HEADER SIGNALING PROTEIN/AGONIST 09-AUG-22 8E0G TITLE RE-REFINED MODEL OF ACTIVE MU-OPIOID RECEPTOR (PDB 5C1M) AS AN ADDUCT TITLE 2 WITH BU72 CAVEAT 8E0G THR A 60 HAS WRONG CHIRALITY AT ATOM CA COMPND MOL_ID: 1; COMPND 2 MOLECULE: MU-TYPE OPIOID RECEPTOR; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: M-OR-1,MOR-1; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: NANOBODY 39; COMPND 8 CHAIN: B; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: OPRM1, MOR, OPRM; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 11 ORGANISM_COMMON: LLAMA; SOURCE 12 ORGANISM_TAXID: 9844; SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS AGONIST, ACTIVE STATE, REVISED STRUCTURE, SIGNALING PROTEIN-AGONIST KEYWDS 2 COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR T.A.MUNRO REVDAT 2 15-NOV-23 8E0G 1 LINK REVDAT 1 18-OCT-23 8E0G 0 JRNL AUTH T.A.MUNRO JRNL TITL REANALYSIS OF A MU OPIOID RECEPTOR CRYSTAL STRUCTURE REVEALS JRNL TITL 2 A COVALENT ADDUCT WITH BU72. JRNL REF BMC BIOL. V. 21 213 2023 JRNL REFN ESSN 1741-7007 JRNL PMID 37817141 JRNL DOI 10.1186/S12915-023-01689-W REMARK 0 REMARK 0 THIS ENTRY 8E0G REFLECTS AN ALTERNATIVE MODELING OF THE ORIGINAL REMARK 0 DATA IN 5C1M, DETERMINED BY W.J.HUANG,A.MANGLIK, REMARK 0 A.J.VENKATAKRISHNAN,T.LAEREMANS,E.N.FEINBERG,A.L.SANBORN, REMARK 0 H.E.KATO,K.E.LIVINGSTON,T.S.THORSEN,R.KLING,S.GRANIER,P.GMEINER, REMARK 0 S.M.HUSBANDS,J.R.TRAYNOR,W.I.WEIS,J.STEYAERT,R.O.DROR,B.K.KOBILKA REMARK 0 ORIGINAL DATA REFERENCE 1 REMARK 0 PDB ID: 5C1M REMARK 0 AUTH W.HUANG,A.MANGLIK,A.J.VENKATAKRISHNAN,T.LAEREMANS, REMARK 0 AUTH 2 E.N.FEINBERG,A.L.SANBORN,H.E.KATO,K.E.LIVINGSTON, REMARK 0 AUTH 3 T.S.THORSEN,R.C.KLING,S.GRANIER,P.GMEINER,S.M.HUSBANDS, REMARK 0 AUTH 4 J.R.TRAYNOR,W.I.WEIS,J.STEYAERT,R.O.DROR,B.K.KOBILKA REMARK 0 TITL STRUCTURAL INSIGHTS INTO MU-OPIOID RECEPTOR ACTIVATION. REMARK 0 REF NATURE V. 524 315 2015 REMARK 0 REFN ESSN 1476-4687 REMARK 0 PMID 26245379 REMARK 0 DOI 10.1038/NATURE14886 REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PDB-REDO 7.32 REMARK 3 AUTHORS : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.50 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 37971 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 SET) : 0.192 REMARK 3 FREE R VALUE : 0.225 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1999 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2775 REMARK 3 BIN R VALUE (WORKING SET) : 0.3050 REMARK 3 BIN FREE R VALUE : 0.3120 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 146 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3276 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 131 REMARK 3 SOLVENT ATOMS : 68 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.32 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.02000 REMARK 3 B22 (A**2) : 3.63000 REMARK 3 B33 (A**2) : -2.61000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : NULL REMARK 3 BOND ANGLES (DEGREES) : NULL REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS REMARK 3 U VALUES : RESIDUAL ONLY REMARK 4 REMARK 4 8E0G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-AUG-22. REMARK 100 THE DEPOSITION ID IS D_1000267645. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-NOV-14 REMARK 200 TEMPERATURE (KELVIN) : 80 REMARK 200 PH : 7.0-7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40051 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 43.500 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : 8.500 REMARK 200 R MERGE (I) : 0.14200 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.5100 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84 REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 1.44510 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: PDB ENTRY 5C1M REMARK 200 REMARK 200 REMARK: AUTHOR USED THE SF DATA FROM ENTRY 5C1M REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 65.78 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.59 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: RECONSTITUTED IN 10:1 REMARK 280 MONOOLEIN:CHOLESTEROL MIX, PRECIPITANT: 15-25% PEG300, 100 MM REMARK 280 HEPES, PH 7.0-7.5, 1% 1,2,3-HEPTANETRIOL, 0.5-1.0% POLYPROPYLENE REMARK 280 GLYCOL P400, 100-300 MM AMMONIUM PHOSPHATE DIBASIC, PH 7.5, REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X,-Y+1/2,Z REMARK 290 7555 -X+1/2,Y,-Z REMARK 290 8555 X,-Y,-Z+1/2 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 22.21500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 104.95000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 72.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 104.95000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.21500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 72.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 22.21500 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 72.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 104.95000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 72.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 22.21500 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 104.95000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4250 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19500 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 UNK B 103 REMARK 465 UNK B 104 REMARK 465 UNK B 105 REMARK 465 UNK B 106 REMARK 465 UNK B 107 REMARK 465 UNK B 108 REMARK 465 UNK B 109 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 TRP B 53 CB TRP B 53 CG -0.141 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 MET A 205 CG - SD - CE ANGL. DEV. = -10.7 DEGREES REMARK 500 ARG B 72 NE - CZ - NH2 ANGL. DEV. = -3.2 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 GLN A 59 -71.34 -101.71 REMARK 500 THR A 60 145.64 -37.74 REMARK 500 TYR A 96 -61.22 -100.33 REMARK 500 LYS A 98 -8.58 85.74 REMARK 500 MET A 99 30.81 70.13 REMARK 500 ARG A 179 45.99 -95.76 REMARK 500 ARG A 211 81.74 -160.61 REMARK 500 GLN A 212 51.04 73.27 REMARK 500 PHE A 241 -61.47 -122.24 REMARK 500 MET A 264 117.98 -173.58 REMARK 500 LEU A 265 -28.50 -37.69 REMARK 500 SER A 266 -61.67 -108.63 REMARK 500 SER A 268 -52.20 -174.81 REMARK 500 LYS A 344 -50.95 -29.91 REMARK 500 ARG B 29 19.99 59.69 REMARK 500 ALA B 126 -174.08 -61.54 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLC A 401 REMARK 610 OLC A 402 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5C1M RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF ACTIVE MU-OPIOID RECEPTOR BOUND TO THE AGONIST REMARK 900 BU72 DBREF 8E0G A 52 347 UNP P42866 OPRM_MOUSE 52 347 DBREF 8E0G B 3 127 PDB 8E0G 8E0G 3 127 SEQADV 8E0G U8S A 54 UNP P42866 HIS 54 CONFLICT SEQRES 1 A 296 GLY SER U8S SER LEU YCM PRO GLN THR GLY SER PRO SER SEQRES 2 A 296 MET VAL THR ALA ILE THR ILE MET ALA LEU TYR SER ILE SEQRES 3 A 296 VAL CYS VAL VAL GLY LEU PHE GLY ASN PHE LEU VAL MET SEQRES 4 A 296 TYR VAL ILE VAL ARG TYR THR LYS MET LYS THR ALA THR SEQRES 5 A 296 ASN ILE TYR ILE PHE ASN LEU ALA LEU ALA ASP ALA LEU SEQRES 6 A 296 ALA THR SER THR LEU PRO PHE GLN SER VAL ASN TYR LEU SEQRES 7 A 296 MET GLY THR TRP PRO PHE GLY ASN ILE LEU CYS LYS ILE SEQRES 8 A 296 VAL ILE SER ILE ASP TYR TYR ASN MET PHE THR SER ILE SEQRES 9 A 296 PHE THR LEU CYS THR MET SER VAL ASP ARG TYR ILE ALA SEQRES 10 A 296 VAL CYS HIS PRO VAL LYS ALA LEU ASP PHE ARG THR PRO SEQRES 11 A 296 ARG ASN ALA LYS ILE VAL ASN VAL CYS ASN TRP ILE LEU SEQRES 12 A 296 SER SER ALA ILE GLY LEU PRO VAL MET PHE MET ALA THR SEQRES 13 A 296 THR LYS TYR ARG GLN GLY SER ILE ASP CYS THR LEU THR SEQRES 14 A 296 PHE SER HIS PRO THR TRP TYR TRP GLU ASN LEU LEU LYS SEQRES 15 A 296 ILE CYS VAL PHE ILE PHE ALA PHE ILE MET PRO VAL LEU SEQRES 16 A 296 ILE ILE THR VAL CYS TYR GLY LEU MET ILE LEU ARG LEU SEQRES 17 A 296 LYS SER VAL ARG MET LEU SER GLY SER LYS GLU LYS ASP SEQRES 18 A 296 ARG ASN LEU ARG ARG ILE THR ARG MET VAL LEU VAL VAL SEQRES 19 A 296 VAL ALA VAL PHE ILE VAL CYS TRP THR PRO ILE HIS ILE SEQRES 20 A 296 TYR VAL ILE ILE LYS ALA LEU ILE THR ILE PRO GLU THR SEQRES 21 A 296 THR PHE GLN THR VAL SER TRP HIS PHE CYS ILE ALA LEU SEQRES 22 A 296 GLY TYR THR ASN SER CYS LEU ASN PRO VAL LEU TYR ALA SEQRES 23 A 296 PHE LEU ASP GLU ASN PHE LYS ARG CYS PHE SEQRES 1 B 125 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL ARG SEQRES 2 B 125 PRO GLY GLY SER LEU ARG LEU SER CYS VAL ASP SER GLU SEQRES 3 B 125 ARG THR SER TYR PRO MET GLY TRP PHE ARG ARG ALA PRO SEQRES 4 B 125 GLY LYS GLU ARG GLU PHE VAL ALA SER ILE THR TRP SER SEQRES 5 B 125 GLY ILE ASP PRO THR TYR ALA ASP SER VAL ALA ASP ARG SEQRES 6 B 125 PHE THR THR SER ARG ASP VAL ALA ASN ASN THR LEU TYR SEQRES 7 B 125 LEU GLN MET ASN SER LEU LYS HIS GLU ASP THR ALA VAL SEQRES 8 B 125 TYR TYR CYS ALA ALA ARG ALA PRO VAL UNK UNK UNK UNK SEQRES 9 B 125 UNK UNK UNK ASP TYR ASP TYR TRP GLY GLN GLY THR GLN SEQRES 10 B 125 VAL THR VAL SER SER ALA ALA ALA MODRES 8E0G YCM A 57 CYS MODIFIED RESIDUE HET U8S A 54 11 HET YCM A 57 10 HET OLC A 401 16 HET OLC A 402 18 HET CLR A 403 28 HET PO4 A 404 5 HET P6G A 405 19 HET PG4 A 406 13 HET VF1 A 407 32 HETNAM U8S 3-[(2S)-2-HYDROXY-2,3-DIHYDRO-1H-IMIDAZOL-4-YL]-L- HETNAM 2 U8S ALANINE HETNAM YCM S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM CLR CHOLESTEROL HETNAM PO4 PHOSPHATE ION HETNAM P6G HEXAETHYLENE GLYCOL HETNAM PG4 TETRAETHYLENE GLYCOL HETNAM VF1 (2R,3S,3AR,5AR,6R,11BR,11CS)-3A-METHOXY-3,14-DIMETHYL- HETNAM 2 VF1 2-PHENYL-2,3,3A,6,7,11C-HEXAHYDRO-1H-6,11B- HETNAM 3 VF1 (EPIMINOETHANO)-3,5A-METHANONAPHTHO[2,1-G]INDOL-10-OL HETSYN YCM CYSTEINE-S-ACETAMIDE HETSYN OLC 1-OLEOYL-R-GLYCEROL HETSYN P6G POLYETHYLENE GLYCOL PEG400 HETSYN VF1 BU72 FORMUL 1 U8S C6 H11 N3 O3 FORMUL 1 YCM C5 H10 N2 O3 S FORMUL 3 OLC 2(C21 H40 O4) FORMUL 5 CLR C27 H46 O FORMUL 6 PO4 O4 P 3- FORMUL 7 P6G C12 H26 O7 FORMUL 8 PG4 C8 H18 O5 FORMUL 9 VF1 C28 H32 N2 O2 FORMUL 10 HOH *68(H2 O) HELIX 1 AA1 SER A 64 TYR A 96 1 33 HELIX 2 AA2 THR A 101 THR A 120 1 20 HELIX 3 AA3 THR A 120 GLY A 131 1 12 HELIX 4 AA4 PHE A 135 HIS A 171 1 37 HELIX 5 AA5 HIS A 171 ARG A 179 1 9 HELIX 6 AA6 THR A 180 MET A 205 1 26 HELIX 7 AA7 PRO A 224 PHE A 241 1 18 HELIX 8 AA8 PHE A 241 SER A 261 1 21 HELIX 9 AA9 SER A 268 ILE A 306 1 39 HELIX 10 AB1 THR A 311 ALA A 337 1 27 HELIX 11 AB2 ASP A 340 ARG A 345 1 6 HELIX 12 AB3 LYS B 87 THR B 91 5 5 SHEET 1 AA1 2 ALA A 206 ARG A 211 0 SHEET 2 AA1 2 SER A 214 LEU A 219 -1 O THR A 218 N THR A 207 SHEET 1 AA2 4 VAL B 7 SER B 9 0 SHEET 2 AA2 4 LEU B 20 VAL B 25 -1 O VAL B 25 N VAL B 7 SHEET 3 AA2 4 THR B 78 MET B 83 -1 O MET B 83 N LEU B 20 SHEET 4 AA2 4 PHE B 68 ASP B 73 -1 N THR B 69 O GLN B 82 SHEET 1 AA3 6 GLY B 12 VAL B 14 0 SHEET 2 AA3 6 THR B 118 VAL B 122 1 O THR B 121 N GLY B 12 SHEET 3 AA3 6 ALA B 92 ARG B 99 -1 N TYR B 94 O THR B 118 SHEET 4 AA3 6 TYR B 32 ARG B 39 -1 N TYR B 32 O ARG B 99 SHEET 5 AA3 6 GLU B 46 ILE B 51 -1 O GLU B 46 N ARG B 38 SHEET 6 AA3 6 PRO B 58 TYR B 60 -1 O THR B 59 N SER B 50 SHEET 1 AA4 4 GLY B 12 VAL B 14 0 SHEET 2 AA4 4 THR B 118 VAL B 122 1 O THR B 121 N GLY B 12 SHEET 3 AA4 4 ALA B 92 ARG B 99 -1 N TYR B 94 O THR B 118 SHEET 4 AA4 4 TYR B 113 TRP B 114 -1 O TYR B 113 N ALA B 98 SSBOND 1 CYS A 140 CYS A 217 1555 1555 2.19 SSBOND 2 CYS B 24 CYS B 96 1555 1555 2.16 LINK C SER A 53 N U8S A 54 1555 1555 1.35 LINK C U8S A 54 N SER A 55 1555 1555 1.35 LINK O12 U8S A 54 NAS VF1 A 407 1555 1555 1.46 LINK C LEU A 56 N YCM A 57 1555 1555 1.35 LINK C YCM A 57 N PRO A 58 1555 1555 1.36 CISPEP 1 THR A 60 GLY A 61 0 12.02 CISPEP 2 HIS A 223 PRO A 224 0 -11.22 CISPEP 3 GLY A 267 SER A 268 0 13.71 CISPEP 4 CYS A 346 PHE A 347 0 -2.52 CRYST1 44.430 144.000 209.900 90.00 90.00 90.00 I 21 21 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.022507 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006944 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004764 0.00000 ATOM 1 N GLY A 52 5.589 11.489 -71.711 1.00 83.73 N ANISOU 1 N GLY A 52 13340 8349 10123 -918 1234 -153 N ATOM 2 CA GLY A 52 4.797 11.799 -70.487 1.00 85.23 C ANISOU 2 CA GLY A 52 13390 8490 10503 -876 1041 -123 C ATOM 3 C GLY A 52 4.735 13.299 -70.261 1.00 90.44 C ANISOU 3 C GLY A 52 14040 9133 11192 -923 954 19 C ATOM 4 O GLY A 52 5.761 13.943 -70.046 1.00 82.33 O ANISOU 4 O GLY A 52 12939 8120 10223 -960 1075 84 O ATOM 5 N SER A 53 3.524 13.853 -70.347 1.00 92.78 N ANISOU 5 N SER A 53 14412 9394 11444 -923 743 69 N ATOM 6 CA SER A 53 3.261 15.243 -70.024 1.00 94.27 C ANISOU 6 CA SER A 53 14602 9538 11678 -941 631 196 C ATOM 7 C SER A 53 2.959 15.302 -68.524 1.00 88.40 C ANISOU 7 C SER A 53 13664 8756 11169 -870 545 180 C ATOM 8 O SER A 53 2.086 14.584 -68.042 1.00 93.66 O ANISOU 8 O SER A 53 14268 9421 11896 -808 439 111 O ATOM 9 CB SER A 53 2.095 15.763 -70.892 1.00 92.68 C ANISOU 9 CB SER A 53 14578 9324 11312 -953 448 259 C ATOM 10 OG SER A 53 1.378 16.823 -70.283 1.00 99.92 O ANISOU 10 OG SER A 53 15463 10179 12321 -914 280 351 O HETATM 11 CE1 U8S A 54 4.533 15.428 -61.930 1.00 46.88 C ANISOU 11 CE1 U8S A 54 7566 3433 6812 -692 540 105 C HETATM 12 ND1 U8S A 54 4.427 16.163 -63.111 1.00 49.27 N ANISOU 12 ND1 U8S A 54 8031 3716 6973 -752 539 168 N HETATM 13 NE2 U8S A 54 3.860 14.256 -62.466 1.00 47.68 N ANISOU 13 NE2 U8S A 54 7708 3559 6849 -646 532 35 N HETATM 14 CD2 U8S A 54 4.032 14.177 -63.778 1.00 46.76 C ANISOU 14 CD2 U8S A 54 7726 3461 6581 -692 596 43 C HETATM 15 CG U8S A 54 4.428 15.391 -64.194 1.00 50.81 C ANISOU 15 CG U8S A 54 8312 3953 7042 -760 607 133 C HETATM 16 CB U8S A 54 4.746 15.866 -65.572 1.00 59.57 C ANISOU 16 CB U8S A 54 9586 5072 7976 -838 674 189 C HETATM 17 CA U8S A 54 3.505 16.315 -66.351 1.00 67.72 C ANISOU 17 CA U8S A 54 10786 6070 8875 -831 519 230 C HETATM 18 N U8S A 54 3.710 16.139 -67.785 1.00 83.05 N ANISOU 18 N U8S A 54 12893 8048 10615 -890 595 242 N HETATM 19 C U8S A 54 3.001 17.739 -66.060 1.00 71.04 C ANISOU 19 C U8S A 54 11259 6411 9323 -834 387 332 C HETATM 20 O U8S A 54 1.793 17.966 -66.085 1.00 70.28 O ANISOU 20 O U8S A 54 11211 6287 9207 -775 224 348 O HETATM 21 O12 U8S A 54 4.045 15.853 -60.621 1.00 47.66 O ANISOU 21 O12 U8S A 54 7576 3495 7036 -646 431 105 O ATOM 22 N SER A 55 3.914 18.690 -65.785 1.00 69.13 N ANISOU 22 N SER A 55 11005 6130 9130 -903 457 401 N ATOM 23 CA SER A 55 3.536 20.040 -65.381 1.00 72.60 C ANISOU 23 CA SER A 55 11503 6467 9614 -904 343 488 C ATOM 24 C SER A 55 2.792 20.803 -66.514 1.00 78.92 C ANISOU 24 C SER A 55 12516 7219 10252 -912 245 584 C ATOM 25 O SER A 55 1.806 21.502 -66.268 1.00 82.01 O ANISOU 25 O SER A 55 12957 7536 10667 -839 87 627 O ATOM 26 CB SER A 55 4.772 20.827 -64.851 1.00 68.16 C ANISOU 26 CB SER A 55 10889 5870 9138 -1004 444 533 C ATOM 27 OG SER A 55 5.712 21.287 -65.867 1.00 69.50 O ANISOU 27 OG SER A 55 11162 6053 9192 -1132 574 612 O ATOM 28 N LEU A 56 3.255 20.590 -67.752 1.00 81.09 N ANISOU 28 N LEU A 56 12911 7543 10357 -989 342 614 N ATOM 29 CA LEU A 56 2.712 21.181 -68.977 1.00 82.55 C ANISOU 29 CA LEU A 56 13312 7702 10352 -1013 269 711 C ATOM 30 C LEU A 56 1.419 20.543 -69.504 1.00 89.34 C ANISOU 30 C LEU A 56 14224 8606 11115 -929 119 674 C ATOM 31 O LEU A 56 1.414 19.367 -69.890 1.00 86.09 O ANISOU 31 O LEU A 56 13788 8284 10638 -931 172 579 O ATOM 32 CB LEU A 56 3.810 21.117 -70.056 1.00 82.11 C ANISOU 32 CB LEU A 56 13358 7701 10140 -1140 456 748 C ATOM 33 CG LEU A 56 3.663 21.925 -71.351 1.00 81.30 C ANISOU 33 CG LEU A 56 13500 7567 9823 -1208 431 878 C ATOM 34 CD1 LEU A 56 3.990 23.373 -71.071 1.00 80.33 C ANISOU 34 CD1 LEU A 56 13448 7318 9756 -1269 409 1009 C ATOM 35 CD2 LEU A 56 4.564 21.336 -72.437 1.00 80.94 C ANISOU 35 CD2 LEU A 56 13529 7623 9601 -1306 631 863 C HETATM 36 N YCM A 57 0.343 21.357 -69.542 1.00 97.14 N ANISOU 36 N YCM A 57 15289 9528 12092 -858 -71 753 N HETATM 37 CA YCM A 57 -0.943 21.030 -70.153 1.00 99.93 C ANISOU 37 CA YCM A 57 15703 9925 12342 -789 -245 755 C HETATM 38 CB YCM A 57 -2.053 21.861 -69.526 1.00107.57 C ANISOU 38 CB YCM A 57 16638 10819 13414 -666 -437 813 C HETATM 39 SG YCM A 57 -2.980 21.095 -68.179 1.00110.47 S ANISOU 39 SG YCM A 57 16758 11230 13985 -544 -525 693 S HETATM 40 CD YCM A 57 -1.687 20.084 -67.389 1.00114.71 C ANISOU 40 CD YCM A 57 17146 11807 14631 -618 -306 567 C HETATM 41 CE YCM A 57 -1.724 18.645 -67.870 1.00105.42 C ANISOU 41 CE YCM A 57 15940 10736 13379 -652 -258 463 C HETATM 42 OZ1 YCM A 57 -0.805 17.877 -67.602 1.00 89.68 O ANISOU 42 OZ1 YCM A 57 13877 8773 11427 -697 -102 386 O HETATM 43 NZ2 YCM A 57 -2.761 18.318 -68.610 1.00102.88 N ANISOU 43 NZ2 YCM A 57 15681 10464 12944 -632 -396 466 N HETATM 44 C YCM A 57 -0.952 21.403 -71.635 1.00110.60 C ANISOU 44 C YCM A 57 17286 11289 13447 -857 -263 853 C HETATM 45 O YCM A 57 -0.756 22.577 -71.961 1.00105.05 O ANISOU 45 O YCM A 57 16720 10497 12697 -883 -281 986 O ATOM 46 N PRO A 58 -1.220 20.444 -72.560 1.00123.89 N ANISOU 46 N PRO A 58 19037 13074 14962 -889 -268 795 N ATOM 47 CA PRO A 58 -1.289 20.761 -73.992 1.00127.33 C ANISOU 47 CA PRO A 58 19708 13533 15137 -954 -297 886 C ATOM 48 C PRO A 58 -2.469 21.681 -74.232 1.00123.01 C ANISOU 48 C PRO A 58 19247 12939 14554 -871 -539 1012 C ATOM 49 O PRO A 58 -3.602 21.240 -74.118 1.00127.17 O ANISOU 49 O PRO A 58 19700 13518 15103 -790 -714 972 O ATOM 50 CB PRO A 58 -1.499 19.384 -74.658 1.00131.48 C ANISOU 50 CB PRO A 58 20256 14176 15525 -988 -277 759 C ATOM 51 CG PRO A 58 -1.993 18.467 -73.571 1.00121.25 C ANISOU 51 CG PRO A 58 18737 12904 14428 -914 -319 626 C ATOM 52 CD PRO A 58 -1.484 19.019 -72.267 1.00124.85 C ANISOU 52 CD PRO A 58 19028 13282 15125 -869 -252 638 C ATOM 53 N GLN A 59 -2.200 22.955 -74.530 1.00134.94 N ANISOU 53 N GLN A 59 20903 14347 16020 -888 -548 1166 N ATOM 54 CA GLN A 59 -3.177 24.010 -74.275 1.00140.40 C ANISOU 54 CA GLN A 59 21624 14946 16777 -769 -755 1283 C ATOM 55 C GLN A 59 -3.979 24.529 -75.460 1.00137.53 C ANISOU 55 C GLN A 59 21466 14592 16199 -745 -937 1422 C ATOM 56 O GLN A 59 -5.173 24.285 -75.550 1.00126.66 O ANISOU 56 O GLN A 59 20037 13275 14814 -645 -1140 1418 O ATOM 57 CB GLN A 59 -2.512 25.176 -73.524 1.00142.75 C ANISOU 57 CB GLN A 59 21931 15085 17223 -771 -680 1361 C ATOM 58 CG GLN A 59 -3.378 25.753 -72.411 1.00144.02 C ANISOU 58 CG GLN A 59 21968 15158 17596 -611 -825 1364 C ATOM 59 CD GLN A 59 -3.692 24.743 -71.312 1.00151.96 C ANISOU 59 CD GLN A 59 22713 16245 18780 -548 -815 1198 C ATOM 60 OE1 GLN A 59 -3.766 23.535 -71.548 1.00148.74 O ANISOU 60 OE1 GLN A 59 22226 15969 18320 -584 -785 1092 O ATOM 61 NE2 GLN A 59 -3.888 25.243 -70.100 1.00161.73 N ANISOU 61 NE2 GLN A 59 23832 17396 20223 -454 -838 1177 N ATOM 62 N THR A 60 -3.327 25.271 -76.354 1.00142.89 N ANISOU 62 N THR A 60 22373 15213 16704 -840 -868 1553 N ATOM 63 CA THR A 60 -4.055 26.110 -77.301 1.00160.43 C ANISOU 63 CA THR A 60 24807 17397 18753 -797 -1055 1728 C ATOM 64 C THR A 60 -5.373 25.626 -77.922 1.00151.59 C ANISOU 64 C THR A 60 23692 16395 17511 -714 -1298 1730 C ATOM 65 O THR A 60 -5.521 24.425 -78.141 1.00147.53 O ANISOU 65 O THR A 60 23101 16022 16932 -759 -1284 1593 O ATOM 66 CB THR A 60 -3.252 27.351 -77.777 1.00180.83 C ANISOU 66 CB THR A 60 27620 19838 21249 -882 -966 1903 C ATOM 67 OG1 THR A 60 -2.077 26.934 -78.490 1.00194.58 O ANISOU 67 OG1 THR A 60 29463 21645 22824 -1064 -737 1880 O ATOM 68 CG2 THR A 60 -2.809 28.162 -76.555 1.00183.97 C ANISOU 68 CG2 THR A 60 27922 20073 21906 -848 -898 1910 C ATOM 69 N GLY A 61 -6.351 26.513 -78.190 1.00144.56 N ANISOU 69 N GLY A 61 22883 15450 16595 -590 -1528 1882 N ATOM 70 CA GLY A 61 -6.234 27.965 -78.183 1.00140.80 C ANISOU 70 CA GLY A 61 22562 14789 16145 -537 -1564 2066 C ATOM 71 C GLY A 61 -6.183 28.626 -76.814 1.00140.04 C ANISOU 71 C GLY A 61 22321 14543 16345 -431 -1531 2045 C ATOM 72 O GLY A 61 -6.888 28.195 -75.898 1.00134.22 O ANISOU 72 O GLY A 61 21351 13851 15796 -309 -1605 1937 O ATOM 73 N SER A 62 -5.375 29.696 -76.705 1.00131.92 N ANISOU 73 N SER A 62 21444 13335 15344 -484 -1424 2152 N ATOM 74 CA SER A 62 -5.024 30.351 -75.433 1.00119.37 C ANISOU 74 CA SER A 62 19759 11586 14012 -435 -1348 2119 C ATOM 75 C SER A 62 -6.243 30.932 -74.719 1.00113.29 C ANISOU 75 C SER A 62 18899 10735 13410 -198 -1551 2148 C ATOM 76 O SER A 62 -7.138 31.468 -75.370 1.00108.69 O ANISOU 76 O SER A 62 18433 10130 12736 -79 -1748 2285 O ATOM 77 CB SER A 62 -3.993 31.453 -75.672 1.00121.83 C ANISOU 77 CB SER A 62 20295 11714 14281 -561 -1221 2252 C ATOM 78 OG SER A 62 -4.485 32.407 -76.585 1.00114.34 O ANISOU 78 OG SER A 62 19601 10663 13179 -510 -1369 2456 O ATOM 79 N PRO A 63 -6.281 30.905 -73.362 1.00101.72 N ANISOU 79 N PRO A 63 17235 9221 12193 -118 -1505 2028 N ATOM 80 CA PRO A 63 -7.555 30.877 -72.641 1.00 94.79 C ANISOU 80 CA PRO A 63 16176 8369 11470 105 -1673 1987 C ATOM 81 C PRO A 63 -8.322 32.196 -72.643 1.00 90.75 C ANISOU 81 C PRO A 63 15797 7680 11005 297 -1836 2142 C ATOM 82 O PRO A 63 -7.847 33.238 -73.103 1.00 86.24 O ANISOU 82 O PRO A 63 15477 6928 10363 257 -1822 2286 O ATOM 83 CB PRO A 63 -7.149 30.448 -71.210 1.00 90.84 C ANISOU 83 CB PRO A 63 15455 7868 11194 101 -1534 1811 C ATOM 84 CG PRO A 63 -5.715 30.853 -71.078 1.00 93.58 C ANISOU 84 CG PRO A 63 15922 8097 11539 -82 -1333 1815 C ATOM 85 CD PRO A 63 -5.112 30.955 -72.462 1.00 97.33 C ANISOU 85 CD PRO A 63 16621 8587 11773 -239 -1293 1935 C ATOM 86 N SER A 64 -9.558 32.126 -72.148 1.00 87.75 N ANISOU 86 N SER A 64 15242 7355 10744 512 -1995 2116 N ATOM 87 CA SER A 64 -10.339 33.306 -71.952 1.00 89.36 C ANISOU 87 CA SER A 64 15527 7394 11033 734 -2137 2237 C ATOM 88 C SER A 64 -9.700 33.972 -70.739 1.00 93.19 C ANISOU 88 C SER A 64 16021 7679 11709 743 -1991 2166 C ATOM 89 O SER A 64 -9.066 33.297 -69.867 1.00 92.78 O ANISOU 89 O SER A 64 15810 7684 11759 636 -1832 2000 O ATOM 90 CB SER A 64 -11.835 33.006 -71.742 1.00 87.12 C ANISOU 90 CB SER A 64 15023 7249 10830 966 -2335 2225 C ATOM 91 OG SER A 64 -12.111 32.489 -70.454 1.00 83.10 O ANISOU 91 OG SER A 64 14244 6802 10528 1039 -2267 2054 O ATOM 92 N MET A 65 -9.847 35.297 -70.720 1.00 90.17 N ANISOU 92 N MET A 65 15840 7055 11364 864 -2052 2297 N ATOM 93 CA MET A 65 -9.416 36.150 -69.659 1.00 89.06 C ANISOU 93 CA MET A 65 15759 6687 11392 901 -1955 2252 C ATOM 94 C MET A 65 -9.831 35.531 -68.357 1.00 80.25 C ANISOU 94 C MET A 65 14353 5671 10467 1002 -1911 2062 C ATOM 95 O MET A 65 -8.978 35.192 -67.525 1.00 77.72 O ANISOU 95 O MET A 65 13957 5346 10227 864 -1747 1926 O ATOM 96 CB MET A 65 -10.111 37.502 -69.786 1.00 91.22 C ANISOU 96 CB MET A 65 16231 6726 11704 1124 -2096 2408 C ATOM 97 CG MET A 65 -9.927 38.423 -68.581 1.00 95.97 C ANISOU 97 CG MET A 65 16891 7077 12497 1217 -2022 2343 C ATOM 98 SD MET A 65 -8.404 39.393 -68.687 1.00114.83 S ANISOU 98 SD MET A 65 19611 9180 14839 957 -1868 2410 S ATOM 99 CE MET A 65 -8.479 40.107 -70.325 1.00 97.99 C ANISOU 99 CE MET A 65 17798 6949 12485 933 -1992 2684 C ATOM 100 N VAL A 66 -11.155 35.417 -68.200 1.00 79.86 N ANISOU 100 N VAL A 66 14141 5716 10485 1245 -2063 2065 N ATOM 101 CA VAL A 66 -11.824 34.988 -66.974 1.00 82.66 C ANISOU 101 CA VAL A 66 14223 6159 11024 1395 -2046 1912 C ATOM 102 C VAL A 66 -11.330 33.602 -66.459 1.00 79.94 C ANISOU 102 C VAL A 66 13648 6028 10699 1216 -1914 1735 C ATOM 103 O VAL A 66 -11.309 33.352 -65.241 1.00 79.29 O ANISOU 103 O VAL A 66 13406 5957 10765 1252 -1821 1593 O ATOM 104 CB VAL A 66 -13.359 34.971 -67.209 1.00 85.04 C ANISOU 104 CB VAL A 66 14373 6580 11358 1660 -2246 1976 C ATOM 105 CG1 VAL A 66 -14.134 34.491 -65.972 1.00 85.03 C ANISOU 105 CG1 VAL A 66 14070 6696 11541 1815 -2220 1825 C ATOM 106 CG2 VAL A 66 -13.817 36.349 -67.681 1.00 87.39 C ANISOU 106 CG2 VAL A 66 14904 6654 11646 1857 -2376 2156 C ATOM 107 N THR A 67 -10.933 32.706 -67.374 1.00 76.64 N ANISOU 107 N THR A 67 13224 5770 10125 1031 -1904 1745 N ATOM 108 CA THR A 67 -10.516 31.380 -66.933 1.00 74.20 C ANISOU 108 CA THR A 67 12709 5648 9836 883 -1787 1585 C ATOM 109 C THR A 67 -9.101 31.512 -66.352 1.00 69.02 C ANISOU 109 C THR A 67 12134 4876 9216 701 -1588 1513 C ATOM 110 O THR A 67 -8.829 30.964 -65.281 1.00 60.57 O ANISOU 110 O THR A 67 10895 3854 8265 674 -1483 1370 O ATOM 111 CB THR A 67 -10.754 30.239 -68.004 1.00 75.79 C ANISOU 111 CB THR A 67 12847 6076 9875 776 -1852 1590 C ATOM 112 OG1 THR A 67 -9.889 30.380 -69.150 1.00 78.20 O ANISOU 112 OG1 THR A 67 13383 6342 9988 601 -1812 1683 O ATOM 113 CG2 THR A 67 -12.247 30.255 -68.460 1.00 74.14 C ANISOU 113 CG2 THR A 67 12540 5977 9651 969 -2077 1668 C ATOM 114 N ALA A 68 -8.235 32.320 -66.993 1.00 71.16 N ANISOU 114 N ALA A 68 12660 4986 9391 583 -1542 1621 N ATOM 115 CA ALA A 68 -6.879 32.560 -66.431 1.00 70.40 C ANISOU 115 CA ALA A 68 12633 4778 9339 402 -1362 1565 C ATOM 116 C ALA A 68 -6.909 33.331 -65.058 1.00 65.41 C ANISOU 116 C ALA A 68 11985 3976 8893 507 -1330 1493 C ATOM 117 O ALA A 68 -6.179 33.019 -64.127 1.00 61.50 O ANISOU 117 O ALA A 68 11394 3488 8485 409 -1205 1371 O ATOM 118 CB ALA A 68 -5.961 33.227 -67.437 1.00 70.99 C ANISOU 118 CB ALA A 68 12971 4733 9268 234 -1314 1702 C ATOM 119 N ILE A 69 -7.826 34.277 -64.920 1.00 67.22 N ANISOU 119 N ILE A 69 12297 4064 9178 724 -1450 1562 N ATOM 120 CA ILE A 69 -7.910 35.043 -63.669 1.00 67.30 C ANISOU 120 CA ILE A 69 12320 3902 9348 837 -1419 1487 C ATOM 121 C ILE A 69 -8.304 34.013 -62.644 1.00 62.72 C ANISOU 121 C ILE A 69 11445 3512 8872 893 -1376 1320 C ATOM 122 O ILE A 69 -7.626 33.864 -61.594 1.00 60.17 O ANISOU 122 O ILE A 69 11060 3166 8634 807 -1258 1195 O ATOM 123 CB ILE A 69 -8.890 36.245 -63.724 1.00 67.55 C ANISOU 123 CB ILE A 69 12498 3740 9426 1093 -1551 1589 C ATOM 124 CG1 ILE A 69 -8.312 37.304 -64.598 1.00 69.50 C ANISOU 124 CG1 ILE A 69 13067 3764 9576 1006 -1571 1752 C ATOM 125 CG2 ILE A 69 -9.140 36.860 -62.339 1.00 67.95 C ANISOU 125 CG2 ILE A 69 12531 3645 9644 1243 -1511 1477 C ATOM 126 CD1 ILE A 69 -9.265 38.494 -64.851 1.00 71.88 C ANISOU 126 CD1 ILE A 69 13546 3859 9905 1266 -1716 1884 C ATOM 127 N THR A 70 -9.344 33.234 -62.979 1.00 62.26 N ANISOU 127 N THR A 70 11203 3654 8797 1011 -1472 1321 N ATOM 128 CA THR A 70 -9.862 32.207 -62.060 1.00 60.63 C ANISOU 128 CA THR A 70 10711 3639 8687 1067 -1441 1177 C ATOM 129 C THR A 70 -8.749 31.293 -61.573 1.00 54.25 C ANISOU 129 C THR A 70 9813 2919 7881 846 -1288 1059 C ATOM 130 O THR A 70 -8.605 31.062 -60.408 1.00 52.48 O ANISOU 130 O THR A 70 9473 2706 7760 856 -1209 940 O ATOM 131 CB THR A 70 -11.046 31.442 -62.697 1.00 63.90 C ANISOU 131 CB THR A 70 10952 4266 9062 1172 -1573 1211 C ATOM 132 OG1 THR A 70 -12.076 32.377 -63.005 1.00 70.14 O ANISOU 132 OG1 THR A 70 11807 4970 9873 1404 -1718 1321 O ATOM 133 CG2 THR A 70 -11.631 30.446 -61.779 1.00 64.39 C ANISOU 133 CG2 THR A 70 10731 4512 9223 1222 -1542 1079 C ATOM 134 N ILE A 71 -7.941 30.775 -62.486 1.00 53.82 N ANISOU 134 N ILE A 71 9818 2928 7704 650 -1245 1097 N ATOM 135 CA ILE A 71 -7.010 29.744 -62.122 1.00 53.46 C ANISOU 135 CA ILE A 71 9654 2999 7661 470 -1111 991 C ATOM 136 C ILE A 71 -5.887 30.321 -61.237 1.00 53.58 C ANISOU 136 C ILE A 71 9740 2870 7747 364 -990 939 C ATOM 137 O ILE A 71 -5.466 29.772 -60.204 1.00 47.68 O ANISOU 137 O ILE A 71 8853 2180 7085 318 -902 819 O ATOM 138 CB ILE A 71 -6.461 29.054 -63.377 1.00 54.35 C ANISOU 138 CB ILE A 71 9816 3217 7619 306 -1086 1042 C ATOM 139 CG1 ILE A 71 -7.571 28.168 -63.990 1.00 55.84 C ANISOU 139 CG1 ILE A 71 9880 3588 7750 387 -1202 1044 C ATOM 140 CG2 ILE A 71 -5.230 28.203 -63.019 1.00 51.01 C ANISOU 140 CG2 ILE A 71 9309 2869 7204 117 -923 945 C ATOM 141 CD1 ILE A 71 -7.305 27.796 -65.437 1.00 57.68 C ANISOU 141 CD1 ILE A 71 10229 3891 7795 268 -1223 1123 C ATOM 142 N MET A 72 -5.372 31.458 -61.678 1.00 54.99 N ANISOU 142 N MET A 72 10151 2857 7885 312 -991 1037 N ATOM 143 CA MET A 72 -4.442 32.209 -60.858 1.00 59.58 C ANISOU 143 CA MET A 72 10826 3275 8538 217 -906 998 C ATOM 144 C MET A 72 -4.890 32.511 -59.434 1.00 54.42 C ANISOU 144 C MET A 72 10098 2557 8021 353 -909 886 C ATOM 145 O MET A 72 -4.096 32.337 -58.509 1.00 50.71 O ANISOU 145 O MET A 72 9568 2088 7610 245 -818 788 O ATOM 146 CB MET A 72 -4.063 33.530 -61.532 1.00 65.25 C ANISOU 146 CB MET A 72 11829 3763 9199 166 -932 1133 C ATOM 147 CG MET A 72 -2.881 33.334 -62.459 1.00 75.71 C ANISOU 147 CG MET A 72 13233 5123 10410 -79 -840 1203 C ATOM 148 SD MET A 72 -1.489 32.435 -61.740 1.00111.18 S ANISOU 148 SD MET A 72 17546 9749 14950 -302 -672 1077 S ATOM 149 CE MET A 72 -1.403 32.933 -59.993 1.00107.85 C ANISOU 149 CE MET A 72 17074 9211 14695 -253 -660 945 C ATOM 150 N ALA A 73 -6.101 33.065 -59.315 1.00 55.03 N ANISOU 150 N ALA A 73 10200 2569 8140 587 -1012 912 N ATOM 151 CA ALA A 73 -6.759 33.313 -58.067 1.00 54.88 C ANISOU 151 CA ALA A 73 10104 2511 8238 758 -1016 809 C ATOM 152 C ALA A 73 -6.878 32.045 -57.267 1.00 55.03 C ANISOU 152 C ALA A 73 9855 2751 8303 745 -958 682 C ATOM 153 O ALA A 73 -6.634 32.043 -56.074 1.00 57.40 O ANISOU 153 O ALA A 73 10102 3032 8676 743 -893 570 O ATOM 154 CB ALA A 73 -8.138 33.877 -58.366 1.00 57.75 C ANISOU 154 CB ALA A 73 10491 2828 8623 1024 -1139 878 C ATOM 155 N LEU A 74 -7.206 30.935 -57.937 1.00 54.22 N ANISOU 155 N LEU A 74 9598 2855 8148 720 -980 699 N ATOM 156 CA LEU A 74 -7.277 29.678 -57.240 1.00 53.76 C ANISOU 156 CA LEU A 74 9303 2994 8130 690 -923 589 C ATOM 157 C LEU A 74 -5.937 29.365 -56.592 1.00 48.74 C ANISOU 157 C LEU A 74 8659 2353 7508 497 -803 513 C ATOM 158 O LEU A 74 -5.869 29.159 -55.418 1.00 46.14 O ANISOU 158 O LEU A 74 8236 2046 7250 516 -753 412 O ATOM 159 CB LEU A 74 -7.622 28.548 -58.189 1.00 59.45 C ANISOU 159 CB LEU A 74 9904 3908 8778 647 -960 621 C ATOM 160 CG LEU A 74 -8.982 27.879 -58.233 1.00 64.92 C ANISOU 160 CG LEU A 74 10413 4761 9494 794 -1046 611 C ATOM 161 CD1 LEU A 74 -8.917 26.777 -59.292 1.00 61.77 C ANISOU 161 CD1 LEU A 74 9956 4519 8994 674 -1068 637 C ATOM 162 CD2 LEU A 74 -9.279 27.337 -56.850 1.00 64.08 C ANISOU 162 CD2 LEU A 74 10121 4735 9492 849 -981 490 C ATOM 163 N TYR A 75 -4.863 29.338 -57.390 1.00 48.70 N ANISOU 163 N TYR A 75 8749 2327 7428 311 -757 569 N ATOM 164 CA TYR A 75 -3.531 29.018 -56.884 1.00 47.23 C ANISOU 164 CA TYR A 75 8532 2156 7256 123 -647 512 C ATOM 165 C TYR A 75 -3.110 30.015 -55.813 1.00 45.94 C ANISOU 165 C TYR A 75 8466 1828 7163 114 -627 462 C ATOM 166 O TYR A 75 -2.585 29.617 -54.792 1.00 43.84 O ANISOU 166 O TYR A 75 8098 1612 6948 55 -569 368 O ATOM 167 CB TYR A 75 -2.467 28.928 -58.009 1.00 50.00 C ANISOU 167 CB TYR A 75 8969 2514 7513 -68 -592 592 C ATOM 168 CG TYR A 75 -2.506 27.606 -58.819 1.00 50.44 C ANISOU 168 CG TYR A 75 8901 2764 7498 -110 -567 592 C ATOM 169 CD1 TYR A 75 -1.904 26.477 -58.354 1.00 50.13 C ANISOU 169 CD1 TYR A 75 8695 2864 7489 -188 -480 509 C ATOM 170 CD2 TYR A 75 -3.120 27.521 -60.067 1.00 54.75 C ANISOU 170 CD2 TYR A 75 9517 3345 7942 -72 -634 678 C ATOM 171 CE1 TYR A 75 -1.946 25.300 -59.069 1.00 52.03 C ANISOU 171 CE1 TYR A 75 8848 3255 7667 -220 -454 500 C ATOM 172 CE2 TYR A 75 -3.142 26.319 -60.801 1.00 56.22 C ANISOU 172 CE2 TYR A 75 9613 3696 8052 -120 -612 663 C ATOM 173 CZ TYR A 75 -2.575 25.214 -60.284 1.00 50.50 C ANISOU 173 CZ TYR A 75 8730 3090 7367 -190 -518 570 C ATOM 174 OH TYR A 75 -2.570 24.011 -60.967 1.00 52.07 O ANISOU 174 OH TYR A 75 8858 3430 7496 -234 -488 544 O ATOM 175 N SER A 76 -3.423 31.307 -55.985 1.00 45.24 N ANISOU 175 N SER A 76 8578 1535 7075 186 -685 520 N ATOM 176 CA SER A 76 -3.004 32.243 -54.988 1.00 47.18 C ANISOU 176 CA SER A 76 8939 1609 7379 164 -666 462 C ATOM 177 C SER A 76 -3.652 32.044 -53.656 1.00 46.13 C ANISOU 177 C SER A 76 8693 1515 7321 307 -663 337 C ATOM 178 O SER A 76 -2.998 32.102 -52.636 1.00 47.32 O ANISOU 178 O SER A 76 8832 1644 7505 222 -615 246 O ATOM 179 CB SER A 76 -3.314 33.691 -55.410 1.00 50.20 C ANISOU 179 CB SER A 76 9585 1738 7753 237 -730 546 C ATOM 180 OG SER A 76 -2.681 33.821 -56.611 1.00 56.42 O ANISOU 180 OG SER A 76 10475 2503 8459 90 -724 666 O ATOM 181 N ILE A 77 -4.972 31.924 -53.675 1.00 46.58 N ANISOU 181 N ILE A 77 8680 1620 7398 529 -718 339 N ATOM 182 CA ILE A 77 -5.724 31.840 -52.458 1.00 47.85 C ANISOU 182 CA ILE A 77 8744 1814 7625 687 -706 229 C ATOM 183 C ILE A 77 -5.308 30.625 -51.650 1.00 45.14 C ANISOU 183 C ILE A 77 8193 1665 7295 593 -636 136 C ATOM 184 O ILE A 77 -5.092 30.735 -50.455 1.00 43.43 O ANISOU 184 O ILE A 77 7965 1426 7108 591 -594 35 O ATOM 185 CB ILE A 77 -7.227 31.856 -52.777 1.00 53.58 C ANISOU 185 CB ILE A 77 9398 2587 8372 936 -777 267 C ATOM 186 CG1 ILE A 77 -7.588 33.267 -53.245 1.00 58.92 C ANISOU 186 CG1 ILE A 77 10311 3026 9052 1060 -843 344 C ATOM 187 CG2 ILE A 77 -8.067 31.534 -51.560 1.00 55.78 C ANISOU 187 CG2 ILE A 77 9523 2956 8713 1095 -743 156 C ATOM 188 CD1 ILE A 77 -8.932 33.337 -53.925 1.00 63.18 C ANISOU 188 CD1 ILE A 77 10792 3615 9601 1286 -937 425 C ATOM 189 N VAL A 78 -5.144 29.477 -52.326 1.00 42.17 N ANISOU 189 N VAL A 78 7670 1467 6886 508 -625 172 N ATOM 190 CA VAL A 78 -4.881 28.251 -51.632 1.00 41.15 C ANISOU 190 CA VAL A 78 7345 1516 6772 444 -565 96 C ATOM 191 C VAL A 78 -3.505 28.358 -51.001 1.00 41.29 C ANISOU 191 C VAL A 78 7404 1491 6792 263 -506 51 C ATOM 192 O VAL A 78 -3.244 27.926 -49.877 1.00 39.04 O ANISOU 192 O VAL A 78 7030 1271 6533 240 -466 -36 O ATOM 193 CB VAL A 78 -4.995 27.080 -52.635 1.00 41.16 C ANISOU 193 CB VAL A 78 7220 1684 6734 394 -570 148 C ATOM 194 CG1 VAL A 78 -4.369 25.840 -52.088 1.00 39.98 C ANISOU 194 CG1 VAL A 78 6911 1683 6595 287 -500 87 C ATOM 195 CG2 VAL A 78 -6.482 26.796 -52.915 1.00 42.49 C ANISOU 195 CG2 VAL A 78 7291 1937 6914 574 -637 167 C ATOM 196 N CYS A 79 -2.588 28.992 -51.736 1.00 44.46 N ANISOU 196 N CYS A 79 7948 1783 7160 122 -504 117 N ATOM 197 CA CYS A 79 -1.212 29.092 -51.308 1.00 44.36 C ANISOU 197 CA CYS A 79 7957 1747 7151 -74 -455 90 C ATOM 198 C CYS A 79 -1.183 29.945 -50.028 1.00 46.80 C ANISOU 198 C CYS A 79 8358 1929 7494 -47 -466 1 C ATOM 199 O CYS A 79 -0.626 29.522 -48.999 1.00 47.01 O ANISOU 199 O CYS A 79 8296 2028 7537 -117 -436 -79 O ATOM 200 CB CYS A 79 -0.412 29.725 -52.416 1.00 46.44 C ANISOU 200 CB CYS A 79 8363 1912 7372 -219 -449 190 C ATOM 201 SG CYS A 79 1.269 30.068 -51.903 1.00 50.42 S ANISOU 201 SG CYS A 79 8892 2375 7889 -473 -397 168 S ATOM 202 N VAL A 80 -1.821 31.121 -50.090 1.00 46.73 N ANISOU 202 N VAL A 80 8535 1730 7490 65 -512 13 N ATOM 203 CA VAL A 80 -1.823 32.086 -49.003 1.00 48.06 C ANISOU 203 CA VAL A 80 8842 1737 7679 97 -521 -75 C ATOM 204 C VAL A 80 -2.496 31.492 -47.759 1.00 47.09 C ANISOU 204 C VAL A 80 8584 1733 7578 229 -498 -188 C ATOM 205 O VAL A 80 -1.948 31.521 -46.690 1.00 45.18 O ANISOU 205 O VAL A 80 8344 1491 7332 153 -478 -278 O ATOM 206 CB VAL A 80 -2.510 33.394 -49.411 1.00 48.64 C ANISOU 206 CB VAL A 80 9146 1577 7759 230 -571 -33 C ATOM 207 CG1 VAL A 80 -2.748 34.277 -48.202 1.00 51.99 C ANISOU 207 CG1 VAL A 80 9710 1841 8204 313 -572 -148 C ATOM 208 CG2 VAL A 80 -1.633 34.147 -50.409 1.00 50.78 C ANISOU 208 CG2 VAL A 80 9596 1697 8002 54 -587 72 C ATOM 209 N VAL A 81 -3.714 30.991 -47.927 1.00 46.54 N ANISOU 209 N VAL A 81 8399 1763 7523 424 -504 -178 N ATOM 210 CA VAL A 81 -4.419 30.375 -46.844 1.00 47.92 C ANISOU 210 CA VAL A 81 8431 2064 7711 545 -470 -270 C ATOM 211 C VAL A 81 -3.604 29.175 -46.260 1.00 45.70 C ANISOU 211 C VAL A 81 7980 1967 7418 392 -426 -307 C ATOM 212 O VAL A 81 -3.489 29.058 -45.078 1.00 44.16 O ANISOU 212 O VAL A 81 7761 1803 7214 391 -399 -397 O ATOM 213 CB VAL A 81 -5.832 29.886 -47.265 1.00 47.99 C ANISOU 213 CB VAL A 81 8304 2185 7744 749 -484 -234 C ATOM 214 CG1 VAL A 81 -6.436 29.006 -46.178 1.00 47.64 C ANISOU 214 CG1 VAL A 81 8077 2313 7711 829 -431 -317 C ATOM 215 CG2 VAL A 81 -6.719 31.077 -47.631 1.00 48.96 C ANISOU 215 CG2 VAL A 81 8579 2136 7888 940 -529 -204 C ATOM 216 N GLY A 82 -3.042 28.322 -47.115 1.00 43.54 N ANISOU 216 N GLY A 82 7601 1804 7137 273 -421 -235 N ATOM 217 CA GLY A 82 -2.207 27.240 -46.644 1.00 44.45 C ANISOU 217 CA GLY A 82 7569 2071 7248 142 -382 -259 C ATOM 218 C GLY A 82 -0.974 27.651 -45.855 1.00 44.41 C ANISOU 218 C GLY A 82 7629 2013 7234 -19 -378 -307 C ATOM 219 O GLY A 82 -0.694 27.088 -44.756 1.00 39.88 O ANISOU 219 O GLY A 82 6966 1535 6653 -46 -360 -373 O ATOM 220 N LEU A 83 -0.248 28.636 -46.398 1.00 42.98 N ANISOU 220 N LEU A 83 7604 1680 7047 -133 -401 -270 N ATOM 221 CA LEU A 83 0.954 29.133 -45.733 1.00 47.57 C ANISOU 221 CA LEU A 83 8250 2203 7620 -313 -410 -309 C ATOM 222 C LEU A 83 0.582 29.756 -44.403 1.00 48.12 C ANISOU 222 C LEU A 83 8419 2191 7674 -244 -429 -423 C ATOM 223 O LEU A 83 1.202 29.485 -43.404 1.00 49.46 O ANISOU 223 O LEU A 83 8539 2426 7825 -331 -432 -486 O ATOM 224 CB LEU A 83 1.791 30.102 -46.575 1.00 50.96 C ANISOU 224 CB LEU A 83 8833 2481 8048 -470 -427 -242 C ATOM 225 CG LEU A 83 2.507 29.326 -47.703 1.00 53.89 C ANISOU 225 CG LEU A 83 9079 2975 8420 -584 -387 -144 C ATOM 226 CD1 LEU A 83 3.265 30.254 -48.651 1.00 57.10 C ANISOU 226 CD1 LEU A 83 9634 3246 8817 -741 -388 -60 C ATOM 227 CD2 LEU A 83 3.451 28.241 -47.192 1.00 55.57 C ANISOU 227 CD2 LEU A 83 9088 3377 8647 -693 -355 -163 C ATOM 228 N PHE A 84 -0.527 30.480 -44.372 1.00 50.77 N ANISOU 228 N PHE A 84 8878 2403 8011 -63 -436 -449 N ATOM 229 CA PHE A 84 -0.889 31.252 -43.198 1.00 53.49 C ANISOU 229 CA PHE A 84 9357 2634 8331 13 -442 -564 C ATOM 230 C PHE A 84 -1.341 30.332 -42.058 1.00 50.46 C ANISOU 230 C PHE A 84 8822 2428 7924 98 -405 -643 C ATOM 231 O PHE A 84 -0.849 30.458 -40.917 1.00 51.16 O ANISOU 231 O PHE A 84 8953 2518 7968 25 -411 -733 O ATOM 232 CB PHE A 84 -1.960 32.293 -43.503 1.00 55.46 C ANISOU 232 CB PHE A 84 9779 2696 8595 208 -451 -569 C ATOM 233 CG PHE A 84 -2.558 32.895 -42.281 1.00 62.01 C ANISOU 233 CG PHE A 84 10722 3440 9400 341 -432 -698 C ATOM 234 CD1 PHE A 84 -1.849 33.820 -41.545 1.00 68.34 C ANISOU 234 CD1 PHE A 84 11727 4074 10166 224 -455 -785 C ATOM 235 CD2 PHE A 84 -3.802 32.503 -41.836 1.00 63.61 C ANISOU 235 CD2 PHE A 84 10823 3740 9607 569 -386 -739 C ATOM 236 CE1 PHE A 84 -2.378 34.365 -40.394 1.00 72.28 C ANISOU 236 CE1 PHE A 84 12348 4490 10624 345 -430 -919 C ATOM 237 CE2 PHE A 84 -4.339 33.048 -40.688 1.00 67.92 C ANISOU 237 CE2 PHE A 84 11474 4215 10119 697 -349 -865 C ATOM 238 CZ PHE A 84 -3.633 33.991 -39.981 1.00 69.10 C ANISOU 238 CZ PHE A 84 11847 4184 10223 591 -370 -959 C ATOM 239 N GLY A 85 -2.301 29.454 -42.358 1.00 46.28 N ANISOU 239 N GLY A 85 8128 2041 7416 245 -372 -607 N ATOM 240 CA GLY A 85 -2.817 28.536 -41.366 1.00 46.40 C ANISOU 240 CA GLY A 85 7996 2225 7408 323 -328 -663 C ATOM 241 C GLY A 85 -1.732 27.640 -40.798 1.00 43.35 C ANISOU 241 C GLY A 85 7497 1976 6997 150 -330 -667 C ATOM 242 O GLY A 85 -1.662 27.391 -39.591 1.00 43.63 O ANISOU 242 O GLY A 85 7517 2078 6984 147 -316 -742 O ATOM 243 N ASN A 86 -0.842 27.167 -41.662 1.00 42.76 N ANISOU 243 N ASN A 86 7349 1948 6951 9 -348 -584 N ATOM 244 CA ASN A 86 0.172 26.225 -41.186 1.00 41.09 C ANISOU 244 CA ASN A 86 7005 1879 6729 -130 -350 -575 C ATOM 245 C ASN A 86 1.320 26.907 -40.438 1.00 42.41 C ANISOU 245 C ASN A 86 7271 1982 6863 -294 -397 -626 C ATOM 246 O ASN A 86 1.823 26.373 -39.466 1.00 41.16 O ANISOU 246 O ASN A 86 7042 1929 6669 -353 -411 -661 O ATOM 247 CB ASN A 86 0.622 25.313 -42.309 1.00 38.67 C ANISOU 247 CB ASN A 86 6559 1668 6464 -193 -334 -476 C ATOM 248 CG ASN A 86 -0.459 24.377 -42.704 1.00 38.22 C ANISOU 248 CG ASN A 86 6382 1713 6425 -56 -297 -446 C ATOM 249 OD1 ASN A 86 -0.835 23.528 -41.886 1.00 37.59 O ANISOU 249 OD1 ASN A 86 6199 1751 6333 -4 -272 -474 O ATOM 250 ND2 ASN A 86 -0.989 24.505 -43.901 1.00 35.85 N ANISOU 250 ND2 ASN A 86 6100 1374 6149 -3 -298 -388 N ATOM 251 N PHE A 87 1.713 28.109 -40.873 1.00 44.50 N ANISOU 251 N PHE A 87 7706 2068 7133 -373 -431 -628 N ATOM 252 CA PHE A 87 2.670 28.878 -40.092 1.00 45.57 C ANISOU 252 CA PHE A 87 7959 2124 7232 -535 -485 -691 C ATOM 253 C PHE A 87 2.120 29.260 -38.728 1.00 44.00 C ANISOU 253 C PHE A 87 7867 1889 6962 -450 -492 -815 C ATOM 254 O PHE A 87 2.862 29.346 -37.699 1.00 43.55 O ANISOU 254 O PHE A 87 7836 1861 6848 -573 -539 -880 O ATOM 255 CB PHE A 87 3.211 30.085 -40.864 1.00 54.30 C ANISOU 255 CB PHE A 87 9238 3033 8361 -657 -517 -662 C ATOM 256 CG PHE A 87 4.473 29.772 -41.619 1.00 60.48 C ANISOU 256 CG PHE A 87 9911 3887 9181 -860 -526 -569 C ATOM 257 CD1 PHE A 87 4.426 29.076 -42.789 1.00 53.71 C ANISOU 257 CD1 PHE A 87 8928 3113 8365 -832 -478 -467 C ATOM 258 CD2 PHE A 87 5.709 30.213 -41.146 1.00 75.26 C ANISOU 258 CD2 PHE A 87 11808 5743 11043 -1083 -581 -590 C ATOM 259 CE1 PHE A 87 5.541 28.824 -43.527 1.00 56.93 C ANISOU 259 CE1 PHE A 87 9241 3586 8804 -1001 -466 -386 C ATOM 260 CE2 PHE A 87 6.860 29.931 -41.866 1.00 79.86 C ANISOU 260 CE2 PHE A 87 12266 6408 11668 -1263 -577 -500 C ATOM 261 CZ PHE A 87 6.768 29.209 -43.065 1.00 69.55 C ANISOU 261 CZ PHE A 87 10835 5188 10404 -1212 -509 -398 C ATOM 262 N LEU A 88 0.817 29.537 -38.695 1.00 42.54 N ANISOU 262 N LEU A 88 7750 1641 6773 -240 -446 -852 N ATOM 263 CA LEU A 88 0.197 29.897 -37.464 1.00 44.06 C ANISOU 263 CA LEU A 88 8045 1803 6894 -135 -428 -973 C ATOM 264 C LEU A 88 0.242 28.708 -36.453 1.00 42.19 C ANISOU 264 C LEU A 88 7641 1787 6602 -135 -408 -992 C ATOM 265 O LEU A 88 0.610 28.882 -35.303 1.00 42.31 O ANISOU 265 O LEU A 88 7730 1815 6533 -196 -434 -1079 O ATOM 266 CB LEU A 88 -1.200 30.395 -37.717 1.00 45.61 C ANISOU 266 CB LEU A 88 8316 1904 7110 103 -372 -996 C ATOM 267 CG LEU A 88 -1.934 30.682 -36.432 1.00 47.68 C ANISOU 267 CG LEU A 88 8667 2157 7294 237 -326 -1125 C ATOM 268 CD1 LEU A 88 -1.247 31.801 -35.603 1.00 50.28 C ANISOU 268 CD1 LEU A 88 9246 2310 7549 124 -374 -1242 C ATOM 269 CD2 LEU A 88 -3.373 31.060 -36.769 1.00 50.59 C ANISOU 269 CD2 LEU A 88 9058 2463 7700 498 -261 -1132 C ATOM 270 N VAL A 89 -0.137 27.508 -36.907 1.00 39.82 N ANISOU 270 N VAL A 89 7132 1652 6345 -71 -367 -909 N ATOM 271 CA VAL A 89 0.016 26.314 -36.086 1.00 40.13 C ANISOU 271 CA VAL A 89 7016 1889 6343 -88 -354 -902 C ATOM 272 C VAL A 89 1.497 26.163 -35.585 1.00 41.84 C ANISOU 272 C VAL A 89 7214 2157 6528 -299 -433 -897 C ATOM 273 O VAL A 89 1.748 26.008 -34.367 1.00 43.98 O ANISOU 273 O VAL A 89 7508 2495 6709 -335 -458 -958 O ATOM 274 CB VAL A 89 -0.433 25.062 -36.879 1.00 37.69 C ANISOU 274 CB VAL A 89 6501 1719 6101 -24 -309 -800 C ATOM 275 CG1 VAL A 89 -0.226 23.795 -36.063 1.00 38.05 C ANISOU 275 CG1 VAL A 89 6401 1948 6109 -48 -296 -779 C ATOM 276 CG2 VAL A 89 -1.891 25.198 -37.211 1.00 37.97 C ANISOU 276 CG2 VAL A 89 6536 1731 6161 171 -246 -808 C ATOM 277 N MET A 90 2.470 26.237 -36.503 1.00 41.69 N ANISOU 277 N MET A 90 7153 2113 6575 -439 -474 -825 N ATOM 278 CA MET A 90 3.857 26.101 -36.120 1.00 43.98 C ANISOU 278 CA MET A 90 7393 2468 6851 -633 -549 -810 C ATOM 279 C MET A 90 4.218 27.126 -35.121 1.00 46.43 C ANISOU 279 C MET A 90 7884 2680 7076 -725 -615 -917 C ATOM 280 O MET A 90 4.961 26.830 -34.217 1.00 47.79 O ANISOU 280 O MET A 90 8017 2951 7191 -829 -678 -937 O ATOM 281 CB MET A 90 4.813 26.148 -37.303 1.00 44.65 C ANISOU 281 CB MET A 90 7405 2537 7021 -768 -566 -718 C ATOM 282 CG MET A 90 4.571 24.888 -38.135 1.00 46.92 C ANISOU 282 CG MET A 90 7501 2954 7374 -684 -503 -622 C ATOM 283 SD MET A 90 5.777 24.647 -39.470 1.00 51.52 S ANISOU 283 SD MET A 90 7962 3570 8043 -830 -497 -511 S ATOM 284 CE MET A 90 5.075 25.743 -40.688 1.00 50.16 C ANISOU 284 CE MET A 90 7960 3203 7895 -788 -464 -499 C ATOM 285 N TYR A 91 3.693 28.353 -35.270 1.00 47.64 N ANISOU 285 N TYR A 91 8251 2632 7220 -684 -606 -987 N ATOM 286 CA TYR A 91 4.086 29.412 -34.371 1.00 48.74 C ANISOU 286 CA TYR A 91 8598 2646 7275 -787 -671 -1101 C ATOM 287 C TYR A 91 3.519 29.113 -33.010 1.00 49.34 C ANISOU 287 C TYR A 91 8711 2803 7235 -691 -655 -1197 C ATOM 288 O TYR A 91 4.203 29.259 -32.016 1.00 49.23 O ANISOU 288 O TYR A 91 8753 2822 7128 -818 -731 -1261 O ATOM 289 CB TYR A 91 3.611 30.774 -34.857 1.00 49.71 C ANISOU 289 CB TYR A 91 8959 2511 7417 -748 -658 -1154 C ATOM 290 CG TYR A 91 3.664 31.865 -33.827 1.00 51.93 C ANISOU 290 CG TYR A 91 9497 2636 7599 -797 -702 -1301 C ATOM 291 CD1 TYR A 91 4.840 32.532 -33.564 1.00 55.32 C ANISOU 291 CD1 TYR A 91 10026 2991 8002 -1046 -804 -1333 C ATOM 292 CD2 TYR A 91 2.512 32.288 -33.149 1.00 53.64 C ANISOU 292 CD2 TYR A 91 9865 2768 7747 -594 -637 -1413 C ATOM 293 CE1 TYR A 91 4.884 33.581 -32.639 1.00 56.24 C ANISOU 293 CE1 TYR A 91 10408 2942 8019 -1104 -851 -1481 C ATOM 294 CE2 TYR A 91 2.547 33.296 -32.207 1.00 54.03 C ANISOU 294 CE2 TYR A 91 10174 2661 7695 -630 -667 -1562 C ATOM 295 CZ TYR A 91 3.738 33.932 -31.941 1.00 56.80 C ANISOU 295 CZ TYR A 91 10640 2929 8013 -890 -780 -1600 C ATOM 296 OH TYR A 91 3.810 34.996 -31.025 1.00 61.34 O ANISOU 296 OH TYR A 91 11503 3324 8479 -948 -820 -1760 O ATOM 297 N VAL A 92 2.228 28.785 -32.974 1.00 49.42 N ANISOU 297 N VAL A 92 8702 2836 7241 -468 -556 -1210 N ATOM 298 CA VAL A 92 1.545 28.519 -31.710 1.00 53.35 C ANISOU 298 CA VAL A 92 9238 3412 7621 -358 -513 -1298 C ATOM 299 C VAL A 92 2.242 27.345 -30.959 1.00 52.59 C ANISOU 299 C VAL A 92 8977 3537 7467 -453 -559 -1250 C ATOM 300 O VAL A 92 2.378 27.398 -29.739 1.00 50.69 O ANISOU 300 O VAL A 92 8821 3344 7095 -487 -588 -1331 O ATOM 301 CB VAL A 92 0.039 28.170 -31.889 1.00 53.63 C ANISOU 301 CB VAL A 92 9218 3478 7680 -108 -388 -1293 C ATOM 302 CG1 VAL A 92 -0.517 27.559 -30.611 1.00 52.76 C ANISOU 302 CG1 VAL A 92 9086 3512 7450 -25 -332 -1350 C ATOM 303 CG2 VAL A 92 -0.744 29.431 -32.230 1.00 56.68 C ANISOU 303 CG2 VAL A 92 9801 3647 8088 21 -347 -1369 C ATOM 304 N ILE A 93 2.689 26.327 -31.699 1.00 50.47 N ANISOU 304 N ILE A 93 8491 3393 7292 -492 -566 -1119 N ATOM 305 CA ILE A 93 3.393 25.198 -31.082 1.00 54.16 C ANISOU 305 CA ILE A 93 8800 4056 7723 -568 -613 -1058 C ATOM 306 C ILE A 93 4.731 25.639 -30.463 1.00 57.00 C ANISOU 306 C ILE A 93 9211 4424 8023 -779 -747 -1088 C ATOM 307 O ILE A 93 5.014 25.337 -29.303 1.00 57.61 O ANISOU 307 O ILE A 93 9303 4602 7982 -820 -800 -1121 O ATOM 308 CB ILE A 93 3.732 24.070 -32.074 1.00 52.97 C ANISOU 308 CB ILE A 93 8419 4014 7693 -571 -596 -916 C ATOM 309 CG1 ILE A 93 2.504 23.437 -32.712 1.00 55.39 C ANISOU 309 CG1 ILE A 93 8647 4341 8059 -392 -484 -873 C ATOM 310 CG2 ILE A 93 4.533 23.000 -31.384 1.00 57.63 C ANISOU 310 CG2 ILE A 93 8867 4782 8248 -640 -655 -853 C ATOM 311 CD1 ILE A 93 1.531 22.760 -31.810 1.00 64.92 C ANISOU 311 CD1 ILE A 93 9831 5647 9187 -265 -416 -894 C ATOM 312 N VAL A 94 5.566 26.309 -31.268 1.00 55.73 N ANISOU 312 N VAL A 94 9064 4167 7943 -921 -803 -1065 N ATOM 313 CA VAL A 94 6.925 26.653 -30.908 1.00 58.25 C ANISOU 313 CA VAL A 94 9379 4512 8239 -1145 -934 -1069 C ATOM 314 C VAL A 94 6.895 27.673 -29.769 1.00 62.24 C ANISOU 314 C VAL A 94 10129 4918 8600 -1213 -998 -1218 C ATOM 315 O VAL A 94 7.693 27.619 -28.876 1.00 64.96 O ANISOU 315 O VAL A 94 10473 5352 8857 -1350 -1108 -1243 O ATOM 316 CB VAL A 94 7.671 27.250 -32.125 1.00 63.06 C ANISOU 316 CB VAL A 94 9964 5024 8971 -1280 -954 -1012 C ATOM 317 CG1 VAL A 94 8.921 27.990 -31.722 1.00 68.32 C ANISOU 317 CG1 VAL A 94 10682 5668 9607 -1531 -1087 -1046 C ATOM 318 CG2 VAL A 94 8.033 26.186 -33.108 1.00 58.55 C ANISOU 318 CG2 VAL A 94 9145 4583 8520 -1257 -911 -871 C ATOM 319 N ARG A 95 5.941 28.596 -29.823 1.00 62.86 N ANISOU 319 N ARG A 95 10420 4810 8653 -1105 -928 -1317 N ATOM 320 CA ARG A 95 5.783 29.659 -28.831 1.00 68.70 C ANISOU 320 CA ARG A 95 11432 5415 9256 -1143 -965 -1478 C ATOM 321 C ARG A 95 5.121 29.210 -27.531 1.00 68.93 C ANISOU 321 C ARG A 95 11513 5551 9127 -1026 -930 -1555 C ATOM 322 O ARG A 95 5.674 29.412 -26.499 1.00 74.11 O ANISOU 322 O ARG A 95 12264 6246 9649 -1148 -1024 -1630 O ATOM 323 CB ARG A 95 4.970 30.836 -29.440 1.00 69.27 C ANISOU 323 CB ARG A 95 11721 5228 9372 -1041 -890 -1551 C ATOM 324 CG ARG A 95 4.652 32.013 -28.531 1.00 75.04 C ANISOU 324 CG ARG A 95 12766 5774 9972 -1041 -902 -1731 C ATOM 325 CD ARG A 95 5.936 32.725 -28.163 1.00 78.55 C ANISOU 325 CD ARG A 95 13324 6153 10369 -1329 -1055 -1782 C ATOM 326 NE ARG A 95 5.740 33.783 -27.195 1.00 84.20 N ANISOU 326 NE ARG A 95 14356 6698 10940 -1356 -1081 -1966 N ATOM 327 CZ ARG A 95 6.270 33.837 -25.967 1.00 95.63 C ANISOU 327 CZ ARG A 95 15898 8215 12222 -1490 -1180 -2066 C ATOM 328 NH1 ARG A 95 7.025 32.847 -25.501 1.00 96.37 N ANISOU 328 NH1 ARG A 95 15778 8563 12276 -1600 -1270 -1986 N ATOM 329 NH2 ARG A 95 6.042 34.909 -25.188 1.00 92.08 N ANISOU 329 NH2 ARG A 95 15774 7572 11640 -1510 -1194 -2249 N ATOM 330 N TYR A 96 3.910 28.648 -27.607 1.00 65.96 N ANISOU 330 N TYR A 96 11081 5221 8761 -796 -794 -1538 N ATOM 331 CA TYR A 96 3.081 28.350 -26.431 1.00 67.65 C ANISOU 331 CA TYR A 96 11367 5517 8822 -665 -724 -1618 C ATOM 332 C TYR A 96 3.120 26.847 -25.976 1.00 66.55 C ANISOU 332 C TYR A 96 11007 5630 8650 -636 -716 -1507 C ATOM 333 O TYR A 96 3.539 26.542 -24.891 1.00 70.31 O ANISOU 333 O TYR A 96 11514 6218 8983 -710 -781 -1533 O ATOM 334 CB TYR A 96 1.624 28.792 -26.683 1.00 66.78 C ANISOU 334 CB TYR A 96 11347 5292 8733 -425 -568 -1680 C ATOM 335 CG TYR A 96 1.455 30.292 -26.872 1.00 77.50 C ANISOU 335 CG TYR A 96 12968 6386 10091 -417 -567 -1806 C ATOM 336 CD1 TYR A 96 1.612 31.176 -25.797 1.00 81.11 C ANISOU 336 CD1 TYR A 96 13689 6742 10388 -474 -603 -1971 C ATOM 337 CD2 TYR A 96 1.151 30.834 -28.142 1.00 76.20 C ANISOU 337 CD2 TYR A 96 12806 6063 10082 -354 -535 -1759 C ATOM 338 CE1 TYR A 96 1.464 32.544 -25.973 1.00 81.12 C ANISOU 338 CE1 TYR A 96 13952 6476 10393 -465 -601 -2089 C ATOM 339 CE2 TYR A 96 1.000 32.195 -28.337 1.00 76.39 C ANISOU 339 CE2 TYR A 96 13083 5828 10113 -340 -537 -1861 C ATOM 340 CZ TYR A 96 1.153 33.036 -27.247 1.00 83.52 C ANISOU 340 CZ TYR A 96 14249 6621 10865 -393 -567 -2027 C ATOM 341 OH TYR A 96 1.012 34.369 -27.435 1.00 85.87 O ANISOU 341 OH TYR A 96 14815 6640 11170 -378 -567 -2130 O ATOM 342 N THR A 97 2.690 25.917 -26.840 1.00 68.88 N ANISOU 342 N THR A 97 11092 6004 9076 -534 -641 -1381 N ATOM 343 CA THR A 97 2.418 24.529 -26.424 1.00 67.05 C ANISOU 343 CA THR A 97 10687 5974 8816 -467 -599 -1285 C ATOM 344 C THR A 97 3.699 23.747 -26.189 1.00 66.62 C ANISOU 344 C THR A 97 10496 6059 8758 -624 -729 -1188 C ATOM 345 O THR A 97 3.757 22.931 -25.282 1.00 66.48 O ANISOU 345 O THR A 97 10435 6189 8636 -619 -746 -1152 O ATOM 346 CB THR A 97 1.434 23.780 -27.357 1.00 64.22 C ANISOU 346 CB THR A 97 10168 5645 8588 -308 -474 -1195 C ATOM 347 OG1 THR A 97 1.986 23.634 -28.668 1.00 63.31 O ANISOU 347 OG1 THR A 97 9927 5492 8637 -363 -509 -1102 O ATOM 348 CG2 THR A 97 0.103 24.514 -27.447 1.00 64.46 C ANISOU 348 CG2 THR A 97 10312 5567 8612 -134 -350 -1287 C ATOM 349 N LYS A 98 4.726 24.020 -26.997 1.00 67.78 N ANISOU 349 N LYS A 98 10576 6162 9017 -759 -820 -1141 N ATOM 350 CA LYS A 98 6.083 23.520 -26.791 1.00 70.38 C ANISOU 350 CA LYS A 98 10777 6612 9351 -919 -958 -1061 C ATOM 351 C LYS A 98 6.531 22.114 -27.321 1.00 77.36 C ANISOU 351 C LYS A 98 11400 7647 10346 -894 -957 -896 C ATOM 352 O LYS A 98 7.734 21.811 -27.282 1.00 92.25 O ANISOU 352 O LYS A 98 13167 9624 12261 -1020 -1072 -828 O ATOM 353 CB LYS A 98 6.445 23.633 -25.326 1.00 72.70 C ANISOU 353 CB LYS A 98 11184 6987 9452 -999 -1056 -1128 C ATOM 354 CG LYS A 98 6.601 25.074 -24.891 1.00 73.60 C ANISOU 354 CG LYS A 98 11544 6949 9471 -1106 -1115 -1286 C ATOM 355 CD LYS A 98 7.611 25.760 -25.794 1.00 77.51 C ANISOU 355 CD LYS A 98 12002 7353 10094 -1276 -1203 -1266 C ATOM 356 CE LYS A 98 8.238 26.952 -25.100 1.00 80.27 C ANISOU 356 CE LYS A 98 12564 7606 10329 -1463 -1328 -1397 C ATOM 357 NZ LYS A 98 7.151 27.897 -24.719 1.00 83.37 N ANISOU 357 NZ LYS A 98 13233 7819 10624 -1353 -1233 -1556 N ATOM 358 N MET A 99 5.623 21.278 -27.823 1.00 56.15 N ANISOU 358 N MET A 99 8623 4985 7725 -739 -834 -834 N ATOM 359 CA MET A 99 6.081 19.984 -28.353 1.00 64.24 C ANISOU 359 CA MET A 99 9430 6124 8855 -718 -832 -690 C ATOM 360 C MET A 99 6.591 18.931 -27.324 1.00 57.52 C ANISOU 360 C MET A 99 8498 5439 7920 -730 -904 -613 C ATOM 361 O MET A 99 7.428 18.105 -27.616 1.00 57.11 O ANISOU 361 O MET A 99 8279 5473 7946 -756 -954 -503 O ATOM 362 CB MET A 99 7.124 20.178 -29.495 1.00 65.48 C ANISOU 362 CB MET A 99 9470 6251 9159 -820 -879 -634 C ATOM 363 CG MET A 99 6.496 19.958 -30.880 1.00 68.20 C ANISOU 363 CG MET A 99 9752 6521 9640 -726 -762 -594 C ATOM 364 SD MET A 99 7.623 19.736 -32.268 1.00 71.99 S ANISOU 364 SD MET A 99 10060 7008 10284 -810 -775 -498 S ATOM 365 CE MET A 99 8.296 21.410 -32.315 1.00 67.38 C ANISOU 365 CE MET A 99 9618 6304 9680 -987 -858 -586 C ATOM 366 N LYS A 100 6.051 18.943 -26.112 1.00 54.86 N ANISOU 366 N LYS A 100 8284 5145 7416 -699 -901 -666 N ATOM 367 CA LYS A 100 6.440 17.951 -25.143 1.00 55.71 C ANISOU 367 CA LYS A 100 8334 5402 7430 -702 -966 -582 C ATOM 368 C LYS A 100 5.574 16.703 -25.274 1.00 49.47 C ANISOU 368 C LYS A 100 7461 4660 6675 -563 -847 -488 C ATOM 369 O LYS A 100 5.887 15.707 -24.675 1.00 49.19 O ANISOU 369 O LYS A 100 7361 4734 6595 -551 -888 -389 O ATOM 370 CB LYS A 100 6.328 18.445 -23.714 1.00 61.40 C ANISOU 370 CB LYS A 100 9233 6165 7931 -745 -1023 -671 C ATOM 371 CG LYS A 100 6.962 19.796 -23.402 1.00 68.65 C ANISOU 371 CG LYS A 100 10294 7013 8777 -889 -1134 -797 C ATOM 372 CD LYS A 100 6.370 20.313 -22.092 1.00 72.88 C ANISOU 372 CD LYS A 100 11054 7555 9083 -882 -1126 -917 C ATOM 373 CE LYS A 100 6.512 21.827 -21.948 1.00 81.97 C ANISOU 373 CE LYS A 100 12409 8566 10169 -983 -1173 -1085 C ATOM 374 NZ LYS A 100 7.815 22.159 -21.329 1.00 87.05 N ANISOU 374 NZ LYS A 100 13071 9275 10730 -1179 -1378 -1096 N ATOM 375 N THR A 101 4.466 16.788 -26.005 1.00 46.99 N ANISOU 375 N THR A 101 7158 4262 6434 -464 -706 -519 N ATOM 376 CA THR A 101 3.500 15.683 -26.063 1.00 45.87 C ANISOU 376 CA THR A 101 6953 4162 6313 -351 -589 -445 C ATOM 377 C THR A 101 3.490 15.116 -27.449 1.00 42.46 C ANISOU 377 C THR A 101 6380 3683 6069 -314 -539 -374 C ATOM 378 O THR A 101 3.814 15.780 -28.442 1.00 39.66 O ANISOU 378 O THR A 101 6005 3245 5819 -345 -551 -407 O ATOM 379 CB THR A 101 2.049 16.166 -25.701 1.00 50.70 C ANISOU 379 CB THR A 101 7682 4739 6843 -260 -457 -539 C ATOM 380 OG1 THR A 101 1.533 17.060 -26.729 1.00 48.59 O ANISOU 380 OG1 THR A 101 7435 4347 6679 -221 -399 -615 O ATOM 381 CG2 THR A 101 2.046 16.885 -24.339 1.00 51.84 C ANISOU 381 CG2 THR A 101 8000 4916 6782 -295 -492 -637 C ATOM 382 N ALA A 102 3.082 13.863 -27.538 1.00 40.27 N ANISOU 382 N ALA A 102 6016 3454 5830 -251 -479 -275 N ATOM 383 CA ALA A 102 2.951 13.207 -28.813 1.00 39.07 C ANISOU 383 CA ALA A 102 5749 3256 5840 -211 -423 -215 C ATOM 384 C ALA A 102 2.004 13.916 -29.780 1.00 36.88 C ANISOU 384 C ALA A 102 5497 2885 5632 -167 -336 -290 C ATOM 385 O ALA A 102 2.248 13.976 -30.988 1.00 36.29 O ANISOU 385 O ALA A 102 5359 2749 5679 -172 -329 -277 O ATOM 386 CB ALA A 102 2.499 11.718 -28.629 1.00 36.99 C ANISOU 386 CB ALA A 102 5421 3044 5589 -155 -365 -105 C ATOM 387 N THR A 103 0.841 14.299 -29.280 1.00 37.42 N ANISOU 387 N THR A 103 5643 2952 5622 -109 -258 -354 N ATOM 388 CA THR A 103 -0.146 14.880 -30.138 1.00 38.36 C ANISOU 388 CA THR A 103 5771 2995 5808 -46 -180 -410 C ATOM 389 C THR A 103 0.414 16.190 -30.800 1.00 37.03 C ANISOU 389 C THR A 103 5668 2721 5681 -87 -237 -485 C ATOM 390 O THR A 103 0.203 16.420 -31.966 1.00 36.29 O ANISOU 390 O THR A 103 5540 2557 5690 -67 -215 -482 O ATOM 391 CB THR A 103 -1.391 15.281 -29.342 1.00 42.87 C ANISOU 391 CB THR A 103 6417 3592 6279 30 -91 -479 C ATOM 392 OG1 THR A 103 -2.024 14.111 -28.943 1.00 45.81 O ANISOU 392 OG1 THR A 103 6722 4053 6632 57 -23 -404 O ATOM 393 CG2 THR A 103 -2.454 16.061 -30.220 1.00 43.08 C ANISOU 393 CG2 THR A 103 6450 3540 6379 116 -20 -543 C ATOM 394 N ASN A 104 1.114 17.019 -30.027 1.00 39.54 N ANISOU 394 N ASN A 104 6088 3027 5909 -154 -313 -547 N ATOM 395 CA ASN A 104 1.739 18.248 -30.569 1.00 40.09 C ANISOU 395 CA ASN A 104 6231 2987 6012 -220 -373 -611 C ATOM 396 C ASN A 104 2.870 17.985 -31.544 1.00 40.70 C ANISOU 396 C ASN A 104 6204 3057 6205 -306 -433 -538 C ATOM 397 O ASN A 104 3.013 18.716 -32.515 1.00 39.36 O ANISOU 397 O ASN A 104 6056 2790 6109 -331 -434 -558 O ATOM 398 CB ASN A 104 2.210 19.129 -29.428 1.00 41.16 C ANISOU 398 CB ASN A 104 6512 3114 6014 -290 -446 -701 C ATOM 399 CG ASN A 104 1.048 19.844 -28.814 1.00 42.23 C ANISOU 399 CG ASN A 104 6787 3203 6055 -193 -366 -808 C ATOM 400 OD1 ASN A 104 -0.046 19.852 -29.420 1.00 42.10 O ANISOU 400 OD1 ASN A 104 6745 3149 6100 -77 -266 -812 O ATOM 401 ND2 ASN A 104 1.232 20.382 -27.632 1.00 42.93 N ANISOU 401 ND2 ASN A 104 7013 3303 5994 -232 -404 -891 N ATOM 402 N ILE A 105 3.572 16.857 -31.350 1.00 38.94 N ANISOU 402 N ILE A 105 5860 2935 6000 -332 -467 -444 N ATOM 403 CA ILE A 105 4.610 16.426 -32.260 1.00 37.51 C ANISOU 403 CA ILE A 105 5555 2766 5932 -387 -502 -368 C ATOM 404 C ILE A 105 4.003 16.041 -33.583 1.00 37.17 C ANISOU 404 C ILE A 105 5455 2669 5997 -322 -413 -337 C ATOM 405 O ILE A 105 4.593 16.343 -34.610 1.00 39.94 O ANISOU 405 O ILE A 105 5769 2975 6431 -368 -419 -322 O ATOM 406 CB ILE A 105 5.466 15.278 -31.643 1.00 38.25 C ANISOU 406 CB ILE A 105 5537 2980 6017 -403 -558 -274 C ATOM 407 CG1 ILE A 105 6.371 15.819 -30.582 1.00 39.25 C ANISOU 407 CG1 ILE A 105 5702 3162 6048 -502 -679 -299 C ATOM 408 CG2 ILE A 105 6.309 14.567 -32.691 1.00 38.15 C ANISOU 408 CG2 ILE A 105 5376 2983 6137 -412 -553 -189 C ATOM 409 CD1 ILE A 105 6.733 14.833 -29.536 1.00 41.92 C ANISOU 409 CD1 ILE A 105 5991 3620 6316 -486 -734 -224 C ATOM 410 N TYR A 106 2.881 15.305 -33.581 1.00 37.09 N ANISOU 410 N TYR A 106 5432 2676 5985 -225 -334 -320 N ATOM 411 CA TYR A 106 2.158 14.978 -34.823 1.00 34.85 C ANISOU 411 CA TYR A 106 5107 2344 5791 -169 -261 -301 C ATOM 412 C TYR A 106 1.597 16.254 -35.541 1.00 36.04 C ANISOU 412 C TYR A 106 5346 2390 5956 -155 -246 -371 C ATOM 413 O TYR A 106 1.653 16.391 -36.783 1.00 36.65 O ANISOU 413 O TYR A 106 5404 2412 6109 -161 -230 -353 O ATOM 414 CB TYR A 106 1.045 14.010 -34.611 1.00 34.32 C ANISOU 414 CB TYR A 106 5005 2319 5715 -92 -190 -272 C ATOM 415 CG TYR A 106 1.517 12.579 -34.158 1.00 34.28 C ANISOU 415 CG TYR A 106 4920 2389 5716 -95 -194 -182 C ATOM 416 CD1 TYR A 106 2.587 11.945 -34.826 1.00 35.04 C ANISOU 416 CD1 TYR A 106 4936 2486 5893 -124 -219 -120 C ATOM 417 CD2 TYR A 106 0.880 11.886 -33.132 1.00 34.53 C ANISOU 417 CD2 TYR A 106 4960 2483 5676 -63 -164 -156 C ATOM 418 CE1 TYR A 106 3.014 10.663 -34.476 1.00 39.05 C ANISOU 418 CE1 TYR A 106 5380 3041 6416 -106 -222 -36 C ATOM 419 CE2 TYR A 106 1.322 10.578 -32.724 1.00 35.41 C ANISOU 419 CE2 TYR A 106 5017 2644 5793 -63 -172 -61 C ATOM 420 CZ TYR A 106 2.349 9.964 -33.439 1.00 34.18 C ANISOU 420 CZ TYR A 106 4787 2471 5728 -76 -202 -3 C ATOM 421 OH TYR A 106 2.866 8.775 -33.122 1.00 39.55 O ANISOU 421 OH TYR A 106 5420 3180 6426 -59 -214 88 O ATOM 422 N ILE A 107 0.995 17.132 -34.756 1.00 37.27 N ANISOU 422 N ILE A 107 5609 2518 6034 -125 -245 -448 N ATOM 423 CA ILE A 107 0.454 18.410 -35.249 1.00 39.11 C ANISOU 423 CA ILE A 107 5949 2638 6274 -93 -236 -517 C ATOM 424 C ILE A 107 1.523 19.227 -35.935 1.00 36.56 C ANISOU 424 C ILE A 107 5668 2231 5990 -196 -296 -518 C ATOM 425 O ILE A 107 1.339 19.632 -37.106 1.00 36.18 O ANISOU 425 O ILE A 107 5635 2106 6007 -185 -280 -503 O ATOM 426 CB ILE A 107 -0.276 19.195 -34.162 1.00 39.65 C ANISOU 426 CB ILE A 107 6135 2684 6244 -33 -218 -609 C ATOM 427 CG1 ILE A 107 -1.542 18.380 -33.739 1.00 39.27 C ANISOU 427 CG1 ILE A 107 6023 2725 6174 78 -131 -595 C ATOM 428 CG2 ILE A 107 -0.683 20.594 -34.715 1.00 39.82 C ANISOU 428 CG2 ILE A 107 6285 2561 6283 7 -217 -677 C ATOM 429 CD1 ILE A 107 -2.230 18.979 -32.506 1.00 41.31 C ANISOU 429 CD1 ILE A 107 6383 2994 6318 144 -91 -684 C ATOM 430 N PHE A 108 2.665 19.348 -35.269 1.00 36.24 N ANISOU 430 N PHE A 108 5631 2222 5914 -303 -366 -521 N ATOM 431 CA PHE A 108 3.803 20.047 -35.830 1.00 38.76 C ANISOU 431 CA PHE A 108 5967 2487 6275 -429 -423 -513 C ATOM 432 C PHE A 108 4.246 19.455 -37.167 1.00 38.06 C ANISOU 432 C PHE A 108 5763 2411 6287 -448 -391 -430 C ATOM 433 O PHE A 108 4.402 20.163 -38.162 1.00 36.17 O ANISOU 433 O PHE A 108 5570 2083 6091 -488 -384 -425 O ATOM 434 CB PHE A 108 4.976 20.256 -34.853 1.00 40.15 C ANISOU 434 CB PHE A 108 6144 2715 6395 -556 -518 -527 C ATOM 435 CG PHE A 108 6.030 21.117 -35.421 1.00 41.97 C ANISOU 435 CG PHE A 108 6395 2883 6669 -700 -572 -525 C ATOM 436 CD1 PHE A 108 6.988 20.598 -36.253 1.00 44.44 C ANISOU 436 CD1 PHE A 108 6563 3253 7068 -767 -572 -441 C ATOM 437 CD2 PHE A 108 6.019 22.508 -35.197 1.00 47.50 C ANISOU 437 CD2 PHE A 108 7271 3451 7324 -768 -612 -610 C ATOM 438 CE1 PHE A 108 7.936 21.442 -36.837 1.00 45.21 C ANISOU 438 CE1 PHE A 108 6674 3298 7207 -913 -608 -433 C ATOM 439 CE2 PHE A 108 6.985 23.358 -35.739 1.00 45.34 C ANISOU 439 CE2 PHE A 108 7029 3107 7091 -925 -662 -604 C ATOM 440 CZ PHE A 108 7.919 22.839 -36.586 1.00 46.31 C ANISOU 440 CZ PHE A 108 6991 3303 7300 -1001 -655 -511 C ATOM 441 N ASN A 109 4.393 18.140 -37.221 1.00 36.27 N ANISOU 441 N ASN A 109 5403 2287 6092 -413 -365 -364 N ATOM 442 CA ASN A 109 4.826 17.467 -38.432 1.00 35.79 C ANISOU 442 CA ASN A 109 5241 2243 6117 -421 -324 -295 C ATOM 443 C ASN A 109 3.806 17.692 -39.564 1.00 36.41 C ANISOU 443 C ASN A 109 5371 2241 6222 -353 -265 -301 C ATOM 444 O ASN A 109 4.155 17.802 -40.735 1.00 34.75 O ANISOU 444 O ASN A 109 5148 1996 6058 -387 -241 -269 O ATOM 445 CB ASN A 109 4.951 15.967 -38.129 1.00 38.21 C ANISOU 445 CB ASN A 109 5424 2652 6442 -368 -301 -235 C ATOM 446 CG ASN A 109 5.906 15.219 -39.106 1.00 40.74 C ANISOU 446 CG ASN A 109 5627 3008 6846 -393 -271 -167 C ATOM 447 OD1 ASN A 109 7.075 15.467 -39.071 1.00 45.76 O ANISOU 447 OD1 ASN A 109 6204 3679 7504 -475 -309 -145 O ATOM 448 ND2 ASN A 109 5.405 14.266 -39.901 1.00 39.33 N ANISOU 448 ND2 ASN A 109 5411 2826 6708 -323 -202 -137 N ATOM 449 N LEU A 110 2.505 17.645 -39.228 1.00 35.61 N ANISOU 449 N LEU A 110 5314 2127 6088 -252 -239 -335 N ATOM 450 CA LEU A 110 1.480 17.827 -40.200 1.00 35.19 C ANISOU 450 CA LEU A 110 5294 2019 6059 -181 -201 -336 C ATOM 451 C LEU A 110 1.554 19.287 -40.770 1.00 36.20 C ANISOU 451 C LEU A 110 5548 2022 6184 -213 -228 -365 C ATOM 452 O LEU A 110 1.524 19.538 -41.995 1.00 36.16 O ANISOU 452 O LEU A 110 5565 1963 6211 -222 -216 -333 O ATOM 453 CB LEU A 110 0.114 17.537 -39.570 1.00 36.10 C ANISOU 453 CB LEU A 110 5408 2165 6142 -72 -171 -365 C ATOM 454 CG LEU A 110 -1.066 17.618 -40.510 1.00 35.59 C ANISOU 454 CG LEU A 110 5348 2069 6106 10 -143 -360 C ATOM 455 CD1 LEU A 110 -0.934 16.581 -41.623 1.00 36.01 C ANISOU 455 CD1 LEU A 110 5320 2154 6207 -13 -122 -300 C ATOM 456 CD2 LEU A 110 -2.374 17.492 -39.772 1.00 36.59 C ANISOU 456 CD2 LEU A 110 5458 2240 6205 112 -110 -391 C ATOM 457 N ALA A 111 1.655 20.269 -39.881 1.00 35.82 N ANISOU 457 N ALA A 111 5601 1919 6089 -233 -265 -426 N ATOM 458 CA ALA A 111 1.706 21.626 -40.318 1.00 36.20 C ANISOU 458 CA ALA A 111 5789 1829 6135 -262 -291 -454 C ATOM 459 C ALA A 111 2.940 21.915 -41.193 1.00 37.87 C ANISOU 459 C ALA A 111 5995 2009 6385 -403 -309 -403 C ATOM 460 O ALA A 111 2.842 22.599 -42.201 1.00 39.88 O ANISOU 460 O ALA A 111 6328 2168 6659 -415 -304 -379 O ATOM 461 CB ALA A 111 1.652 22.567 -39.122 1.00 35.82 C ANISOU 461 CB ALA A 111 5867 1720 6024 -266 -326 -541 C ATOM 462 N LEU A 112 4.107 21.404 -40.823 1.00 38.59 N ANISOU 462 N LEU A 112 5989 2188 6486 -508 -328 -379 N ATOM 463 CA LEU A 112 5.294 21.673 -41.612 1.00 38.45 C ANISOU 463 CA LEU A 112 5942 2161 6508 -644 -333 -329 C ATOM 464 C LEU A 112 5.071 21.073 -43.029 1.00 38.09 C ANISOU 464 C LEU A 112 5842 2129 6502 -602 -266 -265 C ATOM 465 O LEU A 112 5.345 21.690 -44.059 1.00 34.19 O ANISOU 465 O LEU A 112 5407 1564 6020 -662 -249 -231 O ATOM 466 CB LEU A 112 6.498 21.017 -40.942 1.00 39.59 C ANISOU 466 CB LEU A 112 5948 2431 6665 -733 -362 -306 C ATOM 467 CG LEU A 112 7.793 21.073 -41.715 1.00 41.37 C ANISOU 467 CG LEU A 112 6086 2689 6942 -867 -351 -246 C ATOM 468 CD1 LEU A 112 8.284 22.529 -41.873 1.00 44.33 C ANISOU 468 CD1 LEU A 112 6589 2946 7307 -1011 -393 -265 C ATOM 469 CD2 LEU A 112 8.836 20.272 -40.975 1.00 47.01 C ANISOU 469 CD2 LEU A 112 6635 3548 7677 -914 -384 -217 C ATOM 470 N ALA A 113 4.573 19.827 -43.085 1.00 34.77 N ANISOU 470 N ALA A 113 5319 1798 6094 -506 -226 -247 N ATOM 471 CA ALA A 113 4.360 19.203 -44.397 1.00 35.23 C ANISOU 471 CA ALA A 113 5341 1868 6176 -474 -168 -199 C ATOM 472 C ALA A 113 3.349 19.989 -45.225 1.00 36.56 C ANISOU 472 C ALA A 113 5635 1933 6323 -421 -170 -202 C ATOM 473 O ALA A 113 3.505 20.183 -46.424 1.00 38.02 O ANISOU 473 O ALA A 113 5855 2082 6508 -453 -145 -160 O ATOM 474 CB ALA A 113 3.882 17.798 -44.237 1.00 32.55 C ANISOU 474 CB ALA A 113 4900 1618 5849 -387 -134 -190 C ATOM 475 N ASP A 114 2.259 20.395 -44.584 1.00 38.17 N ANISOU 475 N ASP A 114 5902 2095 6504 -326 -199 -248 N ATOM 476 CA ASP A 114 1.225 21.153 -45.267 1.00 41.07 C ANISOU 476 CA ASP A 114 6377 2370 6859 -249 -212 -247 C ATOM 477 C ASP A 114 1.719 22.537 -45.772 1.00 41.45 C ANISOU 477 C ASP A 114 6571 2279 6897 -325 -239 -233 C ATOM 478 O ASP A 114 1.305 22.989 -46.848 1.00 40.79 O ANISOU 478 O ASP A 114 6566 2127 6805 -301 -242 -191 O ATOM 479 CB ASP A 114 -0.014 21.253 -44.385 1.00 42.12 C ANISOU 479 CB ASP A 114 6522 2504 6978 -118 -225 -300 C ATOM 480 CG ASP A 114 -0.805 19.926 -44.382 1.00 50.06 C ANISOU 480 CG ASP A 114 7399 3628 7996 -43 -194 -289 C ATOM 481 OD1 ASP A 114 -0.755 19.139 -45.420 1.00 51.96 O ANISOU 481 OD1 ASP A 114 7583 3910 8250 -63 -174 -242 O ATOM 482 OD2 ASP A 114 -1.445 19.646 -43.339 1.00 55.64 O ANISOU 482 OD2 ASP A 114 8066 4384 8690 24 -185 -328 O ATOM 483 N ALA A 115 2.631 23.145 -45.005 1.00 40.76 N ANISOU 483 N ALA A 115 6523 2158 6808 -428 -263 -262 N ATOM 484 CA ALA A 115 3.196 24.444 -45.338 1.00 43.36 C ANISOU 484 CA ALA A 115 6997 2348 7131 -531 -290 -252 C ATOM 485 C ALA A 115 4.146 24.224 -46.571 1.00 44.73 C ANISOU 485 C ALA A 115 7126 2551 7318 -651 -249 -169 C ATOM 486 O ALA A 115 4.150 25.008 -47.511 1.00 41.64 O ANISOU 486 O ALA A 115 6852 2056 6914 -689 -247 -122 O ATOM 487 CB ALA A 115 3.937 24.985 -44.136 1.00 43.45 C ANISOU 487 CB ALA A 115 7043 2336 7131 -628 -332 -311 C ATOM 488 N LEU A 116 4.896 23.114 -46.566 1.00 40.88 N ANISOU 488 N LEU A 116 6471 2207 6853 -696 -209 -149 N ATOM 489 CA LEU A 116 5.791 22.795 -47.680 1.00 43.51 C ANISOU 489 CA LEU A 116 6746 2589 7198 -791 -149 -79 C ATOM 490 C LEU A 116 5.034 22.462 -48.954 1.00 40.18 C ANISOU 490 C LEU A 116 6362 2156 6747 -712 -110 -38 C ATOM 491 O LEU A 116 5.413 22.928 -50.049 1.00 39.94 O ANISOU 491 O LEU A 116 6402 2081 6694 -787 -78 20 O ATOM 492 CB LEU A 116 6.797 21.659 -47.342 1.00 42.25 C ANISOU 492 CB LEU A 116 6393 2584 7076 -834 -109 -69 C ATOM 493 CG LEU A 116 7.928 22.146 -46.378 1.00 43.79 C ANISOU 493 CG LEU A 116 6541 2803 7295 -968 -154 -84 C ATOM 494 CD1 LEU A 116 8.716 20.992 -45.727 1.00 41.43 C ANISOU 494 CD1 LEU A 116 6044 2663 7035 -966 -143 -78 C ATOM 495 CD2 LEU A 116 8.868 23.093 -47.053 1.00 45.30 C ANISOU 495 CD2 LEU A 116 6780 2940 7492 -1136 -138 -37 C ATOM 496 N ALA A 117 3.950 21.692 -48.809 1.00 40.12 N ANISOU 496 N ALA A 117 6317 2191 6735 -572 -118 -65 N ATOM 497 CA ALA A 117 3.069 21.360 -49.931 1.00 39.57 C ANISOU 497 CA ALA A 117 6284 2119 6632 -495 -106 -35 C ATOM 498 C ALA A 117 2.609 22.639 -50.644 1.00 39.64 C ANISOU 498 C ALA A 117 6465 1991 6604 -493 -146 2 C ATOM 499 O ALA A 117 2.749 22.769 -51.870 1.00 41.12 O ANISOU 499 O ALA A 117 6714 2159 6749 -533 -121 62 O ATOM 500 CB ALA A 117 1.850 20.563 -49.482 1.00 37.62 C ANISOU 500 CB ALA A 117 5977 1927 6392 -359 -129 -74 C ATOM 501 N THR A 118 2.061 23.571 -49.864 1.00 41.10 N ANISOU 501 N THR A 118 6739 2078 6799 -440 -204 -33 N ATOM 502 CA THR A 118 1.559 24.839 -50.409 1.00 43.31 C ANISOU 502 CA THR A 118 7198 2204 7054 -413 -249 1 C ATOM 503 C THR A 118 2.649 25.748 -50.956 1.00 42.29 C ANISOU 503 C THR A 118 7180 1979 6909 -575 -232 55 C ATOM 504 O THR A 118 2.384 26.506 -51.831 1.00 43.31 O ANISOU 504 O THR A 118 7449 2003 7004 -573 -251 116 O ATOM 505 CB THR A 118 0.568 25.543 -49.448 1.00 44.89 C ANISOU 505 CB THR A 118 7469 2318 7271 -282 -304 -58 C ATOM 506 OG1 THR A 118 1.151 25.626 -48.157 1.00 47.23 O ANISOU 506 OG1 THR A 118 7735 2622 7590 -335 -302 -129 O ATOM 507 CG2 THR A 118 -0.707 24.647 -49.312 1.00 47.62 C ANISOU 507 CG2 THR A 118 7701 2769 7623 -120 -313 -82 C ATOM 508 N SER A 119 3.881 25.611 -50.454 1.00 41.95 N ANISOU 508 N SER A 119 7062 1985 6893 -718 -198 41 N ATOM 509 CA SER A 119 5.007 26.378 -50.926 1.00 44.03 C ANISOU 509 CA SER A 119 7395 2184 7150 -898 -173 95 C ATOM 510 C SER A 119 5.367 26.097 -52.368 1.00 44.05 C ANISOU 510 C SER A 119 7400 2228 7108 -956 -106 182 C ATOM 511 O SER A 119 5.995 26.916 -52.982 1.00 44.03 O ANISOU 511 O SER A 119 7501 2143 7083 -1087 -86 245 O ATOM 512 CB SER A 119 6.235 26.202 -50.052 1.00 45.81 C ANISOU 512 CB SER A 119 7503 2485 7419 -1038 -159 63 C ATOM 513 OG SER A 119 6.852 24.971 -50.354 1.00 44.33 O ANISOU 513 OG SER A 119 7127 2470 7245 -1055 -88 81 O ATOM 514 N THR A 120 4.876 24.981 -52.930 1.00 44.94 N ANISOU 514 N THR A 120 7421 2456 7199 -860 -73 184 N ATOM 515 CA THR A 120 5.144 24.701 -54.308 1.00 43.54 C ANISOU 515 CA THR A 120 7267 2316 6959 -906 -7 255 C ATOM 516 C THR A 120 4.263 25.439 -55.256 1.00 45.60 C ANISOU 516 C THR A 120 7711 2465 7151 -851 -55 317 C ATOM 517 O THR A 120 4.666 25.521 -56.432 1.00 46.04 O ANISOU 517 O THR A 120 7831 2527 7136 -929 -1 391 O ATOM 518 CB THR A 120 5.001 23.221 -54.646 1.00 41.70 C ANISOU 518 CB THR A 120 6892 2236 6715 -837 47 230 C ATOM 519 OG1 THR A 120 3.598 22.842 -54.695 1.00 40.17 O ANISOU 519 OG1 THR A 120 6721 2041 6503 -680 -20 204 O ATOM 520 CG2 THR A 120 5.889 22.418 -53.660 1.00 42.91 C ANISOU 520 CG2 THR A 120 6859 2501 6943 -872 89 178 C ATOM 521 N LEU A 121 3.090 25.933 -54.770 1.00 47.03 N ANISOU 521 N LEU A 121 7967 2556 7346 -711 -150 290 N ATOM 522 CA LEU A 121 2.032 26.563 -55.620 1.00 45.55 C ANISOU 522 CA LEU A 121 7935 2271 7100 -612 -219 351 C ATOM 523 C LEU A 121 2.437 27.775 -56.437 1.00 44.67 C ANISOU 523 C LEU A 121 8026 2011 6937 -709 -222 449 C ATOM 524 O LEU A 121 1.972 27.941 -57.564 1.00 44.29 O ANISOU 524 O LEU A 121 8081 1938 6807 -678 -245 529 O ATOM 525 CB LEU A 121 0.704 26.850 -54.875 1.00 45.42 C ANISOU 525 CB LEU A 121 7933 2200 7123 -425 -311 303 C ATOM 526 CG LEU A 121 -0.028 25.598 -54.379 1.00 45.95 C ANISOU 526 CG LEU A 121 7819 2421 7220 -313 -315 233 C ATOM 527 CD1 LEU A 121 -1.220 25.894 -53.452 1.00 46.25 C ANISOU 527 CD1 LEU A 121 7843 2424 7307 -142 -382 178 C ATOM 528 CD2 LEU A 121 -0.483 24.740 -55.551 1.00 47.06 C ANISOU 528 CD2 LEU A 121 7924 2663 7293 -288 -314 274 C ATOM 529 N PRO A 122 3.265 28.708 -55.925 1.00 45.66 N ANISOU 529 N PRO A 122 8230 2020 7098 -836 -211 453 N ATOM 530 CA PRO A 122 3.640 29.851 -56.759 1.00 47.61 C ANISOU 530 CA PRO A 122 8684 2114 7293 -944 -210 559 C ATOM 531 C PRO A 122 4.406 29.328 -57.986 1.00 48.08 C ANISOU 531 C PRO A 122 8715 2283 7271 -1072 -113 637 C ATOM 532 O PRO A 122 4.267 29.943 -59.046 1.00 47.91 O ANISOU 532 O PRO A 122 8864 2176 7164 -1101 -120 742 O ATOM 533 CB PRO A 122 4.507 30.705 -55.826 1.00 47.22 C ANISOU 533 CB PRO A 122 8682 1952 7309 -1086 -207 526 C ATOM 534 CG PRO A 122 4.141 30.229 -54.411 1.00 45.59 C ANISOU 534 CG PRO A 122 8341 1803 7179 -981 -244 397 C ATOM 535 CD PRO A 122 3.859 28.759 -54.581 1.00 44.87 C ANISOU 535 CD PRO A 122 8044 1924 7080 -893 -206 366 C ATOM 536 N PHE A 123 5.168 28.215 -57.838 1.00 47.21 N ANISOU 536 N PHE A 123 8401 2355 7180 -1134 -23 589 N ATOM 537 CA PHE A 123 5.952 27.713 -58.965 1.00 48.20 C ANISOU 537 CA PHE A 123 8497 2589 7228 -1247 91 651 C ATOM 538 C PHE A 123 4.946 27.212 -59.956 1.00 46.88 C ANISOU 538 C PHE A 123 8390 2460 6963 -1119 59 679 C ATOM 539 O PHE A 123 5.079 27.435 -61.140 1.00 47.61 O ANISOU 539 O PHE A 123 8602 2542 6945 -1179 97 768 O ATOM 540 CB PHE A 123 6.956 26.632 -58.597 1.00 48.07 C ANISOU 540 CB PHE A 123 8251 2750 7261 -1314 197 592 C ATOM 541 CG PHE A 123 8.061 27.103 -57.701 1.00 49.52 C ANISOU 541 CG PHE A 123 8358 2923 7534 -1463 221 576 C ATOM 542 CD1 PHE A 123 9.206 27.594 -58.218 1.00 52.73 C ANISOU 542 CD1 PHE A 123 8777 3336 7924 -1659 311 649 C ATOM 543 CD2 PHE A 123 7.943 26.981 -56.281 1.00 50.42 C ANISOU 543 CD2 PHE A 123 8372 3039 7747 -1410 152 483 C ATOM 544 CE1 PHE A 123 10.216 28.063 -57.369 1.00 55.83 C ANISOU 544 CE1 PHE A 123 9088 3724 8402 -1814 317 635 C ATOM 545 CE2 PHE A 123 8.969 27.342 -55.425 1.00 51.13 C ANISOU 545 CE2 PHE A 123 8381 3137 7909 -1554 158 462 C ATOM 546 CZ PHE A 123 10.112 27.921 -55.971 1.00 54.25 C ANISOU 546 CZ PHE A 123 8790 3528 8294 -1762 234 539 C ATOM 547 N GLN A 124 3.895 26.561 -59.455 1.00 46.08 N ANISOU 547 N GLN A 124 8209 2403 6895 -948 -17 605 N ATOM 548 CA GLN A 124 2.854 26.020 -60.307 1.00 45.75 C ANISOU 548 CA GLN A 124 8202 2412 6768 -830 -68 622 C ATOM 549 C GLN A 124 1.962 27.132 -60.976 1.00 45.58 C ANISOU 549 C GLN A 124 8395 2244 6678 -763 -178 719 C ATOM 550 O GLN A 124 1.525 26.993 -62.111 1.00 44.67 O ANISOU 550 O GLN A 124 8369 2157 6447 -742 -202 783 O ATOM 551 CB GLN A 124 2.026 25.016 -59.517 1.00 43.61 C ANISOU 551 CB GLN A 124 7770 2235 6563 -688 -116 521 C ATOM 552 CG GLN A 124 2.814 23.787 -59.050 1.00 43.25 C ANISOU 552 CG GLN A 124 7534 2332 6566 -735 -14 442 C ATOM 553 CD GLN A 124 1.906 22.676 -58.513 1.00 39.58 C ANISOU 553 CD GLN A 124 6936 1960 6142 -606 -58 359 C ATOM 554 OE1 GLN A 124 0.904 22.346 -59.157 1.00 42.19 O ANISOU 554 OE1 GLN A 124 7302 2315 6412 -525 -122 368 O ATOM 555 NE2 GLN A 124 2.184 22.179 -57.288 1.00 37.78 N ANISOU 555 NE2 GLN A 124 6563 1777 6016 -589 -38 284 N ATOM 556 N SER A 125 1.669 28.225 -60.284 1.00 46.26 N ANISOU 556 N SER A 125 8574 2172 6831 -720 -250 730 N ATOM 557 CA SER A 125 0.941 29.301 -60.985 1.00 50.59 C ANISOU 557 CA SER A 125 9338 2568 7317 -653 -346 836 C ATOM 558 C SER A 125 1.717 29.883 -62.153 1.00 50.52 C ANISOU 558 C SER A 125 9500 2501 7194 -812 -288 961 C ATOM 559 O SER A 125 1.146 30.078 -63.221 1.00 52.06 O ANISOU 559 O SER A 125 9826 2679 7276 -767 -343 1055 O ATOM 560 CB SER A 125 0.509 30.431 -60.097 1.00 53.33 C ANISOU 560 CB SER A 125 9783 2727 7751 -570 -424 826 C ATOM 561 OG SER A 125 1.081 30.207 -58.869 1.00 62.73 O ANISOU 561 OG SER A 125 10846 3943 9045 -618 -375 719 O ATOM 562 N VAL A 126 3.006 30.175 -61.938 1.00 50.83 N ANISOU 562 N VAL A 126 9536 2518 7261 -1003 -180 967 N ATOM 563 CA VAL A 126 3.853 30.787 -62.980 1.00 52.12 C ANISOU 563 CA VAL A 126 9855 2626 7320 -1182 -103 1091 C ATOM 564 C VAL A 126 3.903 29.777 -64.137 1.00 52.71 C ANISOU 564 C VAL A 126 9888 2879 7262 -1196 -34 1114 C ATOM 565 O VAL A 126 3.767 30.136 -65.295 1.00 52.36 O ANISOU 565 O VAL A 126 10013 2801 7078 -1227 -39 1227 O ATOM 566 CB VAL A 126 5.281 31.047 -62.471 1.00 51.76 C ANISOU 566 CB VAL A 126 9747 2578 7342 -1397 14 1078 C ATOM 567 CG1 VAL A 126 6.229 31.372 -63.625 1.00 52.68 C ANISOU 567 CG1 VAL A 126 9968 2703 7343 -1596 130 1200 C ATOM 568 CG2 VAL A 126 5.259 32.172 -61.413 1.00 52.29 C ANISOU 568 CG2 VAL A 126 9906 2444 7518 -1409 -62 1057 C ATOM 569 N ASN A 127 4.122 28.497 -63.806 1.00 50.04 N ANISOU 569 N ASN A 127 9331 2721 6960 -1174 32 1005 N ATOM 570 CA ASN A 127 4.199 27.455 -64.854 1.00 51.33 C ANISOU 570 CA ASN A 127 9460 3045 6996 -1184 107 1004 C ATOM 571 C ASN A 127 2.911 27.460 -65.666 1.00 51.73 C ANISOU 571 C ASN A 127 9639 3081 6935 -1051 -24 1052 C ATOM 572 O ASN A 127 2.934 27.448 -66.902 1.00 52.26 O ANISOU 572 O ASN A 127 9839 3179 6839 -1100 0 1133 O ATOM 573 CB ASN A 127 4.518 26.135 -64.201 1.00 50.69 C ANISOU 573 CB ASN A 127 9140 3124 6997 -1155 179 872 C ATOM 574 CG ASN A 127 4.571 24.968 -65.161 1.00 53.10 C ANISOU 574 CG ASN A 127 9410 3581 7183 -1151 259 845 C ATOM 575 OD1 ASN A 127 3.683 24.136 -65.122 1.00 59.47 O ANISOU 575 OD1 ASN A 127 10161 4450 7984 -1029 188 777 O ATOM 576 ND2 ASN A 127 5.652 24.831 -65.894 1.00 53.45 N ANISOU 576 ND2 ASN A 127 9468 3690 7149 -1287 416 882 N ATOM 577 N TYR A 128 1.775 27.560 -64.976 1.00 52.79 N ANISOU 577 N TYR A 128 9739 3168 7151 -883 -169 1011 N ATOM 578 CA TYR A 128 0.516 27.685 -65.678 1.00 55.35 C ANISOU 578 CA TYR A 128 10167 3478 7385 -750 -314 1068 C ATOM 579 C TYR A 128 0.544 29.023 -66.474 1.00 62.23 C ANISOU 579 C TYR A 128 11297 4186 8162 -793 -359 1228 C ATOM 580 O TYR A 128 0.336 29.027 -67.657 1.00 64.26 O ANISOU 580 O TYR A 128 11687 4472 8258 -813 -383 1316 O ATOM 581 CB TYR A 128 -0.689 27.650 -64.745 1.00 55.18 C ANISOU 581 CB TYR A 128 10046 3438 7483 -559 -450 1003 C ATOM 582 CG TYR A 128 -1.920 28.111 -65.455 1.00 58.94 C ANISOU 582 CG TYR A 128 10641 3874 7881 -424 -612 1092 C ATOM 583 CD1 TYR A 128 -2.544 27.293 -66.388 1.00 62.61 C ANISOU 583 CD1 TYR A 128 11093 4474 8221 -395 -669 1099 C ATOM 584 CD2 TYR A 128 -2.431 29.402 -65.269 1.00 63.08 C ANISOU 584 CD2 TYR A 128 11307 4216 8443 -329 -713 1177 C ATOM 585 CE1 TYR A 128 -3.645 27.751 -67.106 1.00 66.83 C ANISOU 585 CE1 TYR A 128 11735 4984 8674 -278 -833 1196 C ATOM 586 CE2 TYR A 128 -3.527 29.863 -65.992 1.00 65.23 C ANISOU 586 CE2 TYR A 128 11690 4454 8642 -193 -868 1277 C ATOM 587 CZ TYR A 128 -4.131 29.037 -66.903 1.00 65.26 C ANISOU 587 CZ TYR A 128 11660 4613 8523 -170 -933 1290 C ATOM 588 OH TYR A 128 -5.224 29.460 -67.609 1.00 69.48 O ANISOU 588 OH TYR A 128 12285 5132 8982 -37 -1104 1393 O ATOM 589 N LEU A 129 0.818 30.149 -65.818 1.00 61.72 N ANISOU 589 N LEU A 129 11317 3944 8192 -815 -371 1264 N ATOM 590 CA LEU A 129 0.598 31.432 -66.467 1.00 71.30 C ANISOU 590 CA LEU A 129 12787 4972 9331 -817 -443 1416 C ATOM 591 C LEU A 129 1.415 31.628 -67.725 1.00 70.38 C ANISOU 591 C LEU A 129 12829 4867 9044 -997 -347 1537 C ATOM 592 O LEU A 129 0.997 32.362 -68.623 1.00 73.74 O ANISOU 592 O LEU A 129 13473 5194 9350 -976 -426 1679 O ATOM 593 CB LEU A 129 0.912 32.608 -65.540 1.00 81.50 C ANISOU 593 CB LEU A 129 14165 6050 10751 -841 -453 1425 C ATOM 594 CG LEU A 129 -0.215 33.049 -64.614 1.00 86.77 C ANISOU 594 CG LEU A 129 14817 6610 11541 -619 -591 1375 C ATOM 595 CD1 LEU A 129 0.311 34.158 -63.703 1.00 88.15 C ANISOU 595 CD1 LEU A 129 15096 6570 11828 -680 -573 1365 C ATOM 596 CD2 LEU A 129 -1.437 33.490 -65.425 1.00 90.83 C ANISOU 596 CD2 LEU A 129 15472 7066 11973 -441 -746 1487 C ATOM 597 N MET A 130 2.608 31.030 -67.740 1.00 64.69 N ANISOU 597 N MET A 130 12000 4261 8318 -1170 -173 1488 N ATOM 598 CA MET A 130 3.581 31.217 -68.801 1.00 65.43 C ANISOU 598 CA MET A 130 12216 4380 8265 -1364 -39 1592 C ATOM 599 C MET A 130 3.481 30.105 -69.840 1.00 63.06 C ANISOU 599 C MET A 130 11884 4276 7798 -1360 14 1574 C ATOM 600 O MET A 130 4.005 30.236 -70.921 1.00 62.41 O ANISOU 600 O MET A 130 11939 4223 7549 -1484 105 1670 O ATOM 601 CB MET A 130 5.015 31.302 -68.226 1.00 65.83 C ANISOU 601 CB MET A 130 12158 4444 8409 -1563 132 1557 C ATOM 602 CG MET A 130 5.219 32.410 -67.217 1.00 67.08 C ANISOU 602 CG MET A 130 12367 4405 8717 -1603 83 1567 C ATOM 603 SD MET A 130 4.828 34.029 -67.991 1.00 81.42 S ANISOU 603 SD MET A 130 14550 5951 10435 -1631 -14 1769 S ATOM 604 CE MET A 130 4.324 34.921 -66.512 1.00 81.94 C ANISOU 604 CE MET A 130 14634 5795 10705 -1519 -144 1699 C ATOM 605 N GLY A 131 2.773 29.024 -69.508 1.00 60.75 N ANISOU 605 N GLY A 131 11426 4111 7545 -1221 -44 1449 N ATOM 606 CA GLY A 131 2.687 27.858 -70.375 1.00 62.79 C ANISOU 606 CA GLY A 131 11648 4550 7660 -1220 7 1401 C ATOM 607 C GLY A 131 4.009 27.102 -70.531 1.00 63.95 C ANISOU 607 C GLY A 131 11683 4827 7786 -1368 234 1340 C ATOM 608 O GLY A 131 4.166 26.343 -71.471 1.00 68.00 O ANISOU 608 O GLY A 131 12230 5464 8143 -1401 314 1324 O ATOM 609 N THR A 132 4.918 27.271 -69.560 1.00 64.81 N ANISOU 609 N THR A 132 11651 4914 8060 -1443 331 1296 N ATOM 610 CA THR A 132 6.252 26.679 -69.553 1.00 63.17 C ANISOU 610 CA THR A 132 11305 4828 7871 -1576 544 1248 C ATOM 611 C THR A 132 6.874 26.783 -68.170 1.00 61.83 C ANISOU 611 C THR A 132 10940 4634 7919 -1602 571 1178 C ATOM 612 O THR A 132 6.442 27.610 -67.359 1.00 66.12 O ANISOU 612 O THR A 132 11515 5036 8571 -1563 446 1193 O ATOM 613 CB THR A 132 7.092 27.330 -70.632 1.00 68.80 C ANISOU 613 CB THR A 132 12182 5531 8429 -1752 676 1381 C ATOM 614 OG1 THR A 132 6.756 26.676 -71.827 1.00 78.20 O ANISOU 614 OG1 THR A 132 13477 6822 9414 -1726 705 1388 O ATOM 615 CG2 THR A 132 8.544 27.163 -70.450 1.00 70.60 C ANISOU 615 CG2 THR A 132 12263 5847 8716 -1910 887 1366 C ATOM 616 N TRP A 133 7.858 25.912 -67.904 1.00 59.04 N ANISOU 616 N TRP A 133 10388 4423 7622 -1656 728 1098 N ATOM 617 CA TRP A 133 8.654 25.902 -66.678 1.00 56.18 C ANISOU 617 CA TRP A 133 9822 4075 7450 -1704 771 1037 C ATOM 618 C TRP A 133 9.906 26.752 -66.853 1.00 57.29 C ANISOU 618 C TRP A 133 9977 4196 7596 -1917 897 1132 C ATOM 619 O TRP A 133 10.828 26.380 -67.589 1.00 58.15 O ANISOU 619 O TRP A 133 10039 4426 7628 -2020 1076 1158 O ATOM 620 CB TRP A 133 9.024 24.464 -66.246 1.00 52.97 C ANISOU 620 CB TRP A 133 9179 3834 7113 -1631 859 907 C ATOM 621 CG TRP A 133 9.828 24.396 -64.991 1.00 48.37 C ANISOU 621 CG TRP A 133 8382 3282 6715 -1670 888 852 C ATOM 622 CD1 TRP A 133 11.175 24.383 -64.888 1.00 48.01 C ANISOU 622 CD1 TRP A 133 8195 3325 6722 -1806 1038 869 C ATOM 623 CD2 TRP A 133 9.316 24.355 -63.680 1.00 45.90 C ANISOU 623 CD2 TRP A 133 7974 2920 6547 -1575 757 778 C ATOM 624 NE1 TRP A 133 11.550 24.333 -63.568 1.00 46.53 N ANISOU 624 NE1 TRP A 133 7826 3147 6705 -1804 993 810 N ATOM 625 CE2 TRP A 133 10.422 24.333 -62.802 1.00 45.08 C ANISOU 625 CE2 TRP A 133 7681 2874 6574 -1666 823 753 C ATOM 626 CE3 TRP A 133 8.021 24.347 -63.150 1.00 45.98 C ANISOU 626 CE3 TRP A 133 8034 2851 6586 -1424 591 732 C ATOM 627 CZ2 TRP A 133 10.290 24.271 -61.446 1.00 44.87 C ANISOU 627 CZ2 TRP A 133 7534 2828 6688 -1612 728 682 C ATOM 628 CZ3 TRP A 133 7.871 24.249 -61.771 1.00 44.57 C ANISOU 628 CZ3 TRP A 133 7725 2656 6554 -1363 513 656 C ATOM 629 CH2 TRP A 133 9.011 24.224 -60.928 1.00 44.58 C ANISOU 629 CH2 TRP A 133 7559 2711 6668 -1459 580 631 C ATOM 630 N PRO A 134 9.969 27.934 -66.195 1.00 56.86 N ANISOU 630 N PRO A 134 9992 3983 7628 -1995 812 1185 N ATOM 631 CA PRO A 134 11.089 28.866 -66.362 1.00 58.25 C ANISOU 631 CA PRO A 134 10205 4117 7810 -2225 913 1286 C ATOM 632 C PRO A 134 12.230 28.764 -65.359 1.00 56.37 C ANISOU 632 C PRO A 134 9728 3956 7734 -2342 985 1232 C ATOM 633 O PRO A 134 13.163 29.523 -65.485 1.00 59.30 O ANISOU 633 O PRO A 134 10114 4303 8117 -2549 1064 1315 O ATOM 634 CB PRO A 134 10.401 30.245 -66.165 1.00 59.31 C ANISOU 634 CB PRO A 134 10580 4004 7951 -2236 755 1367 C ATOM 635 CG PRO A 134 9.342 29.954 -65.099 1.00 56.19 C ANISOU 635 CG PRO A 134 10126 3559 7667 -2026 587 1252 C ATOM 636 CD PRO A 134 8.919 28.486 -65.318 1.00 57.25 C ANISOU 636 CD PRO A 134 10111 3876 7765 -1870 616 1155 C ATOM 637 N PHE A 135 12.128 27.850 -64.387 1.00 56.84 N ANISOU 637 N PHE A 135 9575 4108 7913 -2216 948 1103 N ATOM 638 CA PHE A 135 12.980 27.855 -63.200 1.00 55.83 C ANISOU 638 CA PHE A 135 9237 4027 7950 -2297 953 1049 C ATOM 639 C PHE A 135 14.238 26.962 -63.289 1.00 56.40 C ANISOU 639 C PHE A 135 9046 4321 8062 -2367 1132 1026 C ATOM 640 O PHE A 135 15.037 26.857 -62.316 1.00 55.83 O ANISOU 640 O PHE A 135 8765 4321 8127 -2432 1135 985 O ATOM 641 CB PHE A 135 12.112 27.428 -62.042 1.00 53.41 C ANISOU 641 CB PHE A 135 8865 3686 7742 -2114 802 933 C ATOM 642 CG PHE A 135 10.942 28.350 -61.760 1.00 53.96 C ANISOU 642 CG PHE A 135 9157 3545 7801 -2034 631 946 C ATOM 643 CD1 PHE A 135 11.157 29.674 -61.275 1.00 55.77 C ANISOU 643 CD1 PHE A 135 9514 3598 8079 -2166 562 993 C ATOM 644 CD2 PHE A 135 9.631 27.909 -61.937 1.00 51.59 C ANISOU 644 CD2 PHE A 135 8933 3218 7451 -1827 536 907 C ATOM 645 CE1 PHE A 135 10.088 30.515 -61.005 1.00 55.19 C ANISOU 645 CE1 PHE A 135 9648 3322 8001 -2068 414 999 C ATOM 646 CE2 PHE A 135 8.570 28.733 -61.635 1.00 52.31 C ANISOU 646 CE2 PHE A 135 9198 3130 7546 -1733 386 918 C ATOM 647 CZ PHE A 135 8.796 30.053 -61.178 1.00 53.93 C ANISOU 647 CZ PHE A 135 9540 3152 7798 -1843 329 964 C ATOM 648 N GLY A 136 14.396 26.292 -64.441 1.00 55.89 N ANISOU 648 N GLY A 136 8992 4370 7875 -2340 1278 1048 N ATOM 649 CA GLY A 136 15.545 25.456 -64.674 1.00 56.32 C ANISOU 649 CA GLY A 136 8814 4630 7953 -2383 1469 1031 C ATOM 650 C GLY A 136 15.401 24.065 -64.039 1.00 53.21 C ANISOU 650 C GLY A 136 8219 4354 7644 -2187 1464 902 C ATOM 651 O GLY A 136 14.429 23.712 -63.343 1.00 51.20 O ANISOU 651 O GLY A 136 7988 4032 7433 -2032 1314 824 O ATOM 652 N ASN A 137 16.436 23.265 -64.260 1.00 54.60 N ANISOU 652 N ASN A 137 8186 4712 7849 -2197 1642 885 N ATOM 653 CA ASN A 137 16.432 21.843 -64.015 1.00 53.92 C ANISOU 653 CA ASN A 137 7937 4742 7809 -2012 1690 779 C ATOM 654 C ASN A 137 16.599 21.537 -62.531 1.00 52.50 C ANISOU 654 C ASN A 137 7553 4584 7813 -1955 1576 716 C ATOM 655 O ASN A 137 15.913 20.633 -61.966 1.00 49.54 O ANISOU 655 O ASN A 137 7144 4201 7479 -1775 1495 625 O ATOM 656 CB ASN A 137 17.492 21.208 -64.910 1.00 56.98 C ANISOU 656 CB ASN A 137 8200 5302 8146 -2039 1936 794 C ATOM 657 CG ASN A 137 17.517 19.656 -64.811 1.00 59.60 C ANISOU 657 CG ASN A 137 8391 5741 8515 -1830 2011 682 C ATOM 658 OD1 ASN A 137 16.476 18.953 -64.890 1.00 60.46 O ANISOU 658 OD1 ASN A 137 8619 5783 8569 -1672 1931 604 O ATOM 659 ND2 ASN A 137 18.723 19.125 -64.611 1.00 60.43 N ANISOU 659 ND2 ASN A 137 8234 6007 8718 -1833 2160 677 N ATOM 660 N ILE A 138 17.416 22.351 -61.847 1.00 53.80 N ANISOU 660 N ILE A 138 7602 4761 8079 -2119 1549 766 N ATOM 661 CA ILE A 138 17.659 22.165 -60.406 1.00 55.14 C ANISOU 661 CA ILE A 138 7584 4959 8408 -2090 1430 714 C ATOM 662 C ILE A 138 16.429 22.422 -59.534 1.00 53.27 C ANISOU 662 C ILE A 138 7489 4563 8188 -1995 1219 658 C ATOM 663 O ILE A 138 16.077 21.604 -58.653 1.00 51.62 O ANISOU 663 O ILE A 138 7180 4382 8052 -1846 1143 579 O ATOM 664 CB ILE A 138 18.856 22.960 -59.890 1.00 59.76 C ANISOU 664 CB ILE A 138 8007 5607 9091 -2306 1442 777 C ATOM 665 CG1 ILE A 138 20.157 22.385 -60.509 1.00 61.91 C ANISOU 665 CG1 ILE A 138 8043 6092 9386 -2353 1660 816 C ATOM 666 CG2 ILE A 138 18.884 22.907 -58.363 1.00 59.73 C ANISOU 666 CG2 ILE A 138 7871 5603 9222 -2279 1276 720 C ATOM 667 CD1 ILE A 138 21.325 23.345 -60.475 1.00 66.04 C ANISOU 667 CD1 ILE A 138 8446 6683 9964 -2617 1712 909 C ATOM 668 N LEU A 139 15.729 23.509 -59.839 1.00 52.92 N ANISOU 668 N LEU A 139 7686 4352 8069 -2066 1136 701 N ATOM 669 CA LEU A 139 14.510 23.852 -59.135 1.00 52.43 C ANISOU 669 CA LEU A 139 7771 4135 8013 -1967 953 653 C ATOM 670 C LEU A 139 13.370 22.907 -59.469 1.00 50.24 C ANISOU 670 C LEU A 139 7565 3851 7674 -1756 928 592 C ATOM 671 O LEU A 139 12.520 22.688 -58.645 1.00 49.23 O ANISOU 671 O LEU A 139 7449 3668 7587 -1636 803 528 O ATOM 672 CB LEU A 139 14.079 25.286 -59.417 1.00 54.46 C ANISOU 672 CB LEU A 139 8274 4206 8212 -2082 875 722 C ATOM 673 CG LEU A 139 14.894 26.294 -58.592 1.00 57.33 C ANISOU 673 CG LEU A 139 8594 4524 8666 -2277 825 749 C ATOM 674 CD1 LEU A 139 14.437 27.679 -58.959 1.00 58.35 C ANISOU 674 CD1 LEU A 139 8997 4442 8733 -2381 757 819 C ATOM 675 CD2 LEU A 139 14.700 26.110 -57.101 1.00 57.43 C ANISOU 675 CD2 LEU A 139 8503 4530 8786 -2208 690 657 C ATOM 676 N CYS A 140 13.381 22.346 -60.683 1.00 51.19 N ANISOU 676 N CYS A 140 7731 4032 7688 -1725 1052 611 N ATOM 677 CA CYS A 140 12.441 21.335 -61.101 1.00 48.30 C ANISOU 677 CA CYS A 140 7419 3678 7256 -1550 1043 548 C ATOM 678 C CYS A 140 12.536 20.126 -60.159 1.00 45.50 C ANISOU 678 C CYS A 140 6864 3412 7011 -1420 1034 457 C ATOM 679 O CYS A 140 11.526 19.756 -59.588 1.00 42.27 O ANISOU 679 O CYS A 140 6487 2950 6622 -1298 917 399 O ATOM 680 CB CYS A 140 12.652 20.959 -62.573 1.00 52.57 C ANISOU 680 CB CYS A 140 8042 4279 7652 -1566 1194 580 C ATOM 681 SG CYS A 140 11.684 19.550 -63.146 1.00 53.94 S ANISOU 681 SG CYS A 140 8270 4484 7739 -1376 1199 488 S ATOM 682 N LYS A 141 13.754 19.588 -59.983 1.00 45.15 N ANISOU 682 N LYS A 141 6613 3502 7040 -1452 1157 455 N ATOM 683 CA LYS A 141 14.038 18.507 -59.038 1.00 44.42 C ANISOU 683 CA LYS A 141 6320 3496 7063 -1338 1151 389 C ATOM 684 C LYS A 141 13.608 18.807 -57.621 1.00 43.35 C ANISOU 684 C LYS A 141 6146 3302 7023 -1315 980 360 C ATOM 685 O LYS A 141 12.950 18.038 -56.989 1.00 40.29 O ANISOU 685 O LYS A 141 5734 2905 6669 -1182 911 299 O ATOM 686 CB LYS A 141 15.531 18.144 -59.034 1.00 45.36 C ANISOU 686 CB LYS A 141 6208 3770 7258 -1391 1297 415 C ATOM 687 CG LYS A 141 15.990 17.579 -60.379 1.00 47.20 C ANISOU 687 CG LYS A 141 6455 4081 7396 -1375 1497 424 C ATOM 688 CD LYS A 141 17.457 17.224 -60.441 1.00 49.16 C ANISOU 688 CD LYS A 141 6461 4497 7722 -1412 1662 452 C ATOM 689 CE LYS A 141 17.793 16.548 -61.750 1.00 51.16 C ANISOU 689 CE LYS A 141 6745 4822 7871 -1362 1872 440 C ATOM 690 NZ LYS A 141 17.356 15.092 -61.663 1.00 51.56 N ANISOU 690 NZ LYS A 141 6782 4873 7934 -1146 1892 342 N ATOM 691 N ILE A 142 13.899 20.024 -57.164 1.00 45.39 N ANISOU 691 N ILE A 142 6431 3505 7309 -1458 909 404 N ATOM 692 CA ILE A 142 13.683 20.378 -55.784 1.00 43.80 C ANISOU 692 CA ILE A 142 6192 3260 7191 -1457 762 372 C ATOM 693 C ILE A 142 12.211 20.515 -55.538 1.00 41.75 C ANISOU 693 C ILE A 142 6103 2871 6887 -1346 640 329 C ATOM 694 O ILE A 142 11.732 19.990 -54.574 1.00 42.01 O ANISOU 694 O ILE A 142 6082 2911 6970 -1243 560 272 O ATOM 695 CB ILE A 142 14.458 21.666 -55.445 1.00 46.63 C ANISOU 695 CB ILE A 142 6550 3585 7583 -1659 727 425 C ATOM 696 CG1 ILE A 142 15.936 21.270 -55.256 1.00 49.15 C ANISOU 696 CG1 ILE A 142 6611 4077 7986 -1744 820 454 C ATOM 697 CG2 ILE A 142 13.881 22.330 -54.214 1.00 45.10 C ANISOU 697 CG2 ILE A 142 6424 3284 7427 -1661 559 383 C ATOM 698 CD1 ILE A 142 16.868 22.435 -55.016 1.00 52.74 C ANISOU 698 CD1 ILE A 142 7031 4529 8479 -1975 801 511 C ATOM 699 N VAL A 143 11.482 21.199 -56.424 1.00 41.19 N ANISOU 699 N VAL A 143 6235 2693 6721 -1361 626 362 N ATOM 700 CA VAL A 143 10.047 21.414 -56.222 1.00 40.42 C ANISOU 700 CA VAL A 143 6288 2481 6588 -1248 505 329 C ATOM 701 C VAL A 143 9.233 20.109 -56.415 1.00 40.25 C ANISOU 701 C VAL A 143 6236 2513 6544 -1085 513 273 C ATOM 702 O VAL A 143 8.352 19.801 -55.609 1.00 40.68 O ANISOU 702 O VAL A 143 6283 2543 6632 -979 420 220 O ATOM 703 CB VAL A 143 9.548 22.481 -57.162 1.00 42.78 C ANISOU 703 CB VAL A 143 6802 2657 6793 -1302 484 393 C ATOM 704 CG1 VAL A 143 8.027 22.604 -57.074 1.00 44.09 C ANISOU 704 CG1 VAL A 143 7100 2728 6925 -1161 364 365 C ATOM 705 CG2 VAL A 143 10.196 23.840 -56.783 1.00 43.78 C ANISOU 705 CG2 VAL A 143 6990 2693 6953 -1465 452 442 C ATOM 706 N ILE A 144 9.573 19.314 -57.435 1.00 40.12 N ANISOU 706 N ILE A 144 6198 2572 6472 -1073 631 279 N ATOM 707 CA ILE A 144 8.937 17.994 -57.604 1.00 40.07 C ANISOU 707 CA ILE A 144 6165 2612 6450 -939 646 218 C ATOM 708 C ILE A 144 9.156 17.156 -56.342 1.00 37.20 C ANISOU 708 C ILE A 144 5630 2304 6199 -866 622 165 C ATOM 709 O ILE A 144 8.227 16.600 -55.742 1.00 36.02 O ANISOU 709 O ILE A 144 5480 2135 6071 -765 543 118 O ATOM 710 CB ILE A 144 9.463 17.267 -58.856 1.00 43.55 C ANISOU 710 CB ILE A 144 6613 3122 6810 -945 794 222 C ATOM 711 CG1 ILE A 144 8.875 17.890 -60.111 1.00 49.20 C ANISOU 711 CG1 ILE A 144 7531 3779 7384 -986 789 266 C ATOM 712 CG2 ILE A 144 9.150 15.807 -58.818 1.00 43.45 C ANISOU 712 CG2 ILE A 144 6543 3156 6810 -822 826 149 C ATOM 713 CD1 ILE A 144 7.472 17.422 -60.377 1.00 52.97 C ANISOU 713 CD1 ILE A 144 8114 4213 7800 -882 691 225 C ATOM 714 N SER A 145 10.394 17.124 -55.882 1.00 37.48 N ANISOU 714 N SER A 145 5515 2416 6309 -926 682 183 N ATOM 715 CA SER A 145 10.719 16.347 -54.748 1.00 37.88 C ANISOU 715 CA SER A 145 5406 2528 6457 -861 658 149 C ATOM 716 C SER A 145 9.964 16.773 -53.501 1.00 36.51 C ANISOU 716 C SER A 145 5255 2296 6322 -834 512 124 C ATOM 717 O SER A 145 9.385 15.974 -52.757 1.00 35.65 O ANISOU 717 O SER A 145 5106 2196 6244 -731 464 82 O ATOM 718 CB SER A 145 12.257 16.269 -54.554 1.00 41.50 C ANISOU 718 CB SER A 145 5679 3098 6989 -931 745 184 C ATOM 719 OG SER A 145 12.466 15.389 -53.440 1.00 44.77 O ANISOU 719 OG SER A 145 5947 3572 7492 -842 706 157 O ATOM 720 N ILE A 146 9.981 18.058 -53.219 1.00 36.30 N ANISOU 720 N ILE A 146 5300 2204 6290 -931 445 147 N ATOM 721 CA ILE A 146 9.247 18.584 -52.088 1.00 35.88 C ANISOU 721 CA ILE A 146 5294 2084 6257 -904 318 114 C ATOM 722 C ILE A 146 7.788 18.291 -52.212 1.00 34.72 C ANISOU 722 C ILE A 146 5249 1877 6067 -783 267 80 C ATOM 723 O ILE A 146 7.128 17.899 -51.213 1.00 33.93 O ANISOU 723 O ILE A 146 5117 1780 5995 -700 202 37 O ATOM 724 CB ILE A 146 9.493 20.145 -51.936 1.00 39.03 C ANISOU 724 CB ILE A 146 5795 2388 6646 -1035 262 142 C ATOM 725 CG1 ILE A 146 10.828 20.397 -51.238 1.00 41.11 C ANISOU 725 CG1 ILE A 146 5922 2723 6974 -1160 265 158 C ATOM 726 CG2 ILE A 146 8.462 20.813 -51.083 1.00 39.19 C ANISOU 726 CG2 ILE A 146 5926 2305 6658 -982 147 100 C ATOM 727 CD1 ILE A 146 11.342 21.801 -51.492 1.00 44.90 C ANISOU 727 CD1 ILE A 146 6500 3120 7440 -1331 249 200 C ATOM 728 N ASP A 147 7.251 18.434 -53.433 1.00 35.43 N ANISOU 728 N ASP A 147 5456 1925 6083 -774 295 102 N ATOM 729 CA ASP A 147 5.853 18.223 -53.612 1.00 35.11 C ANISOU 729 CA ASP A 147 5500 1840 6002 -671 233 77 C ATOM 730 C ASP A 147 5.465 16.742 -53.318 1.00 35.29 C ANISOU 730 C ASP A 147 5425 1933 6049 -574 252 30 C ATOM 731 O ASP A 147 4.468 16.472 -52.635 1.00 34.87 O ANISOU 731 O ASP A 147 5367 1870 6013 -494 183 -3 O ATOM 732 CB ASP A 147 5.501 18.511 -55.020 1.00 36.11 C ANISOU 732 CB ASP A 147 5754 1930 6036 -688 257 115 C ATOM 733 CG ASP A 147 4.022 18.713 -55.191 1.00 37.51 C ANISOU 733 CG ASP A 147 6028 2050 6172 -597 160 106 C ATOM 734 OD1 ASP A 147 3.408 19.470 -54.400 1.00 41.77 O ANISOU 734 OD1 ASP A 147 6601 2526 6744 -558 75 97 O ATOM 735 OD2 ASP A 147 3.461 18.118 -56.132 1.00 41.45 O ANISOU 735 OD2 ASP A 147 6572 2572 6606 -563 169 105 O ATOM 736 N TYR A 148 6.209 15.786 -53.874 1.00 35.34 N ANISOU 736 N TYR A 148 5365 2006 6056 -579 352 29 N ATOM 737 CA TYR A 148 5.907 14.352 -53.518 1.00 34.29 C ANISOU 737 CA TYR A 148 5155 1918 5956 -489 370 -14 C ATOM 738 C TYR A 148 6.172 14.058 -52.042 1.00 36.67 C ANISOU 738 C TYR A 148 5339 2252 6342 -459 330 -27 C ATOM 739 O TYR A 148 5.319 13.418 -51.352 1.00 40.47 O ANISOU 739 O TYR A 148 5805 2731 6841 -387 281 -56 O ATOM 740 CB TYR A 148 6.623 13.374 -54.387 1.00 34.54 C ANISOU 740 CB TYR A 148 5157 1995 5971 -482 489 -21 C ATOM 741 CG TYR A 148 5.968 13.188 -55.720 1.00 34.99 C ANISOU 741 CG TYR A 148 5345 2025 5926 -481 512 -33 C ATOM 742 CD1 TYR A 148 5.041 12.205 -55.918 1.00 36.06 C ANISOU 742 CD1 TYR A 148 5518 2147 6037 -420 489 -79 C ATOM 743 CD2 TYR A 148 6.362 13.900 -56.782 1.00 36.32 C ANISOU 743 CD2 TYR A 148 5597 2187 6018 -552 563 3 C ATOM 744 CE1 TYR A 148 4.491 12.008 -57.147 1.00 38.37 C ANISOU 744 CE1 TYR A 148 5931 2423 6225 -431 500 -93 C ATOM 745 CE2 TYR A 148 5.844 13.693 -58.030 1.00 38.50 C ANISOU 745 CE2 TYR A 148 5999 2447 6181 -555 584 -6 C ATOM 746 CZ TYR A 148 4.885 12.778 -58.213 1.00 37.49 C ANISOU 746 CZ TYR A 148 5911 2308 6024 -496 543 -56 C ATOM 747 OH TYR A 148 4.372 12.621 -59.480 1.00 36.09 O ANISOU 747 OH TYR A 148 5870 2121 5721 -513 549 -67 O ATOM 748 N TYR A 149 7.333 14.485 -51.525 1.00 36.79 N ANISOU 748 N TYR A 149 5267 2306 6405 -519 347 -1 N ATOM 749 CA TYR A 149 7.640 14.178 -50.130 1.00 35.94 C ANISOU 749 CA TYR A 149 5052 2240 6363 -494 299 -8 C ATOM 750 C TYR A 149 6.514 14.594 -49.203 1.00 36.54 C ANISOU 750 C TYR A 149 5188 2270 6426 -458 197 -37 C ATOM 751 O TYR A 149 6.155 13.860 -48.291 1.00 34.05 O ANISOU 751 O TYR A 149 4822 1981 6135 -394 169 -53 O ATOM 752 CB TYR A 149 8.892 14.859 -49.646 1.00 38.07 C ANISOU 752 CB TYR A 149 5234 2556 6674 -587 294 23 C ATOM 753 CG TYR A 149 10.042 13.984 -49.510 1.00 40.60 C ANISOU 753 CG TYR A 149 5398 2974 7057 -569 359 46 C ATOM 754 CD1 TYR A 149 10.107 13.088 -48.476 1.00 41.23 C ANISOU 754 CD1 TYR A 149 5385 3098 7183 -491 324 42 C ATOM 755 CD2 TYR A 149 11.119 14.087 -50.359 1.00 42.29 C ANISOU 755 CD2 TYR A 149 5546 3239 7283 -629 456 79 C ATOM 756 CE1 TYR A 149 11.196 12.242 -48.341 1.00 41.03 C ANISOU 756 CE1 TYR A 149 5206 3160 7223 -453 379 72 C ATOM 757 CE2 TYR A 149 12.222 13.280 -50.222 1.00 42.45 C ANISOU 757 CE2 TYR A 149 5398 3360 7372 -594 522 104 C ATOM 758 CZ TYR A 149 12.249 12.371 -49.184 1.00 42.97 C ANISOU 758 CZ TYR A 149 5374 3461 7491 -500 475 101 C ATOM 759 OH TYR A 149 13.326 11.535 -49.015 1.00 45.33 O ANISOU 759 OH TYR A 149 5504 3856 7865 -442 531 133 O ATOM 760 N ASN A 150 5.989 15.807 -49.424 1.00 35.12 N ANISOU 760 N ASN A 150 5120 2018 6206 -496 149 -38 N ATOM 761 CA ASN A 150 5.073 16.402 -48.500 1.00 34.42 C ANISOU 761 CA ASN A 150 5085 1884 6108 -459 65 -68 C ATOM 762 C ASN A 150 3.642 16.076 -48.705 1.00 33.96 C ANISOU 762 C ASN A 150 5078 1801 6022 -369 41 -90 C ATOM 763 O ASN A 150 2.849 16.175 -47.769 1.00 39.03 O ANISOU 763 O ASN A 150 5723 2440 6668 -313 -8 -119 O ATOM 764 CB ASN A 150 5.338 17.945 -48.439 1.00 36.20 C ANISOU 764 CB ASN A 150 5405 2032 6317 -541 21 -62 C ATOM 765 CG ASN A 150 6.645 18.207 -47.742 1.00 40.13 C ANISOU 765 CG ASN A 150 5823 2572 6851 -639 16 -52 C ATOM 766 OD1 ASN A 150 6.713 18.093 -46.528 1.00 41.33 O ANISOU 766 OD1 ASN A 150 5928 2757 7019 -626 -34 -79 O ATOM 767 ND2 ASN A 150 7.707 18.423 -48.504 1.00 38.04 N ANISOU 767 ND2 ASN A 150 5526 2329 6598 -737 71 -10 N ATOM 768 N MET A 151 3.260 15.697 -49.926 1.00 34.45 N ANISOU 768 N MET A 151 5182 1856 6052 -356 73 -78 N ATOM 769 CA MET A 151 2.002 15.022 -50.090 1.00 33.46 C ANISOU 769 CA MET A 151 5064 1737 5910 -282 51 -98 C ATOM 770 C MET A 151 1.988 13.758 -49.127 1.00 35.14 C ANISOU 770 C MET A 151 5174 2010 6168 -241 68 -117 C ATOM 771 O MET A 151 1.018 13.526 -48.399 1.00 33.72 O ANISOU 771 O MET A 151 4976 1843 5995 -189 31 -135 O ATOM 772 CB MET A 151 1.813 14.616 -51.535 1.00 34.66 C ANISOU 772 CB MET A 151 5272 1885 6013 -293 83 -86 C ATOM 773 CG MET A 151 0.679 13.671 -51.753 1.00 36.43 C ANISOU 773 CG MET A 151 5487 2131 6223 -242 61 -109 C ATOM 774 SD MET A 151 0.228 13.209 -53.461 1.00 40.98 S ANISOU 774 SD MET A 151 6153 2702 6716 -263 71 -108 S ATOM 775 CE MET A 151 1.715 12.419 -53.999 1.00 47.30 C ANISOU 775 CE MET A 151 6937 3520 7515 -308 196 -113 C ATOM 776 N PHE A 152 3.059 12.973 -49.148 1.00 34.33 N ANISOU 776 N PHE A 152 5006 1944 6096 -262 129 -106 N ATOM 777 CA PHE A 152 3.056 11.682 -48.419 1.00 35.22 C ANISOU 777 CA PHE A 152 5041 2094 6246 -217 148 -111 C ATOM 778 C PHE A 152 3.229 11.933 -46.898 1.00 34.78 C ANISOU 778 C PHE A 152 4931 2069 6216 -206 102 -107 C ATOM 779 O PHE A 152 2.583 11.320 -46.104 1.00 33.78 O ANISOU 779 O PHE A 152 4781 1959 6095 -165 84 -113 O ATOM 780 CB PHE A 152 4.134 10.753 -48.965 1.00 35.47 C ANISOU 780 CB PHE A 152 5026 2147 6306 -217 230 -98 C ATOM 781 CG PHE A 152 3.779 10.113 -50.246 1.00 37.97 C ANISOU 781 CG PHE A 152 5407 2435 6585 -212 280 -117 C ATOM 782 CD1 PHE A 152 2.712 9.197 -50.309 1.00 40.53 C ANISOU 782 CD1 PHE A 152 5762 2739 6899 -181 264 -142 C ATOM 783 CD2 PHE A 152 4.539 10.323 -51.384 1.00 41.99 C ANISOU 783 CD2 PHE A 152 5947 2944 7065 -246 349 -112 C ATOM 784 CE1 PHE A 152 2.397 8.553 -51.522 1.00 41.33 C ANISOU 784 CE1 PHE A 152 5937 2811 6956 -190 302 -170 C ATOM 785 CE2 PHE A 152 4.215 9.690 -52.599 1.00 43.39 C ANISOU 785 CE2 PHE A 152 6202 3095 7187 -244 398 -139 C ATOM 786 CZ PHE A 152 3.149 8.808 -52.664 1.00 41.97 C ANISOU 786 CZ PHE A 152 6065 2889 6994 -217 368 -172 C ATOM 787 N THR A 153 4.058 12.899 -46.510 1.00 33.63 N ANISOU 787 N THR A 153 4777 1928 6074 -256 79 -99 N ATOM 788 CA THR A 153 4.203 13.223 -45.101 1.00 34.67 C ANISOU 788 CA THR A 153 4878 2086 6208 -258 24 -105 C ATOM 789 C THR A 153 2.880 13.677 -44.510 1.00 37.51 C ANISOU 789 C THR A 153 5301 2421 6532 -214 -19 -139 C ATOM 790 O THR A 153 2.526 13.353 -43.405 1.00 37.24 O ANISOU 790 O THR A 153 5242 2420 6488 -181 -39 -147 O ATOM 791 CB THR A 153 5.312 14.245 -44.940 1.00 35.86 C ANISOU 791 CB THR A 153 5022 2240 6365 -343 0 -97 C ATOM 792 OG1 THR A 153 6.461 13.580 -45.402 1.00 40.00 O ANISOU 792 OG1 THR A 153 5451 2814 6931 -364 52 -60 O ATOM 793 CG2 THR A 153 5.548 14.624 -43.467 1.00 37.05 C ANISOU 793 CG2 THR A 153 5154 2420 6502 -360 -69 -111 C ATOM 794 N SER A 154 2.198 14.561 -45.240 1.00 40.51 N ANISOU 794 N SER A 154 5764 2741 6888 -211 -32 -156 N ATOM 795 CA SER A 154 0.965 15.130 -44.799 1.00 35.55 C ANISOU 795 CA SER A 154 5185 2088 6233 -153 -66 -187 C ATOM 796 C SER A 154 -0.017 13.960 -44.562 1.00 32.47 C ANISOU 796 C SER A 154 4738 1749 5849 -95 -47 -186 C ATOM 797 O SER A 154 -0.600 13.821 -43.491 1.00 30.09 O ANISOU 797 O SER A 154 4415 1482 5536 -57 -54 -202 O ATOM 798 CB SER A 154 0.399 16.051 -45.854 1.00 33.92 C ANISOU 798 CB SER A 154 5067 1812 6009 -143 -83 -187 C ATOM 799 OG SER A 154 -0.907 16.425 -45.449 1.00 42.67 O ANISOU 799 OG SER A 154 6198 2912 7103 -60 -110 -213 O ATOM 800 N ILE A 155 -0.224 13.176 -45.616 1.00 32.59 N ANISOU 800 N ILE A 155 4742 1766 5876 -99 -20 -169 N ATOM 801 CA ILE A 155 -1.142 12.096 -45.607 1.00 33.45 C ANISOU 801 CA ILE A 155 4809 1907 5991 -70 -7 -168 C ATOM 802 C ILE A 155 -0.783 10.996 -44.559 1.00 31.92 C ANISOU 802 C ILE A 155 4553 1756 5818 -69 20 -151 C ATOM 803 O ILE A 155 -1.671 10.493 -43.878 1.00 32.46 O ANISOU 803 O ILE A 155 4592 1858 5883 -45 21 -151 O ATOM 804 CB ILE A 155 -1.278 11.491 -47.000 1.00 35.17 C ANISOU 804 CB ILE A 155 5050 2107 6206 -92 11 -162 C ATOM 805 CG1 ILE A 155 -1.996 12.529 -47.889 1.00 38.56 C ANISOU 805 CG1 ILE A 155 5542 2507 6602 -80 -33 -167 C ATOM 806 CG2 ILE A 155 -2.109 10.219 -46.895 1.00 34.32 C ANISOU 806 CG2 ILE A 155 4902 2027 6111 -87 23 -163 C ATOM 807 CD1 ILE A 155 -1.939 12.122 -49.332 1.00 41.76 C ANISOU 807 CD1 ILE A 155 5993 2894 6980 -115 -23 -161 C ATOM 808 N PHE A 156 0.492 10.611 -44.469 1.00 32.20 N ANISOU 808 N PHE A 156 4565 1794 5876 -92 41 -130 N ATOM 809 CA PHE A 156 0.923 9.603 -43.482 1.00 33.82 C ANISOU 809 CA PHE A 156 4717 2033 6100 -78 54 -100 C ATOM 810 C PHE A 156 0.738 10.128 -42.042 1.00 33.86 C ANISOU 810 C PHE A 156 4715 2079 6071 -67 17 -104 C ATOM 811 O PHE A 156 0.372 9.395 -41.186 1.00 32.53 O ANISOU 811 O PHE A 156 4525 1941 5893 -49 24 -83 O ATOM 812 CB PHE A 156 2.352 9.128 -43.736 1.00 36.16 C ANISOU 812 CB PHE A 156 4973 2331 6433 -88 81 -71 C ATOM 813 CG PHE A 156 2.535 8.401 -45.057 1.00 35.82 C ANISOU 813 CG PHE A 156 4947 2250 6414 -86 138 -74 C ATOM 814 CD1 PHE A 156 1.441 7.970 -45.790 1.00 38.39 C ANISOU 814 CD1 PHE A 156 5322 2542 6723 -88 148 -98 C ATOM 815 CD2 PHE A 156 3.785 8.210 -45.567 1.00 37.19 C ANISOU 815 CD2 PHE A 156 5084 2426 6618 -87 180 -58 C ATOM 816 CE1 PHE A 156 1.614 7.302 -46.988 1.00 35.97 C ANISOU 816 CE1 PHE A 156 5051 2196 6419 -94 197 -111 C ATOM 817 CE2 PHE A 156 3.979 7.569 -46.772 1.00 36.78 C ANISOU 817 CE2 PHE A 156 5061 2339 6574 -80 246 -71 C ATOM 818 CZ PHE A 156 2.887 7.127 -47.478 1.00 38.49 C ANISOU 818 CZ PHE A 156 5351 2512 6762 -85 252 -102 C ATOM 819 N THR A 157 0.910 11.437 -41.791 1.00 32.54 N ANISOU 819 N THR A 157 4584 1904 5876 -82 -19 -134 N ATOM 820 CA THR A 157 0.780 11.946 -40.434 1.00 31.61 C ANISOU 820 CA THR A 157 4481 1819 5710 -73 -51 -152 C ATOM 821 C THR A 157 -0.691 11.950 -40.014 1.00 35.62 C ANISOU 821 C THR A 157 5003 2344 6187 -22 -32 -175 C ATOM 822 O THR A 157 -1.065 11.665 -38.855 1.00 35.36 O ANISOU 822 O THR A 157 4962 2361 6113 -4 -25 -172 O ATOM 823 CB THR A 157 1.333 13.343 -40.378 1.00 32.05 C ANISOU 823 CB THR A 157 4592 1841 5744 -109 -92 -188 C ATOM 824 OG1 THR A 157 2.676 13.276 -40.788 1.00 32.26 O ANISOU 824 OG1 THR A 157 4580 1871 5806 -167 -102 -158 O ATOM 825 CG2 THR A 157 1.295 13.912 -38.932 1.00 32.73 C ANISOU 825 CG2 THR A 157 4716 1955 5765 -108 -129 -221 C ATOM 826 N LEU A 158 -1.562 12.285 -40.963 1.00 36.51 N ANISOU 826 N LEU A 158 5131 2424 6316 0 -23 -194 N ATOM 827 CA LEU A 158 -2.958 12.261 -40.662 1.00 38.29 C ANISOU 827 CA LEU A 158 5340 2683 6526 51 -4 -210 C ATOM 828 C LEU A 158 -3.557 10.876 -40.479 1.00 36.15 C ANISOU 828 C LEU A 158 5005 2459 6270 41 33 -172 C ATOM 829 O LEU A 158 -4.459 10.721 -39.616 1.00 37.38 O ANISOU 829 O LEU A 158 5132 2673 6399 68 60 -174 O ATOM 830 CB LEU A 158 -3.709 13.168 -41.588 1.00 44.18 C ANISOU 830 CB LEU A 158 6115 3389 7282 88 -22 -236 C ATOM 831 CG LEU A 158 -4.084 12.773 -42.965 1.00 41.11 C ANISOU 831 CG LEU A 158 5712 2982 6925 74 -30 -217 C ATOM 832 CD1 LEU A 158 -5.301 11.911 -42.900 1.00 42.57 C ANISOU 832 CD1 LEU A 158 5823 3230 7123 88 -11 -205 C ATOM 833 CD2 LEU A 158 -4.370 14.051 -43.765 1.00 39.95 C ANISOU 833 CD2 LEU A 158 5628 2778 6773 110 -68 -235 C ATOM 834 N CYS A 159 -3.029 9.874 -41.204 1.00 35.01 N ANISOU 834 N CYS A 159 4846 2290 6165 2 41 -139 N ATOM 835 CA CYS A 159 -3.285 8.487 -40.881 1.00 34.94 C ANISOU 835 CA CYS A 159 4803 2301 6170 -19 74 -98 C ATOM 836 C CYS A 159 -2.819 8.150 -39.505 1.00 34.23 C ANISOU 836 C CYS A 159 4709 2249 6048 -15 81 -66 C ATOM 837 O CYS A 159 -3.532 7.516 -38.764 1.00 37.54 O ANISOU 837 O CYS A 159 5109 2708 6448 -20 110 -40 O ATOM 838 CB CYS A 159 -2.612 7.552 -41.888 1.00 36.42 C ANISOU 838 CB CYS A 159 5002 2433 6403 -49 85 -78 C ATOM 839 SG CYS A 159 -3.322 7.684 -43.558 1.00 45.73 S ANISOU 839 SG CYS A 159 6201 3577 7597 -70 74 -112 S ATOM 840 N THR A 160 -1.567 8.505 -39.201 1.00 33.85 N ANISOU 840 N THR A 160 4677 2192 5993 -15 52 -60 N ATOM 841 CA THR A 160 -1.025 8.352 -37.902 1.00 36.12 C ANISOU 841 CA THR A 160 4966 2524 6236 -12 36 -31 C ATOM 842 C THR A 160 -1.901 8.843 -36.777 1.00 35.74 C ANISOU 842 C THR A 160 4936 2532 6111 5 48 -53 C ATOM 843 O THR A 160 -2.057 8.173 -35.777 1.00 34.66 O ANISOU 843 O THR A 160 4798 2440 5931 3 64 -10 O ATOM 844 CB THR A 160 0.402 8.922 -37.793 1.00 36.83 C ANISOU 844 CB THR A 160 5056 2611 6326 -26 -15 -31 C ATOM 845 OG1 THR A 160 1.226 8.216 -38.725 1.00 35.74 O ANISOU 845 OG1 THR A 160 4885 2436 6259 -30 -3 2 O ATOM 846 CG2 THR A 160 0.967 8.680 -36.409 1.00 36.88 C ANISOU 846 CG2 THR A 160 5062 2675 6276 -27 -50 8 C ATOM 847 N MET A 161 -2.482 10.031 -36.924 1.00 37.78 N ANISOU 847 N MET A 161 5220 2787 6348 28 45 -118 N ATOM 848 CA MET A 161 -3.377 10.575 -35.934 1.00 37.60 C ANISOU 848 CA MET A 161 5217 2816 6255 64 73 -153 C ATOM 849 C MET A 161 -4.666 9.747 -35.780 1.00 36.25 C ANISOU 849 C MET A 161 4988 2697 6087 72 139 -124 C ATOM 850 O MET A 161 -5.194 9.583 -34.689 1.00 36.75 O ANISOU 850 O MET A 161 5052 2827 6083 82 182 -116 O ATOM 851 CB MET A 161 -3.692 12.005 -36.285 1.00 40.43 C ANISOU 851 CB MET A 161 5618 3136 6605 104 59 -229 C ATOM 852 CG MET A 161 -2.525 12.981 -36.028 1.00 45.23 C ANISOU 852 CG MET A 161 6301 3700 7183 77 -2 -265 C ATOM 853 SD MET A 161 -2.916 14.634 -36.685 1.00 49.97 S ANISOU 853 SD MET A 161 6979 4214 7793 121 -19 -344 S ATOM 854 CE MET A 161 -1.555 15.602 -36.150 1.00 59.41 C ANISOU 854 CE MET A 161 8267 5362 8943 55 -88 -382 C ATOM 855 N SER A 162 -5.133 9.148 -36.868 1.00 34.52 N ANISOU 855 N SER A 162 4722 2453 5942 53 148 -105 N ATOM 856 CA SER A 162 -6.251 8.228 -36.812 1.00 36.35 C ANISOU 856 CA SER A 162 4892 2731 6188 30 199 -70 C ATOM 857 C SER A 162 -5.885 6.963 -36.044 1.00 34.45 C ANISOU 857 C SER A 162 4661 2500 5928 -18 222 5 C ATOM 858 O SER A 162 -6.639 6.478 -35.184 1.00 33.60 O ANISOU 858 O SER A 162 4530 2456 5779 -35 277 38 O ATOM 859 CB SER A 162 -6.686 7.863 -38.228 1.00 39.81 C ANISOU 859 CB SER A 162 5294 3129 6702 3 182 -71 C ATOM 860 OG SER A 162 -7.926 7.255 -38.187 1.00 49.87 O ANISOU 860 OG SER A 162 6497 4461 7990 -26 222 -50 O ATOM 861 N VAL A 163 -4.733 6.381 -36.368 1.00 35.69 N ANISOU 861 N VAL A 163 4851 2592 6117 -36 186 38 N ATOM 862 CA VAL A 163 -4.280 5.141 -35.684 1.00 34.74 C ANISOU 862 CA VAL A 163 4750 2461 5987 -65 198 121 C ATOM 863 C VAL A 163 -4.068 5.383 -34.187 1.00 34.41 C ANISOU 863 C VAL A 163 4740 2490 5846 -49 200 146 C ATOM 864 O VAL A 163 -4.447 4.611 -33.328 1.00 36.90 O ANISOU 864 O VAL A 163 5066 2840 6116 -74 237 209 O ATOM 865 CB VAL A 163 -2.985 4.672 -36.296 1.00 35.84 C ANISOU 865 CB VAL A 163 4911 2525 6182 -57 159 144 C ATOM 866 CG1 VAL A 163 -2.363 3.544 -35.460 1.00 40.38 C ANISOU 866 CG1 VAL A 163 5514 3086 6744 -58 157 236 C ATOM 867 CG2 VAL A 163 -3.289 4.151 -37.684 1.00 38.15 C ANISOU 867 CG2 VAL A 163 5195 2746 6552 -82 173 126 C ATOM 868 N ASP A 164 -3.462 6.513 -33.865 1.00 36.69 N ANISOU 868 N ASP A 164 5053 2800 6089 -17 157 93 N ATOM 869 CA ASP A 164 -3.259 6.960 -32.481 1.00 35.19 C ANISOU 869 CA ASP A 164 4909 2678 5783 -6 147 93 C ATOM 870 C ASP A 164 -4.562 6.997 -31.676 1.00 35.47 C ANISOU 870 C ASP A 164 4942 2792 5744 -2 230 86 C ATOM 871 O ASP A 164 -4.651 6.439 -30.586 1.00 35.78 O ANISOU 871 O ASP A 164 5011 2885 5698 -20 257 143 O ATOM 872 CB ASP A 164 -2.625 8.308 -32.539 1.00 36.67 C ANISOU 872 CB ASP A 164 5129 2857 5948 14 91 13 C ATOM 873 CG ASP A 164 -2.393 8.875 -31.182 1.00 39.98 C ANISOU 873 CG ASP A 164 5614 3339 6238 17 71 -8 C ATOM 874 OD1 ASP A 164 -1.638 8.257 -30.408 1.00 42.20 O ANISOU 874 OD1 ASP A 164 5915 3651 6469 -4 28 60 O ATOM 875 OD2 ASP A 164 -2.999 9.904 -30.862 1.00 42.05 O ANISOU 875 OD2 ASP A 164 5915 3620 6443 45 98 -90 O ATOM 876 N ARG A 165 -5.605 7.551 -32.291 1.00 34.04 N ANISOU 876 N ARG A 165 4715 2619 5602 21 275 27 N ATOM 877 CA ARG A 165 -6.926 7.607 -31.667 1.00 35.04 C ANISOU 877 CA ARG A 165 4805 2832 5676 33 367 18 C ATOM 878 C ARG A 165 -7.635 6.269 -31.541 1.00 34.56 C ANISOU 878 C ARG A 165 4694 2801 5635 -32 428 107 C ATOM 879 O ARG A 165 -8.202 5.972 -30.510 1.00 33.59 O ANISOU 879 O ARG A 165 4575 2760 5429 -48 500 142 O ATOM 880 CB ARG A 165 -7.760 8.628 -32.379 1.00 36.02 C ANISOU 880 CB ARG A 165 4881 2960 5845 92 385 -65 C ATOM 881 CG ARG A 165 -7.159 10.037 -32.178 1.00 37.05 C ANISOU 881 CG ARG A 165 5092 3057 5927 154 341 -153 C ATOM 882 CD ARG A 165 -7.737 10.895 -33.310 1.00 41.60 C ANISOU 882 CD ARG A 165 5630 3591 6585 210 329 -212 C ATOM 883 NE ARG A 165 -7.451 12.308 -33.131 1.00 45.81 N ANISOU 883 NE ARG A 165 6247 4079 7078 275 303 -300 N ATOM 884 CZ ARG A 165 -7.751 13.273 -33.997 1.00 48.39 C ANISOU 884 CZ ARG A 165 6580 4347 7460 336 280 -352 C ATOM 885 NH1 ARG A 165 -8.351 13.040 -35.159 1.00 46.74 N ANISOU 885 NH1 ARG A 165 6288 4127 7343 343 269 -327 N ATOM 886 NH2 ARG A 165 -7.442 14.506 -33.681 1.00 49.93 N ANISOU 886 NH2 ARG A 165 6877 4485 7609 386 260 -429 N ATOM 887 N TYR A 166 -7.504 5.433 -32.578 1.00 33.81 N ANISOU 887 N TYR A 166 4570 2632 5644 -79 399 144 N ATOM 888 CA TYR A 166 -7.978 4.081 -32.501 1.00 34.13 C ANISOU 888 CA TYR A 166 4592 2667 5709 -159 442 231 C ATOM 889 C TYR A 166 -7.288 3.308 -31.352 1.00 33.13 C ANISOU 889 C TYR A 166 4546 2540 5504 -180 444 322 C ATOM 890 O TYR A 166 -7.952 2.667 -30.564 1.00 33.05 O ANISOU 890 O TYR A 166 4535 2582 5439 -231 513 387 O ATOM 891 CB TYR A 166 -7.794 3.452 -33.889 1.00 34.95 C ANISOU 891 CB TYR A 166 4681 2669 5930 -196 399 233 C ATOM 892 CG TYR A 166 -7.795 1.961 -33.828 1.00 34.67 C ANISOU 892 CG TYR A 166 4677 2574 5924 -277 419 324 C ATOM 893 CD1 TYR A 166 -8.956 1.312 -33.726 1.00 36.06 C ANISOU 893 CD1 TYR A 166 4803 2788 6109 -360 481 361 C ATOM 894 CD2 TYR A 166 -6.594 1.235 -33.824 1.00 35.61 C ANISOU 894 CD2 TYR A 166 4876 2595 6060 -265 376 377 C ATOM 895 CE1 TYR A 166 -9.010 -0.064 -33.625 1.00 37.27 C ANISOU 895 CE1 TYR A 166 5004 2871 6288 -449 502 448 C ATOM 896 CE2 TYR A 166 -6.638 -0.133 -33.770 1.00 37.31 C ANISOU 896 CE2 TYR A 166 5139 2733 6306 -329 397 461 C ATOM 897 CZ TYR A 166 -7.851 -0.781 -33.677 1.00 37.85 C ANISOU 897 CZ TYR A 166 5176 2825 6380 -428 459 496 C ATOM 898 OH TYR A 166 -7.973 -2.183 -33.562 1.00 44.98 O ANISOU 898 OH TYR A 166 6144 3635 7310 -513 484 586 O ATOM 899 N ILE A 167 -5.946 3.419 -31.258 1.00 32.71 N ANISOU 899 N ILE A 167 4554 2434 5440 -143 365 330 N ATOM 900 CA ILE A 167 -5.172 2.807 -30.194 1.00 33.12 C ANISOU 900 CA ILE A 167 4679 2491 5414 -146 340 418 C ATOM 901 C ILE A 167 -5.627 3.244 -28.818 1.00 33.71 C ANISOU 901 C ILE A 167 4789 2681 5340 -144 388 423 C ATOM 902 O ILE A 167 -5.930 2.421 -27.957 1.00 33.47 O ANISOU 902 O ILE A 167 4796 2682 5239 -187 434 516 O ATOM 903 CB ILE A 167 -3.699 3.019 -30.419 1.00 35.65 C ANISOU 903 CB ILE A 167 5026 2759 5760 -100 240 416 C ATOM 904 CG1 ILE A 167 -3.180 2.036 -31.515 1.00 39.25 C ANISOU 904 CG1 ILE A 167 5470 3096 6346 -104 218 456 C ATOM 905 CG2 ILE A 167 -2.853 2.746 -29.123 1.00 36.13 C ANISOU 905 CG2 ILE A 167 5153 2863 5712 -87 189 496 C ATOM 906 CD1 ILE A 167 -1.805 2.436 -32.033 1.00 40.73 C ANISOU 906 CD1 ILE A 167 5646 3246 6583 -51 136 432 C ATOM 907 N ALA A 168 -5.815 4.569 -28.628 1.00 33.78 N ANISOU 907 N ALA A 168 4793 2749 5294 -97 391 317 N ATOM 908 CA ALA A 168 -6.317 5.110 -27.369 1.00 34.34 C ANISOU 908 CA ALA A 168 4907 2928 5211 -84 451 296 C ATOM 909 C ALA A 168 -7.630 4.497 -26.886 1.00 35.44 C ANISOU 909 C ALA A 168 5008 3146 5313 -128 580 346 C ATOM 910 O ALA A 168 -7.840 4.196 -25.677 1.00 37.17 O ANISOU 910 O ALA A 168 5285 3444 5394 -152 636 402 O ATOM 911 CB ALA A 168 -6.484 6.613 -27.510 1.00 34.44 C ANISOU 911 CB ALA A 168 4921 2962 5203 -18 449 159 C ATOM 912 N VAL A 169 -8.563 4.298 -27.810 1.00 35.19 N ANISOU 912 N VAL A 169 4873 3103 5395 -149 630 331 N ATOM 913 CA VAL A 169 -9.874 3.844 -27.419 1.00 36.19 C ANISOU 913 CA VAL A 169 4932 3321 5498 -200 755 370 C ATOM 914 C VAL A 169 -9.921 2.303 -27.430 1.00 36.59 C ANISOU 914 C VAL A 169 4995 3320 5586 -308 768 504 C ATOM 915 O VAL A 169 -10.458 1.708 -26.498 1.00 37.27 O ANISOU 915 O VAL A 169 5099 3476 5584 -369 855 585 O ATOM 916 CB VAL A 169 -10.931 4.367 -28.364 1.00 36.98 C ANISOU 916 CB VAL A 169 4898 3450 5701 -178 795 297 C ATOM 917 CG1 VAL A 169 -12.256 3.722 -28.067 1.00 38.62 C ANISOU 917 CG1 VAL A 169 5006 3760 5908 -253 917 354 C ATOM 918 CG2 VAL A 169 -11.062 5.887 -28.272 1.00 37.54 C ANISOU 918 CG2 VAL A 169 4967 3566 5732 -60 801 171 C ATOM 919 N CYS A 170 -9.350 1.690 -28.463 1.00 35.86 N ANISOU 919 N CYS A 170 4907 3101 5618 -332 687 525 N ATOM 920 CA CYS A 170 -9.480 0.218 -28.655 1.00 37.89 C ANISOU 920 CA CYS A 170 5187 3278 5933 -435 701 637 C ATOM 921 C CYS A 170 -8.429 -0.632 -28.008 1.00 37.99 C ANISOU 921 C CYS A 170 5325 3213 5897 -437 652 745 C ATOM 922 O CYS A 170 -8.701 -1.800 -27.717 1.00 41.45 O ANISOU 922 O CYS A 170 5808 3604 6336 -523 690 856 O ATOM 923 CB CYS A 170 -9.632 -0.183 -30.122 1.00 37.32 C ANISOU 923 CB CYS A 170 5062 3102 6014 -472 660 605 C ATOM 924 SG CYS A 170 -11.178 0.501 -30.848 1.00 40.29 S ANISOU 924 SG CYS A 170 5271 3587 6450 -498 720 519 S ATOM 925 N HIS A 171 -7.254 -0.056 -27.724 1.00 37.62 N ANISOU 925 N HIS A 171 5334 3156 5805 -349 565 721 N ATOM 926 CA HIS A 171 -6.130 -0.695 -27.039 1.00 38.49 C ANISOU 926 CA HIS A 171 5547 3215 5861 -325 495 822 C ATOM 927 C HIS A 171 -5.512 0.192 -25.970 1.00 37.54 C ANISOU 927 C HIS A 171 5476 3195 5593 -267 451 800 C ATOM 928 O HIS A 171 -4.339 0.549 -26.035 1.00 36.05 O ANISOU 928 O HIS A 171 5308 2980 5410 -206 344 783 O ATOM 929 CB HIS A 171 -5.083 -1.057 -28.060 1.00 39.74 C ANISOU 929 CB HIS A 171 5709 3241 6150 -280 404 819 C ATOM 930 CG HIS A 171 -5.596 -2.081 -29.046 1.00 43.11 C ANISOU 930 CG HIS A 171 6125 3551 6705 -343 441 844 C ATOM 931 ND1 HIS A 171 -5.972 -1.756 -30.349 1.00 46.15 N ANISOU 931 ND1 HIS A 171 6437 3898 7201 -353 443 745 N ATOM 932 CD2 HIS A 171 -5.881 -3.378 -28.885 1.00 43.53 C ANISOU 932 CD2 HIS A 171 6242 3518 6779 -413 477 955 C ATOM 933 CE1 HIS A 171 -6.392 -2.840 -30.957 1.00 43.24 C ANISOU 933 CE1 HIS A 171 6090 3425 6914 -427 471 787 C ATOM 934 NE2 HIS A 171 -6.345 -3.833 -30.089 1.00 46.02 N ANISOU 934 NE2 HIS A 171 6528 3739 7220 -466 494 912 N ATOM 935 N PRO A 172 -6.288 0.555 -24.942 1.00 38.38 N ANISOU 935 N PRO A 172 5603 3424 5557 -292 535 798 N ATOM 936 CA PRO A 172 -5.839 1.555 -23.979 1.00 38.77 C ANISOU 936 CA PRO A 172 5710 3571 5451 -242 501 744 C ATOM 937 C PRO A 172 -4.629 1.192 -23.191 1.00 40.27 C ANISOU 937 C PRO A 172 5998 3753 5552 -223 390 834 C ATOM 938 O PRO A 172 -3.834 2.092 -22.757 1.00 39.46 O ANISOU 938 O PRO A 172 5931 3697 5364 -180 301 771 O ATOM 939 CB PRO A 172 -7.044 1.681 -23.043 1.00 40.30 C ANISOU 939 CB PRO A 172 5915 3890 5509 -282 643 748 C ATOM 940 CG PRO A 172 -7.883 0.419 -23.198 1.00 40.65 C ANISOU 940 CG PRO A 172 5930 3904 5613 -374 734 863 C ATOM 941 CD PRO A 172 -7.664 0.078 -24.676 1.00 39.34 C ANISOU 941 CD PRO A 172 5689 3604 5655 -373 675 838 C ATOM 942 N VAL A 173 -4.466 -0.102 -22.937 1.00 40.63 N ANISOU 942 N VAL A 173 6093 3740 5605 -258 385 985 N ATOM 943 CA VAL A 173 -3.279 -0.576 -22.272 1.00 43.20 C ANISOU 943 CA VAL A 173 6500 4049 5864 -225 265 1093 C ATOM 944 C VAL A 173 -2.034 -0.381 -23.111 1.00 43.67 C ANISOU 944 C VAL A 173 6505 4032 6054 -154 134 1059 C ATOM 945 O VAL A 173 -1.094 0.214 -22.643 1.00 44.69 O ANISOU 945 O VAL A 173 6651 4216 6112 -116 25 1041 O ATOM 946 CB VAL A 173 -3.386 -2.031 -21.804 1.00 44.96 C ANISOU 946 CB VAL A 173 6804 4210 6070 -266 290 1276 C ATOM 947 CG1 VAL A 173 -2.062 -2.463 -21.186 1.00 46.88 C ANISOU 947 CG1 VAL A 173 7119 4436 6257 -205 144 1391 C ATOM 948 CG2 VAL A 173 -4.494 -2.152 -20.797 1.00 45.97 C ANISOU 948 CG2 VAL A 173 6991 4440 6037 -345 419 1322 C ATOM 949 N LYS A 174 -2.077 -0.767 -24.387 1.00 44.45 N ANISOU 949 N LYS A 174 6534 4016 6339 -145 151 1034 N ATOM 950 CA LYS A 174 -0.972 -0.512 -25.321 1.00 45.76 C ANISOU 950 CA LYS A 174 6635 4117 6635 -79 54 987 C ATOM 951 C LYS A 174 -0.755 0.959 -25.630 1.00 43.22 C ANISOU 951 C LYS A 174 6257 3861 6305 -63 20 836 C ATOM 952 O LYS A 174 0.350 1.382 -25.969 1.00 42.54 O ANISOU 952 O LYS A 174 6129 3766 6267 -21 -80 809 O ATOM 953 CB LYS A 174 -1.171 -1.304 -26.613 1.00 48.98 C ANISOU 953 CB LYS A 174 7002 4385 7222 -79 98 989 C ATOM 954 CG LYS A 174 -0.962 -2.831 -26.316 1.00 57.50 C ANISOU 954 CG LYS A 174 8160 5361 8325 -74 98 1151 C ATOM 955 CD LYS A 174 -1.395 -3.699 -27.486 1.00 64.34 C ANISOU 955 CD LYS A 174 9021 6080 9346 -98 160 1147 C ATOM 956 CE LYS A 174 -1.183 -5.196 -27.224 1.00 66.87 C ANISOU 956 CE LYS A 174 9443 6268 9697 -92 162 1300 C ATOM 957 NZ LYS A 174 -1.948 -5.916 -28.280 1.00 75.73 N ANISOU 957 NZ LYS A 174 10577 7257 10941 -157 241 1270 N ATOM 958 N ALA A 175 -1.822 1.743 -25.531 1.00 39.98 N ANISOU 958 N ALA A 175 5841 3511 5837 -97 106 741 N ATOM 959 CA ALA A 175 -1.725 3.153 -25.712 1.00 38.55 C ANISOU 959 CA ALA A 175 5636 3376 5634 -80 81 602 C ATOM 960 C ALA A 175 -0.712 3.755 -24.751 1.00 38.60 C ANISOU 960 C ALA A 175 5698 3455 5515 -70 -31 600 C ATOM 961 O ALA A 175 -0.098 4.746 -25.072 1.00 39.03 O ANISOU 961 O ALA A 175 5730 3512 5588 -60 -99 508 O ATOM 962 CB ALA A 175 -3.111 3.822 -25.542 1.00 38.35 C ANISOU 962 CB ALA A 175 5608 3412 5551 -98 201 515 C ATOM 963 N LEU A 176 -0.601 3.188 -23.558 1.00 39.93 N ANISOU 963 N LEU A 176 5945 3683 5542 -84 -50 700 N ATOM 964 CA LEU A 176 0.364 3.664 -22.570 1.00 42.70 C ANISOU 964 CA LEU A 176 6355 4115 5753 -84 -174 709 C ATOM 965 C LEU A 176 1.818 3.620 -23.066 1.00 44.86 C ANISOU 965 C LEU A 176 6559 4356 6130 -54 -321 739 C ATOM 966 O LEU A 176 2.640 4.462 -22.643 1.00 42.20 O ANISOU 966 O LEU A 176 6231 4081 5721 -70 -434 688 O ATOM 967 CB LEU A 176 0.249 2.857 -21.265 1.00 43.06 C ANISOU 967 CB LEU A 176 6503 4227 5630 -102 -175 842 C ATOM 968 CG LEU A 176 -1.103 2.943 -20.561 1.00 43.37 C ANISOU 968 CG LEU A 176 6614 4332 5533 -140 -24 820 C ATOM 969 CD1 LEU A 176 -1.171 1.862 -19.476 1.00 45.25 C ANISOU 969 CD1 LEU A 176 6949 4610 5632 -165 -17 988 C ATOM 970 CD2 LEU A 176 -1.394 4.351 -19.980 1.00 43.69 C ANISOU 970 CD2 LEU A 176 6713 4462 5426 -148 -6 665 C ATOM 971 N ASP A 177 2.121 2.632 -23.941 1.00 46.17 N ANISOU 971 N ASP A 177 6656 4427 6462 -15 -315 819 N ATOM 972 CA ASP A 177 3.445 2.483 -24.578 1.00 47.17 C ANISOU 972 CA ASP A 177 6689 4518 6713 31 -423 850 C ATOM 973 C ASP A 177 3.496 3.251 -25.853 1.00 44.93 C ANISOU 973 C ASP A 177 6323 4182 6566 28 -394 727 C ATOM 974 O ASP A 177 4.490 3.854 -26.136 1.00 48.80 O ANISOU 974 O ASP A 177 6748 4696 7098 30 -484 692 O ATOM 975 CB ASP A 177 3.819 1.022 -24.877 1.00 49.85 C ANISOU 975 CB ASP A 177 7010 4771 7159 94 -424 994 C ATOM 976 CG ASP A 177 3.818 0.115 -23.592 1.00 57.56 C ANISOU 976 CG ASP A 177 8085 5784 8000 102 -461 1149 C ATOM 977 OD1 ASP A 177 4.451 0.500 -22.577 1.00 63.81 O ANISOU 977 OD1 ASP A 177 8906 6685 8654 95 -575 1181 O ATOM 978 OD2 ASP A 177 3.160 -0.981 -23.607 1.00 64.60 O ANISOU 978 OD2 ASP A 177 9035 6593 8918 106 -377 1241 O ATOM 979 N PHE A 178 2.422 3.246 -26.637 1.00 43.33 N ANISOU 979 N PHE A 178 6119 3915 6431 17 -273 666 N ATOM 980 CA PHE A 178 2.436 3.892 -27.943 1.00 41.30 C ANISOU 980 CA PHE A 178 5793 3600 6301 18 -246 563 C ATOM 981 C PHE A 178 2.458 5.457 -27.892 1.00 41.80 C ANISOU 981 C PHE A 178 5865 3709 6306 -18 -276 431 C ATOM 982 O PHE A 178 3.072 6.096 -28.759 1.00 39.10 O ANISOU 982 O PHE A 178 5466 3337 6053 -23 -309 372 O ATOM 983 CB PHE A 178 1.277 3.382 -28.845 1.00 44.52 C ANISOU 983 CB PHE A 178 6195 3927 6795 13 -124 544 C ATOM 984 CG PHE A 178 1.235 4.023 -30.236 1.00 51.60 C ANISOU 984 CG PHE A 178 7032 4765 7808 14 -100 445 C ATOM 985 CD1 PHE A 178 2.154 3.687 -31.219 1.00 56.96 C ANISOU 985 CD1 PHE A 178 7652 5382 8609 45 -128 460 C ATOM 986 CD2 PHE A 178 0.293 5.024 -30.551 1.00 57.35 C ANISOU 986 CD2 PHE A 178 7768 5506 8518 -8 -49 338 C ATOM 987 CE1 PHE A 178 2.135 4.305 -32.474 1.00 55.12 C ANISOU 987 CE1 PHE A 178 7379 5104 8461 39 -103 375 C ATOM 988 CE2 PHE A 178 0.289 5.642 -31.806 1.00 54.74 C ANISOU 988 CE2 PHE A 178 7397 5122 8281 -6 -39 261 C ATOM 989 CZ PHE A 178 1.209 5.273 -32.768 1.00 53.35 C ANISOU 989 CZ PHE A 178 7172 4887 8211 10 -65 281 C ATOM 990 N ARG A 179 1.736 6.067 -26.943 1.00 39.47 N ANISOU 990 N ARG A 179 5651 3477 5866 -43 -250 382 N ATOM 991 CA ARG A 179 1.425 7.490 -27.045 1.00 39.03 C ANISOU 991 CA ARG A 179 5628 3428 5772 -64 -242 244 C ATOM 992 C ARG A 179 2.375 8.366 -26.288 1.00 39.89 C ANISOU 992 C ARG A 179 5782 3594 5781 -103 -360 203 C ATOM 993 O ARG A 179 1.958 9.275 -25.608 1.00 43.19 O ANISOU 993 O ARG A 179 6290 4044 6076 -122 -351 115 O ATOM 994 CB ARG A 179 -0.009 7.771 -26.643 1.00 39.02 C ANISOU 994 CB ARG A 179 5685 3451 5691 -54 -126 189 C ATOM 995 CG ARG A 179 -0.989 6.920 -27.430 1.00 41.07 C ANISOU 995 CG ARG A 179 5885 3664 6055 -37 -20 229 C ATOM 996 CD ARG A 179 -2.429 7.287 -27.100 1.00 40.64 C ANISOU 996 CD ARG A 179 5852 3652 5936 -26 99 172 C ATOM 997 NE ARG A 179 -2.869 8.462 -27.818 1.00 37.66 N ANISOU 997 NE ARG A 179 5461 3241 5607 3 121 51 N ATOM 998 CZ ARG A 179 -3.911 9.184 -27.462 1.00 38.54 C ANISOU 998 CZ ARG A 179 5596 3392 5654 37 204 -26 C ATOM 999 NH1 ARG A 179 -4.569 8.994 -26.329 1.00 39.06 N ANISOU 999 NH1 ARG A 179 5707 3546 5588 39 279 -12 N ATOM 1000 NH2 ARG A 179 -4.290 10.136 -28.270 1.00 40.42 N ANISOU 1000 NH2 ARG A 179 5816 3581 5961 76 217 -118 N ATOM 1001 N THR A 180 3.667 8.095 -26.444 1.00 40.02 N ANISOU 1001 N THR A 180 5730 3622 5854 -115 -470 265 N ATOM 1002 CA THR A 180 4.728 8.843 -25.805 1.00 41.07 C ANISOU 1002 CA THR A 180 5878 3817 5909 -171 -606 239 C ATOM 1003 C THR A 180 5.318 9.772 -26.850 1.00 39.61 C ANISOU 1003 C THR A 180 5633 3579 5839 -209 -635 159 C ATOM 1004 O THR A 180 5.329 9.419 -28.032 1.00 37.86 O ANISOU 1004 O THR A 180 5327 3291 5767 -176 -579 177 O ATOM 1005 CB THR A 180 5.879 7.957 -25.374 1.00 42.29 C ANISOU 1005 CB THR A 180 5962 4035 6071 -160 -721 370 C ATOM 1006 OG1 THR A 180 6.422 7.287 -26.526 1.00 41.62 O ANISOU 1006 OG1 THR A 180 5748 3893 6171 -114 -704 429 O ATOM 1007 CG2 THR A 180 5.427 6.951 -24.324 1.00 43.45 C ANISOU 1007 CG2 THR A 180 6178 4229 6101 -126 -706 476 C ATOM 1008 N PRO A 181 5.881 10.935 -26.428 1.00 39.72 N ANISOU 1008 N PRO A 181 5697 3618 5778 -287 -727 76 N ATOM 1009 CA PRO A 181 6.625 11.800 -27.336 1.00 39.42 C ANISOU 1009 CA PRO A 181 5602 3534 5844 -347 -770 19 C ATOM 1010 C PRO A 181 7.770 11.073 -28.112 1.00 38.79 C ANISOU 1010 C PRO A 181 5350 3475 5912 -337 -815 120 C ATOM 1011 O PRO A 181 8.029 11.325 -29.267 1.00 36.43 O ANISOU 1011 O PRO A 181 4983 3119 5741 -345 -776 101 O ATOM 1012 CB PRO A 181 7.172 12.926 -26.415 1.00 40.23 C ANISOU 1012 CB PRO A 181 5796 3679 5813 -451 -889 -62 C ATOM 1013 CG PRO A 181 6.682 12.680 -25.046 1.00 41.74 C ANISOU 1013 CG PRO A 181 6100 3940 5819 -437 -903 -58 C ATOM 1014 CD PRO A 181 5.812 11.449 -25.048 1.00 41.57 C ANISOU 1014 CD PRO A 181 6058 3922 5815 -333 -791 31 C ATOM 1015 N ARG A 182 8.422 10.138 -27.446 1.00 41.41 N ANISOU 1015 N ARG A 182 5620 3892 6221 -309 -890 231 N ATOM 1016 CA ARG A 182 9.493 9.405 -28.045 1.00 43.31 C ANISOU 1016 CA ARG A 182 5698 4162 6597 -275 -927 329 C ATOM 1017 C ARG A 182 8.998 8.609 -29.241 1.00 41.60 C ANISOU 1017 C ARG A 182 5435 3851 6519 -187 -791 356 C ATOM 1018 O ARG A 182 9.603 8.621 -30.284 1.00 39.62 O ANISOU 1018 O ARG A 182 5081 3576 6398 -182 -766 359 O ATOM 1019 CB ARG A 182 10.121 8.531 -27.002 1.00 47.65 C ANISOU 1019 CB ARG A 182 6210 4811 7082 -239 -1034 449 C ATOM 1020 CG ARG A 182 11.412 7.906 -27.477 1.00 52.87 C ANISOU 1020 CG ARG A 182 6685 5524 7880 -197 -1096 550 C ATOM 1021 CD ARG A 182 12.025 7.127 -26.348 1.00 58.64 C ANISOU 1021 CD ARG A 182 7386 6360 8535 -155 -1223 676 C ATOM 1022 NE ARG A 182 13.391 6.760 -26.681 1.00 69.53 N ANISOU 1022 NE ARG A 182 8565 7815 10037 -120 -1308 765 N ATOM 1023 CZ ARG A 182 13.731 5.649 -27.346 1.00 71.61 C ANISOU 1023 CZ ARG A 182 8722 8042 10444 12 -1248 860 C ATOM 1024 NH1 ARG A 182 12.795 4.775 -27.760 1.00 66.24 N ANISOU 1024 NH1 ARG A 182 8130 7239 9799 105 -1109 878 N ATOM 1025 NH2 ARG A 182 15.020 5.411 -27.590 1.00 72.38 N ANISOU 1025 NH2 ARG A 182 8623 8228 10651 50 -1325 936 N ATOM 1026 N ASN A 183 7.885 7.894 -29.078 1.00 42.27 N ANISOU 1026 N ASN A 183 5600 3888 6571 -125 -700 375 N ATOM 1027 CA ASN A 183 7.306 7.125 -30.159 1.00 39.66 C ANISOU 1027 CA ASN A 183 5247 3464 6356 -59 -578 391 C ATOM 1028 C ASN A 183 6.776 7.909 -31.304 1.00 37.40 C ANISOU 1028 C ASN A 183 4974 3102 6134 -86 -499 290 C ATOM 1029 O ASN A 183 6.891 7.494 -32.426 1.00 35.17 O ANISOU 1029 O ASN A 183 4635 2762 5965 -53 -437 300 O ATOM 1030 CB ASN A 183 6.273 6.165 -29.647 1.00 41.47 C ANISOU 1030 CB ASN A 183 5555 3667 6533 -10 -512 443 C ATOM 1031 CG ASN A 183 6.908 4.912 -29.141 1.00 44.77 C ANISOU 1031 CG ASN A 183 5936 4109 6967 55 -557 580 C ATOM 1032 OD1 ASN A 183 8.005 4.518 -29.573 1.00 44.99 O ANISOU 1032 OD1 ASN A 183 5856 4144 7093 98 -603 636 O ATOM 1033 ND2 ASN A 183 6.267 4.299 -28.183 1.00 47.04 N ANISOU 1033 ND2 ASN A 183 6310 4411 7153 67 -547 640 N ATOM 1034 N ALA A 184 6.241 9.089 -31.013 1.00 38.30 N ANISOU 1034 N ALA A 184 5173 3214 6166 -144 -505 193 N ATOM 1035 CA ALA A 184 5.710 9.942 -32.035 1.00 37.28 C ANISOU 1035 CA ALA A 184 5069 3008 6086 -165 -443 103 C ATOM 1036 C ALA A 184 6.846 10.453 -32.939 1.00 37.84 C ANISOU 1036 C ALA A 184 5056 3071 6252 -213 -478 96 C ATOM 1037 O ALA A 184 6.672 10.560 -34.149 1.00 40.91 O ANISOU 1037 O ALA A 184 5425 3394 6724 -204 -410 74 O ATOM 1038 CB ALA A 184 4.929 11.068 -31.399 1.00 36.41 C ANISOU 1038 CB ALA A 184 5078 2891 5866 -197 -444 6 C ATOM 1039 N LYS A 185 7.993 10.788 -32.336 1.00 38.27 N ANISOU 1039 N LYS A 185 5059 3201 6282 -272 -586 117 N ATOM 1040 CA LYS A 185 9.214 11.098 -33.100 1.00 39.63 C ANISOU 1040 CA LYS A 185 5115 3394 6551 -323 -618 134 C ATOM 1041 C LYS A 185 9.703 9.904 -33.962 1.00 38.21 C ANISOU 1041 C LYS A 185 4811 3213 6493 -238 -556 217 C ATOM 1042 O LYS A 185 9.949 10.056 -35.125 1.00 37.73 O ANISOU 1042 O LYS A 185 4705 3113 6519 -245 -492 202 O ATOM 1043 CB LYS A 185 10.318 11.634 -32.202 1.00 43.51 C ANISOU 1043 CB LYS A 185 5558 3983 6992 -413 -757 146 C ATOM 1044 CG LYS A 185 9.976 13.061 -31.728 1.00 49.08 C ANISOU 1044 CG LYS A 185 6400 4653 7596 -519 -804 36 C ATOM 1045 CD LYS A 185 10.885 13.604 -30.634 1.00 56.10 C ANISOU 1045 CD LYS A 185 7281 5636 8399 -626 -957 32 C ATOM 1046 CE LYS A 185 10.744 15.126 -30.556 1.00 71.25 C ANISOU 1046 CE LYS A 185 9332 7484 10255 -749 -991 -88 C ATOM 1047 NZ LYS A 185 11.548 15.808 -29.478 1.00 81.83 N ANISOU 1047 NZ LYS A 185 10700 8900 11493 -881 -1148 -118 N ATOM 1048 N ILE A 186 9.757 8.699 -33.397 1.00 36.28 N ANISOU 1048 N ILE A 186 4535 3001 6249 -152 -565 302 N ATOM 1049 CA ILE A 186 10.189 7.600 -34.161 1.00 36.68 C ANISOU 1049 CA ILE A 186 4494 3031 6411 -62 -503 369 C ATOM 1050 C ILE A 186 9.205 7.394 -35.337 1.00 36.87 C ANISOU 1050 C ILE A 186 4587 2942 6481 -32 -373 318 C ATOM 1051 O ILE A 186 9.612 7.087 -36.470 1.00 36.32 O ANISOU 1051 O ILE A 186 4456 2838 6504 -2 -303 321 O ATOM 1052 CB ILE A 186 10.255 6.370 -33.237 1.00 38.59 C ANISOU 1052 CB ILE A 186 4730 3302 6631 28 -539 472 C ATOM 1053 CG1 ILE A 186 11.457 6.530 -32.324 1.00 40.20 C ANISOU 1053 CG1 ILE A 186 4831 3631 6810 6 -679 535 C ATOM 1054 CG2 ILE A 186 10.262 5.077 -34.052 1.00 37.72 C ANISOU 1054 CG2 ILE A 186 4587 3117 6627 141 -444 526 C ATOM 1055 CD1 ILE A 186 11.466 5.529 -31.182 1.00 42.37 C ANISOU 1055 CD1 ILE A 186 5128 3945 7025 81 -744 640 C ATOM 1056 N VAL A 187 7.897 7.555 -35.076 1.00 36.62 N ANISOU 1056 N VAL A 187 4676 2860 6377 -41 -340 271 N ATOM 1057 CA VAL A 187 6.901 7.327 -36.104 1.00 36.39 C ANISOU 1057 CA VAL A 187 4703 2739 6383 -19 -238 229 C ATOM 1058 C VAL A 187 7.027 8.297 -37.278 1.00 36.87 C ANISOU 1058 C VAL A 187 4761 2765 6482 -70 -206 162 C ATOM 1059 O VAL A 187 6.901 7.887 -38.452 1.00 35.93 O ANISOU 1059 O VAL A 187 4637 2590 6426 -44 -129 154 O ATOM 1060 CB VAL A 187 5.462 7.294 -35.529 1.00 37.20 C ANISOU 1060 CB VAL A 187 4909 2818 6406 -18 -212 201 C ATOM 1061 CG1 VAL A 187 4.428 7.465 -36.628 1.00 35.88 C ANISOU 1061 CG1 VAL A 187 4787 2576 6268 -20 -133 142 C ATOM 1062 CG2 VAL A 187 5.270 5.954 -34.796 1.00 39.40 C ANISOU 1062 CG2 VAL A 187 5196 3101 6673 38 -205 287 C ATOM 1063 N ASN A 188 7.253 9.574 -36.958 1.00 34.77 N ANISOU 1063 N ASN A 188 4516 2524 6170 -147 -264 114 N ATOM 1064 CA ASN A 188 7.527 10.606 -37.952 1.00 36.71 C ANISOU 1064 CA ASN A 188 4767 2735 6446 -211 -246 65 C ATOM 1065 C ASN A 188 8.778 10.281 -38.791 1.00 37.61 C ANISOU 1065 C ASN A 188 4761 2879 6649 -216 -219 109 C ATOM 1066 O ASN A 188 8.763 10.473 -39.970 1.00 37.01 O ANISOU 1066 O ASN A 188 4692 2758 6612 -227 -152 89 O ATOM 1067 CB ASN A 188 7.727 11.971 -37.262 1.00 35.25 C ANISOU 1067 CB ASN A 188 4633 2564 6195 -303 -327 14 C ATOM 1068 CG ASN A 188 6.394 12.593 -36.800 1.00 36.49 C ANISOU 1068 CG ASN A 188 4925 2669 6270 -290 -321 -54 C ATOM 1069 OD1 ASN A 188 5.306 12.196 -37.251 1.00 38.28 O ANISOU 1069 OD1 ASN A 188 5191 2851 6503 -228 -253 -66 O ATOM 1070 ND2 ASN A 188 6.478 13.586 -35.903 1.00 37.92 N ANISOU 1070 ND2 ASN A 188 5174 2859 6374 -349 -391 -104 N ATOM 1071 N VAL A 189 9.806 9.680 -38.169 1.00 37.17 N ANISOU 1071 N VAL A 189 4593 2907 6624 -194 -267 175 N ATOM 1072 CA VAL A 189 10.984 9.310 -38.915 1.00 37.88 C ANISOU 1072 CA VAL A 189 4549 3040 6806 -178 -230 219 C ATOM 1073 C VAL A 189 10.646 8.134 -39.864 1.00 37.66 C ANISOU 1073 C VAL A 189 4528 2946 6834 -72 -116 233 C ATOM 1074 O VAL A 189 11.007 8.147 -41.025 1.00 35.74 O ANISOU 1074 O VAL A 189 4255 2684 6641 -72 -33 221 O ATOM 1075 CB VAL A 189 12.146 8.955 -37.994 1.00 41.22 C ANISOU 1075 CB VAL A 189 4834 3577 7253 -166 -319 293 C ATOM 1076 CG1 VAL A 189 13.311 8.283 -38.766 1.00 42.15 C ANISOU 1076 CG1 VAL A 189 4787 3746 7482 -104 -258 351 C ATOM 1077 CG2 VAL A 189 12.653 10.209 -37.286 1.00 40.47 C ANISOU 1077 CG2 VAL A 189 4725 3548 7105 -301 -432 268 C ATOM 1078 N CYS A 190 9.960 7.119 -39.324 1.00 38.40 N ANISOU 1078 N CYS A 190 4675 3004 6912 9 -112 260 N ATOM 1079 CA CYS A 190 9.509 5.964 -40.110 1.00 39.73 C ANISOU 1079 CA CYS A 190 4882 3090 7124 96 -15 265 C ATOM 1080 C CYS A 190 8.658 6.417 -41.338 1.00 40.20 C ANISOU 1080 C CYS A 190 5035 3073 7167 54 59 189 C ATOM 1081 O CYS A 190 8.875 5.934 -42.459 1.00 41.02 O ANISOU 1081 O CYS A 190 5136 3135 7314 88 147 176 O ATOM 1082 CB CYS A 190 8.740 4.962 -39.271 1.00 37.63 C ANISOU 1082 CB CYS A 190 4682 2785 6829 155 -31 303 C ATOM 1083 SG CYS A 190 9.764 4.091 -38.040 1.00 40.55 S ANISOU 1083 SG CYS A 190 4958 3227 7224 238 -108 415 S ATOM 1084 N ASN A 191 7.685 7.298 -41.104 1.00 35.86 N ANISOU 1084 N ASN A 191 4571 2505 6550 -10 23 140 N ATOM 1085 CA ASN A 191 6.887 7.839 -42.181 1.00 36.40 C ANISOU 1085 CA ASN A 191 4721 2513 6598 -46 70 80 C ATOM 1086 C ASN A 191 7.740 8.591 -43.193 1.00 36.25 C ANISOU 1086 C ASN A 191 4666 2505 6602 -95 104 67 C ATOM 1087 O ASN A 191 7.494 8.545 -44.398 1.00 35.14 O ANISOU 1087 O ASN A 191 4571 2317 6462 -98 172 40 O ATOM 1088 CB ASN A 191 5.782 8.740 -41.620 1.00 36.99 C ANISOU 1088 CB ASN A 191 4877 2576 6603 -86 19 39 C ATOM 1089 CG ASN A 191 4.674 7.907 -40.965 1.00 38.46 C ANISOU 1089 CG ASN A 191 5105 2745 6763 -43 21 47 C ATOM 1090 OD1 ASN A 191 4.563 6.688 -41.236 1.00 37.52 O ANISOU 1090 OD1 ASN A 191 4983 2594 6679 2 66 75 O ATOM 1091 ND2 ASN A 191 3.907 8.525 -40.076 1.00 34.61 N ANISOU 1091 ND2 ASN A 191 4659 2278 6215 -59 -20 25 N ATOM 1092 N TRP A 192 8.770 9.275 -42.716 1.00 36.17 N ANISOU 1092 N TRP A 192 4575 2562 6605 -146 56 89 N ATOM 1093 CA TRP A 192 9.588 10.004 -43.626 1.00 38.28 C ANISOU 1093 CA TRP A 192 4803 2846 6895 -211 94 85 C ATOM 1094 C TRP A 192 10.391 8.985 -44.505 1.00 38.39 C ANISOU 1094 C TRP A 192 4733 2879 6974 -143 197 114 C ATOM 1095 O TRP A 192 10.582 9.146 -45.727 1.00 38.02 O ANISOU 1095 O TRP A 192 4705 2811 6929 -162 283 96 O ATOM 1096 CB TRP A 192 10.489 10.939 -42.862 1.00 38.26 C ANISOU 1096 CB TRP A 192 4728 2915 6894 -300 13 102 C ATOM 1097 CG TRP A 192 11.354 11.712 -43.778 1.00 43.04 C ANISOU 1097 CG TRP A 192 5287 3541 7525 -389 57 106 C ATOM 1098 CD1 TRP A 192 11.015 12.906 -44.425 1.00 44.12 C ANISOU 1098 CD1 TRP A 192 5526 3615 7621 -484 62 72 C ATOM 1099 CD2 TRP A 192 12.719 11.428 -44.143 1.00 44.69 C ANISOU 1099 CD2 TRP A 192 5333 3841 7805 -399 104 155 C ATOM 1100 NE1 TRP A 192 12.059 13.309 -45.192 1.00 45.48 N ANISOU 1100 NE1 TRP A 192 5620 3831 7829 -561 116 100 N ATOM 1101 CE2 TRP A 192 13.122 12.451 -45.035 1.00 47.78 C ANISOU 1101 CE2 TRP A 192 5739 4226 8190 -514 147 148 C ATOM 1102 CE3 TRP A 192 13.617 10.387 -43.841 1.00 49.12 C ANISOU 1102 CE3 TRP A 192 5739 4489 8437 -311 122 209 C ATOM 1103 CZ2 TRP A 192 14.384 12.478 -45.620 1.00 49.74 C ANISOU 1103 CZ2 TRP A 192 5838 4563 8498 -558 215 190 C ATOM 1104 CZ3 TRP A 192 14.871 10.409 -44.422 1.00 53.08 C ANISOU 1104 CZ3 TRP A 192 6083 5080 9006 -335 186 248 C ATOM 1105 CH2 TRP A 192 15.256 11.460 -45.293 1.00 52.27 C ANISOU 1105 CH2 TRP A 192 5985 4983 8893 -465 235 238 C ATOM 1106 N ILE A 193 10.882 7.939 -43.867 1.00 39.68 N ANISOU 1106 N ILE A 193 4812 3079 7186 -55 191 159 N ATOM 1107 CA ILE A 193 11.555 6.844 -44.578 1.00 39.44 C ANISOU 1107 CA ILE A 193 4716 3050 7221 43 292 182 C ATOM 1108 C ILE A 193 10.669 6.333 -45.705 1.00 38.87 C ANISOU 1108 C ILE A 193 4775 2874 7119 72 383 128 C ATOM 1109 O ILE A 193 11.107 6.201 -46.867 1.00 40.66 O ANISOU 1109 O ILE A 193 4999 3094 7358 84 488 109 O ATOM 1110 CB ILE A 193 12.074 5.788 -43.615 1.00 39.77 C ANISOU 1110 CB ILE A 193 4669 3125 7316 149 256 246 C ATOM 1111 CG1 ILE A 193 13.236 6.381 -42.814 1.00 41.44 C ANISOU 1111 CG1 ILE A 193 4720 3467 7560 107 173 301 C ATOM 1112 CG2 ILE A 193 12.557 4.492 -44.378 1.00 42.58 C ANISOU 1112 CG2 ILE A 193 4995 3442 7741 283 375 259 C ATOM 1113 CD1 ILE A 193 13.650 5.551 -41.607 1.00 44.97 C ANISOU 1113 CD1 ILE A 193 5089 3962 8037 197 92 376 C ATOM 1114 N LEU A 194 9.394 6.123 -45.393 1.00 39.79 N ANISOU 1114 N LEU A 194 5010 2921 7188 71 342 102 N ATOM 1115 CA LEU A 194 8.468 5.508 -46.312 1.00 40.77 C ANISOU 1115 CA LEU A 194 5253 2953 7283 91 404 55 C ATOM 1116 C LEU A 194 8.268 6.494 -47.459 1.00 41.32 C ANISOU 1116 C LEU A 194 5382 3016 7303 12 436 11 C ATOM 1117 O LEU A 194 8.330 6.124 -48.619 1.00 42.76 O ANISOU 1117 O LEU A 194 5614 3162 7470 25 523 -19 O ATOM 1118 CB LEU A 194 7.174 5.220 -45.587 1.00 41.97 C ANISOU 1118 CB LEU A 194 5487 3060 7401 85 340 47 C ATOM 1119 CG LEU A 194 6.117 4.449 -46.366 1.00 45.16 C ANISOU 1119 CG LEU A 194 6005 3374 7779 92 382 3 C ATOM 1120 CD1 LEU A 194 6.593 3.070 -46.860 1.00 46.54 C ANISOU 1120 CD1 LEU A 194 6197 3485 8000 174 466 5 C ATOM 1121 CD2 LEU A 194 4.846 4.371 -45.504 1.00 50.56 C ANISOU 1121 CD2 LEU A 194 6735 4043 8432 67 314 6 C ATOM 1122 N SER A 195 8.040 7.765 -47.120 1.00 37.96 N ANISOU 1122 N SER A 195 4965 2616 6842 -69 365 9 N ATOM 1123 CA SER A 195 7.914 8.822 -48.095 1.00 38.21 C ANISOU 1123 CA SER A 195 5058 2634 6825 -146 382 -15 C ATOM 1124 C SER A 195 9.121 8.916 -49.023 1.00 38.43 C ANISOU 1124 C SER A 195 5025 2702 6873 -164 478 0 C ATOM 1125 O SER A 195 9.000 9.330 -50.176 1.00 39.00 O ANISOU 1125 O SER A 195 5172 2750 6895 -206 532 -19 O ATOM 1126 CB SER A 195 7.771 10.145 -47.339 1.00 38.49 C ANISOU 1126 CB SER A 195 5099 2686 6839 -220 289 -10 C ATOM 1127 OG SER A 195 6.540 10.099 -46.650 1.00 42.15 O ANISOU 1127 OG SER A 195 5627 3116 7274 -195 224 -31 O ATOM 1128 N SER A 196 10.307 8.608 -48.496 1.00 39.63 N ANISOU 1128 N SER A 196 5035 2928 7095 -137 496 41 N ATOM 1129 CA SER A 196 11.537 8.660 -49.304 1.00 42.31 C ANISOU 1129 CA SER A 196 5281 3330 7465 -148 601 61 C ATOM 1130 C SER A 196 11.539 7.631 -50.456 1.00 43.06 C ANISOU 1130 C SER A 196 5428 3385 7548 -67 733 28 C ATOM 1131 O SER A 196 12.194 7.856 -51.472 1.00 43.90 O ANISOU 1131 O SER A 196 5519 3524 7638 -93 839 26 O ATOM 1132 CB SER A 196 12.766 8.459 -48.433 1.00 43.17 C ANISOU 1132 CB SER A 196 5201 3541 7661 -121 582 116 C ATOM 1133 OG SER A 196 12.877 9.488 -47.461 1.00 45.36 O ANISOU 1133 OG SER A 196 5441 3859 7934 -218 462 138 O ATOM 1134 N ALA A 197 10.804 6.517 -50.300 1.00 43.39 N ANISOU 1134 N ALA A 197 5542 3353 7590 22 729 1 N ATOM 1135 CA ALA A 197 10.730 5.525 -51.369 1.00 46.52 C ANISOU 1135 CA ALA A 197 6019 3692 7966 92 846 -45 C ATOM 1136 C ALA A 197 10.228 6.129 -52.689 1.00 50.30 C ANISOU 1136 C ALA A 197 6630 4141 8341 12 892 -89 C ATOM 1137 O ALA A 197 10.599 5.634 -53.749 1.00 48.97 O ANISOU 1137 O ALA A 197 6505 3961 8140 46 1015 -123 O ATOM 1138 CB ALA A 197 9.876 4.369 -50.977 1.00 44.49 C ANISOU 1138 CB ALA A 197 5845 3343 7718 164 817 -69 C ATOM 1139 N ILE A 198 9.432 7.212 -52.618 1.00 46.12 N ANISOU 1139 N ILE A 198 6167 3600 7755 -84 796 -86 N ATOM 1140 CA ILE A 198 9.064 7.995 -53.798 1.00 46.41 C ANISOU 1140 CA ILE A 198 6319 3621 7693 -164 821 -104 C ATOM 1141 C ILE A 198 9.743 9.352 -53.852 1.00 47.28 C ANISOU 1141 C ILE A 198 6378 3787 7798 -262 815 -57 C ATOM 1142 O ILE A 198 10.137 9.825 -54.942 1.00 45.19 O ANISOU 1142 O ILE A 198 6161 3539 7471 -318 898 -51 O ATOM 1143 CB ILE A 198 7.497 8.090 -53.982 1.00 48.44 C ANISOU 1143 CB ILE A 198 6721 3805 7878 -188 724 -139 C ATOM 1144 CG1 ILE A 198 6.957 6.736 -54.532 1.00 51.94 C ANISOU 1144 CG1 ILE A 198 7252 4188 8295 -129 769 -197 C ATOM 1145 CG2 ILE A 198 7.127 9.196 -54.976 1.00 48.25 C ANISOU 1145 CG2 ILE A 198 6804 3773 7757 -273 711 -133 C ATOM 1146 CD1 ILE A 198 5.476 6.423 -54.308 1.00 51.56 C ANISOU 1146 CD1 ILE A 198 7289 4085 8219 -139 665 -225 C ATOM 1147 N GLY A 199 9.918 9.995 -52.695 1.00 44.10 N ANISOU 1147 N GLY A 199 5890 3412 7453 -294 721 -22 N ATOM 1148 CA GLY A 199 10.490 11.344 -52.681 1.00 45.97 C ANISOU 1148 CA GLY A 199 6100 3683 7685 -408 700 19 C ATOM 1149 C GLY A 199 11.886 11.493 -53.233 1.00 47.09 C ANISOU 1149 C GLY A 199 6130 3909 7854 -453 816 55 C ATOM 1150 O GLY A 199 12.220 12.497 -53.856 1.00 48.04 O ANISOU 1150 O GLY A 199 6285 4037 7932 -562 845 83 O ATOM 1151 N LEU A 200 12.721 10.486 -52.983 1.00 48.44 N ANISOU 1151 N LEU A 200 6160 4145 8099 -365 887 60 N ATOM 1152 CA LEU A 200 14.100 10.476 -53.462 1.00 51.82 C ANISOU 1152 CA LEU A 200 6443 4677 8569 -383 1013 95 C ATOM 1153 C LEU A 200 14.244 10.062 -54.925 1.00 49.61 C ANISOU 1153 C LEU A 200 6239 4392 8216 -358 1177 68 C ATOM 1154 O LEU A 200 14.945 10.750 -55.668 1.00 45.58 O ANISOU 1154 O LEU A 200 5703 3940 7676 -451 1268 100 O ATOM 1155 CB LEU A 200 14.970 9.524 -52.630 1.00 59.32 C ANISOU 1155 CB LEU A 200 7199 5705 9633 -273 1027 117 C ATOM 1156 CG LEU A 200 15.491 10.138 -51.357 1.00 62.23 C ANISOU 1156 CG LEU A 200 7426 6144 10073 -337 902 166 C ATOM 1157 CD1 LEU A 200 16.190 9.029 -50.592 1.00 64.48 C ANISOU 1157 CD1 LEU A 200 7543 6498 10460 -199 905 193 C ATOM 1158 CD2 LEU A 200 16.391 11.297 -51.684 1.00 66.20 C ANISOU 1158 CD2 LEU A 200 7844 6729 10581 -493 931 211 C ATOM 1159 N PRO A 201 13.654 8.929 -55.385 1.00 43.75 N ANISOU 1159 N PRO A 201 5598 3586 7441 -242 1228 8 N ATOM 1160 CA PRO A 201 13.682 8.610 -56.812 1.00 46.42 C ANISOU 1160 CA PRO A 201 6047 3910 7680 -231 1374 -31 C ATOM 1161 C PRO A 201 13.236 9.800 -57.736 1.00 48.46 C ANISOU 1161 C PRO A 201 6453 4146 7813 -372 1365 -15 C ATOM 1162 O PRO A 201 13.906 10.068 -58.775 1.00 51.26 O ANISOU 1162 O PRO A 201 6819 4554 8104 -420 1507 -1 O ATOM 1163 CB PRO A 201 12.767 7.405 -56.914 1.00 45.78 C ANISOU 1163 CB PRO A 201 6091 3729 7573 -120 1361 -104 C ATOM 1164 CG PRO A 201 12.935 6.674 -55.570 1.00 44.66 C ANISOU 1164 CG PRO A 201 5820 3589 7561 -22 1289 -87 C ATOM 1165 CD PRO A 201 13.004 7.881 -54.589 1.00 44.09 C ANISOU 1165 CD PRO A 201 5657 3565 7530 -127 1155 -24 C ATOM 1166 N VAL A 202 12.184 10.541 -57.347 1.00 47.50 N ANISOU 1166 N VAL A 202 6436 3953 7658 -434 1209 -7 N ATOM 1167 CA VAL A 202 11.717 11.649 -58.202 1.00 46.79 C ANISOU 1167 CA VAL A 202 6498 3827 7454 -548 1188 18 C ATOM 1168 C VAL A 202 12.727 12.747 -58.326 1.00 46.80 C ANISOU 1168 C VAL A 202 6422 3891 7468 -673 1238 90 C ATOM 1169 O VAL A 202 12.827 13.398 -59.366 1.00 47.70 O ANISOU 1169 O VAL A 202 6641 4004 7481 -760 1304 121 O ATOM 1170 CB VAL A 202 10.341 12.236 -57.840 1.00 45.32 C ANISOU 1170 CB VAL A 202 6441 3547 7230 -568 1016 13 C ATOM 1171 CG1 VAL A 202 9.250 11.174 -57.965 1.00 44.13 C ANISOU 1171 CG1 VAL A 202 6381 3342 7046 -473 976 -54 C ATOM 1172 CG2 VAL A 202 10.362 12.971 -56.516 1.00 46.98 C ANISOU 1172 CG2 VAL A 202 6563 3754 7535 -601 895 45 C ATOM 1173 N MET A 203 13.516 12.927 -57.278 1.00 48.71 N ANISOU 1173 N MET A 203 6482 4194 7831 -690 1207 122 N ATOM 1174 CA MET A 203 14.620 13.856 -57.302 1.00 55.18 C ANISOU 1174 CA MET A 203 7193 5090 8683 -822 1257 189 C ATOM 1175 C MET A 203 15.609 13.497 -58.450 1.00 52.85 C ANISOU 1175 C MET A 203 6841 4890 8350 -829 1468 204 C ATOM 1176 O MET A 203 16.154 14.367 -59.188 1.00 51.51 O ANISOU 1176 O MET A 203 6691 4754 8124 -965 1549 260 O ATOM 1177 CB MET A 203 15.250 13.809 -55.901 1.00 62.07 C ANISOU 1177 CB MET A 203 7864 6025 9694 -816 1174 207 C ATOM 1178 CG MET A 203 16.562 14.546 -55.734 1.00 76.47 C ANISOU 1178 CG MET A 203 9515 7957 11582 -950 1218 274 C ATOM 1179 SD MET A 203 16.331 15.960 -54.666 1.00 93.72 S ANISOU 1179 SD MET A 203 11738 10078 13792 -1106 1027 302 S ATOM 1180 CE MET A 203 15.593 17.092 -55.819 1.00 87.03 C ANISOU 1180 CE MET A 203 11153 9106 12810 -1220 1041 324 C ATOM 1181 N PHE A 204 15.837 12.194 -58.627 1.00 50.70 N ANISOU 1181 N PHE A 204 6506 4654 8101 -680 1568 153 N ATOM 1182 CA PHE A 204 16.687 11.683 -59.715 1.00 52.30 C ANISOU 1182 CA PHE A 204 6669 4943 8262 -648 1786 146 C ATOM 1183 C PHE A 204 15.948 11.720 -61.043 1.00 49.44 C ANISOU 1183 C PHE A 204 6552 4510 7722 -669 1849 112 C ATOM 1184 O PHE A 204 16.508 12.147 -62.049 1.00 50.15 O ANISOU 1184 O PHE A 204 6672 4658 7724 -750 1992 144 O ATOM 1185 CB PHE A 204 17.191 10.242 -59.395 1.00 58.03 C ANISOU 1185 CB PHE A 204 7254 5713 9080 -460 1872 97 C ATOM 1186 CG PHE A 204 18.352 10.233 -58.463 1.00 61.60 C ANISOU 1186 CG PHE A 204 7425 6289 9691 -447 1875 152 C ATOM 1187 CD1 PHE A 204 19.631 10.468 -58.932 1.00 66.78 C ANISOU 1187 CD1 PHE A 204 7901 7090 10380 -493 2037 201 C ATOM 1188 CD2 PHE A 204 18.166 10.040 -57.102 1.00 63.41 C ANISOU 1188 CD2 PHE A 204 7562 6502 10029 -401 1709 162 C ATOM 1189 CE1 PHE A 204 20.719 10.473 -58.064 1.00 71.05 C ANISOU 1189 CE1 PHE A 204 8159 7766 11073 -488 2025 259 C ATOM 1190 CE2 PHE A 204 19.251 10.056 -56.226 1.00 65.03 C ANISOU 1190 CE2 PHE A 204 7504 6833 10372 -396 1691 219 C ATOM 1191 CZ PHE A 204 20.526 10.273 -56.707 1.00 66.92 C ANISOU 1191 CZ PHE A 204 7551 7223 10654 -440 1842 268 C ATOM 1192 N MET A 205 14.659 11.352 -61.032 1.00 46.01 N ANISOU 1192 N MET A 205 6294 3959 7227 -611 1731 55 N ATOM 1193 CA MET A 205 13.886 11.257 -62.270 1.00 47.47 C ANISOU 1193 CA MET A 205 6714 4085 7238 -622 1767 17 C ATOM 1194 C MET A 205 13.458 12.625 -62.851 1.00 46.56 C ANISOU 1194 C MET A 205 6747 3933 7009 -774 1704 86 C ATOM 1195 O MET A 205 13.334 12.796 -64.066 1.00 45.93 O ANISOU 1195 O MET A 205 6826 3853 6774 -821 1787 90 O ATOM 1196 CB MET A 205 12.669 10.401 -62.050 1.00 48.12 C ANISOU 1196 CB MET A 205 6914 4067 7302 -524 1653 -61 C ATOM 1197 CG MET A 205 12.992 8.945 -61.588 1.00 50.73 C ANISOU 1197 CG MET A 205 7146 4400 7727 -367 1719 -131 C ATOM 1198 SD MET A 205 11.446 8.271 -60.839 1.00 54.11 S ANISOU 1198 SD MET A 205 7678 4704 8177 -303 1521 -189 S ATOM 1199 CE MET A 205 10.883 7.814 -62.452 1.00 55.83 C ANISOU 1199 CE MET A 205 8137 4879 8196 -313 1605 -262 C ATOM 1200 N ALA A 206 13.239 13.595 -61.975 1.00 45.04 N ANISOU 1200 N ALA A 206 6517 3705 6891 -848 1557 141 N ATOM 1201 CA ALA A 206 12.731 14.914 -62.428 1.00 46.11 C ANISOU 1201 CA ALA A 206 6813 3775 6932 -976 1477 210 C ATOM 1202 C ALA A 206 13.738 15.582 -63.287 1.00 47.52 C ANISOU 1202 C ALA A 206 6989 4022 7046 -1102 1630 281 C ATOM 1203 O ALA A 206 14.923 15.570 -62.987 1.00 50.57 O ANISOU 1203 O ALA A 206 7183 4508 7524 -1140 1737 308 O ATOM 1204 CB ALA A 206 12.357 15.801 -61.259 1.00 45.37 C ANISOU 1204 CB ALA A 206 6685 3617 6937 -1019 1301 243 C ATOM 1205 N THR A 207 13.276 16.158 -64.390 1.00 48.81 N ANISOU 1205 N THR A 207 7361 4140 7045 -1172 1642 320 N ATOM 1206 CA THR A 207 14.146 16.940 -65.246 1.00 51.91 C ANISOU 1206 CA THR A 207 7781 4585 7356 -1316 1783 406 C ATOM 1207 C THR A 207 13.311 17.825 -66.107 1.00 51.79 C ANISOU 1207 C THR A 207 8025 4474 7177 -1391 1707 467 C ATOM 1208 O THR A 207 12.144 17.599 -66.277 1.00 50.44 O ANISOU 1208 O THR A 207 8000 4228 6938 -1313 1582 429 O ATOM 1209 CB THR A 207 15.053 16.026 -66.129 1.00 55.86 C ANISOU 1209 CB THR A 207 8218 5213 7793 -1278 2026 370 C ATOM 1210 OG1 THR A 207 16.124 16.803 -66.668 1.00 60.46 O ANISOU 1210 OG1 THR A 207 8751 5877 8344 -1431 2178 463 O ATOM 1211 CG2 THR A 207 14.269 15.394 -67.269 1.00 55.08 C ANISOU 1211 CG2 THR A 207 8341 5082 7504 -1210 2060 311 C ATOM 1212 N THR A 208 13.924 18.867 -66.654 1.00 55.92 N ANISOU 1212 N THR A 208 8602 5004 7640 -1551 1780 572 N ATOM 1213 CA THR A 208 13.260 19.677 -67.644 1.00 59.26 C ANISOU 1213 CA THR A 208 9287 5343 7886 -1623 1734 648 C ATOM 1214 C THR A 208 13.582 19.110 -68.995 1.00 63.65 C ANISOU 1214 C THR A 208 9939 5989 8258 -1627 1920 639 C ATOM 1215 O THR A 208 14.728 18.747 -69.237 1.00 65.65 O ANISOU 1215 O THR A 208 10051 6365 8527 -1664 2126 636 O ATOM 1216 CB THR A 208 13.760 21.154 -67.630 1.00 58.03 C ANISOU 1216 CB THR A 208 9179 5129 7739 -1811 1725 780 C ATOM 1217 OG1 THR A 208 15.187 21.187 -67.606 1.00 56.96 O ANISOU 1217 OG1 THR A 208 8855 5119 7669 -1925 1912 814 O ATOM 1218 CG2 THR A 208 13.232 21.863 -66.400 1.00 56.25 C ANISOU 1218 CG2 THR A 208 8931 4781 7659 -1806 1519 784 C ATOM 1219 N LYS A 209 12.592 19.098 -69.891 1.00 66.52 N ANISOU 1219 N LYS A 209 10542 6294 8439 -1596 1849 641 N ATOM 1220 CA LYS A 209 12.871 18.867 -71.295 1.00 76.57 C ANISOU 1220 CA LYS A 209 11964 7637 9492 -1639 2015 657 C ATOM 1221 C LYS A 209 11.939 19.680 -72.221 1.00 80.90 C ANISOU 1221 C LYS A 209 12806 8095 9838 -1695 1894 747 C ATOM 1222 O LYS A 209 10.779 20.003 -71.851 1.00 76.48 O ANISOU 1222 O LYS A 209 12336 7425 9299 -1636 1665 753 O ATOM 1223 CB LYS A 209 12.814 17.352 -71.604 1.00 79.85 C ANISOU 1223 CB LYS A 209 12349 8127 9863 -1498 2111 511 C ATOM 1224 CG LYS A 209 11.415 16.789 -71.709 1.00 80.21 C ANISOU 1224 CG LYS A 209 12542 8096 9838 -1390 1924 435 C ATOM 1225 CD LYS A 209 11.408 15.281 -71.534 1.00 87.66 C ANISOU 1225 CD LYS A 209 13401 9082 10823 -1250 1989 282 C ATOM 1226 CE LYS A 209 12.065 14.564 -72.702 1.00 96.72 C ANISOU 1226 CE LYS A 209 14632 10321 11796 -1248 2224 226 C ATOM 1227 NZ LYS A 209 11.147 14.398 -73.869 1.00 99.53 N ANISOU 1227 NZ LYS A 209 15269 10650 11897 -1259 2163 202 N ATOM 1228 N TYR A 210 12.453 19.980 -73.425 1.00 86.28 N ANISOU 1228 N TYR A 210 13630 8832 10320 -1802 2054 819 N ATOM 1229 CA TYR A 210 11.683 20.600 -74.510 1.00 87.51 C ANISOU 1229 CA TYR A 210 14081 8927 10240 -1852 1970 908 C ATOM 1230 C TYR A 210 10.504 19.739 -75.036 1.00 86.89 C ANISOU 1230 C TYR A 210 14152 8840 10021 -1726 1845 812 C ATOM 1231 O TYR A 210 10.593 18.512 -75.170 1.00 84.51 O ANISOU 1231 O TYR A 210 13794 8615 9701 -1637 1935 676 O ATOM 1232 CB TYR A 210 12.603 20.999 -75.644 1.00 91.02 C ANISOU 1232 CB TYR A 210 14633 9453 10498 -1999 2196 1002 C ATOM 1233 CG TYR A 210 13.570 22.090 -75.275 1.00 99.95 C ANISOU 1233 CG TYR A 210 15670 10570 11736 -2164 2279 1131 C ATOM 1234 CD1 TYR A 210 13.107 23.384 -74.970 1.00109.12 C ANISOU 1234 CD1 TYR A 210 16948 11577 12934 -2245 2101 1260 C ATOM 1235 CD2 TYR A 210 14.958 21.855 -75.254 1.00102.75 C ANISOU 1235 CD2 TYR A 210 15823 11064 12155 -2244 2536 1126 C ATOM 1236 CE1 TYR A 210 13.995 24.407 -74.633 1.00107.81 C ANISOU 1236 CE1 TYR A 210 16716 11382 12865 -2419 2171 1375 C ATOM 1237 CE2 TYR A 210 15.855 22.864 -74.916 1.00103.12 C ANISOU 1237 CE2 TYR A 210 15774 11106 12302 -2421 2605 1247 C ATOM 1238 CZ TYR A 210 15.368 24.140 -74.606 1.00110.41 C ANISOU 1238 CZ TYR A 210 16833 11861 13257 -2518 2419 1369 C ATOM 1239 OH TYR A 210 16.242 25.155 -74.278 1.00112.04 O ANISOU 1239 OH TYR A 210 16966 12045 13560 -2714 2479 1485 O ATOM 1240 N ARG A 211 9.407 20.439 -75.335 1.00 88.01 N ANISOU 1240 N ARG A 211 14488 8883 10068 -1724 1630 892 N ATOM 1241 CA ARG A 211 8.105 19.883 -75.634 1.00 92.80 C ANISOU 1241 CA ARG A 211 15215 9465 10578 -1618 1441 827 C ATOM 1242 C ARG A 211 7.326 20.993 -76.380 1.00104.01 C ANISOU 1242 C ARG A 211 16885 10803 11828 -1669 1278 980 C ATOM 1243 O ARG A 211 6.558 21.742 -75.769 1.00115.31 O ANISOU 1243 O ARG A 211 18319 12125 13367 -1625 1073 1043 O ATOM 1244 CB ARG A 211 7.424 19.497 -74.321 1.00 96.50 C ANISOU 1244 CB ARG A 211 15500 9881 11285 -1495 1274 740 C ATOM 1245 CG ARG A 211 6.011 18.957 -74.440 1.00 98.31 C ANISOU 1245 CG ARG A 211 15808 10087 11457 -1391 1059 677 C ATOM 1246 CD ARG A 211 6.018 17.457 -74.621 1.00101.47 C ANISOU 1246 CD ARG A 211 16164 10568 11823 -1330 1141 512 C ATOM 1247 NE ARG A 211 5.157 17.079 -75.742 1.00112.69 N ANISOU 1247 NE ARG A 211 17802 12014 13002 -1330 1048 490 N ATOM 1248 CZ ARG A 211 5.310 15.991 -76.505 1.00112.31 C ANISOU 1248 CZ ARG A 211 17837 12036 12801 -1329 1159 374 C ATOM 1249 NH1 ARG A 211 6.304 15.132 -76.293 1.00110.12 N ANISOU 1249 NH1 ARG A 211 17441 11807 12592 -1307 1382 269 N ATOM 1250 NH2 ARG A 211 4.456 15.756 -77.499 1.00110.15 N ANISOU 1250 NH2 ARG A 211 17772 11781 12298 -1345 1042 361 N ATOM 1251 N GLN A 212 7.582 21.110 -77.694 1.00107.77 N ANISOU 1251 N GLN A 212 17574 11334 12038 -1756 1383 1042 N ATOM 1252 CA GLN A 212 6.933 22.064 -78.614 1.00104.31 C ANISOU 1252 CA GLN A 212 17407 10836 11391 -1809 1249 1198 C ATOM 1253 C GLN A 212 7.412 23.507 -78.406 1.00105.36 C ANISOU 1253 C GLN A 212 17584 10863 11586 -1917 1258 1377 C ATOM 1254 O GLN A 212 6.603 24.430 -78.257 1.00102.42 O ANISOU 1254 O GLN A 212 17318 10364 11234 -1888 1047 1487 O ATOM 1255 CB GLN A 212 5.399 21.970 -78.519 1.00103.20 C ANISOU 1255 CB GLN A 212 17332 10641 11239 -1686 949 1181 C ATOM 1256 CG GLN A 212 4.884 20.563 -78.241 1.00105.73 C ANISOU 1256 CG GLN A 212 17536 11033 11602 -1579 909 989 C ATOM 1257 CD GLN A 212 3.607 20.220 -78.983 1.00111.13 C ANISOU 1257 CD GLN A 212 18385 11738 12101 -1528 695 974 C ATOM 1258 OE1 GLN A 212 3.481 20.498 -80.178 1.00110.26 O ANISOU 1258 OE1 GLN A 212 18513 11660 11721 -1594 686 1055 O ATOM 1259 NE2 GLN A 212 2.661 19.574 -78.283 1.00102.70 N ANISOU 1259 NE2 GLN A 212 17188 10665 11170 -1419 523 871 N ATOM 1260 N GLY A 213 8.738 23.699 -78.395 1.00106.52 N ANISOU 1260 N GLY A 213 17646 11058 11768 -2043 1504 1406 N ATOM 1261 CA GLY A 213 9.339 24.991 -78.071 1.00108.62 C ANISOU 1261 CA GLY A 213 17923 11224 12124 -2172 1533 1559 C ATOM 1262 C GLY A 213 9.354 25.291 -76.569 1.00106.98 C ANISOU 1262 C GLY A 213 17494 10924 12229 -2125 1436 1519 C ATOM 1263 O GLY A 213 10.367 25.768 -76.052 1.00109.66 O ANISOU 1263 O GLY A 213 17708 11256 12701 -2242 1563 1557 O ATOM 1264 N SER A 214 8.241 24.968 -75.884 1.00102.84 N ANISOU 1264 N SER A 214 16918 10344 11814 -1962 1216 1437 N ATOM 1265 CA SER A 214 8.007 25.197 -74.440 1.00 88.81 C ANISOU 1265 CA SER A 214 14957 8478 10310 -1888 1094 1386 C ATOM 1266 C SER A 214 8.702 24.149 -73.527 1.00 86.72 C ANISOU 1266 C SER A 214 14399 8321 10229 -1849 1217 1229 C ATOM 1267 O SER A 214 9.237 23.160 -74.004 1.00 86.88 O ANISOU 1267 O SER A 214 14358 8477 10174 -1849 1383 1148 O ATOM 1268 CB SER A 214 6.493 25.195 -74.183 1.00 83.89 C ANISOU 1268 CB SER A 214 14396 7776 9705 -1722 827 1365 C ATOM 1269 OG SER A 214 6.120 24.123 -73.342 1.00 87.43 O ANISOU 1269 OG SER A 214 14637 8287 10297 -1595 784 1202 O ATOM 1270 N ILE A 215 8.641 24.361 -72.207 1.00 78.81 N ANISOU 1270 N ILE A 215 13232 7253 9461 -1803 1128 1187 N ATOM 1271 CA ILE A 215 9.385 23.555 -71.224 1.00 70.56 C ANISOU 1271 CA ILE A 215 11910 6295 8603 -1778 1229 1067 C ATOM 1272 C ILE A 215 8.477 22.869 -70.191 1.00 68.44 C ANISOU 1272 C ILE A 215 11515 6009 8481 -1609 1070 946 C ATOM 1273 O ILE A 215 7.716 23.549 -69.449 1.00 59.99 O ANISOU 1273 O ILE A 215 10466 4818 7509 -1555 891 969 O ATOM 1274 CB ILE A 215 10.496 24.368 -70.532 1.00 69.48 C ANISOU 1274 CB ILE A 215 11657 6131 8611 -1921 1315 1127 C ATOM 1275 CG1 ILE A 215 11.404 24.978 -71.586 1.00 69.47 C ANISOU 1275 CG1 ILE A 215 11771 6163 8463 -2102 1489 1250 C ATOM 1276 CG2 ILE A 215 11.285 23.513 -69.544 1.00 67.26 C ANISOU 1276 CG2 ILE A 215 11084 5958 8514 -1889 1408 1013 C ATOM 1277 CD1 ILE A 215 12.501 25.828 -70.990 1.00 70.52 C ANISOU 1277 CD1 ILE A 215 11795 6271 8729 -2275 1570 1320 C ATOM 1278 N ASP A 216 8.537 21.519 -70.202 1.00 63.30 N ANISOU 1278 N ASP A 216 10747 5471 7832 -1526 1145 820 N ATOM 1279 CA ASP A 216 7.867 20.631 -69.271 1.00 63.68 C ANISOU 1279 CA ASP A 216 10655 5527 8013 -1384 1041 699 C ATOM 1280 C ASP A 216 8.900 20.357 -68.152 1.00 63.25 C ANISOU 1280 C ASP A 216 10355 5520 8159 -1399 1140 649 C ATOM 1281 O ASP A 216 10.107 20.206 -68.426 1.00 66.08 O ANISOU 1281 O ASP A 216 10630 5965 8515 -1482 1331 661 O ATOM 1282 CB ASP A 216 7.445 19.315 -69.992 1.00 68.28 C ANISOU 1282 CB ASP A 216 11276 6194 8475 -1305 1077 597 C ATOM 1283 CG ASP A 216 6.405 18.464 -69.220 1.00 72.87 C ANISOU 1283 CG ASP A 216 11771 6762 9156 -1168 928 490 C ATOM 1284 OD1 ASP A 216 5.945 18.832 -68.101 1.00 79.70 O ANISOU 1284 OD1 ASP A 216 12538 7565 10180 -1116 799 489 O ATOM 1285 OD2 ASP A 216 6.055 17.364 -69.738 1.00 88.79 O ANISOU 1285 OD2 ASP A 216 13821 8832 11085 -1116 949 399 O ATOM 1286 N CYS A 217 8.414 20.347 -66.898 1.00 60.15 N ANISOU 1286 N CYS A 217 9846 5076 7934 -1320 1006 602 N ATOM 1287 CA CYS A 217 9.166 19.901 -65.745 1.00 56.30 C ANISOU 1287 CA CYS A 217 9126 4638 7628 -1305 1058 542 C ATOM 1288 C CYS A 217 8.516 18.556 -65.531 1.00 51.71 C ANISOU 1288 C CYS A 217 8483 4100 7065 -1164 1027 427 C ATOM 1289 O CYS A 217 7.361 18.473 -65.102 1.00 48.33 O ANISOU 1289 O CYS A 217 8087 3614 6661 -1076 866 396 O ATOM 1290 CB CYS A 217 9.025 20.828 -64.503 1.00 53.61 C ANISOU 1290 CB CYS A 217 8729 4204 7437 -1322 928 567 C ATOM 1291 SG CYS A 217 9.581 20.094 -62.909 1.00 53.64 S ANISOU 1291 SG CYS A 217 8459 4270 7652 -1264 930 476 S ATOM 1292 N THR A 218 9.262 17.496 -65.839 1.00 53.90 N ANISOU 1292 N THR A 218 8670 4477 7332 -1142 1187 364 N ATOM 1293 CA THR A 218 8.647 16.151 -65.983 1.00 55.24 C ANISOU 1293 CA THR A 218 8842 4673 7475 -1024 1179 256 C ATOM 1294 C THR A 218 9.503 15.076 -65.338 1.00 52.39 C ANISOU 1294 C THR A 218 8283 4383 7239 -960 1299 181 C ATOM 1295 O THR A 218 10.497 15.378 -64.724 1.00 52.04 O ANISOU 1295 O THR A 218 8085 4382 7308 -1000 1368 213 O ATOM 1296 CB THR A 218 8.340 15.889 -67.502 1.00 57.92 C ANISOU 1296 CB THR A 218 9386 5032 7591 -1046 1237 252 C ATOM 1297 OG1 THR A 218 7.319 14.915 -67.610 1.00 61.66 O ANISOU 1297 OG1 THR A 218 9914 5490 8024 -956 1146 162 O ATOM 1298 CG2 THR A 218 9.562 15.486 -68.286 1.00 59.65 C ANISOU 1298 CG2 THR A 218 9586 5342 7736 -1090 1474 243 C ATOM 1299 N LEU A 219 9.038 13.826 -65.401 1.00 52.82 N ANISOU 1299 N LEU A 219 8345 4443 7282 -859 1302 82 N ATOM 1300 CA LEU A 219 9.719 12.650 -64.816 1.00 50.28 C ANISOU 1300 CA LEU A 219 7859 4168 7076 -768 1406 7 C ATOM 1301 C LEU A 219 10.201 11.807 -65.998 1.00 49.50 C ANISOU 1301 C LEU A 219 7844 4116 6847 -746 1588 -51 C ATOM 1302 O LEU A 219 9.476 11.628 -66.959 1.00 49.80 O ANISOU 1302 O LEU A 219 8073 4127 6722 -758 1563 -82 O ATOM 1303 CB LEU A 219 8.775 11.857 -63.972 1.00 48.94 C ANISOU 1303 CB LEU A 219 7659 3944 6990 -673 1273 -60 C ATOM 1304 CG LEU A 219 8.242 12.544 -62.748 1.00 50.84 C ANISOU 1304 CG LEU A 219 7820 4144 7352 -675 1107 -21 C ATOM 1305 CD1 LEU A 219 7.274 11.636 -61.971 1.00 51.59 C ANISOU 1305 CD1 LEU A 219 7887 4198 7516 -584 995 -88 C ATOM 1306 CD2 LEU A 219 9.373 12.985 -61.844 1.00 51.67 C ANISOU 1306 CD2 LEU A 219 7742 4295 7594 -702 1158 25 C ATOM 1307 N THR A 220 11.483 11.455 -66.002 1.00 49.83 N ANISOU 1307 N THR A 220 7747 4239 6947 -726 1776 -56 N ATOM 1308 CA THR A 220 11.993 10.483 -66.968 1.00 53.98 C ANISOU 1308 CA THR A 220 8332 4806 7370 -669 1970 -132 C ATOM 1309 C THR A 220 12.109 9.114 -66.271 1.00 49.56 C ANISOU 1309 C THR A 220 7666 4225 6938 -519 1998 -226 C ATOM 1310 O THR A 220 12.336 9.009 -65.069 1.00 50.83 O ANISOU 1310 O THR A 220 7646 4388 7278 -471 1934 -208 O ATOM 1311 CB THR A 220 13.295 10.929 -67.587 1.00 60.10 C ANISOU 1311 CB THR A 220 9036 5691 8110 -730 2184 -77 C ATOM 1312 OG1 THR A 220 14.148 11.340 -66.528 1.00 69.26 O ANISOU 1312 OG1 THR A 220 9949 6906 9460 -744 2186 -14 O ATOM 1313 CG2 THR A 220 13.050 12.132 -68.481 1.00 63.55 C ANISOU 1313 CG2 THR A 220 9640 6126 8380 -879 2163 13 C ATOM 1314 N PHE A 221 11.850 8.050 -67.012 1.00 48.62 N ANISOU 1314 N PHE A 221 7685 4073 6717 -449 2076 -330 N ATOM 1315 CA PHE A 221 11.707 6.730 -66.412 1.00 46.58 C ANISOU 1315 CA PHE A 221 7384 3753 6562 -313 2074 -422 C ATOM 1316 C PHE A 221 12.603 5.864 -67.128 1.00 47.93 C ANISOU 1316 C PHE A 221 7568 3957 6687 -225 2306 -495 C ATOM 1317 O PHE A 221 12.873 6.097 -68.282 1.00 48.28 O ANISOU 1317 O PHE A 221 7735 4045 6563 -275 2435 -507 O ATOM 1318 CB PHE A 221 10.304 6.252 -66.632 1.00 45.78 C ANISOU 1318 CB PHE A 221 7475 3548 6370 -325 1917 -491 C ATOM 1319 CG PHE A 221 9.320 6.982 -65.836 1.00 45.55 C ANISOU 1319 CG PHE A 221 7419 3486 6402 -384 1689 -428 C ATOM 1320 CD1 PHE A 221 9.077 6.629 -64.550 1.00 43.76 C ANISOU 1320 CD1 PHE A 221 7057 3223 6348 -325 1588 -424 C ATOM 1321 CD2 PHE A 221 8.667 8.115 -66.361 1.00 46.39 C ANISOU 1321 CD2 PHE A 221 7635 3600 6391 -496 1580 -363 C ATOM 1322 CE1 PHE A 221 8.146 7.347 -63.803 1.00 44.98 C ANISOU 1322 CE1 PHE A 221 7187 3352 6550 -374 1389 -370 C ATOM 1323 CE2 PHE A 221 7.754 8.810 -65.628 1.00 44.34 C ANISOU 1323 CE2 PHE A 221 7349 3307 6191 -531 1380 -308 C ATOM 1324 CZ PHE A 221 7.511 8.469 -64.325 1.00 43.50 C ANISOU 1324 CZ PHE A 221 7101 3172 6257 -471 1290 -313 C ATOM 1325 N SER A 222 12.990 4.754 -66.493 1.00 50.26 N ANISOU 1325 N SER A 222 7762 4217 7118 -80 2362 -553 N ATOM 1326 CA SER A 222 13.700 3.681 -67.211 1.00 53.47 C ANISOU 1326 CA SER A 222 8218 4620 7478 43 2587 -651 C ATOM 1327 C SER A 222 12.805 2.981 -68.260 1.00 53.45 C ANISOU 1327 C SER A 222 8516 4517 7277 30 2586 -774 C ATOM 1328 O SER A 222 11.575 3.123 -68.291 1.00 50.12 O ANISOU 1328 O SER A 222 8239 4021 6782 -57 2392 -787 O ATOM 1329 CB SER A 222 14.192 2.591 -66.260 1.00 56.86 C ANISOU 1329 CB SER A 222 8498 5006 8101 216 2624 -684 C ATOM 1330 OG SER A 222 14.507 3.096 -64.986 1.00 58.00 O ANISOU 1330 OG SER A 222 8402 5202 8433 214 2515 -580 O ATOM 1331 N HIS A 223 13.456 2.183 -69.076 1.00 56.02 N ANISOU 1331 N HIS A 223 8923 4841 7522 125 2806 -869 N ATOM 1332 CA HIS A 223 12.797 1.344 -70.041 1.00 61.46 C ANISOU 1332 CA HIS A 223 9897 5427 8027 130 2833 -1006 C ATOM 1333 C HIS A 223 12.120 0.127 -69.395 1.00 59.04 C ANISOU 1333 C HIS A 223 9655 4960 7818 216 2730 -1096 C ATOM 1334 O HIS A 223 12.564 -0.368 -68.365 1.00 58.37 O ANISOU 1334 O HIS A 223 9393 4847 7939 336 2735 -1072 O ATOM 1335 CB HIS A 223 13.807 0.970 -71.115 1.00 66.63 C ANISOU 1335 CB HIS A 223 10617 6140 8558 206 3126 -1079 C ATOM 1336 CG HIS A 223 14.355 2.172 -71.836 1.00 74.77 C ANISOU 1336 CG HIS A 223 11616 7326 9467 91 3224 -986 C ATOM 1337 ND1 HIS A 223 13.679 3.374 -71.885 1.00 74.83 N ANISOU 1337 ND1 HIS A 223 11658 7370 9404 -84 3043 -880 N ATOM 1338 CD2 HIS A 223 15.489 2.349 -72.558 1.00 80.79 C ANISOU 1338 CD2 HIS A 223 12327 8211 10161 122 3489 -980 C ATOM 1339 CE1 HIS A 223 14.376 4.238 -72.598 1.00 80.99 C ANISOU 1339 CE1 HIS A 223 12421 8276 10076 -163 3186 -808 C ATOM 1340 NE2 HIS A 223 15.473 3.639 -73.025 1.00 82.41 N ANISOU 1340 NE2 HIS A 223 12543 8517 10251 -48 3461 -866 N ATOM 1341 N PRO A 224 10.916 -0.273 -69.859 1.00 57.53 N ANISOU 1341 N PRO A 224 9706 4663 7491 134 2592 -1179 N ATOM 1342 CA PRO A 224 10.129 0.548 -70.784 1.00 55.35 C ANISOU 1342 CA PRO A 224 9603 4432 6998 -32 2490 -1164 C ATOM 1343 C PRO A 224 9.350 1.583 -70.014 1.00 50.10 C ANISOU 1343 C PRO A 224 8821 3802 6412 -140 2249 -1037 C ATOM 1344 O PRO A 224 8.822 1.304 -68.913 1.00 46.74 O ANISOU 1344 O PRO A 224 8292 3315 6152 -117 2101 -1015 O ATOM 1345 CB PRO A 224 9.221 -0.451 -71.462 1.00 58.19 C ANISOU 1345 CB PRO A 224 10240 4663 7208 -61 2435 -1311 C ATOM 1346 CG PRO A 224 9.131 -1.622 -70.497 1.00 58.85 C ANISOU 1346 CG PRO A 224 10269 4609 7481 52 2411 -1369 C ATOM 1347 CD PRO A 224 10.221 -1.505 -69.457 1.00 58.37 C ANISOU 1347 CD PRO A 224 9922 4603 7654 187 2509 -1279 C ATOM 1348 N THR A 225 9.323 2.817 -70.546 1.00 48.32 N ANISOU 1348 N THR A 225 8610 3677 6073 -251 2219 -945 N ATOM 1349 CA THR A 225 8.731 3.950 -69.833 1.00 46.29 C ANISOU 1349 CA THR A 225 8238 3455 5896 -337 2016 -817 C ATOM 1350 C THR A 225 7.294 3.710 -69.511 1.00 44.29 C ANISOU 1350 C THR A 225 8066 3122 5641 -388 1776 -842 C ATOM 1351 O THR A 225 6.836 4.080 -68.444 1.00 42.04 O ANISOU 1351 O THR A 225 7638 2828 5509 -392 1626 -774 O ATOM 1352 CB THR A 225 8.870 5.306 -70.614 1.00 46.73 C ANISOU 1352 CB THR A 225 8346 3606 5804 -453 2022 -715 C ATOM 1353 OG1 THR A 225 8.420 5.051 -71.945 1.00 49.15 O ANISOU 1353 OG1 THR A 225 8914 3904 5857 -511 2045 -788 O ATOM 1354 CG2 THR A 225 10.327 5.677 -70.716 1.00 47.73 C ANISOU 1354 CG2 THR A 225 8335 3829 5972 -422 2251 -664 C ATOM 1355 N TRP A 226 6.590 3.062 -70.440 1.00 46.05 N ANISOU 1355 N TRP A 226 8518 3292 5686 -431 1745 -945 N ATOM 1356 CA TRP A 226 5.178 2.767 -70.241 1.00 45.86 C ANISOU 1356 CA TRP A 226 8569 3205 5649 -497 1515 -974 C ATOM 1357 C TRP A 226 4.909 1.769 -69.085 1.00 45.90 C ANISOU 1357 C TRP A 226 8470 3115 5854 -427 1465 -1017 C ATOM 1358 O TRP A 226 3.794 1.741 -68.515 1.00 47.58 O ANISOU 1358 O TRP A 226 8655 3297 6124 -480 1266 -1000 O ATOM 1359 CB TRP A 226 4.493 2.313 -71.526 1.00 47.03 C ANISOU 1359 CB TRP A 226 8989 3327 5551 -580 1478 -1074 C ATOM 1360 CG TRP A 226 5.221 1.318 -72.263 1.00 49.04 C ANISOU 1360 CG TRP A 226 9392 3534 5707 -522 1687 -1205 C ATOM 1361 CD1 TRP A 226 6.007 1.549 -73.318 1.00 50.73 C ANISOU 1361 CD1 TRP A 226 9722 3808 5745 -521 1870 -1226 C ATOM 1362 CD2 TRP A 226 5.270 -0.096 -72.019 1.00 48.81 C ANISOU 1362 CD2 TRP A 226 9425 3379 5743 -449 1753 -1337 C ATOM 1363 NE1 TRP A 226 6.556 0.371 -73.767 1.00 52.10 N ANISOU 1363 NE1 TRP A 226 10023 3906 5867 -440 2056 -1373 N ATOM 1364 CE2 TRP A 226 6.126 -0.643 -72.960 1.00 51.21 C ANISOU 1364 CE2 TRP A 226 9880 3669 5908 -391 1983 -1441 C ATOM 1365 CE3 TRP A 226 4.698 -0.936 -71.069 1.00 47.93 C ANISOU 1365 CE3 TRP A 226 9255 3159 5796 -425 1648 -1372 C ATOM 1366 CZ2 TRP A 226 6.406 -2.026 -73.026 1.00 52.64 C ANISOU 1366 CZ2 TRP A 226 10177 3717 6108 -299 2108 -1590 C ATOM 1367 CZ3 TRP A 226 4.993 -2.346 -71.132 1.00 48.91 C ANISOU 1367 CZ3 TRP A 226 9499 3144 5940 -344 1770 -1513 C ATOM 1368 CH2 TRP A 226 5.833 -2.843 -72.068 1.00 51.15 C ANISOU 1368 CH2 TRP A 226 9939 3406 6092 -277 1992 -1618 C ATOM 1369 N TYR A 227 5.916 1.013 -68.647 1.00 44.45 N ANISOU 1369 N TYR A 227 8207 2891 5789 -304 1639 -1057 N ATOM 1370 CA TYR A 227 5.652 0.228 -67.457 1.00 42.36 C ANISOU 1370 CA TYR A 227 7837 2540 5717 -243 1574 -1067 C ATOM 1371 C TYR A 227 5.886 1.082 -66.260 1.00 40.11 C ANISOU 1371 C TYR A 227 7308 2324 5610 -219 1508 -936 C ATOM 1372 O TYR A 227 4.988 1.270 -65.368 1.00 38.00 O ANISOU 1372 O TYR A 227 6961 2043 5436 -259 1329 -888 O ATOM 1373 CB TYR A 227 6.496 -1.044 -67.499 1.00 43.63 C ANISOU 1373 CB TYR A 227 8044 2607 5926 -112 1764 -1167 C ATOM 1374 CG TYR A 227 6.315 -1.921 -66.316 1.00 42.84 C ANISOU 1374 CG TYR A 227 7856 2405 6015 -41 1711 -1168 C ATOM 1375 CD1 TYR A 227 6.908 -1.611 -65.096 1.00 41.81 C ANISOU 1375 CD1 TYR A 227 7485 2320 6083 41 1712 -1064 C ATOM 1376 CD2 TYR A 227 5.500 -3.059 -66.397 1.00 43.13 C ANISOU 1376 CD2 TYR A 227 8062 2298 6029 -71 1647 -1270 C ATOM 1377 CE1 TYR A 227 6.694 -2.422 -63.986 1.00 41.50 C ANISOU 1377 CE1 TYR A 227 7378 2186 6202 102 1654 -1055 C ATOM 1378 CE2 TYR A 227 5.265 -3.820 -65.314 1.00 42.44 C ANISOU 1378 CE2 TYR A 227 7906 2113 6106 -24 1592 -1257 C ATOM 1379 CZ TYR A 227 5.906 -3.554 -64.147 1.00 41.82 C ANISOU 1379 CZ TYR A 227 7599 2079 6212 73 1608 -1152 C ATOM 1380 OH TYR A 227 5.736 -4.387 -63.096 1.00 42.23 O ANISOU 1380 OH TYR A 227 7604 2029 6414 128 1565 -1135 O ATOM 1381 N TRP A 228 7.103 1.603 -66.138 1.00 40.40 N ANISOU 1381 N TRP A 228 7209 2439 5703 -156 1652 -878 N ATOM 1382 CA TRP A 228 7.476 2.236 -64.862 1.00 39.44 C ANISOU 1382 CA TRP A 228 6849 2369 5766 -124 1599 -768 C ATOM 1383 C TRP A 228 6.683 3.527 -64.591 1.00 38.40 C ANISOU 1383 C TRP A 228 6678 2292 5618 -233 1419 -675 C ATOM 1384 O TRP A 228 6.385 3.859 -63.434 1.00 36.69 O ANISOU 1384 O TRP A 228 6323 2080 5537 -227 1304 -613 O ATOM 1385 CB TRP A 228 9.022 2.508 -64.801 1.00 40.48 C ANISOU 1385 CB TRP A 228 6826 2586 5967 -45 1790 -725 C ATOM 1386 CG TRP A 228 9.785 1.265 -64.949 1.00 42.29 C ANISOU 1386 CG TRP A 228 7070 2762 6236 90 1963 -808 C ATOM 1387 CD1 TRP A 228 10.459 0.870 -65.998 1.00 44.26 C ANISOU 1387 CD1 TRP A 228 7418 3021 6378 136 2156 -879 C ATOM 1388 CD2 TRP A 228 9.851 0.213 -63.993 1.00 42.08 C ANISOU 1388 CD2 TRP A 228 6977 2648 6365 204 1951 -830 C ATOM 1389 NE1 TRP A 228 10.962 -0.379 -65.767 1.00 45.97 N ANISOU 1389 NE1 TRP A 228 7632 3154 6680 286 2271 -952 N ATOM 1390 CE2 TRP A 228 10.612 -0.761 -64.510 1.00 44.26 C ANISOU 1390 CE2 TRP A 228 7310 2877 6631 327 2140 -912 C ATOM 1391 CE3 TRP A 228 9.369 0.067 -62.696 1.00 42.01 C ANISOU 1391 CE3 TRP A 228 6860 2600 6502 216 1801 -777 C ATOM 1392 CZ2 TRP A 228 10.878 -1.910 -63.843 1.00 45.52 C ANISOU 1392 CZ2 TRP A 228 7440 2935 6921 466 2177 -945 C ATOM 1393 CZ3 TRP A 228 9.661 -1.062 -62.021 1.00 41.92 C ANISOU 1393 CZ3 TRP A 228 6814 2499 6613 342 1840 -802 C ATOM 1394 CH2 TRP A 228 10.368 -2.041 -62.598 1.00 43.71 C ANISOU 1394 CH2 TRP A 228 7115 2664 6828 465 2017 -883 C ATOM 1395 N GLU A 229 6.324 4.250 -65.651 1.00 40.24 N ANISOU 1395 N GLU A 229 7045 2562 5680 -324 1395 -666 N ATOM 1396 CA GLU A 229 5.505 5.452 -65.452 1.00 42.03 C ANISOU 1396 CA GLU A 229 7255 2825 5891 -409 1219 -578 C ATOM 1397 C GLU A 229 4.108 5.099 -64.897 1.00 39.88 C ANISOU 1397 C GLU A 229 6998 2499 5656 -431 1024 -598 C ATOM 1398 O GLU A 229 3.601 5.728 -63.971 1.00 37.73 O ANISOU 1398 O GLU A 229 6611 2240 5484 -437 898 -531 O ATOM 1399 CB GLU A 229 5.395 6.239 -66.747 1.00 45.73 C ANISOU 1399 CB GLU A 229 7879 3336 6159 -494 1228 -554 C ATOM 1400 CG GLU A 229 4.499 7.390 -66.534 1.00 52.68 C ANISOU 1400 CG GLU A 229 8752 4232 7030 -557 1042 -464 C ATOM 1401 CD GLU A 229 4.474 8.408 -67.682 1.00 61.42 C ANISOU 1401 CD GLU A 229 10001 5381 7956 -639 1038 -403 C ATOM 1402 OE1 GLU A 229 4.756 8.047 -68.856 1.00 62.83 O ANISOU 1402 OE1 GLU A 229 10336 5575 7962 -666 1143 -452 O ATOM 1403 OE2 GLU A 229 4.122 9.565 -67.344 1.00 67.01 O ANISOU 1403 OE2 GLU A 229 10667 6098 8696 -670 924 -304 O ATOM 1404 N ASN A 230 3.495 4.045 -65.419 1.00 40.67 N ANISOU 1404 N ASN A 230 7234 2539 5680 -445 1006 -695 N ATOM 1405 CA ASN A 230 2.200 3.639 -64.892 1.00 41.81 C ANISOU 1405 CA ASN A 230 7376 2644 5868 -481 831 -712 C ATOM 1406 C ASN A 230 2.253 3.004 -63.496 1.00 43.79 C ANISOU 1406 C ASN A 230 7476 2849 6312 -414 823 -705 C ATOM 1407 O ASN A 230 1.378 3.246 -62.617 1.00 41.40 O ANISOU 1407 O ASN A 230 7081 2556 6095 -434 682 -660 O ATOM 1408 CB ASN A 230 1.498 2.787 -65.919 1.00 43.60 C ANISOU 1408 CB ASN A 230 7801 2822 5942 -545 797 -814 C ATOM 1409 CG ASN A 230 1.112 3.612 -67.113 1.00 44.89 C ANISOU 1409 CG ASN A 230 8098 3048 5910 -626 736 -793 C ATOM 1410 OD1 ASN A 230 0.513 4.629 -66.946 1.00 44.72 O ANISOU 1410 OD1 ASN A 230 8018 3081 5892 -657 603 -705 O ATOM 1411 ND2 ASN A 230 1.567 3.255 -68.272 1.00 46.18 N ANISOU 1411 ND2 ASN A 230 8436 3204 5908 -645 847 -863 N ATOM 1412 N LEU A 231 3.322 2.256 -63.234 1.00 44.74 N ANISOU 1412 N LEU A 231 7563 2930 6507 -326 980 -737 N ATOM 1413 CA LEU A 231 3.550 1.802 -61.878 1.00 44.23 C ANISOU 1413 CA LEU A 231 7349 2835 6622 -253 976 -706 C ATOM 1414 C LEU A 231 3.648 2.984 -60.908 1.00 41.02 C ANISOU 1414 C LEU A 231 6767 2509 6310 -251 904 -598 C ATOM 1415 O LEU A 231 3.070 3.006 -59.798 1.00 40.42 O ANISOU 1415 O LEU A 231 6593 2429 6335 -248 801 -559 O ATOM 1416 CB LEU A 231 4.844 1.012 -61.836 1.00 47.92 C ANISOU 1416 CB LEU A 231 7791 3267 7149 -140 1160 -739 C ATOM 1417 CG LEU A 231 5.082 0.371 -60.452 1.00 53.56 C ANISOU 1417 CG LEU A 231 8371 3938 8042 -55 1150 -704 C ATOM 1418 CD1 LEU A 231 3.974 -0.642 -60.089 1.00 51.87 C ANISOU 1418 CD1 LEU A 231 8243 3618 7848 -91 1052 -749 C ATOM 1419 CD2 LEU A 231 6.427 -0.323 -60.509 1.00 54.09 C ANISOU 1419 CD2 LEU A 231 8403 3983 8168 76 1331 -726 C ATOM 1420 N LEU A 232 4.396 4.013 -61.302 1.00 40.60 N ANISOU 1420 N LEU A 232 6679 2527 6218 -260 962 -549 N ATOM 1421 CA LEU A 232 4.493 5.156 -60.406 1.00 38.37 C ANISOU 1421 CA LEU A 232 6256 2304 6019 -270 890 -456 C ATOM 1422 C LEU A 232 3.088 5.674 -60.132 1.00 36.88 C ANISOU 1422 C LEU A 232 6087 2113 5812 -326 711 -434 C ATOM 1423 O LEU A 232 2.725 5.912 -58.979 1.00 38.68 O ANISOU 1423 O LEU A 232 6206 2348 6143 -309 629 -395 O ATOM 1424 CB LEU A 232 5.433 6.232 -60.913 1.00 41.62 C ANISOU 1424 CB LEU A 232 6643 2781 6388 -298 969 -402 C ATOM 1425 CG LEU A 232 5.407 7.598 -60.154 1.00 42.17 C ANISOU 1425 CG LEU A 232 6612 2892 6517 -335 876 -313 C ATOM 1426 CD1 LEU A 232 5.920 7.344 -58.757 1.00 47.21 C ANISOU 1426 CD1 LEU A 232 7083 3542 7313 -276 873 -289 C ATOM 1427 CD2 LEU A 232 6.261 8.709 -60.729 1.00 43.02 C ANISOU 1427 CD2 LEU A 232 6720 3051 6575 -391 947 -254 C ATOM 1428 N LYS A 233 2.272 5.886 -61.163 1.00 36.70 N ANISOU 1428 N LYS A 233 6199 2090 5656 -390 646 -456 N ATOM 1429 CA LYS A 233 0.905 6.435 -60.955 1.00 35.92 C ANISOU 1429 CA LYS A 233 6098 2004 5543 -431 471 -427 C ATOM 1430 C LYS A 233 0.046 5.590 -60.060 1.00 35.27 C ANISOU 1430 C LYS A 233 5955 1895 5550 -422 395 -453 C ATOM 1431 O LYS A 233 -0.655 6.050 -59.147 1.00 32.94 O ANISOU 1431 O LYS A 233 5562 1624 5331 -414 296 -410 O ATOM 1432 CB LYS A 233 0.222 6.603 -62.285 1.00 36.70 C ANISOU 1432 CB LYS A 233 6353 2114 5477 -497 411 -447 C ATOM 1433 CG LYS A 233 0.790 7.827 -62.972 1.00 37.68 C ANISOU 1433 CG LYS A 233 6525 2274 5518 -517 443 -383 C ATOM 1434 CD LYS A 233 0.268 7.951 -64.353 1.00 40.29 C ANISOU 1434 CD LYS A 233 7027 2618 5664 -579 396 -397 C ATOM 1435 CE LYS A 233 0.972 9.151 -65.010 1.00 43.48 C ANISOU 1435 CE LYS A 233 7488 3050 5984 -602 450 -320 C ATOM 1436 NZ LYS A 233 0.260 9.334 -66.285 1.00 47.21 N ANISOU 1436 NZ LYS A 233 8132 3539 6265 -662 368 -319 N ATOM 1437 N ILE A 234 0.102 4.282 -60.321 1.00 37.75 N ANISOU 1437 N ILE A 234 6338 2151 5855 -424 452 -528 N ATOM 1438 CA ILE A 234 -0.531 3.321 -59.474 1.00 37.14 C ANISOU 1438 CA ILE A 234 6215 2030 5865 -424 408 -551 C ATOM 1439 C ILE A 234 -0.093 3.402 -58.059 1.00 36.11 C ANISOU 1439 C ILE A 234 5935 1907 5878 -358 428 -497 C ATOM 1440 O ILE A 234 -0.956 3.361 -57.157 1.00 36.88 O ANISOU 1440 O ILE A 234 5955 2017 6041 -371 338 -471 O ATOM 1441 CB ILE A 234 -0.260 1.900 -59.996 1.00 41.60 C ANISOU 1441 CB ILE A 234 6903 2504 6401 -427 494 -641 C ATOM 1442 CG1 ILE A 234 -1.070 1.723 -61.212 1.00 45.88 C ANISOU 1442 CG1 ILE A 234 7595 3040 6796 -520 427 -701 C ATOM 1443 CG2 ILE A 234 -0.593 0.827 -58.948 1.00 42.05 C ANISOU 1443 CG2 ILE A 234 6911 2492 6573 -415 482 -649 C ATOM 1444 CD1 ILE A 234 -2.471 2.176 -61.019 1.00 51.75 C ANISOU 1444 CD1 ILE A 234 8289 3841 7534 -594 251 -666 C ATOM 1445 N CYS A 235 1.222 3.457 -57.812 1.00 37.55 N ANISOU 1445 N CYS A 235 6068 2089 6110 -289 545 -479 N ATOM 1446 CA CYS A 235 1.678 3.478 -56.443 1.00 38.10 C ANISOU 1446 CA CYS A 235 5998 2172 6307 -230 551 -427 C ATOM 1447 C CYS A 235 1.230 4.702 -55.740 1.00 41.38 C ANISOU 1447 C CYS A 235 6323 2652 6746 -246 455 -366 C ATOM 1448 O CYS A 235 0.940 4.683 -54.521 1.00 39.94 O ANISOU 1448 O CYS A 235 6048 2482 6645 -224 407 -332 O ATOM 1449 CB CYS A 235 3.202 3.305 -56.328 1.00 42.32 C ANISOU 1449 CB CYS A 235 6477 2711 6893 -153 683 -415 C ATOM 1450 SG CYS A 235 3.631 1.551 -56.720 1.00 56.05 S ANISOU 1450 SG CYS A 235 8311 4342 8646 -90 799 -489 S ATOM 1451 N VAL A 236 1.270 5.842 -56.450 1.00 39.11 N ANISOU 1451 N VAL A 236 6069 2404 6388 -278 435 -345 N ATOM 1452 CA VAL A 236 0.875 7.057 -55.816 1.00 34.16 C ANISOU 1452 CA VAL A 236 5378 1818 5785 -283 349 -292 C ATOM 1453 C VAL A 236 -0.578 6.933 -55.472 1.00 32.76 C ANISOU 1453 C VAL A 236 5191 1646 5610 -300 235 -298 C ATOM 1454 O VAL A 236 -0.956 7.281 -54.390 1.00 39.74 O ANISOU 1454 O VAL A 236 5988 2552 6558 -276 187 -270 O ATOM 1455 CB VAL A 236 1.095 8.254 -56.732 1.00 35.06 C ANISOU 1455 CB VAL A 236 5555 1951 5816 -317 343 -264 C ATOM 1456 CG1 VAL A 236 0.456 9.486 -56.132 1.00 33.27 C ANISOU 1456 CG1 VAL A 236 5290 1741 5610 -315 240 -217 C ATOM 1457 CG2 VAL A 236 2.568 8.452 -56.874 1.00 36.44 C ANISOU 1457 CG2 VAL A 236 5701 2137 6005 -311 462 -247 C ATOM 1458 N PHE A 237 -1.407 6.464 -56.399 1.00 32.69 N ANISOU 1458 N PHE A 237 5268 1627 5525 -346 192 -335 N ATOM 1459 CA PHE A 237 -2.795 6.317 -56.136 1.00 34.97 C ANISOU 1459 CA PHE A 237 5527 1939 5821 -373 83 -337 C ATOM 1460 C PHE A 237 -3.125 5.414 -54.896 1.00 40.91 C ANISOU 1460 C PHE A 237 6192 2681 6671 -362 88 -338 C ATOM 1461 O PHE A 237 -3.979 5.751 -54.085 1.00 41.30 O ANISOU 1461 O PHE A 237 6154 2774 6764 -354 21 -310 O ATOM 1462 CB PHE A 237 -3.455 5.840 -57.376 1.00 35.47 C ANISOU 1462 CB PHE A 237 5699 1996 5782 -439 37 -380 C ATOM 1463 CG PHE A 237 -4.941 5.565 -57.214 1.00 38.73 C ANISOU 1463 CG PHE A 237 6066 2448 6203 -485 -84 -383 C ATOM 1464 CD1 PHE A 237 -5.824 6.578 -56.933 1.00 41.68 C ANISOU 1464 CD1 PHE A 237 6360 2889 6590 -461 -185 -334 C ATOM 1465 CD2 PHE A 237 -5.479 4.298 -57.409 1.00 42.47 C ANISOU 1465 CD2 PHE A 237 6578 2890 6669 -557 -98 -436 C ATOM 1466 CE1 PHE A 237 -7.194 6.374 -56.841 1.00 42.96 C ANISOU 1466 CE1 PHE A 237 6454 3108 6761 -500 -294 -331 C ATOM 1467 CE2 PHE A 237 -6.848 4.069 -57.322 1.00 40.32 C ANISOU 1467 CE2 PHE A 237 6248 2669 6403 -620 -212 -434 C ATOM 1468 CZ PHE A 237 -7.716 5.095 -57.049 1.00 42.90 C ANISOU 1468 CZ PHE A 237 6469 3084 6746 -590 -310 -379 C ATOM 1469 N AILE A 238 -2.390 4.309 -54.722 0.54 41.83 N ANISOU 1469 N AILE A 238 6334 2739 6822 -352 176 -365 N ATOM 1470 N BILE A 238 -2.405 4.293 -54.744 0.46 43.93 N ANISOU 1470 N BILE A 238 6602 3004 7087 -353 175 -366 N ATOM 1471 CA AILE A 238 -2.667 3.418 -53.599 0.54 41.77 C ANISOU 1471 CA AILE A 238 6266 2709 6897 -346 181 -354 C ATOM 1472 CA BILE A 238 -2.600 3.406 -53.594 0.46 45.33 C ANISOU 1472 CA BILE A 238 6717 3157 7349 -343 186 -354 C ATOM 1473 C AILE A 238 -2.084 3.854 -52.222 0.54 40.36 C ANISOU 1473 C AILE A 238 5978 2560 6798 -280 203 -299 C ATOM 1474 C BILE A 238 -2.147 3.997 -52.256 0.46 42.57 C ANISOU 1474 C BILE A 238 6255 2847 7073 -281 196 -298 C ATOM 1475 O AILE A 238 -2.754 3.748 -51.211 0.54 45.96 O ANISOU 1475 O AILE A 238 6617 3295 7550 -282 166 -272 O ATOM 1476 O BILE A 238 -2.943 4.113 -51.321 0.46 45.94 O ANISOU 1476 O BILE A 238 6608 3312 7534 -286 145 -271 O ATOM 1477 CB AILE A 238 -2.403 1.946 -53.957 0.54 45.92 C ANISOU 1477 CB AILE A 238 6883 3140 7425 -366 244 -403 C ATOM 1478 CB BILE A 238 -1.930 2.053 -53.797 0.46 53.83 C ANISOU 1478 CB BILE A 238 7869 4140 8442 -335 274 -393 C ATOM 1479 CG1AILE A 238 -0.894 1.689 -54.135 0.54 46.46 C ANISOU 1479 CG1AILE A 238 6979 3162 7511 -289 364 -411 C ATOM 1480 CG1BILE A 238 -2.823 1.196 -54.702 0.46 55.76 C ANISOU 1480 CG1BILE A 238 8223 4336 8627 -424 237 -454 C ATOM 1481 CG2AILE A 238 -3.240 1.554 -55.179 0.54 46.85 C ANISOU 1481 CG2AILE A 238 7110 3236 7453 -456 194 -464 C ATOM 1482 CG2BILE A 238 -1.702 1.364 -52.449 0.46 55.50 C ANISOU 1482 CG2BILE A 238 8012 4324 8749 -294 302 -352 C ATOM 1483 CD1AILE A 238 -0.581 0.479 -54.993 0.54 44.42 C ANISOU 1483 CD1AILE A 238 6855 2804 7220 -296 438 -481 C ATOM 1484 CD1BILE A 238 -2.055 0.361 -55.687 0.46 58.60 C ANISOU 1484 CD1BILE A 238 8722 4605 8938 -416 328 -522 C ATOM 1485 N PHE A 239 -0.896 4.445 -52.201 1.00 38.22 N ANISOU 1485 N PHE A 239 5689 2297 6536 -231 257 -282 N ATOM 1486 CA PHE A 239 -0.335 4.917 -51.011 1.00 38.32 C ANISOU 1486 CA PHE A 239 5610 2344 6606 -185 261 -237 C ATOM 1487 C PHE A 239 -0.807 6.293 -50.589 1.00 41.75 C ANISOU 1487 C PHE A 239 5999 2835 7028 -186 192 -213 C ATOM 1488 O PHE A 239 -0.755 6.596 -49.418 1.00 39.53 O ANISOU 1488 O PHE A 239 5651 2583 6785 -160 175 -186 O ATOM 1489 CB PHE A 239 1.170 4.971 -51.131 1.00 43.45 C ANISOU 1489 CB PHE A 239 6242 2989 7279 -143 341 -225 C ATOM 1490 CG PHE A 239 1.811 3.651 -50.943 1.00 46.45 C ANISOU 1490 CG PHE A 239 6626 3315 7706 -98 412 -229 C ATOM 1491 CD1 PHE A 239 1.913 3.095 -49.667 1.00 52.63 C ANISOU 1491 CD1 PHE A 239 7348 4097 8554 -60 400 -188 C ATOM 1492 CD2 PHE A 239 2.312 2.965 -52.007 1.00 51.43 C ANISOU 1492 CD2 PHE A 239 7335 3895 8313 -85 492 -272 C ATOM 1493 CE1 PHE A 239 2.471 1.854 -49.481 1.00 46.34 C ANISOU 1493 CE1 PHE A 239 6567 3236 7806 -6 460 -181 C ATOM 1494 CE2 PHE A 239 2.906 1.723 -51.822 1.00 57.02 C ANISOU 1494 CE2 PHE A 239 8057 4536 9072 -24 563 -277 C ATOM 1495 CZ PHE A 239 2.985 1.194 -50.559 1.00 51.16 C ANISOU 1495 CZ PHE A 239 7252 3784 8403 18 542 -227 C ATOM 1496 N ALA A 240 -1.192 7.160 -51.532 1.00 38.06 N ANISOU 1496 N ALA A 240 5581 2377 6501 -209 155 -223 N ATOM 1497 CA ALA A 240 -1.640 8.498 -51.145 1.00 37.10 C ANISOU 1497 CA ALA A 240 5435 2289 6374 -194 91 -201 C ATOM 1498 C ALA A 240 -3.136 8.551 -51.001 1.00 35.54 C ANISOU 1498 C ALA A 240 5213 2121 6168 -194 16 -205 C ATOM 1499 O ALA A 240 -3.656 9.373 -50.254 1.00 39.99 O ANISOU 1499 O ALA A 240 5730 2714 6748 -158 -25 -190 O ATOM 1500 CB ALA A 240 -1.165 9.566 -52.122 1.00 40.81 C ANISOU 1500 CB ALA A 240 5972 2745 6791 -209 90 -191 C ATOM 1501 N PHE A 241 -3.866 7.631 -51.628 1.00 34.46 N ANISOU 1501 N PHE A 241 5099 1983 6012 -236 -2 -227 N ATOM 1502 CA PHE A 241 -5.294 7.711 -51.579 1.00 34.21 C ANISOU 1502 CA PHE A 241 5021 2000 5976 -246 -80 -225 C ATOM 1503 C PHE A 241 -5.961 6.444 -50.988 1.00 36.76 C ANISOU 1503 C PHE A 241 5294 2334 6339 -289 -72 -233 C ATOM 1504 O PHE A 241 -6.633 6.490 -49.964 1.00 37.10 O ANISOU 1504 O PHE A 241 5248 2425 6422 -272 -83 -213 O ATOM 1505 CB PHE A 241 -5.829 8.021 -52.973 1.00 35.97 C ANISOU 1505 CB PHE A 241 5312 2229 6126 -278 -145 -235 C ATOM 1506 CG PHE A 241 -7.282 8.293 -52.963 1.00 36.89 C ANISOU 1506 CG PHE A 241 5358 2413 6244 -276 -240 -222 C ATOM 1507 CD1 PHE A 241 -7.771 9.426 -52.314 1.00 38.26 C ANISOU 1507 CD1 PHE A 241 5464 2626 6446 -196 -276 -193 C ATOM 1508 CD2 PHE A 241 -8.176 7.361 -53.439 1.00 42.55 C ANISOU 1508 CD2 PHE A 241 6062 3159 6945 -350 -289 -242 C ATOM 1509 CE1 PHE A 241 -9.141 9.641 -52.229 1.00 41.42 C ANISOU 1509 CE1 PHE A 241 5773 3105 6862 -176 -354 -178 C ATOM 1510 CE2 PHE A 241 -9.559 7.579 -53.358 1.00 47.02 C ANISOU 1510 CE2 PHE A 241 6527 3812 7526 -352 -379 -224 C ATOM 1511 CZ PHE A 241 -10.043 8.736 -52.769 1.00 44.02 C ANISOU 1511 CZ PHE A 241 6065 3482 7178 -255 -409 -189 C ATOM 1512 N ILE A 242 -5.772 5.285 -51.636 1.00 43.03 N ANISOU 1512 N ILE A 242 6157 3077 7118 -350 -46 -263 N ATOM 1513 CA ILE A 242 -6.521 4.101 -51.254 1.00 42.49 C ANISOU 1513 CA ILE A 242 6062 3002 7079 -414 -50 -270 C ATOM 1514 C ILE A 242 -6.248 3.650 -49.830 1.00 38.33 C ANISOU 1514 C ILE A 242 5476 2471 6618 -386 5 -235 C ATOM 1515 O ILE A 242 -7.183 3.486 -49.069 1.00 42.80 O ANISOU 1515 O ILE A 242 5962 3090 7212 -411 -16 -212 O ATOM 1516 CB ILE A 242 -6.273 2.920 -52.198 1.00 45.61 C ANISOU 1516 CB ILE A 242 6573 3314 7444 -483 -26 -318 C ATOM 1517 CG1 ILE A 242 -6.770 3.265 -53.588 1.00 47.86 C ANISOU 1517 CG1 ILE A 242 6922 3618 7643 -531 -97 -352 C ATOM 1518 CG2 ILE A 242 -6.946 1.669 -51.647 1.00 47.00 C ANISOU 1518 CG2 ILE A 242 6735 3460 7662 -560 -23 -317 C ATOM 1519 CD1 ILE A 242 -8.250 3.512 -53.703 1.00 52.18 C ANISOU 1519 CD1 ILE A 242 7389 4254 8182 -586 -208 -340 C ATOM 1520 N MET A 243 -4.981 3.460 -49.511 1.00 35.07 N ANISOU 1520 N MET A 243 5098 2004 6225 -336 73 -227 N ATOM 1521 CA MET A 243 -4.562 3.004 -48.231 1.00 40.43 C ANISOU 1521 CA MET A 243 5735 2673 6951 -305 116 -187 C ATOM 1522 C MET A 243 -4.981 3.988 -47.134 1.00 44.25 C ANISOU 1522 C MET A 243 6127 3245 7442 -265 91 -155 C ATOM 1523 O MET A 243 -5.498 3.597 -46.092 1.00 36.36 O ANISOU 1523 O MET A 243 5077 2276 6462 -276 101 -124 O ATOM 1524 CB MET A 243 -3.031 2.782 -48.231 1.00 46.42 C ANISOU 1524 CB MET A 243 6533 3375 7728 -245 181 -182 C ATOM 1525 CG MET A 243 -2.313 2.502 -46.855 1.00 57.46 C ANISOU 1525 CG MET A 243 7884 4777 9171 -192 211 -127 C ATOM 1526 SD MET A 243 -0.454 2.496 -46.691 1.00 71.15 S ANISOU 1526 SD MET A 243 9608 6487 10937 -106 266 -104 S ATOM 1527 CE MET A 243 -0.062 4.197 -46.228 1.00 70.18 C ANISOU 1527 CE MET A 243 9416 6456 10793 -87 225 -95 C ATOM 1528 N PRO A 244 -4.712 5.303 -47.297 1.00 39.70 N ANISOU 1528 N PRO A 244 5539 2703 6844 -218 67 -163 N ATOM 1529 CA PRO A 244 -5.172 6.282 -46.306 1.00 37.82 C ANISOU 1529 CA PRO A 244 5234 2532 6604 -174 46 -148 C ATOM 1530 C PRO A 244 -6.679 6.263 -46.076 1.00 34.71 C ANISOU 1530 C PRO A 244 4771 2206 6211 -193 15 -146 C ATOM 1531 O PRO A 244 -7.097 6.240 -44.923 1.00 34.66 O ANISOU 1531 O PRO A 244 4706 2250 6213 -177 37 -125 O ATOM 1532 CB PRO A 244 -4.673 7.599 -46.888 1.00 36.95 C ANISOU 1532 CB PRO A 244 5157 2414 6468 -136 20 -164 C ATOM 1533 CG PRO A 244 -3.468 7.204 -47.634 1.00 36.87 C ANISOU 1533 CG PRO A 244 5207 2345 6456 -152 57 -169 C ATOM 1534 CD PRO A 244 -3.820 5.901 -48.304 1.00 39.68 C ANISOU 1534 CD PRO A 244 5595 2666 6814 -202 72 -183 C ATOM 1535 N VAL A 245 -7.465 6.144 -47.145 1.00 34.93 N ANISOU 1535 N VAL A 245 4801 2243 6228 -235 -31 -163 N ATOM 1536 CA VAL A 245 -8.892 6.139 -46.992 1.00 36.02 C ANISOU 1536 CA VAL A 245 4846 2463 6376 -257 -67 -156 C ATOM 1537 C VAL A 245 -9.269 4.897 -46.168 1.00 40.60 C ANISOU 1537 C VAL A 245 5387 3053 6985 -326 -22 -131 C ATOM 1538 O VAL A 245 -10.124 4.972 -45.310 1.00 40.52 O ANISOU 1538 O VAL A 245 5282 3124 6988 -323 -7 -109 O ATOM 1539 CB VAL A 245 -9.675 6.122 -48.297 1.00 37.37 C ANISOU 1539 CB VAL A 245 5019 2652 6527 -305 -143 -173 C ATOM 1540 CG1 VAL A 245 -11.177 5.812 -48.039 1.00 39.27 C ANISOU 1540 CG1 VAL A 245 5132 2996 6794 -350 -178 -157 C ATOM 1541 CG2 VAL A 245 -9.600 7.475 -48.991 1.00 40.20 C ANISOU 1541 CG2 VAL A 245 5403 3016 6853 -229 -196 -179 C ATOM 1542 N LEU A 246 -8.635 3.752 -46.444 1.00 38.53 N ANISOU 1542 N LEU A 246 5206 2703 6731 -386 6 -133 N ATOM 1543 CA LEU A 246 -8.959 2.530 -45.708 1.00 39.00 C ANISOU 1543 CA LEU A 246 5255 2747 6817 -459 47 -100 C ATOM 1544 C LEU A 246 -8.546 2.661 -44.241 1.00 37.43 C ANISOU 1544 C LEU A 246 5027 2573 6622 -402 102 -56 C ATOM 1545 O LEU A 246 -9.303 2.339 -43.334 1.00 39.55 O ANISOU 1545 O LEU A 246 5231 2901 6896 -436 130 -19 O ATOM 1546 CB LEU A 246 -8.270 1.304 -46.352 1.00 39.68 C ANISOU 1546 CB LEU A 246 5460 2705 6912 -515 68 -115 C ATOM 1547 CG LEU A 246 -8.899 0.982 -47.701 1.00 44.92 C ANISOU 1547 CG LEU A 246 6163 3351 7556 -601 10 -163 C ATOM 1548 CD1 LEU A 246 -8.053 -0.105 -48.342 1.00 54.50 C ANISOU 1548 CD1 LEU A 246 7519 4422 8766 -631 46 -194 C ATOM 1549 CD2 LEU A 246 -10.332 0.510 -47.553 1.00 47.07 C ANISOU 1549 CD2 LEU A 246 6350 3691 7844 -714 -28 -149 C ATOM 1550 N ILE A 247 -7.333 3.158 -44.010 1.00 37.33 N ANISOU 1550 N ILE A 247 5061 2523 6598 -322 117 -57 N ATOM 1551 CA ILE A 247 -6.815 3.300 -42.654 1.00 38.73 C ANISOU 1551 CA ILE A 247 5225 2726 6765 -273 153 -18 C ATOM 1552 C ILE A 247 -7.734 4.149 -41.740 1.00 37.27 C ANISOU 1552 C ILE A 247 4956 2653 6554 -243 159 -14 C ATOM 1553 O ILE A 247 -8.160 3.692 -40.673 1.00 35.21 O ANISOU 1553 O ILE A 247 4663 2436 6279 -264 201 27 O ATOM 1554 CB ILE A 247 -5.387 3.824 -42.611 1.00 38.27 C ANISOU 1554 CB ILE A 247 5212 2630 6701 -203 152 -24 C ATOM 1555 CG1 ILE A 247 -4.435 2.756 -43.102 1.00 39.77 C ANISOU 1555 CG1 ILE A 247 5470 2721 6921 -213 174 -11 C ATOM 1556 CG2 ILE A 247 -5.000 4.154 -41.196 1.00 40.69 C ANISOU 1556 CG2 ILE A 247 5498 2983 6978 -160 166 10 C ATOM 1557 CD1 ILE A 247 -3.053 3.279 -43.494 1.00 40.50 C ANISOU 1557 CD1 ILE A 247 5585 2785 7018 -154 174 -25 C ATOM 1558 N ILE A 248 -8.080 5.350 -42.188 1.00 36.57 N ANISOU 1558 N ILE A 248 4836 2604 6454 -192 125 -55 N ATOM 1559 CA ILE A 248 -8.807 6.280 -41.360 1.00 36.06 C ANISOU 1559 CA ILE A 248 4706 2631 6365 -133 139 -64 C ATOM 1560 C ILE A 248 -10.246 5.825 -41.207 1.00 35.72 C ANISOU 1560 C ILE A 248 4560 2675 6338 -180 159 -46 C ATOM 1561 O ILE A 248 -10.814 5.959 -40.154 1.00 37.87 O ANISOU 1561 O ILE A 248 4774 3026 6587 -160 210 -30 O ATOM 1562 CB ILE A 248 -8.707 7.752 -41.852 1.00 35.33 C ANISOU 1562 CB ILE A 248 4628 2535 6261 -50 97 -110 C ATOM 1563 CG1 ILE A 248 -9.486 7.942 -43.127 1.00 39.78 C ANISOU 1563 CG1 ILE A 248 5160 3106 6848 -61 44 -125 C ATOM 1564 CG2 ILE A 248 -7.240 8.151 -41.974 1.00 35.40 C ANISOU 1564 CG2 ILE A 248 4728 2464 6257 -30 83 -121 C ATOM 1565 CD1 ILE A 248 -9.638 9.367 -43.623 1.00 43.36 C ANISOU 1565 CD1 ILE A 248 5627 3556 7293 27 -1 -155 C ATOM 1566 N THR A 249 -10.860 5.289 -42.257 1.00 34.85 N ANISOU 1566 N THR A 249 4422 2559 6261 -250 119 -49 N ATOM 1567 CA THR A 249 -12.228 4.841 -42.119 1.00 37.58 C ANISOU 1567 CA THR A 249 4649 3002 6629 -314 130 -27 C ATOM 1568 C THR A 249 -12.296 3.603 -41.183 1.00 38.85 C ANISOU 1568 C THR A 249 4813 3160 6790 -406 198 28 C ATOM 1569 O THR A 249 -13.253 3.445 -40.426 1.00 40.19 O ANISOU 1569 O THR A 249 4880 3431 6958 -436 249 59 O ATOM 1570 CB THR A 249 -12.930 4.521 -43.440 1.00 39.80 C ANISOU 1570 CB THR A 249 4895 3289 6940 -389 55 -42 C ATOM 1571 OG1 THR A 249 -12.233 3.462 -44.087 1.00 45.04 O ANISOU 1571 OG1 THR A 249 5670 3835 7606 -478 41 -45 O ATOM 1572 CG2 THR A 249 -12.859 5.716 -44.326 1.00 40.27 C ANISOU 1572 CG2 THR A 249 4965 3348 6989 -296 -13 -79 C ATOM 1573 N VAL A 250 -11.287 2.732 -41.213 1.00 40.77 N ANISOU 1573 N VAL A 250 5172 3286 7033 -446 206 46 N ATOM 1574 CA VAL A 250 -11.354 1.498 -40.372 1.00 39.81 C ANISOU 1574 CA VAL A 250 5075 3140 6912 -534 264 111 C ATOM 1575 C VAL A 250 -11.039 1.862 -38.925 1.00 36.87 C ANISOU 1575 C VAL A 250 4702 2821 6487 -467 324 147 C ATOM 1576 O VAL A 250 -11.772 1.471 -38.013 1.00 38.13 O ANISOU 1576 O VAL A 250 4807 3054 6626 -516 386 196 O ATOM 1577 CB VAL A 250 -10.465 0.380 -40.896 1.00 42.58 C ANISOU 1577 CB VAL A 250 5554 3338 7286 -585 252 122 C ATOM 1578 CG1 VAL A 250 -10.312 -0.796 -39.897 1.00 44.45 C ANISOU 1578 CG1 VAL A 250 5845 3524 7519 -646 310 202 C ATOM 1579 CG2 VAL A 250 -11.115 -0.137 -42.171 1.00 47.87 C ANISOU 1579 CG2 VAL A 250 6223 3974 7990 -686 202 86 C ATOM 1580 N CYS A 251 -10.004 2.658 -38.725 1.00 33.84 N ANISOU 1580 N CYS A 251 4375 2409 6073 -363 307 121 N ATOM 1581 CA CYS A 251 -9.564 3.040 -37.395 1.00 35.26 C ANISOU 1581 CA CYS A 251 4576 2633 6188 -304 346 145 C ATOM 1582 C CYS A 251 -10.660 3.847 -36.720 1.00 36.92 C ANISOU 1582 C CYS A 251 4690 2977 6360 -269 394 127 C ATOM 1583 O CYS A 251 -10.983 3.566 -35.598 1.00 37.76 O ANISOU 1583 O CYS A 251 4785 3148 6414 -286 460 170 O ATOM 1584 CB CYS A 251 -8.267 3.826 -37.453 1.00 38.23 C ANISOU 1584 CB CYS A 251 5021 2958 6545 -217 302 111 C ATOM 1585 SG CYS A 251 -6.887 2.739 -37.842 1.00 44.90 S ANISOU 1585 SG CYS A 251 5962 3671 7427 -237 275 152 S ATOM 1586 N TYR A 252 -11.276 4.813 -37.430 1.00 37.04 N ANISOU 1586 N TYR A 252 4636 3036 6402 -216 366 67 N ATOM 1587 CA TYR A 252 -12.276 5.682 -36.813 1.00 36.72 C ANISOU 1587 CA TYR A 252 4501 3119 6332 -150 418 42 C ATOM 1588 C TYR A 252 -13.558 4.963 -36.656 1.00 37.80 C ANISOU 1588 C TYR A 252 4513 3354 6494 -233 472 85 C ATOM 1589 O TYR A 252 -14.253 5.140 -35.659 1.00 38.67 O ANISOU 1589 O TYR A 252 4556 3575 6560 -212 559 99 O ATOM 1590 CB TYR A 252 -12.507 6.959 -37.603 1.00 36.06 C ANISOU 1590 CB TYR A 252 4388 3039 6274 -49 366 -26 C ATOM 1591 CG TYR A 252 -11.396 7.977 -37.454 1.00 36.04 C ANISOU 1591 CG TYR A 252 4500 2963 6233 39 334 -74 C ATOM 1592 CD1 TYR A 252 -10.871 8.312 -36.190 1.00 38.14 C ANISOU 1592 CD1 TYR A 252 4830 3242 6418 78 378 -82 C ATOM 1593 CD2 TYR A 252 -10.919 8.649 -38.540 1.00 35.75 C ANISOU 1593 CD2 TYR A 252 4507 2848 6228 74 258 -110 C ATOM 1594 CE1 TYR A 252 -9.903 9.274 -36.032 1.00 37.78 C ANISOU 1594 CE1 TYR A 252 4884 3134 6336 139 340 -129 C ATOM 1595 CE2 TYR A 252 -9.927 9.608 -38.406 1.00 38.48 C ANISOU 1595 CE2 TYR A 252 4953 3127 6542 135 229 -150 C ATOM 1596 CZ TYR A 252 -9.436 9.943 -37.153 1.00 39.57 C ANISOU 1596 CZ TYR A 252 5147 3279 6610 165 267 -163 C ATOM 1597 OH TYR A 252 -8.452 10.911 -37.086 1.00 37.87 O ANISOU 1597 OH TYR A 252 5029 2993 6366 203 226 -206 O ATOM 1598 N GLY A 253 -13.888 4.104 -37.629 1.00 37.26 N ANISOU 1598 N GLY A 253 4416 3251 6491 -340 427 106 N ATOM 1599 CA GLY A 253 -15.114 3.320 -37.504 1.00 38.60 C ANISOU 1599 CA GLY A 253 4461 3516 6691 -453 471 153 C ATOM 1600 C GLY A 253 -15.004 2.312 -36.320 1.00 39.60 C ANISOU 1600 C GLY A 253 4632 3642 6771 -540 559 231 C ATOM 1601 O GLY A 253 -15.950 2.133 -35.582 1.00 40.30 O ANISOU 1601 O GLY A 253 4617 3853 6843 -584 644 270 O ATOM 1602 N LEU A 254 -13.866 1.641 -36.161 1.00 37.74 N ANISOU 1602 N LEU A 254 4549 3275 6516 -564 541 261 N ATOM 1603 CA LEU A 254 -13.684 0.752 -34.987 1.00 38.33 C ANISOU 1603 CA LEU A 254 4686 3342 6536 -628 615 348 C ATOM 1604 C LEU A 254 -13.692 1.544 -33.650 1.00 38.46 C ANISOU 1604 C LEU A 254 4695 3467 6451 -534 692 349 C ATOM 1605 O LEU A 254 -14.175 1.072 -32.609 1.00 37.22 O ANISOU 1605 O LEU A 254 4522 3384 6234 -591 783 416 O ATOM 1606 CB LEU A 254 -12.399 -0.055 -35.109 1.00 37.22 C ANISOU 1606 CB LEU A 254 4707 3036 6400 -641 569 382 C ATOM 1607 CG LEU A 254 -12.448 -1.187 -36.190 1.00 38.29 C ANISOU 1607 CG LEU A 254 4885 3046 6618 -758 524 394 C ATOM 1608 CD1 LEU A 254 -11.149 -2.001 -36.169 1.00 38.55 C ANISOU 1608 CD1 LEU A 254 5078 2913 6654 -741 499 433 C ATOM 1609 CD2 LEU A 254 -13.630 -2.117 -36.025 1.00 40.07 C ANISOU 1609 CD2 LEU A 254 5045 3312 6866 -921 575 454 C ATOM 1610 N MET A 255 -13.166 2.775 -33.709 1.00 37.80 N ANISOU 1610 N MET A 255 4633 3389 6342 -397 656 271 N ATOM 1611 CA MET A 255 -13.155 3.641 -32.523 1.00 39.07 C ANISOU 1611 CA MET A 255 4806 3639 6398 -304 720 249 C ATOM 1612 C MET A 255 -14.611 3.951 -32.114 1.00 39.57 C ANISOU 1612 C MET A 255 4718 3866 6452 -301 824 243 C ATOM 1613 O MET A 255 -15.044 3.754 -30.983 1.00 40.13 O ANISOU 1613 O MET A 255 4776 4033 6439 -321 929 285 O ATOM 1614 CB MET A 255 -12.271 4.854 -32.806 1.00 38.37 C ANISOU 1614 CB MET A 255 4786 3497 6297 -179 649 162 C ATOM 1615 CG MET A 255 -12.165 5.840 -31.655 1.00 40.80 C ANISOU 1615 CG MET A 255 5137 3874 6491 -83 700 117 C ATOM 1616 SD MET A 255 -11.479 7.466 -32.235 1.00 41.41 S ANISOU 1616 SD MET A 255 5272 3883 6578 51 617 0 S ATOM 1617 CE MET A 255 -13.001 8.115 -32.959 1.00 39.68 C ANISOU 1617 CE MET A 255 4893 3748 6435 114 657 -46 C ATOM 1618 N ILE A 256 -15.417 4.350 -33.086 1.00 40.84 N ANISOU 1618 N ILE A 256 4751 4067 6701 -284 795 201 N ATOM 1619 CA ILE A 256 -16.805 4.671 -32.828 1.00 43.86 C ANISOU 1619 CA ILE A 256 4957 4613 7094 -267 885 197 C ATOM 1620 C ILE A 256 -17.520 3.452 -32.317 1.00 45.79 C ANISOU 1620 C ILE A 256 5132 4930 7335 -427 969 293 C ATOM 1621 O ILE A 256 -18.292 3.556 -31.370 1.00 45.68 O ANISOU 1621 O ILE A 256 5033 5058 7264 -420 1095 315 O ATOM 1622 CB ILE A 256 -17.483 5.243 -34.063 1.00 44.45 C ANISOU 1622 CB ILE A 256 4904 4715 7272 -222 813 148 C ATOM 1623 CG1 ILE A 256 -17.049 6.702 -34.193 1.00 46.09 C ANISOU 1623 CG1 ILE A 256 5167 4887 7459 -37 776 57 C ATOM 1624 CG2 ILE A 256 -18.988 5.153 -33.994 1.00 46.03 C ANISOU 1624 CG2 ILE A 256 4882 5092 7517 -252 888 173 C ATOM 1625 CD1 ILE A 256 -17.187 7.105 -35.639 1.00 50.26 C ANISOU 1625 CD1 ILE A 256 5649 5367 8080 -10 658 24 C ATOM 1626 N LEU A 257 -17.268 2.295 -32.940 1.00 45.67 N ANISOU 1626 N LEU A 257 5162 4812 7378 -574 907 349 N ATOM 1627 CA LEU A 257 -17.928 1.072 -32.496 1.00 48.27 C ANISOU 1627 CA LEU A 257 5445 5184 7710 -749 981 448 C ATOM 1628 C LEU A 257 -17.623 0.779 -31.042 1.00 45.26 C ANISOU 1628 C LEU A 257 5159 4832 7206 -757 1088 514 C ATOM 1629 O LEU A 257 -18.533 0.488 -30.284 1.00 46.21 O ANISOU 1629 O LEU A 257 5182 5087 7289 -827 1210 570 O ATOM 1630 CB LEU A 257 -17.572 -0.114 -33.394 1.00 53.87 C ANISOU 1630 CB LEU A 257 6233 5740 8494 -898 892 488 C ATOM 1631 CG LEU A 257 -18.583 -0.717 -34.396 1.00 65.75 C ANISOU 1631 CG LEU A 257 7604 7275 10103 -1048 850 496 C ATOM 1632 CD1 LEU A 257 -19.943 -0.045 -34.564 1.00 69.30 C ANISOU 1632 CD1 LEU A 257 7808 7928 10594 -1031 884 471 C ATOM 1633 CD2 LEU A 257 -17.882 -0.841 -35.759 1.00 69.46 C ANISOU 1633 CD2 LEU A 257 8170 7586 10636 -1046 708 439 C ATOM 1634 N AARG A 258 -16.347 0.866 -30.624 0.62 42.88 N ANISOU 1634 N AARG A 258 5041 4418 6835 -687 1045 512 N ATOM 1635 N BARG A 258 -16.345 0.876 -30.652 0.38 43.93 N ANISOU 1635 N BARG A 258 5172 4548 6969 -686 1043 510 N ATOM 1636 CA AARG A 258 -16.057 0.606 -29.194 0.62 43.21 C ANISOU 1636 CA AARG A 258 5181 4498 6739 -693 1135 580 C ATOM 1637 CA BARG A 258 -15.968 0.646 -29.257 0.38 44.56 C ANISOU 1637 CA BARG A 258 5360 4659 6914 -685 1124 574 C ATOM 1638 C AARG A 258 -16.838 1.600 -28.302 0.62 44.42 C ANISOU 1638 C AARG A 258 5240 4836 6801 -599 1259 534 C ATOM 1639 C BARG A 258 -16.764 1.594 -28.315 0.38 45.33 C ANISOU 1639 C BARG A 258 5365 4943 6916 -597 1252 533 C ATOM 1640 O AARG A 258 -17.462 1.223 -27.295 0.62 45.17 O ANISOU 1640 O AARG A 258 5307 5045 6809 -662 1390 602 O ATOM 1641 O BARG A 258 -17.336 1.169 -27.305 0.38 46.27 O ANISOU 1641 O BARG A 258 5465 5167 6947 -664 1379 605 O ATOM 1642 CB AARG A 258 -14.553 0.607 -28.879 0.62 41.62 C ANISOU 1642 CB AARG A 258 5173 4164 6475 -626 1051 586 C ATOM 1643 CB BARG A 258 -14.453 0.799 -29.093 0.38 43.66 C ANISOU 1643 CB BARG A 258 5428 4410 6750 -603 1029 562 C ATOM 1644 CG AARG A 258 -14.213 0.317 -27.409 0.62 42.44 C ANISOU 1644 CG AARG A 258 5390 4311 6424 -635 1122 665 C ATOM 1645 CG BARG A 258 -13.853 -0.077 -28.004 0.38 44.96 C ANISOU 1645 CG BARG A 258 5735 4538 6811 -661 1058 675 C ATOM 1646 CD AARG A 258 -14.449 -1.139 -26.900 0.62 43.31 C ANISOU 1646 CD AARG A 258 5554 4388 6514 -795 1177 814 C ATOM 1647 CD BARG A 258 -13.882 -1.579 -28.371 0.38 46.07 C ANISOU 1647 CD BARG A 258 5919 4561 7024 -813 1043 785 C ATOM 1648 NE AARG A 258 -13.663 -2.095 -27.689 0.62 43.18 N ANISOU 1648 NE AARG A 258 5630 4180 6595 -849 1069 861 N ATOM 1649 NE BARG A 258 -15.152 -2.229 -28.050 0.38 47.63 N ANISOU 1649 NE BARG A 258 6020 4855 7223 -957 1158 857 N ATOM 1650 CZ AARG A 258 -12.343 -2.269 -27.593 0.62 42.74 C ANISOU 1650 CZ AARG A 258 5718 4003 6518 -782 975 882 C ATOM 1651 CZ BARG A 258 -16.014 -2.729 -28.938 0.38 48.18 C ANISOU 1651 CZ BARG A 258 5976 4919 7410 -1076 1158 857 C ATOM 1652 NH1AARG A 258 -11.613 -1.620 -26.693 0.62 43.75 N ANISOU 1652 NH1AARG A 258 5923 4177 6522 -681 959 872 N ATOM 1653 NH1BARG A 258 -17.137 -3.299 -28.515 0.38 50.76 N ANISOU 1653 NH1BARG A 258 6207 5350 7730 -1220 1268 931 N ATOM 1654 NH2AARG A 258 -11.745 -3.083 -28.412 0.62 42.26 N ANISOU 1654 NH2AARG A 258 5722 3777 6559 -814 895 910 N ATOM 1655 NH2BARG A 258 -15.769 -2.680 -30.227 0.38 46.34 N ANISOU 1655 NH2BARG A 258 5728 4586 7294 -1063 1049 788 N ATOM 1656 N LEU A 259 -16.804 2.880 -28.680 1.00 43.93 N ANISOU 1656 N LEU A 259 5139 4799 6756 -445 1225 418 N ATOM 1657 CA LEU A 259 -17.476 3.887 -27.907 1.00 47.10 C ANISOU 1657 CA LEU A 259 5470 5350 7076 -329 1341 356 C ATOM 1658 C LEU A 259 -18.988 3.597 -27.776 1.00 52.56 C ANISOU 1658 C LEU A 259 5948 6218 7804 -394 1473 396 C ATOM 1659 O LEU A 259 -19.550 3.671 -26.680 1.00 55.42 O ANISOU 1659 O LEU A 259 6279 6719 8059 -386 1625 418 O ATOM 1660 CB LEU A 259 -17.193 5.326 -28.470 1.00 45.46 C ANISOU 1660 CB LEU A 259 5268 5106 6897 -148 1271 224 C ATOM 1661 CG LEU A 259 -15.753 5.734 -28.220 1.00 43.28 C ANISOU 1661 CG LEU A 259 5198 4699 6549 -90 1178 186 C ATOM 1662 CD1 LEU A 259 -15.415 6.999 -28.950 1.00 43.35 C ANISOU 1662 CD1 LEU A 259 5224 4642 6606 48 1094 72 C ATOM 1663 CD2 LEU A 259 -15.500 5.835 -26.734 1.00 44.22 C ANISOU 1663 CD2 LEU A 259 5429 4882 6490 -72 1269 197 C ATOM 1664 N LYS A 260 -19.634 3.219 -28.881 1.00 55.03 N ANISOU 1664 N LYS A 260 6112 6535 8262 -471 1417 410 N ATOM 1665 CA LYS A 260 -21.054 2.998 -28.849 1.00 61.66 C ANISOU 1665 CA LYS A 260 6721 7555 9153 -537 1524 447 C ATOM 1666 C LYS A 260 -21.364 1.769 -27.968 1.00 62.40 C ANISOU 1666 C LYS A 260 6828 7699 9182 -727 1637 574 C ATOM 1667 O LYS A 260 -22.459 1.633 -27.445 1.00 64.41 O ANISOU 1667 O LYS A 260 6915 8134 9424 -780 1780 616 O ATOM 1668 CB LYS A 260 -21.646 2.940 -30.277 1.00 69.43 C ANISOU 1668 CB LYS A 260 7544 8537 10300 -579 1412 428 C ATOM 1669 CG LYS A 260 -21.714 1.569 -30.938 1.00 80.84 C ANISOU 1669 CG LYS A 260 8989 9902 11824 -807 1342 513 C ATOM 1670 CD LYS A 260 -22.920 1.446 -31.868 1.00 89.76 C ANISOU 1670 CD LYS A 260 9875 11149 13083 -888 1307 517 C ATOM 1671 CE LYS A 260 -24.207 1.243 -31.071 1.00 95.08 C ANISOU 1671 CE LYS A 260 10328 12051 13746 -961 1475 578 C ATOM 1672 NZ LYS A 260 -25.374 0.959 -31.934 1.00 95.69 N ANISOU 1672 NZ LYS A 260 10152 12254 13952 -1076 1431 600 N ATOM 1673 N SER A 261 -20.382 0.887 -27.758 1.00 60.80 N ANISOU 1673 N SER A 261 6828 7338 8935 -823 1579 643 N ATOM 1674 CA SER A 261 -20.657 -0.325 -26.988 1.00 63.11 C ANISOU 1674 CA SER A 261 7156 7653 9172 -1010 1674 778 C ATOM 1675 C SER A 261 -20.601 -0.119 -25.487 1.00 64.97 C ANISOU 1675 C SER A 261 7473 7990 9224 -965 1821 813 C ATOM 1676 O SER A 261 -20.951 -0.985 -24.775 1.00 69.51 O ANISOU 1676 O SER A 261 8064 8610 9738 -1109 1922 927 O ATOM 1677 CB SER A 261 -19.728 -1.453 -27.360 1.00 61.51 C ANISOU 1677 CB SER A 261 7135 7234 9000 -1130 1561 851 C ATOM 1678 OG SER A 261 -18.394 -1.167 -26.947 1.00 63.23 O ANISOU 1678 OG SER A 261 7564 7332 9129 -1013 1493 832 O ATOM 1679 N VAL A 262 -20.173 1.049 -25.002 1.00 69.42 N ANISOU 1679 N VAL A 262 8098 8586 9691 -772 1835 713 N ATOM 1680 CA VAL A 262 -20.007 1.194 -23.577 1.00 71.89 C ANISOU 1680 CA VAL A 262 8526 8981 9808 -739 1960 741 C ATOM 1681 C VAL A 262 -21.357 1.413 -22.936 1.00 78.38 C ANISOU 1681 C VAL A 262 9160 10037 10585 -747 2167 750 C ATOM 1682 O VAL A 262 -22.191 2.171 -23.452 1.00 74.88 O ANISOU 1682 O VAL A 262 8517 9702 10234 -653 2204 666 O ATOM 1683 CB VAL A 262 -19.047 2.318 -23.163 1.00 74.50 C ANISOU 1683 CB VAL A 262 9014 9263 10028 -550 1905 629 C ATOM 1684 CG1 VAL A 262 -19.563 3.674 -23.585 1.00 77.05 C ANISOU 1684 CG1 VAL A 262 9212 9661 10403 -371 1926 482 C ATOM 1685 CG2 VAL A 262 -18.872 2.305 -21.643 1.00 78.25 C ANISOU 1685 CG2 VAL A 262 9631 9825 10278 -546 2027 670 C ATOM 1686 N ARG A 263 -21.564 0.721 -21.813 1.00 86.13 N ANISOU 1686 N ARG A 263 10205 11096 11423 -859 2304 861 N ATOM 1687 CA ARG A 263 -22.690 0.946 -20.919 1.00 94.96 C ANISOU 1687 CA ARG A 263 11183 12449 12446 -860 2534 876 C ATOM 1688 C ARG A 263 -22.188 1.588 -19.648 1.00 95.56 C ANISOU 1688 C ARG A 263 11445 12575 12289 -738 2621 832 C ATOM 1689 O ARG A 263 -20.999 1.758 -19.450 1.00110.04 O ANISOU 1689 O ARG A 263 13504 14266 14042 -680 2494 807 O ATOM 1690 CB ARG A 263 -23.404 -0.374 -20.618 1.00 98.72 C ANISOU 1690 CB ARG A 263 11588 12992 12930 -1108 2640 1046 C ATOM 1691 CG ARG A 263 -24.172 -0.938 -21.809 1.00105.06 C ANISOU 1691 CG ARG A 263 12170 13793 13955 -1246 2581 1077 C ATOM 1692 CD ARG A 263 -25.305 -0.009 -22.276 1.00113.96 C ANISOU 1692 CD ARG A 263 12998 15115 15186 -1131 2657 977 C ATOM 1693 NE ARG A 263 -25.261 0.197 -23.735 1.00121.05 N ANISOU 1693 NE ARG A 263 13797 15913 16283 -1102 2468 907 N ATOM 1694 CZ ARG A 263 -25.466 1.351 -24.387 1.00117.14 C ANISOU 1694 CZ ARG A 263 13181 15458 15868 -901 2415 776 C ATOM 1695 NH1 ARG A 263 -25.747 2.487 -23.748 1.00110.50 N ANISOU 1695 NH1 ARG A 263 12297 14745 14941 -690 2538 682 N ATOM 1696 NH2 ARG A 263 -25.370 1.370 -25.715 1.00115.76 N ANISOU 1696 NH2 ARG A 263 12945 15181 15858 -907 2235 737 N ATOM 1697 N MET A 264 -23.121 1.989 -18.795 1.00110.50 N ANISOU 1697 N MET A 264 13234 14681 14070 -696 2842 816 N ATOM 1698 CA MET A 264 -22.819 2.479 -17.462 1.00114.38 C ANISOU 1698 CA MET A 264 13904 15248 14308 -609 2961 783 C ATOM 1699 C MET A 264 -24.172 2.656 -16.819 1.00110.90 C ANISOU 1699 C MET A 264 13264 15064 13808 -604 3230 789 C ATOM 1700 O MET A 264 -24.978 3.445 -17.310 1.00111.97 O ANISOU 1700 O MET A 264 13182 15304 14057 -473 3293 686 O ATOM 1701 CB MET A 264 -22.053 3.802 -17.516 1.00117.67 C ANISOU 1701 CB MET A 264 14450 15581 14677 -382 2863 605 C ATOM 1702 CG MET A 264 -22.779 4.930 -18.233 1.00126.54 C ANISOU 1702 CG MET A 264 15373 16768 15939 -200 2895 457 C ATOM 1703 SD MET A 264 -23.454 4.670 -19.899 1.00130.44 S ANISOU 1703 SD MET A 264 15580 17232 16749 -245 2784 474 S ATOM 1704 CE MET A 264 -21.947 4.725 -20.866 1.00125.09 C ANISOU 1704 CE MET A 264 15101 16269 16160 -231 2486 437 C ATOM 1705 N LEU A 265 -24.426 1.912 -15.735 1.00111.34 N ANISOU 1705 N LEU A 265 13390 15227 13687 -744 3390 917 N ATOM 1706 CA LEU A 265 -25.757 1.840 -15.114 1.00112.37 C ANISOU 1706 CA LEU A 265 13312 15618 13764 -787 3668 958 C ATOM 1707 C LEU A 265 -26.529 3.195 -15.115 1.00111.21 C ANISOU 1707 C LEU A 265 12988 15633 13634 -541 3808 781 C ATOM 1708 O LEU A 265 -27.765 3.206 -15.186 1.00114.03 O ANISOU 1708 O LEU A 265 13058 16197 14073 -553 3987 798 O ATOM 1709 CB LEU A 265 -25.674 1.210 -13.704 1.00114.06 C ANISOU 1709 CB LEU A 265 13712 15918 13706 -909 3830 1083 C ATOM 1710 CG LEU A 265 -25.395 2.106 -12.486 1.00117.10 C ANISOU 1710 CG LEU A 265 14292 16394 13808 -743 3958 978 C ATOM 1711 CD1 LEU A 265 -25.350 1.297 -11.196 1.00114.21 C ANISOU 1711 CD1 LEU A 265 14105 16112 13179 -901 4103 1134 C ATOM 1712 CD2 LEU A 265 -24.115 2.915 -12.671 1.00113.44 C ANISOU 1712 CD2 LEU A 265 14064 15733 13307 -577 3734 841 C ATOM 1713 N SER A 266 -25.782 4.311 -15.095 1.00105.63 N ANISOU 1713 N SER A 266 12447 14822 12866 -322 3714 616 N ATOM 1714 CA SER A 266 -26.311 5.663 -14.963 1.00105.16 C ANISOU 1714 CA SER A 266 12302 14868 12787 -64 3836 437 C ATOM 1715 C SER A 266 -26.218 6.491 -16.251 1.00109.39 C ANISOU 1715 C SER A 266 12727 15282 13554 96 3659 315 C ATOM 1716 O SER A 266 -27.235 6.939 -16.795 1.00112.07 O ANISOU 1716 O SER A 266 12788 15746 14047 198 3740 270 O ATOM 1717 CB SER A 266 -25.568 6.356 -13.831 1.00100.54 C ANISOU 1717 CB SER A 266 12024 14254 11924 55 3883 336 C ATOM 1718 OG SER A 266 -26.014 7.674 -13.703 1.00 97.49 O ANISOU 1718 OG SER A 266 11591 13936 11515 311 3996 151 O ATOM 1719 N GLY A 267 -24.985 6.707 -16.713 1.00109.28 N ANISOU 1719 N GLY A 267 12931 15033 13558 121 3418 267 N ATOM 1720 CA GLY A 267 -24.716 7.274 -18.023 1.00119.65 C ANISOU 1720 CA GLY A 267 14175 16199 15087 221 3218 186 C ATOM 1721 C GLY A 267 -25.200 8.709 -18.204 1.00121.15 C ANISOU 1721 C GLY A 267 14287 16429 15316 494 3281 12 C ATOM 1722 O GLY A 267 -25.133 9.486 -17.258 1.00126.97 O ANISOU 1722 O GLY A 267 15166 17207 15869 634 3409 -94 O ATOM 1723 N SER A 268 -25.715 9.058 -19.394 1.00112.13 N ANISOU 1723 N SER A 268 12927 15274 14405 571 3197 -16 N ATOM 1724 CA SER A 268 -26.117 8.133 -20.446 1.00110.99 C ANISOU 1724 CA SER A 268 12567 15137 14466 403 3092 105 C ATOM 1725 C SER A 268 -26.520 8.979 -21.661 1.00110.58 C ANISOU 1725 C SER A 268 12343 15052 14621 569 2984 22 C ATOM 1726 O SER A 268 -26.042 8.767 -22.794 1.00109.24 O ANISOU 1726 O SER A 268 12178 14733 14596 509 2768 42 O ATOM 1727 CB SER A 268 -27.309 7.268 -19.998 1.00113.96 C ANISOU 1727 CB SER A 268 12697 15755 14846 257 3295 227 C ATOM 1728 OG SER A 268 -27.690 6.357 -21.008 1.00112.58 O ANISOU 1728 OG SER A 268 12329 15580 14865 72 3184 338 O ATOM 1729 N LYS A 269 -27.416 9.937 -21.405 1.00102.57 N ANISOU 1729 N LYS A 269 11180 14181 13613 787 3143 -69 N ATOM 1730 CA LYS A 269 -27.591 11.116 -22.233 1.00103.55 C ANISOU 1730 CA LYS A 269 11239 14239 13866 1025 3058 -184 C ATOM 1731 C LYS A 269 -26.220 11.803 -22.518 1.00101.42 C ANISOU 1731 C LYS A 269 11289 13693 13551 1098 2864 -281 C ATOM 1732 O LYS A 269 -26.014 12.301 -23.631 1.00 98.30 O ANISOU 1732 O LYS A 269 10872 13172 13304 1175 2690 -316 O ATOM 1733 CB LYS A 269 -28.611 12.064 -21.561 1.00103.37 C ANISOU 1733 CB LYS A 269 11078 14396 13801 1272 3297 -278 C ATOM 1734 CG LYS A 269 -28.429 13.555 -21.822 1.00102.29 C ANISOU 1734 CG LYS A 269 11047 14132 13686 1573 3257 -441 C ATOM 1735 CD LYS A 269 -29.466 14.393 -21.079 1.00106.92 C ANISOU 1735 CD LYS A 269 11502 14899 14224 1823 3518 -532 C ATOM 1736 CE LYS A 269 -30.888 14.184 -21.595 1.00110.59 C ANISOU 1736 CE LYS A 269 11537 15608 14874 1866 3610 -456 C ATOM 1737 NZ LYS A 269 -31.032 14.301 -23.080 1.00107.47 N ANISOU 1737 NZ LYS A 269 10979 15140 14716 1887 3377 -417 N ATOM 1738 N GLU A 270 -25.318 11.815 -21.516 1.00100.40 N ANISOU 1738 N GLU A 270 11446 13486 13217 1063 2894 -317 N ATOM 1739 CA GLU A 270 -23.917 12.313 -21.635 1.00103.25 C ANISOU 1739 CA GLU A 270 12113 13602 13513 1083 2711 -392 C ATOM 1740 C GLU A 270 -23.101 11.489 -22.601 1.00 93.80 C ANISOU 1740 C GLU A 270 10951 12260 12430 899 2483 -298 C ATOM 1741 O GLU A 270 -22.319 12.030 -23.386 1.00100.68 O ANISOU 1741 O GLU A 270 11933 12949 13372 949 2304 -353 O ATOM 1742 CB GLU A 270 -23.155 12.296 -20.295 1.00106.38 C ANISOU 1742 CB GLU A 270 12785 13979 13654 1044 2782 -426 C ATOM 1743 CG GLU A 270 -23.485 13.434 -19.343 1.00113.26 C ANISOU 1743 CG GLU A 270 13757 14904 14371 1257 2958 -577 C ATOM 1744 CD GLU A 270 -24.757 13.194 -18.537 1.00122.99 C ANISOU 1744 CD GLU A 270 14799 16396 15536 1293 3238 -550 C ATOM 1745 OE1 GLU A 270 -25.522 12.258 -18.869 1.00124.41 O ANISOU 1745 OE1 GLU A 270 14724 16720 15827 1164 3287 -416 O ATOM 1746 OE2 GLU A 270 -24.994 13.946 -17.564 1.00124.26 O ANISOU 1746 OE2 GLU A 270 15067 16617 15527 1444 3413 -666 O ATOM 1747 N LYS A 271 -23.273 10.167 -22.526 1.00 89.97 N ANISOU 1747 N LYS A 271 10379 11850 11954 682 2500 -155 N ATOM 1748 CA LYS A 271 -22.659 9.247 -23.481 1.00 82.60 C ANISOU 1748 CA LYS A 271 9454 10790 11141 504 2307 -59 C ATOM 1749 C LYS A 271 -23.209 9.429 -24.927 1.00 76.55 C ANISOU 1749 C LYS A 271 8480 10007 10597 541 2193 -61 C ATOM 1750 O LYS A 271 -22.416 9.558 -25.871 1.00 71.75 O ANISOU 1750 O LYS A 271 7963 9226 10072 534 2002 -79 O ATOM 1751 CB LYS A 271 -22.786 7.806 -22.988 1.00 82.10 C ANISOU 1751 CB LYS A 271 9366 10800 11029 271 2367 92 C ATOM 1752 CG LYS A 271 -21.886 6.844 -23.718 1.00 84.10 C ANISOU 1752 CG LYS A 271 9712 10884 11357 99 2177 178 C ATOM 1753 CD LYS A 271 -22.556 6.160 -24.906 1.00 87.48 C ANISOU 1753 CD LYS A 271 9926 11329 11984 -15 2105 247 C ATOM 1754 CE LYS A 271 -23.266 4.878 -24.508 1.00 88.15 C ANISOU 1754 CE LYS A 271 9897 11531 12063 -229 2213 387 C ATOM 1755 NZ LYS A 271 -22.966 3.813 -25.503 1.00 88.71 N ANISOU 1755 NZ LYS A 271 9966 11475 12264 -413 2059 470 N ATOM 1756 N ASP A 272 -24.541 9.457 -25.099 1.00 74.05 N ANISOU 1756 N ASP A 272 7886 9878 10371 580 2307 -40 N ATOM 1757 CA ASP A 272 -25.141 9.754 -26.420 1.00 76.55 C ANISOU 1757 CA ASP A 272 7998 10202 10886 637 2194 -46 C ATOM 1758 C ASP A 272 -24.501 11.025 -27.034 1.00 74.19 C ANISOU 1758 C ASP A 272 7839 9731 10619 841 2065 -165 C ATOM 1759 O ASP A 272 -24.142 11.043 -28.219 1.00 67.69 O ANISOU 1759 O ASP A 272 7020 8788 9913 817 1880 -157 O ATOM 1760 CB ASP A 272 -26.663 9.988 -26.363 1.00 80.77 C ANISOU 1760 CB ASP A 272 8211 10979 11498 726 2347 -36 C ATOM 1761 CG ASP A 272 -27.487 8.705 -26.209 1.00 88.46 C ANISOU 1761 CG ASP A 272 8971 12130 12509 494 2433 99 C ATOM 1762 OD1 ASP A 272 -27.065 7.617 -26.680 1.00 88.58 O ANISOU 1762 OD1 ASP A 272 9033 12059 12563 263 2315 189 O ATOM 1763 OD2 ASP A 272 -28.607 8.798 -25.621 1.00 99.70 O ANISOU 1763 OD2 ASP A 272 10170 13783 13927 544 2629 114 O ATOM 1764 N ARG A 273 -24.352 12.055 -26.188 1.00 74.16 N ANISOU 1764 N ARG A 273 7966 9713 10496 1028 2169 -274 N ATOM 1765 CA ARG A 273 -23.983 13.398 -26.553 1.00 76.13 C ANISOU 1765 CA ARG A 273 8338 9823 10764 1243 2098 -395 C ATOM 1766 C ARG A 273 -22.593 13.390 -27.083 1.00 75.13 C ANISOU 1766 C ARG A 273 8449 9468 10629 1160 1900 -406 C ATOM 1767 O ARG A 273 -22.327 13.878 -28.174 1.00 74.01 O ANISOU 1767 O ARG A 273 8318 9204 10599 1214 1748 -426 O ATOM 1768 CB ARG A 273 -24.078 14.291 -25.310 1.00 86.89 C ANISOU 1768 CB ARG A 273 9825 11221 11968 1417 2276 -508 C ATOM 1769 CG ARG A 273 -24.154 15.783 -25.577 1.00 98.04 C ANISOU 1769 CG ARG A 273 11307 12530 13413 1683 2262 -640 C ATOM 1770 CD ARG A 273 -22.784 16.464 -25.607 1.00108.69 C ANISOU 1770 CD ARG A 273 12981 13630 14687 1695 2122 -726 C ATOM 1771 NE ARG A 273 -22.860 17.810 -26.210 1.00114.39 N ANISOU 1771 NE ARG A 273 13757 14218 15486 1921 2065 -827 N ATOM 1772 CZ ARG A 273 -22.474 18.138 -27.448 1.00107.77 C ANISOU 1772 CZ ARG A 273 12935 13233 14781 1930 1876 -809 C ATOM 1773 NH1 ARG A 273 -21.952 17.233 -28.274 1.00103.88 N ANISOU 1773 NH1 ARG A 273 12407 12703 14359 1730 1722 -708 N ATOM 1774 NH2 ARG A 273 -22.614 19.395 -27.866 1.00104.47 N ANISOU 1774 NH2 ARG A 273 12581 12695 14417 2146 1845 -896 N ATOM 1775 N ASN A 274 -21.684 12.819 -26.291 1.00 78.37 N ANISOU 1775 N ASN A 274 9050 9827 10901 1027 1904 -385 N ATOM 1776 CA ASN A 274 -20.303 12.601 -26.687 1.00 74.15 C ANISOU 1776 CA ASN A 274 8720 9100 10354 921 1726 -375 C ATOM 1777 C ASN A 274 -20.092 11.891 -28.009 1.00 69.37 C ANISOU 1777 C ASN A 274 8033 8425 9902 797 1564 -294 C ATOM 1778 O ASN A 274 -19.331 12.358 -28.852 1.00 67.41 O ANISOU 1778 O ASN A 274 7884 8019 9711 823 1414 -329 O ATOM 1779 CB ASN A 274 -19.604 11.799 -25.593 1.00 85.00 C ANISOU 1779 CB ASN A 274 10244 10484 11567 779 1769 -327 C ATOM 1780 CG ASN A 274 -18.644 12.637 -24.810 1.00 84.20 C ANISOU 1780 CG ASN A 274 10397 10281 11314 853 1753 -428 C ATOM 1781 OD1 ASN A 274 -17.494 12.826 -25.230 1.00 86.27 O ANISOU 1781 OD1 ASN A 274 10812 10380 11586 817 1594 -446 O ATOM 1782 ND2 ASN A 274 -19.110 13.170 -23.687 1.00 81.02 N ANISOU 1782 ND2 ASN A 274 10041 9976 10768 954 1918 -498 N ATOM 1783 N LEU A 275 -20.735 10.728 -28.158 1.00 66.41 N ANISOU 1783 N LEU A 275 7489 8162 9581 647 1599 -187 N ATOM 1784 CA LEU A 275 -20.716 9.972 -29.398 1.00 65.50 C ANISOU 1784 CA LEU A 275 7286 7997 9605 519 1461 -115 C ATOM 1785 C LEU A 275 -21.148 10.776 -30.604 1.00 62.95 C ANISOU 1785 C LEU A 275 6856 7647 9414 640 1363 -159 C ATOM 1786 O LEU A 275 -20.637 10.546 -31.702 1.00 61.98 O ANISOU 1786 O LEU A 275 6768 7409 9371 575 1208 -140 O ATOM 1787 CB LEU A 275 -21.623 8.748 -29.359 1.00 67.42 C ANISOU 1787 CB LEU A 275 7338 8385 9895 351 1530 -6 C ATOM 1788 CG LEU A 275 -20.967 7.443 -28.993 1.00 73.68 C ANISOU 1788 CG LEU A 275 8241 9120 10634 144 1516 87 C ATOM 1789 CD1 LEU A 275 -19.767 7.154 -29.884 1.00 75.64 C ANISOU 1789 CD1 LEU A 275 8646 9166 10927 83 1334 90 C ATOM 1790 CD2 LEU A 275 -20.575 7.513 -27.530 1.00 78.92 C ANISOU 1790 CD2 LEU A 275 9050 9816 11121 165 1640 81 C ATOM 1791 N ARG A 276 -22.132 11.658 -30.409 1.00 62.76 N ANISOU 1791 N ARG A 276 6696 7737 9411 817 1458 -210 N ATOM 1792 CA ARG A 276 -22.655 12.507 -31.478 1.00 64.70 C ANISOU 1792 CA ARG A 276 6834 7971 9780 962 1370 -243 C ATOM 1793 C ARG A 276 -21.586 13.484 -31.957 1.00 59.26 C ANISOU 1793 C ARG A 276 6372 7068 9078 1062 1246 -319 C ATOM 1794 O ARG A 276 -21.400 13.683 -33.143 1.00 56.14 O ANISOU 1794 O ARG A 276 5975 6584 8772 1065 1099 -308 O ATOM 1795 CB ARG A 276 -23.869 13.255 -30.978 1.00 70.79 C ANISOU 1795 CB ARG A 276 7425 8907 10566 1155 1519 -282 C ATOM 1796 CG ARG A 276 -24.637 14.056 -31.992 1.00 79.53 C ANISOU 1796 CG ARG A 276 8372 10039 11806 1321 1442 -295 C ATOM 1797 CD ARG A 276 -25.986 14.360 -31.362 1.00 88.52 C ANISOU 1797 CD ARG A 276 9266 11401 12968 1465 1621 -302 C ATOM 1798 NE ARG A 276 -26.830 15.240 -32.165 1.00104.49 N ANISOU 1798 NE ARG A 276 11116 13470 15116 1672 1568 -314 N ATOM 1799 CZ ARG A 276 -26.819 16.571 -32.128 1.00112.63 C ANISOU 1799 CZ ARG A 276 12241 14407 16145 1935 1583 -404 C ATOM 1800 NH1 ARG A 276 -25.975 17.229 -31.344 1.00123.81 N ANISOU 1800 NH1 ARG A 276 13934 15670 17438 2012 1643 -502 N ATOM 1801 NH2 ARG A 276 -27.658 17.254 -32.898 1.00109.99 N ANISOU 1801 NH2 ARG A 276 11729 14126 15936 2120 1526 -393 N ATOM 1802 N ARG A 277 -20.891 14.104 -31.008 1.00 59.24 N ANISOU 1802 N ARG A 277 6570 6986 8952 1134 1308 -396 N ATOM 1803 CA ARG A 277 -19.819 15.041 -31.311 1.00 60.50 C ANISOU 1803 CA ARG A 277 6958 6943 9086 1205 1202 -470 C ATOM 1804 C ARG A 277 -18.633 14.317 -31.990 1.00 54.28 C ANISOU 1804 C ARG A 277 6286 6025 8313 1024 1051 -418 C ATOM 1805 O ARG A 277 -18.047 14.799 -32.963 1.00 47.15 O ANISOU 1805 O ARG A 277 5463 4984 7466 1042 920 -432 O ATOM 1806 CB ARG A 277 -19.358 15.703 -30.023 1.00 68.67 C ANISOU 1806 CB ARG A 277 8179 7941 9971 1284 1304 -562 C ATOM 1807 CG ARG A 277 -18.436 16.878 -30.173 1.00 75.76 C ANISOU 1807 CG ARG A 277 9305 8642 10837 1376 1218 -656 C ATOM 1808 CD ARG A 277 -18.785 17.935 -29.129 1.00 93.51 C ANISOU 1808 CD ARG A 277 11648 10896 12985 1558 1354 -773 C ATOM 1809 NE ARG A 277 -17.616 18.769 -28.879 1.00112.34 N ANISOU 1809 NE ARG A 277 14307 13091 15287 1564 1279 -862 N ATOM 1810 CZ ARG A 277 -17.112 19.660 -29.736 1.00125.04 C ANISOU 1810 CZ ARG A 277 16025 14521 16963 1622 1156 -898 C ATOM 1811 NH1 ARG A 277 -17.671 19.881 -30.923 1.00132.88 N ANISOU 1811 NH1 ARG A 277 16890 15497 18100 1695 1088 -854 N ATOM 1812 NH2 ARG A 277 -16.030 20.344 -29.400 1.00130.62 N ANISOU 1812 NH2 ARG A 277 16976 15069 17586 1596 1095 -975 N ATOM 1813 N ILE A 278 -18.304 13.126 -31.497 1.00 50.10 N ANISOU 1813 N ILE A 278 5762 5540 7734 852 1078 -351 N ATOM 1814 CA ILE A 278 -17.164 12.406 -32.048 1.00 49.05 C ANISOU 1814 CA ILE A 278 5738 5285 7613 701 953 -305 C ATOM 1815 C ILE A 278 -17.474 11.887 -33.426 1.00 46.36 C ANISOU 1815 C ILE A 278 5279 4933 7401 631 849 -249 C ATOM 1816 O ILE A 278 -16.672 12.022 -34.359 1.00 46.07 O ANISOU 1816 O ILE A 278 5334 4766 7405 605 725 -253 O ATOM 1817 CB ILE A 278 -16.641 11.325 -31.081 1.00 51.88 C ANISOU 1817 CB ILE A 278 6162 5673 7877 558 1005 -247 C ATOM 1818 CG1 ILE A 278 -16.036 12.027 -29.844 1.00 55.70 C ANISOU 1818 CG1 ILE A 278 6816 6134 8214 628 1064 -317 C ATOM 1819 CG2 ILE A 278 -15.584 10.460 -31.733 1.00 49.47 C ANISOU 1819 CG2 ILE A 278 5937 5252 7607 417 884 -189 C ATOM 1820 CD1 ILE A 278 -16.013 11.118 -28.614 1.00 62.70 C ANISOU 1820 CD1 ILE A 278 7729 7114 8981 530 1163 -259 C ATOM 1821 N THR A 279 -18.664 11.336 -33.584 1.00 46.54 N ANISOU 1821 N THR A 279 5097 5102 7485 599 900 -199 N ATOM 1822 CA THR A 279 -19.080 10.809 -34.866 1.00 47.84 C ANISOU 1822 CA THR A 279 5143 5273 7760 519 796 -149 C ATOM 1823 C THR A 279 -19.089 11.914 -35.930 1.00 45.27 C ANISOU 1823 C THR A 279 4831 4872 7497 655 688 -195 C ATOM 1824 O THR A 279 -18.638 11.713 -37.041 1.00 43.74 O ANISOU 1824 O THR A 279 4681 4588 7350 591 563 -177 O ATOM 1825 CB THR A 279 -20.439 10.069 -34.719 1.00 50.35 C ANISOU 1825 CB THR A 279 5219 5783 8128 450 874 -88 C ATOM 1826 OG1 THR A 279 -20.257 9.076 -33.710 1.00 57.24 O ANISOU 1826 OG1 THR A 279 6126 6694 8928 316 972 -39 O ATOM 1827 CG2 THR A 279 -20.892 9.365 -36.009 1.00 48.86 C ANISOU 1827 CG2 THR A 279 4910 5610 8043 328 756 -35 C ATOM 1828 N ARG A 280 -19.577 13.088 -35.560 1.00 47.49 N ANISOU 1828 N ARG A 280 5091 5182 7770 847 744 -253 N ATOM 1829 CA ARG A 280 -19.682 14.184 -36.502 1.00 50.68 C ANISOU 1829 CA ARG A 280 5512 5511 8232 992 648 -286 C ATOM 1830 C ARG A 280 -18.284 14.579 -36.923 1.00 46.66 C ANISOU 1830 C ARG A 280 5240 4801 7688 963 551 -316 C ATOM 1831 O ARG A 280 -18.030 14.761 -38.108 1.00 44.49 O ANISOU 1831 O ARG A 280 4995 4445 7464 951 428 -298 O ATOM 1832 CB ARG A 280 -20.501 15.338 -35.924 1.00 56.97 C ANISOU 1832 CB ARG A 280 6250 6366 9029 1219 742 -344 C ATOM 1833 CG ARG A 280 -20.482 16.581 -36.810 1.00 67.59 C ANISOU 1833 CG ARG A 280 7661 7596 10426 1386 642 -376 C ATOM 1834 CD ARG A 280 -21.494 17.656 -36.394 1.00 81.85 C ANISOU 1834 CD ARG A 280 9374 9466 12258 1635 731 -423 C ATOM 1835 NE ARG A 280 -21.115 18.312 -35.135 1.00 91.47 N ANISOU 1835 NE ARG A 280 10751 10628 13376 1731 860 -516 N ATOM 1836 CZ ARG A 280 -21.705 18.126 -33.953 1.00 95.22 C ANISOU 1836 CZ ARG A 280 11143 11242 13794 1773 1030 -544 C ATOM 1837 NH1 ARG A 280 -22.751 17.303 -33.822 1.00100.97 N ANISOU 1837 NH1 ARG A 280 11611 12184 14567 1726 1104 -480 N ATOM 1838 NH2 ARG A 280 -21.242 18.777 -32.889 1.00 89.42 N ANISOU 1838 NH2 ARG A 280 10593 10433 12949 1852 1128 -639 N ATOM 1839 N MET A 281 -17.350 14.603 -35.965 1.00 45.53 N ANISOU 1839 N MET A 281 5257 4589 7451 931 604 -354 N ATOM 1840 CA MET A 281 -15.966 14.946 -36.270 1.00 46.64 C ANISOU 1840 CA MET A 281 5604 4557 7559 889 518 -380 C ATOM 1841 C MET A 281 -15.307 13.929 -37.202 1.00 44.44 C ANISOU 1841 C MET A 281 5335 4232 7318 723 423 -317 C ATOM 1842 O MET A 281 -14.652 14.291 -38.159 1.00 42.44 O ANISOU 1842 O MET A 281 5168 3866 7090 713 325 -319 O ATOM 1843 CB MET A 281 -15.101 15.126 -35.017 1.00 49.01 C ANISOU 1843 CB MET A 281 6059 4814 7750 876 580 -429 C ATOM 1844 CG MET A 281 -13.759 15.781 -35.322 1.00 55.14 C ANISOU 1844 CG MET A 281 7031 5419 8501 856 488 -465 C ATOM 1845 SD MET A 281 -13.963 17.512 -36.014 1.00 64.84 S ANISOU 1845 SD MET A 281 8347 6521 9770 1035 436 -532 S ATOM 1846 CE MET A 281 -15.449 18.062 -35.214 1.00 66.06 C ANISOU 1846 CE MET A 281 8387 6796 9918 1223 567 -578 C ATOM 1847 N VAL A 282 -15.511 12.638 -36.919 1.00 44.20 N ANISOU 1847 N VAL A 282 5221 4286 7287 593 461 -261 N ATOM 1848 CA VAL A 282 -15.072 11.602 -37.820 1.00 40.06 C ANISOU 1848 CA VAL A 282 4699 3720 6804 447 383 -208 C ATOM 1849 C VAL A 282 -15.611 11.795 -39.231 1.00 39.85 C ANISOU 1849 C VAL A 282 4600 3689 6853 460 285 -194 C ATOM 1850 O VAL A 282 -14.820 11.775 -40.205 1.00 38.15 O ANISOU 1850 O VAL A 282 4482 3366 6649 414 196 -192 O ATOM 1851 CB VAL A 282 -15.396 10.224 -37.269 1.00 40.47 C ANISOU 1851 CB VAL A 282 4674 3855 6848 313 445 -148 C ATOM 1852 CG1 VAL A 282 -15.097 9.193 -38.342 1.00 39.82 C ANISOU 1852 CG1 VAL A 282 4597 3716 6817 175 363 -105 C ATOM 1853 CG2 VAL A 282 -14.540 9.979 -36.034 1.00 40.09 C ANISOU 1853 CG2 VAL A 282 4741 3779 6711 287 509 -149 C ATOM 1854 N LEU A 283 -16.925 12.018 -39.359 1.00 40.91 N ANISOU 1854 N LEU A 283 4565 3946 7033 527 301 -184 N ATOM 1855 CA LEU A 283 -17.483 12.207 -40.676 1.00 42.58 C ANISOU 1855 CA LEU A 283 4703 4168 7307 541 192 -164 C ATOM 1856 C LEU A 283 -16.888 13.425 -41.395 1.00 43.28 C ANISOU 1856 C LEU A 283 4927 4126 7390 654 112 -196 C ATOM 1857 O LEU A 283 -16.646 13.365 -42.583 1.00 40.68 O ANISOU 1857 O LEU A 283 4638 3741 7079 608 7 -176 O ATOM 1858 CB LEU A 283 -18.991 12.306 -40.644 1.00 45.22 C ANISOU 1858 CB LEU A 283 4812 4673 7698 606 215 -141 C ATOM 1859 CG LEU A 283 -19.691 11.068 -40.150 1.00 50.10 C ANISOU 1859 CG LEU A 283 5277 5428 8332 464 282 -96 C ATOM 1860 CD1 LEU A 283 -21.187 11.242 -39.982 1.00 53.00 C ANISOU 1860 CD1 LEU A 283 5393 5988 8757 534 323 -73 C ATOM 1861 CD2 LEU A 283 -19.415 9.891 -41.084 1.00 51.37 C ANISOU 1861 CD2 LEU A 283 5461 5548 8512 267 190 -58 C ATOM 1862 N VAL A 284 -16.633 14.518 -40.659 1.00 42.55 N ANISOU 1862 N VAL A 284 4921 3980 7266 792 165 -247 N ATOM 1863 CA VAL A 284 -16.019 15.666 -41.275 1.00 41.54 C ANISOU 1863 CA VAL A 284 4942 3709 7132 881 94 -273 C ATOM 1864 C VAL A 284 -14.598 15.385 -41.767 1.00 39.71 C ANISOU 1864 C VAL A 284 4876 3345 6867 757 41 -270 C ATOM 1865 O VAL A 284 -14.264 15.743 -42.925 1.00 39.08 O ANISOU 1865 O VAL A 284 4865 3184 6799 749 -52 -252 O ATOM 1866 CB VAL A 284 -16.047 16.889 -40.360 1.00 43.82 C ANISOU 1866 CB VAL A 284 5308 3950 7392 1045 162 -337 C ATOM 1867 CG1 VAL A 284 -15.223 18.069 -40.949 1.00 43.14 C ANISOU 1867 CG1 VAL A 284 5416 3683 7294 1107 89 -363 C ATOM 1868 CG2 VAL A 284 -17.495 17.352 -40.137 1.00 47.14 C ANISOU 1868 CG2 VAL A 284 5558 4493 7859 1210 208 -339 C ATOM 1869 N VAL A 285 -13.735 14.801 -40.927 1.00 38.63 N ANISOU 1869 N VAL A 285 4806 3188 6685 667 98 -284 N ATOM 1870 CA VAL A 285 -12.360 14.657 -41.349 1.00 38.31 C ANISOU 1870 CA VAL A 285 4905 3030 6621 573 53 -282 C ATOM 1871 C VAL A 285 -12.251 13.689 -42.537 1.00 39.19 C ANISOU 1871 C VAL A 285 4986 3142 6761 459 -9 -236 C ATOM 1872 O VAL A 285 -11.388 13.882 -43.394 1.00 38.90 O ANISOU 1872 O VAL A 285 5052 3011 6718 419 -64 -231 O ATOM 1873 CB VAL A 285 -11.308 14.365 -40.235 1.00 38.55 C ANISOU 1873 CB VAL A 285 5021 3031 6596 515 107 -303 C ATOM 1874 CG1 VAL A 285 -11.517 15.231 -39.014 1.00 41.81 C ANISOU 1874 CG1 VAL A 285 5471 3453 6960 616 172 -358 C ATOM 1875 CG2 VAL A 285 -11.241 12.920 -39.833 1.00 42.06 C ANISOU 1875 CG2 VAL A 285 5402 3543 7038 401 146 -261 C ATOM 1876 N VAL A 286 -13.124 12.668 -42.594 1.00 40.35 N ANISOU 1876 N VAL A 286 5000 3394 6935 398 3 -204 N ATOM 1877 CA VAL A 286 -13.100 11.688 -43.683 1.00 38.36 C ANISOU 1877 CA VAL A 286 4734 3140 6703 280 -56 -172 C ATOM 1878 C VAL A 286 -13.613 12.328 -44.969 1.00 39.45 C ANISOU 1878 C VAL A 286 4862 3271 6857 326 -154 -162 C ATOM 1879 O VAL A 286 -13.007 12.195 -46.016 1.00 37.35 O ANISOU 1879 O VAL A 286 4684 2934 6573 269 -214 -155 O ATOM 1880 CB VAL A 286 -13.870 10.376 -43.314 1.00 39.60 C ANISOU 1880 CB VAL A 286 4765 3398 6882 178 -18 -142 C ATOM 1881 CG1 VAL A 286 -13.962 9.396 -44.470 1.00 38.33 C ANISOU 1881 CG1 VAL A 286 4602 3224 6737 53 -86 -122 C ATOM 1882 CG2 VAL A 286 -13.141 9.648 -42.214 1.00 40.02 C ANISOU 1882 CG2 VAL A 286 4868 3429 6908 120 64 -137 C ATOM 1883 N ALA A 287 -14.742 13.030 -44.858 1.00 40.87 N ANISOU 1883 N ALA A 287 4932 3532 7064 439 -167 -158 N ATOM 1884 CA ALA A 287 -15.364 13.723 -45.965 1.00 43.61 C ANISOU 1884 CA ALA A 287 5256 3887 7427 509 -269 -136 C ATOM 1885 C ALA A 287 -14.411 14.792 -46.564 1.00 42.17 C ANISOU 1885 C ALA A 287 5256 3558 7211 566 -313 -145 C ATOM 1886 O ALA A 287 -14.240 14.866 -47.768 1.00 42.78 O ANISOU 1886 O ALA A 287 5393 3594 7268 532 -399 -119 O ATOM 1887 CB ALA A 287 -16.694 14.357 -45.565 1.00 42.83 C ANISOU 1887 CB ALA A 287 4996 3902 7373 652 -262 -128 C ATOM 1888 N VAL A 288 -13.740 15.564 -45.718 1.00 41.28 N ANISOU 1888 N VAL A 288 5239 3363 7082 633 -251 -180 N ATOM 1889 CA VAL A 288 -12.760 16.503 -46.243 1.00 41.18 C ANISOU 1889 CA VAL A 288 5401 3206 7039 653 -287 -185 C ATOM 1890 C VAL A 288 -11.626 15.820 -47.035 1.00 38.15 C ANISOU 1890 C VAL A 288 5113 2761 6622 507 -306 -172 C ATOM 1891 O VAL A 288 -11.286 16.217 -48.159 1.00 35.30 O ANISOU 1891 O VAL A 288 4842 2335 6236 491 -370 -145 O ATOM 1892 CB VAL A 288 -12.221 17.376 -45.117 1.00 42.61 C ANISOU 1892 CB VAL A 288 5672 3312 7206 725 -220 -234 C ATOM 1893 CG1 VAL A 288 -10.955 18.100 -45.557 1.00 45.73 C ANISOU 1893 CG1 VAL A 288 6249 3557 7569 685 -246 -238 C ATOM 1894 CG2 VAL A 288 -13.303 18.323 -44.687 1.00 41.84 C ANISOU 1894 CG2 VAL A 288 5521 3240 7136 901 -210 -250 C ATOM 1895 N PHE A 289 -11.038 14.782 -46.445 1.00 37.01 N ANISOU 1895 N PHE A 289 4950 2638 6473 406 -245 -186 N ATOM 1896 CA PHE A 289 -10.033 14.005 -47.127 1.00 37.15 C ANISOU 1896 CA PHE A 289 5038 2610 6469 286 -247 -177 C ATOM 1897 C PHE A 289 -10.509 13.522 -48.498 1.00 37.68 C ANISOU 1897 C PHE A 289 5094 2701 6523 233 -319 -151 C ATOM 1898 O PHE A 289 -9.781 13.638 -49.522 1.00 36.66 O ANISOU 1898 O PHE A 289 5071 2504 6354 187 -348 -140 O ATOM 1899 CB PHE A 289 -9.548 12.808 -46.287 1.00 36.63 C ANISOU 1899 CB PHE A 289 4936 2572 6410 204 -177 -186 C ATOM 1900 CG PHE A 289 -8.323 12.137 -46.875 1.00 35.82 C ANISOU 1900 CG PHE A 289 4915 2405 6292 110 -164 -182 C ATOM 1901 CD1 PHE A 289 -8.439 11.207 -47.851 1.00 34.19 C ANISOU 1901 CD1 PHE A 289 4709 2203 6077 34 -185 -174 C ATOM 1902 CD2 PHE A 289 -7.075 12.509 -46.489 1.00 35.89 C ANISOU 1902 CD2 PHE A 289 4998 2351 6290 102 -131 -191 C ATOM 1903 CE1 PHE A 289 -7.316 10.709 -48.456 1.00 34.05 C ANISOU 1903 CE1 PHE A 289 4772 2124 6042 -28 -161 -177 C ATOM 1904 CE2 PHE A 289 -5.950 11.967 -47.040 1.00 34.85 C ANISOU 1904 CE2 PHE A 289 4919 2172 6149 33 -111 -185 C ATOM 1905 CZ PHE A 289 -6.068 11.039 -48.057 1.00 32.83 C ANISOU 1905 CZ PHE A 289 4670 1917 5885 -25 -118 -179 C ATOM 1906 N ILE A 290 -11.733 12.985 -48.529 1.00 39.15 N ANISOU 1906 N ILE A 290 5152 2991 6734 232 -349 -140 N ATOM 1907 CA ILE A 290 -12.283 12.427 -49.745 1.00 40.32 C ANISOU 1907 CA ILE A 290 5281 3177 6862 165 -431 -120 C ATOM 1908 C ILE A 290 -12.594 13.478 -50.806 1.00 40.02 C ANISOU 1908 C ILE A 290 5295 3117 6793 236 -528 -90 C ATOM 1909 O ILE A 290 -12.290 13.307 -51.971 1.00 38.52 O ANISOU 1909 O ILE A 290 5193 2896 6548 173 -583 -78 O ATOM 1910 CB ILE A 290 -13.480 11.524 -49.405 1.00 42.98 C ANISOU 1910 CB ILE A 290 5454 3639 7239 120 -440 -114 C ATOM 1911 CG1 ILE A 290 -12.925 10.251 -48.764 1.00 43.41 C ANISOU 1911 CG1 ILE A 290 5516 3676 7303 8 -357 -133 C ATOM 1912 CG2 ILE A 290 -14.293 11.184 -50.633 1.00 43.71 C ANISOU 1912 CG2 ILE A 290 5507 3790 7311 62 -553 -94 C ATOM 1913 CD1 ILE A 290 -14.020 9.344 -48.235 1.00 47.08 C ANISOU 1913 CD1 ILE A 290 5829 4252 7809 -55 -345 -121 C ATOM 1914 N VAL A 291 -13.211 14.576 -50.398 1.00 39.05 N ANISOU 1914 N VAL A 291 5131 3007 6700 376 -547 -76 N ATOM 1915 CA VAL A 291 -13.559 15.637 -51.343 1.00 41.96 C ANISOU 1915 CA VAL A 291 5555 3344 7044 465 -645 -34 C ATOM 1916 C VAL A 291 -12.300 16.289 -51.921 1.00 39.58 C ANISOU 1916 C VAL A 291 5452 2901 6686 441 -636 -27 C ATOM 1917 O VAL A 291 -12.240 16.582 -53.100 1.00 40.30 O ANISOU 1917 O VAL A 291 5630 2962 6721 424 -714 12 O ATOM 1918 CB VAL A 291 -14.453 16.680 -50.649 1.00 42.42 C ANISOU 1918 CB VAL A 291 5531 3429 7156 643 -649 -26 C ATOM 1919 CG1 VAL A 291 -14.546 17.938 -51.487 1.00 45.77 C ANISOU 1919 CG1 VAL A 291 6060 3772 7557 753 -737 22 C ATOM 1920 CG2 VAL A 291 -15.828 16.045 -50.365 1.00 43.51 C ANISOU 1920 CG2 VAL A 291 5447 3736 7347 660 -671 -16 C ATOM 1921 N CYS A 292 -11.281 16.482 -51.083 1.00 39.33 N ANISOU 1921 N CYS A 292 5488 2792 6665 427 -543 -61 N ATOM 1922 CA CYS A 292 -10.057 17.169 -51.494 1.00 38.94 C ANISOU 1922 CA CYS A 292 5606 2616 6573 395 -525 -53 C ATOM 1923 C CYS A 292 -9.152 16.391 -52.418 1.00 39.31 C ANISOU 1923 C CYS A 292 5726 2646 6564 261 -511 -48 C ATOM 1924 O CYS A 292 -8.602 16.952 -53.365 1.00 39.36 O ANISOU 1924 O CYS A 292 5857 2583 6514 236 -535 -15 O ATOM 1925 CB CYS A 292 -9.284 17.603 -50.260 1.00 40.07 C ANISOU 1925 CB CYS A 292 5782 2699 6746 412 -442 -93 C ATOM 1926 SG CYS A 292 -10.110 19.096 -49.461 1.00 43.58 S ANISOU 1926 SG CYS A 292 6235 3094 7228 597 -459 -102 S ATOM 1927 N TRP A 293 -9.020 15.084 -52.148 1.00 37.57 N ANISOU 1927 N TRP A 293 5435 2486 6356 177 -464 -80 N ATOM 1928 CA TRP A 293 -8.051 14.246 -52.823 1.00 38.88 C ANISOU 1928 CA TRP A 293 5668 2627 6479 65 -421 -92 C ATOM 1929 C TRP A 293 -8.561 13.306 -53.949 1.00 40.59 C ANISOU 1929 C TRP A 293 5887 2892 6642 -8 -473 -92 C ATOM 1930 O TRP A 293 -7.784 12.909 -54.845 1.00 41.34 O ANISOU 1930 O TRP A 293 6081 2951 6674 -83 -446 -99 O ATOM 1931 CB TRP A 293 -7.336 13.418 -51.796 1.00 37.63 C ANISOU 1931 CB TRP A 293 5462 2471 6364 25 -329 -127 C ATOM 1932 CG TRP A 293 -6.209 14.113 -51.174 1.00 38.46 C ANISOU 1932 CG TRP A 293 5619 2511 6482 34 -273 -130 C ATOM 1933 CD1 TRP A 293 -6.000 14.320 -49.835 1.00 37.57 C ANISOU 1933 CD1 TRP A 293 5462 2400 6415 69 -234 -149 C ATOM 1934 CD2 TRP A 293 -5.014 14.542 -51.836 1.00 37.03 C ANISOU 1934 CD2 TRP A 293 5541 2263 6265 -15 -243 -116 C ATOM 1935 NE1 TRP A 293 -4.785 14.926 -49.652 1.00 40.18 N ANISOU 1935 NE1 TRP A 293 5861 2666 6740 42 -199 -148 N ATOM 1936 CE2 TRP A 293 -4.143 15.034 -50.854 1.00 38.45 C ANISOU 1936 CE2 TRP A 293 5723 2408 6479 -13 -197 -125 C ATOM 1937 CE3 TRP A 293 -4.602 14.553 -53.152 1.00 38.81 C ANISOU 1937 CE3 TRP A 293 5857 2463 6426 -67 -246 -95 C ATOM 1938 CZ2 TRP A 293 -2.902 15.592 -51.160 1.00 39.91 C ANISOU 1938 CZ2 TRP A 293 5981 2537 6648 -67 -162 -110 C ATOM 1939 CZ3 TRP A 293 -3.332 15.138 -53.469 1.00 40.27 C ANISOU 1939 CZ3 TRP A 293 6123 2589 6589 -114 -194 -77 C ATOM 1940 CH2 TRP A 293 -2.490 15.584 -52.466 1.00 38.05 C ANISOU 1940 CH2 TRP A 293 5820 2280 6356 -119 -152 -84 C ATOM 1941 N THR A 294 -9.837 12.906 -53.881 1.00 39.96 N ANISOU 1941 N THR A 294 5699 2900 6585 5 -540 -91 N ATOM 1942 CA THR A 294 -10.378 11.962 -54.836 1.00 38.62 C ANISOU 1942 CA THR A 294 5528 2781 6366 -84 -600 -100 C ATOM 1943 C THR A 294 -10.318 12.576 -56.232 1.00 38.75 C ANISOU 1943 C THR A 294 5666 2773 6283 -90 -679 -67 C ATOM 1944 O THR A 294 -10.006 11.883 -57.189 1.00 37.17 O ANISOU 1944 O THR A 294 5555 2565 6005 -183 -684 -88 O ATOM 1945 CB THR A 294 -11.864 11.522 -54.488 1.00 40.49 C ANISOU 1945 CB THR A 294 5599 3134 6653 -80 -672 -96 C ATOM 1946 OG1 THR A 294 -11.899 10.970 -53.168 1.00 39.02 O ANISOU 1946 OG1 THR A 294 5312 2969 6545 -81 -587 -118 O ATOM 1947 CG2 THR A 294 -12.361 10.507 -55.454 1.00 42.73 C ANISOU 1947 CG2 THR A 294 5892 3462 6882 -199 -743 -113 C ATOM 1948 N PRO A 295 -10.656 13.881 -56.443 1.00 38.27 N ANISOU 1948 N PRO A 295 5630 2699 6214 11 -746 -12 N ATOM 1949 CA PRO A 295 -10.759 14.382 -57.813 1.00 38.95 C ANISOU 1949 CA PRO A 295 5833 2773 6194 0 -838 34 C ATOM 1950 C PRO A 295 -9.437 14.280 -58.581 1.00 37.99 C ANISOU 1950 C PRO A 295 5881 2572 5983 -83 -760 25 C ATOM 1951 O PRO A 295 -9.413 13.790 -59.714 1.00 37.13 O ANISOU 1951 O PRO A 295 5860 2479 5767 -162 -797 20 O ATOM 1952 CB PRO A 295 -11.293 15.805 -57.628 1.00 40.43 C ANISOU 1952 CB PRO A 295 6012 2938 6412 143 -906 98 C ATOM 1953 CG PRO A 295 -12.107 15.662 -56.361 1.00 41.10 C ANISOU 1953 CG PRO A 295 5914 3089 6613 218 -890 73 C ATOM 1954 CD PRO A 295 -11.250 14.798 -55.470 1.00 38.43 C ANISOU 1954 CD PRO A 295 5557 2728 6316 141 -757 9 C ATOM 1955 N ILE A 296 -8.354 14.785 -57.994 1.00 37.29 N ANISOU 1955 N ILE A 296 5837 2401 5930 -67 -655 23 N ATOM 1956 CA ILE A 296 -7.073 14.778 -58.691 1.00 36.14 C ANISOU 1956 CA ILE A 296 5828 2194 5710 -141 -570 22 C ATOM 1957 C ILE A 296 -6.599 13.348 -58.932 1.00 37.25 C ANISOU 1957 C ILE A 296 5969 2359 5826 -235 -494 -45 C ATOM 1958 O ILE A 296 -6.112 13.034 -60.037 1.00 36.44 O ANISOU 1958 O ILE A 296 5985 2247 5615 -302 -469 -52 O ATOM 1959 CB ILE A 296 -6.006 15.671 -58.053 1.00 34.98 C ANISOU 1959 CB ILE A 296 5717 1964 5608 -120 -484 40 C ATOM 1960 CG1 ILE A 296 -4.745 15.812 -58.929 1.00 34.48 C ANISOU 1960 CG1 ILE A 296 5786 1853 5461 -202 -400 58 C ATOM 1961 CG2 ILE A 296 -5.613 15.220 -56.655 1.00 34.94 C ANISOU 1961 CG2 ILE A 296 5599 1964 5714 -108 -405 -9 C ATOM 1962 CD1 ILE A 296 -5.043 16.182 -60.371 1.00 35.10 C ANISOU 1962 CD1 ILE A 296 6000 1931 5404 -229 -468 110 C ATOM 1963 N HIS A 297 -6.817 12.475 -57.946 1.00 36.32 N ANISOU 1963 N HIS A 297 5732 2270 5799 -235 -461 -92 N ATOM 1964 CA HIS A 297 -6.457 11.061 -58.117 1.00 36.34 C ANISOU 1964 CA HIS A 297 5744 2276 5789 -313 -395 -155 C ATOM 1965 C HIS A 297 -7.129 10.369 -59.252 1.00 39.22 C ANISOU 1965 C HIS A 297 6172 2675 6054 -384 -468 -180 C ATOM 1966 O HIS A 297 -6.481 9.627 -60.009 1.00 39.70 O ANISOU 1966 O HIS A 297 6339 2706 6040 -449 -404 -224 O ATOM 1967 CB HIS A 297 -6.596 10.296 -56.840 1.00 34.06 C ANISOU 1967 CB HIS A 297 5331 2000 5610 -302 -351 -186 C ATOM 1968 CG HIS A 297 -5.425 10.490 -55.937 1.00 35.01 C ANISOU 1968 CG HIS A 297 5431 2076 5794 -271 -243 -185 C ATOM 1969 ND1 HIS A 297 -4.165 10.036 -56.253 1.00 38.17 N ANISOU 1969 ND1 HIS A 297 5894 2434 6175 -304 -138 -206 N ATOM 1970 CD2 HIS A 297 -5.304 11.124 -54.752 1.00 35.28 C ANISOU 1970 CD2 HIS A 297 5389 2109 5907 -212 -229 -166 C ATOM 1971 CE1 HIS A 297 -3.321 10.387 -55.315 1.00 36.74 C ANISOU 1971 CE1 HIS A 297 5662 2235 6062 -271 -75 -193 C ATOM 1972 NE2 HIS A 297 -3.988 11.056 -54.394 1.00 37.20 N ANISOU 1972 NE2 HIS A 297 5648 2314 6174 -221 -132 -172 N ATOM 1973 N ILE A 298 -8.429 10.605 -59.397 1.00 40.49 N ANISOU 1973 N ILE A 298 6272 2903 6211 -371 -604 -154 N ATOM 1974 CA ILE A 298 -9.185 9.967 -60.418 1.00 42.48 C ANISOU 1974 CA ILE A 298 6570 3202 6368 -450 -702 -176 C ATOM 1975 C ILE A 298 -8.842 10.562 -61.757 1.00 44.00 C ANISOU 1975 C ILE A 298 6926 3379 6412 -469 -736 -147 C ATOM 1976 O ILE A 298 -8.742 9.858 -62.769 1.00 43.48 O ANISOU 1976 O ILE A 298 6979 3314 6228 -557 -744 -191 O ATOM 1977 CB ILE A 298 -10.702 10.075 -60.103 1.00 45.67 C ANISOU 1977 CB ILE A 298 6824 3705 6825 -429 -844 -147 C ATOM 1978 CG1 ILE A 298 -10.992 9.196 -58.855 1.00 46.95 C ANISOU 1978 CG1 ILE A 298 6842 3884 7113 -447 -787 -185 C ATOM 1979 CG2 ILE A 298 -11.586 9.715 -61.317 1.00 46.47 C ANISOU 1979 CG2 ILE A 298 6971 3875 6811 -512 -990 -151 C ATOM 1980 CD1 ILE A 298 -10.683 7.719 -59.008 1.00 51.01 C ANISOU 1980 CD1 ILE A 298 7412 4361 7610 -566 -728 -260 C ATOM 1981 N TYR A 299 -8.666 11.883 -61.778 1.00 41.01 N ANISOU 1981 N TYR A 299 6572 2979 6030 -388 -756 -71 N ATOM 1982 CA TYR A 299 -8.339 12.565 -62.989 1.00 42.28 C ANISOU 1982 CA TYR A 299 6894 3120 6048 -403 -786 -23 C ATOM 1983 C TYR A 299 -6.990 12.067 -63.536 1.00 41.71 C ANISOU 1983 C TYR A 299 6957 2993 5898 -475 -632 -69 C ATOM 1984 O TYR A 299 -6.867 11.796 -64.728 1.00 43.97 O ANISOU 1984 O TYR A 299 7386 3290 6031 -542 -643 -82 O ATOM 1985 CB TYR A 299 -8.275 14.051 -62.727 1.00 43.38 C ANISOU 1985 CB TYR A 299 7041 3219 6222 -304 -812 67 C ATOM 1986 CG TYR A 299 -8.664 14.951 -63.875 1.00 45.10 C ANISOU 1986 CG TYR A 299 7386 3441 6310 -288 -930 153 C ATOM 1987 CD1 TYR A 299 -8.369 14.643 -65.165 1.00 47.18 C ANISOU 1987 CD1 TYR A 299 7808 3715 6402 -376 -937 152 C ATOM 1988 CD2 TYR A 299 -9.290 16.185 -63.636 1.00 45.79 C ANISOU 1988 CD2 TYR A 299 7446 3510 6442 -173 -1028 241 C ATOM 1989 CE1 TYR A 299 -8.719 15.488 -66.197 1.00 49.51 C ANISOU 1989 CE1 TYR A 299 8230 4016 6567 -362 -1050 243 C ATOM 1990 CE2 TYR A 299 -9.649 17.019 -64.666 1.00 46.90 C ANISOU 1990 CE2 TYR A 299 7709 3645 6466 -147 -1144 334 C ATOM 1991 CZ TYR A 299 -9.324 16.706 -65.937 1.00 49.15 C ANISOU 1991 CZ TYR A 299 8154 3947 6575 -245 -1154 342 C ATOM 1992 OH TYR A 299 -9.616 17.598 -66.996 1.00 53.56 O ANISOU 1992 OH TYR A 299 8858 4495 6998 -222 -1270 450 O ATOM 1993 N VAL A 300 -6.004 11.893 -62.664 1.00 38.94 N ANISOU 1993 N VAL A 300 6555 2594 5647 -458 -488 -97 N ATOM 1994 CA VAL A 300 -4.725 11.444 -63.116 1.00 39.54 C ANISOU 1994 CA VAL A 300 6726 2631 5667 -506 -336 -135 C ATOM 1995 C VAL A 300 -4.871 10.002 -63.759 1.00 42.28 C ANISOU 1995 C VAL A 300 7136 2990 5937 -581 -316 -229 C ATOM 1996 O VAL A 300 -4.306 9.724 -64.810 1.00 42.11 O ANISOU 1996 O VAL A 300 7259 2959 5781 -632 -251 -257 O ATOM 1997 CB VAL A 300 -3.703 11.454 -61.957 1.00 37.37 C ANISOU 1997 CB VAL A 300 6353 2317 5529 -469 -205 -144 C ATOM 1998 CG1 VAL A 300 -2.512 10.606 -62.283 1.00 40.16 C ANISOU 1998 CG1 VAL A 300 6756 2648 5853 -507 -46 -201 C ATOM 1999 CG2 VAL A 300 -3.225 12.849 -61.649 1.00 37.98 C ANISOU 1999 CG2 VAL A 300 6432 2363 5638 -432 -196 -66 C ATOM 2000 N ILE A 301 -5.635 9.118 -63.119 1.00 43.36 N ANISOU 2000 N ILE A 301 7175 3145 6156 -591 -367 -277 N ATOM 2001 CA ILE A 301 -5.877 7.773 -63.705 1.00 46.14 C ANISOU 2001 CA ILE A 301 7604 3490 6439 -675 -364 -369 C ATOM 2002 C ILE A 301 -6.604 7.849 -65.033 1.00 47.36 C ANISOU 2002 C ILE A 301 7886 3688 6419 -744 -489 -371 C ATOM 2003 O ILE A 301 -6.272 7.140 -65.992 1.00 49.21 O ANISOU 2003 O ILE A 301 8277 3902 6521 -813 -444 -440 O ATOM 2004 CB ILE A 301 -6.725 6.890 -62.804 1.00 46.27 C ANISOU 2004 CB ILE A 301 7494 3516 6570 -695 -418 -405 C ATOM 2005 CG1 ILE A 301 -6.075 6.700 -61.438 1.00 46.79 C ANISOU 2005 CG1 ILE A 301 7439 3542 6796 -630 -306 -402 C ATOM 2006 CG2 ILE A 301 -6.990 5.492 -63.433 1.00 48.15 C ANISOU 2006 CG2 ILE A 301 7835 3725 6736 -798 -422 -504 C ATOM 2007 CD1 ILE A 301 -4.573 6.482 -61.505 1.00 54.88 C ANISOU 2007 CD1 ILE A 301 8531 4502 7818 -601 -132 -427 C ATOM 2008 N ILE A 302 -7.625 8.692 -65.106 1.00 49.37 N ANISOU 2008 N ILE A 302 8083 4009 6667 -722 -652 -296 N ATOM 2009 CA ILE A 302 -8.380 8.773 -66.331 1.00 53.63 C ANISOU 2009 CA ILE A 302 8732 4605 7040 -787 -797 -287 C ATOM 2010 C ILE A 302 -7.457 9.178 -67.444 1.00 54.36 C ANISOU 2010 C ILE A 302 9023 4669 6963 -805 -718 -275 C ATOM 2011 O ILE A 302 -7.549 8.654 -68.526 1.00 54.73 O ANISOU 2011 O ILE A 302 9223 4731 6842 -889 -747 -325 O ATOM 2012 CB ILE A 302 -9.605 9.686 -66.246 1.00 54.31 C ANISOU 2012 CB ILE A 302 8710 4773 7152 -736 -991 -193 C ATOM 2013 CG1 ILE A 302 -10.573 9.025 -65.280 1.00 58.83 C ANISOU 2013 CG1 ILE A 302 9090 5394 7870 -747 -1055 -223 C ATOM 2014 CG2 ILE A 302 -10.259 9.795 -67.606 1.00 56.34 C ANISOU 2014 CG2 ILE A 302 9096 5094 7217 -803 -1147 -173 C ATOM 2015 CD1 ILE A 302 -11.764 9.855 -64.936 1.00 59.62 C ANISOU 2015 CD1 ILE A 302 9032 5582 8038 -672 -1216 -137 C ATOM 2016 N LYS A 303 -6.516 10.077 -67.168 1.00 52.85 N ANISOU 2016 N LYS A 303 8835 4436 6811 -739 -607 -214 N ATOM 2017 CA LYS A 303 -5.650 10.564 -68.255 1.00 56.07 C ANISOU 2017 CA LYS A 303 9427 4827 7051 -766 -525 -185 C ATOM 2018 C LYS A 303 -4.646 9.502 -68.634 1.00 50.28 C ANISOU 2018 C LYS A 303 8791 4056 6257 -816 -344 -291 C ATOM 2019 O LYS A 303 -4.123 9.546 -69.696 1.00 49.38 O ANISOU 2019 O LYS A 303 8844 3945 5972 -861 -279 -299 O ATOM 2020 CB LYS A 303 -4.934 11.869 -67.919 1.00 53.89 C ANISOU 2020 CB LYS A 303 9134 4514 6828 -703 -461 -83 C ATOM 2021 CG LYS A 303 -5.926 13.012 -67.951 1.00 63.36 C ANISOU 2021 CG LYS A 303 10310 5736 8027 -649 -644 27 C ATOM 2022 CD LYS A 303 -5.385 14.317 -67.377 1.00 72.25 C ANISOU 2022 CD LYS A 303 11409 6802 9241 -581 -600 123 C ATOM 2023 CE LYS A 303 -4.199 14.791 -68.182 1.00 77.07 C ANISOU 2023 CE LYS A 303 12179 7376 9729 -635 -465 162 C ATOM 2024 NZ LYS A 303 -3.724 16.085 -67.655 1.00 84.32 N ANISOU 2024 NZ LYS A 303 13083 8224 10729 -592 -438 257 N ATOM 2025 N ALA A 304 -4.315 8.618 -67.701 1.00 47.78 N ANISOU 2025 N ALA A 304 8366 3701 6088 -795 -250 -364 N ATOM 2026 CA ALA A 304 -3.443 7.535 -68.040 1.00 52.53 C ANISOU 2026 CA ALA A 304 9057 4258 6644 -822 -84 -468 C ATOM 2027 C ALA A 304 -4.136 6.613 -69.067 1.00 55.46 C ANISOU 2027 C ALA A 304 9586 4638 6849 -915 -163 -559 C ATOM 2028 O ALA A 304 -3.472 6.009 -69.867 1.00 62.36 O ANISOU 2028 O ALA A 304 10615 5483 7595 -946 -41 -637 O ATOM 2029 CB ALA A 304 -3.008 6.777 -66.820 1.00 49.73 C ANISOU 2029 CB ALA A 304 8561 3853 6480 -771 14 -515 C ATOM 2030 N LEU A 305 -5.473 6.555 -69.057 1.00 58.10 N ANISOU 2030 N LEU A 305 9878 5018 7179 -961 -368 -548 N ATOM 2031 CA LEU A 305 -6.216 5.502 -69.737 1.00 57.58 C ANISOU 2031 CA LEU A 305 9923 4954 6999 -1067 -460 -648 C ATOM 2032 C LEU A 305 -6.796 5.919 -71.038 1.00 62.35 C ANISOU 2032 C LEU A 305 10684 5627 7379 -1140 -600 -625 C ATOM 2033 O LEU A 305 -6.836 5.099 -71.960 1.00 64.42 O ANISOU 2033 O LEU A 305 11128 5875 7474 -1232 -599 -726 O ATOM 2034 CB LEU A 305 -7.341 4.997 -68.881 1.00 54.12 C ANISOU 2034 CB LEU A 305 9324 4536 6704 -1097 -599 -657 C ATOM 2035 CG LEU A 305 -6.842 4.111 -67.775 1.00 53.97 C ANISOU 2035 CG LEU A 305 9211 4432 6862 -1063 -463 -714 C ATOM 2036 CD1 LEU A 305 -8.014 4.056 -66.837 1.00 54.75 C ANISOU 2036 CD1 LEU A 305 9117 4579 7106 -1078 -608 -676 C ATOM 2037 CD2 LEU A 305 -6.427 2.670 -68.194 1.00 55.36 C ANISOU 2037 CD2 LEU A 305 9547 4511 6977 -1128 -358 -856 C ATOM 2038 N ILE A 306 -7.303 7.155 -71.119 1.00 59.72 N ANISOU 2038 N ILE A 306 10293 5364 7034 -1099 -732 -496 N ATOM 2039 CA ILE A 306 -7.967 7.651 -72.324 1.00 67.36 C ANISOU 2039 CA ILE A 306 11399 6408 7788 -1158 -900 -448 C ATOM 2040 C ILE A 306 -7.402 9.004 -72.731 1.00 72.46 C ANISOU 2040 C ILE A 306 12109 7062 8362 -1092 -865 -321 C ATOM 2041 O ILE A 306 -6.665 9.606 -71.959 1.00 77.44 O ANISOU 2041 O ILE A 306 12644 7646 9134 -1007 -739 -268 O ATOM 2042 CB ILE A 306 -9.491 7.708 -72.128 1.00 71.40 C ANISOU 2042 CB ILE A 306 11775 7007 8348 -1186 -1158 -409 C ATOM 2043 CG1 ILE A 306 -9.917 9.059 -71.588 1.00 74.06 C ANISOU 2043 CG1 ILE A 306 11960 7386 8794 -1069 -1254 -257 C ATOM 2044 CG2 ILE A 306 -9.928 6.621 -71.149 1.00 75.06 C ANISOU 2044 CG2 ILE A 306 12086 7446 8986 -1221 -1153 -497 C ATOM 2045 CD1 ILE A 306 -11.307 9.066 -70.987 1.00 79.23 C ANISOU 2045 CD1 ILE A 306 12405 8126 9574 -1057 -1455 -222 C ATOM 2046 N THR A 307 -7.758 9.471 -73.936 1.00 76.06 N ANISOU 2046 N THR A 307 12732 7574 8591 -1142 -983 -269 N ATOM 2047 CA THR A 307 -7.366 10.787 -74.453 1.00 83.38 C ANISOU 2047 CA THR A 307 13751 8506 9424 -1095 -979 -130 C ATOM 2048 C THR A 307 -8.588 11.696 -74.479 1.00 87.57 C ANISOU 2048 C THR A 307 14204 9104 9967 -1048 -1236 -1 C ATOM 2049 O THR A 307 -9.507 11.485 -75.266 1.00100.05 O ANISOU 2049 O THR A 307 15852 10763 11398 -1110 -1431 1 O ATOM 2050 CB THR A 307 -6.737 10.698 -75.871 1.00 94.39 C ANISOU 2050 CB THR A 307 15423 9913 10528 -1178 -900 -151 C ATOM 2051 OG1 THR A 307 -5.334 10.413 -75.751 1.00103.15 O ANISOU 2051 OG1 THR A 307 16578 10958 11657 -1170 -618 -211 O ATOM 2052 CG2 THR A 307 -6.907 12.029 -76.666 1.00 91.64 C ANISOU 2052 CG2 THR A 307 15196 9598 10025 -1161 -1008 16 C ATOM 2053 N ILE A 308 -8.566 12.725 -73.627 1.00 88.08 N ANISOU 2053 N ILE A 308 14130 9133 10205 -934 -1237 106 N ATOM 2054 CA ILE A 308 -9.719 13.577 -73.368 1.00 95.18 C ANISOU 2054 CA ILE A 308 14910 10080 11176 -848 -1458 221 C ATOM 2055 C ILE A 308 -9.556 14.855 -74.186 1.00 94.74 C ANISOU 2055 C ILE A 308 15016 10005 10975 -810 -1513 373 C ATOM 2056 O ILE A 308 -8.448 15.378 -74.286 1.00 94.23 O ANISOU 2056 O ILE A 308 15060 9863 10881 -810 -1339 408 O ATOM 2057 CB ILE A 308 -9.929 13.838 -71.836 1.00 96.11 C ANISOU 2057 CB ILE A 308 14776 10163 11580 -737 -1430 229 C ATOM 2058 CG1 ILE A 308 -9.072 14.992 -71.278 1.00 94.82 C ANISOU 2058 CG1 ILE A 308 14615 9899 11512 -646 -1304 316 C ATOM 2059 CG2 ILE A 308 -9.717 12.535 -71.048 1.00 94.43 C ANISOU 2059 CG2 ILE A 308 14448 9940 11491 -789 -1314 83 C ATOM 2060 CD1 ILE A 308 -7.854 14.560 -70.490 1.00 97.74 C ANISOU 2060 CD1 ILE A 308 14942 10196 11997 -662 -1064 235 C ATOM 2061 N PRO A 309 -10.636 15.394 -74.800 1.00 96.05 N ANISOU 2061 N PRO A 309 15204 10244 11047 -779 -1756 475 N ATOM 2062 CA PRO A 309 -10.484 16.512 -75.733 1.00 98.37 C ANISOU 2062 CA PRO A 309 15693 10516 11166 -755 -1817 625 C ATOM 2063 C PRO A 309 -9.975 17.702 -74.952 1.00 90.19 C ANISOU 2063 C PRO A 309 14611 9364 10293 -638 -1726 727 C ATOM 2064 O PRO A 309 -10.481 17.950 -73.860 1.00 89.39 O ANISOU 2064 O PRO A 309 14302 9246 10416 -530 -1767 732 O ATOM 2065 CB PRO A 309 -11.918 16.747 -76.261 1.00100.24 C ANISOU 2065 CB PRO A 309 15893 10864 11330 -717 -2123 709 C ATOM 2066 CG PRO A 309 -12.825 16.117 -75.255 1.00 99.09 C ANISOU 2066 CG PRO A 309 15467 10781 11400 -679 -2205 632 C ATOM 2067 CD PRO A 309 -12.043 15.013 -74.576 1.00 95.37 C ANISOU 2067 CD PRO A 309 14942 10266 11029 -760 -1983 465 C ATOM 2068 N GLU A 310 -8.942 18.378 -75.459 1.00 90.06 N ANISOU 2068 N GLU A 310 14786 9267 10167 -671 -1588 798 N ATOM 2069 CA GLU A 310 -8.520 19.634 -74.857 1.00 93.54 C ANISOU 2069 CA GLU A 310 15218 9585 10736 -578 -1532 911 C ATOM 2070 C GLU A 310 -9.677 20.616 -75.030 1.00 90.20 C ANISOU 2070 C GLU A 310 14790 9166 10316 -450 -1780 1059 C ATOM 2071 O GLU A 310 -10.145 20.824 -76.144 1.00 96.29 O ANISOU 2071 O GLU A 310 15715 9992 10880 -472 -1931 1147 O ATOM 2072 CB GLU A 310 -7.246 20.168 -75.506 1.00103.16 C ANISOU 2072 CB GLU A 310 16653 10728 11814 -664 -1350 972 C ATOM 2073 CG GLU A 310 -6.665 21.400 -74.815 1.00108.71 C ANISOU 2073 CG GLU A 310 17355 11289 12662 -601 -1269 1073 C ATOM 2074 CD GLU A 310 -7.175 22.721 -75.379 1.00113.33 C ANISOU 2074 CD GLU A 310 18093 11805 13164 -528 -1429 1264 C ATOM 2075 OE1 GLU A 310 -7.088 22.924 -76.611 1.00119.27 O ANISOU 2075 OE1 GLU A 310 19063 12582 13670 -598 -1468 1351 O ATOM 2076 OE2 GLU A 310 -7.632 23.575 -74.585 1.00114.91 O ANISOU 2076 OE2 GLU A 310 18206 11915 13538 -397 -1509 1329 O ATOM 2077 N THR A 311 -10.158 21.174 -73.912 1.00 85.88 N ANISOU 2077 N THR A 311 14062 8566 10002 -309 -1824 1083 N ATOM 2078 CA THR A 311 -11.230 22.183 -73.886 1.00 82.49 C ANISOU 2078 CA THR A 311 13600 8121 9621 -148 -2039 1221 C ATOM 2079 C THR A 311 -11.048 23.044 -72.641 1.00 78.41 C ANISOU 2079 C THR A 311 12981 7471 9342 -19 -1961 1242 C ATOM 2080 O THR A 311 -10.276 22.710 -71.740 1.00 73.09 O ANISOU 2080 O THR A 311 12221 6749 8800 -59 -1775 1138 O ATOM 2081 CB THR A 311 -12.662 21.568 -73.847 1.00 83.79 C ANISOU 2081 CB THR A 311 13571 8443 9823 -89 -2259 1192 C ATOM 2082 OG1 THR A 311 -12.773 20.645 -72.739 1.00 80.48 O ANISOU 2082 OG1 THR A 311 12916 8070 9594 -99 -2172 1040 O ATOM 2083 CG2 THR A 311 -13.004 20.851 -75.156 1.00 83.88 C ANISOU 2083 CG2 THR A 311 13704 8586 9580 -214 -2387 1186 C ATOM 2084 N THR A 312 -11.787 24.151 -72.591 1.00 77.02 N ANISOU 2084 N THR A 312 12816 7233 9215 144 -2113 1375 N ATOM 2085 CA THR A 312 -11.771 25.048 -71.457 1.00 76.29 C ANISOU 2085 CA THR A 312 12647 7005 9334 286 -2064 1395 C ATOM 2086 C THR A 312 -12.156 24.308 -70.191 1.00 75.23 C ANISOU 2086 C THR A 312 12235 6941 9408 332 -2014 1252 C ATOM 2087 O THR A 312 -11.450 24.393 -69.171 1.00 70.09 O ANISOU 2087 O THR A 312 11532 6201 8897 325 -1848 1178 O ATOM 2088 CB THR A 312 -12.678 26.242 -71.736 1.00 75.53 C ANISOU 2088 CB THR A 312 12610 6845 9244 474 -2258 1560 C ATOM 2089 OG1 THR A 312 -12.094 26.939 -72.828 1.00 77.77 O ANISOU 2089 OG1 THR A 312 13179 7036 9332 407 -2265 1695 O ATOM 2090 CG2 THR A 312 -12.811 27.204 -70.524 1.00 75.08 C ANISOU 2090 CG2 THR A 312 12478 6637 9412 650 -2218 1570 C ATOM 2091 N PHE A 313 -13.245 23.534 -70.287 1.00 78.98 N ANISOU 2091 N PHE A 313 12537 7584 9889 359 -2158 1214 N ATOM 2092 CA PHE A 313 -13.753 22.731 -69.181 1.00 79.62 C ANISOU 2092 CA PHE A 313 12350 7756 10148 388 -2126 1089 C ATOM 2093 C PHE A 313 -12.679 21.744 -68.628 1.00 73.27 C ANISOU 2093 C PHE A 313 11520 6940 9377 232 -1907 941 C ATOM 2094 O PHE A 313 -12.489 21.648 -67.406 1.00 73.80 O ANISOU 2094 O PHE A 313 11450 6973 9618 274 -1795 864 O ATOM 2095 CB PHE A 313 -15.051 21.993 -69.577 1.00 80.59 C ANISOU 2095 CB PHE A 313 12308 8073 10242 397 -2323 1081 C ATOM 2096 CG PHE A 313 -15.627 21.179 -68.447 1.00 82.03 C ANISOU 2096 CG PHE A 313 12210 8351 10605 416 -2288 966 C ATOM 2097 CD1 PHE A 313 -16.246 21.811 -67.364 1.00 82.86 C ANISOU 2097 CD1 PHE A 313 12143 8436 10906 601 -2292 982 C ATOM 2098 CD2 PHE A 313 -15.473 19.801 -68.419 1.00 78.73 C ANISOU 2098 CD2 PHE A 313 11723 8028 10163 249 -2228 839 C ATOM 2099 CE1 PHE A 313 -16.737 21.064 -66.303 1.00 82.83 C ANISOU 2099 CE1 PHE A 313 11891 8525 11058 608 -2241 881 C ATOM 2100 CE2 PHE A 313 -15.968 19.057 -67.371 1.00 76.79 C ANISOU 2100 CE2 PHE A 313 11237 7861 10079 254 -2187 744 C ATOM 2101 CZ PHE A 313 -16.596 19.684 -66.309 1.00 78.89 C ANISOU 2101 CZ PHE A 313 11323 8123 10529 428 -2191 768 C ATOM 2102 N GLN A 314 -11.968 21.073 -69.545 1.00 68.99 N ANISOU 2102 N GLN A 314 11124 6426 8662 66 -1847 908 N ATOM 2103 CA GLN A 314 -10.873 20.137 -69.237 1.00 70.52 C ANISOU 2103 CA GLN A 314 11323 6608 8864 -74 -1642 781 C ATOM 2104 C GLN A 314 -9.725 20.855 -68.512 1.00 64.55 C ANISOU 2104 C GLN A 314 10619 5706 8203 -63 -1462 787 C ATOM 2105 O GLN A 314 -9.249 20.387 -67.484 1.00 62.12 O ANISOU 2105 O GLN A 314 10189 5383 8032 -78 -1331 691 O ATOM 2106 CB GLN A 314 -10.377 19.453 -70.520 1.00 75.63 C ANISOU 2106 CB GLN A 314 12148 7305 9283 -229 -1619 759 C ATOM 2107 CG GLN A 314 -9.201 18.501 -70.361 1.00 85.70 C ANISOU 2107 CG GLN A 314 13447 8566 10551 -357 -1401 636 C ATOM 2108 CD GLN A 314 -7.843 19.202 -70.289 1.00 96.24 C ANISOU 2108 CD GLN A 314 14903 9781 11882 -388 -1215 673 C ATOM 2109 OE1 GLN A 314 -7.413 19.877 -71.247 1.00102.05 O ANISOU 2109 OE1 GLN A 314 15839 10477 12459 -429 -1209 769 O ATOM 2110 NE2 GLN A 314 -7.149 19.035 -69.143 1.00 98.39 N ANISOU 2110 NE2 GLN A 314 15054 10004 12328 -380 -1064 603 N ATOM 2111 N THR A 315 -9.287 21.989 -69.067 1.00 61.04 N ANISOU 2111 N THR A 315 10361 5153 7677 -48 -1464 906 N ATOM 2112 CA THR A 315 -8.246 22.809 -68.470 1.00 60.30 C ANISOU 2112 CA THR A 315 10334 4913 7663 -54 -1317 927 C ATOM 2113 C THR A 315 -8.643 23.330 -67.096 1.00 55.30 C ANISOU 2113 C THR A 315 9551 4217 7245 82 -1323 903 C ATOM 2114 O THR A 315 -7.915 23.122 -66.104 1.00 53.61 O ANISOU 2114 O THR A 315 9255 3966 7151 49 -1181 819 O ATOM 2115 CB THR A 315 -7.882 23.983 -69.374 1.00 61.63 C ANISOU 2115 CB THR A 315 10743 4972 7702 -66 -1343 1076 C ATOM 2116 OG1 THR A 315 -7.214 23.444 -70.501 1.00 66.03 O ANISOU 2116 OG1 THR A 315 11444 5585 8061 -217 -1274 1078 O ATOM 2117 CG2 THR A 315 -6.919 24.873 -68.692 1.00 61.82 C ANISOU 2117 CG2 THR A 315 10825 4839 7823 -81 -1211 1099 C ATOM 2118 N VAL A 316 -9.814 23.952 -67.029 1.00 52.19 N ANISOU 2118 N VAL A 316 9113 3822 6894 240 -1489 973 N ATOM 2119 CA VAL A 316 -10.256 24.492 -65.776 1.00 52.75 C ANISOU 2119 CA VAL A 316 9055 3833 7153 386 -1491 948 C ATOM 2120 C VAL A 316 -10.480 23.430 -64.715 1.00 49.95 C ANISOU 2120 C VAL A 316 8466 3585 6926 379 -1426 811 C ATOM 2121 O VAL A 316 -10.005 23.542 -63.590 1.00 48.73 O ANISOU 2121 O VAL A 316 8247 3369 6897 394 -1313 744 O ATOM 2122 CB VAL A 316 -11.504 25.341 -65.954 1.00 53.78 C ANISOU 2122 CB VAL A 316 9173 3952 7308 578 -1676 1051 C ATOM 2123 CG1 VAL A 316 -11.938 25.903 -64.629 1.00 53.58 C ANISOU 2123 CG1 VAL A 316 9023 3861 7473 740 -1654 1013 C ATOM 2124 CG2 VAL A 316 -11.149 26.469 -66.847 1.00 55.42 C ANISOU 2124 CG2 VAL A 316 9635 4019 7402 586 -1721 1194 C ATOM 2125 N SER A 317 -11.147 22.331 -65.083 1.00 51.67 N ANISOU 2125 N SER A 317 8568 3962 7102 337 -1496 765 N ATOM 2126 CA SER A 317 -11.425 21.291 -64.093 1.00 47.79 C ANISOU 2126 CA SER A 317 7861 3567 6729 323 -1439 646 C ATOM 2127 C SER A 317 -10.114 20.688 -63.557 1.00 43.83 C ANISOU 2127 C SER A 317 7378 3021 6254 197 -1245 554 C ATOM 2128 O SER A 317 -9.981 20.393 -62.375 1.00 42.32 O ANISOU 2128 O SER A 317 7058 2830 6193 218 -1160 479 O ATOM 2129 CB SER A 317 -12.398 20.300 -64.685 1.00 49.94 C ANISOU 2129 CB SER A 317 8029 4003 6944 283 -1564 626 C ATOM 2130 OG SER A 317 -11.797 19.706 -65.807 1.00 54.08 O ANISOU 2130 OG SER A 317 8702 4548 7299 132 -1547 618 O ATOM 2131 N TRP A 318 -9.100 20.569 -64.413 1.00 43.34 N ANISOU 2131 N TRP A 318 7479 2923 6066 71 -1170 567 N ATOM 2132 CA TRP A 318 -7.815 20.001 -64.028 1.00 42.04 C ANISOU 2132 CA TRP A 318 7323 2729 5921 -41 -988 490 C ATOM 2133 C TRP A 318 -7.151 20.829 -62.947 1.00 41.29 C ANISOU 2133 C TRP A 318 7217 2523 5950 1 -898 490 C ATOM 2134 O TRP A 318 -6.754 20.312 -61.908 1.00 37.99 O ANISOU 2134 O TRP A 318 6680 2116 5638 -12 -804 408 O ATOM 2135 CB TRP A 318 -6.898 19.890 -65.247 1.00 43.64 C ANISOU 2135 CB TRP A 318 7708 2918 5956 -166 -922 519 C ATOM 2136 CG TRP A 318 -5.473 19.454 -64.974 1.00 44.21 C ANISOU 2136 CG TRP A 318 7791 2962 6045 -271 -727 459 C ATOM 2137 CD1 TRP A 318 -4.378 20.215 -65.072 1.00 46.66 C ANISOU 2137 CD1 TRP A 318 8206 3186 6338 -325 -623 507 C ATOM 2138 CD2 TRP A 318 -5.009 18.154 -64.623 1.00 44.91 C ANISOU 2138 CD2 TRP A 318 7781 3113 6168 -332 -620 349 C ATOM 2139 NE1 TRP A 318 -3.265 19.495 -64.790 1.00 45.64 N ANISOU 2139 NE1 TRP A 318 8027 3076 6235 -410 -461 435 N ATOM 2140 CE2 TRP A 318 -3.618 18.229 -64.493 1.00 44.59 C ANISOU 2140 CE2 TRP A 318 7775 3028 6137 -405 -455 338 C ATOM 2141 CE3 TRP A 318 -5.631 16.949 -64.372 1.00 43.89 C ANISOU 2141 CE3 TRP A 318 7538 3069 6071 -333 -649 263 C ATOM 2142 CZ2 TRP A 318 -2.831 17.136 -64.156 1.00 45.83 C ANISOU 2142 CZ2 TRP A 318 7855 3224 6334 -457 -320 247 C ATOM 2143 CZ3 TRP A 318 -4.849 15.875 -64.039 1.00 44.76 C ANISOU 2143 CZ3 TRP A 318 7595 3197 6215 -394 -514 172 C ATOM 2144 CH2 TRP A 318 -3.471 15.961 -63.956 1.00 43.56 C ANISOU 2144 CH2 TRP A 318 7478 3002 6071 -445 -353 166 C ATOM 2145 N HIS A 319 -7.033 22.151 -63.185 1.00 42.45 N ANISOU 2145 N HIS A 319 7500 2552 6076 48 -933 585 N ATOM 2146 CA HIS A 319 -6.455 23.017 -62.169 1.00 42.33 C ANISOU 2146 CA HIS A 319 7495 2416 6171 78 -863 580 C ATOM 2147 C HIS A 319 -7.268 23.069 -60.889 1.00 42.27 C ANISOU 2147 C HIS A 319 7329 2420 6309 211 -897 523 C ATOM 2148 O HIS A 319 -6.697 23.074 -59.797 1.00 41.36 O ANISOU 2148 O HIS A 319 7156 2271 6290 198 -805 459 O ATOM 2149 CB HIS A 319 -6.157 24.420 -62.756 1.00 43.25 C ANISOU 2149 CB HIS A 319 7820 2383 6230 87 -894 696 C ATOM 2150 CG HIS A 319 -5.056 24.347 -63.739 1.00 44.33 C ANISOU 2150 CG HIS A 319 8096 2508 6239 -72 -805 738 C ATOM 2151 ND1 HIS A 319 -5.278 24.329 -65.101 1.00 48.02 N ANISOU 2151 ND1 HIS A 319 8694 3009 6543 -108 -866 818 N ATOM 2152 CD2 HIS A 319 -3.743 24.103 -63.570 1.00 43.99 C ANISOU 2152 CD2 HIS A 319 8059 2454 6200 -209 -650 701 C ATOM 2153 CE1 HIS A 319 -4.128 24.149 -65.724 1.00 48.57 C ANISOU 2153 CE1 HIS A 319 8858 3079 6519 -259 -739 829 C ATOM 2154 NE2 HIS A 319 -3.174 24.030 -64.818 1.00 46.61 N ANISOU 2154 NE2 HIS A 319 8528 2805 6377 -320 -606 761 N ATOM 2155 N PHE A 320 -8.598 23.028 -61.031 1.00 44.13 N ANISOU 2155 N PHE A 320 7486 2725 6556 332 -1027 546 N ATOM 2156 CA PHE A 320 -9.458 22.952 -59.889 1.00 44.51 C ANISOU 2156 CA PHE A 320 7363 2815 6732 458 -1047 492 C ATOM 2157 C PHE A 320 -9.178 21.685 -59.049 1.00 42.48 C ANISOU 2157 C PHE A 320 6946 2658 6535 380 -949 381 C ATOM 2158 O PHE A 320 -9.020 21.769 -57.794 1.00 40.29 O ANISOU 2158 O PHE A 320 6592 2357 6361 419 -877 321 O ATOM 2159 CB PHE A 320 -10.927 23.104 -60.305 1.00 49.91 C ANISOU 2159 CB PHE A 320 7970 3578 7415 596 -1205 547 C ATOM 2160 CG PHE A 320 -11.807 23.383 -59.141 1.00 59.64 C ANISOU 2160 CG PHE A 320 9049 4830 8782 755 -1215 510 C ATOM 2161 CD1 PHE A 320 -12.004 24.686 -58.699 1.00 62.44 C ANISOU 2161 CD1 PHE A 320 9481 5049 9194 907 -1231 548 C ATOM 2162 CD2 PHE A 320 -12.342 22.343 -58.383 1.00 65.72 C ANISOU 2162 CD2 PHE A 320 9608 5740 9623 748 -1185 429 C ATOM 2163 CE1 PHE A 320 -12.750 24.935 -57.548 1.00 66.18 C ANISOU 2163 CE1 PHE A 320 9819 5540 9787 1061 -1214 498 C ATOM 2164 CE2 PHE A 320 -13.118 22.621 -57.245 1.00 69.93 C ANISOU 2164 CE2 PHE A 320 9999 6299 10273 894 -1171 393 C ATOM 2165 CZ PHE A 320 -13.307 23.909 -56.822 1.00 61.45 C ANISOU 2165 CZ PHE A 320 9000 5099 9249 1054 -1179 422 C ATOM 2166 N CYS A 321 -9.058 20.521 -59.721 1.00 39.55 N ANISOU 2166 N CYS A 321 6546 2387 6094 267 -941 354 N ATOM 2167 CA CYS A 321 -8.778 19.290 -59.005 1.00 39.59 C ANISOU 2167 CA CYS A 321 6422 2468 6152 195 -851 261 C ATOM 2168 C CYS A 321 -7.409 19.362 -58.343 1.00 37.48 C ANISOU 2168 C CYS A 321 6197 2124 5921 126 -711 223 C ATOM 2169 O CYS A 321 -7.228 18.920 -57.206 1.00 35.40 O ANISOU 2169 O CYS A 321 5825 1881 5745 131 -643 160 O ATOM 2170 CB CYS A 321 -8.866 18.073 -59.959 1.00 41.08 C ANISOU 2170 CB CYS A 321 6609 2750 6248 86 -870 236 C ATOM 2171 SG CYS A 321 -10.618 17.842 -60.459 1.00 45.93 S ANISOU 2171 SG CYS A 321 7115 3489 6846 154 -1054 268 S ATOM 2172 N ILE A 322 -6.426 19.953 -59.033 1.00 37.58 N ANISOU 2172 N ILE A 322 6363 2054 5863 57 -668 268 N ATOM 2173 CA ILE A 322 -5.116 20.110 -58.416 1.00 37.78 C ANISOU 2173 CA ILE A 322 6410 2018 5928 -15 -546 240 C ATOM 2174 C ILE A 322 -5.222 20.979 -57.129 1.00 37.68 C ANISOU 2174 C ILE A 322 6365 1932 6020 69 -546 223 C ATOM 2175 O ILE A 322 -4.611 20.684 -56.078 1.00 34.16 O ANISOU 2175 O ILE A 322 5845 1491 5644 41 -470 165 O ATOM 2176 CB ILE A 322 -4.134 20.769 -59.391 1.00 41.87 C ANISOU 2176 CB ILE A 322 7094 2460 6353 -106 -503 306 C ATOM 2177 CG1 ILE A 322 -3.782 19.823 -60.513 1.00 43.18 C ANISOU 2177 CG1 ILE A 322 7296 2701 6411 -199 -463 300 C ATOM 2178 CG2 ILE A 322 -2.834 21.173 -58.680 1.00 44.55 C ANISOU 2178 CG2 ILE A 322 7444 2735 6750 -181 -394 290 C ATOM 2179 CD1 ILE A 322 -2.924 20.486 -61.549 1.00 42.98 C ANISOU 2179 CD1 ILE A 322 7436 2617 6277 -287 -415 374 C ATOM 2180 N ALA A 323 -5.946 22.103 -57.253 1.00 39.41 N ANISOU 2180 N ALA A 323 6660 2074 6241 173 -634 278 N ATOM 2181 CA ALA A 323 -6.108 23.006 -56.110 1.00 41.70 C ANISOU 2181 CA ALA A 323 6950 2276 6617 265 -633 254 C ATOM 2182 C ALA A 323 -6.802 22.319 -54.929 1.00 42.06 C ANISOU 2182 C ALA A 323 6819 2416 6746 341 -619 176 C ATOM 2183 O ALA A 323 -6.433 22.559 -53.789 1.00 40.44 O ANISOU 2183 O ALA A 323 6591 2173 6599 351 -565 122 O ATOM 2184 CB ALA A 323 -6.856 24.305 -56.478 1.00 40.41 C ANISOU 2184 CB ALA A 323 6906 2002 6446 392 -729 327 C ATOM 2185 N LEU A 324 -7.810 21.488 -55.225 1.00 42.93 N ANISOU 2185 N LEU A 324 6810 2650 6853 383 -672 173 N ATOM 2186 CA LEU A 324 -8.502 20.709 -54.181 1.00 43.82 C ANISOU 2186 CA LEU A 324 6746 2868 7037 432 -651 108 C ATOM 2187 C LEU A 324 -7.570 19.878 -53.343 1.00 39.85 C ANISOU 2187 C LEU A 324 6188 2391 6561 334 -546 44 C ATOM 2188 O LEU A 324 -7.704 19.856 -52.134 1.00 39.42 O ANISOU 2188 O LEU A 324 6061 2352 6566 379 -505 -5 O ATOM 2189 CB LEU A 324 -9.556 19.814 -54.776 1.00 44.04 C ANISOU 2189 CB LEU A 324 6658 3026 7048 441 -721 120 C ATOM 2190 CG LEU A 324 -10.845 20.593 -54.948 1.00 46.82 C ANISOU 2190 CG LEU A 324 6973 3393 7422 598 -826 167 C ATOM 2191 CD1 LEU A 324 -11.839 19.590 -55.529 1.00 50.74 C ANISOU 2191 CD1 LEU A 324 7334 4041 7902 574 -903 176 C ATOM 2192 CD2 LEU A 324 -11.380 21.119 -53.619 1.00 46.58 C ANISOU 2192 CD2 LEU A 324 6859 3355 7483 732 -788 126 C ATOM 2193 N GLY A 325 -6.566 19.257 -53.975 1.00 41.29 N ANISOU 2193 N GLY A 325 6415 2576 6696 206 -498 47 N ATOM 2194 CA GLY A 325 -5.528 18.505 -53.269 1.00 38.93 C ANISOU 2194 CA GLY A 325 6070 2296 6425 119 -401 -1 C ATOM 2195 C GLY A 325 -4.797 19.347 -52.222 1.00 36.36 C ANISOU 2195 C GLY A 325 5781 1893 6141 124 -361 -22 C ATOM 2196 O GLY A 325 -4.502 18.939 -51.085 1.00 38.59 O ANISOU 2196 O GLY A 325 5987 2207 6468 118 -313 -69 O ATOM 2197 N TYR A 326 -4.414 20.553 -52.626 1.00 38.22 N ANISOU 2197 N TYR A 326 6150 2019 6353 120 -381 16 N ATOM 2198 CA TYR A 326 -3.676 21.440 -51.771 1.00 38.04 C ANISOU 2198 CA TYR A 326 6190 1906 6360 100 -354 -5 C ATOM 2199 C TYR A 326 -4.578 22.084 -50.712 1.00 40.15 C ANISOU 2199 C TYR A 326 6445 2140 6669 231 -385 -45 C ATOM 2200 O TYR A 326 -4.048 22.551 -49.678 1.00 41.70 O ANISOU 2200 O TYR A 326 6669 2286 6889 215 -356 -91 O ATOM 2201 CB TYR A 326 -2.964 22.495 -52.637 1.00 39.40 C ANISOU 2201 CB TYR A 326 6523 1958 6489 32 -363 56 C ATOM 2202 CG TYR A 326 -1.855 21.797 -53.448 1.00 36.29 C ANISOU 2202 CG TYR A 326 6121 1614 6055 -107 -298 81 C ATOM 2203 CD1 TYR A 326 -0.644 21.567 -52.895 1.00 36.47 C ANISOU 2203 CD1 TYR A 326 6101 1653 6105 -208 -229 56 C ATOM 2204 CD2 TYR A 326 -2.049 21.395 -54.701 1.00 35.39 C ANISOU 2204 CD2 TYR A 326 6038 1535 5874 -126 -306 125 C ATOM 2205 CE1 TYR A 326 0.342 20.986 -53.593 1.00 35.45 C ANISOU 2205 CE1 TYR A 326 5950 1571 5947 -313 -159 78 C ATOM 2206 CE2 TYR A 326 -1.063 20.858 -55.430 1.00 35.12 C ANISOU 2206 CE2 TYR A 326 6009 1538 5796 -238 -233 142 C ATOM 2207 CZ TYR A 326 0.125 20.632 -54.879 1.00 35.04 C ANISOU 2207 CZ TYR A 326 5944 1545 5824 -324 -153 118 C ATOM 2208 OH TYR A 326 1.123 19.958 -55.572 1.00 37.33 O ANISOU 2208 OH TYR A 326 6211 1893 6081 -419 -62 129 O ATOM 2209 N ATHR A 327 -5.896 22.093 -50.982 0.62 37.63 N ANISOU 2209 N ATHR A 327 6083 1858 6356 355 -440 -30 N ATOM 2210 N BTHR A 327 -5.900 22.122 -50.939 0.38 40.29 N ANISOU 2210 N BTHR A 327 6421 2193 6695 357 -440 -32 N ATOM 2211 CA ATHR A 327 -6.930 22.544 -50.045 0.62 39.53 C ANISOU 2211 CA ATHR A 327 6279 2100 6640 503 -454 -69 C ATOM 2212 CA BTHR A 327 -6.817 22.635 -49.917 0.38 43.16 C ANISOU 2212 CA BTHR A 327 6750 2547 7101 499 -448 -75 C ATOM 2213 C ATHR A 327 -7.027 21.671 -48.793 0.62 38.23 C ANISOU 2213 C ATHR A 327 5979 2039 6506 501 -393 -136 C ATOM 2214 C BTHR A 327 -6.947 21.698 -48.731 0.38 40.62 C ANISOU 2214 C BTHR A 327 6287 2338 6809 496 -390 -139 C ATOM 2215 O ATHR A 327 -7.362 22.123 -47.697 0.62 40.04 O ANISOU 2215 O ATHR A 327 6204 2253 6758 583 -368 -188 O ATOM 2216 O BTHR A 327 -7.291 22.123 -47.626 0.38 41.75 O ANISOU 2216 O BTHR A 327 6423 2467 6974 577 -364 -192 O ATOM 2217 CB ATHR A 327 -8.315 22.720 -50.743 0.62 39.27 C ANISOU 2217 CB ATHR A 327 6203 2105 6611 638 -533 -23 C ATOM 2218 CB BTHR A 327 -8.246 22.910 -50.411 0.38 45.44 C ANISOU 2218 CB BTHR A 327 6996 2866 7402 651 -519 -39 C ATOM 2219 OG1ATHR A 327 -8.171 23.618 -51.846 0.62 39.99 O ANISOU 2219 OG1ATHR A 327 6445 2086 6663 644 -595 50 O ATOM 2220 OG1BTHR A 327 -8.916 21.661 -50.586 0.38 47.71 O ANISOU 2220 OG1BTHR A 327 7119 3314 7697 637 -525 -39 O ATOM 2221 CG2ATHR A 327 -9.390 23.298 -49.803 0.62 38.88 C ANISOU 2221 CG2ATHR A 327 6102 2059 6614 814 -534 -60 C ATOM 2222 CG2BTHR A 327 -8.245 23.725 -51.687 0.38 46.49 C ANISOU 2222 CG2BTHR A 327 7268 2902 7495 663 -593 43 C ATOM 2223 N ASN A 328 -6.649 20.421 -48.935 1.00 38.64 N ANISOU 2223 N ASN A 328 5940 2190 6553 402 -362 -136 N ATOM 2224 CA ASN A 328 -6.562 19.512 -47.805 1.00 38.97 C ANISOU 2224 CA ASN A 328 5872 2320 6615 379 -304 -183 C ATOM 2225 C ASN A 328 -5.524 20.096 -46.824 1.00 40.42 C ANISOU 2225 C ASN A 328 6131 2433 6795 336 -268 -224 C ATOM 2226 O ASN A 328 -5.724 20.085 -45.609 1.00 40.77 O ANISOU 2226 O ASN A 328 6140 2506 6844 377 -237 -273 O ATOM 2227 CB ASN A 328 -6.174 18.056 -48.261 1.00 38.78 C ANISOU 2227 CB ASN A 328 5766 2382 6585 274 -279 -169 C ATOM 2228 CG ASN A 328 -6.405 17.026 -47.175 1.00 39.71 C ANISOU 2228 CG ASN A 328 5768 2594 6727 269 -230 -200 C ATOM 2229 OD1 ASN A 328 -5.432 16.393 -46.679 1.00 43.34 O ANISOU 2229 OD1 ASN A 328 6215 3063 7187 192 -186 -210 O ATOM 2230 ND2 ASN A 328 -7.677 16.855 -46.778 1.00 37.04 N ANISOU 2230 ND2 ASN A 328 5336 2328 6408 350 -237 -208 N ATOM 2231 N SER A 329 -4.413 20.603 -47.364 1.00 39.75 N ANISOU 2231 N SER A 329 6148 2263 6693 243 -274 -202 N ATOM 2232 CA SER A 329 -3.368 21.153 -46.557 1.00 42.00 C ANISOU 2232 CA SER A 329 6497 2487 6973 175 -256 -235 C ATOM 2233 C SER A 329 -3.816 22.441 -45.880 1.00 45.50 C ANISOU 2233 C SER A 329 7050 2824 7414 262 -277 -278 C ATOM 2234 O SER A 329 -3.327 22.734 -44.796 1.00 45.50 O ANISOU 2234 O SER A 329 7081 2803 7403 234 -262 -332 O ATOM 2235 CB SER A 329 -2.085 21.377 -47.380 1.00 44.61 C ANISOU 2235 CB SER A 329 6894 2765 7292 41 -251 -193 C ATOM 2236 OG SER A 329 -1.477 20.156 -47.677 1.00 45.02 O ANISOU 2236 OG SER A 329 6842 2914 7349 -33 -212 -175 O ATOM 2237 N CYS A 330 -4.742 23.182 -46.517 1.00 43.60 N ANISOU 2237 N CYS A 330 6871 2517 7178 373 -315 -254 N ATOM 2238 CA CYS A 330 -5.389 24.331 -45.906 1.00 45.53 C ANISOU 2238 CA CYS A 330 7214 2658 7427 498 -327 -297 C ATOM 2239 C CYS A 330 -6.371 23.994 -44.787 1.00 47.43 C ANISOU 2239 C CYS A 330 7354 2989 7677 622 -288 -359 C ATOM 2240 O CYS A 330 -6.536 24.788 -43.885 1.00 41.25 O ANISOU 2240 O CYS A 330 6655 2134 6884 694 -271 -425 O ATOM 2241 CB CYS A 330 -6.187 25.130 -46.926 1.00 50.02 C ANISOU 2241 CB CYS A 330 7860 3141 8005 609 -382 -242 C ATOM 2242 SG CYS A 330 -5.158 25.777 -48.266 1.00 48.57 S ANISOU 2242 SG CYS A 330 7835 2827 7794 475 -422 -158 S ATOM 2243 N LEU A 331 -7.055 22.842 -44.870 1.00 42.32 N ANISOU 2243 N LEU A 331 6537 2498 7045 645 -271 -339 N ATOM 2244 CA LEU A 331 -8.084 22.522 -43.889 1.00 43.45 C ANISOU 2244 CA LEU A 331 6572 2740 7197 758 -225 -385 C ATOM 2245 C LEU A 331 -7.531 21.711 -42.705 1.00 42.16 C ANISOU 2245 C LEU A 331 6353 2661 7005 676 -167 -429 C ATOM 2246 O LEU A 331 -8.052 21.800 -41.622 1.00 43.66 O ANISOU 2246 O LEU A 331 6520 2891 7177 752 -117 -484 O ATOM 2247 CB LEU A 331 -9.277 21.839 -44.539 1.00 42.15 C ANISOU 2247 CB LEU A 331 6255 2695 7067 830 -242 -337 C ATOM 2248 CG LEU A 331 -9.990 22.731 -45.539 1.00 45.34 C ANISOU 2248 CG LEU A 331 6707 3027 7492 945 -310 -292 C ATOM 2249 CD1 LEU A 331 -10.968 21.862 -46.303 1.00 45.05 C ANISOU 2249 CD1 LEU A 331 6506 3130 7480 965 -347 -237 C ATOM 2250 CD2 LEU A 331 -10.730 23.915 -44.933 1.00 47.65 C ANISOU 2250 CD2 LEU A 331 7062 3241 7802 1130 -296 -335 C ATOM 2251 N ASN A 332 -6.442 20.972 -42.928 1.00 38.22 N ANISOU 2251 N ASN A 332 5840 2185 6498 527 -172 -402 N ATOM 2252 CA ASN A 332 -5.778 20.220 -41.853 1.00 40.30 C ANISOU 2252 CA ASN A 332 6060 2519 6733 447 -134 -428 C ATOM 2253 C ASN A 332 -5.501 20.980 -40.557 1.00 44.25 C ANISOU 2253 C ASN A 332 6655 2975 7185 466 -116 -504 C ATOM 2254 O ASN A 332 -5.757 20.455 -39.485 1.00 44.40 O ANISOU 2254 O ASN A 332 6620 3082 7169 483 -71 -533 O ATOM 2255 CB ASN A 332 -4.528 19.520 -42.368 1.00 38.67 C ANISOU 2255 CB ASN A 332 5838 2322 6534 303 -149 -385 C ATOM 2256 CG ASN A 332 -4.888 18.298 -43.176 1.00 39.40 C ANISOU 2256 CG ASN A 332 5815 2499 6654 283 -140 -332 C ATOM 2257 OD1 ASN A 332 -6.074 17.933 -43.194 1.00 42.27 O ANISOU 2257 OD1 ASN A 332 6100 2928 7032 359 -129 -328 O ATOM 2258 ND2 ASN A 332 -3.946 17.756 -43.929 1.00 36.08 N ANISOU 2258 ND2 ASN A 332 5390 2075 6244 185 -146 -294 N ATOM 2259 N PRO A 333 -5.031 22.253 -40.615 1.00 43.32 N ANISOU 2259 N PRO A 333 6693 2712 7053 462 -149 -539 N ATOM 2260 CA PRO A 333 -4.862 23.069 -39.421 1.00 44.45 C ANISOU 2260 CA PRO A 333 6953 2794 7140 483 -137 -626 C ATOM 2261 C PRO A 333 -6.149 23.238 -38.671 1.00 45.03 C ANISOU 2261 C PRO A 333 7005 2911 7195 647 -76 -679 C ATOM 2262 O PRO A 333 -6.116 23.343 -37.452 1.00 48.19 O ANISOU 2262 O PRO A 333 7447 3335 7529 659 -39 -750 O ATOM 2263 CB PRO A 333 -4.473 24.430 -40.000 1.00 48.90 C ANISOU 2263 CB PRO A 333 7693 3172 7715 473 -185 -639 C ATOM 2264 CG PRO A 333 -3.795 24.065 -41.254 1.00 46.50 C ANISOU 2264 CG PRO A 333 7350 2866 7453 365 -222 -551 C ATOM 2265 CD PRO A 333 -4.552 22.927 -41.821 1.00 43.94 C ANISOU 2265 CD PRO A 333 6860 2675 7161 416 -199 -494 C ATOM 2266 N VAL A 334 -7.270 23.343 -39.389 1.00 43.53 N ANISOU 2266 N VAL A 334 6752 2730 7056 777 -67 -648 N ATOM 2267 CA VAL A 334 -8.507 23.521 -38.721 1.00 44.13 C ANISOU 2267 CA VAL A 334 6782 2860 7125 943 0 -694 C ATOM 2268 C VAL A 334 -8.864 22.219 -38.021 1.00 45.89 C ANISOU 2268 C VAL A 334 6839 3270 7326 913 61 -679 C ATOM 2269 O VAL A 334 -9.163 22.230 -36.812 1.00 45.52 O ANISOU 2269 O VAL A 334 6802 3277 7217 960 132 -743 O ATOM 2270 CB VAL A 334 -9.641 23.903 -39.651 1.00 49.14 C ANISOU 2270 CB VAL A 334 7360 3483 7827 1093 -15 -654 C ATOM 2271 CG1 VAL A 334 -10.927 24.074 -38.835 1.00 51.54 C ANISOU 2271 CG1 VAL A 334 7589 3866 8128 1276 71 -705 C ATOM 2272 CG2 VAL A 334 -9.344 25.238 -40.331 1.00 55.39 C ANISOU 2272 CG2 VAL A 334 8337 4072 8636 1136 -75 -657 C ATOM 2273 N LEU A 335 -8.763 21.104 -38.778 1.00 43.39 N ANISOU 2273 N LEU A 335 6393 3041 7052 823 36 -597 N ATOM 2274 CA LEU A 335 -9.274 19.801 -38.382 1.00 42.94 C ANISOU 2274 CA LEU A 335 6175 3147 6995 795 87 -563 C ATOM 2275 C LEU A 335 -8.462 19.193 -37.302 1.00 40.71 C ANISOU 2275 C LEU A 335 5914 2910 6645 695 115 -579 C ATOM 2276 O LEU A 335 -9.029 18.722 -36.394 1.00 41.11 O ANISOU 2276 O LEU A 335 5903 3062 6656 725 184 -592 O ATOM 2277 CB LEU A 335 -9.376 18.862 -39.573 1.00 45.12 C ANISOU 2277 CB LEU A 335 6339 3472 7332 726 45 -480 C ATOM 2278 CG LEU A 335 -10.375 19.195 -40.701 1.00 50.45 C ANISOU 2278 CG LEU A 335 6953 4146 8068 818 5 -445 C ATOM 2279 CD1 LEU A 335 -10.294 18.150 -41.796 1.00 53.79 C ANISOU 2279 CD1 LEU A 335 7293 4618 8527 716 -41 -375 C ATOM 2280 CD2 LEU A 335 -11.787 19.288 -40.171 1.00 55.03 C ANISOU 2280 CD2 LEU A 335 7416 4828 8665 957 65 -463 C ATOM 2281 N TYR A 336 -7.133 19.329 -37.358 1.00 38.02 N ANISOU 2281 N TYR A 336 5668 2494 6284 583 59 -579 N ATOM 2282 CA TYR A 336 -6.244 18.648 -36.491 1.00 37.72 C ANISOU 2282 CA TYR A 336 5633 2507 6191 480 60 -574 C ATOM 2283 C TYR A 336 -5.443 19.468 -35.471 1.00 41.90 C ANISOU 2283 C TYR A 336 6305 2977 6636 447 40 -647 C ATOM 2284 O TYR A 336 -4.792 18.910 -34.627 1.00 45.65 O ANISOU 2284 O TYR A 336 6779 3513 7052 372 34 -641 O ATOM 2285 CB TYR A 336 -5.286 17.882 -37.367 1.00 39.34 C ANISOU 2285 CB TYR A 336 5793 2706 6446 364 9 -503 C ATOM 2286 CG TYR A 336 -5.949 16.784 -38.172 1.00 37.90 C ANISOU 2286 CG TYR A 336 5481 2595 6325 365 28 -437 C ATOM 2287 CD1 TYR A 336 -6.353 15.593 -37.573 1.00 41.18 C ANISOU 2287 CD1 TYR A 336 5801 3119 6729 347 75 -403 C ATOM 2288 CD2 TYR A 336 -6.171 16.945 -39.514 1.00 38.04 C ANISOU 2288 CD2 TYR A 336 5485 2567 6403 374 -6 -408 C ATOM 2289 CE1 TYR A 336 -6.946 14.535 -38.323 1.00 37.50 C ANISOU 2289 CE1 TYR A 336 5226 2704 6317 325 87 -346 C ATOM 2290 CE2 TYR A 336 -6.780 15.949 -40.260 1.00 37.79 C ANISOU 2290 CE2 TYR A 336 5347 2597 6415 361 1 -358 C ATOM 2291 CZ TYR A 336 -7.122 14.719 -39.655 1.00 36.37 C ANISOU 2291 CZ TYR A 336 5073 2515 6230 329 46 -330 C ATOM 2292 OH TYR A 336 -7.776 13.869 -40.453 1.00 35.45 O ANISOU 2292 OH TYR A 336 4869 2441 6158 306 44 -289 O ATOM 2293 N ALA A 337 -5.456 20.801 -35.574 1.00 42.29 N ANISOU 2293 N ALA A 337 6490 2902 6678 497 20 -713 N ATOM 2294 CA ALA A 337 -4.818 21.662 -34.618 1.00 42.33 C ANISOU 2294 CA ALA A 337 6650 2837 6597 463 -1 -797 C ATOM 2295 C ALA A 337 -5.890 22.437 -33.903 1.00 44.21 C ANISOU 2295 C ALA A 337 6964 3051 6784 615 72 -887 C ATOM 2296 O ALA A 337 -6.113 22.280 -32.698 1.00 44.21 O ANISOU 2296 O ALA A 337 6989 3124 6687 638 125 -940 O ATOM 2297 CB ALA A 337 -3.829 22.606 -35.339 1.00 44.05 C ANISOU 2297 CB ALA A 337 6986 2902 6848 375 -84 -804 C ATOM 2298 N PHE A 338 -6.536 23.351 -34.628 1.00 46.58 N ANISOU 2298 N PHE A 338 7315 3240 7141 728 76 -907 N ATOM 2299 CA PHE A 338 -7.408 24.331 -33.999 1.00 50.39 C ANISOU 2299 CA PHE A 338 7903 3661 7582 889 142 -1005 C ATOM 2300 C PHE A 338 -8.603 23.672 -33.340 1.00 52.14 C ANISOU 2300 C PHE A 338 7988 4044 7779 1009 254 -1009 C ATOM 2301 O PHE A 338 -9.132 24.194 -32.394 1.00 52.01 O ANISOU 2301 O PHE A 338 8047 4026 7687 1114 332 -1100 O ATOM 2302 CB PHE A 338 -7.829 25.431 -34.984 1.00 55.62 C ANISOU 2302 CB PHE A 338 8648 4162 8323 999 114 -1009 C ATOM 2303 CG PHE A 338 -6.678 26.358 -35.353 1.00 63.76 C ANISOU 2303 CG PHE A 338 9869 5006 9352 880 23 -1029 C ATOM 2304 CD1 PHE A 338 -6.049 27.132 -34.375 1.00 75.56 C ANISOU 2304 CD1 PHE A 338 11555 6400 10754 826 12 -1136 C ATOM 2305 CD2 PHE A 338 -6.229 26.464 -36.667 1.00 69.63 C ANISOU 2305 CD2 PHE A 338 10604 5676 10177 812 -49 -943 C ATOM 2306 CE1 PHE A 338 -4.984 27.957 -34.698 1.00 80.18 C ANISOU 2306 CE1 PHE A 338 12305 6819 11341 691 -74 -1151 C ATOM 2307 CE2 PHE A 338 -5.180 27.303 -37.000 1.00 65.47 C ANISOU 2307 CE2 PHE A 338 10241 4986 9648 688 -122 -953 C ATOM 2308 CZ PHE A 338 -4.540 28.010 -36.014 1.00 73.24 C ANISOU 2308 CZ PHE A 338 11397 5879 10553 618 -137 -1053 C ATOM 2309 N LEU A 339 -8.996 22.477 -33.805 1.00 53.96 N ANISOU 2309 N LEU A 339 8019 4418 8066 980 267 -912 N ATOM 2310 CA LEU A 339 -10.066 21.730 -33.148 1.00 53.39 C ANISOU 2310 CA LEU A 339 7802 4513 7970 1056 375 -903 C ATOM 2311 C LEU A 339 -9.557 20.661 -32.162 1.00 54.63 C ANISOU 2311 C LEU A 339 7927 4793 8037 932 400 -879 C ATOM 2312 O LEU A 339 -10.330 20.037 -31.485 1.00 57.69 O ANISOU 2312 O LEU A 339 8217 5317 8385 970 496 -869 O ATOM 2313 CB LEU A 339 -10.947 21.104 -34.198 1.00 55.78 C ANISOU 2313 CB LEU A 339 7913 4895 8385 1098 375 -814 C ATOM 2314 CG LEU A 339 -11.811 22.178 -34.889 1.00 58.75 C ANISOU 2314 CG LEU A 339 8302 5189 8832 1274 374 -838 C ATOM 2315 CD1 LEU A 339 -12.660 21.526 -35.964 1.00 60.58 C ANISOU 2315 CD1 LEU A 339 8335 5515 9167 1299 351 -745 C ATOM 2316 CD2 LEU A 339 -12.682 22.973 -33.928 1.00 59.44 C ANISOU 2316 CD2 LEU A 339 8433 5284 8868 1455 485 -934 C ATOM 2317 N ASP A 340 -8.241 20.467 -32.085 1.00 52.74 N ANISOU 2317 N ASP A 340 7765 4507 7766 783 313 -864 N ATOM 2318 CA ASP A 340 -7.643 19.594 -31.087 1.00 48.87 C ANISOU 2318 CA ASP A 340 7271 4116 7181 677 318 -841 C ATOM 2319 C ASP A 340 -7.959 20.059 -29.670 1.00 55.23 C ANISOU 2319 C ASP A 340 8186 4959 7841 734 396 -935 C ATOM 2320 O ASP A 340 -7.878 21.254 -29.335 1.00 53.24 O ANISOU 2320 O ASP A 340 8095 4598 7536 791 394 -1043 O ATOM 2321 CB ASP A 340 -6.132 19.457 -31.289 1.00 49.92 C ANISOU 2321 CB ASP A 340 7462 4191 7314 523 200 -810 C ATOM 2322 CG ASP A 340 -5.456 18.630 -30.140 1.00 50.40 C ANISOU 2322 CG ASP A 340 7531 4355 7265 426 188 -783 C ATOM 2323 OD1 ASP A 340 -5.418 17.380 -30.253 1.00 52.76 O ANISOU 2323 OD1 ASP A 340 7707 4745 7596 378 195 -685 O ATOM 2324 OD2 ASP A 340 -5.101 19.241 -29.104 1.00 50.44 O ANISOU 2324 OD2 ASP A 340 7673 4346 7145 412 178 -863 O ATOM 2325 N GLU A 341 -8.333 19.109 -28.809 1.00 57.49 N ANISOU 2325 N GLU A 341 8400 5393 8051 717 470 -897 N ATOM 2326 CA GLU A 341 -8.758 19.420 -27.433 1.00 65.08 C ANISOU 2326 CA GLU A 341 9457 6418 8854 774 567 -980 C ATOM 2327 C GLU A 341 -7.761 20.300 -26.696 1.00 57.84 C ANISOU 2327 C GLU A 341 8756 5407 7815 720 496 -1079 C ATOM 2328 O GLU A 341 -8.135 21.270 -26.110 1.00 57.92 O ANISOU 2328 O GLU A 341 8901 5364 7741 812 553 -1198 O ATOM 2329 CB GLU A 341 -8.940 18.121 -26.608 1.00 76.69 C ANISOU 2329 CB GLU A 341 10840 8056 10244 709 629 -896 C ATOM 2330 CG GLU A 341 -10.358 17.564 -26.587 1.00 89.38 C ANISOU 2330 CG GLU A 341 12285 9791 11885 796 773 -856 C ATOM 2331 CD GLU A 341 -11.364 18.527 -25.976 1.00 99.08 C ANISOU 2331 CD GLU A 341 13563 11039 13046 960 907 -971 C ATOM 2332 OE1 GLU A 341 -11.197 18.921 -24.805 1.00111.57 O ANISOU 2332 OE1 GLU A 341 15293 12640 14459 972 958 -1052 O ATOM 2333 OE2 GLU A 341 -12.325 18.901 -26.677 1.00111.88 O ANISOU 2333 OE2 GLU A 341 15075 12656 14778 1084 961 -981 O ATOM 2334 N ASN A 342 -6.483 19.898 -26.689 1.00 52.68 N ANISOU 2334 N ASN A 342 8130 4739 7146 565 369 -1029 N ATOM 2335 CA ASN A 342 -5.507 20.589 -25.862 1.00 55.37 C ANISOU 2335 CA ASN A 342 8659 5023 7355 484 288 -1113 C ATOM 2336 C ASN A 342 -5.039 21.884 -26.547 1.00 56.32 C ANISOU 2336 C ASN A 342 8904 4956 7540 480 211 -1196 C ATOM 2337 O ASN A 342 -4.968 22.930 -25.913 1.00 53.77 O ANISOU 2337 O ASN A 342 8771 4544 7116 502 212 -1323 O ATOM 2338 CB ASN A 342 -4.315 19.701 -25.542 1.00 56.20 C ANISOU 2338 CB ASN A 342 8732 5200 7423 325 175 -1023 C ATOM 2339 CG ASN A 342 -4.665 18.546 -24.588 1.00 56.42 C ANISOU 2339 CG ASN A 342 8700 5395 7343 317 241 -951 C ATOM 2340 OD1 ASN A 342 -4.633 17.376 -24.975 1.00 61.25 O ANISOU 2340 OD1 ASN A 342 9163 6078 8032 283 238 -823 O ATOM 2341 ND2 ASN A 342 -4.989 18.871 -23.376 1.00 54.42 N ANISOU 2341 ND2 ASN A 342 8573 5193 6910 347 303 -1030 N ATOM 2342 N PHE A 343 -4.740 21.781 -27.849 1.00 55.43 N ANISOU 2342 N PHE A 343 8694 4780 7589 450 151 -1121 N ATOM 2343 CA PHE A 343 -4.219 22.892 -28.655 1.00 61.90 C ANISOU 2343 CA PHE A 343 9617 5421 8482 424 74 -1167 C ATOM 2344 C PHE A 343 -5.253 23.993 -28.672 1.00 64.01 C ANISOU 2344 C PHE A 343 9994 5579 8747 592 159 -1271 C ATOM 2345 O PHE A 343 -4.948 25.116 -28.406 1.00 69.41 O ANISOU 2345 O PHE A 343 10870 6120 9381 587 128 -1375 O ATOM 2346 CB PHE A 343 -3.893 22.410 -30.052 1.00 58.41 C ANISOU 2346 CB PHE A 343 9032 4961 8199 378 22 -1054 C ATOM 2347 CG PHE A 343 -3.347 23.451 -30.945 1.00 56.36 C ANISOU 2347 CG PHE A 343 8871 4531 8013 337 -50 -1078 C ATOM 2348 CD1 PHE A 343 -4.167 24.432 -31.454 1.00 56.79 C ANISOU 2348 CD1 PHE A 343 9006 4457 8113 468 -7 -1131 C ATOM 2349 CD2 PHE A 343 -2.023 23.414 -31.327 1.00 55.79 C ANISOU 2349 CD2 PHE A 343 8797 4429 7971 170 -158 -1034 C ATOM 2350 CE1 PHE A 343 -3.663 25.420 -32.305 1.00 57.49 C ANISOU 2350 CE1 PHE A 343 9206 4372 8267 425 -74 -1141 C ATOM 2351 CE2 PHE A 343 -1.516 24.395 -32.162 1.00 55.71 C ANISOU 2351 CE2 PHE A 343 8882 4261 8026 116 -216 -1048 C ATOM 2352 CZ PHE A 343 -2.333 25.392 -32.670 1.00 53.61 C ANISOU 2352 CZ PHE A 343 8721 3850 7798 239 -176 -1098 C ATOM 2353 N LYS A 344 -6.504 23.626 -28.941 1.00 68.24 N ANISOU 2353 N LYS A 344 10401 6188 9338 742 269 -1240 N ATOM 2354 CA LYS A 344 -7.635 24.499 -28.739 1.00 68.98 C ANISOU 2354 CA LYS A 344 10565 6225 9419 935 374 -1334 C ATOM 2355 C LYS A 344 -7.425 25.481 -27.610 1.00 73.10 C ANISOU 2355 C LYS A 344 11326 6658 9790 953 395 -1485 C ATOM 2356 O LYS A 344 -7.640 26.656 -27.814 1.00 76.73 O ANISOU 2356 O LYS A 344 11938 6948 10269 1047 401 -1574 O ATOM 2357 CB LYS A 344 -8.901 23.710 -28.466 1.00 69.78 C ANISOU 2357 CB LYS A 344 10488 6499 9524 1058 510 -1295 C ATOM 2358 CG LYS A 344 -10.200 24.426 -28.677 1.00 78.01 C ANISOU 2358 CG LYS A 344 11511 7511 10618 1280 617 -1348 C ATOM 2359 CD LYS A 344 -11.336 23.447 -28.406 1.00 79.93 C ANISOU 2359 CD LYS A 344 11537 7963 10870 1356 743 -1288 C ATOM 2360 CE LYS A 344 -11.827 22.800 -29.681 1.00 84.14 C ANISOU 2360 CE LYS A 344 11853 8549 11568 1362 708 -1164 C ATOM 2361 NZ LYS A 344 -12.659 21.593 -29.399 1.00 93.82 N ANISOU 2361 NZ LYS A 344 12863 9986 12797 1356 803 -1085 N ATOM 2362 N ARG A 345 -7.020 25.011 -26.423 1.00 83.58 N ANISOU 2362 N ARG A 345 12701 8093 10963 866 403 -1514 N ATOM 2363 CA ARG A 345 -7.011 25.873 -25.217 1.00 83.90 C ANISOU 2363 CA ARG A 345 12975 8075 10828 898 444 -1672 C ATOM 2364 C ARG A 345 -6.121 27.116 -25.269 1.00 90.00 C ANISOU 2364 C ARG A 345 13991 8629 11575 817 334 -1777 C ATOM 2365 O ARG A 345 -6.391 28.077 -24.569 1.00 84.45 O ANISOU 2365 O ARG A 345 13501 7820 10765 896 386 -1926 O ATOM 2366 CB ARG A 345 -6.689 25.091 -23.962 1.00 85.48 C ANISOU 2366 CB ARG A 345 13187 8441 10850 804 458 -1671 C ATOM 2367 CG ARG A 345 -7.885 24.406 -23.329 1.00 90.16 C ANISOU 2367 CG ARG A 345 13666 9211 11381 935 632 -1654 C ATOM 2368 CD ARG A 345 -7.423 23.662 -22.092 1.00 94.55 C ANISOU 2368 CD ARG A 345 14264 9917 11745 819 627 -1640 C ATOM 2369 NE ARG A 345 -6.317 22.801 -22.508 1.00101.44 N ANISOU 2369 NE ARG A 345 15035 10830 12677 637 471 -1508 N ATOM 2370 CZ ARG A 345 -5.377 22.291 -21.719 1.00 96.11 C ANISOU 2370 CZ ARG A 345 14413 10233 11871 487 376 -1477 C ATOM 2371 NH1 ARG A 345 -5.390 22.499 -20.408 1.00103.15 N ANISOU 2371 NH1 ARG A 345 15470 11182 12541 478 413 -1566 N ATOM 2372 NH2 ARG A 345 -4.412 21.560 -22.264 1.00 89.14 N ANISOU 2372 NH2 ARG A 345 13415 9374 11079 352 241 -1353 N ATOM 2373 N CYS A 346 -5.075 27.112 -26.102 1.00 99.20 N ANISOU 2373 N CYS A 346 15131 9722 12838 657 189 -1704 N ATOM 2374 CA CYS A 346 -4.253 28.329 -26.321 1.00106.19 C ANISOU 2374 CA CYS A 346 16236 10388 13725 562 84 -1788 C ATOM 2375 C CYS A 346 -4.665 29.029 -27.624 1.00106.21 C ANISOU 2375 C CYS A 346 16238 10222 13896 662 88 -1758 C ATOM 2376 O CYS A 346 -4.859 28.343 -28.632 1.00 89.02 O ANISOU 2376 O CYS A 346 13855 8115 11853 679 85 -1626 O ATOM 2377 CB CYS A 346 -2.768 27.923 -26.343 1.00104.71 C ANISOU 2377 CB CYS A 346 16018 10240 13527 307 -77 -1723 C ATOM 2378 SG CYS A 346 -2.405 26.334 -25.517 1.00102.26 S ANISOU 2378 SG CYS A 346 15521 10209 13123 217 -91 -1624 S ATOM 2379 N PHE A 347 -4.814 30.371 -27.647 1.00102.32 N ANISOU 2379 N PHE A 347 15981 9502 13396 730 92 -1874 N ATOM 2380 CA PHE A 347 -4.671 31.281 -26.513 1.00123.64 C ANISOU 2380 CA PHE A 347 18956 12087 15935 724 103 -2050 C ATOM 2381 C PHE A 347 -6.023 31.485 -25.810 1.00121.78 C ANISOU 2381 C PHE A 347 18761 11880 15628 983 280 -2150 C ATOM 2382 O PHE A 347 -6.236 32.494 -25.119 1.00 98.44 O ANISOU 2382 O PHE A 347 16061 8771 12569 1061 326 -2312 O ATOM 2383 CB PHE A 347 -4.047 32.668 -26.922 1.00120.84 C ANISOU 2383 CB PHE A 347 18865 11438 15611 645 12 -2129 C ATOM 2384 CG PHE A 347 -4.904 33.515 -27.874 1.00122.76 C ANISOU 2384 CG PHE A 347 19167 11487 15988 850 71 -2125 C ATOM 2385 CD1 PHE A 347 -5.908 34.360 -27.397 1.00119.55 C ANISOU 2385 CD1 PHE A 347 18933 10953 15537 1087 190 -2258 C ATOM 2386 CD2 PHE A 347 -4.681 33.491 -29.259 1.00124.01 C ANISOU 2386 CD2 PHE A 347 19218 11588 16312 811 5 -1986 C ATOM 2387 CE1 PHE A 347 -6.674 35.132 -28.273 1.00120.69 C ANISOU 2387 CE1 PHE A 347 19127 10919 15809 1288 232 -2243 C ATOM 2388 CE2 PHE A 347 -5.457 34.263 -30.131 1.00114.00 C ANISOU 2388 CE2 PHE A 347 18012 10147 15158 1000 44 -1970 C ATOM 2389 CZ PHE A 347 -6.450 35.081 -29.640 1.00106.87 C ANISOU 2389 CZ PHE A 347 17268 9118 14219 1242 151 -2093 C ATOM 2390 OXT PHE A 347 -6.919 30.627 -25.937 1.00117.27 O ANISOU 2390 OXT PHE A 347 17964 11491 15103 1115 382 -2069 O TER 2391 PHE A 347 ATOM 2392 N GLN B 3 -21.595 5.460 -0.975 1.00 97.30 N ANISOU 2392 N GLN B 3 8035 18871 10062 -1223 2336 197 N ATOM 2393 CA GLN B 3 -21.441 6.006 -2.363 1.00 93.19 C ANISOU 2393 CA GLN B 3 7641 17861 9907 -959 2111 -15 C ATOM 2394 C GLN B 3 -20.142 5.512 -3.066 1.00 90.20 C ANISOU 2394 C GLN B 3 7769 16692 9809 -1079 1898 150 C ATOM 2395 O GLN B 3 -19.578 4.518 -2.659 1.00 94.19 O ANISOU 2395 O GLN B 3 8476 17026 10284 -1425 1908 465 O ATOM 2396 CB GLN B 3 -21.480 7.511 -2.279 1.00 91.07 C ANISOU 2396 CB GLN B 3 7341 17685 9576 -361 2091 -446 C ATOM 2397 CG GLN B 3 -20.238 8.104 -1.642 1.00 91.42 C ANISOU 2397 CG GLN B 3 7790 17411 9536 -142 2038 -545 C ATOM 2398 CD GLN B 3 -20.016 9.500 -2.167 1.00 92.36 C ANISOU 2398 CD GLN B 3 8053 17257 9783 385 1893 -935 C ATOM 2399 OE1 GLN B 3 -20.915 10.057 -2.833 1.00 98.32 O ANISOU 2399 OE1 GLN B 3 8565 18160 10632 639 1860 -1137 O ATOM 2400 NE2 GLN B 3 -18.832 10.078 -1.903 1.00 85.71 N ANISOU 2400 NE2 GLN B 3 7606 16011 8949 547 1786 -1035 N ATOM 2401 N VAL B 4 -19.666 6.237 -4.086 1.00 84.86 N ANISOU 2401 N VAL B 4 7296 15563 9384 -771 1709 -63 N ATOM 2402 CA VAL B 4 -18.467 5.883 -4.860 1.00 77.17 C ANISOU 2402 CA VAL B 4 6750 13906 8665 -835 1519 47 C ATOM 2403 C VAL B 4 -17.249 5.434 -4.072 1.00 75.65 C ANISOU 2403 C VAL B 4 6882 13477 8383 -952 1517 237 C ATOM 2404 O VAL B 4 -16.891 6.035 -3.084 1.00 81.63 O ANISOU 2404 O VAL B 4 7675 14422 8919 -775 1589 138 O ATOM 2405 CB VAL B 4 -18.046 7.062 -5.746 1.00 75.20 C ANISOU 2405 CB VAL B 4 6666 13315 8593 -420 1358 -243 C ATOM 2406 CG1 VAL B 4 -16.645 6.857 -6.350 1.00 69.96 C ANISOU 2406 CG1 VAL B 4 6429 12028 8126 -451 1197 -153 C ATOM 2407 CG2 VAL B 4 -19.109 7.297 -6.817 1.00 75.92 C ANISOU 2407 CG2 VAL B 4 6502 13515 8828 -329 1293 -369 C ATOM 2408 N GLN B 5 -16.583 4.392 -4.574 1.00 74.11 N ANISOU 2408 N GLN B 5 6937 12852 8369 -1219 1412 489 N ATOM 2409 CA GLN B 5 -15.368 3.839 -4.005 1.00 72.75 C ANISOU 2409 CA GLN B 5 7082 12403 8156 -1310 1368 692 C ATOM 2410 C GLN B 5 -14.248 3.567 -5.054 1.00 67.86 C ANISOU 2410 C GLN B 5 6794 11167 7822 -1263 1173 715 C ATOM 2411 O GLN B 5 -14.271 2.573 -5.766 1.00 63.75 O ANISOU 2411 O GLN B 5 6369 10373 7482 -1490 1100 881 O ATOM 2412 CB GLN B 5 -15.687 2.550 -3.276 1.00 81.32 C ANISOU 2412 CB GLN B 5 8142 13646 9111 -1723 1460 1057 C ATOM 2413 CG GLN B 5 -14.497 2.130 -2.444 1.00 85.66 C ANISOU 2413 CG GLN B 5 8987 14014 9544 -1744 1421 1258 C ATOM 2414 CD GLN B 5 -14.785 0.951 -1.572 1.00 94.83 C ANISOU 2414 CD GLN B 5 10161 15341 10528 -2129 1509 1648 C ATOM 2415 OE1 GLN B 5 -15.786 0.908 -0.833 1.00 97.36 O ANISOU 2415 OE1 GLN B 5 10202 16189 10603 -2305 1691 1719 O ATOM 2416 NE2 GLN B 5 -13.895 -0.028 -1.641 1.00 98.68 N ANISOU 2416 NE2 GLN B 5 10978 15386 11127 -2260 1378 1914 N ATOM 2417 N LEU B 6 -13.266 4.471 -5.126 1.00 61.54 N ANISOU 2417 N LEU B 6 6165 10172 7047 -974 1093 534 N ATOM 2418 CA LEU B 6 -12.174 4.371 -6.056 1.00 58.36 C ANISOU 2418 CA LEU B 6 6023 9282 6867 -903 936 530 C ATOM 2419 C LEU B 6 -11.086 3.476 -5.485 1.00 62.16 C ANISOU 2419 C LEU B 6 6726 9578 7312 -1018 892 774 C ATOM 2420 O LEU B 6 -10.599 3.708 -4.382 1.00 68.92 O ANISOU 2420 O LEU B 6 7612 10614 7961 -967 928 808 O ATOM 2421 CB LEU B 6 -11.630 5.773 -6.368 1.00 54.77 C ANISOU 2421 CB LEU B 6 5635 8731 6444 -587 871 247 C ATOM 2422 CG LEU B 6 -12.683 6.749 -6.921 1.00 55.98 C ANISOU 2422 CG LEU B 6 5603 9036 6631 -404 887 2 C ATOM 2423 CD1 LEU B 6 -12.171 8.171 -7.057 1.00 55.42 C ANISOU 2423 CD1 LEU B 6 5648 8840 6568 -105 814 -257 C ATOM 2424 CD2 LEU B 6 -13.195 6.240 -8.265 1.00 56.46 C ANISOU 2424 CD2 LEU B 6 5630 8913 6908 -499 814 40 C ATOM 2425 N VAL B 7 -10.696 2.453 -6.250 1.00 63.37 N ANISOU 2425 N VAL B 7 7045 9373 7660 -1146 797 930 N ATOM 2426 CA VAL B 7 -9.616 1.553 -5.867 1.00 63.40 C ANISOU 2426 CA VAL B 7 7279 9144 7667 -1193 722 1154 C ATOM 2427 C VAL B 7 -8.444 1.892 -6.750 1.00 56.62 C ANISOU 2427 C VAL B 7 6573 7965 6976 -981 599 1020 C ATOM 2428 O VAL B 7 -8.513 1.711 -7.943 1.00 53.84 O ANISOU 2428 O VAL B 7 6265 7372 6821 -972 540 945 O ATOM 2429 CB VAL B 7 -9.985 0.037 -6.044 1.00 67.92 C ANISOU 2429 CB VAL B 7 7965 9507 8333 -1480 692 1432 C ATOM 2430 CG1 VAL B 7 -8.984 -0.849 -5.309 1.00 68.93 C ANISOU 2430 CG1 VAL B 7 8329 9461 8400 -1495 621 1696 C ATOM 2431 CG2 VAL B 7 -11.384 -0.254 -5.519 1.00 72.10 C ANISOU 2431 CG2 VAL B 7 8285 10373 8736 -1763 824 1544 C ATOM 2432 N GLU B 8 -7.371 2.393 -6.143 1.00 57.10 N ANISOU 2432 N GLU B 8 6695 8065 6936 -825 563 989 N ATOM 2433 CA GLU B 8 -6.150 2.700 -6.814 1.00 57.56 C ANISOU 2433 CA GLU B 8 6860 7896 7115 -655 459 891 C ATOM 2434 C GLU B 8 -5.206 1.541 -6.625 1.00 58.45 C ANISOU 2434 C GLU B 8 7135 7814 7261 -653 371 1112 C ATOM 2435 O GLU B 8 -5.169 1.000 -5.544 1.00 63.53 O ANISOU 2435 O GLU B 8 7812 8579 7747 -723 379 1311 O ATOM 2436 CB GLU B 8 -5.579 3.913 -6.149 1.00 64.20 C ANISOU 2436 CB GLU B 8 7650 8933 7810 -522 458 731 C ATOM 2437 CG GLU B 8 -6.416 5.163 -6.444 1.00 71.53 C ANISOU 2437 CG GLU B 8 8465 9979 8732 -457 515 479 C ATOM 2438 CD GLU B 8 -6.466 6.146 -5.289 1.00 66.81 C ANISOU 2438 CD GLU B 8 7807 9669 7908 -382 555 343 C ATOM 2439 OE1 GLU B 8 -6.543 5.704 -4.127 1.00 69.87 O ANISOU 2439 OE1 GLU B 8 8166 10294 8089 -448 604 473 O ATOM 2440 OE2 GLU B 8 -6.488 7.349 -5.561 1.00 55.06 O ANISOU 2440 OE2 GLU B 8 6318 8164 6439 -259 534 105 O ATOM 2441 N SER B 9 -4.482 1.134 -7.675 1.00 50.79 N ANISOU 2441 N SER B 9 6267 6554 6477 -558 286 1079 N ATOM 2442 CA SER B 9 -3.423 0.139 -7.536 1.00 51.72 C ANISOU 2442 CA SER B 9 6534 6489 6630 -464 185 1244 C ATOM 2443 C SER B 9 -2.168 0.519 -8.206 1.00 48.72 C ANISOU 2443 C SER B 9 6144 6041 6326 -259 117 1109 C ATOM 2444 O SER B 9 -2.182 1.390 -9.056 1.00 46.99 O ANISOU 2444 O SER B 9 5849 5831 6173 -229 147 908 O ATOM 2445 CB SER B 9 -3.840 -1.161 -8.196 1.00 55.29 C ANISOU 2445 CB SER B 9 7149 6615 7242 -551 141 1364 C ATOM 2446 OG SER B 9 -5.205 -1.249 -8.103 1.00 60.83 O ANISOU 2446 OG SER B 9 7795 7391 7928 -789 221 1401 O ATOM 2447 N GLY B 10 -1.093 -0.204 -7.889 1.00 49.23 N ANISOU 2447 N GLY B 10 6287 6034 6383 -115 21 1235 N ATOM 2448 CA GLY B 10 0.138 -0.159 -8.639 1.00 51.83 C ANISOU 2448 CA GLY B 10 6590 6304 6799 93 -43 1130 C ATOM 2449 C GLY B 10 1.205 0.801 -8.115 1.00 58.07 C ANISOU 2449 C GLY B 10 7221 7377 7467 178 -72 1052 C ATOM 2450 O GLY B 10 2.282 0.968 -8.728 1.00 62.73 O ANISOU 2450 O GLY B 10 7729 7996 8108 322 -111 958 O ATOM 2451 N GLY B 11 0.930 1.441 -6.978 1.00 58.72 N ANISOU 2451 N GLY B 11 7244 7695 7371 78 -53 1077 N ATOM 2452 CA GLY B 11 1.897 2.376 -6.419 1.00 61.23 C ANISOU 2452 CA GLY B 11 7426 8277 7563 117 -102 982 C ATOM 2453 C GLY B 11 3.064 1.673 -5.753 1.00 60.88 C ANISOU 2453 C GLY B 11 7360 8334 7438 280 -230 1133 C ATOM 2454 O GLY B 11 3.280 0.499 -5.928 1.00 66.31 O ANISOU 2454 O GLY B 11 8152 8841 8202 414 -286 1289 O ATOM 2455 N GLY B 12 3.800 2.424 -4.941 1.00 60.29 N ANISOU 2455 N GLY B 12 7158 8550 7199 274 -294 1078 N ATOM 2456 CA GLY B 12 4.794 1.876 -4.051 1.00 59.26 C ANISOU 2456 CA GLY B 12 6983 8601 6934 419 -434 1230 C ATOM 2457 C GLY B 12 6.185 2.378 -4.353 1.00 57.62 C ANISOU 2457 C GLY B 12 6564 8593 6738 511 -523 1105 C ATOM 2458 O GLY B 12 6.370 3.505 -4.839 1.00 54.17 O ANISOU 2458 O GLY B 12 6014 8234 6333 377 -478 894 O ATOM 2459 N LEU B 13 7.160 1.509 -4.077 1.00 61.02 N ANISOU 2459 N LEU B 13 6940 9103 7140 743 -655 1249 N ATOM 2460 CA LEU B 13 8.595 1.791 -4.147 1.00 64.47 C ANISOU 2460 CA LEU B 13 7119 9828 7547 864 -765 1172 C ATOM 2461 C LEU B 13 9.237 1.512 -5.474 1.00 61.88 C ANISOU 2461 C LEU B 13 6681 9418 7412 1017 -727 1081 C ATOM 2462 O LEU B 13 9.233 0.400 -5.920 1.00 68.09 O ANISOU 2462 O LEU B 13 7580 9983 8310 1252 -742 1180 O ATOM 2463 CB LEU B 13 9.285 0.896 -3.149 1.00 71.43 C ANISOU 2463 CB LEU B 13 7988 10865 8286 1098 -943 1389 C ATOM 2464 CG LEU B 13 9.632 1.598 -1.864 1.00 78.06 C ANISOU 2464 CG LEU B 13 8718 12082 8861 980 -1052 1383 C ATOM 2465 CD1 LEU B 13 9.665 0.543 -0.761 1.00 86.06 C ANISOU 2465 CD1 LEU B 13 9866 13130 9701 1167 -1194 1680 C ATOM 2466 CD2 LEU B 13 10.974 2.322 -2.077 1.00 80.29 C ANISOU 2466 CD2 LEU B 13 8662 12720 9124 983 -1145 1211 C ATOM 2467 N VAL B 14 9.877 2.523 -6.062 1.00 62.73 N ANISOU 2467 N VAL B 14 6565 9729 7540 886 -689 891 N ATOM 2468 CA VAL B 14 10.672 2.356 -7.275 1.00 62.54 C ANISOU 2468 CA VAL B 14 6369 9753 7642 1022 -643 799 C ATOM 2469 C VAL B 14 12.005 3.041 -7.164 1.00 62.17 C ANISOU 2469 C VAL B 14 5967 10150 7506 975 -716 710 C ATOM 2470 O VAL B 14 12.111 4.096 -6.524 1.00 61.21 O ANISOU 2470 O VAL B 14 5767 10218 7272 702 -758 640 O ATOM 2471 CB VAL B 14 10.043 3.017 -8.525 1.00 60.35 C ANISOU 2471 CB VAL B 14 6157 9280 7493 828 -474 652 C ATOM 2472 CG1 VAL B 14 9.430 1.995 -9.446 1.00 60.68 C ANISOU 2472 CG1 VAL B 14 6392 8981 7682 1013 -401 679 C ATOM 2473 CG2 VAL B 14 9.098 4.127 -8.137 1.00 57.87 C ANISOU 2473 CG2 VAL B 14 5972 8881 7136 508 -424 586 C ATOM 2474 N ARG B 15 12.996 2.488 -7.867 1.00 64.55 N ANISOU 2474 N ARG B 15 6046 10623 7858 1226 -724 688 N ATOM 2475 CA ARG B 15 14.310 3.107 -7.996 1.00 70.39 C ANISOU 2475 CA ARG B 15 6380 11840 8524 1165 -765 596 C ATOM 2476 C ARG B 15 14.227 4.310 -8.930 1.00 65.18 C ANISOU 2476 C ARG B 15 5654 11202 7909 794 -617 450 C ATOM 2477 O ARG B 15 13.404 4.326 -9.849 1.00 58.90 O ANISOU 2477 O ARG B 15 5069 10086 7223 745 -473 414 O ATOM 2478 CB ARG B 15 15.351 2.125 -8.508 1.00 76.02 C ANISOU 2478 CB ARG B 15 6850 12770 9266 1584 -800 604 C ATOM 2479 CG ARG B 15 15.631 0.992 -7.542 1.00 84.63 C ANISOU 2479 CG ARG B 15 7990 13866 10301 1977 -990 767 C ATOM 2480 CD ARG B 15 16.676 0.023 -8.080 1.00 94.86 C ANISOU 2480 CD ARG B 15 9048 15363 11631 2461 -1037 747 C ATOM 2481 NE ARG B 15 18.027 0.588 -8.101 1.00104.94 N ANISOU 2481 NE ARG B 15 9802 17266 12803 2442 -1083 654 N ATOM 2482 CZ ARG B 15 18.777 0.794 -7.015 1.00116.25 C ANISOU 2482 CZ ARG B 15 10987 19099 14084 2445 -1279 718 C ATOM 2483 NH1 ARG B 15 18.303 0.527 -5.797 1.00121.92 N ANISOU 2483 NH1 ARG B 15 11951 19659 14714 2465 -1439 881 N ATOM 2484 NH2 ARG B 15 20.007 1.294 -7.141 1.00118.91 N ANISOU 2484 NH2 ARG B 15 10810 20037 14333 2401 -1315 620 N ATOM 2485 N PRO B 16 15.070 5.347 -8.706 1.00 64.42 N ANISOU 2485 N PRO B 16 5277 11478 7720 508 -664 375 N ATOM 2486 CA PRO B 16 15.135 6.482 -9.625 1.00 63.87 C ANISOU 2486 CA PRO B 16 5148 11433 7687 136 -539 271 C ATOM 2487 C PRO B 16 15.371 5.976 -11.038 1.00 62.70 C ANISOU 2487 C PRO B 16 4905 11299 7618 309 -378 250 C ATOM 2488 O PRO B 16 16.168 5.075 -11.256 1.00 62.90 O ANISOU 2488 O PRO B 16 4694 11577 7629 653 -392 260 O ATOM 2489 CB PRO B 16 16.311 7.301 -9.088 1.00 65.44 C ANISOU 2489 CB PRO B 16 4990 12110 7765 -126 -656 222 C ATOM 2490 CG PRO B 16 16.342 6.964 -7.635 1.00 67.19 C ANISOU 2490 CG PRO B 16 5236 12418 7874 1 -851 271 C ATOM 2491 CD PRO B 16 15.969 5.504 -7.556 1.00 66.41 C ANISOU 2491 CD PRO B 16 5279 12133 7822 492 -857 394 C ATOM 2492 N GLY B 17 14.600 6.508 -11.985 1.00 60.98 N ANISOU 2492 N GLY B 17 4899 10795 7473 113 -233 213 N ATOM 2493 CA GLY B 17 14.739 6.146 -13.382 1.00 62.04 C ANISOU 2493 CA GLY B 17 4973 10951 7646 235 -72 179 C ATOM 2494 C GLY B 17 13.808 5.011 -13.749 1.00 60.96 C ANISOU 2494 C GLY B 17 5131 10424 7608 577 -33 189 C ATOM 2495 O GLY B 17 13.648 4.724 -14.926 1.00 60.56 O ANISOU 2495 O GLY B 17 5120 10302 7586 669 96 136 O ATOM 2496 N GLY B 18 13.163 4.404 -12.741 1.00 59.73 N ANISOU 2496 N GLY B 18 5192 10018 7486 728 -146 259 N ATOM 2497 CA GLY B 18 12.237 3.296 -12.941 1.00 57.72 C ANISOU 2497 CA GLY B 18 5237 9365 7330 995 -135 291 C ATOM 2498 C GLY B 18 10.846 3.715 -13.375 1.00 53.57 C ANISOU 2498 C GLY B 18 5029 8449 6877 783 -52 276 C ATOM 2499 O GLY B 18 10.544 4.887 -13.531 1.00 53.95 O ANISOU 2499 O GLY B 18 5098 8495 6905 463 -7 241 O ATOM 2500 N SER B 19 9.993 2.710 -13.555 1.00 53.87 N ANISOU 2500 N SER B 19 5321 8144 7003 974 -51 303 N ATOM 2501 CA SER B 19 8.615 2.839 -14.025 1.00 52.83 C ANISOU 2501 CA SER B 19 5468 7659 6948 831 13 287 C ATOM 2502 C SER B 19 7.595 2.247 -13.025 1.00 50.48 C ANISOU 2502 C SER B 19 5406 7090 6686 843 -60 399 C ATOM 2503 O SER B 19 7.931 1.316 -12.287 1.00 52.01 O ANISOU 2503 O SER B 19 5620 7271 6872 1050 -155 501 O ATOM 2504 CB SER B 19 8.514 2.095 -15.354 1.00 54.41 C ANISOU 2504 CB SER B 19 5739 7726 7209 1014 88 197 C ATOM 2505 OG SER B 19 9.093 2.882 -16.377 1.00 61.20 O ANISOU 2505 OG SER B 19 6425 8823 8007 903 193 107 O ATOM 2506 N LEU B 20 6.381 2.816 -13.001 1.00 47.05 N ANISOU 2506 N LEU B 20 5133 6470 6275 624 -16 392 N ATOM 2507 CA LEU B 20 5.223 2.283 -12.268 1.00 48.78 C ANISOU 2507 CA LEU B 20 5556 6460 6519 588 -44 490 C ATOM 2508 C LEU B 20 4.020 2.540 -13.117 1.00 44.44 C ANISOU 2508 C LEU B 20 5141 5700 6042 456 33 419 C ATOM 2509 O LEU B 20 3.971 3.534 -13.853 1.00 42.95 O ANISOU 2509 O LEU B 20 4903 5567 5849 337 91 317 O ATOM 2510 CB LEU B 20 4.965 2.959 -10.890 1.00 51.64 C ANISOU 2510 CB LEU B 20 5898 6955 6766 438 -83 551 C ATOM 2511 CG LEU B 20 6.002 2.768 -9.786 1.00 58.65 C ANISOU 2511 CG LEU B 20 6659 8084 7539 537 -190 639 C ATOM 2512 CD1 LEU B 20 5.713 3.759 -8.668 1.00 62.09 C ANISOU 2512 CD1 LEU B 20 7073 8679 7837 345 -212 622 C ATOM 2513 CD2 LEU B 20 6.032 1.326 -9.267 1.00 58.75 C ANISOU 2513 CD2 LEU B 20 6791 7969 7564 753 -271 815 C ATOM 2514 N ARG B 21 3.037 1.656 -13.003 1.00 42.89 N ANISOU 2514 N ARG B 21 5118 5269 5909 461 21 488 N ATOM 2515 CA ARG B 21 1.722 1.839 -13.622 1.00 45.09 C ANISOU 2515 CA ARG B 21 5501 5383 6247 318 73 434 C ATOM 2516 C ARG B 21 0.669 1.892 -12.529 1.00 45.30 C ANISOU 2516 C ARG B 21 5575 5404 6231 174 75 532 C ATOM 2517 O ARG B 21 0.546 0.951 -11.730 1.00 49.13 O ANISOU 2517 O ARG B 21 6142 5821 6705 194 32 682 O ATOM 2518 CB ARG B 21 1.396 0.712 -14.610 1.00 46.76 C ANISOU 2518 CB ARG B 21 5854 5347 6566 407 58 401 C ATOM 2519 CG ARG B 21 0.057 0.919 -15.313 1.00 45.90 C ANISOU 2519 CG ARG B 21 5818 5114 6506 248 91 334 C ATOM 2520 CD ARG B 21 -0.212 -0.101 -16.370 1.00 45.43 C ANISOU 2520 CD ARG B 21 5898 4826 6536 312 60 261 C ATOM 2521 NE ARG B 21 0.817 -0.002 -17.378 1.00 48.62 N ANISOU 2521 NE ARG B 21 6251 5306 6915 485 83 135 N ATOM 2522 CZ ARG B 21 0.930 -0.806 -18.430 1.00 53.34 C ANISOU 2522 CZ ARG B 21 6955 5760 7552 611 63 17 C ATOM 2523 NH1 ARG B 21 0.045 -1.740 -18.651 1.00 56.49 N ANISOU 2523 NH1 ARG B 21 7538 5888 8037 555 0 3 N ATOM 2524 NH2 ARG B 21 1.924 -0.652 -19.268 1.00 55.44 N ANISOU 2524 NH2 ARG B 21 7135 6172 7756 777 107 -97 N ATOM 2525 N LEU B 22 -0.038 3.022 -12.445 1.00 42.00 N ANISOU 2525 N LEU B 22 5108 5078 5772 40 123 454 N ATOM 2526 CA LEU B 22 -1.154 3.123 -11.542 1.00 41.85 C ANISOU 2526 CA LEU B 22 5099 5105 5695 -77 151 509 C ATOM 2527 C LEU B 22 -2.390 2.802 -12.319 1.00 40.29 C ANISOU 2527 C LEU B 22 4951 4770 5586 -159 180 478 C ATOM 2528 O LEU B 22 -2.449 3.039 -13.520 1.00 42.00 O ANISOU 2528 O LEU B 22 5182 4899 5877 -134 180 369 O ATOM 2529 CB LEU B 22 -1.286 4.510 -10.916 1.00 42.79 C ANISOU 2529 CB LEU B 22 5138 5411 5708 -131 175 411 C ATOM 2530 CG LEU B 22 -0.039 5.167 -10.314 1.00 46.80 C ANISOU 2530 CG LEU B 22 5580 6076 6125 -99 129 383 C ATOM 2531 CD1 LEU B 22 -0.365 6.492 -9.616 1.00 46.98 C ANISOU 2531 CD1 LEU B 22 5578 6230 6043 -168 137 259 C ATOM 2532 CD2 LEU B 22 0.618 4.237 -9.305 1.00 52.54 C ANISOU 2532 CD2 LEU B 22 6300 6892 6772 -37 76 541 C ATOM 2533 N SER B 23 -3.417 2.337 -11.608 1.00 40.65 N ANISOU 2533 N SER B 23 5002 4842 5601 -277 206 575 N ATOM 2534 CA SER B 23 -4.706 2.199 -12.199 1.00 40.71 C ANISOU 2534 CA SER B 23 4996 4801 5671 -390 231 535 C ATOM 2535 C SER B 23 -5.770 2.475 -11.174 1.00 40.80 C ANISOU 2535 C SER B 23 4901 5027 5574 -510 298 583 C ATOM 2536 O SER B 23 -5.596 2.384 -9.983 1.00 43.38 O ANISOU 2536 O SER B 23 5212 5496 5777 -535 324 691 O ATOM 2537 CB SER B 23 -4.813 0.776 -12.792 1.00 41.53 C ANISOU 2537 CB SER B 23 5239 4649 5892 -440 176 615 C ATOM 2538 OG SER B 23 -4.999 -0.116 -11.751 1.00 43.91 O ANISOU 2538 OG SER B 23 5602 4931 6152 -544 171 816 O ATOM 2539 N CYS B 24 -6.953 2.776 -11.659 1.00 42.68 N ANISOU 2539 N CYS B 24 5048 5328 5842 -582 328 499 N ATOM 2540 CA CYS B 24 -8.016 3.088 -10.767 1.00 45.15 C ANISOU 2540 CA CYS B 24 5209 5906 6039 -670 408 515 C ATOM 2541 C CYS B 24 -9.295 2.702 -11.389 1.00 44.67 C ANISOU 2541 C CYS B 24 5052 5875 6047 -809 416 500 C ATOM 2542 O CYS B 24 -9.570 3.069 -12.523 1.00 44.56 O ANISOU 2542 O CYS B 24 5025 5779 6127 -749 366 366 O ATOM 2543 CB CYS B 24 -8.077 4.617 -10.587 1.00 45.85 C ANISOU 2543 CB CYS B 24 5209 6164 6048 -510 434 326 C ATOM 2544 SG CYS B 24 -9.453 5.219 -9.555 1.00 53.83 S ANISOU 2544 SG CYS B 24 5997 7564 6891 -525 546 263 S ATOM 2545 N VAL B 25 -10.148 2.097 -10.595 1.00 46.82 N ANISOU 2545 N VAL B 25 5224 6324 6243 -1003 482 635 N ATOM 2546 CA VAL B 25 -11.423 1.679 -11.095 1.00 54.97 C ANISOU 2546 CA VAL B 25 6117 7440 7329 -1189 489 632 C ATOM 2547 C VAL B 25 -12.496 2.078 -10.082 1.00 57.03 C ANISOU 2547 C VAL B 25 6113 8136 7419 -1268 617 647 C ATOM 2548 O VAL B 25 -12.216 2.215 -8.885 1.00 56.28 O ANISOU 2548 O VAL B 25 6007 8220 7158 -1255 699 731 O ATOM 2549 CB VAL B 25 -11.401 0.154 -11.371 1.00 59.07 C ANISOU 2549 CB VAL B 25 6804 7683 7959 -1439 423 812 C ATOM 2550 CG1 VAL B 25 -11.313 -0.626 -10.047 1.00 60.74 C ANISOU 2550 CG1 VAL B 25 7070 7957 8053 -1620 484 1077 C ATOM 2551 CG2 VAL B 25 -12.622 -0.254 -12.168 1.00 64.76 C ANISOU 2551 CG2 VAL B 25 7396 8445 8764 -1653 388 766 C ATOM 2552 N ASP B 26 -13.672 2.408 -10.615 1.00 65.53 N ANISOU 2552 N ASP B 26 6961 9420 8518 -1297 627 529 N ATOM 2553 CA ASP B 26 -14.947 2.387 -9.901 1.00 73.55 C ANISOU 2553 CA ASP B 26 7667 10881 9398 -1453 747 565 C ATOM 2554 C ASP B 26 -15.732 1.260 -10.670 1.00 82.07 C ANISOU 2554 C ASP B 26 8697 11876 10608 -1791 682 664 C ATOM 2555 O ASP B 26 -16.308 1.499 -11.786 1.00 77.52 O ANISOU 2555 O ASP B 26 8020 11293 10143 -1748 591 509 O ATOM 2556 CB ASP B 26 -15.658 3.754 -9.967 1.00 70.68 C ANISOU 2556 CB ASP B 26 7053 10842 8960 -1166 786 313 C ATOM 2557 CG ASP B 26 -16.981 3.773 -9.197 1.00 75.05 C ANISOU 2557 CG ASP B 26 7228 11942 9346 -1281 929 322 C ATOM 2558 OD1 ASP B 26 -17.149 2.982 -8.251 1.00 84.30 O ANISOU 2558 OD1 ASP B 26 8348 13292 10390 -1558 1039 534 O ATOM 2559 OD2 ASP B 26 -17.841 4.608 -9.499 1.00 70.98 O ANISOU 2559 OD2 ASP B 26 6458 11704 8808 -1080 935 123 O ATOM 2560 N SER B 27 -15.668 0.041 -10.107 1.00 79.34 N ANISOU 2560 N SER B 27 8465 11428 10252 -2122 703 923 N ATOM 2561 CA SER B 27 -16.223 -1.184 -10.713 1.00 85.01 C ANISOU 2561 CA SER B 27 9232 11963 11105 -2500 618 1045 C ATOM 2562 C SER B 27 -17.752 -1.165 -10.758 1.00 86.07 C ANISOU 2562 C SER B 27 8965 12552 11186 -2746 678 1018 C ATOM 2563 O SER B 27 -18.365 -1.973 -11.465 1.00 87.87 O ANISOU 2563 O SER B 27 9175 12676 11535 -3056 582 1048 O ATOM 2564 CB SER B 27 -15.775 -2.453 -9.935 1.00 89.25 C ANISOU 2564 CB SER B 27 10027 12256 11628 -2798 621 1364 C ATOM 2565 OG SER B 27 -14.352 -2.612 -9.904 1.00 86.76 O ANISOU 2565 OG SER B 27 10065 11534 11367 -2565 546 1400 O ATOM 2566 N GLU B 28 -18.350 -0.244 -9.987 1.00 87.33 N ANISOU 2566 N GLU B 28 8794 13232 11155 -2600 830 944 N ATOM 2567 CA GLU B 28 -19.799 -0.100 -9.849 1.00 91.96 C ANISOU 2567 CA GLU B 28 8918 14376 11645 -2773 920 906 C ATOM 2568 C GLU B 28 -20.330 0.640 -11.077 1.00 89.58 C ANISOU 2568 C GLU B 28 8443 14134 11458 -2533 798 627 C ATOM 2569 O GLU B 28 -21.520 0.715 -11.312 1.00 97.18 O ANISOU 2569 O GLU B 28 9021 15513 12392 -2649 810 559 O ATOM 2570 CB GLU B 28 -20.187 0.651 -8.536 1.00 87.33 C ANISOU 2570 CB GLU B 28 8045 14355 10783 -2632 1137 896 C ATOM 2571 CG GLU B 28 -19.787 -0.026 -7.218 1.00 90.69 C ANISOU 2571 CG GLU B 28 8599 14834 11027 -2877 1271 1192 C ATOM 2572 CD GLU B 28 -18.263 -0.052 -6.963 1.00 91.98 C ANISOU 2572 CD GLU B 28 9220 14504 11224 -2675 1200 1256 C ATOM 2573 OE1 GLU B 28 -17.672 0.985 -6.538 1.00 84.04 O ANISOU 2573 OE1 GLU B 28 8248 13571 10114 -2286 1237 1087 O ATOM 2574 OE2 GLU B 28 -17.638 -1.124 -7.188 1.00 89.56 O ANISOU 2574 OE2 GLU B 28 9244 13734 11051 -2902 1093 1467 O ATOM 2575 N ARG B 29 -19.427 1.193 -11.876 1.00 91.18 N ANISOU 2575 N ARG B 29 8925 13941 11780 -2197 673 476 N ATOM 2576 CA ARG B 29 -19.804 2.026 -13.022 1.00 99.25 C ANISOU 2576 CA ARG B 29 9835 14994 12880 -1916 547 232 C ATOM 2577 C ARG B 29 -20.617 3.234 -12.542 1.00 92.86 C ANISOU 2577 C ARG B 29 8656 14703 11924 -1605 643 63 C ATOM 2578 O ARG B 29 -21.314 3.860 -13.357 1.00 93.31 O ANISOU 2578 O ARG B 29 8512 14926 12016 -1405 545 -113 O ATOM 2579 CB ARG B 29 -20.624 1.271 -14.113 1.00103.46 C ANISOU 2579 CB ARG B 29 10250 15525 13534 -2208 402 213 C ATOM 2580 CG ARG B 29 -20.125 -0.103 -14.548 1.00106.46 C ANISOU 2580 CG ARG B 29 10955 15442 14053 -2579 301 360 C ATOM 2581 CD ARG B 29 -18.655 -0.098 -14.933 1.00104.98 C ANISOU 2581 CD ARG B 29 11226 14710 13951 -2350 234 345 C ATOM 2582 NE ARG B 29 -18.267 -1.362 -15.567 1.00108.22 N ANISOU 2582 NE ARG B 29 11940 14677 14503 -2626 106 416 N ATOM 2583 CZ ARG B 29 -17.995 -1.525 -16.863 1.00103.66 C ANISOU 2583 CZ ARG B 29 11540 13816 14030 -2554 -58 265 C ATOM 2584 NH1 ARG B 29 -18.049 -0.511 -17.723 1.00 95.80 N ANISOU 2584 NH1 ARG B 29 10459 12927 13015 -2235 -121 70 N ATOM 2585 NH2 ARG B 29 -17.649 -2.721 -17.307 1.00104.92 N ANISOU 2585 NH2 ARG B 29 11991 13570 14304 -2794 -167 311 N ATOM 2586 N THR B 30 -20.505 3.573 -11.246 1.00 81.15 N ANISOU 2586 N THR B 30 7102 13467 10266 -1529 820 104 N ATOM 2587 CA THR B 30 -21.130 4.789 -10.742 1.00 78.65 C ANISOU 2587 CA THR B 30 6493 13594 9799 -1155 909 -102 C ATOM 2588 C THR B 30 -20.360 6.088 -11.001 1.00 69.26 C ANISOU 2588 C THR B 30 5546 12130 8639 -659 830 -310 C ATOM 2589 O THR B 30 -20.879 7.141 -10.788 1.00 74.41 O ANISOU 2589 O THR B 30 6013 13056 9205 -304 855 -513 O ATOM 2590 CB THR B 30 -21.498 4.699 -9.258 1.00 78.75 C ANISOU 2590 CB THR B 30 6279 14078 9566 -1258 1138 -20 C ATOM 2591 OG1 THR B 30 -20.324 4.449 -8.523 1.00 78.23 O ANISOU 2591 OG1 THR B 30 6567 13706 9449 -1307 1183 118 O ATOM 2592 CG2 THR B 30 -22.514 3.578 -9.019 1.00 80.59 C ANISOU 2592 CG2 THR B 30 6185 14692 9742 -1763 1227 182 C ATOM 2593 N SER B 31 -19.119 6.013 -11.471 1.00 67.05 N ANISOU 2593 N SER B 31 5683 11311 8482 -638 730 -261 N ATOM 2594 CA SER B 31 -18.375 7.225 -11.823 1.00 63.49 C ANISOU 2594 CA SER B 31 5472 10581 8071 -240 641 -431 C ATOM 2595 C SER B 31 -17.303 6.876 -12.810 1.00 56.83 C ANISOU 2595 C SER B 31 4984 9219 7391 -312 508 -356 C ATOM 2596 O SER B 31 -17.039 5.732 -13.035 1.00 55.45 O ANISOU 2596 O SER B 31 4898 8887 7285 -618 495 -196 O ATOM 2597 CB SER B 31 -17.743 7.889 -10.583 1.00 64.66 C ANISOU 2597 CB SER B 31 5725 10776 8069 -67 752 -487 C ATOM 2598 OG SER B 31 -16.623 7.150 -10.132 1.00 62.73 O ANISOU 2598 OG SER B 31 5740 10268 7827 -289 779 -303 O ATOM 2599 N TYR B 32 -16.706 7.906 -13.398 1.00 55.29 N ANISOU 2599 N TYR B 32 4996 8766 7247 -19 408 -479 N ATOM 2600 CA TYR B 32 -15.681 7.789 -14.398 1.00 54.83 C ANISOU 2600 CA TYR B 32 5245 8277 7310 -40 294 -433 C ATOM 2601 C TYR B 32 -14.351 8.318 -13.880 1.00 50.77 C ANISOU 2601 C TYR B 32 5003 7513 6774 54 317 -429 C ATOM 2602 O TYR B 32 -14.110 9.518 -13.885 1.00 50.28 O ANISOU 2602 O TYR B 32 5040 7370 6692 307 275 -555 O ATOM 2603 CB TYR B 32 -16.019 8.640 -15.639 1.00 59.38 C ANISOU 2603 CB TYR B 32 5853 8763 7947 195 143 -551 C ATOM 2604 CG TYR B 32 -17.305 8.343 -16.301 1.00 62.23 C ANISOU 2604 CG TYR B 32 5937 9385 8322 162 75 -588 C ATOM 2605 CD1 TYR B 32 -17.589 7.050 -16.748 1.00 67.90 C ANISOU 2605 CD1 TYR B 32 6585 10120 9094 -173 55 -489 C ATOM 2606 CD2 TYR B 32 -18.239 9.345 -16.538 1.00 64.69 C ANISOU 2606 CD2 TYR B 32 6065 9916 8598 471 5 -732 C ATOM 2607 CE1 TYR B 32 -18.788 6.754 -17.371 1.00 66.83 C ANISOU 2607 CE1 TYR B 32 6172 10254 8968 -248 -27 -533 C ATOM 2608 CE2 TYR B 32 -19.420 9.061 -17.192 1.00 67.32 C ANISOU 2608 CE2 TYR B 32 6105 10535 8937 444 -79 -769 C ATOM 2609 CZ TYR B 32 -19.679 7.765 -17.607 1.00 69.25 C ANISOU 2609 CZ TYR B 32 6260 10823 9228 62 -94 -670 C ATOM 2610 OH TYR B 32 -20.858 7.455 -18.235 1.00 81.79 O ANISOU 2610 OH TYR B 32 7536 12723 10816 -10 -191 -715 O ATOM 2611 N PRO B 33 -13.421 7.444 -13.469 1.00 48.62 N ANISOU 2611 N PRO B 33 4872 7092 6510 -147 363 -285 N ATOM 2612 CA PRO B 33 -12.062 7.877 -13.163 1.00 46.52 C ANISOU 2612 CA PRO B 33 4842 6599 6233 -78 357 -277 C ATOM 2613 C PRO B 33 -11.484 8.580 -14.368 1.00 45.88 C ANISOU 2613 C PRO B 33 4941 6251 6240 48 244 -340 C ATOM 2614 O PRO B 33 -11.368 7.963 -15.451 1.00 42.06 O ANISOU 2614 O PRO B 33 4516 5625 5840 -37 183 -288 O ATOM 2615 CB PRO B 33 -11.326 6.554 -12.897 1.00 45.09 C ANISOU 2615 CB PRO B 33 4752 6302 6077 -307 386 -93 C ATOM 2616 CG PRO B 33 -12.416 5.638 -12.445 1.00 50.65 C ANISOU 2616 CG PRO B 33 5260 7238 6746 -505 452 -1 C ATOM 2617 CD PRO B 33 -13.642 6.012 -13.225 1.00 49.28 C ANISOU 2617 CD PRO B 33 4895 7221 6609 -449 410 -117 C ATOM 2618 N MET B 34 -11.133 9.861 -14.186 1.00 45.03 N ANISOU 2618 N MET B 34 4936 6074 6100 238 213 -451 N ATOM 2619 CA MET B 34 -10.599 10.652 -15.268 1.00 44.03 C ANISOU 2619 CA MET B 34 4998 5697 6035 332 108 -480 C ATOM 2620 C MET B 34 -9.365 11.455 -14.975 1.00 44.47 C ANISOU 2620 C MET B 34 5256 5564 6074 346 90 -495 C ATOM 2621 O MET B 34 -8.701 11.860 -15.884 1.00 44.65 O ANISOU 2621 O MET B 34 5438 5388 6140 335 24 -462 O ATOM 2622 CB MET B 34 -11.676 11.509 -15.862 1.00 47.07 C ANISOU 2622 CB MET B 34 5328 6127 6428 542 25 -586 C ATOM 2623 CG MET B 34 -12.642 10.743 -16.784 1.00 51.36 C ANISOU 2623 CG MET B 34 5710 6792 7011 489 -18 -552 C ATOM 2624 SD MET B 34 -14.144 11.681 -17.182 1.00 60.71 S ANISOU 2624 SD MET B 34 6726 8163 8178 785 -118 -688 S ATOM 2625 CE MET B 34 -13.455 13.028 -18.116 1.00 64.69 C ANISOU 2625 CE MET B 34 7564 8308 8707 979 -263 -695 C ATOM 2626 N GLY B 35 -9.043 11.697 -13.703 1.00 45.02 N ANISOU 2626 N GLY B 35 5318 5724 6065 350 144 -545 N ATOM 2627 CA GLY B 35 -7.869 12.480 -13.391 1.00 42.98 C ANISOU 2627 CA GLY B 35 5239 5304 5787 328 107 -576 C ATOM 2628 C GLY B 35 -6.959 11.883 -12.370 1.00 42.64 C ANISOU 2628 C GLY B 35 5170 5356 5674 195 165 -516 C ATOM 2629 O GLY B 35 -7.339 10.932 -11.632 1.00 40.59 O ANISOU 2629 O GLY B 35 4769 5299 5355 142 246 -451 O ATOM 2630 N TRP B 36 -5.715 12.381 -12.408 1.00 43.15 N ANISOU 2630 N TRP B 36 5369 5281 5744 117 115 -510 N ATOM 2631 CA TRP B 36 -4.648 12.070 -11.462 1.00 42.48 C ANISOU 2631 CA TRP B 36 5270 5287 5583 9 130 -472 C ATOM 2632 C TRP B 36 -4.042 13.384 -10.917 1.00 42.35 C ANISOU 2632 C TRP B 36 5390 5186 5514 2 53 -617 C ATOM 2633 O TRP B 36 -3.642 14.249 -11.658 1.00 41.49 O ANISOU 2633 O TRP B 36 5425 4866 5472 -34 -21 -645 O ATOM 2634 CB TRP B 36 -3.543 11.304 -12.113 1.00 38.77 C ANISOU 2634 CB TRP B 36 4793 4767 5171 -109 128 -326 C ATOM 2635 CG TRP B 36 -3.908 9.956 -12.608 1.00 40.74 C ANISOU 2635 CG TRP B 36 4960 5044 5475 -115 179 -202 C ATOM 2636 CD1 TRP B 36 -4.107 9.610 -13.891 1.00 38.24 C ANISOU 2636 CD1 TRP B 36 4666 4616 5248 -112 172 -164 C ATOM 2637 CD2 TRP B 36 -4.049 8.748 -11.840 1.00 39.01 C ANISOU 2637 CD2 TRP B 36 4655 4951 5215 -144 228 -95 C ATOM 2638 NE1 TRP B 36 -4.426 8.303 -13.979 1.00 40.28 N ANISOU 2638 NE1 TRP B 36 4865 4901 5538 -135 206 -75 N ATOM 2639 CE2 TRP B 36 -4.372 7.729 -12.742 1.00 41.71 C ANISOU 2639 CE2 TRP B 36 4990 5207 5651 -164 239 -13 C ATOM 2640 CE3 TRP B 36 -3.954 8.444 -10.507 1.00 41.52 C ANISOU 2640 CE3 TRP B 36 4923 5437 5414 -163 253 -55 C ATOM 2641 CZ2 TRP B 36 -4.614 6.396 -12.341 1.00 42.54 C ANISOU 2641 CZ2 TRP B 36 5064 5340 5760 -217 267 116 C ATOM 2642 CZ3 TRP B 36 -4.208 7.126 -10.106 1.00 45.54 C ANISOU 2642 CZ3 TRP B 36 5390 6004 5909 -211 291 103 C ATOM 2643 CH2 TRP B 36 -4.542 6.130 -11.029 1.00 41.18 C ANISOU 2643 CH2 TRP B 36 4855 5313 5478 -245 293 188 C ATOM 2644 N PHE B 37 -3.948 13.446 -9.595 1.00 44.09 N ANISOU 2644 N PHE B 37 5573 5581 5599 11 66 -697 N ATOM 2645 CA PHE B 37 -3.347 14.491 -8.837 1.00 46.44 C ANISOU 2645 CA PHE B 37 5990 5840 5816 -18 -14 -856 C ATOM 2646 C PHE B 37 -2.341 13.839 -7.889 1.00 46.93 C ANISOU 2646 C PHE B 37 5958 6114 5760 -142 -13 -782 C ATOM 2647 O PHE B 37 -2.368 12.598 -7.651 1.00 45.41 O ANISOU 2647 O PHE B 37 5626 6095 5533 -151 59 -615 O ATOM 2648 CB PHE B 37 -4.446 15.136 -8.009 1.00 49.88 C ANISOU 2648 CB PHE B 37 6444 6363 6143 176 3 -1067 C ATOM 2649 CG PHE B 37 -5.367 15.955 -8.825 1.00 52.09 C ANISOU 2649 CG PHE B 37 6828 6437 6528 348 -35 -1169 C ATOM 2650 CD1 PHE B 37 -6.386 15.326 -9.588 1.00 52.15 C ANISOU 2650 CD1 PHE B 37 6702 6503 6609 444 32 -1073 C ATOM 2651 CD2 PHE B 37 -5.220 17.349 -8.884 1.00 52.38 C ANISOU 2651 CD2 PHE B 37 7109 6200 6594 410 -160 -1355 C ATOM 2652 CE1 PHE B 37 -7.221 16.078 -10.414 1.00 52.61 C ANISOU 2652 CE1 PHE B 37 6844 6388 6758 627 -28 -1152 C ATOM 2653 CE2 PHE B 37 -6.065 18.103 -9.681 1.00 53.08 C ANISOU 2653 CE2 PHE B 37 7319 6068 6781 606 -220 -1425 C ATOM 2654 CZ PHE B 37 -7.067 17.478 -10.445 1.00 55.68 C ANISOU 2654 CZ PHE B 37 7488 6497 7171 730 -155 -1322 C ATOM 2655 N ARG B 38 -1.478 14.663 -7.298 1.00 46.26 N ANISOU 2655 N ARG B 38 5962 6011 5605 -238 -110 -905 N ATOM 2656 CA ARG B 38 -0.561 14.157 -6.306 1.00 48.68 C ANISOU 2656 CA ARG B 38 6169 6558 5769 -332 -137 -857 C ATOM 2657 C ARG B 38 -0.244 15.228 -5.329 1.00 51.04 C ANISOU 2657 C ARG B 38 6579 6883 5931 -372 -240 -1091 C ATOM 2658 O ARG B 38 -0.406 16.393 -5.629 1.00 53.47 O ANISOU 2658 O ARG B 38 7070 6944 6300 -376 -312 -1267 O ATOM 2659 CB ARG B 38 0.724 13.647 -6.941 1.00 45.90 C ANISOU 2659 CB ARG B 38 5733 6205 5503 -483 -174 -687 C ATOM 2660 CG ARG B 38 1.576 14.734 -7.521 1.00 47.04 C ANISOU 2660 CG ARG B 38 5979 6169 5725 -661 -274 -766 C ATOM 2661 CD ARG B 38 2.772 14.148 -8.191 1.00 47.67 C ANISOU 2661 CD ARG B 38 5912 6332 5867 -790 -278 -596 C ATOM 2662 NE ARG B 38 3.539 15.201 -8.803 1.00 49.45 N ANISOU 2662 NE ARG B 38 6220 6413 6157 -1011 -356 -643 N ATOM 2663 CZ ARG B 38 4.539 15.035 -9.651 1.00 48.90 C ANISOU 2663 CZ ARG B 38 6034 6399 6148 -1160 -347 -519 C ATOM 2664 NH1 ARG B 38 4.934 13.842 -10.056 1.00 46.83 N ANISOU 2664 NH1 ARG B 38 5575 6315 5902 -1065 -271 -365 N ATOM 2665 NH2 ARG B 38 5.156 16.099 -10.088 1.00 49.99 N ANISOU 2665 NH2 ARG B 38 6262 6412 6320 -1410 -419 -556 N ATOM 2666 N ARG B 39 0.229 14.814 -4.163 1.00 54.77 N ANISOU 2666 N ARG B 39 6961 7642 6208 -402 -262 -1089 N ATOM 2667 CA ARG B 39 0.680 15.729 -3.107 1.00 60.86 C ANISOU 2667 CA ARG B 39 7826 8494 6806 -464 -381 -1327 C ATOM 2668 C ARG B 39 1.957 15.170 -2.544 1.00 60.36 C ANISOU 2668 C ARG B 39 7622 8678 6636 -613 -464 -1210 C ATOM 2669 O ARG B 39 1.968 14.061 -1.993 1.00 57.40 O ANISOU 2669 O ARG B 39 7101 8566 6141 -546 -410 -1030 O ATOM 2670 CB ARG B 39 -0.343 15.893 -2.012 1.00 64.35 C ANISOU 2670 CB ARG B 39 8294 9128 7029 -279 -320 -1505 C ATOM 2671 CG ARG B 39 0.006 17.013 -1.026 1.00 73.78 C ANISOU 2671 CG ARG B 39 9640 10349 8043 -314 -456 -1826 C ATOM 2672 CD ARG B 39 -0.986 17.020 0.131 1.00 83.22 C ANISOU 2672 CD ARG B 39 10821 11834 8965 -102 -367 -1999 C ATOM 2673 NE ARG B 39 -1.194 15.626 0.540 1.00 90.79 N ANISOU 2673 NE ARG B 39 11560 13140 9798 -82 -236 -1709 N ATOM 2674 CZ ARG B 39 -0.484 14.968 1.462 1.00101.65 C ANISOU 2674 CZ ARG B 39 12837 14833 10954 -169 -277 -1587 C ATOM 2675 NH1 ARG B 39 0.464 15.579 2.185 1.00101.60 N ANISOU 2675 NH1 ARG B 39 12896 14914 10794 -280 -445 -1762 N ATOM 2676 NH2 ARG B 39 -0.762 13.687 1.698 1.00 99.01 N ANISOU 2676 NH2 ARG B 39 12350 14730 10538 -148 -164 -1285 N ATOM 2677 N ALA B 40 3.043 15.911 -2.785 1.00 64.06 N ANISOU 2677 N ALA B 40 8130 9049 7162 -828 -603 -1287 N ATOM 2678 CA ALA B 40 4.360 15.647 -2.212 1.00 67.12 C ANISOU 2678 CA ALA B 40 8364 9702 7438 -989 -724 -1234 C ATOM 2679 C ALA B 40 4.334 16.148 -0.776 1.00 73.05 C ANISOU 2679 C ALA B 40 9181 10660 7915 -986 -824 -1465 C ATOM 2680 O ALA B 40 3.595 17.084 -0.455 1.00 71.88 O ANISOU 2680 O ALA B 40 9239 10355 7717 -928 -836 -1727 O ATOM 2681 CB ALA B 40 5.449 16.368 -2.987 1.00 64.39 C ANISOU 2681 CB ALA B 40 8015 9211 7239 -1263 -832 -1252 C ATOM 2682 N PRO B 41 5.164 15.553 0.112 1.00 78.69 N ANISOU 2682 N PRO B 41 9726 11740 8432 -1027 -911 -1385 N ATOM 2683 CA PRO B 41 5.208 15.984 1.510 1.00 81.58 C ANISOU 2683 CA PRO B 41 10147 12358 8490 -1031 -1020 -1605 C ATOM 2684 C PRO B 41 5.694 17.457 1.583 1.00 83.30 C ANISOU 2684 C PRO B 41 10545 12379 8727 -1261 -1195 -1938 C ATOM 2685 O PRO B 41 6.674 17.785 0.904 1.00 80.38 O ANISOU 2685 O PRO B 41 10116 11905 8522 -1508 -1293 -1894 O ATOM 2686 CB PRO B 41 6.203 15.006 2.157 1.00 82.55 C ANISOU 2686 CB PRO B 41 10032 12887 8446 -1049 -1109 -1393 C ATOM 2687 CG PRO B 41 6.892 14.292 1.037 1.00 79.50 C ANISOU 2687 CG PRO B 41 9469 12427 8310 -1082 -1077 -1123 C ATOM 2688 CD PRO B 41 6.141 14.501 -0.228 1.00 77.40 C ANISOU 2688 CD PRO B 41 9317 11766 8324 -1052 -929 -1101 C ATOM 2689 N GLY B 42 4.972 18.307 2.333 1.00 82.76 N ANISOU 2689 N GLY B 42 10698 12248 8498 -1177 -1222 -2261 N ATOM 2690 CA GLY B 42 5.240 19.730 2.424 1.00 86.67 C ANISOU 2690 CA GLY B 42 11445 12466 9019 -1361 -1395 -2609 C ATOM 2691 C GLY B 42 4.600 20.628 1.373 1.00 87.81 C ANISOU 2691 C GLY B 42 11849 12074 9443 -1345 -1361 -2708 C ATOM 2692 O GLY B 42 4.501 21.840 1.587 1.00 93.36 O ANISOU 2692 O GLY B 42 12842 12486 10143 -1413 -1496 -3035 O ATOM 2693 N LYS B 43 4.162 20.039 0.253 1.00 84.85 N ANISOU 2693 N LYS B 43 11391 11552 9295 -1247 -1198 -2434 N ATOM 2694 CA LYS B 43 3.598 20.766 -0.880 1.00 82.85 C ANISOU 2694 CA LYS B 43 11357 10816 9304 -1224 -1170 -2458 C ATOM 2695 C LYS B 43 2.062 20.703 -0.981 1.00 78.55 C ANISOU 2695 C LYS B 43 10900 10177 8769 -846 -1013 -2522 C ATOM 2696 O LYS B 43 1.388 19.954 -0.255 1.00 76.52 O ANISOU 2696 O LYS B 43 10495 10255 8324 -622 -886 -2504 O ATOM 2697 CB LYS B 43 4.222 20.259 -2.175 1.00 86.26 C ANISOU 2697 CB LYS B 43 11638 11164 9972 -1396 -1116 -2127 C ATOM 2698 CG LYS B 43 5.666 20.676 -2.409 1.00 94.57 C ANISOU 2698 CG LYS B 43 12635 12221 11078 -1803 -1272 -2090 C ATOM 2699 CD LYS B 43 6.178 20.060 -3.711 1.00 99.02 C ANISOU 2699 CD LYS B 43 13008 12780 11836 -1912 -1174 -1763 C ATOM 2700 CE LYS B 43 5.735 20.818 -4.960 1.00103.42 C ANISOU 2700 CE LYS B 43 13808 12872 12615 -1967 -1148 -1723 C ATOM 2701 NZ LYS B 43 6.652 21.967 -5.242 1.00110.86 N ANISOU 2701 NZ LYS B 43 14910 13584 13628 -2386 -1318 -1794 N ATOM 2702 N GLU B 44 1.523 21.524 -1.888 1.00 77.77 N ANISOU 2702 N GLU B 44 11037 9633 8879 -790 -1031 -2588 N ATOM 2703 CA GLU B 44 0.103 21.566 -2.187 1.00 81.47 C ANISOU 2703 CA GLU B 44 11568 9994 9394 -432 -906 -2644 C ATOM 2704 C GLU B 44 -0.248 20.517 -3.248 1.00 76.06 C ANISOU 2704 C GLU B 44 10668 9366 8867 -380 -742 -2292 C ATOM 2705 O GLU B 44 0.588 20.190 -4.057 1.00 71.52 O ANISOU 2705 O GLU B 44 10018 8727 8430 -611 -757 -2059 O ATOM 2706 CB GLU B 44 -0.295 22.969 -2.674 1.00 92.08 C ANISOU 2706 CB GLU B 44 13291 10812 10885 -363 -1039 -2877 C ATOM 2707 CG GLU B 44 -0.951 23.847 -1.601 1.00104.16 C ANISOU 2707 CG GLU B 44 15037 12303 12234 -107 -1111 -3310 C ATOM 2708 CD GLU B 44 -2.230 23.217 -1.029 1.00112.10 C ANISOU 2708 CD GLU B 44 15837 13691 13066 296 -913 -3375 C ATOM 2709 OE1 GLU B 44 -2.812 22.244 -1.646 1.00 99.78 O ANISOU 2709 OE1 GLU B 44 14022 12308 11581 392 -737 -3090 O ATOM 2710 OE2 GLU B 44 -2.630 23.695 0.058 1.00103.01 O ANISOU 2710 OE2 GLU B 44 14772 12681 11684 495 -936 -3721 O ATOM 2711 N ARG B 45 -1.490 20.007 -3.211 1.00 74.45 N ANISOU 2711 N ARG B 45 10356 9309 8625 -81 -589 -2278 N ATOM 2712 CA ARG B 45 -2.049 19.080 -4.190 1.00 70.44 C ANISOU 2712 CA ARG B 45 9675 8832 8259 -9 -448 -2000 C ATOM 2713 C ARG B 45 -1.726 19.649 -5.565 1.00 66.29 C ANISOU 2713 C ARG B 45 9312 7895 7981 -127 -527 -1899 C ATOM 2714 O ARG B 45 -1.971 20.794 -5.803 1.00 70.44 O ANISOU 2714 O ARG B 45 10101 8086 8577 -66 -636 -2077 O ATOM 2715 CB ARG B 45 -3.576 18.996 -3.977 1.00 75.01 C ANISOU 2715 CB ARG B 45 10188 9539 8773 327 -325 -2109 C ATOM 2716 CG ARG B 45 -4.308 17.793 -4.591 1.00 79.82 C ANISOU 2716 CG ARG B 45 10552 10325 9450 389 -164 -1845 C ATOM 2717 CD ARG B 45 -5.783 18.076 -4.952 1.00 86.79 C ANISOU 2717 CD ARG B 45 11405 11199 10373 689 -96 -1952 C ATOM 2718 NE ARG B 45 -6.767 17.751 -3.893 1.00104.05 N ANISOU 2718 NE ARG B 45 13403 13798 12333 880 39 -2072 N ATOM 2719 CZ ARG B 45 -8.092 17.963 -3.982 1.00103.76 C ANISOU 2719 CZ ARG B 45 13264 13881 12278 1161 116 -2196 C ATOM 2720 NH1 ARG B 45 -8.602 18.511 -5.079 1.00107.90 N ANISOU 2720 NH1 ARG B 45 13879 14113 13004 1308 47 -2217 N ATOM 2721 NH2 ARG B 45 -8.921 17.635 -2.980 1.00 97.80 N ANISOU 2721 NH2 ARG B 45 12300 13574 11287 1300 261 -2292 N ATOM 2722 N GLU B 46 -1.154 18.853 -6.463 1.00 60.44 N ANISOU 2722 N GLU B 46 8430 7177 7355 -289 -477 -1614 N ATOM 2723 CA GLU B 46 -0.963 19.278 -7.836 1.00 58.88 C ANISOU 2723 CA GLU B 46 8361 6657 7353 -388 -519 -1488 C ATOM 2724 C GLU B 46 -1.543 18.307 -8.898 1.00 55.10 C ANISOU 2724 C GLU B 46 7726 6233 6976 -290 -394 -1259 C ATOM 2725 O GLU B 46 -1.543 17.112 -8.733 1.00 51.12 O ANISOU 2725 O GLU B 46 6995 5998 6431 -276 -288 -1122 O ATOM 2726 CB GLU B 46 0.516 19.574 -8.095 1.00 62.14 C ANISOU 2726 CB GLU B 46 8804 7006 7803 -743 -612 -1402 C ATOM 2727 CG GLU B 46 1.431 18.411 -8.392 1.00 65.46 C ANISOU 2727 CG GLU B 46 8945 7706 8221 -893 -533 -1162 C ATOM 2728 CD GLU B 46 2.910 18.776 -8.341 1.00 71.04 C ANISOU 2728 CD GLU B 46 9617 8459 8915 -1232 -632 -1132 C ATOM 2729 OE1 GLU B 46 3.375 19.425 -7.373 1.00 86.00 O ANISOU 2729 OE1 GLU B 46 11586 10378 10711 -1356 -752 -1313 O ATOM 2730 OE2 GLU B 46 3.640 18.401 -9.261 1.00 69.86 O ANISOU 2730 OE2 GLU B 46 9346 8359 8839 -1385 -591 -937 O ATOM 2731 N PHE B 47 -2.043 18.895 -9.981 1.00 51.42 N ANISOU 2731 N PHE B 47 7419 5480 6639 -224 -431 -1228 N ATOM 2732 CA PHE B 47 -2.514 18.243 -11.122 1.00 49.14 C ANISOU 2732 CA PHE B 47 7041 5189 6442 -162 -358 -1045 C ATOM 2733 C PHE B 47 -1.396 17.480 -11.811 1.00 47.76 C ANISOU 2733 C PHE B 47 6738 5107 6300 -401 -312 -825 C ATOM 2734 O PHE B 47 -0.295 17.973 -11.939 1.00 48.68 O ANISOU 2734 O PHE B 47 6923 5150 6423 -638 -375 -792 O ATOM 2735 CB PHE B 47 -3.125 19.244 -12.089 1.00 50.39 C ANISOU 2735 CB PHE B 47 7440 5006 6701 -56 -450 -1063 C ATOM 2736 CG PHE B 47 -3.569 18.603 -13.394 1.00 49.28 C ANISOU 2736 CG PHE B 47 7214 4876 6633 -9 -394 -870 C ATOM 2737 CD1 PHE B 47 -4.796 17.895 -13.455 1.00 46.77 C ANISOU 2737 CD1 PHE B 47 6723 4735 6310 227 -320 -884 C ATOM 2738 CD2 PHE B 47 -2.789 18.717 -14.561 1.00 46.03 C ANISOU 2738 CD2 PHE B 47 6886 4330 6274 -216 -416 -683 C ATOM 2739 CE1 PHE B 47 -5.209 17.309 -14.635 1.00 44.35 C ANISOU 2739 CE1 PHE B 47 6346 4446 6058 254 -292 -735 C ATOM 2740 CE2 PHE B 47 -3.212 18.114 -15.739 1.00 46.02 C ANISOU 2740 CE2 PHE B 47 6814 4367 6305 -161 -371 -534 C ATOM 2741 CZ PHE B 47 -4.396 17.387 -15.772 1.00 44.41 C ANISOU 2741 CZ PHE B 47 6452 4317 6103 70 -318 -567 C ATOM 2742 N VAL B 48 -1.686 16.248 -12.236 1.00 44.61 N ANISOU 2742 N VAL B 48 6144 4888 5916 -335 -204 -688 N ATOM 2743 CA VAL B 48 -0.713 15.418 -12.961 1.00 43.66 C ANISOU 2743 CA VAL B 48 5897 4869 5823 -487 -153 -507 C ATOM 2744 C VAL B 48 -1.129 15.128 -14.384 1.00 42.32 C ANISOU 2744 C VAL B 48 5746 4606 5726 -444 -119 -392 C ATOM 2745 O VAL B 48 -0.371 15.350 -15.320 1.00 43.89 O ANISOU 2745 O VAL B 48 5986 4748 5944 -589 -125 -291 O ATOM 2746 CB VAL B 48 -0.450 14.084 -12.231 1.00 43.72 C ANISOU 2746 CB VAL B 48 5688 5151 5773 -456 -76 -446 C ATOM 2747 CG1 VAL B 48 0.483 13.190 -13.056 1.00 44.80 C ANISOU 2747 CG1 VAL B 48 5702 5377 5945 -535 -29 -290 C ATOM 2748 CG2 VAL B 48 0.194 14.339 -10.905 1.00 43.52 C ANISOU 2748 CG2 VAL B 48 5632 5263 5641 -526 -124 -532 C ATOM 2749 N ALA B 49 -2.330 14.566 -14.534 1.00 41.74 N ANISOU 2749 N ALA B 49 5620 4565 5674 -258 -79 -405 N ATOM 2750 CA ALA B 49 -2.860 14.225 -15.835 1.00 40.97 C ANISOU 2750 CA ALA B 49 5532 4410 5627 -204 -65 -320 C ATOM 2751 C ALA B 49 -4.334 14.016 -15.779 1.00 40.13 C ANISOU 2751 C ALA B 49 5377 4333 5537 -9 -63 -385 C ATOM 2752 O ALA B 49 -4.895 13.706 -14.738 1.00 43.71 O ANISOU 2752 O ALA B 49 5727 4924 5955 67 -25 -459 O ATOM 2753 CB ALA B 49 -2.180 12.967 -16.355 1.00 39.92 C ANISOU 2753 CB ALA B 49 5260 4413 5495 -273 12 -206 C ATOM 2754 N SER B 50 -4.993 14.139 -16.934 1.00 40.22 N ANISOU 2754 N SER B 50 5439 4259 5582 65 -102 -347 N ATOM 2755 CA SER B 50 -6.381 13.764 -17.016 1.00 38.74 C ANISOU 2755 CA SER B 50 5144 4167 5410 229 -103 -397 C ATOM 2756 C SER B 50 -6.662 13.326 -18.426 1.00 37.09 C ANISOU 2756 C SER B 50 4939 3937 5219 226 -130 -312 C ATOM 2757 O SER B 50 -5.822 13.467 -19.289 1.00 36.83 O ANISOU 2757 O SER B 50 5011 3813 5169 123 -141 -224 O ATOM 2758 CB SER B 50 -7.274 14.917 -16.637 1.00 40.29 C ANISOU 2758 CB SER B 50 5418 4287 5603 429 -180 -528 C ATOM 2759 OG SER B 50 -7.207 15.880 -17.696 1.00 42.56 O ANISOU 2759 OG SER B 50 5919 4337 5913 469 -292 -482 O ATOM 2760 N ILE B 51 -7.872 12.831 -18.649 1.00 36.39 N ANISOU 2760 N ILE B 51 4720 3965 5143 330 -143 -348 N ATOM 2761 CA ILE B 51 -8.230 12.309 -19.935 1.00 38.15 C ANISOU 2761 CA ILE B 51 4930 4202 5365 322 -184 -294 C ATOM 2762 C ILE B 51 -9.690 12.396 -20.074 1.00 38.68 C ANISOU 2762 C ILE B 51 4873 4383 5439 478 -249 -364 C ATOM 2763 O ILE B 51 -10.426 12.357 -19.110 1.00 40.33 O ANISOU 2763 O ILE B 51 4933 4736 5656 550 -215 -444 O ATOM 2764 CB ILE B 51 -7.636 10.875 -20.129 1.00 38.85 C ANISOU 2764 CB ILE B 51 4942 4357 5461 166 -103 -242 C ATOM 2765 CG1 ILE B 51 -7.661 10.490 -21.607 1.00 40.18 C ANISOU 2765 CG1 ILE B 51 5163 4508 5597 148 -152 -209 C ATOM 2766 CG2 ILE B 51 -8.348 9.876 -19.202 1.00 38.50 C ANISOU 2766 CG2 ILE B 51 4718 4460 5451 131 -48 -272 C ATOM 2767 CD1 ILE B 51 -6.755 9.302 -21.921 1.00 41.89 C ANISOU 2767 CD1 ILE B 51 5374 4735 5809 37 -82 -184 C ATOM 2768 N THR B 52 -10.137 12.608 -21.307 1.00 42.45 N ANISOU 2768 N THR B 52 5404 4833 5893 545 -352 -334 N ATOM 2769 CA THR B 52 -11.542 12.739 -21.564 1.00 43.01 C ANISOU 2769 CA THR B 52 5331 5050 5963 714 -443 -401 C ATOM 2770 C THR B 52 -12.230 11.384 -21.402 1.00 45.35 C ANISOU 2770 C THR B 52 5376 5575 6280 587 -392 -433 C ATOM 2771 O THR B 52 -11.585 10.306 -21.399 1.00 42.39 O ANISOU 2771 O THR B 52 5006 5177 5922 384 -315 -389 O ATOM 2772 CB THR B 52 -11.766 13.231 -22.989 1.00 45.15 C ANISOU 2772 CB THR B 52 5730 5248 6177 804 -587 -340 C ATOM 2773 OG1 THR B 52 -11.057 12.382 -23.901 1.00 43.71 O ANISOU 2773 OG1 THR B 52 5605 5053 5948 616 -556 -270 O ATOM 2774 CG2 THR B 52 -11.250 14.703 -23.173 1.00 46.55 C ANISOU 2774 CG2 THR B 52 6192 5160 6333 925 -667 -278 C ATOM 2775 N TRP B 53 -13.550 11.471 -21.316 1.00 45.76 N ANISOU 2775 N TRP B 53 5216 5840 6331 712 -450 -508 N ATOM 2776 CA TRP B 53 -14.448 10.359 -21.256 1.00 50.86 C ANISOU 2776 CA TRP B 53 5601 6731 6993 574 -434 -537 C ATOM 2777 C TRP B 53 -14.107 9.267 -22.310 1.00 48.23 C ANISOU 2777 C TRP B 53 5338 6327 6661 363 -472 -492 C ATOM 2778 O TRP B 53 -13.964 8.094 -22.003 1.00 48.07 O ANISOU 2778 O TRP B 53 5267 6317 6680 140 -403 -474 O ATOM 2779 CB TRP B 53 -15.888 10.896 -21.476 1.00 54.17 C ANISOU 2779 CB TRP B 53 5787 7407 7387 787 -545 -623 C ATOM 2780 CG TRP B 53 -16.741 9.844 -21.565 1.00 60.37 C ANISOU 2780 CG TRP B 53 6311 8444 8182 604 -548 -643 C ATOM 2781 CD1 TRP B 53 -17.198 9.083 -20.522 1.00 71.57 C ANISOU 2781 CD1 TRP B 53 7496 10080 9618 424 -423 -648 C ATOM 2782 CD2 TRP B 53 -17.181 9.211 -22.752 1.00 59.82 C ANISOU 2782 CD2 TRP B 53 6197 8434 8098 493 -677 -646 C ATOM 2783 NE1 TRP B 53 -17.993 8.061 -21.000 1.00 72.02 N ANISOU 2783 NE1 TRP B 53 7350 10325 9689 196 -477 -650 N ATOM 2784 CE2 TRP B 53 -17.960 8.098 -22.371 1.00 67.61 C ANISOU 2784 CE2 TRP B 53 6912 9662 9116 235 -639 -665 C ATOM 2785 CE3 TRP B 53 -17.021 9.482 -24.088 1.00 61.55 C ANISOU 2785 CE3 TRP B 53 6578 8545 8263 572 -827 -632 C ATOM 2786 CZ2 TRP B 53 -18.543 7.256 -23.289 1.00 68.95 C ANISOU 2786 CZ2 TRP B 53 6985 9934 9281 46 -759 -696 C ATOM 2787 CZ3 TRP B 53 -17.610 8.660 -24.987 1.00 65.71 C ANISOU 2787 CZ3 TRP B 53 6998 9206 8762 419 -940 -670 C ATOM 2788 CH2 TRP B 53 -18.363 7.560 -24.593 1.00 67.03 C ANISOU 2788 CH2 TRP B 53 6905 9586 8978 156 -914 -714 C ATOM 2789 N SER B 54 -13.972 9.700 -23.553 1.00 44.97 N ANISOU 2789 N SER B 54 5067 5829 6191 451 -591 -477 N ATOM 2790 CA SER B 54 -13.780 8.826 -24.689 1.00 46.44 C ANISOU 2790 CA SER B 54 5321 5987 6336 309 -649 -477 C ATOM 2791 C SER B 54 -12.424 8.058 -24.655 1.00 42.79 C ANISOU 2791 C SER B 54 5036 5333 5889 149 -534 -438 C ATOM 2792 O SER B 54 -12.211 7.143 -25.419 1.00 45.65 O ANISOU 2792 O SER B 54 5455 5664 6225 34 -560 -474 O ATOM 2793 CB SER B 54 -13.814 9.702 -25.943 1.00 44.96 C ANISOU 2793 CB SER B 54 5276 5768 6039 474 -790 -446 C ATOM 2794 OG SER B 54 -12.629 10.436 -25.870 1.00 44.17 O ANISOU 2794 OG SER B 54 5410 5456 5917 511 -720 -357 O ATOM 2795 N GLY B 55 -11.501 8.519 -23.818 1.00 41.48 N ANISOU 2795 N GLY B 55 4959 5049 5751 172 -423 -382 N ATOM 2796 CA GLY B 55 -10.126 8.068 -23.786 1.00 40.84 C ANISOU 2796 CA GLY B 55 5023 4825 5668 83 -326 -338 C ATOM 2797 C GLY B 55 -9.223 8.623 -24.876 1.00 38.33 C ANISOU 2797 C GLY B 55 4887 4430 5247 124 -343 -292 C ATOM 2798 O GLY B 55 -8.093 8.263 -24.933 1.00 37.40 O ANISOU 2798 O GLY B 55 4847 4254 5111 65 -259 -268 O ATOM 2799 N ILE B 56 -9.738 9.515 -25.724 1.00 41.39 N ANISOU 2799 N ILE B 56 5332 4841 5553 230 -453 -268 N ATOM 2800 CA ILE B 56 -8.994 10.018 -26.859 1.00 42.58 C ANISOU 2800 CA ILE B 56 5659 4951 5568 237 -472 -193 C ATOM 2801 C ILE B 56 -7.897 11.052 -26.478 1.00 45.64 C ANISOU 2801 C ILE B 56 6183 5211 5945 215 -401 -81 C ATOM 2802 O ILE B 56 -6.730 10.937 -26.900 1.00 45.49 O ANISOU 2802 O ILE B 56 6240 5194 5850 118 -314 -27 O ATOM 2803 CB ILE B 56 -9.967 10.578 -27.885 1.00 43.42 C ANISOU 2803 CB ILE B 56 5796 5127 5575 354 -637 -178 C ATOM 2804 CG1 ILE B 56 -10.899 9.460 -28.365 1.00 44.56 C ANISOU 2804 CG1 ILE B 56 5796 5423 5712 316 -715 -303 C ATOM 2805 CG2 ILE B 56 -9.214 11.173 -29.065 1.00 43.28 C ANISOU 2805 CG2 ILE B 56 5982 5084 5379 344 -654 -60 C ATOM 2806 CD1 ILE B 56 -12.019 9.897 -29.309 1.00 45.87 C ANISOU 2806 CD1 ILE B 56 5931 5722 5775 439 -907 -309 C ATOM 2807 N ASP B 57 -8.259 12.027 -25.631 1.00 47.70 N ANISOU 2807 N ASP B 57 6462 5381 6282 298 -436 -65 N ATOM 2808 CA ASP B 57 -7.469 13.243 -25.435 1.00 46.81 C ANISOU 2808 CA ASP B 57 6528 5104 6153 272 -431 35 C ATOM 2809 C ASP B 57 -6.939 13.346 -24.010 1.00 46.33 C ANISOU 2809 C ASP B 57 6418 4991 6195 220 -344 -12 C ATOM 2810 O ASP B 57 -7.670 13.724 -23.083 1.00 44.04 O ANISOU 2810 O ASP B 57 6077 4678 5977 337 -377 -92 O ATOM 2811 CB ASP B 57 -8.272 14.488 -25.798 1.00 50.40 C ANISOU 2811 CB ASP B 57 7128 5434 6586 441 -589 85 C ATOM 2812 CG ASP B 57 -8.755 14.450 -27.223 1.00 51.96 C ANISOU 2812 CG ASP B 57 7386 5705 6650 498 -697 155 C ATOM 2813 OD1 ASP B 57 -7.848 14.484 -28.055 1.00 52.05 O ANISOU 2813 OD1 ASP B 57 7521 5717 6539 358 -652 270 O ATOM 2814 OD2 ASP B 57 -9.996 14.327 -27.505 1.00 55.62 O ANISOU 2814 OD2 ASP B 57 7746 6272 7113 669 -818 90 O ATOM 2815 N PRO B 58 -5.648 12.988 -23.802 1.00 41.39 N ANISOU 2815 N PRO B 58 5787 4386 5555 56 -231 27 N ATOM 2816 CA PRO B 58 -4.983 13.230 -22.529 1.00 40.75 C ANISOU 2816 CA PRO B 58 5679 4267 5537 -11 -173 0 C ATOM 2817 C PRO B 58 -4.429 14.677 -22.415 1.00 40.82 C ANISOU 2817 C PRO B 58 5886 4090 5533 -82 -228 64 C ATOM 2818 O PRO B 58 -4.087 15.309 -23.406 1.00 40.65 O ANISOU 2818 O PRO B 58 6019 3988 5437 -155 -268 183 O ATOM 2819 CB PRO B 58 -3.841 12.216 -22.594 1.00 38.66 C ANISOU 2819 CB PRO B 58 5311 4131 5245 -134 -57 22 C ATOM 2820 CG PRO B 58 -3.477 12.248 -24.050 1.00 39.08 C ANISOU 2820 CG PRO B 58 5441 4223 5184 -179 -55 101 C ATOM 2821 CD PRO B 58 -4.776 12.296 -24.760 1.00 40.48 C ANISOU 2821 CD PRO B 58 5662 4373 5344 -49 -159 78 C ATOM 2822 N THR B 59 -4.285 15.114 -21.168 1.00 42.04 N ANISOU 2822 N THR B 59 6041 4185 5747 -86 -228 -13 N ATOM 2823 CA THR B 59 -3.715 16.390 -20.785 1.00 42.52 C ANISOU 2823 CA THR B 59 6296 4045 5816 -182 -291 3 C ATOM 2824 C THR B 59 -2.765 16.115 -19.651 1.00 41.59 C ANISOU 2824 C THR B 59 6067 4025 5710 -320 -220 -51 C ATOM 2825 O THR B 59 -3.160 15.511 -18.617 1.00 42.58 O ANISOU 2825 O THR B 59 6047 4271 5860 -222 -180 -161 O ATOM 2826 CB THR B 59 -4.805 17.312 -20.297 1.00 44.63 C ANISOU 2826 CB THR B 59 6693 4132 6132 35 -408 -105 C ATOM 2827 OG1 THR B 59 -5.728 17.487 -21.367 1.00 44.44 O ANISOU 2827 OG1 THR B 59 6738 4057 6089 196 -493 -47 O ATOM 2828 CG2 THR B 59 -4.260 18.654 -19.893 1.00 47.75 C ANISOU 2828 CG2 THR B 59 7347 4248 6547 -59 -501 -115 C ATOM 2829 N TYR B 60 -1.506 16.531 -19.843 1.00 41.48 N ANISOU 2829 N TYR B 60 6104 3995 5660 -564 -204 38 N ATOM 2830 CA TYR B 60 -0.422 16.324 -18.904 1.00 41.72 C ANISOU 2830 CA TYR B 60 6010 4159 5683 -723 -156 4 C ATOM 2831 C TYR B 60 0.052 17.626 -18.295 1.00 44.97 C ANISOU 2831 C TYR B 60 6608 4370 6107 -888 -255 -35 C ATOM 2832 O TYR B 60 0.144 18.629 -18.974 1.00 46.51 O ANISOU 2832 O TYR B 60 7031 4340 6302 -1005 -332 51 O ATOM 2833 CB TYR B 60 0.727 15.707 -19.659 1.00 42.31 C ANISOU 2833 CB TYR B 60 5940 4443 5694 -889 -59 125 C ATOM 2834 CG TYR B 60 0.355 14.370 -20.250 1.00 40.64 C ANISOU 2834 CG TYR B 60 5575 4397 5468 -724 25 130 C ATOM 2835 CD1 TYR B 60 0.156 13.255 -19.427 1.00 40.32 C ANISOU 2835 CD1 TYR B 60 5372 4483 5466 -593 68 52 C ATOM 2836 CD2 TYR B 60 0.130 14.239 -21.605 1.00 40.23 C ANISOU 2836 CD2 TYR B 60 5576 4351 5357 -704 44 211 C ATOM 2837 CE1 TYR B 60 -0.231 12.008 -19.955 1.00 39.20 C ANISOU 2837 CE1 TYR B 60 5136 4430 5329 -461 122 47 C ATOM 2838 CE2 TYR B 60 -0.229 13.031 -22.149 1.00 41.15 C ANISOU 2838 CE2 TYR B 60 5583 4594 5459 -563 100 181 C ATOM 2839 CZ TYR B 60 -0.383 11.897 -21.305 1.00 39.42 C ANISOU 2839 CZ TYR B 60 5214 4459 5304 -448 136 93 C ATOM 2840 OH TYR B 60 -0.762 10.747 -21.888 1.00 37.11 O ANISOU 2840 OH TYR B 60 4864 4228 5008 -334 167 59 O ATOM 2841 N ALA B 61 0.388 17.605 -17.004 1.00 46.51 N ANISOU 2841 N ALA B 61 6728 4641 6303 -915 -266 -160 N ATOM 2842 CA ALA B 61 1.213 18.682 -16.417 1.00 48.16 C ANISOU 2842 CA ALA B 61 7074 4717 6507 -1157 -360 -205 C ATOM 2843 C ALA B 61 2.563 18.696 -17.108 1.00 50.26 C ANISOU 2843 C ALA B 61 7249 5116 6730 -1481 -317 -43 C ATOM 2844 O ALA B 61 3.126 17.644 -17.499 1.00 49.85 O ANISOU 2844 O ALA B 61 6939 5366 6637 -1483 -198 41 O ATOM 2845 CB ALA B 61 1.379 18.506 -14.924 1.00 47.28 C ANISOU 2845 CB ALA B 61 6861 4739 6366 -1125 -378 -375 C ATOM 2846 N ASP B 62 3.054 19.916 -17.329 1.00 54.07 N ANISOU 2846 N ASP B 62 7958 5364 7221 -1753 -415 6 N ATOM 2847 CA ASP B 62 4.288 20.219 -18.028 1.00 56.77 C ANISOU 2847 CA ASP B 62 8245 5814 7511 -2131 -385 179 C ATOM 2848 C ASP B 62 5.438 19.450 -17.441 1.00 55.60 C ANISOU 2848 C ASP B 62 7737 6081 7309 -2260 -308 157 C ATOM 2849 O ASP B 62 6.289 18.973 -18.177 1.00 56.77 O ANISOU 2849 O ASP B 62 7663 6517 7388 -2399 -198 293 O ATOM 2850 CB ASP B 62 4.639 21.749 -17.904 1.00 60.90 C ANISOU 2850 CB ASP B 62 9099 5972 8066 -2459 -545 194 C ATOM 2851 CG ASP B 62 4.179 22.578 -19.084 1.00 66.92 C ANISOU 2851 CG ASP B 62 10192 6395 8838 -2517 -601 375 C ATOM 2852 OD1 ASP B 62 3.697 22.031 -20.100 1.00 71.27 O ANISOU 2852 OD1 ASP B 62 10696 7039 9345 -2343 -512 502 O ATOM 2853 OD2 ASP B 62 4.296 23.846 -19.027 1.00 85.45 O ANISOU 2853 OD2 ASP B 62 12891 8348 11230 -2749 -757 400 O ATOM 2854 N SER B 63 5.511 19.406 -16.108 1.00 53.03 N ANISOU 2854 N SER B 63 7354 5803 6993 -2214 -375 -19 N ATOM 2855 CA SER B 63 6.622 18.766 -15.461 1.00 57.27 C ANISOU 2855 CA SER B 63 7560 6731 7469 -2325 -341 -38 C ATOM 2856 C SER B 63 6.586 17.216 -15.630 1.00 54.18 C ANISOU 2856 C SER B 63 6873 6662 7051 -2030 -201 2 C ATOM 2857 O SER B 63 7.533 16.578 -15.281 1.00 52.57 O ANISOU 2857 O SER B 63 6383 6796 6795 -2068 -169 14 O ATOM 2858 CB SER B 63 6.606 19.080 -13.988 1.00 58.98 C ANISOU 2858 CB SER B 63 7814 6923 7673 -2319 -463 -237 C ATOM 2859 OG SER B 63 5.375 18.573 -13.523 1.00 61.75 O ANISOU 2859 OG SER B 63 8237 7183 8043 -1942 -440 -338 O ATOM 2860 N VAL B 64 5.487 16.639 -16.145 1.00 52.09 N ANISOU 2860 N VAL B 64 6691 6276 6824 -1739 -139 15 N ATOM 2861 CA VAL B 64 5.438 15.218 -16.386 1.00 52.35 C ANISOU 2861 CA VAL B 64 6506 6539 6844 -1497 -28 48 C ATOM 2862 C VAL B 64 5.216 14.796 -17.847 1.00 50.51 C ANISOU 2862 C VAL B 64 6279 6312 6601 -1427 71 156 C ATOM 2863 O VAL B 64 5.281 13.630 -18.150 1.00 50.36 O ANISOU 2863 O VAL B 64 6100 6464 6569 -1242 154 165 O ATOM 2864 CB VAL B 64 4.398 14.506 -15.477 1.00 50.71 C ANISOU 2864 CB VAL B 64 6320 6278 6669 -1210 -40 -49 C ATOM 2865 CG1 VAL B 64 4.621 14.853 -14.018 1.00 51.50 C ANISOU 2865 CG1 VAL B 64 6407 6427 6732 -1258 -129 -162 C ATOM 2866 CG2 VAL B 64 2.961 14.761 -15.938 1.00 49.71 C ANISOU 2866 CG2 VAL B 64 6409 5881 6598 -1050 -47 -76 C ATOM 2867 N ALA B 65 4.949 15.739 -18.746 1.00 51.96 N ANISOU 2867 N ALA B 65 6670 6295 6777 -1569 50 233 N ATOM 2868 CA ALA B 65 4.608 15.411 -20.136 1.00 52.07 C ANISOU 2868 CA ALA B 65 6721 6317 6746 -1494 128 330 C ATOM 2869 C ALA B 65 5.587 14.459 -20.873 1.00 53.72 C ANISOU 2869 C ALA B 65 6658 6892 6860 -1489 266 384 C ATOM 2870 O ALA B 65 5.185 13.582 -21.647 1.00 59.59 O ANISOU 2870 O ALA B 65 7370 7698 7574 -1286 335 376 O ATOM 2871 CB ALA B 65 4.418 16.703 -20.923 1.00 53.55 C ANISOU 2871 CB ALA B 65 7179 6259 6909 -1699 66 447 C ATOM 2872 N ASP B 66 6.882 14.629 -20.633 1.00 54.86 N ANISOU 2872 N ASP B 66 6596 7300 6950 -1705 299 420 N ATOM 2873 CA ASP B 66 7.880 13.873 -21.336 1.00 58.44 C ANISOU 2873 CA ASP B 66 6766 8144 7295 -1689 433 458 C ATOM 2874 C ASP B 66 7.949 12.426 -20.876 1.00 56.69 C ANISOU 2874 C ASP B 66 6348 8085 7107 -1348 469 346 C ATOM 2875 O ASP B 66 8.557 11.633 -21.555 1.00 59.24 O ANISOU 2875 O ASP B 66 6476 8685 7349 -1225 576 338 O ATOM 2876 CB ASP B 66 9.281 14.543 -21.260 1.00 66.50 C ANISOU 2876 CB ASP B 66 7573 9461 8233 -2047 459 538 C ATOM 2877 CG ASP B 66 9.793 14.734 -19.804 1.00 83.83 C ANISOU 2877 CG ASP B 66 9653 11706 10495 -2135 349 455 C ATOM 2878 OD1 ASP B 66 8.964 15.113 -18.903 1.00 86.40 O ANISOU 2878 OD1 ASP B 66 10206 11702 10919 -2083 224 375 O ATOM 2879 OD2 ASP B 66 11.038 14.540 -19.568 1.00 91.96 O ANISOU 2879 OD2 ASP B 66 10345 13139 11457 -2255 383 462 O ATOM 2880 N ARG B 67 7.314 12.076 -19.743 1.00 55.38 N ANISOU 2880 N ARG B 67 6250 7746 7048 -1188 379 263 N ATOM 2881 CA ARG B 67 7.561 10.795 -19.079 1.00 51.11 C ANISOU 2881 CA ARG B 67 5537 7347 6536 -919 384 197 C ATOM 2882 C ARG B 67 6.349 9.980 -18.698 1.00 46.01 C ANISOU 2882 C ARG B 67 5047 6454 5979 -670 348 144 C ATOM 2883 O ARG B 67 6.499 8.801 -18.376 1.00 43.68 O ANISOU 2883 O ARG B 67 4660 6229 5707 -443 354 116 O ATOM 2884 CB ARG B 67 8.386 11.015 -17.774 1.00 53.41 C ANISOU 2884 CB ARG B 67 5662 7807 6823 -1014 304 181 C ATOM 2885 CG ARG B 67 9.677 11.778 -17.944 1.00 63.15 C ANISOU 2885 CG ARG B 67 6685 9338 7973 -1308 320 228 C ATOM 2886 CD ARG B 67 10.307 12.035 -16.572 1.00 65.80 C ANISOU 2886 CD ARG B 67 6886 9811 8303 -1409 203 189 C ATOM 2887 NE ARG B 67 9.625 13.119 -15.843 1.00 60.52 N ANISOU 2887 NE ARG B 67 6481 8838 7678 -1603 90 146 N ATOM 2888 CZ ARG B 67 9.193 13.031 -14.607 1.00 57.28 C ANISOU 2888 CZ ARG B 67 6143 8337 7285 -1507 -10 68 C ATOM 2889 NH1 ARG B 67 9.344 11.915 -13.934 1.00 60.04 N ANISOU 2889 NH1 ARG B 67 6344 8851 7618 -1246 -21 62 N ATOM 2890 NH2 ARG B 67 8.624 14.068 -14.029 1.00 56.03 N ANISOU 2890 NH2 ARG B 67 6219 7923 7145 -1662 -104 -4 N ATOM 2891 N PHE B 68 5.195 10.639 -18.564 1.00 44.67 N ANISOU 2891 N PHE B 68 5105 6005 5861 -720 294 133 N ATOM 2892 CA PHE B 68 3.955 10.012 -18.119 1.00 41.92 C ANISOU 2892 CA PHE B 68 4876 5463 5587 -541 261 90 C ATOM 2893 C PHE B 68 3.006 9.901 -19.287 1.00 41.67 C ANISOU 2893 C PHE B 68 4980 5284 5567 -478 285 86 C ATOM 2894 O PHE B 68 2.998 10.751 -20.163 1.00 42.26 O ANISOU 2894 O PHE B 68 5140 5320 5595 -596 292 124 O ATOM 2895 CB PHE B 68 3.247 10.788 -17.023 1.00 42.66 C ANISOU 2895 CB PHE B 68 5082 5414 5712 -598 183 51 C ATOM 2896 CG PHE B 68 3.930 10.806 -15.643 1.00 42.76 C ANISOU 2896 CG PHE B 68 4986 5568 5693 -637 134 31 C ATOM 2897 CD1 PHE B 68 5.270 10.519 -15.469 1.00 47.09 C ANISOU 2897 CD1 PHE B 68 5334 6366 6192 -680 138 62 C ATOM 2898 CD2 PHE B 68 3.201 11.216 -14.528 1.00 41.39 C ANISOU 2898 CD2 PHE B 68 4902 5307 5516 -628 76 -32 C ATOM 2899 CE1 PHE B 68 5.850 10.596 -14.217 1.00 46.76 C ANISOU 2899 CE1 PHE B 68 5193 6471 6103 -718 67 43 C ATOM 2900 CE2 PHE B 68 3.778 11.320 -13.268 1.00 43.24 C ANISOU 2900 CE2 PHE B 68 5057 5685 5686 -672 18 -62 C ATOM 2901 CZ PHE B 68 5.110 11.024 -13.119 1.00 45.68 C ANISOU 2901 CZ PHE B 68 5177 6230 5950 -727 3 -20 C ATOM 2902 N THR B 69 2.213 8.819 -19.303 1.00 41.25 N ANISOU 2902 N THR B 69 4954 5151 5566 -306 286 50 N ATOM 2903 CA THR B 69 1.120 8.607 -20.243 1.00 41.34 C ANISOU 2903 CA THR B 69 5084 5031 5593 -246 278 23 C ATOM 2904 C THR B 69 -0.097 8.175 -19.497 1.00 38.51 C ANISOU 2904 C THR B 69 4771 4548 5315 -180 232 -6 C ATOM 2905 O THR B 69 -0.014 7.524 -18.472 1.00 39.31 O ANISOU 2905 O THR B 69 4817 4670 5450 -141 229 5 O ATOM 2906 CB THR B 69 1.464 7.582 -21.359 1.00 44.56 C ANISOU 2906 CB THR B 69 5463 5509 5960 -137 330 -13 C ATOM 2907 OG1 THR B 69 1.871 6.379 -20.752 1.00 52.42 O ANISOU 2907 OG1 THR B 69 6386 6528 7004 -4 335 -37 O ATOM 2908 CG2 THR B 69 2.614 8.040 -22.116 1.00 47.96 C ANISOU 2908 CG2 THR B 69 5813 6132 6279 -207 399 18 C ATOM 2909 N THR B 70 -1.262 8.563 -19.986 1.00 36.87 N ANISOU 2909 N THR B 70 4652 4237 5122 -174 193 -30 N ATOM 2910 CA THR B 70 -2.497 8.178 -19.315 1.00 37.25 C ANISOU 2910 CA THR B 70 4694 4229 5230 -132 161 -59 C ATOM 2911 C THR B 70 -3.437 7.589 -20.357 1.00 34.92 C ANISOU 2911 C THR B 70 4432 3885 4949 -94 131 -96 C ATOM 2912 O THR B 70 -3.344 7.882 -21.492 1.00 36.36 O ANISOU 2912 O THR B 70 4671 4065 5080 -88 117 -105 O ATOM 2913 CB THR B 70 -3.162 9.359 -18.560 1.00 38.73 C ANISOU 2913 CB THR B 70 4908 4390 5417 -140 124 -85 C ATOM 2914 OG1 THR B 70 -4.245 8.856 -17.729 1.00 41.15 O ANISOU 2914 OG1 THR B 70 5147 4733 5755 -103 126 -110 O ATOM 2915 CG2 THR B 70 -3.727 10.389 -19.518 1.00 40.70 C ANISOU 2915 CG2 THR B 70 5262 4555 5649 -117 66 -99 C ATOM 2916 N SER B 71 -4.279 6.648 -19.950 1.00 36.98 N ANISOU 2916 N SER B 71 4655 4126 5269 -93 118 -111 N ATOM 2917 CA SER B 71 -5.263 6.087 -20.830 1.00 36.80 C ANISOU 2917 CA SER B 71 4648 4070 5263 -97 67 -162 C ATOM 2918 C SER B 71 -6.455 5.708 -20.046 1.00 35.37 C ANISOU 2918 C SER B 71 4383 3918 5136 -151 49 -159 C ATOM 2919 O SER B 71 -6.390 5.575 -18.844 1.00 34.08 O ANISOU 2919 O SER B 71 4170 3792 4988 -180 92 -107 O ATOM 2920 CB SER B 71 -4.717 4.874 -21.589 1.00 38.93 C ANISOU 2920 CB SER B 71 4978 4275 5538 -80 68 -200 C ATOM 2921 OG SER B 71 -4.533 3.850 -20.677 1.00 39.63 O ANISOU 2921 OG SER B 71 5062 4299 5696 -98 84 -160 O ATOM 2922 N ARG B 72 -7.563 5.560 -20.769 1.00 36.86 N ANISOU 2922 N ARG B 72 4541 4131 5334 -173 -17 -213 N ATOM 2923 CA ARG B 72 -8.792 5.160 -20.220 1.00 38.08 C ANISOU 2923 CA ARG B 72 4571 4369 5528 -256 -34 -214 C ATOM 2924 C ARG B 72 -9.345 3.989 -21.016 1.00 38.53 C ANISOU 2924 C ARG B 72 4648 4366 5625 -369 -102 -258 C ATOM 2925 O ARG B 72 -9.531 4.074 -22.218 1.00 36.62 O ANISOU 2925 O ARG B 72 4451 4117 5346 -335 -177 -336 O ATOM 2926 CB ARG B 72 -9.791 6.264 -20.346 1.00 41.11 C ANISOU 2926 CB ARG B 72 4853 4890 5879 -170 -78 -262 C ATOM 2927 CG ARG B 72 -10.618 6.367 -19.156 1.00 44.04 C ANISOU 2927 CG ARG B 72 5058 5423 6254 -196 -31 -251 C ATOM 2928 CD ARG B 72 -11.779 7.339 -19.301 1.00 48.16 C ANISOU 2928 CD ARG B 72 5438 6116 6745 -64 -85 -328 C ATOM 2929 NE ARG B 72 -12.787 6.710 -18.498 1.00 57.93 N ANISOU 2929 NE ARG B 72 6458 7567 7987 -183 -38 -318 N ATOM 2930 CZ ARG B 72 -13.936 6.251 -18.927 1.00 53.91 C ANISOU 2930 CZ ARG B 72 5769 7223 7491 -270 -95 -350 C ATOM 2931 NH1 ARG B 72 -14.378 6.491 -20.132 1.00 63.34 N ANISOU 2931 NH1 ARG B 72 6960 8421 8684 -200 -220 -415 N ATOM 2932 NH2 ARG B 72 -14.668 5.611 -18.077 1.00 61.60 N ANISOU 2932 NH2 ARG B 72 6548 8397 8459 -438 -26 -307 N ATOM 2933 N ASP B 73 -9.763 2.950 -20.282 1.00 39.42 N ANISOU 2933 N ASP B 73 4726 4453 5801 -526 -88 -205 N ATOM 2934 CA ASP B 73 -10.445 1.825 -20.849 1.00 41.64 C ANISOU 2934 CA ASP B 73 5030 4657 6135 -693 -169 -246 C ATOM 2935 C ASP B 73 -11.912 2.085 -20.674 1.00 42.53 C ANISOU 2935 C ASP B 73 4916 5000 6243 -808 -201 -258 C ATOM 2936 O ASP B 73 -12.450 1.867 -19.630 1.00 45.23 O ANISOU 2936 O ASP B 73 5131 5456 6598 -935 -142 -170 O ATOM 2937 CB ASP B 73 -9.948 0.534 -20.181 1.00 43.64 C ANISOU 2937 CB ASP B 73 5417 4702 6464 -812 -151 -156 C ATOM 2938 CG ASP B 73 -10.639 -0.752 -20.751 1.00 48.04 C ANISOU 2938 CG ASP B 73 6058 5098 7097 -1031 -258 -205 C ATOM 2939 OD1 ASP B 73 -11.680 -0.676 -21.465 1.00 50.64 O ANISOU 2939 OD1 ASP B 73 6277 5547 7416 -1140 -341 -298 O ATOM 2940 OD2 ASP B 73 -10.102 -1.852 -20.449 1.00 52.52 O ANISOU 2940 OD2 ASP B 73 6816 5405 7735 -1089 -276 -149 O ATOM 2941 N VAL B 74 -12.571 2.591 -21.714 1.00 43.78 N ANISOU 2941 N VAL B 74 5004 5270 6360 -751 -296 -364 N ATOM 2942 CA VAL B 74 -13.955 2.921 -21.617 1.00 45.75 C ANISOU 2942 CA VAL B 74 4995 5793 6596 -811 -340 -391 C ATOM 2943 C VAL B 74 -14.863 1.724 -21.413 1.00 52.10 C ANISOU 2943 C VAL B 74 5690 6645 7462 -1130 -378 -372 C ATOM 2944 O VAL B 74 -15.996 1.898 -21.008 1.00 55.95 O ANISOU 2944 O VAL B 74 5902 7423 7934 -1224 -376 -365 O ATOM 2945 CB VAL B 74 -14.418 3.660 -22.855 1.00 46.98 C ANISOU 2945 CB VAL B 74 5114 6052 6684 -662 -466 -497 C ATOM 2946 CG1 VAL B 74 -13.662 4.974 -23.034 1.00 44.55 C ANISOU 2946 CG1 VAL B 74 4917 5698 6311 -382 -438 -484 C ATOM 2947 CG2 VAL B 74 -14.308 2.776 -24.088 1.00 48.88 C ANISOU 2947 CG2 VAL B 74 5501 6155 6918 -769 -584 -589 C ATOM 2948 N ALA B 75 -14.408 0.520 -21.776 1.00 52.80 N ANISOU 2948 N ALA B 75 5991 6455 7614 -1298 -427 -378 N ATOM 2949 CA ALA B 75 -15.242 -0.682 -21.662 1.00 58.15 C ANISOU 2949 CA ALA B 75 6624 7106 8364 -1655 -492 -356 C ATOM 2950 C ALA B 75 -15.363 -1.159 -20.193 1.00 57.94 C ANISOU 2950 C ALA B 75 6537 7106 8372 -1853 -369 -160 C ATOM 2951 O ALA B 75 -16.403 -1.644 -19.777 1.00 57.11 O ANISOU 2951 O ALA B 75 6240 7178 8282 -2154 -374 -96 O ATOM 2952 CB ALA B 75 -14.714 -1.823 -22.553 1.00 57.88 C ANISOU 2952 CB ALA B 75 6894 6708 8391 -1752 -609 -450 C ATOM 2953 N ASN B 76 -14.298 -1.014 -19.406 1.00 57.75 N ANISOU 2953 N ASN B 76 6662 6942 8338 -1698 -261 -56 N ATOM 2954 CA ASN B 76 -14.433 -1.294 -17.971 1.00 61.80 C ANISOU 2954 CA ASN B 76 7102 7548 8832 -1851 -142 140 C ATOM 2955 C ASN B 76 -14.098 -0.157 -17.003 1.00 55.38 C ANISOU 2955 C ASN B 76 6163 6965 7914 -1618 -4 184 C ATOM 2956 O ASN B 76 -13.808 -0.388 -15.841 1.00 57.15 O ANISOU 2956 O ASN B 76 6407 7214 8094 -1679 93 341 O ATOM 2957 CB ASN B 76 -13.671 -2.537 -17.615 1.00 64.19 C ANISOU 2957 CB ASN B 76 7706 7469 9213 -1985 -164 273 C ATOM 2958 CG ASN B 76 -12.257 -2.396 -17.921 1.00 64.96 C ANISOU 2958 CG ASN B 76 8045 7314 9322 -1682 -170 222 C ATOM 2959 OD1 ASN B 76 -11.726 -1.309 -17.803 1.00 76.68 O ANISOU 2959 OD1 ASN B 76 9455 8947 10735 -1424 -100 179 O ATOM 2960 ND2 ASN B 76 -11.637 -3.455 -18.398 1.00 73.68 N ANISOU 2960 ND2 ASN B 76 9436 8042 10516 -1701 -262 204 N ATOM 2961 N AASN B 77 -14.198 1.080 -17.497 0.43 52.08 N ANISOU 2961 N AASN B 77 5628 6713 7445 -1357 -10 42 N ATOM 2962 N BASN B 77 -14.118 1.080 -17.502 0.57 51.92 N ANISOU 2962 N BASN B 77 5625 6676 7427 -1348 -10 43 N ATOM 2963 CA AASN B 77 -13.974 2.278 -16.708 0.43 48.53 C ANISOU 2963 CA AASN B 77 5082 6454 6903 -1124 90 31 C ATOM 2964 CA BASN B 77 -14.067 2.233 -16.642 0.57 48.51 C ANISOU 2964 CA BASN B 77 5061 6473 6898 -1145 95 38 C ATOM 2965 C AASN B 77 -12.789 2.216 -15.778 0.43 46.92 C ANISOU 2965 C AASN B 77 5050 6109 6669 -1059 170 138 C ATOM 2966 C BASN B 77 -12.779 2.304 -15.787 0.57 46.69 C ANISOU 2966 C BASN B 77 5016 6087 6636 -1042 171 130 C ATOM 2967 O AASN B 77 -12.908 2.470 -14.588 0.43 49.39 O ANISOU 2967 O AASN B 77 5260 6615 6889 -1067 272 211 O ATOM 2968 O BASN B 77 -12.816 2.775 -14.658 0.57 48.66 O ANISOU 2968 O BASN B 77 5168 6531 6790 -999 271 177 O ATOM 2969 CB AASN B 77 -15.205 2.588 -15.913 0.43 50.75 C ANISOU 2969 CB AASN B 77 5042 7137 7104 -1202 168 43 C ATOM 2970 CB BASN B 77 -15.310 2.146 -15.749 0.57 51.62 C ANISOU 2970 CB BASN B 77 5149 7240 7222 -1319 177 95 C ATOM 2971 CG AASN B 77 -16.060 3.570 -16.607 0.43 51.20 C ANISOU 2971 CG AASN B 77 4895 7422 7139 -1013 106 -119 C ATOM 2972 CG BASN B 77 -15.655 3.440 -15.126 0.57 51.06 C ANISOU 2972 CG BASN B 77 4884 7476 7041 -1068 258 7 C ATOM 2973 OD1AASN B 77 -16.503 3.353 -17.736 0.43 50.96 O ANISOU 2973 OD1AASN B 77 4845 7355 7162 -1057 -20 -193 O ATOM 2974 OD1BASN B 77 -15.303 4.482 -15.668 0.57 49.28 O ANISOU 2974 OD1BASN B 77 4726 7181 6818 -783 206 -120 O ATOM 2975 ND2AASN B 77 -16.249 4.712 -15.965 0.43 52.40 N ANISOU 2975 ND2AASN B 77 4917 7791 7200 -767 175 -189 N ATOM 2976 ND2BASN B 77 -16.370 3.399 -13.982 0.57 53.56 N ANISOU 2976 ND2BASN B 77 4964 8139 7247 -1172 384 72 N ATOM 2977 N THR B 78 -11.636 1.881 -16.352 1.00 44.93 N ANISOU 2977 N THR B 78 5042 5553 6476 -979 118 134 N ATOM 2978 CA THR B 78 -10.378 1.871 -15.662 1.00 42.68 C ANISOU 2978 CA THR B 78 4905 5146 6165 -878 164 214 C ATOM 2979 C THR B 78 -9.544 3.032 -16.187 1.00 40.31 C ANISOU 2979 C THR B 78 4654 4821 5839 -635 155 100 C ATOM 2980 O THR B 78 -9.516 3.302 -17.382 1.00 42.11 O ANISOU 2980 O THR B 78 4928 4974 6098 -564 91 -2 O ATOM 2981 CB THR B 78 -9.692 0.494 -15.857 1.00 44.22 C ANISOU 2981 CB THR B 78 5320 5036 6446 -968 110 304 C ATOM 2982 OG1 THR B 78 -10.593 -0.508 -15.393 1.00 50.81 O ANISOU 2982 OG1 THR B 78 6128 5869 7307 -1246 105 428 O ATOM 2983 CG2 THR B 78 -8.383 0.374 -15.098 1.00 43.75 C ANISOU 2983 CG2 THR B 78 5386 4882 6355 -842 139 402 C ATOM 2984 N LEU B 79 -8.877 3.748 -15.283 1.00 38.30 N ANISOU 2984 N LEU B 79 4397 4645 5512 -532 213 123 N ATOM 2985 CA LEU B 79 -7.961 4.835 -15.672 1.00 37.74 C ANISOU 2985 CA LEU B 79 4392 4528 5418 -362 199 40 C ATOM 2986 C LEU B 79 -6.554 4.332 -15.357 1.00 36.72 C ANISOU 2986 C LEU B 79 4377 4286 5290 -336 206 117 C ATOM 2987 O LEU B 79 -6.313 3.705 -14.296 1.00 36.73 O ANISOU 2987 O LEU B 79 4380 4318 5259 -388 234 230 O ATOM 2988 CB LEU B 79 -8.289 6.101 -14.852 1.00 37.38 C ANISOU 2988 CB LEU B 79 4257 4657 5287 -271 237 -25 C ATOM 2989 CG LEU B 79 -7.359 7.296 -14.947 1.00 37.47 C ANISOU 2989 CG LEU B 79 4360 4606 5269 -151 216 -94 C ATOM 2990 CD1 LEU B 79 -7.523 7.974 -16.291 1.00 38.47 C ANISOU 2990 CD1 LEU B 79 4549 4630 5438 -78 148 -165 C ATOM 2991 CD2 LEU B 79 -7.622 8.234 -13.811 1.00 40.07 C ANISOU 2991 CD2 LEU B 79 4637 5079 5507 -83 248 -164 C ATOM 2992 N TYR B 80 -5.611 4.600 -16.260 1.00 36.84 N ANISOU 2992 N TYR B 80 4471 4202 5324 -250 179 66 N ATOM 2993 CA TYR B 80 -4.241 4.231 -16.022 1.00 36.66 C ANISOU 2993 CA TYR B 80 4501 4135 5292 -193 185 117 C ATOM 2994 C TYR B 80 -3.356 5.421 -16.049 1.00 36.00 C ANISOU 2994 C TYR B 80 4400 4126 5154 -141 194 71 C ATOM 2995 O TYR B 80 -3.592 6.365 -16.791 1.00 38.38 O ANISOU 2995 O TYR B 80 4716 4421 5446 -134 183 1 O ATOM 2996 CB TYR B 80 -3.765 3.280 -17.077 1.00 36.59 C ANISOU 2996 CB TYR B 80 4581 3981 5342 -145 155 94 C ATOM 2997 CG TYR B 80 -4.541 1.957 -17.175 1.00 41.17 C ANISOU 2997 CG TYR B 80 5234 4411 5996 -225 116 128 C ATOM 2998 CD1 TYR B 80 -4.165 0.820 -16.408 1.00 45.54 C ANISOU 2998 CD1 TYR B 80 5869 4849 6584 -228 95 246 C ATOM 2999 CD2 TYR B 80 -5.589 1.803 -18.073 1.00 40.12 C ANISOU 2999 CD2 TYR B 80 5110 4235 5900 -305 78 49 C ATOM 3000 CE1 TYR B 80 -4.818 -0.399 -16.566 1.00 43.78 C ANISOU 3000 CE1 TYR B 80 5764 4428 6443 -334 41 284 C ATOM 3001 CE2 TYR B 80 -6.245 0.591 -18.216 1.00 43.30 C ANISOU 3001 CE2 TYR B 80 5592 4483 6376 -425 24 67 C ATOM 3002 CZ TYR B 80 -5.864 -0.494 -17.441 1.00 43.67 C ANISOU 3002 CZ TYR B 80 5748 4377 6470 -454 8 189 C ATOM 3003 OH TYR B 80 -6.534 -1.679 -17.579 1.00 50.75 O ANISOU 3003 OH TYR B 80 6764 5071 7450 -612 -61 220 O ATOM 3004 N LEU B 81 -2.245 5.298 -15.341 1.00 38.01 N ANISOU 3004 N LEU B 81 4633 4439 5372 -112 199 124 N ATOM 3005 CA LEU B 81 -1.128 6.205 -15.479 1.00 38.19 C ANISOU 3005 CA LEU B 81 4626 4537 5349 -105 199 91 C ATOM 3006 C LEU B 81 0.157 5.425 -15.531 1.00 38.64 C ANISOU 3006 C LEU B 81 4640 4640 5402 -27 196 137 C ATOM 3007 O LEU B 81 0.536 4.732 -14.593 1.00 39.73 O ANISOU 3007 O LEU B 81 4753 4819 5524 20 174 214 O ATOM 3008 CB LEU B 81 -1.133 7.153 -14.261 1.00 39.44 C ANISOU 3008 CB LEU B 81 4752 4799 5433 -155 188 74 C ATOM 3009 CG LEU B 81 -0.095 8.258 -14.289 1.00 40.71 C ANISOU 3009 CG LEU B 81 4898 5020 5550 -213 166 30 C ATOM 3010 CD1 LEU B 81 -0.394 9.255 -15.417 1.00 44.23 C ANISOU 3010 CD1 LEU B 81 5426 5357 6023 -257 160 -26 C ATOM 3011 CD2 LEU B 81 -0.052 8.968 -12.946 1.00 43.63 C ANISOU 3011 CD2 LEU B 81 5256 5485 5837 -256 135 -12 C ATOM 3012 N GLN B 82 0.858 5.540 -16.642 1.00 38.61 N ANISOU 3012 N GLN B 82 4618 4656 5395 4 217 93 N ATOM 3013 CA GLN B 82 2.172 4.966 -16.785 1.00 41.36 C ANISOU 3013 CA GLN B 82 4877 5116 5722 110 225 107 C ATOM 3014 C GLN B 82 3.164 6.093 -16.524 1.00 42.44 C ANISOU 3014 C GLN B 82 4891 5448 5785 6 231 106 C ATOM 3015 O GLN B 82 3.144 7.168 -17.176 1.00 40.05 O ANISOU 3015 O GLN B 82 4607 5156 5454 -126 254 77 O ATOM 3016 CB GLN B 82 2.346 4.375 -18.186 1.00 43.04 C ANISOU 3016 CB GLN B 82 5119 5289 5944 209 260 39 C ATOM 3017 CG GLN B 82 3.735 3.791 -18.458 1.00 44.80 C ANISOU 3017 CG GLN B 82 5216 5676 6128 372 283 19 C ATOM 3018 CD GLN B 82 3.938 2.479 -17.759 1.00 45.05 C ANISOU 3018 CD GLN B 82 5284 5613 6219 564 223 57 C ATOM 3019 OE1 GLN B 82 3.014 1.680 -17.610 1.00 45.50 O ANISOU 3019 OE1 GLN B 82 5506 5429 6353 580 180 77 O ATOM 3020 NE2 GLN B 82 5.139 2.268 -17.303 1.00 46.89 N ANISOU 3020 NE2 GLN B 82 5364 6038 6412 697 209 82 N ATOM 3021 N MET B 83 4.010 5.857 -15.528 1.00 44.16 N ANISOU 3021 N MET B 83 4998 5813 5969 48 193 150 N ATOM 3022 CA MET B 83 5.010 6.791 -15.073 1.00 48.49 C ANISOU 3022 CA MET B 83 5407 6573 6444 -76 173 146 C ATOM 3023 C MET B 83 6.352 6.195 -15.431 1.00 48.77 C ANISOU 3023 C MET B 83 5246 6838 6447 47 187 155 C ATOM 3024 O MET B 83 6.732 5.218 -14.871 1.00 50.87 O ANISOU 3024 O MET B 83 5460 7152 6717 236 143 195 O ATOM 3025 CB MET B 83 4.903 6.946 -13.570 1.00 49.71 C ANISOU 3025 CB MET B 83 5559 6775 6553 -109 99 175 C ATOM 3026 CG MET B 83 3.613 7.602 -13.087 1.00 53.42 C ANISOU 3026 CG MET B 83 6184 7086 7027 -202 95 138 C ATOM 3027 SD MET B 83 3.556 7.860 -11.255 1.00 64.82 S ANISOU 3027 SD MET B 83 7614 8661 8355 -237 22 143 S ATOM 3028 CE MET B 83 2.899 6.309 -10.850 1.00 57.04 C ANISOU 3028 CE MET B 83 6679 7605 7389 -77 37 275 C ATOM 3029 N ASN B 84 7.093 6.826 -16.338 1.00 49.78 N ANISOU 3029 N ASN B 84 5256 7130 6528 -59 247 126 N ATOM 3030 CA ASN B 84 8.468 6.401 -16.649 1.00 52.32 C ANISOU 3030 CA ASN B 84 5318 7771 6790 50 277 119 C ATOM 3031 C ASN B 84 9.528 7.347 -16.124 1.00 53.56 C ANISOU 3031 C ASN B 84 5255 8226 6870 -170 244 136 C ATOM 3032 O ASN B 84 9.211 8.472 -15.731 1.00 53.06 O ANISOU 3032 O ASN B 84 5285 8075 6800 -439 204 140 O ATOM 3033 CB ASN B 84 8.611 6.259 -18.182 1.00 52.16 C ANISOU 3033 CB ASN B 84 5278 7804 6735 94 393 71 C ATOM 3034 CG ASN B 84 7.711 5.157 -18.734 1.00 54.45 C ANISOU 3034 CG ASN B 84 5767 7827 7094 327 403 21 C ATOM 3035 OD1 ASN B 84 7.448 4.152 -18.073 1.00 57.85 O ANISOU 3035 OD1 ASN B 84 6272 8113 7595 526 335 31 O ATOM 3036 ND2 ASN B 84 7.207 5.360 -19.914 1.00 57.82 N ANISOU 3036 ND2 ASN B 84 6299 8176 7493 278 472 -21 N ATOM 3037 N SER B 85 10.793 6.898 -16.133 1.00 57.30 N ANISOU 3037 N SER B 85 5432 9058 7282 -51 250 133 N ATOM 3038 CA SER B 85 11.912 7.758 -15.765 1.00 60.43 C ANISOU 3038 CA SER B 85 5558 9807 7594 -295 218 145 C ATOM 3039 C SER B 85 11.647 8.504 -14.465 1.00 57.55 C ANISOU 3039 C SER B 85 5285 9353 7229 -498 86 153 C ATOM 3040 O SER B 85 11.703 9.718 -14.420 1.00 58.28 O ANISOU 3040 O SER B 85 5415 9430 7299 -842 66 142 O ATOM 3041 CB SER B 85 12.133 8.797 -16.885 1.00 62.28 C ANISOU 3041 CB SER B 85 5763 10122 7777 -612 327 156 C ATOM 3042 OG SER B 85 12.659 8.149 -18.008 1.00 68.35 O ANISOU 3042 OG SER B 85 6365 11116 8489 -433 456 134 O ATOM 3043 N LEU B 86 11.297 7.774 -13.409 1.00 57.03 N ANISOU 3043 N LEU B 86 5292 9200 7177 -286 -8 171 N ATOM 3044 CA LEU B 86 10.776 8.414 -12.197 1.00 56.96 C ANISOU 3044 CA LEU B 86 5427 9074 7141 -442 -116 158 C ATOM 3045 C LEU B 86 11.886 9.169 -11.483 1.00 57.43 C ANISOU 3045 C LEU B 86 5247 9470 7101 -666 -221 128 C ATOM 3046 O LEU B 86 13.026 8.762 -11.534 1.00 56.75 O ANISOU 3046 O LEU B 86 4849 9747 6964 -584 -243 148 O ATOM 3047 CB LEU B 86 10.128 7.348 -11.304 1.00 57.15 C ANISOU 3047 CB LEU B 86 5581 8963 7171 -168 -173 217 C ATOM 3048 CG LEU B 86 8.659 7.063 -11.725 1.00 55.39 C ANISOU 3048 CG LEU B 86 5658 8347 7041 -109 -95 224 C ATOM 3049 CD1 LEU B 86 8.073 5.766 -11.196 1.00 52.59 C ANISOU 3049 CD1 LEU B 86 5422 7849 6710 147 -123 317 C ATOM 3050 CD2 LEU B 86 7.763 8.230 -11.281 1.00 56.21 C ANISOU 3050 CD2 LEU B 86 5944 8284 7130 -344 -108 157 C ATOM 3051 N LYS B 87 11.552 10.282 -10.822 1.00 59.85 N ANISOU 3051 N LYS B 87 5696 9668 7377 -945 -297 61 N ATOM 3052 CA LYS B 87 12.559 11.099 -10.097 1.00 63.92 C ANISOU 3052 CA LYS B 87 6018 10476 7795 -1220 -425 4 C ATOM 3053 C LYS B 87 12.095 11.400 -8.689 1.00 62.35 C ANISOU 3053 C LYS B 87 5970 10210 7510 -1244 -561 -68 C ATOM 3054 O LYS B 87 10.905 11.337 -8.414 1.00 58.00 O ANISOU 3054 O LYS B 87 5697 9355 6984 -1135 -529 -87 O ATOM 3055 CB LYS B 87 12.796 12.426 -10.811 1.00 65.75 C ANISOU 3055 CB LYS B 87 6293 10636 8053 -1634 -400 -39 C ATOM 3056 CG LYS B 87 13.000 12.243 -12.285 1.00 73.24 C ANISOU 3056 CG LYS B 87 7160 11611 9056 -1633 -239 40 C ATOM 3057 CD LYS B 87 13.380 13.533 -12.969 1.00 81.15 C ANISOU 3057 CD LYS B 87 8191 12586 10058 -2082 -222 49 C ATOM 3058 CE LYS B 87 12.207 14.489 -12.982 1.00 80.51 C ANISOU 3058 CE LYS B 87 8546 11997 10047 -2218 -252 3 C ATOM 3059 NZ LYS B 87 12.181 15.151 -14.303 1.00 87.09 N ANISOU 3059 NZ LYS B 87 9480 12701 10908 -2446 -153 94 N ATOM 3060 N HIS B 88 13.030 11.781 -7.812 1.00 62.84 N ANISOU 3060 N HIS B 88 5833 10591 7454 -1403 -711 -122 N ATOM 3061 CA HIS B 88 12.679 12.158 -6.458 1.00 65.12 C ANISOU 3061 CA HIS B 88 6259 10866 7617 -1448 -850 -220 C ATOM 3062 C HIS B 88 11.437 13.089 -6.444 1.00 63.66 C ANISOU 3062 C HIS B 88 6462 10247 7480 -1571 -812 -341 C ATOM 3063 O HIS B 88 10.572 12.947 -5.597 1.00 62.60 O ANISOU 3063 O HIS B 88 6510 10004 7270 -1427 -830 -387 O ATOM 3064 CB HIS B 88 13.849 12.831 -5.724 1.00 69.97 C ANISOU 3064 CB HIS B 88 6640 11844 8103 -1728 -1033 -313 C ATOM 3065 CG HIS B 88 13.380 13.774 -4.658 1.00 77.65 C ANISOU 3065 CG HIS B 88 7850 12687 8965 -1915 -1162 -495 C ATOM 3066 ND1 HIS B 88 12.728 13.337 -3.516 1.00 86.76 N ANISOU 3066 ND1 HIS B 88 9139 13849 9975 -1691 -1215 -518 N ATOM 3067 CD2 HIS B 88 13.345 15.127 -4.610 1.00 79.90 C ANISOU 3067 CD2 HIS B 88 8312 12785 9261 -2285 -1237 -670 C ATOM 3068 CE1 HIS B 88 12.361 14.378 -2.787 1.00 82.03 C ANISOU 3068 CE1 HIS B 88 8756 13128 9285 -1893 -1313 -728 C ATOM 3069 NE2 HIS B 88 12.718 15.477 -3.433 1.00 82.74 N ANISOU 3069 NE2 HIS B 88 8894 13064 9480 -2246 -1338 -832 N ATOM 3070 N GLU B 89 11.370 14.032 -7.398 1.00 66.30 N ANISOU 3070 N GLU B 89 6909 10356 7926 -1823 -760 -383 N ATOM 3071 CA GLU B 89 10.263 15.008 -7.563 1.00 65.71 C ANISOU 3071 CA GLU B 89 7204 9845 7917 -1915 -741 -496 C ATOM 3072 C GLU B 89 8.870 14.363 -7.676 1.00 60.20 C ANISOU 3072 C GLU B 89 6700 8904 7269 -1590 -622 -459 C ATOM 3073 O GLU B 89 7.847 15.012 -7.434 1.00 57.03 O ANISOU 3073 O GLU B 89 6566 8226 6878 -1568 -625 -579 O ATOM 3074 CB GLU B 89 10.462 15.833 -8.854 1.00 72.84 C ANISOU 3074 CB GLU B 89 8182 10549 8944 -2180 -685 -456 C ATOM 3075 CG GLU B 89 11.624 16.810 -8.843 1.00 84.40 C ANISOU 3075 CG GLU B 89 9537 12154 10378 -2619 -801 -501 C ATOM 3076 CD GLU B 89 13.010 16.163 -8.699 1.00 90.61 C ANISOU 3076 CD GLU B 89 9869 13476 11081 -2675 -829 -423 C ATOM 3077 OE1 GLU B 89 13.264 15.110 -9.325 1.00 87.41 O ANISOU 3077 OE1 GLU B 89 9236 13278 10697 -2432 -706 -285 O ATOM 3078 OE2 GLU B 89 13.845 16.728 -7.949 1.00 91.78 O ANISOU 3078 OE2 GLU B 89 9888 13844 11140 -2953 -990 -518 O ATOM 3079 N ASP B 90 8.854 13.098 -8.109 1.00 55.73 N ANISOU 3079 N ASP B 90 5992 8442 6739 -1341 -523 -303 N ATOM 3080 CA ASP B 90 7.649 12.324 -8.336 1.00 51.62 C ANISOU 3080 CA ASP B 90 5611 7726 6277 -1077 -413 -241 C ATOM 3081 C ASP B 90 7.204 11.570 -7.087 1.00 50.47 C ANISOU 3081 C ASP B 90 5471 7698 6008 -886 -445 -218 C ATOM 3082 O ASP B 90 6.158 10.949 -7.075 1.00 49.69 O ANISOU 3082 O ASP B 90 5482 7465 5933 -714 -364 -164 O ATOM 3083 CB ASP B 90 7.898 11.330 -9.492 1.00 51.67 C ANISOU 3083 CB ASP B 90 5496 7754 6384 -932 -306 -97 C ATOM 3084 CG ASP B 90 8.261 12.044 -10.823 1.00 52.04 C ANISOU 3084 CG ASP B 90 5540 7717 6515 -1124 -248 -95 C ATOM 3085 OD1 ASP B 90 7.643 13.067 -11.180 1.00 50.95 O ANISOU 3085 OD1 ASP B 90 5617 7321 6422 -1273 -247 -160 O ATOM 3086 OD2 ASP B 90 9.148 11.571 -11.524 1.00 52.65 O ANISOU 3086 OD2 ASP B 90 5408 7994 6601 -1110 -201 -21 O ATOM 3087 N THR B 91 8.014 11.608 -6.032 1.00 52.29 N ANISOU 3087 N THR B 91 5573 8208 6089 -936 -570 -246 N ATOM 3088 CA THR B 91 7.618 11.013 -4.773 1.00 52.72 C ANISOU 3088 CA THR B 91 5653 8401 5978 -785 -611 -213 C ATOM 3089 C THR B 91 6.469 11.793 -4.174 1.00 53.51 C ANISOU 3089 C THR B 91 5979 8348 6004 -815 -589 -374 C ATOM 3090 O THR B 91 6.591 12.963 -3.891 1.00 56.04 O ANISOU 3090 O THR B 91 6385 8627 6281 -989 -666 -571 O ATOM 3091 CB THR B 91 8.793 10.979 -3.803 1.00 55.12 C ANISOU 3091 CB THR B 91 5763 9070 6110 -837 -774 -218 C ATOM 3092 OG1 THR B 91 9.678 9.947 -4.250 1.00 56.57 O ANISOU 3092 OG1 THR B 91 5723 9424 6347 -687 -782 -43 O ATOM 3093 CG2 THR B 91 8.352 10.714 -2.346 1.00 54.54 C ANISOU 3093 CG2 THR B 91 5760 9162 5800 -740 -838 -220 C ATOM 3094 N ALA B 92 5.339 11.123 -3.974 1.00 51.78 N ANISOU 3094 N ALA B 92 5853 8051 5768 -643 -485 -296 N ATOM 3095 CA ALA B 92 4.109 11.783 -3.564 1.00 50.68 C ANISOU 3095 CA ALA B 92 5889 7798 5569 -621 -428 -451 C ATOM 3096 C ALA B 92 3.063 10.718 -3.312 1.00 48.11 C ANISOU 3096 C ALA B 92 5576 7496 5206 -457 -310 -294 C ATOM 3097 O ALA B 92 3.209 9.582 -3.736 1.00 45.28 O ANISOU 3097 O ALA B 92 5153 7120 4929 -379 -274 -80 O ATOM 3098 CB ALA B 92 3.615 12.703 -4.687 1.00 49.48 C ANISOU 3098 CB ALA B 92 5868 7324 5607 -683 -383 -570 C ATOM 3099 N VAL B 93 1.976 11.122 -2.663 1.00 50.38 N ANISOU 3099 N VAL B 93 5954 7816 5372 -410 -249 -414 N ATOM 3100 CA VAL B 93 0.722 10.357 -2.692 1.00 50.51 C ANISOU 3100 CA VAL B 93 5979 7822 5392 -309 -107 -295 C ATOM 3101 C VAL B 93 -0.012 10.756 -3.986 1.00 47.67 C ANISOU 3101 C VAL B 93 5677 7170 5265 -289 -37 -362 C ATOM 3102 O VAL B 93 -0.218 11.913 -4.242 1.00 48.34 O ANISOU 3102 O VAL B 93 5851 7124 5390 -297 -64 -573 O ATOM 3103 CB VAL B 93 -0.152 10.622 -1.451 1.00 52.77 C ANISOU 3103 CB VAL B 93 6284 8348 5417 -259 -52 -400 C ATOM 3104 CG1 VAL B 93 -1.398 9.739 -1.499 1.00 53.05 C ANISOU 3104 CG1 VAL B 93 6280 8426 5451 -208 102 -239 C ATOM 3105 CG2 VAL B 93 0.615 10.406 -0.160 1.00 54.67 C ANISOU 3105 CG2 VAL B 93 6487 8899 5385 -284 -144 -360 C ATOM 3106 N TYR B 94 -0.369 9.761 -4.799 1.00 46.61 N ANISOU 3106 N TYR B 94 5510 6923 5278 -260 34 -177 N ATOM 3107 CA TYR B 94 -1.087 9.926 -6.025 1.00 44.94 C ANISOU 3107 CA TYR B 94 5337 6480 5259 -237 90 -208 C ATOM 3108 C TYR B 94 -2.566 9.551 -5.781 1.00 46.88 C ANISOU 3108 C TYR B 94 5552 6800 5462 -181 202 -188 C ATOM 3109 O TYR B 94 -2.877 8.493 -5.191 1.00 45.83 O ANISOU 3109 O TYR B 94 5364 6808 5242 -202 255 -11 O ATOM 3110 CB TYR B 94 -0.448 9.039 -7.118 1.00 44.18 C ANISOU 3110 CB TYR B 94 5215 6239 5333 -249 82 -44 C ATOM 3111 CG TYR B 94 0.820 9.632 -7.683 1.00 42.04 C ANISOU 3111 CG TYR B 94 4935 5914 5124 -314 2 -95 C ATOM 3112 CD1 TYR B 94 2.018 9.527 -6.999 1.00 45.11 C ANISOU 3112 CD1 TYR B 94 5244 6480 5417 -350 -80 -62 C ATOM 3113 CD2 TYR B 94 0.822 10.290 -8.900 1.00 41.41 C ANISOU 3113 CD2 TYR B 94 4910 5642 5182 -353 7 -161 C ATOM 3114 CE1 TYR B 94 3.203 10.079 -7.495 1.00 46.39 C ANISOU 3114 CE1 TYR B 94 5348 6655 5624 -448 -148 -105 C ATOM 3115 CE2 TYR B 94 2.012 10.841 -9.426 1.00 41.31 C ANISOU 3115 CE2 TYR B 94 4870 5619 5205 -462 -51 -181 C ATOM 3116 CZ TYR B 94 3.191 10.732 -8.693 1.00 43.63 C ANISOU 3116 CZ TYR B 94 5052 6120 5407 -520 -123 -159 C ATOM 3117 OH TYR B 94 4.344 11.275 -9.129 1.00 43.49 O ANISOU 3117 OH TYR B 94 4961 6154 5409 -661 -176 -178 O ATOM 3118 N TYR B 95 -3.454 10.456 -6.208 1.00 46.70 N ANISOU 3118 N TYR B 95 5560 6695 5489 -113 229 -364 N ATOM 3119 CA TYR B 95 -4.865 10.325 -6.070 1.00 46.19 C ANISOU 3119 CA TYR B 95 5419 6746 5385 -46 329 -391 C ATOM 3120 C TYR B 95 -5.517 10.290 -7.423 1.00 46.24 C ANISOU 3120 C TYR B 95 5424 6553 5591 -17 337 -383 C ATOM 3121 O TYR B 95 -5.264 11.130 -8.301 1.00 45.20 O ANISOU 3121 O TYR B 95 5392 6204 5578 25 268 -485 O ATOM 3122 CB TYR B 95 -5.487 11.500 -5.311 1.00 48.93 C ANISOU 3122 CB TYR B 95 5780 7226 5587 83 341 -649 C ATOM 3123 CG TYR B 95 -4.891 11.831 -3.954 1.00 50.50 C ANISOU 3123 CG TYR B 95 6004 7634 5550 74 313 -739 C ATOM 3124 CD1 TYR B 95 -3.814 12.680 -3.851 1.00 50.21 C ANISOU 3124 CD1 TYR B 95 6098 7466 5515 37 185 -871 C ATOM 3125 CD2 TYR B 95 -5.442 11.338 -2.790 1.00 49.97 C ANISOU 3125 CD2 TYR B 95 5829 7917 5241 82 411 -696 C ATOM 3126 CE1 TYR B 95 -3.304 13.030 -2.611 1.00 54.01 C ANISOU 3126 CE1 TYR B 95 6603 8153 5763 22 137 -985 C ATOM 3127 CE2 TYR B 95 -4.928 11.671 -1.560 1.00 53.10 C ANISOU 3127 CE2 TYR B 95 6256 8535 5387 84 377 -793 C ATOM 3128 CZ TYR B 95 -3.844 12.523 -1.488 1.00 54.11 C ANISOU 3128 CZ TYR B 95 6518 8515 5526 59 229 -951 C ATOM 3129 OH TYR B 95 -3.312 12.886 -0.288 1.00 57.85 O ANISOU 3129 OH TYR B 95 7024 9214 5742 49 170 -1074 O ATOM 3130 N CYS B 96 -6.422 9.334 -7.555 1.00 46.99 N ANISOU 3130 N CYS B 96 5409 6740 5704 -57 416 -257 N ATOM 3131 CA CYS B 96 -7.355 9.206 -8.644 1.00 48.35 C ANISOU 3131 CA CYS B 96 5532 6822 6017 -34 429 -263 C ATOM 3132 C CYS B 96 -8.509 10.156 -8.377 1.00 44.40 C ANISOU 3132 C CYS B 96 4943 6482 5446 122 465 -459 C ATOM 3133 O CYS B 96 -8.957 10.288 -7.301 1.00 45.50 O ANISOU 3133 O CYS B 96 4989 6884 5414 161 538 -518 O ATOM 3134 CB CYS B 96 -7.846 7.713 -8.644 1.00 53.13 C ANISOU 3134 CB CYS B 96 6047 7497 6641 -189 490 -48 C ATOM 3135 SG CYS B 96 -9.023 7.294 -9.958 1.00 65.68 S ANISOU 3135 SG CYS B 96 7549 9014 8392 -224 486 -44 S ATOM 3136 N ALA B 97 -8.980 10.827 -9.414 1.00 46.63 N ANISOU 3136 N ALA B 97 5255 6612 5852 238 407 -563 N ATOM 3137 CA ALA B 97 -10.180 11.658 -9.366 1.00 49.25 C ANISOU 3137 CA ALA B 97 5486 7083 6145 444 421 -747 C ATOM 3138 C ALA B 97 -11.184 11.236 -10.459 1.00 47.28 C ANISOU 3138 C ALA B 97 5105 6847 6012 451 409 -698 C ATOM 3139 O ALA B 97 -10.804 10.930 -11.576 1.00 46.87 O ANISOU 3139 O ALA B 97 5148 6565 6096 375 337 -606 O ATOM 3140 CB ALA B 97 -9.806 13.127 -9.514 1.00 49.77 C ANISOU 3140 CB ALA B 97 5752 6926 6233 632 315 -947 C ATOM 3141 N ALA B 98 -12.458 11.200 -10.081 1.00 51.40 N ANISOU 3141 N ALA B 98 5386 7690 6455 535 483 -767 N ATOM 3142 CA ALA B 98 -13.570 10.707 -10.898 1.00 53.02 C ANISOU 3142 CA ALA B 98 5388 8023 6734 511 477 -728 C ATOM 3143 C ALA B 98 -14.686 11.726 -10.979 1.00 57.29 C ANISOU 3143 C ALA B 98 5777 8750 7239 822 452 -939 C ATOM 3144 O ALA B 98 -14.951 12.465 -9.985 1.00 59.05 O ANISOU 3144 O ALA B 98 5947 9167 7321 1023 512 -1111 O ATOM 3145 CB ALA B 98 -14.135 9.411 -10.295 1.00 52.48 C ANISOU 3145 CB ALA B 98 5094 8254 6591 246 602 -565 C ATOM 3146 N ARG B 99 -15.360 11.734 -12.139 1.00 61.25 N ANISOU 3146 N ARG B 99 6202 9218 7852 883 357 -938 N ATOM 3147 CA ARG B 99 -16.656 12.397 -12.337 1.00 66.80 C ANISOU 3147 CA ARG B 99 6669 10185 8527 1170 324 -1102 C ATOM 3148 C ARG B 99 -17.838 11.447 -12.239 1.00 69.91 C ANISOU 3148 C ARG B 99 6660 11029 8874 1005 414 -1041 C ATOM 3149 O ARG B 99 -17.801 10.278 -12.756 1.00 64.24 O ANISOU 3149 O ARG B 99 5903 10276 8229 667 411 -858 O ATOM 3150 CB ARG B 99 -16.757 13.052 -13.698 1.00 69.50 C ANISOU 3150 CB ARG B 99 7152 10259 8996 1356 137 -1132 C ATOM 3151 CG ARG B 99 -15.562 13.901 -14.077 1.00 73.99 C ANISOU 3151 CG ARG B 99 8135 10348 9631 1430 31 -1135 C ATOM 3152 CD ARG B 99 -16.031 15.025 -14.986 1.00 83.93 C ANISOU 3152 CD ARG B 99 9505 11439 10946 1764 -146 -1229 C ATOM 3153 NE ARG B 99 -14.919 15.788 -15.532 1.00 91.03 N ANISOU 3153 NE ARG B 99 10810 11866 11911 1764 -257 -1182 N ATOM 3154 CZ ARG B 99 -14.126 16.590 -14.824 1.00 96.05 C ANISOU 3154 CZ ARG B 99 11692 12275 12526 1813 -258 -1267 C ATOM 3155 NH1 ARG B 99 -14.300 16.742 -13.515 1.00 96.12 N ANISOU 3155 NH1 ARG B 99 11601 12486 12435 1897 -155 -1424 N ATOM 3156 NH2 ARG B 99 -13.129 17.234 -15.434 1.00 99.35 N ANISOU 3156 NH2 ARG B 99 12460 12281 13009 1747 -364 -1192 N ATOM 3157 N ALA B 100 -18.894 11.985 -11.616 1.00 69.37 N ANISOU 3157 N ALA B 100 6294 11379 8683 1253 482 -1212 N ATOM 3158 CA ALA B 100 -20.256 11.490 -11.689 1.00 72.18 C ANISOU 3158 CA ALA B 100 6197 12237 8990 1204 535 -1217 C ATOM 3159 C ALA B 100 -20.741 11.541 -13.137 1.00 75.21 C ANISOU 3159 C ALA B 100 6544 12512 9519 1271 344 -1212 C ATOM 3160 O ALA B 100 -20.417 12.471 -13.864 1.00 72.03 O ANISOU 3160 O ALA B 100 6391 11780 9197 1564 184 -1295 O ATOM 3161 CB ALA B 100 -21.147 12.352 -10.822 1.00 74.34 C ANISOU 3161 CB ALA B 100 6192 12958 9097 1577 626 -1457 C ATOM 3162 N PRO B 101 -21.560 10.572 -13.604 1.00 84.93 N ANISOU 3162 N PRO B 101 7468 14025 10775 994 341 -1111 N ATOM 3163 CA PRO B 101 -22.126 10.662 -14.953 1.00 90.27 C ANISOU 3163 CA PRO B 101 8072 14672 11553 1080 143 -1133 C ATOM 3164 C PRO B 101 -22.956 11.942 -15.148 1.00 91.46 C ANISOU 3164 C PRO B 101 8058 15027 11665 1623 40 -1352 C ATOM 3165 O PRO B 101 -22.922 12.472 -16.267 1.00 94.36 O ANISOU 3165 O PRO B 101 8591 15144 12116 1829 -166 -1370 O ATOM 3166 CB PRO B 101 -23.003 9.400 -15.073 1.00 94.70 C ANISOU 3166 CB PRO B 101 8258 15615 12107 659 186 -1023 C ATOM 3167 CG PRO B 101 -22.678 8.542 -13.885 1.00 96.59 C ANISOU 3167 CG PRO B 101 8476 15956 12268 298 401 -883 C ATOM 3168 CD PRO B 101 -22.030 9.401 -12.839 1.00 88.97 C ANISOU 3168 CD PRO B 101 7689 14915 11200 579 514 -973 C ATOM 3169 N VAL B 102 -23.668 12.390 -14.091 1.00 98.44 N ANISOU 3169 N VAL B 102 8634 16360 12409 1854 179 -1507 N ATOM 3170 CA VAL B 102 -24.440 13.654 -14.066 1.00103.05 C ANISOU 3170 CA VAL B 102 9067 17148 12941 2450 97 -1756 C ATOM 3171 C VAL B 102 -23.500 14.804 -13.759 1.00102.35 C ANISOU 3171 C VAL B 102 9456 16562 12869 2789 48 -1871 C ATOM 3172 O VAL B 102 -23.098 15.536 -14.662 1.00111.86 O ANISOU 3172 O VAL B 102 11000 17318 14185 3011 -158 -1873 O ATOM 3173 CB VAL B 102 -25.603 13.722 -13.019 1.00108.75 C ANISOU 3173 CB VAL B 102 9238 18605 13477 2616 279 -1922 C ATOM 3174 CG1 VAL B 102 -26.782 12.847 -13.425 1.00108.32 C ANISOU 3174 CG1 VAL B 102 8628 19126 13402 2360 287 -1851 C ATOM 3175 CG2 VAL B 102 -25.123 13.448 -11.582 1.00108.48 C ANISOU 3175 CG2 VAL B 102 9232 18697 13288 2434 538 -1916 C ATOM 3176 N ASP B 110 -13.867 20.944 -11.852 1.00104.37 N ANISOU 3176 N ASP B 110 13500 12736 13419 2761 -464 -2135 N ATOM 3177 CA ASP B 110 -13.494 20.210 -10.642 1.00 97.42 C ANISOU 3177 CA ASP B 110 12435 12182 12397 2547 -281 -2173 C ATOM 3178 C ASP B 110 -13.760 18.710 -10.850 1.00 94.10 C ANISOU 3178 C ASP B 110 11648 12149 11959 2277 -124 -1941 C ATOM 3179 O ASP B 110 -14.076 18.285 -11.956 1.00 88.90 O ANISOU 3179 O ASP B 110 10913 11462 11403 2224 -169 -1772 O ATOM 3180 CB ASP B 110 -14.301 20.742 -9.455 1.00 99.67 C ANISOU 3180 CB ASP B 110 12597 12755 12519 2906 -218 -2502 C ATOM 3181 CG ASP B 110 -13.437 21.084 -8.264 1.00103.76 C ANISOU 3181 CG ASP B 110 13299 13215 12910 2802 -190 -2664 C ATOM 3182 OD1 ASP B 110 -12.255 20.682 -8.217 1.00108.74 O ANISOU 3182 OD1 ASP B 110 14059 13693 13564 2417 -187 -2496 O ATOM 3183 OD2 ASP B 110 -13.947 21.768 -7.364 1.00103.13 O ANISOU 3183 OD2 ASP B 110 13224 13269 12693 3127 -178 -2981 O ATOM 3184 N TYR B 111 -13.607 17.916 -9.785 1.00 85.70 N ANISOU 3184 N TYR B 111 10386 11422 10752 2096 45 -1930 N ATOM 3185 CA TYR B 111 -13.967 16.496 -9.794 1.00 75.86 C ANISOU 3185 CA TYR B 111 8813 10537 9475 1845 192 -1724 C ATOM 3186 C TYR B 111 -14.802 16.254 -8.583 1.00 74.93 C ANISOU 3186 C TYR B 111 8395 10924 9152 1949 356 -1857 C ATOM 3187 O TYR B 111 -14.640 16.914 -7.576 1.00 79.06 O ANISOU 3187 O TYR B 111 9000 11507 9531 2102 381 -2066 O ATOM 3188 CB TYR B 111 -12.746 15.569 -9.720 1.00 70.65 C ANISOU 3188 CB TYR B 111 8245 9764 8836 1446 235 -1494 C ATOM 3189 CG TYR B 111 -11.914 15.580 -10.964 1.00 66.83 C ANISOU 3189 CG TYR B 111 7986 8881 8526 1301 114 -1335 C ATOM 3190 CD1 TYR B 111 -10.961 16.549 -11.150 1.00 64.72 C ANISOU 3190 CD1 TYR B 111 8039 8239 8311 1309 -5 -1389 C ATOM 3191 CD2 TYR B 111 -12.080 14.625 -11.963 1.00 66.22 C ANISOU 3191 CD2 TYR B 111 7802 8813 8545 1138 119 -1139 C ATOM 3192 CE1 TYR B 111 -10.187 16.579 -12.282 1.00 61.80 C ANISOU 3192 CE1 TYR B 111 7853 7560 8068 1156 -94 -1230 C ATOM 3193 CE2 TYR B 111 -11.313 14.672 -13.124 1.00 64.59 C ANISOU 3193 CE2 TYR B 111 7796 8284 8460 1027 20 -1012 C ATOM 3194 CZ TYR B 111 -10.361 15.666 -13.255 1.00 61.32 C ANISOU 3194 CZ TYR B 111 7676 7546 8078 1036 -75 -1050 C ATOM 3195 OH TYR B 111 -9.549 15.769 -14.353 1.00 68.09 O ANISOU 3195 OH TYR B 111 8718 8130 9021 901 -152 -914 O ATOM 3196 N ASP B 112 -15.664 15.249 -8.671 1.00 71.02 N ANISOU 3196 N ASP B 112 7550 10811 8625 1826 471 -1727 N ATOM 3197 CA ASP B 112 -16.636 14.966 -7.651 1.00 72.69 C ANISOU 3197 CA ASP B 112 7408 11585 8627 1899 646 -1821 C ATOM 3198 C ASP B 112 -16.152 13.985 -6.597 1.00 67.98 C ANISOU 3198 C ASP B 112 6742 11222 7865 1566 806 -1657 C ATOM 3199 O ASP B 112 -16.606 14.043 -5.477 1.00 71.04 O ANISOU 3199 O ASP B 112 6949 12027 8017 1645 949 -1771 O ATOM 3200 CB ASP B 112 -17.877 14.449 -8.372 1.00 78.74 C ANISOU 3200 CB ASP B 112 7815 12653 9449 1910 666 -1755 C ATOM 3201 CG ASP B 112 -18.303 15.383 -9.511 1.00 79.21 C ANISOU 3201 CG ASP B 112 7965 12463 9670 2251 473 -1879 C ATOM 3202 OD1 ASP B 112 -18.598 16.555 -9.184 1.00 83.77 O ANISOU 3202 OD1 ASP B 112 8617 13018 10194 2671 419 -2150 O ATOM 3203 OD2 ASP B 112 -18.322 14.964 -10.695 1.00 71.74 O ANISOU 3203 OD2 ASP B 112 7040 11333 8886 2114 367 -1714 O ATOM 3204 N TYR B 113 -15.232 13.085 -6.977 1.00 64.40 N ANISOU 3204 N TYR B 113 6439 10509 7521 1215 776 -1388 N ATOM 3205 CA TYR B 113 -14.753 11.980 -6.114 1.00 61.63 C ANISOU 3205 CA TYR B 113 6046 10331 7039 885 898 -1167 C ATOM 3206 C TYR B 113 -13.256 11.859 -6.212 1.00 55.94 C ANISOU 3206 C TYR B 113 5650 9203 6401 733 799 -1055 C ATOM 3207 O TYR B 113 -12.681 12.154 -7.275 1.00 54.08 O ANISOU 3207 O TYR B 113 5611 8566 6370 748 662 -1041 O ATOM 3208 CB TYR B 113 -15.438 10.635 -6.442 1.00 61.26 C ANISOU 3208 CB TYR B 113 5754 10489 7031 582 980 -909 C ATOM 3209 CG TYR B 113 -16.957 10.730 -6.558 1.00 64.77 C ANISOU 3209 CG TYR B 113 5820 11367 7423 698 1059 -1009 C ATOM 3210 CD1 TYR B 113 -17.762 10.883 -5.447 1.00 67.88 C ANISOU 3210 CD1 TYR B 113 5931 12305 7557 786 1231 -1115 C ATOM 3211 CD2 TYR B 113 -17.585 10.686 -7.816 1.00 66.44 C ANISOU 3211 CD2 TYR B 113 5934 11482 7827 731 956 -1008 C ATOM 3212 CE1 TYR B 113 -19.148 11.015 -5.563 1.00 71.26 C ANISOU 3212 CE1 TYR B 113 5958 13190 7926 918 1307 -1225 C ATOM 3213 CE2 TYR B 113 -18.960 10.829 -7.945 1.00 68.13 C ANISOU 3213 CE2 TYR B 113 5765 12129 7991 861 1006 -1115 C ATOM 3214 CZ TYR B 113 -19.732 10.975 -6.810 1.00 70.97 C ANISOU 3214 CZ TYR B 113 5817 13046 8100 950 1187 -1221 C ATOM 3215 OH TYR B 113 -21.078 11.075 -6.943 1.00 74.86 O ANISOU 3215 OH TYR B 113 5880 14026 8536 1076 1245 -1324 O ATOM 3216 N TRP B 114 -12.637 11.411 -5.110 1.00 55.62 N ANISOU 3216 N TRP B 114 5644 9306 6181 587 870 -964 N ATOM 3217 CA TRP B 114 -11.181 11.370 -4.888 1.00 55.12 C ANISOU 3217 CA TRP B 114 5839 8972 6133 475 781 -889 C ATOM 3218 C TRP B 114 -10.879 10.074 -4.221 1.00 54.45 C ANISOU 3218 C TRP B 114 5697 9053 5938 210 861 -606 C ATOM 3219 O TRP B 114 -11.519 9.729 -3.273 1.00 55.23 O ANISOU 3219 O TRP B 114 5627 9541 5816 165 993 -566 O ATOM 3220 CB TRP B 114 -10.719 12.492 -3.933 1.00 60.52 C ANISOU 3220 CB TRP B 114 6652 9702 6641 654 748 -1150 C ATOM 3221 CG TRP B 114 -10.954 13.759 -4.548 1.00 64.96 C ANISOU 3221 CG TRP B 114 7331 10030 7320 912 647 -1412 C ATOM 3222 CD1 TRP B 114 -12.132 14.462 -4.550 1.00 70.65 C ANISOU 3222 CD1 TRP B 114 7924 10922 7998 1197 684 -1638 C ATOM 3223 CD2 TRP B 114 -10.068 14.444 -5.417 1.00 63.80 C ANISOU 3223 CD2 TRP B 114 7450 9419 7373 915 481 -1449 C ATOM 3224 NE1 TRP B 114 -12.009 15.565 -5.360 1.00 73.19 N ANISOU 3224 NE1 TRP B 114 8461 10859 8491 1399 530 -1809 N ATOM 3225 CE2 TRP B 114 -10.754 15.574 -5.908 1.00 66.28 C ANISOU 3225 CE2 TRP B 114 7833 9588 7761 1202 409 -1683 C ATOM 3226 CE3 TRP B 114 -8.745 14.223 -5.822 1.00 64.34 C ANISOU 3226 CE3 TRP B 114 7695 9200 7553 706 386 -1302 C ATOM 3227 CZ2 TRP B 114 -10.158 16.498 -6.749 1.00 67.09 C ANISOU 3227 CZ2 TRP B 114 8215 9239 8038 1249 243 -1748 C ATOM 3228 CZ3 TRP B 114 -8.150 15.145 -6.661 1.00 64.37 C ANISOU 3228 CZ3 TRP B 114 7927 8811 7718 737 243 -1380 C ATOM 3229 CH2 TRP B 114 -8.859 16.277 -7.105 1.00 66.29 C ANISOU 3229 CH2 TRP B 114 8275 8886 8027 990 171 -1589 C ATOM 3230 N GLY B 115 -9.861 9.361 -4.707 1.00 53.74 N ANISOU 3230 N GLY B 115 5758 8671 5988 46 777 -404 N ATOM 3231 CA GLY B 115 -9.351 8.204 -3.997 1.00 54.00 C ANISOU 3231 CA GLY B 115 5808 8793 5916 -159 810 -134 C ATOM 3232 C GLY B 115 -8.650 8.616 -2.717 1.00 53.27 C ANISOU 3232 C GLY B 115 5778 8890 5572 -113 805 -196 C ATOM 3233 O GLY B 115 -8.401 9.780 -2.500 1.00 53.78 O ANISOU 3233 O GLY B 115 5907 8943 5584 54 756 -461 O ATOM 3234 N GLN B 116 -8.355 7.645 -1.865 1.00 53.64 N ANISOU 3234 N GLN B 116 5823 9101 5456 -268 841 53 N ATOM 3235 CA GLN B 116 -7.653 7.893 -0.647 1.00 57.30 C ANISOU 3235 CA GLN B 116 6344 9773 5653 -242 819 29 C ATOM 3236 C GLN B 116 -6.166 8.023 -0.893 1.00 54.99 C ANISOU 3236 C GLN B 116 6220 9204 5468 -226 647 35 C ATOM 3237 O GLN B 116 -5.443 8.452 -0.024 1.00 55.26 O ANISOU 3237 O GLN B 116 6307 9379 5311 -190 584 -46 O ATOM 3238 CB GLN B 116 -7.908 6.795 0.344 1.00 60.14 C ANISOU 3238 CB GLN B 116 6648 10426 5776 -413 910 329 C ATOM 3239 CG GLN B 116 -9.331 6.838 0.836 1.00 65.81 C ANISOU 3239 CG GLN B 116 7150 11550 6304 -443 1102 292 C ATOM 3240 CD GLN B 116 -9.497 5.946 1.986 1.00 70.47 C ANISOU 3240 CD GLN B 116 7700 12484 6589 -627 1197 581 C ATOM 3241 OE1 GLN B 116 -9.151 6.308 3.107 1.00 74.53 O ANISOU 3241 OE1 GLN B 116 8234 13297 6788 -564 1210 520 O ATOM 3242 NE2 GLN B 116 -9.958 4.737 1.720 1.00 74.25 N ANISOU 3242 NE2 GLN B 116 8156 12904 7153 -875 1246 916 N ATOM 3243 N GLY B 117 -5.724 7.610 -2.074 1.00 54.35 N ANISOU 3243 N GLY B 117 6203 8771 5675 -261 575 130 N ATOM 3244 CA GLY B 117 -4.389 7.876 -2.561 1.00 56.67 C ANISOU 3244 CA GLY B 117 6606 8824 6102 -233 430 96 C ATOM 3245 C GLY B 117 -3.483 6.674 -2.486 1.00 58.41 C ANISOU 3245 C GLY B 117 6873 8972 6349 -299 361 379 C ATOM 3246 O GLY B 117 -3.731 5.763 -1.732 1.00 62.41 O ANISOU 3246 O GLY B 117 7373 9630 6710 -368 401 602 O ATOM 3247 N THR B 118 -2.413 6.692 -3.273 1.00 56.40 N ANISOU 3247 N THR B 118 6667 8492 6270 -268 255 373 N ATOM 3248 CA THR B 118 -1.330 5.719 -3.140 1.00 58.31 C ANISOU 3248 CA THR B 118 6939 8693 6522 -256 161 589 C ATOM 3249 C THR B 118 0.024 6.367 -3.086 1.00 53.36 C ANISOU 3249 C THR B 118 6288 8104 5881 -214 35 477 C ATOM 3250 O THR B 118 0.347 7.234 -3.906 1.00 50.75 O ANISOU 3250 O THR B 118 5952 7646 5687 -220 13 296 O ATOM 3251 CB THR B 118 -1.278 4.797 -4.349 1.00 62.28 C ANISOU 3251 CB THR B 118 7488 8898 7277 -244 156 713 C ATOM 3252 OG1 THR B 118 -2.619 4.491 -4.726 1.00 74.55 O ANISOU 3252 OG1 THR B 118 9046 10386 8896 -322 263 739 O ATOM 3253 CG2 THR B 118 -0.550 3.550 -3.980 1.00 63.54 C ANISOU 3253 CG2 THR B 118 7705 9022 7414 -198 76 970 C ATOM 3254 N GLN B 119 0.839 5.898 -2.152 1.00 53.47 N ANISOU 3254 N GLN B 119 6286 8304 5728 -185 -57 610 N ATOM 3255 CA GLN B 119 2.187 6.363 -1.979 1.00 53.22 C ANISOU 3255 CA GLN B 119 6184 8379 5656 -162 -195 532 C ATOM 3256 C GLN B 119 3.024 5.874 -3.142 1.00 52.25 C ANISOU 3256 C GLN B 119 6020 8063 5769 -96 -238 593 C ATOM 3257 O GLN B 119 3.102 4.676 -3.422 1.00 50.61 O ANISOU 3257 O GLN B 119 5849 7737 5643 0 -244 799 O ATOM 3258 CB GLN B 119 2.762 5.858 -0.669 1.00 56.14 C ANISOU 3258 CB GLN B 119 6533 9032 5766 -123 -296 685 C ATOM 3259 CG GLN B 119 4.174 6.349 -0.402 1.00 59.93 C ANISOU 3259 CG GLN B 119 6898 9691 6181 -111 -461 594 C ATOM 3260 CD GLN B 119 4.228 7.843 -0.265 1.00 58.60 C ANISOU 3260 CD GLN B 119 6715 9592 5956 -238 -482 276 C ATOM 3261 OE1 GLN B 119 3.484 8.413 0.524 1.00 62.37 O ANISOU 3261 OE1 GLN B 119 7261 10190 6248 -277 -438 147 O ATOM 3262 NE2 GLN B 119 5.086 8.486 -1.041 1.00 57.53 N ANISOU 3262 NE2 GLN B 119 6502 9380 5976 -307 -546 145 N ATOM 3263 N VAL B 120 3.623 6.827 -3.856 1.00 49.50 N ANISOU 3263 N VAL B 120 5611 7673 5524 -153 -265 405 N ATOM 3264 CA VAL B 120 4.736 6.526 -4.747 1.00 51.03 C ANISOU 3264 CA VAL B 120 5701 7827 5862 -96 -317 438 C ATOM 3265 C VAL B 120 6.036 7.036 -4.135 1.00 50.46 C ANISOU 3265 C VAL B 120 5473 8035 5664 -138 -456 378 C ATOM 3266 O VAL B 120 6.172 8.203 -3.828 1.00 50.88 O ANISOU 3266 O VAL B 120 5517 8169 5645 -296 -494 194 O ATOM 3267 CB VAL B 120 4.452 7.130 -6.121 1.00 49.90 C ANISOU 3267 CB VAL B 120 5586 7461 5914 -165 -234 313 C ATOM 3268 CG1 VAL B 120 5.677 7.141 -7.031 1.00 49.50 C ANISOU 3268 CG1 VAL B 120 5393 7453 5963 -152 -269 302 C ATOM 3269 CG2 VAL B 120 3.299 6.371 -6.750 1.00 47.87 C ANISOU 3269 CG2 VAL B 120 5446 6967 5775 -104 -129 395 C ATOM 3270 N THR B 121 6.970 6.127 -3.869 1.00 53.57 N ANISOU 3270 N THR B 121 5753 8582 6019 13 -551 532 N ATOM 3271 CA THR B 121 8.261 6.531 -3.269 1.00 58.22 C ANISOU 3271 CA THR B 121 6141 9503 6477 -19 -705 483 C ATOM 3272 C THR B 121 9.398 6.163 -4.186 1.00 57.66 C ANISOU 3272 C THR B 121 5864 9507 6537 82 -734 510 C ATOM 3273 O THR B 121 9.601 4.972 -4.474 1.00 57.09 O ANISOU 3273 O THR B 121 5784 9375 6533 332 -740 670 O ATOM 3274 CB THR B 121 8.455 5.918 -1.868 1.00 60.56 C ANISOU 3274 CB THR B 121 6436 10040 6534 91 -830 631 C ATOM 3275 OG1 THR B 121 7.447 6.444 -1.002 1.00 62.64 O ANISOU 3275 OG1 THR B 121 6856 10313 6632 -27 -784 563 O ATOM 3276 CG2 THR B 121 9.790 6.245 -1.298 1.00 63.31 C ANISOU 3276 CG2 THR B 121 6551 10760 6745 76 -1010 584 C ATOM 3277 N VAL B 122 10.105 7.198 -4.654 1.00 56.97 N ANISOU 3277 N VAL B 122 5622 9543 6480 -119 -750 348 N ATOM 3278 CA VAL B 122 11.302 7.059 -5.488 1.00 59.14 C ANISOU 3278 CA VAL B 122 5631 10004 6837 -77 -765 347 C ATOM 3279 C VAL B 122 12.575 7.174 -4.621 1.00 61.15 C ANISOU 3279 C VAL B 122 5601 10705 6928 -88 -949 343 C ATOM 3280 O VAL B 122 12.935 8.222 -4.087 1.00 63.08 O ANISOU 3280 O VAL B 122 5775 11125 7068 -362 -1038 209 O ATOM 3281 CB VAL B 122 11.318 8.050 -6.668 1.00 59.55 C ANISOU 3281 CB VAL B 122 5669 9942 7016 -324 -656 216 C ATOM 3282 CG1 VAL B 122 12.398 7.668 -7.670 1.00 61.73 C ANISOU 3282 CG1 VAL B 122 5668 10423 7363 -236 -620 242 C ATOM 3283 CG2 VAL B 122 9.957 8.082 -7.364 1.00 57.49 C ANISOU 3283 CG2 VAL B 122 5695 9267 6880 -324 -509 206 C ATOM 3284 N SER B 123 13.236 6.041 -4.451 1.00 61.63 N ANISOU 3284 N SER B 123 5514 10940 6964 231 -1027 488 N ATOM 3285 CA SER B 123 14.365 5.947 -3.582 1.00 64.28 C ANISOU 3285 CA SER B 123 5574 11718 7133 297 -1223 515 C ATOM 3286 C SER B 123 15.282 4.879 -4.071 1.00 66.06 C ANISOU 3286 C SER B 123 5561 12120 7417 661 -1261 621 C ATOM 3287 O SER B 123 14.821 3.909 -4.658 1.00 64.20 O ANISOU 3287 O SER B 123 5489 11593 7310 933 -1173 718 O ATOM 3288 CB SER B 123 13.907 5.596 -2.172 1.00 65.19 C ANISOU 3288 CB SER B 123 5860 11861 7047 381 -1348 623 C ATOM 3289 OG SER B 123 15.026 5.431 -1.323 1.00 65.80 O ANISOU 3289 OG SER B 123 5665 12393 6943 479 -1566 665 O ATOM 3290 N SER B 124 16.579 5.083 -3.833 1.00 70.85 N ANISOU 3290 N SER B 124 5775 13216 7929 663 -1399 580 N ATOM 3291 CA SER B 124 17.611 4.118 -4.128 1.00 75.78 C ANISOU 3291 CA SER B 124 6101 14122 8570 1061 -1471 658 C ATOM 3292 C SER B 124 17.610 2.930 -3.140 1.00 81.60 C ANISOU 3292 C SER B 124 6955 14847 9204 1478 -1649 867 C ATOM 3293 O SER B 124 18.158 1.882 -3.449 1.00 84.57 O ANISOU 3293 O SER B 124 7224 15274 9635 1914 -1699 957 O ATOM 3294 CB SER B 124 18.966 4.801 -4.115 1.00 77.84 C ANISOU 3294 CB SER B 124 5862 14973 8740 893 -1571 546 C ATOM 3295 OG SER B 124 19.339 5.143 -2.786 1.00 81.48 O ANISOU 3295 OG SER B 124 6229 15741 8988 784 -1800 556 O ATOM 3296 N ALA B 125 16.991 3.093 -1.960 1.00 84.79 N ANISOU 3296 N ALA B 125 7592 15180 9445 1357 -1746 946 N ATOM 3297 CA ALA B 125 16.834 1.984 -0.996 1.00 90.76 C ANISOU 3297 CA ALA B 125 8530 15877 10078 1704 -1904 1194 C ATOM 3298 C ALA B 125 15.819 0.899 -1.443 1.00 92.34 C ANISOU 3298 C ALA B 125 9131 15514 10439 1933 -1785 1360 C ATOM 3299 O ALA B 125 15.673 -0.122 -0.778 1.00 95.48 O ANISOU 3299 O ALA B 125 9724 15791 10765 2218 -1909 1599 O ATOM 3300 CB ALA B 125 16.492 2.522 0.396 1.00 90.98 C ANISOU 3300 CB ALA B 125 8671 16061 9837 1479 -2029 1225 C ATOM 3301 N ALA B 126 15.141 1.145 -2.578 1.00 99.95 N ANISOU 3301 N ALA B 126 10222 16143 11612 1786 -1561 1237 N ATOM 3302 CA ALA B 126 14.259 0.187 -3.287 1.00100.03 C ANISOU 3302 CA ALA B 126 10563 15633 11810 1963 -1440 1333 C ATOM 3303 C ALA B 126 14.990 -1.078 -3.780 1.00105.41 C ANISOU 3303 C ALA B 126 11194 16260 12598 2465 -1526 1420 C ATOM 3304 O ALA B 126 16.159 -1.276 -3.459 1.00119.84 O ANISOU 3304 O ALA B 126 12718 18479 14336 2720 -1689 1436 O ATOM 3305 CB ALA B 126 13.584 0.894 -4.462 1.00 92.73 C ANISOU 3305 CB ALA B 126 9698 14477 11057 1690 -1208 1141 C ATOM 3306 N ALA B 127 14.284 -1.933 -4.536 1.00107.41 N ANISOU 3306 N ALA B 127 11747 16030 13035 2616 -1430 1463 N ATOM 3307 CA ALA B 127 14.869 -3.126 -5.178 1.00115.63 C ANISOU 3307 CA ALA B 127 12802 16926 14205 3111 -1495 1488 C ATOM 3308 C ALA B 127 14.500 -3.229 -6.659 1.00114.85 C ANISOU 3308 C ALA B 127 12775 16551 14311 3114 -1299 1296 C ATOM 3309 O ALA B 127 15.362 -3.303 -7.537 1.00122.31 O ANISOU 3309 O ALA B 127 13452 17709 15310 3347 -1259 1129 O ATOM 3310 CB ALA B 127 14.449 -4.394 -4.443 1.00118.88 C ANISOU 3310 CB ALA B 127 13600 16958 14612 3377 -1654 1775 C ATOM 3311 OXT ALA B 127 13.331 -3.246 -7.027 1.00109.05 O ANISOU 3311 OXT ALA B 127 12352 15409 13674 2888 -1174 1298 O TER 3312 ALA B 127 HETATM 3313 C9 OLC A 401 -13.449 6.447 -51.764 1.00 66.89 C HETATM 3314 C8 OLC A 401 -14.222 7.270 -52.752 1.00 77.22 C HETATM 3315 C24 OLC A 401 -15.982 8.526 -66.215 1.00 86.16 C HETATM 3316 C7 OLC A 401 -14.299 6.641 -54.116 1.00 87.14 C HETATM 3317 C6 OLC A 401 -15.036 7.467 -55.166 1.00 83.90 C HETATM 3318 C5 OLC A 401 -14.738 7.061 -56.597 1.00 71.42 C HETATM 3319 C4 OLC A 401 -15.624 7.711 -57.645 1.00 71.87 C HETATM 3320 C3 OLC A 401 -15.474 7.102 -59.031 1.00 75.71 C HETATM 3321 C2 OLC A 401 -16.008 7.975 -60.138 1.00 83.88 C HETATM 3322 C21 OLC A 401 -15.996 7.846 -63.777 1.00 86.34 C HETATM 3323 C1 OLC A 401 -15.383 7.687 -61.486 1.00 87.16 C HETATM 3324 C22 OLC A 401 -15.520 8.846 -64.809 1.00 85.73 C HETATM 3325 O19 OLC A 401 -14.491 6.904 -61.678 1.00115.70 O HETATM 3326 O25 OLC A 401 -15.499 9.483 -67.156 1.00 88.60 O HETATM 3327 O23 OLC A 401 -15.973 10.153 -64.459 1.00 96.09 O HETATM 3328 O20 OLC A 401 -15.920 8.429 -62.454 1.00 84.18 O HETATM 3329 C10 OLC A 402 -11.786 3.749 -55.761 1.00 70.12 C HETATM 3330 C9 OLC A 402 -12.062 3.267 -56.938 1.00 71.33 C HETATM 3331 C11 OLC A 402 -11.432 5.172 -55.466 1.00 93.01 C HETATM 3332 C8 OLC A 402 -12.021 4.028 -58.224 1.00 73.73 C HETATM 3333 C24 OLC A 402 -14.921 6.374 -68.923 1.00100.76 C HETATM 3334 C7 OLC A 402 -11.525 3.217 -59.384 1.00 77.91 C HETATM 3335 C6 OLC A 402 -10.195 3.680 -59.962 1.00 72.89 C HETATM 3336 C5 OLC A 402 -10.186 3.821 -61.463 1.00 75.90 C HETATM 3337 C4 OLC A 402 -10.873 5.057 -61.981 1.00 64.65 C HETATM 3338 C3 OLC A 402 -11.928 4.814 -63.048 1.00 61.95 C HETATM 3339 C2 OLC A 402 -11.427 5.073 -64.433 1.00 62.31 C HETATM 3340 C21 OLC A 402 -13.110 6.269 -67.155 1.00 89.45 C HETATM 3341 C1 OLC A 402 -12.422 4.729 -65.506 1.00 84.25 C HETATM 3342 C22 OLC A 402 -13.544 5.867 -68.547 1.00100.97 C HETATM 3343 O19 OLC A 402 -13.375 4.010 -65.352 1.00112.78 O HETATM 3344 O25 OLC A 402 -15.211 6.128 -70.298 1.00 88.04 O HETATM 3345 O23 OLC A 402 -12.575 6.335 -69.484 1.00 89.60 O HETATM 3346 O20 OLC A 402 -12.134 5.321 -66.664 1.00 88.27 O HETATM 3347 C1 CLR A 403 -13.913 13.272 -67.437 1.00 93.12 C HETATM 3348 C2 CLR A 403 -13.491 13.430 -68.897 1.00 95.17 C HETATM 3349 C3 CLR A 403 -13.673 14.854 -69.364 1.00107.13 C HETATM 3350 C4 CLR A 403 -12.926 15.822 -68.463 1.00100.79 C HETATM 3351 C5 CLR A 403 -13.189 15.618 -66.983 1.00 87.52 C HETATM 3352 C6 CLR A 403 -13.408 16.658 -66.190 1.00 81.76 C HETATM 3353 C7 CLR A 403 -13.611 16.595 -64.708 1.00 88.88 C HETATM 3354 C8 CLR A 403 -13.318 15.221 -64.105 1.00 76.84 C HETATM 3355 C9 CLR A 403 -13.797 14.108 -65.055 1.00 83.61 C HETATM 3356 C10 CLR A 403 -13.130 14.184 -66.462 1.00 89.69 C HETATM 3357 C11 CLR A 403 -13.689 12.719 -64.400 1.00 83.28 C HETATM 3358 C12 CLR A 403 -14.301 12.630 -62.997 1.00 85.92 C HETATM 3359 C13 CLR A 403 -13.768 13.713 -62.051 1.00 75.74 C HETATM 3360 C14 CLR A 403 -14.020 15.061 -62.762 1.00 82.53 C HETATM 3361 C15 CLR A 403 -13.809 16.116 -61.678 1.00 84.90 C HETATM 3362 C16 CLR A 403 -14.321 15.432 -60.395 1.00 87.02 C HETATM 3363 C17 CLR A 403 -14.571 13.934 -60.731 1.00 70.12 C HETATM 3364 C18 CLR A 403 -12.282 13.469 -61.738 1.00 61.55 C HETATM 3365 C19 CLR A 403 -11.648 13.759 -66.425 1.00 93.96 C HETATM 3366 C20 CLR A 403 -14.339 13.029 -59.505 1.00 69.17 C HETATM 3367 C21 CLR A 403 -14.348 11.540 -59.835 1.00 76.43 C HETATM 3368 C22 CLR A 403 -15.389 13.341 -58.428 1.00 69.62 C HETATM 3369 C23 CLR A 403 -15.113 12.792 -57.051 1.00 61.10 C HETATM 3370 C24 CLR A 403 -16.042 13.370 -56.017 1.00 63.62 C HETATM 3371 C25 CLR A 403 -15.799 12.934 -54.582 1.00 65.26 C HETATM 3372 C26 CLR A 403 -16.550 13.829 -53.610 1.00 69.51 C HETATM 3373 C27 CLR A 403 -16.191 11.480 -54.374 1.00 71.82 C HETATM 3374 O1 CLR A 403 -13.182 14.975 -70.707 1.00102.71 O HETATM 3375 P PO4 A 404 10.464 3.071 -74.226 1.00110.86 P HETATM 3376 O1 PO4 A 404 11.383 3.979 -75.045 1.00121.77 O HETATM 3377 O2 PO4 A 404 9.054 3.673 -74.175 1.00 92.66 O HETATM 3378 O3 PO4 A 404 10.411 1.688 -74.870 1.00123.12 O HETATM 3379 O4 PO4 A 404 11.017 2.942 -72.815 1.00 65.77 O HETATM 3380 O1 P6G A 405 4.536 0.575 -28.531 1.00 76.31 O HETATM 3381 C2 P6G A 405 3.831 -0.665 -28.589 1.00 99.94 C HETATM 3382 C3 P6G A 405 2.373 -0.500 -28.943 1.00 93.84 C HETATM 3383 O4 P6G A 405 2.149 -0.900 -30.294 1.00 85.44 O HETATM 3384 C5 P6G A 405 1.250 -0.053 -31.007 1.00 76.90 C HETATM 3385 C6 P6G A 405 1.000 -0.607 -32.388 1.00 84.96 C HETATM 3386 O7 P6G A 405 1.197 0.405 -33.375 1.00 87.65 O HETATM 3387 C8 P6G A 405 0.401 0.232 -34.547 1.00 83.21 C HETATM 3388 C9 P6G A 405 1.252 0.400 -35.774 1.00 89.11 C HETATM 3389 O10 P6G A 405 1.074 1.687 -36.361 1.00 80.10 O HETATM 3390 C11 P6G A 405 1.303 2.771 -35.458 1.00 92.57 C HETATM 3391 C12 P6G A 405 1.936 3.947 -36.164 1.00 66.56 C HETATM 3392 O13 P6G A 405 1.056 4.477 -37.151 1.00 69.59 O HETATM 3393 C14 P6G A 405 1.459 4.205 -38.488 1.00 65.52 C HETATM 3394 C15 P6G A 405 0.963 5.277 -39.389 1.00 67.20 C HETATM 3395 O16 P6G A 405 0.474 4.700 -40.593 1.00 66.39 O HETATM 3396 C17 P6G A 405 0.860 5.400 -41.770 1.00 60.99 C HETATM 3397 C18 P6G A 405 1.835 4.567 -42.537 1.00 70.78 C HETATM 3398 O19 P6G A 405 1.299 4.140 -43.772 1.00 89.66 O HETATM 3399 O1 PG4 A 406 3.933 36.753 -35.132 1.00 88.28 O HETATM 3400 C1 PG4 A 406 2.826 35.904 -35.382 1.00 86.65 C HETATM 3401 C2 PG4 A 406 3.129 34.880 -36.432 1.00 72.45 C HETATM 3402 O2 PG4 A 406 1.925 34.236 -36.834 1.00 81.29 O HETATM 3403 C3 PG4 A 406 2.096 33.393 -37.968 1.00 75.85 C HETATM 3404 C4 PG4 A 406 1.354 33.948 -39.137 1.00 77.61 C HETATM 3405 O3 PG4 A 406 2.215 33.954 -40.271 1.00 97.90 O HETATM 3406 C5 PG4 A 406 1.510 34.117 -41.497 1.00107.74 C HETATM 3407 C6 PG4 A 406 2.462 34.164 -42.654 1.00104.67 C HETATM 3408 O4 PG4 A 406 1.725 34.374 -43.856 1.00 89.38 O HETATM 3409 C7 PG4 A 406 2.544 34.380 -45.021 1.00 87.33 C HETATM 3410 C8 PG4 A 406 1.692 34.248 -46.247 1.00 77.62 C HETATM 3411 O5 PG4 A 406 0.329 34.087 -45.868 1.00 86.30 O HETATM 3412 CAP VF1 A 407 2.347 15.505 -57.853 1.00 35.62 C ANISOU 3412 CAP VF1 A 407 5849 1944 5740 -483 217 31 C HETATM 3413 CAO VF1 A 407 1.978 15.627 -56.389 1.00 35.56 C ANISOU 3413 CAO VF1 A 407 5742 1928 5840 -430 154 10 C HETATM 3414 NBB VF1 A 407 1.134 16.818 -56.160 1.00 38.35 N ANISOU 3414 NBB VF1 A 407 6161 2221 6191 -399 48 41 N HETATM 3415 CAB VF1 A 407 0.889 16.973 -54.733 1.00 37.63 C ANISOU 3415 CAB VF1 A 407 5984 2124 6190 -350 8 13 C HETATM 3416 CAZ VF1 A 407 -0.126 16.735 -56.923 1.00 36.18 C ANISOU 3416 CAZ VF1 A 407 5952 1947 5848 -351 -34 49 C HETATM 3417 CAQ VF1 A 407 -1.015 15.520 -56.647 1.00 35.75 C ANISOU 3417 CAQ VF1 A 407 5815 1953 5816 -301 -64 -5 C HETATM 3418 CAW VF1 A 407 -0.740 14.319 -57.522 1.00 34.78 C ANISOU 3418 CAW VF1 A 407 5710 1871 5634 -343 -1 -38 C HETATM 3419 CAM VF1 A 407 -1.479 13.152 -57.340 1.00 35.11 C ANISOU 3419 CAM VF1 A 407 5695 1951 5693 -321 -25 -88 C HETATM 3420 CAL VF1 A 407 -1.250 12.014 -58.111 1.00 36.83 C ANISOU 3420 CAL VF1 A 407 5951 2186 5856 -358 33 -131 C HETATM 3421 CAU VF1 A 407 -0.233 12.026 -59.039 1.00 37.81 C ANISOU 3421 CAU VF1 A 407 6157 2302 5906 -404 130 -126 C HETATM 3422 OAD VF1 A 407 0.108 10.990 -59.824 1.00 35.37 O ANISOU 3422 OAD VF1 A 407 5903 2002 5534 -431 207 -175 O HETATM 3423 CAN VF1 A 407 0.527 13.179 -59.211 1.00 35.21 C ANISOU 3423 CAN VF1 A 407 5864 1952 5561 -430 162 -68 C HETATM 3424 CAX VF1 A 407 0.264 14.338 -58.495 1.00 35.54 C ANISOU 3424 CAX VF1 A 407 5883 1963 5656 -407 90 -22 C HETATM 3425 CBF VF1 A 407 1.105 15.607 -58.756 1.00 36.49 C ANISOU 3425 CBF VF1 A 407 6069 2041 5755 -457 124 43 C HETATM 3426 CBA VF1 A 407 1.531 15.811 -60.223 1.00 38.61 C ANISOU 3426 CBA VF1 A 407 6470 2309 5890 -523 178 80 C HETATM 3427 NAS VF1 A 407 2.821 16.556 -60.232 1.00 42.03 N ANISOU 3427 NAS VF1 A 407 6907 2725 6335 -598 275 126 N HETATM 3428 CBE VF1 A 407 0.671 16.837 -60.980 1.00 38.53 C ANISOU 3428 CBE VF1 A 407 6598 2254 5789 -519 68 147 C HETATM 3429 OAT VF1 A 407 0.816 16.776 -62.382 1.00 39.22 O ANISOU 3429 OAT VF1 A 407 6819 2356 5726 -573 101 174 O HETATM 3430 CAA VF1 A 407 0.617 15.479 -63.035 1.00 38.62 C ANISOU 3430 CAA VF1 A 407 6755 2341 5577 -577 135 105 C HETATM 3431 CAF VF1 A 407 -0.772 16.738 -60.576 1.00 37.73 C ANISOU 3431 CAF VF1 A 407 6461 2157 5717 -432 -74 130 C HETATM 3432 CAE VF1 A 407 -1.012 16.750 -59.282 1.00 35.69 C ANISOU 3432 CAE VF1 A 407 6086 1893 5582 -377 -99 101 C HETATM 3433 CBD VF1 A 407 0.195 16.837 -58.421 1.00 36.26 C ANISOU 3433 CBD VF1 A 407 6085 1953 5739 -413 -1 88 C HETATM 3434 CAR VF1 A 407 0.913 18.113 -58.850 1.00 38.68 C ANISOU 3434 CAR VF1 A 407 6497 2193 6008 -476 21 159 C HETATM 3435 CBC VF1 A 407 1.239 18.158 -60.345 1.00 40.65 C ANISOU 3435 CBC VF1 A 407 6874 2449 6120 -543 68 204 C HETATM 3436 CAC VF1 A 407 0.698 19.427 -61.040 1.00 38.92 C ANISOU 3436 CAC VF1 A 407 6812 2151 5823 -542 -21 292 C HETATM 3437 CAY VF1 A 407 2.706 17.902 -60.785 1.00 42.83 C ANISOU 3437 CAY VF1 A 407 7141 2760 6372 -640 226 209 C HETATM 3438 CAV VF1 A 407 3.782 18.863 -60.319 1.00 41.71 C ANISOU 3438 CAV VF1 A 407 6982 2578 6288 -719 282 256 C HETATM 3439 CAJ VF1 A 407 4.105 19.911 -61.159 1.00 44.32 C ANISOU 3439 CAJ VF1 A 407 7454 2853 6534 -801 296 341 C HETATM 3440 CAH VF1 A 407 4.872 20.986 -60.704 1.00 44.46 C ANISOU 3440 CAH VF1 A 407 7482 2807 6605 -886 314 391 C HETATM 3441 CAG VF1 A 407 5.345 20.991 -59.414 1.00 43.94 C ANISOU 3441 CAG VF1 A 407 7280 2746 6669 -890 313 348 C HETATM 3442 CAI VF1 A 407 5.091 19.905 -58.584 1.00 44.04 C ANISOU 3442 CAI VF1 A 407 7147 2829 6757 -802 304 266 C HETATM 3443 CAK VF1 A 407 4.327 18.841 -59.044 1.00 41.52 C ANISOU 3443 CAK VF1 A 407 6822 2562 6392 -719 294 223 C HETATM 3444 O HOH A 501 -30.109 10.401 -25.957 1.00 78.88 O HETATM 3445 O HOH A 502 0.424 8.892 -29.758 1.00 54.10 O HETATM 3446 O HOH A 503 -2.946 24.359 -68.172 1.00 63.89 O HETATM 3447 O HOH A 504 -9.800 -3.300 -32.383 1.00 59.40 O HETATM 3448 O HOH A 505 13.222 26.128 -66.916 1.00 49.19 O HETATM 3449 O HOH A 506 18.502 16.742 -65.338 1.00 66.91 O HETATM 3450 O HOH A 507 -10.808 2.562 -24.160 1.00 37.64 O HETATM 3451 O HOH A 508 -7.733 16.023 -44.397 1.00 47.61 O HETATM 3452 O HOH A 509 5.535 23.160 -68.218 1.00 66.97 O HETATM 3453 O HOH A 510 17.002 25.560 -61.363 1.00 53.83 O HETATM 3454 O HOH A 511 -8.759 14.344 -42.748 1.00 40.67 O HETATM 3455 O HOH A 512 -9.687 -4.137 -29.482 1.00 65.74 O HETATM 3456 O HOH A 513 8.207 17.150 -37.506 1.00 57.46 O HETATM 3457 O HOH A 514 -14.294 -1.613 -32.033 1.00 48.07 O HETATM 3458 O HOH A 515 2.375 8.076 -30.700 1.00 57.22 O HETATM 3459 O HOH A 516 0.715 7.041 -67.815 1.00 53.42 O HETATM 3460 O HOH A 517 8.143 5.562 -25.640 1.00 45.81 O HETATM 3461 O HOH A 518 -8.566 16.838 -55.966 1.00 39.41 O HETATM 3462 O HOH A 519 4.264 11.151 -39.398 1.00 42.12 O HETATM 3463 O HOH A 520 -2.191 18.606 -49.655 1.00 47.43 O HETATM 3464 O HOH A 521 -11.958 -0.145 -24.563 1.00 59.76 O HETATM 3465 O HOH A 522 -1.780 21.041 -41.136 1.00 45.71 O HETATM 3466 O HOH A 523 0.868 24.734 -63.294 1.00 44.83 O HETATM 3467 O HOH A 524 3.564 20.316 -25.697 1.00 55.07 O HETATM 3468 O HOH A 525 -7.070 11.371 -39.314 1.00 36.66 O HETATM 3469 O HOH A 526 -2.105 10.661 -65.996 1.00 39.28 O HETATM 3470 O HOH A 527 2.886 10.471 -60.063 1.00 41.58 O HETATM 3471 O HOH A 528 2.753 18.412 -51.937 1.00 46.51 O HETATM 3472 O HOH A 529 -0.209 22.883 -61.588 1.00 43.23 O HETATM 3473 O HOH A 530 -1.341 8.767 -59.311 1.00 32.58 O HETATM 3474 O HOH A 531 -2.851 16.507 -47.515 1.00 41.65 O HETATM 3475 O HOH A 532 -4.478 7.177 -24.313 1.00 40.90 O HETATM 3476 O HOH A 533 6.895 1.389 -27.450 1.00 74.20 O HETATM 3477 O HOH A 534 16.147 12.619 -65.197 1.00 58.92 O HETATM 3478 O HOH A 535 -1.070 17.701 -26.184 1.00 47.38 O HETATM 3479 O HOH A 536 7.150 12.261 -41.307 1.00 41.28 O HETATM 3480 O HOH A 537 5.213 4.507 -21.658 1.00 55.41 O HETATM 3481 O HOH A 538 9.813 4.602 -27.473 1.00 53.10 O HETATM 3482 O HOH A 539 -3.741 8.931 -58.787 1.00 38.96 O HETATM 3483 O HOH A 540 8.579 -0.486 -75.513 1.00 67.50 O HETATM 3484 O HOH A 541 12.358 9.314 -30.379 1.00 51.69 O HETATM 3485 O HOH A 542 -4.569 26.861 -43.592 1.00 50.11 O HETATM 3486 O HOH A 543 -3.211 18.152 -56.017 1.00 39.33 O HETATM 3487 O HOH A 544 0.177 23.769 -65.429 1.00 60.36 O HETATM 3488 O HOH A 545 0.897 11.884 -62.499 1.00 52.51 O HETATM 3489 O HOH A 546 6.884 3.774 -24.377 1.00 62.07 O HETATM 3490 O HOH A 547 2.272 12.349 -25.066 1.00 42.14 O HETATM 3491 O HOH A 548 -0.536 14.889 -66.480 1.00 67.24 O HETATM 3492 O HOH A 549 -0.120 13.618 -26.294 1.00 44.44 O HETATM 3493 O HOH A 550 -0.525 21.481 -63.951 1.00 49.37 O HETATM 3494 O HOH A 551 -1.790 11.541 -26.626 1.00 54.51 O HETATM 3495 O HOH A 552 3.219 10.731 -62.715 1.00 58.55 O HETATM 3496 O HOH A 553 -0.735 12.763 -64.734 1.00 54.95 O HETATM 3497 O HOH A 554 0.130 17.647 -51.224 1.00 45.92 O HETATM 3498 O HOH B 201 -8.748 15.844 -19.439 1.00 52.66 O HETATM 3499 O HOH B 202 3.150 12.538 -22.570 1.00 51.03 O HETATM 3500 O HOH B 203 3.083 -0.215 -10.756 1.00 60.01 O HETATM 3501 O HOH B 204 -7.909 15.968 -21.768 1.00 48.10 O HETATM 3502 O HOH B 205 -9.061 4.986 -2.673 1.00 52.15 O HETATM 3503 O HOH B 206 -6.886 6.183 -23.783 1.00 35.26 O HETATM 3504 O HOH B 207 -0.446 10.423 -24.556 1.00 44.90 O HETATM 3505 O HOH B 208 -14.792 13.973 -21.159 1.00 52.55 O HETATM 3506 O HOH B 209 11.594 4.257 -16.868 1.00 53.96 O HETATM 3507 O HOH B 210 -9.412 -2.832 -14.170 1.00 61.60 O HETATM 3508 O HOH B 211 -1.548 15.649 -24.943 1.00 48.50 O HETATM 3509 O HOH B 212 -1.606 21.887 -10.310 1.00 59.70 O HETATM 3510 O HOH B 213 3.770 21.444 -14.582 1.00 59.10 O HETATM 3511 O HOH B 214 8.692 9.843 -24.219 1.00 47.59 O CONECT 7 18 CONECT 11 12 13 21 CONECT 12 11 15 CONECT 13 11 14 CONECT 14 13 15 CONECT 15 12 14 16 CONECT 16 15 17 CONECT 17 16 18 19 CONECT 18 7 17 CONECT 19 17 20 22 CONECT 20 19 CONECT 21 11 3427 CONECT 22 19 CONECT 30 36 CONECT 36 30 37 CONECT 37 36 38 44 CONECT 38 37 39 CONECT 39 38 40 CONECT 40 39 41 CONECT 41 40 42 43 CONECT 42 41 CONECT 43 41 CONECT 44 37 45 46 CONECT 45 44 CONECT 46 44 CONECT 681 1291 CONECT 1291 681 CONECT 2544 3135 CONECT 3135 2544 CONECT 3313 3314 CONECT 3314 3313 3316 CONECT 3315 3324 3326 CONECT 3316 3314 3317 CONECT 3317 3316 3318 CONECT 3318 3317 3319 CONECT 3319 3318 3320 CONECT 3320 3319 3321 CONECT 3321 3320 3323 CONECT 3322 3324 3328 CONECT 3323 3321 3325 3328 CONECT 3324 3315 3322 3327 CONECT 3325 3323 CONECT 3326 3315 CONECT 3327 3324 CONECT 3328 3322 3323 CONECT 3329 3330 3331 CONECT 3330 3329 3332 CONECT 3331 3329 CONECT 3332 3330 3334 CONECT 3333 3342 3344 CONECT 3334 3332 3335 CONECT 3335 3334 3336 CONECT 3336 3335 3337 CONECT 3337 3336 3338 CONECT 3338 3337 3339 CONECT 3339 3338 3341 CONECT 3340 3342 3346 CONECT 3341 3339 3343 3346 CONECT 3342 3333 3340 3345 CONECT 3343 3341 CONECT 3344 3333 CONECT 3345 3342 CONECT 3346 3340 3341 CONECT 3347 3348 3356 CONECT 3348 3347 3349 CONECT 3349 3348 3350 3374 CONECT 3350 3349 3351 CONECT 3351 3350 3352 3356 CONECT 3352 3351 3353 CONECT 3353 3352 3354 CONECT 3354 3353 3355 3360 CONECT 3355 3354 3356 3357 CONECT 3356 3347 3351 3355 3365 CONECT 3357 3355 3358 CONECT 3358 3357 3359 CONECT 3359 3358 3360 3363 3364 CONECT 3360 3354 3359 3361 CONECT 3361 3360 3362 CONECT 3362 3361 3363 CONECT 3363 3359 3362 3366 CONECT 3364 3359 CONECT 3365 3356 CONECT 3366 3363 3367 3368 CONECT 3367 3366 CONECT 3368 3366 3369 CONECT 3369 3368 3370 CONECT 3370 3369 3371 CONECT 3371 3370 3372 3373 CONECT 3372 3371 CONECT 3373 3371 CONECT 3374 3349 CONECT 3375 3376 3377 3378 3379 CONECT 3376 3375 CONECT 3377 3375 CONECT 3378 3375 CONECT 3379 3375 CONECT 3380 3381 CONECT 3381 3380 3382 CONECT 3382 3381 3383 CONECT 3383 3382 3384 CONECT 3384 3383 3385 CONECT 3385 3384 3386 CONECT 3386 3385 3387 CONECT 3387 3386 3388 CONECT 3388 3387 3389 CONECT 3389 3388 3390 CONECT 3390 3389 3391 CONECT 3391 3390 3392 CONECT 3392 3391 3393 CONECT 3393 3392 3394 CONECT 3394 3393 3395 CONECT 3395 3394 3396 CONECT 3396 3395 3397 CONECT 3397 3396 3398 CONECT 3398 3397 CONECT 3399 3400 CONECT 3400 3399 3401 CONECT 3401 3400 3402 CONECT 3402 3401 3403 CONECT 3403 3402 3404 CONECT 3404 3403 3405 CONECT 3405 3404 3406 CONECT 3406 3405 3407 CONECT 3407 3406 3408 CONECT 3408 3407 3409 CONECT 3409 3408 3410 CONECT 3410 3409 3411 CONECT 3411 3410 CONECT 3412 3413 3425 CONECT 3413 3412 3414 CONECT 3414 3413 3415 3416 CONECT 3415 3414 CONECT 3416 3414 3417 3433 CONECT 3417 3416 3418 CONECT 3418 3417 3419 3424 CONECT 3419 3418 3420 CONECT 3420 3419 3421 CONECT 3421 3420 3422 3423 CONECT 3422 3421 CONECT 3423 3421 3424 CONECT 3424 3418 3423 3425 CONECT 3425 3412 3424 3426 3433 CONECT 3426 3425 3427 3428 CONECT 3427 21 3426 3437 CONECT 3428 3426 3429 3431 3435 CONECT 3429 3428 3430 CONECT 3430 3429 CONECT 3431 3428 3432 CONECT 3432 3431 3433 CONECT 3433 3416 3425 3432 3434 CONECT 3434 3433 3435 CONECT 3435 3428 3434 3436 3437 CONECT 3436 3435 CONECT 3437 3427 3435 3438 CONECT 3438 3437 3439 3443 CONECT 3439 3438 3440 CONECT 3440 3439 3441 CONECT 3441 3440 3442 CONECT 3442 3441 3443 CONECT 3443 3438 3442 MASTER 341 0 9 12 16 0 0 6 3475 2 160 33 END