.196 28.738 -9.531 1.00 23.41 O ANISOU 8286 O HOH B 584 3000 2982 2912 -14 -16 4 O HETATM 8287 O HOH B 585 -26.045 39.948 -17.202 1.00 41.29 O ANISOU 8287 O HOH B 585 5271 5182 5236 11 4 14 O HETATM 8288 O HOH B 586 -16.403 39.689 -12.255 1.00 28.70 O ANISOU 8288 O HOH B 586 3624 3631 3648 -36 -18 7 O HETATM 8289 O HOH B 587 -1.124 1.319 -21.301 1.00 41.82 O ANISOU 8289 O HOH B 587 5308 5260 5319 -5 -3 0 O HETATM 8290 O HOH B 588 -9.215 2.879 -28.670 1.00 46.51 O ANISOU 8290 O HOH B 588 5908 5860 5905 -3 0 -6 O HETATM 8291 O HOH B 589 -18.066 4.767 5.302 1.00 59.08 O ANISOU 8291 O HOH B 589 7498 7442 7506 -2 0 -4 O HETATM 8292 O HOH B 590 -34.352 33.689 1.600 1.00 48.22 O ANISOU 8292 O HOH B 590 6118 6073 6131 12 3 -6 O HETATM 8293 O HOH B 591 -10.955 9.628 -28.341 1.00 31.41 O ANISOU 8293 O HOH B 591 4042 3941 3952 -9 12 -8 O HETATM 8294 O HOH B 592 -36.843 28.878 -3.950 1.00 42.96 O ANISOU 8294 O HOH B 592 5462 5413 5449 7 8 -3 O HETATM 8295 O HOH B 593 -26.666 34.017 -11.397 1.00 19.44 O ANISOU 8295 O HOH B 593 2441 2403 2543 -89 -82 76 O HETATM 8296 O HOH B 594 -36.050 9.273 -1.256 1.00 33.24 O ANISOU 8296 O HOH B 594 4221 4166 4242 -1 -15 9 O HETATM 8297 O HOH B 595 -17.129 -5.625 -12.549 1.00 25.88 O ANISOU 8297 O HOH B 595 3264 3245 3323 21 -12 53 O HETATM 8298 O HOH B 596 -28.349 1.561 -8.825 1.00 41.98 O ANISOU 8298 O HOH B 596 5327 5278 5346 19 7 12 O HETATM 8299 O HOH B 597 0.713 22.542 -37.220 1.00 35.68 O ANISOU 8299 O HOH B 597 4565 4496 4498 -15 -38 5 O HETATM 8300 O HOH B 598 -27.284 28.163 5.535 1.00 45.63 O ANISOU 8300 O HOH B 598 5807 5747 5784 -1 7 0 O HETATM 8301 O HOH B 599 -30.795 26.325 -19.079 1.00 36.05 O ANISOU 8301 O HOH B 599 4561 4534 4603 -13 -13 14 O HETATM 8302 O HOH B 600 -22.864 13.209 11.914 1.00 48.43 O ANISOU 8302 O HOH B 600 6150 6107 6142 -3 -2 1 O HETATM 8303 O HOH B 601 -19.927 35.530 -21.574 1.00 40.22 O ANISOU 8303 O HOH B 601 5091 5084 5107 -10 15 -4 O HETATM 8304 O HOH B 602 -24.319 -1.219 -1.873 1.00 41.22 O ANISOU 8304 O HOH B 602 5224 5201 5237 -12 7 9 O HETATM 8305 O HOH B 603 -28.536 2.118 -3.886 1.00 44.26 O ANISOU 8305 O HOH B 603 5604 5570 5641 -4 -3 15 O HETATM 8306 O HOH B 604 -20.654 36.710 3.128 1.00 34.64 O ANISOU 8306 O HOH B 604 4378 4357 4427 4 -5 3 O HETATM 8307 O HOH B 605 -33.396 34.858 -5.704 1.00 49.49 O ANISOU 8307 O HOH B 605 6271 6248 6284 7 -1 -11 O HETATM 8308 O HOH B 606 -12.534 25.624 -18.075 1.00 48.27 O ANISOU 8308 O HOH B 606 6145 6070 6123 2 -2 -8 O HETATM 8309 O HOH B 607 -23.614 4.558 -33.999 1.00 31.99 O ANISOU 8309 O HOH B 607 4070 4006 4081 -6 -10 -19 O HETATM 8310 O HOH B 608 -11.059 22.135 -8.326 1.00 43.54 O ANISOU 8310 O HOH B 608 5516 5491 5538 3 14 3 O HETATM 8311 O HOH B 609 -30.546 1.803 -26.364 1.00 31.51 O ANISOU 8311 O HOH B 609 3954 3995 4024 -18 -42 -3 O HETATM 8312 O HOH B 610 -1.968 1.086 -17.435 1.00 42.87 O ANISOU 8312 O HOH B 610 5443 5403 5442 10 4 -13 O HETATM 8313 O HOH B 611 -14.038 23.892 0.406 1.00 34.80 O ANISOU 8313 O HOH B 611 4380 4415 4428 0 9 4 O HETATM 8314 O HOH B 612 -31.955 24.787 -21.906 1.00 37.26 O ANISOU 8314 O HOH B 612 4708 4711 4738 -8 -15 2 O HETATM 8315 O HOH B 613 -20.535 22.369 -28.897 1.00 29.39 O ANISOU 8315 O HOH B 613 3748 3691 3727 -16 20 1 O HETATM 8316 O HOH B 614 -11.151 24.470 0.608 1.00 47.73 O ANISOU 8316 O HOH B 614 6060 5995 6082 0 -1 -2 O HETATM 8317 O HOH B 615 -35.436 24.270 -22.443 1.00 45.90 O ANISOU 8317 O HOH B 615 5842 5785 5811 10 -3 -3 O HETATM 8318 O HOH B 616 -24.156 35.030 0.684 1.00 27.48 O ANISOU 8318 O HOH B 616 3480 3441 3518 3 -15 1 O HETATM 8319 O HOH B 617 -23.320 34.714 -2.000 1.00 27.25 O ANISOU 8319 O HOH B 617 3444 3456 3454 16 -8 -1 O HETATM 8320 O HOH B 618 -35.425 34.491 -14.209 1.00 36.88 O ANISOU 8320 O HOH B 618 4657 4655 4701 9 -18 11 O HETATM 8321 O HOH B 619 -21.585 3.694 1.678 1.00 43.23 O ANISOU 8321 O HOH B 619 5509 5433 5485 1 6 -1 O HETATM 8322 O HOH B 620 -14.612 23.192 -28.156 1.00 30.40 O ANISOU 8322 O HOH B 620 3860 3895 3795 -14 5 15 O HETATM 8323 O HOH B 621 -26.079 35.012 4.422 1.00 42.51 O ANISOU 8323 O HOH B 621 5409 5358 5385 6 -3 -1 O HETATM 8324 O HOH B 622 -28.824 38.539 -11.695 1.00 34.18 O ANISOU 8324 O HOH B 622 4357 4312 4317 -13 -7 6 O HETATM 8325 O HOH B 623 -10.485 -1.834 -23.304 1.00 42.67 O ANISOU 8325 O HOH B 623 5432 5384 5396 13 2 -1 O HETATM 8326 O HOH B 624 -13.510 -6.017 -15.176 1.00 45.95 O ANISOU 8326 O HOH B 624 5841 5782 5838 -6 -1 -8 O HETATM 8327 O HOH B 625 -1.743 27.914 -32.653 1.00 32.99 O ANISOU 8327 O HOH B 625 4151 4187 4196 -9 4 -7 O HETATM 8328 O HOH B 626 -11.337 22.977 -3.718 1.00 45.13 O ANISOU 8328 O HOH B 626 5726 5691 5732 -3 -1 5 O HETATM 8329 O HOH B 627 -22.877 15.558 -35.833 1.00 27.73 O ANISOU 8329 O HOH B 627 3517 3494 3526 -22 -23 12 O HETATM 8330 O HOH B 628 -27.766 -1.024 -28.636 1.00 33.95 O ANISOU 8330 O HOH B 628 4330 4262 4308 -5 -21 2 O HETATM 8331 O HOH B 629 -38.638 30.070 -7.468 1.00 40.92 O ANISOU 8331 O HOH B 629 5182 5150 5214 2 7 5 O HETATM 8332 O HOH B 630 -22.413 0.662 -32.211 1.00 38.09 O ANISOU 8332 O HOH B 630 4875 4793 4804 -5 -5 -7 O HETATM 8333 O HOH B 631 -10.599 17.069 7.957 1.00 41.44 O ANISOU 8333 O HOH B 631 5281 5214 5250 5 -19 -2 O HETATM 8334 O HOH B 632 -8.738 14.084 -28.577 1.00 34.73 O ANISOU 8334 O HOH B 632 4418 4398 4380 -22 2 3 O HETATM 8335 O HOH B 633 -20.942 36.022 -2.190 1.00 40.59 O ANISOU 8335 O HOH B 633 5128 5131 5162 1 -13 -11 O HETATM 8336 O HOH B 634 -4.295 14.666 -35.368 1.00 34.25 O ANISOU 8336 O HOH B 634 4372 4316 4325 0 -24 -5 O HETATM 8337 O HOH B 635 -26.338 2.553 0.356 1.00 29.94 O ANISOU 8337 O HOH B 635 3810 3770 3795 3 9 22 O HETATM 8338 O HOH B 636 -30.460 25.465 -25.276 1.00 42.77 O ANISOU 8338 O HOH B 636 5452 5388 5412 10 -3 0 O HETATM 8339 O HOH B 637 -1.874 28.067 -17.337 1.00 42.94 O ANISOU 8339 O HOH B 637 5437 5414 5463 9 -17 -2 O HETATM 8340 O HOH B 638 -4.871 13.303 10.573 1.00 28.19 O ANISOU 8340 O HOH B 638 3608 3551 3552 -2 -21 21 O HETATM 8341 O HOH B 639 -18.677 -4.906 -7.597 1.00 43.65 O ANISOU 8341 O HOH B 639 5548 5492 5544 -3 -12 2 O HETATM 8342 O HOH B 640 2.198 8.087 -21.172 1.00 36.82 O ANISOU 8342 O HOH B 640 4653 4657 4679 9 15 2 O HETATM 8343 O HOH B 641 -30.795 -0.523 -24.886 1.00 33.79 O ANISOU 8343 O HOH B 641 4237 4243 4358 -17 -23 11 O HETATM 8344 O HOH B 642 -23.564 -1.343 -30.665 1.00 35.89 O ANISOU 8344 O HOH B 642 4554 4531 4553 -10 -24 -14 O HETATM 8345 O HOH B 643 1.292 26.782 -27.157 1.00 38.02 O ANISOU 8345 O HOH B 643 4825 4788 4831 -5 9 -15 O HETATM 8346 O HOH B 644 1.033 3.612 -18.703 1.00 38.30 O ANISOU 8346 O HOH B 644 4876 4832 4845 7 7 13 O HETATM 8347 O HOH B 645 -16.473 24.435 -26.315 1.00 39.43 O ANISOU 8347 O HOH B 645 5009 4961 5012 26 -24 14 O HETATM 8348 O HOH B 646 -29.185 -2.279 -26.370 1.00 44.25 O ANISOU 8348 O HOH B 646 5630 5571 5613 -10 -1 -1 O HETATM 8349 O HOH C 401 5.060 25.160 36.355 1.00 31.53 O ANISOU 8349 O HOH C 401 4003 4020 3956 38 -42 -52 O HETATM 8350 O HOH C 402 -14.800 42.057 55.123 1.00 16.84 O ANISOU 8350 O HOH C 402 2174 2031 2194 52 22 9 O HETATM 8351 O HOH C 403 2.774 3.451 33.184 1.00 20.75 O ANISOU 8351 O HOH C 403 2705 2591 2589 32 27 -11 O HETATM 8352 O HOH C 404 8.858 24.102 57.018 1.00 29.19 O ANISOU 8352 O HOH C 404 3699 3685 3708 -27 -2 -10 O HETATM 8353 O HOH C 405 -8.226 21.198 66.247 1.00 29.27 O ANISOU 8353 O HOH C 405 3726 3704 3691 3 3 17 O HETATM 8354 O HOH C 406 -1.676 11.518 53.405 1.00 17.82 O ANISOU 8354 O HOH C 406 2283 2256 2233 -17 -24 6 O HETATM 8355 O HOH C 407 -2.273 16.636 42.050 1.00 17.95 O ANISOU 8355 O HOH C 407 2339 2216 2266 -3 -76 -9 O HETATM 8356 O HOH C 408 -27.705 18.639 49.209 1.00 24.82 O ANISOU 8356 O HOH C 408 3138 3118 3176 6 -43 -7 O HETATM 8357 O HOH C 409 -3.845 10.631 30.511 1.00 27.65 O ANISOU 8357 O HOH C 409 3567 3476 3462 -19 -38 17 O HETATM 8358 O HOH C 410 -7.430 46.112 52.248 1.00 34.67 O ANISOU 8358 O HOH C 410 4415 4333 4427 -27 -4 0 O HETATM 8359 O HOH C 411 2.235 4.183 37.075 1.00 25.57 O ANISOU 8359 O HOH C 411 3337 3193 3184 -1 2 -9 O HETATM 8360 O HOH C 412 -21.280 24.887 48.655 1.00 11.06 O ANISOU 8360 O HOH C 412 1451 1424 1328 -28 -76 -66 O HETATM 8361 O HOH C 413 -0.137 13.829 53.616 1.00 18.20 O ANISOU 8361 O HOH C 413 2450 2315 2148 5 -17 -35 O HETATM 8362 O HOH C 414 -19.956 25.627 62.729 1.00 24.15 O ANISOU 8362 O HOH C 414 3088 3056 3032 7 7 -26 O HETATM 8363 O HOH C 415 -18.370 31.533 47.332 1.00 13.60 O ANISOU 8363 O HOH C 415 1843 1662 1662 -16 -9 -23 O HETATM 8364 O HOH C 416 -20.543 30.358 44.251 1.00 30.63 O ANISOU 8364 O HOH C 416 3940 3842 3856 20 -16 31 O HETATM 8365 O HOH C 417 -11.464 30.356 67.406 1.00 17.28 O ANISOU 8365 O HOH C 417 2264 2197 2103 -1 25 33 O HETATM 8366 O HOH C 418 -28.030 28.219 45.831 1.00 27.22 O ANISOU 8366 O HOH C 418 3472 3391 3478 9 -27 0 O HETATM 8367 O HOH C 419 -12.799 21.765 30.527 1.00 28.23 O ANISOU 8367 O HOH C 419 3592 3548 3586 17 -5 -7 O HETATM 8368 O HOH C 420 -25.837 16.108 57.315 1.00 22.21 O ANISOU 8368 O HOH C 420 2899 2810 2730 -10 -81 14 O HETATM 8369 O HOH C 421 -23.283 23.289 57.736 1.00 28.09 O ANISOU 8369 O HOH C 421 3586 3582 3504 -40 2 35 O HETATM 8370 O HOH C 422 -31.005 17.156 37.660 1.00 23.57 O ANISOU 8370 O HOH C 422 3045 3019 2891 -26 -21 -10 O HETATM 8371 O HOH C 423 -9.829 32.156 41.262 1.00 23.35 O ANISOU 8371 O HOH C 423 2973 2964 2935 43 3 15 O HETATM 8372 O HOH C 424 -13.704 30.994 70.535 1.00 34.28 O ANISOU 8372 O HOH C 424 4375 4343 4306 -2 -10 8 O HETATM 8373 O HOH C 425 -18.432 13.664 36.256 1.00 24.07 O ANISOU 8373 O HOH C 425 3094 3116 2934 -68 -33 28 O HETATM 8374 O HOH C 426 -27.357 24.695 53.962 1.00 26.65 O ANISOU 8374 O HOH C 426 3390 3398 3337 -19 -2 1 O HETATM 8375 O HOH C 427 -9.743 27.254 50.627 1.00 10.36 O ANISOU 8375 O HOH C 427 1515 1256 1165 19 -117 -53 O HETATM 8376 O HOH C 428 -20.763 8.314 38.769 1.00 29.61 O ANISOU 8376 O HOH C 428 3807 3722 3723 5 0 -24 O HETATM 8377 O HOH C 429 0.496 9.486 32.497 1.00 15.36 O ANISOU 8377 O HOH C 429 1978 2018 1841 25 -28 -18 O HETATM 8378 O HOH C 430 5.134 39.511 61.048 1.00 30.77 O ANISOU 8378 O HOH C 430 3912 3870 3907 11 -11 14 O HETATM 8379 O HOH C 431 -5.860 35.908 42.477 1.00 17.11 O ANISOU 8379 O HOH C 431 2274 2162 2066 29 -27 -8 O HETATM 8380 O HOH C 432 -10.165 29.390 38.243 1.00 17.19 O ANISOU 8380 O HOH C 432 2256 2148 2129 28 -73 -6 O HETATM 8381 O HOH C 433 -15.794 34.254 43.547 1.00 25.63 O ANISOU 8381 O HOH C 433 3241 3223 3274 27 -9 19 O HETATM 8382 O HOH C 434 -9.806 30.730 65.328 1.00 18.53 O ANISOU 8382 O HOH C 434 2444 2345 2250 -25 -22 -1 O HETATM 8383 O HOH C 435 -7.340 18.969 77.104 1.00 26.26 O ANISOU 8383 O HOH C 435 3287 3369 3320 -15 -26 34 O HETATM 8384 O HOH C 436 1.721 40.330 46.684 1.00 35.56 O ANISOU 8384 O HOH C 436 4504 4490 4520 -11 -2 -7 O HETATM 8385 O HOH C 437 -30.213 21.780 48.474 1.00 24.13 O ANISOU 8385 O HOH C 437 3109 3006 3056 23 -20 -2 O HETATM 8386 O HOH C 438 5.209 15.793 55.843 1.00 50.83 O ANISOU 8386 O HOH C 438 6427 6423 6463 4 -9 11 O HETATM 8387 O HOH C 439 8.547 32.579 50.394 1.00 25.67 O ANISOU 8387 O HOH C 439 3294 3227 3232 3 -8 -9 O HETATM 8388 O HOH C 440 -2.966 44.266 57.509 1.00 17.34 O ANISOU 8388 O HOH C 440 2257 2104 2227 -11 -33 -7 O HETATM 8389 O HOH C 441 -31.829 13.404 48.023 1.00 26.91 O ANISOU 8389 O HOH C 441 3408 3413 3405 13 12 -15 O HETATM 8390 O HOH C 442 2.541 32.752 38.598 1.00 25.52 O ANISOU 8390 O HOH C 442 3236 3162 3297 -5 -8 41 O HETATM 8391 O HOH C 443 14.610 25.663 58.999 1.00 37.37 O ANISOU 8391 O HOH C 443 4733 4728 4738 11 -19 0 O HETATM 8392 O HOH C 444 -12.711 8.213 34.283 1.00 31.78 O ANISOU 8392 O HOH C 444 4069 3977 4028 6 -21 2 O HETATM 8393 O HOH C 445 -5.714 12.119 49.910 1.00 24.97 O ANISOU 8393 O HOH C 445 3195 3113 3178 -22 14 -10 O HETATM 8394 O HOH C 446 -23.048 15.435 34.931 1.00 41.34 O ANISOU 8394 O HOH C 446 5244 5206 5256 -10 -4 7 O HETATM 8395 O HOH C 447 -3.519 18.601 53.401 1.00 21.35 O ANISOU 8395 O HOH C 447 2761 2687 2665 59 -57 -18 O HETATM 8396 O HOH C 448 2.141 22.671 67.305 1.00 33.21 O ANISOU 8396 O HOH C 448 4219 4211 4189 6 -30 -14 O HETATM 8397 O HOH C 449 8.105 34.900 46.417 1.00 22.83 O ANISOU 8397 O HOH C 449 2871 2895 2908 -51 12 -26 O HETATM 8398 O HOH C 450 -18.528 27.872 63.795 1.00 30.57 O ANISOU 8398 O HOH C 450 3898 3893 3826 8 17 -18 O HETATM 8399 O HOH C 451 3.281 6.742 48.106 1.00 34.41 O ANISOU 8399 O HOH C 451 4354 4343 4375 -10 -30 19 O HETATM 8400 O HOH C 452 2.073 16.190 39.148 1.00 16.22 O ANISOU 8400 O HOH C 452 2169 2018 1978 4 -58 -58 O HETATM 8401 O HOH C 453 -2.654 19.477 33.602 1.00 35.87 O ANISOU 8401 O HOH C 453 4562 4544 4523 19 -14 7 O HETATM 8402 O HOH C 454 -6.364 37.998 69.451 1.00 46.76 O ANISOU 8402 O HOH C 454 5938 5891 5937 -8 4 -8 O HETATM 8403 O HOH C 455 -10.200 38.312 67.155 1.00 35.10 O ANISOU 8403 O HOH C 455 4470 4436 4429 7 0 9 O HETATM 8404 O HOH C 456 -15.491 36.493 45.559 1.00 24.94 O ANISOU 8404 O HOH C 456 3203 3127 3148 23 23 8 O HETATM 8405 O HOH C 457 -27.139 2.816 54.291 1.00 26.02 O ANISOU 8405 O HOH C 457 3299 3245 3341 1 -32 31 O HETATM 8406 O HOH C 458 -32.279 20.589 40.641 1.00 35.50 O ANISOU 8406 O HOH C 458 4471 4515 4504 -4 -12 -6 O HETATM 8407 O HOH C 459 -3.958 17.140 29.589 1.00 30.66 O ANISOU 8407 O HOH C 459 3912 3862 3875 -3 -10 11 O HETATM 8408 O HOH C 460 8.166 21.510 45.905 1.00 24.31 O ANISOU 8408 O HOH C 460 3108 3038 3093 -22 3 -41 O HETATM 8409 O HOH C 461 9.941 23.834 70.937 1.00 34.45 O ANISOU 8409 O HOH C 461 4402 4359 4329 -22 2 8 O HETATM 8410 O HOH C 462 -6.298 43.661 61.887 1.00 33.99 O ANISOU 8410 O HOH C 462 4342 4293 4281 -17 7 -42 O HETATM 8411 O HOH C 463 -22.607 34.803 52.228 1.00 18.51 O ANISOU 8411 O HOH C 463 2358 2405 2270 58 -88 48 O HETATM 8412 O HOH C 464 -21.679 6.865 50.524 1.00 26.69 O ANISOU 8412 O HOH C 464 3445 3288 3408 10 -28 -3 O HETATM 8413 O HOH C 465 -6.436 18.396 31.076 1.00 28.04 O ANISOU 8413 O HOH C 465 3600 3516 3537 -6 24 -23 O HETATM 8414 O HOH C 466 -23.590 7.640 58.396 1.00 37.94 O ANISOU 8414 O HOH C 466 4838 4790 4788 -15 -5 15 O HETATM 8415 O HOH C 467 -1.377 31.921 68.654 1.00 29.72 O ANISOU 8415 O HOH C 467 3838 3689 3765 -22 0 -7 O HETATM 8416 O HOH C 468 -3.981 41.981 63.720 1.00 21.88 O ANISOU 8416 O HOH C 468 2821 2741 2753 4 -51 8 O HETATM 8417 O HOH C 469 -12.866 8.314 55.289 1.00 24.94 O ANISOU 8417 O HOH C 469 3154 3161 3163 27 -45 16 O HETATM 8418 O HOH C 470 -20.890 32.774 61.766 1.00 20.33 O ANISOU 8418 O HOH C 470 2636 2631 2459 -46 5 15 O HETATM 8419 O HOH C 471 -19.353 6.776 52.282 1.00 24.51 O ANISOU 8419 O HOH C 471 3108 3127 3077 -12 -35 -21 O HETATM 8420 O HOH C 472 -6.618 15.872 52.975 1.00 12.91 O ANISOU 8420 O HOH C 472 1632 1805 1469 21 -37 -61 O HETATM 8421 O HOH C 473 -2.081 14.997 35.382 1.00 14.96 O ANISOU 8421 O HOH C 473 1923 1987 1775 7 0 -39 O HETATM 8422 O HOH C 474 12.523 28.252 61.171 1.00 29.87 O ANISOU 8422 O HOH C 474 3794 3759 3796 -16 -17 -24 O HETATM 8423 O HOH C 475 0.514 5.515 39.353 1.00 18.25 O ANISOU 8423 O HOH C 475 2378 2246 2310 -49 -55 -47 O HETATM 8424 O HOH C 476 -7.349 32.494 37.586 1.00 30.47 O ANISOU 8424 O HOH C 476 3880 3867 3830 -1 14 2 O HETATM 8425 O HOH C 477 -16.459 7.053 62.177 1.00 31.92 O ANISOU 8425 O HOH C 477 4085 4011 4034 4 -19 3 O HETATM 8426 O HOH C 478 -15.647 43.561 57.249 1.00 44.11 O ANISOU 8426 O HOH C 478 5639 5534 5588 6 4 4 O HETATM 8427 O HOH C 479 7.975 34.667 52.273 1.00 23.65 O ANISOU 8427 O HOH C 479 2969 2932 3086 -34 -14 5 O HETATM 8428 O HOH C 480 -29.912 17.192 44.274 1.00 20.84 O ANISOU 8428 O HOH C 480 2651 2580 2687 3 -30 -35 O HETATM 8429 O HOH C 481 -24.224 25.791 41.127 1.00 27.45 O ANISOU 8429 O HOH C 481 3539 3445 3446 17 -3 5 O HETATM 8430 O HOH C 482 -17.694 31.609 42.766 1.00 27.63 O ANISOU 8430 O HOH C 482 3536 3447 3517 12 6 -2 O HETATM 8431 O HOH C 483 -23.556 14.541 60.659 1.00 25.26 O ANISOU 8431 O HOH C 483 3235 3158 3205 -30 31 -46 O HETATM 8432 O HOH C 484 -28.753 11.944 37.434 1.00 41.74 O ANISOU 8432 O HOH C 484 5276 5272 5312 -2 4 2 O HETATM 8433 O HOH C 485 -20.455 36.130 47.814 1.00 27.55 O ANISOU 8433 O HOH C 485 3546 3480 3443 5 -19 42 O HETATM 8434 O HOH C 486 -21.544 6.844 43.100 1.00 37.37 O ANISOU 8434 O HOH C 486 4742 4698 4760 -8 25 -25 O HETATM 8435 O HOH C 487 -6.494 14.687 56.000 1.00 45.32 O ANISOU 8435 O HOH C 487 5747 5709 5766 6 -13 -5 O HETATM 8436 O HOH C 488 2.564 28.287 35.521 1.00 29.47 O ANISOU 8436 O HOH C 488 3744 3703 3749 5 11 -2 O HETATM 8437 O HOH C 489 -7.755 24.238 34.368 1.00 22.19 O ANISOU 8437 O HOH C 489 2859 2827 2744 -42 -10 -16 O HETATM 8438 O HOH C 490 -24.577 31.948 46.722 1.00 35.10 O ANISOU 8438 O HOH C 490 4471 4390 4476 -3 -10 4 O HETATM 8439 O HOH C 491 -20.242 33.104 65.686 1.00 42.37 O ANISOU 8439 O HOH C 491 5381 5354 5364 6 12 -8 O HETATM 8440 O HOH C 492 -30.217 21.864 42.946 1.00 27.94 O ANISOU 8440 O HOH C 492 3520 3479 3616 -10 -11 -21 O HETATM 8441 O HOH C 493 -12.780 40.013 43.833 1.00 33.39 O ANISOU 8441 O HOH C 493 4229 4209 4248 4 2 -1 O HETATM 8442 O HOH C 494 1.465 19.394 38.684 1.00 28.76 O ANISOU 8442 O HOH C 494 3714 3583 3629 -29 2 -25 O HETATM 8443 O HOH C 495 -22.873 9.319 36.588 1.00 36.17 O ANISOU 8443 O HOH C 495 4580 4566 4597 4 -9 -15 O HETATM 8444 O HOH C 496 5.000 42.792 57.471 1.00 33.94 O ANISOU 8444 O HOH C 496 4303 4286 4306 15 -39 -19 O HETATM 8445 O HOH C 497 -16.030 11.881 71.883 1.00 49.24 O ANISOU 8445 O HOH C 497 6260 6208 6242 -4 -4 6 O HETATM 8446 O HOH C 498 0.056 7.894 48.523 1.00 22.56 O ANISOU 8446 O HOH C 498 2900 2796 2875 15 1 -5 O HETATM 8447 O HOH C 499 6.187 23.074 51.008 1.00 29.18 O ANISOU 8447 O HOH C 499 3729 3620 3738 9 -52 -36 O HETATM 8448 O HOH C 500 -27.732 19.783 34.639 1.00 29.35 O ANISOU 8448 O HOH C 500 3713 3753 3686 3 -49 10 O HETATM 8449 O HOH C 501 -16.790 28.053 37.163 1.00 37.84 O ANISOU 8449 O HOH C 501 4798 4790 4792 -6 -7 -11 O HETATM 8450 O HOH C 502 -22.252 40.268 58.065 1.00 19.02 O ANISOU 8450 O HOH C 502 2414 2441 2371 95 17 -30 O HETATM 8451 O HOH C 503 1.839 25.615 68.586 1.00 41.95 O ANISOU 8451 O HOH C 503 5325 5293 5319 5 -11 9 O HETATM 8452 O HOH C 504 -26.382 13.612 59.853 1.00 46.08 O ANISOU 8452 O HOH C 504 5834 5807 5868 -8 4 -21 O HETATM 8453 O HOH C 505 -5.939 20.662 59.074 1.00 21.97 O ANISOU 8453 O HOH C 505 2895 2795 2656 -3 -35 -8 O HETATM 8454 O HOH C 506 -2.245 40.088 40.138 1.00 52.90 O ANISOU 8454 O HOH C 506 6723 6660 6718 -3 -1 3 O HETATM 8455 O HOH C 507 -11.456 32.082 43.415 1.00 11.47 O ANISOU 8455 O HOH C 507 1681 1358 1320 -14 -111 -80 O HETATM 8456 O HOH C 508 -3.104 4.799 35.578 1.00 31.04 O ANISOU 8456 O HOH C 508 3988 3869 3936 -17 5 4 O HETATM 8457 O HOH C 509 5.314 32.738 60.828 1.00 35.21 O ANISOU 8457 O HOH C 509 4487 4421 4469 1 -9 0 O HETATM 8458 O HOH C 510 -0.437 40.197 44.967 1.00 28.59 O ANISOU 8458 O HOH C 510 3698 3541 3623 -8 -2 -14 O HETATM 8459 O HOH C 511 -13.761 32.784 41.932 1.00 16.79 O ANISOU 8459 O HOH C 511 2244 2023 2110 -16 -32 41 O HETATM 8460 O HOH C 512 -9.942 41.601 64.909 1.00 19.06 O ANISOU 8460 O HOH C 512 2482 2371 2390 17 -42 -6 O HETATM 8461 O HOH C 513 -3.310 15.064 60.218 1.00 24.45 O ANISOU 8461 O HOH C 513 3120 3059 3111 23 -13 -11 O HETATM 8462 O HOH C 514 6.509 37.959 42.805 1.00 46.68 O ANISOU 8462 O HOH C 514 5937 5862 5939 -6 17 9 O HETATM 8463 O HOH C 515 -29.154 14.872 37.277 1.00 22.90 O ANISOU 8463 O HOH C 515 2859 2987 2856 -40 -30 -18 O HETATM 8464 O HOH C 516 -16.778 6.742 56.087 1.00 25.45 O ANISOU 8464 O HOH C 516 3256 3212 3204 25 -12 35 O HETATM 8465 O HOH C 517 2.552 35.234 39.839 1.00 32.33 O ANISOU 8465 O HOH C 517 4114 4062 4110 -7 7 3 O HETATM 8466 O HOH C 518 -18.368 3.705 44.161 1.00 27.07 O ANISOU 8466 O HOH C 518 3488 3334 3464 -8 16 -30 O HETATM 8467 O HOH C 519 -6.781 0.153 33.535 1.00 39.50 O ANISOU 8467 O HOH C 519 5036 4986 4987 -3 -10 -1 O HETATM 8468 O HOH C 520 -0.523 19.668 41.054 1.00 22.73 O ANISOU 8468 O HOH C 520 2873 2934 2829 32 26 50 O HETATM 8469 O HOH C 521 -0.308 35.341 38.905 1.00 26.50 O ANISOU 8469 O HOH C 521 3411 3324 3334 -25 31 -19 O HETATM 8470 O HOH C 522 -28.552 19.288 57.887 1.00 44.13 O ANISOU 8470 O HOH C 522 5591 5575 5600 5 -13 1 O HETATM 8471 O HOH C 523 -19.138 40.108 63.091 1.00 30.86 O ANISOU 8471 O HOH C 523 3925 3901 3901 -4 -21 -14 O HETATM 8472 O HOH C 524 -21.274 27.688 57.419 1.00 18.82 O ANISOU 8472 O HOH C 524 2403 2430 2319 -9 40 -21 O HETATM 8473 O HOH C 525 -6.135 12.815 52.775 1.00 29.67 O ANISOU 8473 O HOH C 525 3764 3754 3757 -15 -14 3 O HETATM 8474 O HOH C 526 8.392 29.677 65.768 1.00 36.92 O ANISOU 8474 O HOH C 526 4712 4667 4650 -25 -8 -7 O HETATM 8475 O HOH C 527 -3.834 16.921 64.285 1.00 28.15 O ANISOU 8475 O HOH C 527 3568 3566 3560 3 8 31 O HETATM 8476 O HOH C 528 10.011 37.356 55.509 1.00 39.60 O ANISOU 8476 O HOH C 528 5027 5002 5017 -11 -12 -2 O HETATM 8477 O HOH C 529 -18.893 37.120 63.245 1.00 24.54 O ANISOU 8477 O HOH C 529 3131 3081 3113 38 -22 -31 O HETATM 8478 O HOH C 530 -8.340 13.420 57.783 1.00 49.74 O ANISOU 8478 O HOH C 530 6326 6256 6318 3 -9 1 O HETATM 8479 O HOH C 531 0.199 31.314 35.503 1.00 25.05 O ANISOU 8479 O HOH C 531 3219 3174 3124 -4 -14 5 O HETATM 8480 O HOH C 532 -23.426 7.458 39.360 1.00 45.36 O ANISOU 8480 O HOH C 532 5761 5704 5770 5 -6 -9 O HETATM 8481 O HOH C 533 -6.492 9.926 33.294 1.00 26.37 O ANISOU 8481 O HOH C 533 3353 3263 3401 12 -23 26 O HETATM 8482 O HOH C 534 7.142 22.292 54.818 1.00 28.87 O ANISOU 8482 O HOH C 534 3680 3672 3617 -25 -3 -15 O HETATM 8483 O HOH C 535 -9.386 7.226 34.452 1.00 36.25 O ANISOU 8483 O HOH C 535 4601 4578 4594 -14 7 -9 O HETATM 8484 O HOH C 536 -5.754 18.503 55.315 1.00 14.43 O ANISOU 8484 O HOH C 536 1899 1838 1744 48 -36 30 O HETATM 8485 O HOH C 537 -31.419 20.840 45.290 1.00 40.06 O ANISOU 8485 O HOH C 537 5064 5068 5090 7 -12 -20 O HETATM 8486 O HOH C 538 -23.223 3.171 56.096 1.00 44.24 O ANISOU 8486 O HOH C 538 5609 5563 5636 9 -2 8 O HETATM 8487 O HOH C 539 -11.338 3.621 35.423 1.00 34.61 O ANISOU 8487 O HOH C 539 4416 4354 4381 21 -5 -14 O HETATM 8488 O HOH C 540 -24.347 33.366 49.057 1.00 27.10 O ANISOU 8488 O HOH C 540 3432 3423 3442 14 -19 24 O HETATM 8489 O HOH C 541 6.188 20.142 51.378 1.00 28.50 O ANISOU 8489 O HOH C 541 3676 3587 3565 17 -9 -9 O HETATM 8490 O HOH C 542 -3.839 15.219 55.368 1.00 28.02 O ANISOU 8490 O HOH C 542 3629 3559 3458 6 15 -30 O HETATM 8491 O HOH C 543 3.837 41.508 59.758 1.00 30.76 O ANISOU 8491 O HOH C 543 3932 3830 3926 -16 -21 3 O HETATM 8492 O HOH C 544 -15.316 12.467 35.853 1.00 34.54 O ANISOU 8492 O HOH C 544 4398 4365 4361 -2 2 -2 O HETATM 8493 O HOH C 545 -25.659 14.669 34.377 1.00 45.48 O ANISOU 8493 O HOH C 545 5784 5745 5750 9 2 -4 O HETATM 8494 O HOH C 546 3.769 24.832 66.673 1.00 41.34 O ANISOU 8494 O HOH C 546 5259 5191 5258 8 3 13 O HETATM 8495 O HOH C 547 -26.602 11.188 63.323 1.00 38.77 O ANISOU 8495 O HOH C 547 4899 4896 4936 1 -14 11 O HETATM 8496 O HOH C 548 -17.541 41.577 51.651 1.00 45.28 O ANISOU 8496 O HOH C 548 5767 5702 5736 7 -5 5 O HETATM 8497 O HOH C 549 -1.230 17.462 34.715 1.00 26.66 O ANISOU 8497 O HOH C 549 3366 3306 3456 14 10 3 O HETATM 8498 O HOH C 550 -23.438 7.676 65.716 1.00 33.30 O ANISOU 8498 O HOH C 550 4298 4164 4190 -6 -21 7 O HETATM 8499 O HOH C 551 7.704 35.774 49.123 1.00 23.99 O ANISOU 8499 O HOH C 551 3098 3013 3004 -66 -33 -21 O HETATM 8500 O HOH C 552 2.503 31.419 63.552 1.00 30.42 O ANISOU 8500 O HOH C 552 3868 3825 3867 20 13 -16 O HETATM 8501 O HOH C 553 -6.228 21.199 31.941 1.00 30.27 O ANISOU 8501 O HOH C 553 3837 3789 3876 11 7 6 O HETATM 8502 O HOH C 554 -7.314 16.001 58.630 1.00 47.08 O ANISOU 8502 O HOH C 554 5966 5926 5996 10 -6 10 O HETATM 8503 O HOH C 555 -16.550 8.541 33.486 1.00 41.03 O ANISOU 8503 O HOH C 555 5198 5182 5210 5 -4 2 O HETATM 8504 O HOH C 556 -4.095 16.611 69.764 1.00 41.71 O ANISOU 8504 O HOH C 556 5285 5257 5305 13 -2 2 O HETATM 8505 O HOH C 557 -27.942 24.716 68.800 1.00 33.67 O ANISOU 8505 O HOH C 557 4291 4229 4273 27 5 6 O HETATM 8506 O HOH C 558 6.547 40.543 57.278 1.00 34.29 O ANISOU 8506 O HOH C 558 4379 4279 4372 -5 -19 -4 O HETATM 8507 O HOH C 559 3.263 42.631 52.876 1.00 45.78 O ANISOU 8507 O HOH C 559 5819 5750 5825 -8 7 -1 O HETATM 8508 O HOH C 560 1.093 42.844 51.137 1.00 33.61 O ANISOU 8508 O HOH C 560 4328 4245 4200 -25 3 2 O HETATM 8509 O HOH C 561 -21.161 13.577 35.840 1.00 25.18 O ANISOU 8509 O HOH C 561 3230 3167 3171 -7 18 -18 O HETATM 8510 O HOH C 562 -3.059 6.371 37.815 1.00 23.94 O ANISOU 8510 O HOH C 562 3115 2975 3005 -1 -26 -10 O HETATM 8511 O HOH C 563 -24.796 28.246 54.699 1.00 43.44 O ANISOU 8511 O HOH C 563 5532 5472 5503 6 8 -3 O HETATM 8512 O HOH C 564 -27.687 14.730 65.742 1.00 41.43 O ANISOU 8512 O HOH C 564 5266 5239 5234 -9 -6 -4 O HETATM 8513 O HOH C 565 -7.345 43.853 46.419 1.00 33.92 O ANISOU 8513 O HOH C 565 4320 4262 4307 -2 12 -8 O HETATM 8514 O HOH C 566 3.679 33.831 62.731 1.00 39.33 O ANISOU 8514 O HOH C 566 5010 4940 4995 8 2 -8 O HETATM 8515 O HOH C 567 -6.124 28.965 70.779 1.00 40.35 O ANISOU 8515 O HOH C 567 5152 5082 5098 -11 -12 -4 O HETATM 8516 O HOH C 568 -16.973 15.951 35.956 1.00 29.55 O ANISOU 8516 O HOH C 568 3714 3771 3743 -8 -29 -11 O HETATM 8517 O HOH C 569 -20.376 39.742 51.250 1.00 23.50 O ANISOU 8517 O HOH C 569 3076 2872 2980 -2 3 -20 O HETATM 8518 O HOH C 570 -1.997 14.819 64.195 1.00 33.65 O ANISOU 8518 O HOH C 570 4283 4250 4251 -19 -4 -3 O HETATM 8519 O HOH C 571 -20.168 42.008 58.732 1.00 16.59 O ANISOU 8519 O HOH C 571 2098 1995 2212 19 -79 -19 O HETATM 8520 O HOH C 572 -25.482 26.305 61.769 1.00 43.00 O ANISOU 8520 O HOH C 572 5477 5399 5460 -14 7 15 O HETATM 8521 O HOH C 573 -17.387 9.338 67.856 1.00 45.75 O ANISOU 8521 O HOH C 573 5801 5748 5834 -5 -10 2 O HETATM 8522 O HOH C 574 -10.848 27.990 33.649 1.00 40.01 O ANISOU 8522 O HOH C 574 5099 5057 5046 9 -1 -1 O HETATM 8523 O HOH C 575 -28.570 20.534 51.827 1.00 31.27 O ANISOU 8523 O HOH C 575 3982 4007 3891 -24 -15 9 O HETATM 8524 O HOH C 576 7.546 38.302 50.343 1.00 43.63 O ANISOU 8524 O HOH C 576 5539 5502 5537 -5 5 0 O HETATM 8525 O HOH C 577 -31.631 18.633 42.555 1.00 51.17 O ANISOU 8525 O HOH C 577 6481 6433 6527 -10 12 0 O HETATM 8526 O HOH C 578 8.253 22.918 48.807 1.00 29.73 O ANISOU 8526 O HOH C 578 3777 3717 3801 -6 -12 -7 O HETATM 8527 O HOH C 579 -7.722 29.868 36.793 1.00 26.38 O ANISOU 8527 O HOH C 579 3367 3371 3284 12 8 27 O HETATM 8528 O HOH C 580 -5.180 25.937 74.838 1.00 36.62 O ANISOU 8528 O HOH C 580 4693 4622 4598 1 -11 -4 O HETATM 8529 O HOH C 581 -11.561 12.463 57.810 1.00 19.29 O ANISOU 8529 O HOH C 581 2572 2365 2393 -56 -27 -39 O HETATM 8530 O HOH C 582 -8.375 29.478 34.085 1.00 31.92 O ANISOU 8530 O HOH C 582 4082 4034 4010 17 -18 -3 O HETATM 8531 O HOH C 583 -5.996 4.833 40.328 1.00 35.90 O ANISOU 8531 O HOH C 583 4512 4585 4543 -2 -6 19 O HETATM 8532 O HOH C 584 10.350 22.175 55.529 1.00 28.14 O ANISOU 8532 O HOH C 584 3616 3497 3578 8 -26 -2 O HETATM 8533 O HOH C 585 -22.028 26.632 61.184 1.00 43.60 O ANISOU 8533 O HOH C 585 5504 5503 5560 -21 -12 13 O HETATM 8534 O HOH C 586 -23.822 32.461 53.285 1.00 24.99 O ANISOU 8534 O HOH C 586 3137 3176 3182 1 -32 -22 O HETATM 8535 O HOH C 587 -21.647 5.573 66.076 1.00 53.09 O ANISOU 8535 O HOH C 587 6742 6700 6732 -4 -1 4 O HETATM 8536 O HOH C 588 -19.981 7.146 59.298 1.00 34.74 O ANISOU 8536 O HOH C 588 4445 4359 4395 -2 -18 6 O HETATM 8537 O HOH C 589 -17.335 42.484 54.221 1.00 30.62 O ANISOU 8537 O HOH C 589 3856 3848 3931 -3 16 -13 O HETATM 8538 O HOH C 590 -18.384 25.910 37.964 1.00 50.78 O ANISOU 8538 O HOH C 590 6466 6398 6432 1 0 -9 O HETATM 8539 O HOH C 591 -12.229 7.436 52.742 1.00 30.92 O ANISOU 8539 O HOH C 591 3929 3877 3943 10 -29 5 O HETATM 8540 O HOH C 592 -27.025 30.748 46.286 1.00 33.15 O ANISOU 8540 O HOH C 592 4221 4137 4236 -2 -7 -1 O HETATM 8541 O HOH C 593 -9.057 45.381 50.058 1.00 29.16 O ANISOU 8541 O HOH C 593 3764 3571 3743 -5 1 10 O HETATM 8542 O HOH C 594 -6.718 5.380 42.903 1.00 40.42 O ANISOU 8542 O HOH C 594 5119 5077 5162 11 -20 9 O HETATM 8543 O HOH C 595 -10.294 32.345 69.262 1.00 41.40 O ANISOU 8543 O HOH C 595 5246 5236 5250 5 7 -20 O HETATM 8544 O HOH C 596 -20.100 22.317 70.188 1.00 33.00 O ANISOU 8544 O HOH C 596 4203 4194 4142 10 -7 29 O HETATM 8545 O HOH C 597 -8.181 34.499 41.389 1.00 35.72 O ANISOU 8545 O HOH C 597 4576 4497 4498 -5 -16 -2 O HETATM 8546 O HOH C 598 -18.587 16.272 70.049 1.00 42.74 O ANISOU 8546 O HOH C 598 5424 5410 5406 -4 -5 -2 O HETATM 8547 O HOH C 599 -22.137 25.513 58.673 1.00 37.00 O ANISOU 8547 O HOH C 599 4688 4656 4714 12 -6 10 O HETATM 8548 O HOH C 600 -30.941 24.637 41.453 1.00 31.48 O ANISOU 8548 O HOH C 600 3968 3985 4010 3 -13 2 O HETATM 8549 O HOH C 601 -28.944 26.687 41.272 1.00 36.32 O ANISOU 8549 O HOH C 601 4629 4557 4613 20 -15 4 O HETATM 8550 O HOH C 602 3.629 30.599 34.436 1.00 63.91 O ANISOU 8550 O HOH C 602 8105 8073 8104 0 -1 2 O HETATM 8551 O HOH C 603 -20.666 38.807 48.682 1.00 28.92 O ANISOU 8551 O HOH C 603 3651 3676 3662 8 7 -34 O HETATM 8552 O HOH C 604 -3.963 12.611 54.518 1.00 25.57 O ANISOU 8552 O HOH C 604 3279 3219 3219 -5 26 4 O HETATM 8553 O HOH C 605 2.197 30.374 68.007 1.00 51.69 O ANISOU 8553 O HOH C 605 6564 6514 6563 -4 -3 0 O HETATM 8554 O HOH C 606 2.584 27.868 70.070 1.00 37.56 O ANISOU 8554 O HOH C 606 4781 4748 4740 12 15 -4 O HETATM 8555 O HOH C 607 -21.066 24.185 65.084 1.00 33.60 O ANISOU 8555 O HOH C 607 4294 4231 4243 4 9 -2 O HETATM 8556 O HOH C 608 -6.455 46.414 61.083 1.00 15.88 O ANISOU 8556 O HOH C 608 2343 1790 1898 15 -38 24 O HETATM 8557 O HOH C 609 -28.654 23.192 50.413 1.00 41.42 O ANISOU 8557 O HOH C 609 5238 5208 5290 3 0 -22 O HETATM 8558 O HOH C 610 -3.777 21.981 33.111 1.00 29.97 O ANISOU 8558 O HOH C 610 3855 3781 3749 11 -9 -17 O HETATM 8559 O HOH C 611 -3.739 44.522 62.474 1.00 38.28 O ANISOU 8559 O HOH C 611 4877 4795 4874 8 -14 -3 O HETATM 8560 O HOH C 612 -8.605 5.417 47.376 1.00 28.14 O ANISOU 8560 O HOH C 612 3554 3640 3498 -57 -51 -7 O HETATM 8561 O HOH C 613 -11.893 38.400 69.331 1.00 40.42 O ANISOU 8561 O HOH C 613 5136 5060 5160 3 4 4 O HETATM 8562 O HOH C 614 4.181 32.573 36.323 1.00 34.35 O ANISOU 8562 O HOH C 614 4345 4341 4368 1 -7 17 O HETATM 8563 O HOH C 615 -1.457 44.022 50.373 1.00 43.53 O ANISOU 8563 O HOH C 615 5558 5464 5518 -6 22 3 O HETATM 8564 O HOH C 616 -13.992 5.907 55.980 1.00 46.57 O ANISOU 8564 O HOH C 616 5918 5873 5902 5 -7 2 O HETATM 8565 O HOH C 617 -30.278 18.775 35.150 1.00 34.15 O ANISOU 8565 O HOH C 617 4322 4341 4312 -4 -8 17 O HETATM 8566 O HOH C 618 -29.793 28.074 43.650 1.00 27.04 O ANISOU 8566 O HOH C 618 3451 3353 3471 33 -34 -5 O HETATM 8567 O HOH C 619 -32.274 27.224 44.983 1.00 33.88 O ANISOU 8567 O HOH C 619 4319 4242 4312 -12 -25 2 O HETATM 8568 O HOH C 620 -4.711 13.350 58.580 1.00 39.86 O ANISOU 8568 O HOH C 620 5051 5031 5063 -7 -8 2 O HETATM 8569 O HOH C 621 -7.003 25.518 32.000 1.00 35.00 O ANISOU 8569 O HOH C 621 4467 4434 4397 -7 4 -9 O HETATM 8570 O HOH C 622 -8.473 43.380 63.462 1.00 31.47 O ANISOU 8570 O HOH C 622 4012 3931 4013 8 -15 -3 O HETATM 8571 O HOH C 623 -4.675 41.277 66.359 1.00 31.68 O ANISOU 8571 O HOH C 623 4055 3987 3997 14 -9 -26 O HETATM 8572 O HOH C 624 3.826 30.369 65.754 1.00 38.43 O ANISOU 8572 O HOH C 624 4892 4849 4861 10 -9 -4 O HETATM 8573 O HOH C 625 -28.665 32.044 44.488 1.00 40.28 O ANISOU 8573 O HOH C 625 5124 5053 5129 4 3 0 O HETATM 8574 O HOH C 626 -30.355 26.203 53.418 1.00 51.38 O ANISOU 8574 O HOH C 626 6534 6457 6532 4 0 -2 O HETATM 8575 O HOH C 627 -33.066 24.929 43.355 1.00 42.21 O ANISOU 8575 O HOH C 627 5357 5326 5354 -8 -25 -9 O HETATM 8576 O HOH C 628 -11.356 7.636 59.151 1.00 46.16 O ANISOU 8576 O HOH C 628 5864 5822 5853 7 -4 -4 O HETATM 8577 O HOH C 629 1.593 45.963 50.575 1.00 33.75 O ANISOU 8577 O HOH C 629 4287 4246 4289 1 7 5 O HETATM 8578 O HOH C 630 -13.227 5.453 58.638 1.00 43.02 O ANISOU 8578 O HOH C 630 5473 5404 5471 7 -3 7 O HETATM 8579 O HOH D 401 18.189 -8.056 1.605 1.00 31.24 O ANISOU 8579 O HOH D 401 3953 3911 4006 -19 24 -14 O HETATM 8580 O HOH D 402 18.738 -4.001 5.491 1.00 49.93 O ANISOU 8580 O HOH D 402 6350 6278 6343 3 11 -3 O HETATM 8581 O HOH D 403 -4.553 23.001 -14.480 1.00 25.92 O ANISOU 8581 O HOH D 403 3356 3231 3262 18 -4 -17 O HETATM 8582 O HOH D 404 -4.425 23.845 -18.268 1.00 22.00 O ANISOU 8582 O HOH D 404 2837 2727 2794 19 -52 38 O HETATM 8583 O HOH D 405 17.099 -2.378 -3.726 1.00 20.79 O ANISOU 8583 O HOH D 405 2635 2673 2590 59 25 -12 O HETATM 8584 O HOH D 406 5.520 0.065 1.001 1.00 11.41 O ANISOU 8584 O HOH D 406 1573 1450 1313 -22 -53 -25 O HETATM 8585 O HOH D 407 -13.654 2.440 3.798 1.00 28.20 O ANISOU 8585 O HOH D 407 3609 3559 3545 -34 -39 40 O HETATM 8586 O HOH D 408 16.237 -7.219 13.386 1.00 20.38 O ANISOU 8586 O HOH D 408 2660 2480 2605 25 29 -17 O HETATM 8587 O HOH D 409 10.069 -14.512 6.225 1.00 17.02 O ANISOU 8587 O HOH D 409 2198 2100 2167 102 -14 -23 O HETATM 8588 O HOH D 410 -1.876 17.919 -18.545 1.00 15.35 O ANISOU 8588 O HOH D 410 1908 2063 1859 29 -20 9 O HETATM 8589 O HOH D 411 4.419 -3.032 17.769 1.00 18.98 O ANISOU 8589 O HOH D 411 2480 2425 2305 24 -11 24 O HETATM 8590 O HOH D 412 15.881 12.891 11.122 1.00 30.03 O ANISOU 8590 O HOH D 412 3788 3813 3807 -13 -17 -6 O HETATM 8591 O HOH D 413 7.380 -4.637 -8.207 1.00 23.97 O ANISOU 8591 O HOH D 413 3092 3013 3004 36 -49 1 O HETATM 8592 O HOH D 414 -0.658 10.678 -8.764 1.00 17.07 O ANISOU 8592 O HOH D 414 2214 2160 2112 -35 42 28 O HETATM 8593 O HOH D 415 6.819 17.520 -15.436 1.00 36.35 O ANISOU 8593 O HOH D 415 4629 4587 4594 -2 -3 12 O HETATM 8594 O HOH D 416 17.053 2.998 1.017 1.00 9.99 O ANISOU 8594 O HOH D 416 1416 1284 1096 -14 -75 5 O HETATM 8595 O HOH D 417 19.605 15.046 14.183 1.00 39.94 O ANISOU 8595 O HOH D 417 5067 5045 5062 20 -4 7 O HETATM 8596 O HOH D 418 8.222 -1.845 -11.166 1.00 16.90 O ANISOU 8596 O HOH D 418 2150 2142 2129 27 -66 22 O HETATM 8597 O HOH D 419 13.420 -1.189 -12.738 1.00 29.90 O ANISOU 8597 O HOH D 419 3809 3728 3825 3 -21 9 O HETATM 8598 O HOH D 420 5.925 -3.484 21.104 1.00 31.39 O ANISOU 8598 O HOH D 420 3977 4002 3947 -18 26 1 O HETATM 8599 O HOH D 421 12.431 -8.689 -3.148 1.00 20.28 O ANISOU 8599 O HOH D 421 2636 2587 2483 50 -53 -14 O HETATM 8600 O HOH D 422 -3.465 15.575 2.397 1.00 20.49 O ANISOU 8600 O HOH D 422 2617 2635 2532 16 42 -13 O HETATM 8601 O HOH D 423 -4.819 -13.208 -5.056 1.00 33.18 O ANISOU 8601 O HOH D 423 4226 4172 4208 9 -1 10 O HETATM 8602 O HOH D 424 24.197 -0.145 -0.330 1.00 27.14 O ANISOU 8602 O HOH D 424 3468 3373 3472 35 -12 0 O HETATM 8603 O HOH D 425 1.261 7.832 -16.982 1.00 35.28 O ANISOU 8603 O HOH D 425 4460 4488 4457 1 -1 -3 O HETATM 8604 O HOH D 426 -4.909 13.220 2.174 1.00 20.88 O ANISOU 8604 O HOH D 426 2703 2669 2560 -4 2 29 O HETATM 8605 O HOH D 427 22.206 3.327 7.343 1.00 25.76 O ANISOU 8605 O HOH D 427 3207 3323 3257 -29 -2 49 O HETATM 8606 O HOH D 428 1.276 6.160 15.876 1.00 28.37 O ANISOU 8606 O HOH D 428 3618 3625 3538 23 -9 -23 O HETATM 8607 O HOH D 429 3.582 10.492 -20.582 1.00 44.81 O ANISOU 8607 O HOH D 429 5689 5658 5677 6 6 -9 O HETATM 8608 O HOH D 430 -1.268 8.653 2.754 1.00 25.04 O ANISOU 8608 O HOH D 430 3153 3184 3178 31 32 48 O HETATM 8609 O HOH D 431 9.255 -14.427 14.473 1.00 28.69 O ANISOU 8609 O HOH D 431 3651 3625 3626 -19 6 -31 O HETATM 8610 O HOH D 432 -17.318 2.800 17.559 1.00 38.09 O ANISOU 8610 O HOH D 432 4815 4829 4827 5 16 9 O HETATM 8611 O HOH D 433 -3.557 16.047 -17.496 1.00 12.02 O ANISOU 8611 O HOH D 433 1536 1667 1363 -15 -7 65 O HETATM 8612 O HOH D 434 -2.680 2.053 23.973 1.00 30.31 O ANISOU 8612 O HOH D 434 3850 3843 3821 5 6 -15 O HETATM 8613 O HOH D 435 -11.974 -7.838 -0.583 1.00 23.56 O ANISOU 8613 O HOH D 435 2923 2958 3072 -42 -38 13 O HETATM 8614 O HOH D 436 14.849 -3.898 -5.409 1.00 23.58 O ANISOU 8614 O HOH D 436 3052 2981 2925 4 19 -12 O HETATM 8615 O HOH D 437 11.939 -0.447 15.413 1.00 22.68 O ANISOU 8615 O HOH D 437 2892 2876 2848 -47 -15 4 O HETATM 8616 O HOH D 438 27.933 8.549 0.944 1.00 30.90 O ANISOU 8616 O HOH D 438 3937 3900 3902 5 -26 15 O HETATM 8617 O HOH D 439 9.471 -2.483 21.861 1.00 29.20 O ANISOU 8617 O HOH D 439 3696 3711 3687 1 -21 -5 O HETATM 8618 O HOH D 440 2.994 16.824 -19.837 1.00 38.45 O ANISOU 8618 O HOH D 440 4902 4837 4870 -6 31 -18 O HETATM 8619 O HOH D 441 10.621 20.835 7.740 1.00 27.95 O ANISOU 8619 O HOH D 441 3583 3511 3525 38 -5 -32 O HETATM 8620 O HOH D 442 -11.077 -7.882 -6.405 1.00 24.07 O ANISOU 8620 O HOH D 442 3031 3007 3107 -61 5 36 O HETATM 8621 O HOH D 443 6.390 -13.388 12.342 1.00 17.89 O ANISOU 8621 O HOH D 443 2386 2330 2081 33 2 -11 O HETATM 8622 O HOH D 444 -3.625 7.760 -12.887 1.00 41.18 O ANISOU 8622 O HOH D 444 5261 5146 5240 -5 7 3 O HETATM 8623 O HOH D 445 21.696 2.349 -5.751 1.00 24.82 O ANISOU 8623 O HOH D 445 3166 3099 3167 -3 -11 -14 O HETATM 8624 O HOH D 446 -4.263 19.344 -2.719 1.00 20.56 O ANISOU 8624 O HOH D 446 2657 2548 2608 19 -21 -4 O HETATM 8625 O HOH D 447 10.082 0.937 16.862 1.00 42.34 O ANISOU 8625 O HOH D 447 5379 5349 5361 7 10 15 O HETATM 8626 O HOH D 448 -4.226 -5.642 -13.163 1.00 28.02 O ANISOU 8626 O HOH D 448 3538 3534 3572 -4 -37 -41 O HETATM 8627 O HOH D 449 17.460 4.258 10.318 1.00 23.49 O ANISOU 8627 O HOH D 449 3034 2966 2925 -14 -13 -76 O HETATM 8628 O HOH D 450 -1.744 8.498 26.533 1.00 19.91 O ANISOU 8628 O HOH D 450 2504 2528 2535 -27 -36 -48 O HETATM 8629 O HOH D 451 13.407 1.743 14.643 1.00 23.84 O ANISOU 8629 O HOH D 451 3050 3052 2957 -23 -20 51 O HETATM 8630 O HOH D 452 3.559 -18.803 1.977 1.00 41.62 O ANISOU 8630 O HOH D 452 5279 5209 5326 -7 12 2 O HETATM 8631 O HOH D 453 11.183 -4.997 -6.918 1.00 16.47 O ANISOU 8631 O HOH D 453 2133 2172 1953 17 -27 -38 O HETATM 8632 O HOH D 454 3.134 -3.487 15.400 1.00 17.02 O ANISOU 8632 O HOH D 454 2246 2222 1999 27 -59 49 O HETATM 8633 O HOH D 455 -4.353 11.168 -12.304 1.00 17.04 O ANISOU 8633 O HOH D 455 2172 2223 2078 -7 38 72 O HETATM 8634 O HOH D 456 22.742 8.734 10.986 1.00 27.25 O ANISOU 8634 O HOH D 456 3399 3476 3480 16 -32 -4 O HETATM 8635 O HOH D 457 -10.651 -12.379 8.657 1.00 31.55 O ANISOU 8635 O HOH D 457 3966 4011 4011 12 23 15 O HETATM 8636 O HOH D 458 -11.205 2.771 0.671 1.00 53.05 O ANISOU 8636 O HOH D 458 6736 6681 6739 -12 0 10 O HETATM 8637 O HOH D 459 -7.399 20.532 -3.623 1.00 37.93 O ANISOU 8637 O HOH D 459 4796 4778 4840 -5 6 -2 O HETATM 8638 O HOH D 460 -9.186 4.288 15.291 1.00 31.18 O ANISOU 8638 O HOH D 460 3925 3984 3938 12 -7 21 O HETATM 8639 O HOH D 461 14.030 24.030 -3.695 1.00 31.57 O ANISOU 8639 O HOH D 461 3989 3971 4035 -18 10 2 O HETATM 8640 O HOH D 462 3.324 -8.542 -7.804 1.00 19.61 O ANISOU 8640 O HOH D 462 2556 2483 2412 -46 -20 31 O HETATM 8641 O HOH D 463 -12.339 -5.693 -2.676 1.00 28.74 O ANISOU 8641 O HOH D 463 3663 3581 3675 -11 10 9 O HETATM 8642 O HOH D 464 -4.498 -8.138 -11.768 1.00 32.90 O ANISOU 8642 O HOH D 464 4208 4108 4185 -10 -10 -13 O HETATM 8643 O HOH D 465 22.563 21.841 -4.467 1.00 27.12 O ANISOU 8643 O HOH D 465 3441 3433 3431 -35 -4 -4 O HETATM 8644 O HOH D 466 4.425 17.815 -16.629 1.00 50.58 O ANISOU 8644 O HOH D 466 6426 6378 6415 -1 3 -3 O HETATM 8645 O HOH D 467 18.590 -3.666 -1.868 1.00 24.46 O ANISOU 8645 O HOH D 467 3156 3170 2969 -32 -8 8 O HETATM 8646 O HOH D 468 -9.136 1.300 16.731 1.00 54.50 O ANISOU 8646 O HOH D 468 6910 6866 6932 -1 5 -5 O HETATM 8647 O HOH D 469 14.693 -3.799 -0.804 1.00 12.51 O ANISOU 8647 O HOH D 469 1620 1535 1596 33 -53 -33 O HETATM 8648 O HOH D 470 6.593 14.875 -19.512 1.00 49.70 O ANISOU 8648 O HOH D 470 6334 6239 6310 -3 1 -8 O HETATM 8649 O HOH D 471 25.712 11.645 -0.038 1.00 28.37 O ANISOU 8649 O HOH D 471 3545 3584 3651 -11 -5 12 O HETATM 8650 O HOH D 472 17.698 4.250 -13.072 1.00 34.24 O ANISOU 8650 O HOH D 472 4381 4308 4320 25 -9 -42 O HETATM 8651 O HOH D 473 3.400 -11.045 17.422 1.00 34.75 O ANISOU 8651 O HOH D 473 4408 4374 4421 -1 0 -10 O HETATM 8652 O HOH D 474 28.718 11.208 -7.550 1.00 37.63 O ANISOU 8652 O HOH D 474 4777 4743 4777 -26 -1 -6 O HETATM 8653 O HOH D 475 11.867 5.910 -18.432 1.00 33.87 O ANISOU 8653 O HOH D 475 4293 4237 4338 4 33 12 O HETATM 8654 O HOH D 476 1.627 11.404 2.857 1.00 12.25 O ANISOU 8654 O HOH D 476 1527 1699 1429 50 -16 162 O HETATM 8655 O HOH D 477 -0.401 10.469 6.811 1.00 37.26 O ANISOU 8655 O HOH D 477 4758 4666 4732 -8 9 7 O HETATM 8656 O HOH D 478 21.646 0.548 14.273 1.00 48.51 O ANISOU 8656 O HOH D 478 6164 6106 6160 6 -9 -2 O HETATM 8657 O HOH D 479 23.566 22.793 2.355 1.00 25.08 O ANISOU 8657 O HOH D 479 3187 3184 3160 -27 19 -17 O HETATM 8658 O HOH D 480 29.401 11.306 -3.718 1.00 48.95 O ANISOU 8658 O HOH D 480 6218 6165 6217 4 -6 8 O HETATM 8659 O HOH D 481 23.203 -0.965 8.951 1.00 41.22 O ANISOU 8659 O HOH D 481 5227 5203 5231 -9 -10 -1 O HETATM 8660 O HOH D 482 18.478 18.761 -1.033 1.00 18.81 O ANISOU 8660 O HOH D 482 2336 2426 2385 -46 -65 -31 O HETATM 8661 O HOH D 483 -11.336 5.356 -6.965 1.00 32.34 O ANISOU 8661 O HOH D 483 4128 4062 4099 -15 -26 17 O HETATM 8662 O HOH D 484 6.364 3.358 -15.304 1.00 22.63 O ANISOU 8662 O HOH D 484 2925 2871 2804 -37 -12 -19 O HETATM 8663 O HOH D 485 23.251 5.435 9.019 1.00 42.27 O ANISOU 8663 O HOH D 485 5371 5329 5361 5 -10 -5 O HETATM 8664 O HOH D 486 1.143 15.200 -0.029 1.00 26.67 O ANISOU 8664 O HOH D 486 3392 3328 3413 -12 -29 2 O HETATM 8665 O HOH D 487 7.096 19.071 6.480 1.00 26.94 O ANISOU 8665 O HOH D 487 3357 3417 3460 6 -8 -14 O HETATM 8666 O HOH D 488 18.993 -6.169 4.056 1.00 24.91 O ANISOU 8666 O HOH D 488 3172 3115 3178 36 -27 -30 O HETATM 8667 O HOH D 489 25.707 14.517 -9.657 1.00 31.34 O ANISOU 8667 O HOH D 489 4013 3957 3938 -11 8 -9 O HETATM 8668 O HOH D 490 -3.537 -4.927 18.840 1.00 41.79 O ANISOU 8668 O HOH D 490 5306 5263 5308 -20 9 12 O HETATM 8669 O HOH D 491 5.742 -5.171 -12.207 1.00 33.43 O ANISOU 8669 O HOH D 491 4224 4284 4194 2 -34 -3 O HETATM 8670 O HOH D 492 24.266 12.005 19.383 1.00 28.24 O ANISOU 8670 O HOH D 492 3585 3583 3562 -29 0 -26 O HETATM 8671 O HOH D 493 21.692 8.937 13.465 1.00 28.71 O ANISOU 8671 O HOH D 493 3649 3614 3644 -39 -4 1 O HETATM 8672 O HOH D 494 10.580 19.657 -14.540 1.00 41.51 O ANISOU 8672 O HOH D 494 5263 5234 5274 -4 14 1 O HETATM 8673 O HOH D 495 -1.956 -17.175 6.285 1.00 17.79 O ANISOU 8673 O HOH D 495 2176 2284 2300 -18 -68 78 O HETATM 8674 O HOH D 496 7.421 -9.403 -8.442 1.00 44.88 O ANISOU 8674 O HOH D 496 5691 5663 5697 -2 -11 3 O HETATM 8675 O HOH D 497 8.698 -4.600 -5.811 1.00 14.82 O ANISOU 8675 O HOH D 497 1978 1897 1756 42 -4 41 O HETATM 8676 O HOH D 498 -5.748 -4.952 17.169 1.00 31.35 O ANISOU 8676 O HOH D 498 4002 3939 3970 13 -11 24 O HETATM 8677 O HOH D 499 19.931 11.759 10.368 1.00 18.97 O ANISOU 8677 O HOH D 499 2463 2336 2409 -13 -17 0 O HETATM 8678 O HOH D 500 -10.418 3.787 -1.749 1.00 22.13 O ANISOU 8678 O HOH D 500 2727 2791 2892 31 15 40 O HETATM 8679 O HOH D 501 20.590 4.429 25.610 1.00 41.84 O ANISOU 8679 O HOH D 501 5318 5287 5292 -5 -6 -5 O HETATM 8680 O HOH D 502 -2.758 11.986 9.398 1.00 24.25 O ANISOU 8680 O HOH D 502 3010 3115 3087 -4 -32 -17 O HETATM 8681 O HOH D 503 15.059 0.014 -10.518 1.00 44.57 O ANISOU 8681 O HOH D 503 5643 5651 5642 4 11 6 O HETATM 8682 O HOH D 504 11.477 16.964 -14.394 1.00 42.46 O ANISOU 8682 O HOH D 504 5388 5329 5415 -21 2 6 O HETATM 8683 O HOH D 505 16.940 -2.763 -8.392 1.00 40.19 O ANISOU 8683 O HOH D 505 5117 5079 5075 18 -5 5 O HETATM 8684 O HOH D 506 -8.354 -10.940 -9.846 1.00 59.90 O ANISOU 8684 O HOH D 506 7611 7538 7610 1 -2 -4 O HETATM 8685 O HOH D 507 0.365 12.334 -15.265 1.00 13.41 O ANISOU 8685 O HOH D 507 1762 1735 1598 45 -111 30 O HETATM 8686 O HOH D 508 28.417 12.547 18.434 1.00 53.87 O ANISOU 8686 O HOH D 508 6834 6788 6846 -4 -1 0 O HETATM 8687 O HOH D 509 -2.304 -13.174 -6.322 1.00 38.66 O ANISOU 8687 O HOH D 509 4897 4873 4920 2 0 9 O HETATM 8688 O HOH D 510 -2.000 -14.975 12.648 1.00 36.40 O ANISOU 8688 O HOH D 510 4622 4592 4618 2 -14 4 O HETATM 8689 O HOH D 511 19.153 1.851 13.794 1.00 35.40 O ANISOU 8689 O HOH D 511 4475 4454 4522 7 -10 -8 O HETATM 8690 O HOH D 512 17.160 13.106 13.418 1.00 22.12 O ANISOU 8690 O HOH D 512 2816 2735 2854 -41 -52 9 O HETATM 8691 O HOH D 513 -1.428 -8.153 -12.276 1.00 37.07 O ANISOU 8691 O HOH D 513 4727 4669 4690 -2 -2 -8 O HETATM 8692 O HOH D 514 -10.606 6.770 -1.176 1.00 22.09 O ANISOU 8692 O HOH D 514 2873 2815 2706 23 51 36 O HETATM 8693 O HOH D 515 5.474 9.109 -18.909 1.00 29.40 O ANISOU 8693 O HOH D 515 3786 3698 3686 16 -31 6 O HETATM 8694 O HOH D 516 -17.936 -2.018 7.262 1.00 35.49 O ANISOU 8694 O HOH D 516 4516 4485 4482 -6 -10 16 O HETATM 8695 O HOH D 517 10.252 18.202 18.851 1.00 49.51 O ANISOU 8695 O HOH D 517 6281 6248 6283 8 5 -6 O HETATM 8696 O HOH D 518 3.533 -14.271 15.077 1.00 24.48 O ANISOU 8696 O HOH D 518 3183 3039 3078 9 15 10 O HETATM 8697 O HOH D 519 13.648 21.215 4.471 1.00 29.27 O ANISOU 8697 O HOH D 519 3751 3690 3679 -16 -14 1 O HETATM 8698 O HOH D 520 24.304 14.972 6.193 1.00 33.70 O ANISOU 8698 O HOH D 520 4251 4242 4314 5 9 -13 O HETATM 8699 O HOH D 521 21.603 12.672 12.653 1.00 43.30 O ANISOU 8699 O HOH D 521 5492 5456 5502 0 7 7 O HETATM 8700 O HOH D 522 0.065 6.407 8.604 1.00 19.47 O ANISOU 8700 O HOH D 522 2517 2495 2387 -26 31 -8 O HETATM 8701 O HOH D 523 17.479 4.239 23.775 1.00 46.99 O ANISOU 8701 O HOH D 523 5979 5885 5992 -2 -2 -1 O HETATM 8702 O HOH D 524 24.643 13.116 2.343 1.00 61.45 O ANISOU 8702 O HOH D 524 7817 7744 7786 -3 1 0 O HETATM 8703 O HOH D 525 5.165 6.279 -17.849 1.00 29.44 O ANISOU 8703 O HOH D 525 3746 3705 3734 -17 -6 -28 O HETATM 8704 O HOH D 526 25.652 6.175 2.157 1.00 16.78 O ANISOU 8704 O HOH D 526 2095 2148 2135 -29 -44 20 O HETATM 8705 O HOH D 527 22.421 15.604 13.504 1.00 41.07 O ANISOU 8705 O HOH D 527 5210 5175 5220 -8 2 -2 O HETATM 8706 O HOH D 528 25.806 18.408 7.821 1.00 51.54 O ANISOU 8706 O HOH D 528 6546 6506 6532 2 -4 0 O HETATM 8707 O HOH D 529 7.425 20.116 -14.582 1.00 42.55 O ANISOU 8707 O HOH D 529 5407 5374 5388 -17 0 -11 O HETATM 8708 O HOH D 530 -10.493 2.011 14.424 1.00 37.49 O ANISOU 8708 O HOH D 530 4740 4732 4775 22 15 -11 O HETATM 8709 O HOH D 531 8.904 -18.436 5.055 1.00 45.29 O ANISOU 8709 O HOH D 531 5751 5704 5752 2 -1 -4 O HETATM 8710 O HOH D 532 7.140 -1.917 -15.591 1.00 39.82 O ANISOU 8710 O HOH D 532 5069 5018 5042 14 7 -6 O HETATM 8711 O HOH D 533 -14.839 -2.940 12.388 1.00 37.43 O ANISOU 8711 O HOH D 533 4777 4713 4732 -19 -3 13 O HETATM 8712 O HOH D 534 15.737 -0.245 9.714 1.00 17.03 O ANISOU 8712 O HOH D 534 2159 2206 2107 -60 -71 -26 O HETATM 8713 O HOH D 535 -9.587 -14.910 5.359 1.00 32.80 O ANISOU 8713 O HOH D 535 4150 4118 4193 -14 19 -2 O HETATM 8714 O HOH D 536 26.880 10.801 -2.397 1.00 50.01 O ANISOU 8714 O HOH D 536 6339 6293 6369 2 -9 1 O HETATM 8715 O HOH D 537 12.253 9.506 -18.207 1.00 33.51 O ANISOU 8715 O HOH D 537 4239 4235 4257 -3 24 -10 O HETATM 8716 O HOH D 538 -15.309 4.370 2.086 1.00 31.71 O ANISOU 8716 O HOH D 538 4025 3975 4049 -15 27 5 O HETATM 8717 O HOH D 539 7.578 -15.762 11.570 1.00 37.25 O ANISOU 8717 O HOH D 539 4749 4642 4762 2 -27 5 O HETATM 8718 O HOH D 540 18.882 14.425 -11.708 1.00 29.60 O ANISOU 8718 O HOH D 540 3825 3710 3712 6 21 20 O HETATM 8719 O HOH D 541 0.088 -16.503 11.484 1.00 33.34 O ANISOU 8719 O HOH D 541 4278 4182 4208 1 -28 39 O HETATM 8720 O HOH D 542 3.146 2.536 14.103 1.00 26.64 O ANISOU 8720 O HOH D 542 3405 3426 3290 10 -27 -3 O HETATM 8721 O HOH D 543 10.717 11.726 21.659 1.00 42.74 O ANISOU 8721 O HOH D 543 5431 5405 5402 5 -12 1 O HETATM 8722 O HOH D 544 -1.756 -19.216 0.558 1.00 40.74 O ANISOU 8722 O HOH D 544 5180 5123 5175 9 -1 -6 O HETATM 8723 O HOH D 545 22.658 11.853 3.899 1.00 23.61 O ANISOU 8723 O HOH D 545 2974 3042 2956 -52 -1 -15 O HETATM 8724 O HOH D 546 -11.959 3.937 -4.112 1.00 31.35 O ANISOU 8724 O HOH D 546 3976 3926 4010 4 2 0 O HETATM 8725 O HOH D 547 23.326 7.189 5.562 1.00 23.57 O ANISOU 8725 O HOH D 547 2985 3025 2947 -47 -7 -46 O HETATM 8726 O HOH D 548 9.663 0.222 -15.768 1.00 38.22 O ANISOU 8726 O HOH D 548 4880 4818 4823 4 1 5 O HETATM 8727 O HOH D 549 0.944 14.496 2.709 1.00 31.62 O ANISOU 8727 O HOH D 549 4004 4015 3995 -3 -16 -21 O HETATM 8728 O HOH D 550 -4.871 -15.592 -0.685 1.00 30.50 O ANISOU 8728 O HOH D 550 3916 3818 3854 -12 8 5 O HETATM 8729 O HOH D 551 -11.892 7.761 8.061 1.00 15.19 O ANISOU 8729 O HOH D 551 1924 1956 1893 48 -22 43 O HETATM 8730 O HOH D 552 15.821 19.827 18.524 1.00 33.50 O ANISOU 8730 O HOH D 552 4289 4212 4229 -6 -1 -17 O HETATM 8731 O HOH D 553 -0.131 -1.224 -17.223 1.00 38.70 O ANISOU 8731 O HOH D 553 4922 4905 4876 -3 -29 -4 O HETATM 8732 O HOH D 554 0.510 8.732 4.840 1.00 13.33 O ANISOU 8732 O HOH D 554 1653 1733 1680 22 31 -18 O HETATM 8733 O HOH D 555 18.855 -1.761 -5.743 1.00 25.18 O ANISOU 8733 O HOH D 555 3171 3191 3204 24 -19 -6 O HETATM 8734 O HOH D 556 -7.229 1.435 21.823 1.00 44.29 O ANISOU 8734 O HOH D 556 5643 5587 5597 -3 13 9 O HETATM 8735 O HOH D 557 1.745 11.291 8.443 1.00 42.53 O ANISOU 8735 O HOH D 557 5388 5358 5412 8 4 0 O HETATM 8736 O HOH D 558 4.315 -16.422 -3.695 1.00 28.57 O ANISOU 8736 O HOH D 558 3639 3616 3598 -4 -23 19 O HETATM 8737 O HOH D 559 -2.215 7.289 -9.979 1.00 25.50 O ANISOU 8737 O HOH D 559 3229 3299 3160 36 -2 -26 O HETATM 8738 O HOH D 560 25.155 22.571 4.678 1.00 29.90 O ANISOU 8738 O HOH D 560 3792 3788 3780 -24 21 -19 O HETATM 8739 O HOH D 561 -5.080 -10.932 -9.982 1.00 54.33 O ANISOU 8739 O HOH D 561 6910 6833 6901 -5 3 -3 O HETATM 8740 O HOH D 562 -3.904 -1.351 -16.164 1.00 30.47 O ANISOU 8740 O HOH D 562 3865 3829 3883 19 -23 10 O HETATM 8741 O HOH D 563 26.183 8.451 -11.055 1.00 27.02 O ANISOU 8741 O HOH D 563 3410 3418 3438 -5 28 -18 O HETATM 8742 O HOH D 564 -10.808 10.343 19.461 1.00 37.61 O ANISOU 8742 O HOH D 564 4756 4752 4781 4 3 6 O HETATM 8743 O HOH D 565 15.955 -12.493 3.032 1.00 22.13 O ANISOU 8743 O HOH D 565 2822 2798 2790 7 -40 -11 O HETATM 8744 O HOH D 566 -10.511 -0.788 17.931 1.00 40.97 O ANISOU 8744 O HOH D 566 5221 5168 5177 2 -18 10 O HETATM 8745 O HOH D 567 19.765 18.890 -10.549 1.00 43.64 O ANISOU 8745 O HOH D 567 5551 5502 5528 8 -5 10 O HETATM 8746 O HOH D 568 23.184 9.416 2.757 1.00 37.98 O ANISOU 8746 O HOH D 568 4793 4824 4813 6 13 -1 O HETATM 8747 O HOH D 569 10.309 -12.753 -5.164 1.00 32.91 O ANISOU 8747 O HOH D 569 4210 4157 4137 10 -9 3 O HETATM 8748 O HOH D 570 26.926 6.591 -2.389 1.00 29.74 O ANISOU 8748 O HOH D 570 3707 3803 3790 -27 -10 -9 O HETATM 8749 O HOH D 571 15.200 10.921 -12.942 1.00 50.62 O ANISOU 8749 O HOH D 571 6424 6395 6415 -3 6 18 O HETATM 8750 O HOH D 572 -3.717 10.366 18.462 1.00 45.71 O ANISOU 8750 O HOH D 572 5801 5756 5810 1 3 -1 O HETATM 8751 O HOH D 573 0.529 22.719 -14.670 1.00 36.28 O ANISOU 8751 O HOH D 573 4640 4552 4591 -11 -2 -13 O HETATM 8752 O HOH D 574 8.700 16.756 -18.949 1.00 45.47 O ANISOU 8752 O HOH D 574 5760 5731 5785 9 0 10 O HETATM 8753 O HOH D 575 -3.148 10.283 13.523 1.00 29.60 O ANISOU 8753 O HOH D 575 3729 3758 3759 10 -30 -25 O HETATM 8754 O HOH D 576 12.943 -6.510 -5.008 1.00 22.79 O ANISOU 8754 O HOH D 576 2914 2800 2945 17 30 -4 O HETATM 8755 O HOH D 577 14.282 -4.465 14.065 1.00 36.85 O ANISOU 8755 O HOH D 577 4698 4658 4645 1 -1 8 O HETATM 8756 O HOH D 578 -8.746 -4.415 11.545 1.00 36.32 O ANISOU 8756 O HOH D 578 4629 4576 4593 16 -19 18 O HETATM 8757 O HOH D 579 -20.587 -2.833 1.218 1.00 39.28 O ANISOU 8757 O HOH D 579 4976 4956 4994 13 -17 -16 O HETATM 8758 O HOH D 580 10.129 -16.538 12.494 1.00 37.51 O ANISOU 8758 O HOH D 580 4747 4721 4785 -15 0 -12 O HETATM 8759 O HOH D 581 2.119 -16.039 13.470 1.00 44.04 O ANISOU 8759 O HOH D 581 5605 5504 5624 2 -8 -8 O HETATM 8760 O HOH D 582 19.947 16.779 16.636 1.00 35.06 O ANISOU 8760 O HOH D 582 4448 4419 4455 -2 15 -6 O HETATM 8761 O HOH D 583 0.571 20.908 -12.578 1.00 26.85 O ANISOU 8761 O HOH D 583 3442 3370 3391 1 1 16 O HETATM 8762 O HOH D 584 10.353 -16.004 8.172 1.00 47.66 O ANISOU 8762 O HOH D 584 6057 5996 6056 -8 -4 5 O HETATM 8763 O HOH D 585 -1.387 -4.220 -15.819 1.00 30.04 O ANISOU 8763 O HOH D 585 3832 3799 3783 -14 -11 -30 O HETATM 8764 O HOH D 586 -11.248 -8.907 -3.820 1.00 28.84 O ANISOU 8764 O HOH D 586 3636 3613 3709 -30 7 -6 O HETATM 8765 O HOH D 587 12.745 3.978 17.941 1.00 40.39 O ANISOU 8765 O HOH D 587 5110 5097 5138 -14 -27 -8 O HETATM 8766 O HOH D 588 12.951 -8.709 16.098 1.00 35.05 O ANISOU 8766 O HOH D 588 4461 4396 4459 19 11 24 O HETATM 8767 O HOH D 589 24.031 13.861 11.728 1.00 42.55 O ANISOU 8767 O HOH D 589 5401 5364 5401 -4 -9 5 O HETATM 8768 O HOH D 590 13.139 15.728 -12.547 1.00 33.25 O ANISOU 8768 O HOH D 590 4206 4217 4211 -12 5 -2 O HETATM 8769 O HOH D 591 18.979 2.318 -14.747 1.00 43.78 O ANISOU 8769 O HOH D 591 5580 5508 5547 20 6 -10 O HETATM 8770 O HOH D 592 8.905 13.561 23.870 1.00 32.63 O ANISOU 8770 O HOH D 592 4162 4111 4125 0 -5 -12 O HETATM 8771 O HOH D 593 -11.108 -11.312 -2.346 1.00 48.07 O ANISOU 8771 O HOH D 593 6097 6076 6092 0 -11 0 O HETATM 8772 O HOH D 594 28.855 7.470 -5.200 1.00 45.65 O ANISOU 8772 O HOH D 594 5795 5754 5796 -5 0 4 O HETATM 8773 O HOH D 595 -1.705 -2.095 20.296 1.00 47.49 O ANISOU 8773 O HOH D 595 6041 5981 6021 -4 9 0 O HETATM 8774 O HOH D 596 6.230 -2.508 -12.970 1.00 23.86 O ANISOU 8774 O HOH D 596 3027 3026 3011 7 -19 -2 O HETATM 8775 O HOH D 597 -19.536 -1.202 -0.874 1.00 58.78 O ANISOU 8775 O HOH D 597 7470 7403 7461 -6 -8 -3 O HETATM 8776 O HOH D 598 0.372 -19.228 10.494 1.00 6.94 O ANISOU 8776 O HOH D 598 1145 666 828 -83 -12 44 O HETATM 8777 O HOH D 599 9.578 24.632 0.746 1.00 42.23 O ANISOU 8777 O HOH D 599 5362 5319 5366 7 10 -2 O HETATM 8778 O HOH D 600 12.884 -12.732 14.810 1.00 39.19 O ANISOU 8778 O HOH D 600 4967 4972 4949 10 2 -7 O HETATM 8779 O HOH D 601 5.533 14.908 8.460 1.00 24.46 O ANISOU 8779 O HOH D 601 3151 3063 3078 -76 -14 13 O HETATM 8780 O HOH D 602 -12.311 4.763 2.229 1.00 26.48 O ANISOU 8780 O HOH D 602 3380 3408 3273 -32 -25 20 O HETATM 8781 O HOH D 603 24.880 1.108 9.766 1.00 52.20 O ANISOU 8781 O HOH D 603 6622 6581 6629 2 -4 2 O HETATM 8782 O HOH D 604 -3.272 11.272 20.992 1.00 32.65 O ANISOU 8782 O HOH D 604 4153 4119 4135 7 -8 12 O HETATM 8783 O HOH D 605 24.619 15.671 3.483 1.00 34.24 O ANISOU 8783 O HOH D 605 4319 4327 4363 -8 24 -3 O HETATM 8784 O HOH D 606 -1.152 -6.824 -14.849 1.00 39.75 O ANISOU 8784 O HOH D 606 5039 5023 5042 -5 -7 -4 O HETATM 8785 O HOH D 607 14.271 20.626 12.164 1.00 37.66 O ANISOU 8785 O HOH D 607 4787 4716 4806 6 10 14 O HETATM 8786 O HOH D 608 2.886 -4.888 19.253 1.00 39.04 O ANISOU 8786 O HOH D 608 4959 4950 4925 6 -4 16 O HETATM 8787 O HOH D 609 4.918 13.119 -21.023 1.00 48.50 O ANISOU 8787 O HOH D 609 6148 6119 6159 -2 -1 1 O HETATM 8788 O HOH D 610 -0.265 10.034 -16.544 1.00 35.76 O ANISOU 8788 O HOH D 610 4502 4497 4589 17 -30 23 O HETATM 8789 O HOH D 611 -1.158 12.014 4.668 1.00 19.57 O ANISOU 8789 O HOH D 611 2618 2465 2354 57 19 62 O HETATM 8790 O HOH D 612 21.141 3.690 9.934 1.00 54.28 O ANISOU 8790 O HOH D 612 6880 6850 6893 3 -1 -10 O HETATM 8791 O HOH D 613 1.186 4.782 13.371 1.00 32.02 O ANISOU 8791 O HOH D 613 4052 4050 4065 1 23 -2 O HETATM 8792 O HOH D 614 15.807 0.751 13.659 1.00 42.80 O ANISOU 8792 O HOH D 614 5433 5408 5420 -11 -2 -14 O HETATM 8793 O HOH D 615 16.016 2.082 11.199 1.00 37.98 O ANISOU 8793 O HOH D 615 4839 4764 4830 4 -31 6 O HETATM 8794 O HOH D 616 6.879 19.927 3.788 1.00 28.42 O ANISOU 8794 O HOH D 616 3620 3563 3615 21 -5 0 O HETATM 8795 O HOH D 617 -9.689 -6.614 10.092 1.00 44.53 O ANISOU 8795 O HOH D 617 5645 5615 5658 3 3 -2 O HETATM 8796 O HOH D 618 12.544 -11.268 -6.249 1.00 48.89 O ANISOU 8796 O HOH D 618 6234 6148 6194 6 1 -9 O HETATM 8797 O HOH D 619 22.538 -2.621 1.038 1.00 43.69 O ANISOU 8797 O HOH D 619 5543 5504 5553 -9 2 8 O HETATM 8798 O HOH D 620 5.847 -7.047 -8.306 1.00 45.57 O ANISOU 8798 O HOH D 620 5793 5741 5781 -3 9 -2 O HETATM 8799 O HOH D 621 20.135 4.668 -15.860 1.00 47.00 O ANISOU 8799 O HOH D 621 5956 5931 5970 0 7 -2 O HETATM 8800 O HOH D 622 4.724 16.793 -3.759 1.00 42.46 O ANISOU 8800 O HOH D 622 5407 5352 5373 -10 12 -21 O HETATM 8801 O HOH D 623 19.170 21.005 -5.535 1.00 31.06 O ANISOU 8801 O HOH D 623 3943 3904 3954 13 -59 18 O HETATM 8802 O HOH D 624 2.666 18.752 -3.785 1.00 13.14 O ANISOU 8802 O HOH D 624 1548 1825 1618 -8 -38 -87 O HETATM 8803 O HOH D 625 5.611 -18.090 0.197 1.00 34.98 O ANISOU 8803 O HOH D 625 4462 4374 4456 3 8 -18 O HETATM 8804 O HOH D 626 11.695 20.273 10.346 1.00 43.59 O ANISOU 8804 O HOH D 626 5537 5507 5517 6 4 -16 O HETATM 8805 O HOH D 627 -1.095 10.812 11.691 1.00 35.66 O ANISOU 8805 O HOH D 627 4529 4492 4526 -19 -15 -16 O HETATM 8806 O HOH D 628 14.941 2.735 16.766 1.00 42.25 O ANISOU 8806 O HOH D 628 5380 5321 5352 -4 5 -3 O HETATM 8807 O HOH D 629 24.366 3.987 3.210 1.00 35.48 O ANISOU 8807 O HOH D 629 4476 4505 4499 8 -19 15 O HETATM 8808 O HOH D 630 12.015 4.831 22.105 1.00 27.18 O ANISOU 8808 O HOH D 630 3467 3484 3376 11 -9 22 O HETATM 8809 O HOH D 631 17.556 1.288 -10.952 1.00 38.48 O ANISOU 8809 O HOH D 631 4872 4876 4871 -5 -10 -5 O HETATM 8810 O HOH D 632 12.635 -15.230 5.450 1.00 36.70 O ANISOU 8810 O HOH D 632 4655 4613 4677 3 -8 -9 O HETATM 8811 O HOH D 633 3.288 -0.533 18.366 1.00 31.72 O ANISOU 8811 O HOH D 633 4014 4040 3999 7 -14 -6 O HETATM 8812 O HOH D 634 19.047 2.042 10.910 1.00 46.11 O ANISOU 8812 O HOH D 634 5881 5802 5836 5 -5 -15 O HETATM 8813 O HOH D 635 3.241 17.873 1.483 1.00 48.53 O ANISOU 8813 O HOH D 635 6169 6094 6178 11 0 12 O HETATM 8814 O HOH D 636 11.423 -6.722 -9.105 1.00 36.91 O ANISOU 8814 O HOH D 636 4699 4659 4667 -8 3 -9 O HETATM 8815 O HOH D 637 -1.538 14.580 3.954 1.00 29.67 O ANISOU 8815 O HOH D 637 3782 3774 3716 1 5 -11 O HETATM 8816 O HOH D 638 3.220 17.568 -1.321 1.00 28.09 O ANISOU 8816 O HOH D 638 3572 3510 3589 26 -14 9 O HETATM 8817 O HOH D 639 13.696 13.170 -13.478 1.00 43.39 O ANISOU 8817 O HOH D 639 5522 5455 5508 -9 3 -2 O HETATM 8818 O HOH D 640 16.255 13.351 -12.006 1.00 36.63 O ANISOU 8818 O HOH D 640 4686 4633 4599 3 -26 -5 O HETATM 8819 O HOH D 641 17.749 20.481 -3.288 1.00 30.31 O ANISOU 8819 O HOH D 641 3873 3737 3905 -35 -51 -13 O HETATM 8820 O HOH D 642 -1.585 15.845 6.433 1.00 48.68 O ANISOU 8820 O HOH D 642 6190 6130 6177 4 -5 -4 O HETATM 8821 O HOH D 643 10.113 24.462 4.741 1.00 50.17 O ANISOU 8821 O HOH D 643 6372 6322 6370 6 8 -5 O HETATM 8822 O HOH D 644 -13.595 -10.419 -0.967 1.00 42.70 O ANISOU 8822 O HOH D 644 5405 5395 5425 -12 -19 1 O HETATM 8823 O HOH D 645 16.763 -10.012 0.237 1.00 28.90 O ANISOU 8823 O HOH D 645 3656 3715 3610 21 4 -39 O HETATM 8824 O HOH D 646 23.190 -4.059 -1.773 1.00 40.67 O ANISOU 8824 O HOH D 646 5174 5109 5171 1 -21 3 O HETATM 8825 O HOH D 647 2.598 5.522 -17.422 1.00 30.09 O ANISOU 8825 O HOH D 647 3855 3815 3763 2 26 13 O HETATM 8826 O HOH D 648 25.377 -3.013 -3.266 1.00 39.33 O ANISOU 8826 O HOH D 648 5019 4947 4979 -1 -2 -16 O HETATM 8827 O HOH D 649 7.943 21.590 7.608 1.00 36.41 O ANISOU 8827 O HOH D 649 4630 4581 4624 5 4 2 O HETATM 8828 O HOH D 650 -5.292 -5.367 -15.695 1.00 34.27 O ANISOU 8828 O HOH D 650 4331 4343 4348 22 -18 -13 O HETATM 8829 O HOH D 651 6.130 2.103 -17.774 1.00 26.81 O ANISOU 8829 O HOH D 651 3445 3421 3321 -24 0 -19 O HETATM 8830 O HOH D 652 10.251 -3.699 -11.312 1.00 28.33 O ANISOU 8830 O HOH D 652 3637 3530 3595 18 -16 -1 O HETATM 8831 O HOH D 653 8.118 22.293 2.851 1.00 46.19 O ANISOU 8831 O HOH D 653 5879 5815 5858 13 0 -2 O HETATM 8832 O HOH D 654 19.853 6.308 -18.587 1.00 40.82 O ANISOU 8832 O HOH D 654 5174 5154 5183 -7 -5 0 O HETATM 8833 O HOH D 655 -3.085 -17.398 13.462 1.00 45.53 O ANISOU 8833 O HOH D 655 5793 5723 5784 -2 1 3 O HETATM 8834 O HOH D 656 -2.059 -14.080 15.549 1.00 41.26 O ANISOU 8834 O HOH D 656 5249 5209 5219 -2 9 5 O HETATM 8835 O HOH D 657 -3.979 -20.355 2.162 1.00 31.76 O ANISOU 8835 O HOH D 657 4076 3927 4063 10 -21 -38 O HETATM 8836 O HOH D 658 -21.538 0.903 1.260 1.00 41.24 O ANISOU 8836 O HOH D 658 5215 5197 5255 0 5 13 O HETATM 8837 O HOH D 659 -6.917 -2.423 20.574 1.00 40.18 O ANISOU 8837 O HOH D 659 5129 5078 5058 -2 12 25 O CONECT 179 229 CONECT 229 179 CONECT 2121 2171 CONECT 2171 2121 CONECT 4071 4121 CONECT 4121 4071 CONECT 5989 6037 CONECT 6037 5989 CONECT 7726 7727 7729 7889 CONECT 7727 7726 7728 CONECT 7728 7727 CONECT 7729 7726 7730 CONECT 7730 7729 CONECT 7731 7732 7733 7734 7735 CONECT 7732 7731 CONECT 7733 7731 CONECT 7734 7731 CONECT 7735 7731 CONECT 7736 7737 7738 7739 7740 CONECT 7737 7736 CONECT 7738 7736 CONECT 7739 7736 CONECT 7740 7736 CONECT 7741 7742 7743 7744 7745 CONECT 7742 7741 CONECT 7743 7741 CONECT 7744 7741 CONECT 7745 7741 CONECT 7746 7747 7748 7749 7750 CONECT 7747 7746 CONECT 7748 7746 CONECT 7749 7746 CONECT 7750 7746 CONECT 7751 7752 7753 7754 7755 CONECT 7752 7751 CONECT 7753 7751 CONECT 7754 7751 CONECT 7755 7751 CONECT 7756 7757 7758 7759 7760 CONECT 7757 7756 CONECT 7758 7756 CONECT 7759 7756 CONECT 7760 7756 CONECT 7761 7762 7763 CONECT 7762 7761 CONECT 7763 7761 7764 CONECT 7764 7763 CONECT 7765 7766 7767 CONECT 7766 7765 CONECT 7767 7765 7768 CONECT 7768 7767 CONECT 7769 7770 7772 CONECT 7770 7769 7771 CONECT 7771 7770 CONECT 7772 7769 7773 CONECT 7773 7772 CONECT 7774 7775 7776 7777 7778 CONECT 7775 7774 CONECT 7776 7774 CONECT 7777 7774 CONECT 7778 7774 CONECT 7779 7780 7781 7782 7783 CONECT 7780 7779 CONECT 7781 7779 CONECT 7782 7779 CONECT 7783 7779 CONECT 7784 7785 7786 7787 7788 CONECT 7785 7784 CONECT 7786 7784 CONECT 7787 7784 CONECT 7788 7784 CONECT 7789 7790 7791 7792 7793 CONECT 7790 7789 CONECT 7791 7789 CONECT 7792 7789 CONECT 7793 7789 CONECT 7794 7795 7796 CONECT 7795 7794 CONECT 7796 7794 7797 CONECT 7797 7796 CONECT 7798 7799 7800 CONECT 7799 7798 CONECT 7800 7798 7801 CONECT 7801 7800 CONECT 7802 7803 7804 CONECT 7803 7802 CONECT 7804 7802 7805 CONECT 7805 7804 CONECT 7806 7807 7808 CONECT 7807 7806 CONECT 7808 7806 7809 CONECT 7809 7808 CONECT 7810 7811 7812 CONECT 7811 7810 CONECT 7812 7810 7813 CONECT 7813 7812 CONECT 7814 7815 7816 CONECT 7815 7814 CONECT 7816 7814 7817 CONECT 7817 7816 CONECT 7818 7819 7821 CONECT 7819 7818 7820 CONECT 7820 7819 CONECT 7821 7818 7822 CONECT 7822 7821 CONECT 7823 7824 7826 CONECT 7824 7823 7825 CONECT 7825 7824 CONECT 7826 7823 7827 CONECT 7827 7826 CONECT 7828 7829 7831 CONECT 7829 7828 7830 CONECT 7830 7829 CONECT 7831 7828 7832 CONECT 7832 7831 CONECT 7833 7834 7835 7836 7837 CONECT 7834 7833 CONECT 7835 7833 CONECT 7836 7833 CONECT 7837 7833 CONECT 7838 7839 7840 7841 7842 CONECT 7839 7838 CONECT 7840 7838 CONECT 7841 7838 CONECT 7842 7838 CONECT 7843 7844 7845 CONECT 7844 7843 CONECT 7845 7843 7846 CONECT 7846 7845 CONECT 7847 7848 7849 CONECT 7848 7847 CONECT 7849 7847 7850 CONECT 7850 7849 CONECT 7851 7852 7853 CONECT 7852 7851 CONECT 7853 7851 7854 CONECT 7854 7853 CONECT 7855 7856 7858 CONECT 7856 7855 7857 CONECT 7857 7856 CONECT 7858 7855 7859 CONECT 7859 7858 CONECT 7860 7861 7863 CONECT 7861 7860 7862 CONECT 7862 7861 CONECT 7863 7860 7864 CONECT 7864 7863 CONECT 7865 7866 7868 CONECT 7866 7865 7867 CONECT 7867 7866 CONECT 7868 7865 7869 CONECT 7869 7868 CONECT 7870 7871 7872 7873 7874 CONECT 7871 7870 CONECT 7872 7870 CONECT 7873 7870 CONECT 7874 7870 CONECT 7875 7876 7877 7878 7879 CONECT 7876 7875 CONECT 7877 7875 CONECT 7878 7875 CONECT 7879 7875 CONECT 7880 7881 7882 7883 7884 CONECT 7881 7880 CONECT 7882 7880 CONECT 7883 7880 CONECT 7884 7880 CONECT 7885 7886 7887 CONECT 7886 7885 CONECT 7887 7885 7888 CONECT 7888 7887 CONECT 7889 7726 MASTER 459 0 35 49 24 0 68 15 8755 4 172 76 END
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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
1e3u
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
BETA-LACTAMASE OXA-10 dimer
Ligand Name
BETA-LACTAMASE OXA-10
EC.Number
E.C.3.5.2.6
Resolution
1.66(Å)
Affinity (Kd/Ki/IC50)
Kd=1uM
Release Year
2001
Protein/NA Sequence
Check fasta file
Primary Reference
(2000) Structure Vol. 8: pp. 1289
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):
P14489
Entrez Gene ID
NCBI Entrez Gene ID:
56327504
60671677
ASD
Information of known allosteric effects of PDB entries
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