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*** ENDOCYTOSIS 29-OCT-19 6L6O ***elNémo ID: 23041815440915724Job options:ID = 23041815440915724 JOBID = ENDOCYTOSIS 29-OCT-19 6L6O USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER ENDOCYTOSIS 29-OCT-19 6L6O TITLE CRYSTAL STRUCTURE OF STABILIZED RAB5A GTPASE DOMAIN FROM LEISHMANIA TITLE 2 DONOVANI COMPND MOL_ID: 1; COMPND 2 MOLECULE: RAB5A; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES; COMPND 6 OTHER_DETAILS: RESIDUE 60-79 DELETION SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LEISHMANIA DONOVANI; SOURCE 3 ORGANISM_TAXID: 5661; SOURCE 4 GENE: RAB5A; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX4T1 KEYWDS INTRACELLULAR TRAFFICKING, GTPASE, ENDOCYTOSIS EXPDTA X-RAY DIFFRACTION AUTHOR A.ARORA,M.ZOHIB,B.K.BISWAL,D.MAHESHWARI,R.K.PAL REVDAT 1 11-NOV-20 6L6O 0 JRNL AUTH M.ZOHIB,D.MAHESHWARI,R.K.PAL,S.FREITAG-POHL,B.K.BISWAL, JRNL AUTH 2 E.POHL,A.ARORA JRNL TITL CRYSTAL STRUCTURE OF THE GDP-BOUND GTPASE DOMAIN OF RAB5A JRNL TITL 2 FROM LEISHMANIA DONOVANI. JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 76 544 2020 JRNL REFN ESSN 2053-230X JRNL PMID 33135673 JRNL DOI 10.1107/S2053230X20013722 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0257 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.42 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8 REMARK 3 NUMBER OF REFLECTIONS : 18075 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.167 REMARK 3 R VALUE (WORKING SET) : 0.165 REMARK 3 FREE R VALUE : 0.203 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 938 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1134 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.66 REMARK 3 BIN R VALUE (WORKING SET) : 0.3740 REMARK 3 BIN FREE R VALUE SET COUNT : 55 REMARK 3 BIN FREE R VALUE : 0.3690 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1266 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 39 REMARK 3 SOLVENT ATOMS : 124 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.10 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.71000 REMARK 3 B22 (A**2) : 0.71000 REMARK 3 B33 (A**2) : -2.29000 REMARK 3 B12 (A**2) : 0.35000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.104 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.106 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.079 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.151 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.960 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1344 ; 0.017 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 1271 ; 0.001 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1827 ; 2.146 ; 1.665 REMARK 3 BOND ANGLES OTHERS (DEGREES): 2940 ; 1.537 ; 1.587 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 173 ; 7.658 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 65 ;33.024 ;22.308 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 233 ;13.271 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;21.764 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 181 ; 0.094 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1506 ; 0.012 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 285 ; 0.002 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 11 A 175 REMARK 3 RESIDUE RANGE : A 201 A 203 REMARK 3 ORIGIN FOR THE GROUP (A): -23.061 20.903 -13.316 REMARK 3 T TENSOR REMARK 3 T11: 0.0227 T22: 0.1200 REMARK 3 T33: 0.0320 T12: 0.0131 REMARK 3 T13: 0.0120 T23: -0.0061 REMARK 3 L TENSOR REMARK 3 L11: 0.4433 L22: 0.4654 REMARK 3 L33: 1.0121 L12: 0.0042 REMARK 3 L13: -0.5223 L23: 0.2046 REMARK 3 S TENSOR REMARK 3 S11: -0.0259 S12: -0.1163 S13: 0.0649 REMARK 3 S21: -0.0290 S22: 0.0093 S23: 0.0454 REMARK 3 S31: 0.0942 S32: 0.1440 S33: 0.0166 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS U VALUES : WITH TLS ADDED REMARK 4 REMARK 4 6L6O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-NOV-19. REMARK 100 THE DEPOSITION ID IS D_1300013547. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-MAY-19 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E+ SUPERBRIGHT REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++ REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19056 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 35.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9 REMARK 200 DATA REDUNDANCY : 15.10 REMARK 200 R MERGE (I) : 0.05700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 16.0000 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) : 1.86 REMARK 200 COMPLETENESS FOR SHELL (%) : 89.7 REMARK 200 DATA REDUNDANCY IN SHELL : 8.80 REMARK 200 R MERGE FOR SHELL (I) : 0.74800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 2HEI REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 55.80 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 200MM AMMONIUM ACETATE, 100MM TRIS REMARK 280 HCL, PH 8.5 15% PEG 3350, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+2/3 REMARK 290 6555 -X,-X+Y,-Z+1/3 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 34.47267 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 68.94533 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 68.94533 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 34.47267 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 900 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 7880 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A -1 REMARK 465 SER A 0 REMARK 465 MET A 1 REMARK 465 ASN A 2 REMARK 465 THR A 3 REMARK 465 HIS A 4 REMARK 465 PRO A 5 REMARK 465 PRO A 6 REMARK 465 GLN A 7 REMARK 465 LEU A 8 REMARK 465 MET A 9 REMARK 465 GLU A 10 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ASN A 41 OD1 ND2 REMARK 470 ILE A 57 CD1 REMARK 470 LYS A 174 CD CE NZ 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 GLU A 110 CD GLU A 110 OE2 0.084 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 ASN A 41 49.12 38.03 REMARK 500 ILE A 57 -165.32 -100.66 REMARK 500 ALA A 173 -58.09 -26.09 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 424 DISTANCE = 5.86 ANGSTROMS REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG A 204 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 SER A 27 OG REMARK 620 2 GDP A 201 O2B 89.6 REMARK 620 N 1 DBREF1 6L6O A 1 175 UNP A0A109NYM0_LEIDO DBREF2 6L6O A A0A109NYM0 1 195 SEQADV 6L6O GLY A -1 UNP A0A109NYM EXPRESSION TAG SEQADV 6L6O SER A 0 UNP A0A109NYM EXPRESSION TAG SEQADV 6L6O ASP A 58 UNP A0A109NYM PRO 58 ENGINEERED MUTATION SEQADV 6L6O GLY A 59 UNP A0A109NYM PRO 59 ENGINEERED MUTATION SEQADV 6L6O A UNP A0A109NYM PRO 60 DELETION SEQADV 6L6O A UNP A0A109NYM ARG 61 DELETION SEQADV 6L6O A UNP A0A109NYM GLY 62 DELETION SEQADV 6L6O A UNP A0A109NYM ALA 63 DELETION SEQADV 6L6O A UNP A0A109NYM ALA 64 DELETION SEQADV 6L6O A UNP A0A109NYM ALA 65 DELETION SEQADV 6L6O A UNP A0A109NYM ALA 66 DELETION SEQADV 6L6O A UNP A0A109NYM PRO 67 DELETION SEQADV 6L6O A UNP A0A109NYM GLY 68 DELETION SEQADV 6L6O A UNP A0A109NYM GLY 69 DELETION SEQADV 6L6O A UNP A0A109NYM ALA 70 DELETION SEQADV 6L6O A UNP A0A109NYM THR 71 DELETION SEQADV 6L6O A UNP A0A109NYM SER 72 DELETION SEQADV 6L6O A UNP A0A109NYM ALA 73 DELETION SEQADV 6L6O A UNP A0A109NYM HIS 74 DELETION SEQADV 6L6O A UNP A0A109NYM ALA 75 DELETION SEQADV 6L6O A UNP A0A109NYM LEU 76 DELETION SEQADV 6L6O A UNP A0A109NYM GLN 77 DELETION SEQADV 6L6O A UNP A0A109NYM GLN 78 DELETION SEQADV 6L6O A UNP A0A109NYM MET 79 DELETION SEQADV 6L6O LEU A 72 UNP A0A109NYM GLN 92 ENGINEERED MUTATION SEQADV 6L6O SER A 87 UNP A0A109NYM CYS 107 ENGINEERED MUTATION SEQRES 1 A 177 GLY SER MET ASN THR HIS PRO PRO GLN LEU MET GLU ALA SEQRES 2 A 177 THR SER ALA LYS ILE VAL MET LEU GLY GLU SER GLY ALA SEQRES 3 A 177 GLY LYS SER SER ILE ALA LEU ARG PHE THR ARG ASN GLU SEQRES 4 A 177 PHE LEU ALA ASN GLN GLU THR THR ILE GLY ALA ALA PHE SEQRES 5 A 177 LEU SER LYS THR VAL MET ILE ASP GLY ARG ALA LEU LYS SEQRES 6 A 177 TYR GLU ILE TRP ASP THR ALA GLY LEU GLU ARG PHE ARG SEQRES 7 A 177 SER LEU ALA PRO ILE TYR TYR ARG GLY ALA SER GLY ALA SEQRES 8 A 177 LEU VAL VAL TYR ASP ILE THR ASN SER GLU SER LEU LYS SEQRES 9 A 177 LYS ALA GLN THR TRP ILE LYS GLU LEU ARG ALA ASN ALA SEQRES 10 A 177 ASP PRO SER LEU ILE ILE VAL LEU VAL GLY ASN LYS LYS SEQRES 11 A 177 ASP LEU GLY SER LEU ARG GLN VAL SER PHE GLU ASP GLY SEQRES 12 A 177 GLN ARG LEU ALA ALA GLU GLU GLN LEU ALA ALA PHE TYR SEQRES 13 A 177 GLU ALA SER ALA LYS ASP ASN ASN ASN VAL GLU GLN VAL SEQRES 14 A 177 PHE LEU ASP LEU ALA ALA LYS LEU HET GDP A 201 28 HET GOL A 202 6 HET ACT A 203 4 HET MG A 204 1 HETNAM GDP GUANOSINE-5'-DIPHOSPHATE HETNAM GOL GLYCEROL HETNAM ACT ACETATE ION HETNAM MG MAGNESIUM ION HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 2 GDP C10 H15 N5 O11 P2 FORMUL 3 GOL C3 H8 O3 FORMUL 4 ACT C2 H3 O2 1- FORMUL 5 MG MG 2+ FORMUL 6 HOH *124(H2 O) HELIX 1 AA1 GLY A 25 ASN A 36 1 12 HELIX 2 AA2 GLY A 71 ARG A 76 5 6 HELIX 3 AA3 ALA A 79 ARG A 84 1 6 HELIX 4 AA4 ASN A 97 ALA A 115 1 19 HELIX 5 AA5 LEU A 130 ARG A 134 5 5 HELIX 6 AA6 SER A 137 GLU A 148 1 12 HELIX 7 AA7 ASN A 163 LEU A 175 1 13 SHEET 1 AA1 6 PHE A 50 MET A 56 0 SHEET 2 AA1 6 ALA A 61 TRP A 67 -1 O TYR A 64 N LYS A 53 SHEET 3 AA1 6 THR A 12 GLY A 20 1 N ALA A 14 O GLU A 65 SHEET 4 AA1 6 GLY A 88 ASP A 94 1 O LEU A 90 N LEU A 19 SHEET 5 AA1 6 ILE A 120 ASN A 126 1 O ASN A 126 N TYR A 93 SHEET 6 AA1 6 ALA A 152 GLU A 155 1 O TYR A 154 N GLY A 125 LINK OG SER A 27 MG MG A 204 1555 1555 2.05 LINK O2B GDP A 201 MG MG A 204 1555 1555 2.05 CRYST1 58.018 58.018 103.418 90.00 90.00 120.00 P 31 2 1 6 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.017236 0.009951 0.000000 0.00000 SCALE2 0.000000 0.019902 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009669 0.00000 ATOM 1 N ALA A 11 -15.280 22.585 9.211 1.00 69.20 N ANISOU 1 N ALA A 11 7760 11070 7459 358 89 -448 N ATOM 2 CA ALA A 11 -15.592 22.751 7.745 1.00 61.89 C ANISOU 2 CA ALA A 11 6859 10016 6641 325 102 -435 C ATOM 3 C ALA A 11 -16.487 23.981 7.549 1.00 64.49 C ANISOU 3 C ALA A 11 7190 10244 7068 206 129 -495 C ATOM 4 O ALA A 11 -17.564 23.993 8.160 1.00 64.83 O ANISOU 4 O ALA A 11 7284 10214 7133 186 153 -494 O ATOM 5 CB ALA A 11 -16.289 21.525 7.204 1.00 58.34 C ANISOU 5 CB ALA A 11 6504 9448 6215 401 118 -348 C ATOM 6 N THR A 12 -16.116 24.940 6.682 1.00 59.34 N ANISOU 6 N THR A 12 6493 9576 6476 133 130 -542 N ATOM 7 CA THR A 12 -17.068 25.968 6.188 1.00 51.16 C ANISOU 7 CA THR A 12 5480 8411 5546 40 162 -580 C ATOM 8 C THR A 12 -17.825 25.276 5.051 1.00 45.01 C ANISOU 8 C THR A 12 4772 7492 4837 77 168 -512 C ATOM 9 O THR A 12 -17.237 24.450 4.405 1.00 43.69 O ANISOU 9 O THR A 12 4610 7342 4646 143 150 -464 O ATOM 10 CB THR A 12 -16.385 27.298 5.820 1.00 56.17 C ANISOU 10 CB THR A 12 6049 9083 6209 -53 169 -658 C ATOM 11 OG1 THR A 12 -15.611 27.171 4.639 1.00 55.28 O ANISOU 11 OG1 THR A 12 5916 8974 6113 -36 156 -641 O ATOM 12 CG2 THR A 12 -15.451 27.828 6.892 1.00 60.47 C ANISOU 12 CG2 THR A 12 6515 9790 6669 -87 159 -728 C ATOM 13 N SER A 13 -19.069 25.647 4.825 1.00 43.55 N ANISOU 13 N SER A 13 4633 7178 4734 35 194 -513 N ATOM 14 CA SER A 13 -19.964 24.993 3.830 1.00 41.21 C ANISOU 14 CA SER A 13 4403 6750 4502 63 200 -454 C ATOM 15 C SER A 13 -20.205 25.947 2.663 1.00 40.20 C ANISOU 15 C SER A 13 4270 6537 4465 2 209 -477 C ATOM 16 O SER A 13 -20.396 27.138 2.927 1.00 39.97 O ANISOU 16 O SER A 13 4216 6499 4471 -70 227 -535 O ATOM 17 CB SER A 13 -21.248 24.618 4.456 1.00 43.77 C ANISOU 17 CB SER A 13 4782 7000 4847 67 223 -437 C ATOM 18 OG SER A 13 -21.083 23.487 5.289 1.00 42.59 O ANISOU 18 OG SER A 13 4659 6905 4615 139 220 -396 O ATOM 19 N ALA A 14 -20.315 25.410 1.448 1.00 35.96 N ANISOU 19 N ALA A 14 3767 5932 3965 32 200 -430 N ATOM 20 CA ALA A 14 -20.743 26.135 0.224 1.00 32.76 C ANISOU 20 CA ALA A 14 3372 5428 3644 -11 207 -435 C ATOM 21 C ALA A 14 -21.822 25.275 -0.466 1.00 32.66 C ANISOU 21 C ALA A 14 3423 5309 3674 22 207 -379 C ATOM 22 O ALA A 14 -21.579 24.065 -0.745 1.00 31.64 O ANISOU 22 O ALA A 14 3325 5188 3508 85 196 -328 O ATOM 23 CB ALA A 14 -19.572 26.390 -0.693 1.00 33.79 C ANISOU 23 CB ALA A 14 3471 5600 3766 -15 194 -442 C ATOM 24 N LYS A 15 -22.981 25.888 -0.696 1.00 30.67 N ANISOU 24 N LYS A 15 3190 4965 3496 -17 222 -390 N ATOM 25 CA LYS A 15 -24.042 25.343 -1.537 1.00 28.09 C ANISOU 25 CA LYS A 15 2911 4539 3221 -2 220 -350 C ATOM 26 C LYS A 15 -23.643 25.512 -3.020 1.00 28.25 C ANISOU 26 C LYS A 15 2938 4523 3273 -3 205 -332 C ATOM 27 O LYS A 15 -23.362 26.640 -3.509 1.00 28.54 O ANISOU 27 O LYS A 15 2952 4548 3344 -44 209 -362 O ATOM 28 CB LYS A 15 -25.341 26.087 -1.274 1.00 27.24 C ANISOU 28 CB LYS A 15 2807 4360 3179 -44 240 -374 C ATOM 29 CG LYS A 15 -26.470 25.663 -2.198 1.00 26.05 C ANISOU 29 CG LYS A 15 2694 4118 3086 -35 235 -341 C ATOM 30 CD LYS A 15 -27.763 26.266 -1.864 1.00 26.52 C ANISOU 30 CD LYS A 15 2751 4120 3205 -65 254 -363 C ATOM 31 CE LYS A 15 -28.806 26.033 -2.964 1.00 26.34 C ANISOU 31 CE LYS A 15 2749 4017 3239 -60 243 -336 C ATOM 32 NZ LYS A 15 -30.123 26.488 -2.552 1.00 26.62 N ANISOU 32 NZ LYS A 15 2776 4007 3329 -81 261 -355 N ATOM 33 N ILE A 16 -23.646 24.398 -3.701 1.00 28.12 N ANISOU 33 N ILE A 16 2957 4484 3240 41 193 -284 N ATOM 34 CA ILE A 16 -23.321 24.344 -5.142 1.00 28.75 C ANISOU 34 CA ILE A 16 3053 4527 3343 46 179 -260 C ATOM 35 C ILE A 16 -24.523 23.655 -5.801 1.00 27.77 C ANISOU 35 C ILE A 16 2976 4317 3257 56 176 -227 C ATOM 36 O ILE A 16 -24.866 22.520 -5.427 1.00 29.11 O ANISOU 36 O ILE A 16 3179 4483 3398 88 183 -200 O ATOM 37 CB ILE A 16 -22.029 23.548 -5.390 1.00 28.78 C ANISOU 37 CB ILE A 16 3054 4597 3284 93 169 -236 C ATOM 38 CG1 ILE A 16 -20.808 24.009 -4.573 1.00 32.22 C ANISOU 38 CG1 ILE A 16 3432 5141 3666 90 169 -271 C ATOM 39 CG2 ILE A 16 -21.753 23.438 -6.909 1.00 28.69 C ANISOU 39 CG2 ILE A 16 3065 4541 3295 97 158 -211 C ATOM 40 CD1 ILE A 16 -20.340 25.377 -4.931 1.00 34.80 C ANISOU 40 CD1 ILE A 16 3719 5477 4025 31 174 -317 C ATOM 41 N VAL A 17 -25.075 24.242 -6.854 1.00 26.45 N ANISOU 41 N VAL A 17 2817 4087 3147 31 168 -225 N ATOM 42 CA VAL A 17 -26.274 23.674 -7.541 1.00 25.00 C ANISOU 42 CA VAL A 17 2668 3830 2999 34 161 -201 C ATOM 43 C VAL A 17 -25.880 23.095 -8.895 1.00 25.30 C ANISOU 43 C VAL A 17 2737 3845 3029 52 145 -167 C ATOM 44 O VAL A 17 -25.057 23.715 -9.602 1.00 25.52 O ANISOU 44 O VAL A 17 2754 3884 3058 46 137 -170 O ATOM 45 CB VAL A 17 -27.421 24.665 -7.675 1.00 25.84 C ANISOU 45 CB VAL A 17 2760 3885 3172 0 161 -221 C ATOM 46 CG1 VAL A 17 -27.926 25.073 -6.257 1.00 25.51 C ANISOU 46 CG1 VAL A 17 2693 3860 3136 -16 184 -254 C ATOM 47 CG2 VAL A 17 -27.102 25.890 -8.486 1.00 24.83 C ANISOU 47 CG2 VAL A 17 2618 3737 3079 -19 155 -233 C ATOM 48 N MET A 18 -26.477 21.955 -9.209 1.00 23.43 N ANISOU 48 N MET A 18 2541 3577 2784 69 146 -140 N ATOM 49 CA MET A 18 -26.362 21.362 -10.534 1.00 24.74 C ANISOU 49 CA MET A 18 2742 3710 2947 79 134 -112 C ATOM 50 C MET A 18 -27.495 21.900 -11.430 1.00 26.46 C ANISOU 50 C MET A 18 2960 3871 3221 50 115 -116 C ATOM 51 O MET A 18 -28.702 21.807 -11.067 1.00 25.29 O ANISOU 51 O MET A 18 2808 3698 3102 34 118 -126 O ATOM 52 CB MET A 18 -26.459 19.833 -10.424 1.00 25.47 C ANISOU 52 CB MET A 18 2884 3794 2999 107 151 -85 C ATOM 53 CG MET A 18 -25.437 19.153 -9.542 1.00 25.81 C ANISOU 53 CG MET A 18 2934 3892 2980 151 170 -72 C ATOM 54 SD MET A 18 -23.752 19.588 -9.858 1.00 27.70 S ANISOU 54 SD MET A 18 3143 4195 3184 177 160 -70 S ATOM 55 CE MET A 18 -23.557 18.900 -11.500 1.00 28.61 C ANISOU 55 CE MET A 18 3308 4263 3300 186 154 -38 C ATOM 56 N LEU A 19 -27.177 22.252 -12.683 1.00 26.33 N ANISOU 56 N LEU A 19 2954 3835 3214 47 97 -103 N ATOM 57 CA LEU A 19 -28.169 22.789 -13.629 1.00 24.53 C ANISOU 57 CA LEU A 19 2726 3562 3032 29 74 -102 C ATOM 58 C LEU A 19 -27.831 22.265 -15.021 1.00 23.74 C ANISOU 58 C LEU A 19 2664 3443 2913 36 59 -76 C ATOM 59 O LEU A 19 -26.721 21.743 -15.222 1.00 23.73 O ANISOU 59 O LEU A 19 2682 3461 2871 54 69 -62 O ATOM 60 CB LEU A 19 -28.105 24.327 -13.678 1.00 26.91 C ANISOU 60 CB LEU A 19 2997 3857 3371 16 71 -119 C ATOM 61 CG LEU A 19 -28.553 25.043 -12.424 1.00 31.07 C ANISOU 61 CG LEU A 19 3487 4394 3923 3 88 -149 C ATOM 62 CD1 LEU A 19 -28.247 26.507 -12.552 1.00 36.17 C ANISOU 62 CD1 LEU A 19 4115 5028 4597 -9 95 -166 C ATOM 63 CD2 LEU A 19 -30.022 24.833 -12.212 1.00 33.46 C ANISOU 63 CD2 LEU A 19 3781 4672 4260 -2 82 -154 C ATOM 64 N GLY A 20 -28.821 22.383 -15.910 1.00 23.11 N ANISOU 64 N GLY A 20 2591 3329 2860 25 36 -70 N ATOM 65 CA GLY A 20 -28.672 21.853 -17.279 1.00 23.92 C ANISOU 65 CA GLY A 20 2732 3412 2942 26 19 -48 C ATOM 66 C GLY A 20 -29.831 20.950 -17.658 1.00 23.70 C ANISOU 66 C GLY A 20 2720 3367 2917 11 8 -48 C ATOM 67 O GLY A 20 -30.635 20.485 -16.825 1.00 25.37 O ANISOU 67 O GLY A 20 2919 3581 3138 0 21 -64 O ATOM 68 N GLU A 21 -29.945 20.675 -18.931 1.00 24.54 N ANISOU 68 N GLU A 21 2855 3457 3011 6 -11 -34 N ATOM 69 CA GLU A 21 -31.024 19.846 -19.504 1.00 24.83 C ANISOU 69 CA GLU A 21 2905 3483 3044 -17 -24 -40 C ATOM 70 C GLU A 21 -31.011 18.454 -18.940 1.00 24.88 C ANISOU 70 C GLU A 21 2945 3486 3022 -26 11 -46 C ATOM 71 O GLU A 21 -29.921 17.907 -18.643 1.00 24.33 O ANISOU 71 O GLU A 21 2907 3418 2918 -5 40 -31 O ATOM 72 CB GLU A 21 -30.864 19.661 -21.008 1.00 29.78 C ANISOU 72 CB GLU A 21 3567 4098 3648 -21 -47 -24 C ATOM 73 CG GLU A 21 -31.305 20.870 -21.745 1.00 36.62 C ANISOU 73 CG GLU A 21 4408 4964 4540 -14 -86 -17 C ATOM 74 CD GLU A 21 -32.745 21.290 -21.487 1.00 36.56 C ANISOU 74 CD GLU A 21 4351 4968 4571 -22 -111 -35 C ATOM 75 OE1 GLU A 21 -33.597 20.726 -22.187 0.70 34.60 O ANISOU 75 OE1 GLU A 21 4104 4728 4312 -43 -133 -43 O ATOM 76 OE2 GLU A 21 -33.014 22.134 -20.584 1.00 36.39 O ANISOU 76 OE2 GLU A 21 4289 4950 4587 -11 -105 -45 O ATOM 77 N SER A 22 -32.201 17.883 -18.849 1.00 25.40 N ANISOU 77 N SER A 22 3004 3547 3097 -57 12 -66 N ATOM 78 CA SER A 22 -32.397 16.445 -18.555 1.00 26.60 C ANISOU 78 CA SER A 22 3202 3684 3221 -77 52 -74 C ATOM 79 C SER A 22 -31.432 15.620 -19.378 1.00 26.96 C ANISOU 79 C SER A 22 3311 3711 3219 -67 69 -52 C ATOM 80 O SER A 22 -31.363 15.844 -20.631 1.00 27.61 O ANISOU 80 O SER A 22 3404 3791 3295 -74 38 -45 O ATOM 81 CB SER A 22 -33.847 15.994 -18.834 1.00 31.24 C ANISOU 81 CB SER A 22 3776 4270 3823 -126 45 -105 C ATOM 82 OG SER A 22 -34.805 16.706 -18.021 1.00 34.68 O ANISOU 82 OG SER A 22 4149 4724 4304 -134 34 -127 O ATOM 83 N GLY A 23 -30.782 14.636 -18.788 1.00 26.26 N ANISOU 83 N GLY A 23 3270 3609 3097 -49 117 -41 N ATOM 84 CA GLY A 23 -29.923 13.694 -19.518 1.00 27.33 C ANISOU 84 CA GLY A 23 3473 3722 3188 -36 143 -21 C ATOM 85 C GLY A 23 -28.492 14.142 -19.717 1.00 26.94 C ANISOU 85 C GLY A 23 3425 3689 3121 11 138 6 C ATOM 86 O GLY A 23 -27.682 13.350 -20.240 1.00 29.66 O ANISOU 86 O GLY A 23 3823 4018 3427 31 165 25 O ATOM 87 N ALA A 24 -28.149 15.350 -19.334 1.00 27.07 N ANISOU 87 N ALA A 24 3386 3736 3163 28 111 7 N ATOM 88 CA ALA A 24 -26.796 15.888 -19.567 1.00 27.08 C ANISOU 88 CA ALA A 24 3379 3758 3149 63 107 26 C ATOM 89 C ALA A 24 -25.745 15.173 -18.697 1.00 26.46 C ANISOU 89 C ALA A 24 3320 3700 3033 110 147 42 C ATOM 90 O ALA A 24 -24.593 15.078 -19.147 1.00 26.10 O ANISOU 90 O ALA A 24 3288 3667 2961 140 156 59 O ATOM 91 CB ALA A 24 -26.814 17.344 -19.312 1.00 26.26 C ANISOU 91 CB ALA A 24 3216 3679 3083 60 76 15 C ATOM 92 N GLY A 25 -26.135 14.678 -17.508 1.00 25.83 N ANISOU 92 N GLY A 25 3241 3624 2947 118 172 37 N ATOM 93 CA GLY A 25 -25.182 14.075 -16.564 1.00 26.67 C ANISOU 93 CA GLY A 25 3361 3757 3013 172 207 55 C ATOM 94 C GLY A 25 -25.043 14.847 -15.251 1.00 26.74 C ANISOU 94 C GLY A 25 3312 3814 3032 185 199 43 C ATOM 95 O GLY A 25 -24.098 14.599 -14.568 1.00 25.36 O ANISOU 95 O GLY A 25 3134 3679 2821 233 216 57 O ATOM 96 N LYS A 26 -25.999 15.663 -14.856 1.00 24.00 N ANISOU 96 N LYS A 26 2924 3465 2728 147 178 18 N ATOM 97 CA LYS A 26 -25.942 16.424 -13.572 1.00 24.47 C ANISOU 97 CA LYS A 26 2932 3567 2797 153 175 1 C ATOM 98 C LYS A 26 -25.751 15.415 -12.429 1.00 25.54 C ANISOU 98 C LYS A 26 3099 3716 2889 191 214 15 C ATOM 99 O LYS A 26 -24.923 15.672 -11.526 1.00 25.42 O ANISOU 99 O LYS A 26 3055 3756 2845 225 217 17 O ATOM 100 CB LYS A 26 -27.223 17.235 -13.395 1.00 24.09 C ANISOU 100 CB LYS A 26 2848 3500 2804 107 155 -26 C ATOM 101 CG LYS A 26 -27.387 18.373 -14.413 1.00 24.27 C ANISOU 101 CG LYS A 26 2840 3513 2867 81 118 -35 C ATOM 102 CD LYS A 26 -28.659 19.216 -14.215 1.00 23.52 C ANISOU 102 CD LYS A 26 2707 3403 2826 47 100 -60 C ATOM 103 CE LYS A 26 -29.914 18.442 -14.346 1.00 22.88 C ANISOU 103 CE LYS A 26 2644 3291 2756 22 105 -67 C ATOM 104 NZ LYS A 26 -30.034 17.725 -15.625 1.00 22.79 N ANISOU 104 NZ LYS A 26 2674 3254 2730 12 96 -54 N ATOM 105 N SER A 27 -26.690 14.504 -12.342 1.00 26.41 N ANISOU 105 N SER A 27 3255 3779 2997 174 241 16 N ATOM 106 CA SER A 27 -26.743 13.538 -11.213 1.00 28.54 C ANISOU 106 CA SER A 27 3566 4048 3228 205 286 29 C ATOM 107 C SER A 27 -25.432 12.720 -11.196 1.00 29.88 C ANISOU 107 C SER A 27 3775 4240 3336 275 310 66 C ATOM 108 O SER A 27 -24.834 12.504 -10.106 1.00 29.27 O ANISOU 108 O SER A 27 3697 4207 3217 326 327 81 O ATOM 109 CB SER A 27 -27.967 12.700 -11.343 1.00 27.63 C ANISOU 109 CB SER A 27 3500 3872 3126 164 317 19 C ATOM 110 OG SER A 27 -29.155 13.486 -11.166 1.00 26.93 O ANISOU 110 OG SER A 27 3362 3776 3091 108 295 -16 O ATOM 111 N SER A 28 -24.929 12.349 -12.367 1.00 28.56 N ANISOU 111 N SER A 28 3638 4053 3161 284 310 82 N ATOM 112 CA SER A 28 -23.751 11.461 -12.481 1.00 28.17 C ANISOU 112 CA SER A 28 3632 4016 3054 354 339 120 C ATOM 113 C SER A 28 -22.512 12.281 -12.085 1.00 30.13 C ANISOU 113 C SER A 28 3811 4351 3285 396 310 122 C ATOM 114 O SER A 28 -21.607 11.729 -11.457 1.00 31.18 O ANISOU 114 O SER A 28 3954 4526 3364 467 331 148 O ATOM 115 CB SER A 28 -23.649 10.849 -13.883 1.00 28.50 C ANISOU 115 CB SER A 28 3725 4006 3094 343 350 131 C ATOM 116 OG SER A 28 -24.725 9.988 -14.211 1.00 26.93 O ANISOU 116 OG SER A 28 3592 3734 2903 302 384 124 O ATOM 117 N ILE A 29 -22.416 13.550 -12.466 1.00 25.41 N ANISOU 117 N ILE A 29 3146 3781 2726 356 266 94 N ATOM 118 CA ILE A 29 -21.285 14.377 -12.000 1.00 28.05 C ANISOU 118 CA ILE A 29 3412 4201 3045 383 244 86 C ATOM 119 C ILE A 29 -21.317 14.462 -10.448 1.00 31.09 C ANISOU 119 C ILE A 29 3770 4637 3404 406 250 80 C ATOM 120 O ILE A 29 -20.268 14.301 -9.830 1.00 29.23 O ANISOU 120 O ILE A 29 3511 4475 3118 464 254 92 O ATOM 121 CB ILE A 29 -21.283 15.728 -12.705 1.00 26.16 C ANISOU 121 CB ILE A 29 3117 3966 2854 328 207 56 C ATOM 122 CG1 ILE A 29 -20.971 15.494 -14.193 1.00 28.57 C ANISOU 122 CG1 ILE A 29 3454 4233 3165 322 205 70 C ATOM 123 CG2 ILE A 29 -20.348 16.740 -12.063 1.00 29.22 C ANISOU 123 CG2 ILE A 29 3430 4439 3233 333 189 33 C ATOM 124 CD1 ILE A 29 -21.091 16.733 -14.990 1.00 30.75 C ANISOU 124 CD1 ILE A 29 3694 4500 3488 270 174 46 C ATOM 125 N ALA A 30 -22.458 14.778 -9.887 1.00 29.31 N ANISOU 125 N ALA A 30 3542 4382 3212 362 249 59 N ATOM 126 CA ALA A 30 -22.579 15.009 -8.423 1.00 31.04 C ANISOU 126 CA ALA A 30 3734 4648 3411 373 254 46 C ATOM 127 C ALA A 30 -22.175 13.695 -7.756 1.00 32.17 C ANISOU 127 C ALA A 30 3934 4802 3486 447 292 87 C ATOM 128 O ALA A 30 -21.450 13.725 -6.735 1.00 34.57 O ANISOU 128 O ALA A 30 4211 5183 3740 495 292 92 O ATOM 129 CB ALA A 30 -24.003 15.427 -8.067 1.00 29.50 C ANISOU 129 CB ALA A 30 3535 4404 3266 312 254 19 C ATOM 130 N LEU A 31 -22.662 12.584 -8.279 1.00 30.65 N ANISOU 130 N LEU A 31 3821 4535 3288 455 328 112 N ATOM 131 CA LEU A 31 -22.464 11.279 -7.606 1.00 33.43 C ANISOU 131 CA LEU A 31 4246 4878 3578 525 377 153 C ATOM 132 C LEU A 31 -21.036 10.775 -7.807 1.00 35.88 C ANISOU 132 C LEU A 31 4560 5241 3830 611 382 190 C ATOM 133 O LEU A 31 -20.421 10.216 -6.853 1.00 36.94 O ANISOU 133 O LEU A 31 4710 5426 3900 690 402 219 O ATOM 134 CB LEU A 31 -23.473 10.285 -8.154 1.00 35.54 C ANISOU 134 CB LEU A 31 4600 5040 3860 495 421 162 C ATOM 135 CG LEU A 31 -23.419 8.907 -7.510 1.00 42.45 C ANISOU 135 CG LEU A 31 5569 5884 4675 558 486 203 C ATOM 136 CD1 LEU A 31 -24.110 8.936 -6.124 1.00 46.16 C ANISOU 136 CD1 LEU A 31 6043 6361 5132 552 505 194 C ATOM 137 CD2 LEU A 31 -24.054 7.824 -8.396 1.00 44.02 C ANISOU 137 CD2 LEU A 31 5861 5981 4883 533 537 212 C ATOM 138 N ARG A 32 -20.437 11.077 -8.934 1.00 31.65 N ANISOU 138 N ARG A 32 4001 4710 3313 603 361 186 N ATOM 139 CA ARG A 32 -19.002 10.789 -9.126 1.00 33.56 C ANISOU 139 CA ARG A 32 4226 5018 3505 682 360 214 C ATOM 140 C ARG A 32 -18.178 11.584 -8.121 1.00 35.02 C ANISOU 140 C ARG A 32 4323 5322 3659 710 327 198 C ATOM 141 O ARG A 32 -17.293 10.971 -7.494 1.00 34.12 O ANISOU 141 O ARG A 32 4212 5274 3478 800 341 230 O ATOM 142 CB ARG A 32 -18.559 10.979 -10.573 1.00 31.24 C ANISOU 142 CB ARG A 32 3927 4702 3239 660 348 210 C ATOM 143 CG ARG A 32 -17.075 10.833 -10.806 1.00 32.38 C ANISOU 143 CG ARG A 32 4040 4923 3340 733 346 230 C ATOM 144 CD ARG A 32 -16.654 9.418 -10.554 1.00 34.43 C ANISOU 144 CD ARG A 32 4375 5168 3537 830 397 283 C ATOM 145 NE ARG A 32 -16.957 8.529 -11.639 1.00 34.18 N ANISOU 145 NE ARG A 32 4431 5038 3516 825 437 303 N ATOM 146 CZ ARG A 32 -16.718 7.227 -11.619 1.00 39.94 C ANISOU 146 CZ ARG A 32 5247 5727 4199 900 494 349 C ATOM 147 NH1 ARG A 32 -17.021 6.481 -12.659 1.00 41.94 N ANISOU 147 NH1 ARG A 32 5581 5888 4465 883 533 360 N ATOM 148 NH2 ARG A 32 -16.224 6.663 -10.516 1.00 41.50 N ANISOU 148 NH2 ARG A 32 5457 5976 4335 994 516 384 N ATOM 149 N PHE A 33 -18.412 12.869 -7.953 1.00 32.48 N ANISOU 149 N PHE A 33 3927 5032 3379 641 288 151 N ATOM 150 CA PHE A 33 -17.549 13.664 -7.073 1.00 30.87 C ANISOU 150 CA PHE A 33 3636 4947 3144 658 259 127 C ATOM 151 C PHE A 33 -17.744 13.194 -5.632 1.00 35.45 C ANISOU 151 C PHE A 33 4233 5565 3671 705 274 143 C ATOM 152 O PHE A 33 -16.772 13.090 -4.900 1.00 34.42 O ANISOU 152 O PHE A 33 4063 5537 3476 771 266 152 O ATOM 153 CB PHE A 33 -17.887 15.128 -7.183 1.00 32.03 C ANISOU 153 CB PHE A 33 3715 5103 3350 567 226 72 C ATOM 154 CG PHE A 33 -17.140 16.008 -6.210 1.00 32.25 C ANISOU 154 CG PHE A 33 3656 5247 3349 565 202 36 C ATOM 155 CD1 PHE A 33 -15.757 16.050 -6.195 1.00 35.64 C ANISOU 155 CD1 PHE A 33 4029 5781 3729 613 190 36 C ATOM 156 CD2 PHE A 33 -17.842 16.789 -5.328 1.00 33.25 C ANISOU 156 CD2 PHE A 33 3755 5379 3496 513 193 0 C ATOM 157 CE1 PHE A 33 -15.078 16.875 -5.325 1.00 35.01 C ANISOU 157 CE1 PHE A 33 3864 5816 3620 602 168 -4 C ATOM 158 CE2 PHE A 33 -17.161 17.588 -4.437 1.00 37.03 C ANISOU 158 CE2 PHE A 33 4158 5966 3945 505 175 -37 C ATOM 159 CZ PHE A 33 -15.799 17.662 -4.478 1.00 36.74 C ANISOU 159 CZ PHE A 33 4063 6036 3861 543 161 -42 C ATOM 160 N THR A 34 -18.985 13.019 -5.217 1.00 33.61 N ANISOU 160 N THR A 34 4047 5257 3464 666 294 139 N ATOM 161 CA THR A 34 -19.263 12.823 -3.783 1.00 35.70 C ANISOU 161 CA THR A 34 4321 5559 3685 694 306 143 C ATOM 162 C THR A 34 -18.987 11.386 -3.376 1.00 39.80 C ANISOU 162 C THR A 34 4922 6067 4132 792 350 204 C ATOM 163 O THR A 34 -18.572 11.218 -2.219 1.00 41.81 O ANISOU 163 O THR A 34 5166 6398 4321 851 352 217 O ATOM 164 CB THR A 34 -20.663 13.276 -3.369 1.00 34.48 C ANISOU 164 CB THR A 34 4178 5338 3582 614 313 112 C ATOM 165 OG1 THR A 34 -21.626 12.490 -4.049 1.00 32.29 O ANISOU 165 OG1 THR A 34 3981 4947 3339 591 348 129 O ATOM 166 CG2 THR A 34 -20.826 14.773 -3.531 1.00 36.48 C ANISOU 166 CG2 THR A 34 4348 5616 3896 532 273 55 C ATOM 167 N ARG A 35 -19.303 10.397 -4.195 1.00 38.37 N ANISOU 167 N ARG A 35 4826 5792 3960 807 390 237 N ATOM 168 CA ARG A 35 -19.297 8.986 -3.771 1.00 43.65 C ANISOU 168 CA ARG A 35 5595 6421 4567 892 448 293 C ATOM 169 C ARG A 35 -18.274 8.213 -4.600 1.00 44.34 C ANISOU 169 C ARG A 35 5712 6513 4621 971 464 335 C ATOM 170 O ARG A 35 -18.113 7.032 -4.351 1.00 42.61 O ANISOU 170 O ARG A 35 5579 6262 4347 1052 517 387 O ATOM 171 CB ARG A 35 -20.710 8.428 -3.892 1.00 46.42 C ANISOU 171 CB ARG A 35 6033 6647 4957 831 495 290 C ATOM 172 CG ARG A 35 -21.641 8.898 -2.782 1.00 54.15 C ANISOU 172 CG ARG A 35 6998 7626 5947 782 495 261 C ATOM 173 CD ARG A 35 -22.949 8.091 -2.750 1.00 58.63 C ANISOU 173 CD ARG A 35 7663 8077 6537 739 555 264 C ATOM 174 NE ARG A 35 -22.744 6.634 -2.649 1.00 62.42 N ANISOU 174 NE ARG A 35 8257 8503 6956 817 626 320 N ATOM 175 CZ ARG A 35 -22.742 5.925 -1.513 1.00 61.83 C ANISOU 175 CZ ARG A 35 8245 8431 6814 882 672 355 C ATOM 176 NH1 ARG A 35 -22.967 6.513 -0.352 1.00 59.64 N ANISOU 176 NH1 ARG A 35 7927 8210 6520 873 654 338 N ATOM 177 NH2 ARG A 35 -22.510 4.624 -1.547 1.00 66.03 N ANISOU 177 NH2 ARG A 35 8888 8906 7293 956 740 409 N ATOM 178 N ASN A 36 -17.665 8.828 -5.620 1.00 42.29 N ANISOU 178 N ASN A 36 5391 6280 4395 944 428 315 N ATOM 179 CA ASN A 36 -16.782 8.122 -6.571 1.00 43.75 C ANISOU 179 CA ASN A 36 5604 6457 4559 1007 448 349 C ATOM 180 C ASN A 36 -17.518 6.886 -7.092 1.00 43.03 C ANISOU 180 C ASN A 36 5641 6234 4472 1012 515 382 C ATOM 181 O ASN A 36 -16.878 5.862 -7.185 1.00 44.26 O ANISOU 181 O ASN A 36 5858 6381 4575 1105 558 431 O ATOM 182 CB ASN A 36 -15.422 7.746 -5.958 1.00 47.23 C ANISOU 182 CB ASN A 36 6014 7012 4917 1131 446 387 C ATOM 183 CG ASN A 36 -14.414 7.383 -7.011 1.00 49.70 C ANISOU 183 CG ASN A 36 6323 7337 5221 1181 453 407 C ATOM 184 OD1 ASN A 36 -14.629 7.609 -8.201 1.00 42.48 O ANISOU 184 OD1 ASN A 36 5416 6360 4364 1116 450 387 O ATOM 185 ND2 ASN A 36 -13.326 6.779 -6.581 1.00 48.89 N ANISOU 185 ND2 ASN A 36 6213 7316 5044 1303 464 450 N ATOM 186 N GLU A 37 -18.809 7.006 -7.421 1.00 40.36 N ANISOU 186 N GLU A 37 5338 5802 4192 914 524 353 N ATOM 187 CA GLU A 37 -19.603 5.976 -8.133 1.00 41.15 C ANISOU 187 CA GLU A 37 5549 5776 4308 888 584 366 C ATOM 188 C GLU A 37 -20.157 6.504 -9.466 1.00 43.09 C ANISOU 188 C GLU A 37 5777 5969 4626 788 559 327 C ATOM 189 O GLU A 37 -20.251 7.727 -9.628 1.00 39.32 O ANISOU 189 O GLU A 37 5209 5537 4194 729 498 287 O ATOM 190 CB GLU A 37 -20.863 5.606 -7.372 1.00 44.76 C ANISOU 190 CB GLU A 37 6066 6167 4773 844 623 358 C ATOM 191 CG GLU A 37 -20.607 4.881 -6.087 1.00 54.45 C ANISOU 191 CG GLU A 37 7344 7415 5927 934 665 400 C ATOM 192 CD GLU A 37 -21.929 4.416 -5.509 1.00 58.89 C ANISOU 192 CD GLU A 37 7980 7893 6502 879 716 389 C ATOM 193 OE1 GLU A 37 -22.343 3.302 -5.912 1.00 62.94 O ANISOU 193 OE1 GLU A 37 8603 8306 7006 880 788 408 O ATOM 194 OE2 GLU A 37 -22.578 5.219 -4.731 1.00 56.64 O ANISOU 194 OE2 GLU A 37 7639 7638 6241 825 685 354 O ATOM 195 N PHE A 38 -20.599 5.587 -10.307 1.00 42.13 N ANISOU 195 N PHE A 38 5745 5751 4511 769 608 337 N ATOM 196 CA PHE A 38 -21.312 5.876 -11.565 1.00 43.20 C ANISOU 196 CA PHE A 38 5881 5827 4706 673 592 301 C ATOM 197 C PHE A 38 -22.432 4.853 -11.745 1.00 46.60 C ANISOU 197 C PHE A 38 6415 6149 5141 626 656 297 C ATOM 198 O PHE A 38 -22.146 3.642 -11.714 1.00 46.42 O ANISOU 198 O PHE A 38 6490 6076 5072 683 726 334 O ATOM 199 CB PHE A 38 -20.334 5.872 -12.726 1.00 39.35 C ANISOU 199 CB PHE A 38 5385 5351 4214 699 581 313 C ATOM 200 CG PHE A 38 -21.043 6.079 -14.036 1.00 40.03 C ANISOU 200 CG PHE A 38 5482 5376 4351 607 567 281 C ATOM 201 CD1 PHE A 38 -21.387 7.371 -14.453 1.00 38.62 C ANISOU 201 CD1 PHE A 38 5218 5229 4225 536 499 241 C ATOM 202 CD2 PHE A 38 -21.363 5.000 -14.847 1.00 42.34 C ANISOU 202 CD2 PHE A 38 5872 5580 4632 592 623 289 C ATOM 203 CE1 PHE A 38 -22.023 7.559 -15.673 1.00 37.71 C ANISOU 203 CE1 PHE A 38 5112 5064 4148 460 483 216 C ATOM 204 CE2 PHE A 38 -21.982 5.203 -16.082 1.00 43.51 C ANISOU 204 CE2 PHE A 38 6026 5684 4820 507 606 257 C ATOM 205 CZ PHE A 38 -22.316 6.483 -16.481 1.00 37.40 C ANISOU 205 CZ PHE A 38 5165 4950 4096 445 533 223 C ATOM 206 N LEU A 39 -23.658 5.324 -11.951 1.00 45.17 N ANISOU 206 N LEU A 39 6212 5935 5013 526 635 252 N ATOM 207 CA LEU A 39 -24.836 4.456 -12.211 1.00 50.38 C ANISOU 207 CA LEU A 39 6955 6501 5684 460 692 233 C ATOM 208 C LEU A 39 -25.389 4.804 -13.601 1.00 49.96 C ANISOU 208 C LEU A 39 6883 6420 5678 373 660 196 C ATOM 209 O LEU A 39 -25.356 6.036 -14.014 1.00 56.95 O ANISOU 209 O LEU A 39 7673 7358 6604 342 583 174 O ATOM 210 CB LEU A 39 -25.876 4.678 -11.103 1.00 52.72 C ANISOU 210 CB LEU A 39 7237 6794 5997 418 699 210 C ATOM 211 CG LEU A 39 -25.363 4.553 -9.656 1.00 57.54 C ANISOU 211 CG LEU A 39 7853 7447 6560 500 718 243 C ATOM 212 CD1 LEU A 39 -26.443 4.932 -8.640 1.00 56.71 C ANISOU 212 CD1 LEU A 39 7724 7343 6479 448 719 213 C ATOM 213 CD2 LEU A 39 -24.798 3.156 -9.350 1.00 59.00 C ANISOU 213 CD2 LEU A 39 8154 7584 6676 585 803 295 C ATOM 214 N ALA A 40 -25.756 3.771 -14.357 1.00 50.56 N ANISOU 214 N ALA A 40 7048 6418 5742 342 717 192 N ATOM 215 CA ALA A 40 -26.299 3.826 -15.749 1.00 54.02 C ANISOU 215 CA ALA A 40 7489 6824 6211 260 698 158 C ATOM 216 C ALA A 40 -27.841 3.902 -15.741 1.00 55.42 C ANISOU 216 C ALA A 40 7655 6972 6427 156 697 106 C ATOM 217 O ALA A 40 -28.463 3.214 -14.895 1.00 53.69 O ANISOU 217 O ALA A 40 7489 6715 6196 143 756 101 O ATOM 218 CB ALA A 40 -25.831 2.606 -16.503 1.00 51.92 C ANISOU 218 CB ALA A 40 7329 6490 5904 282 768 178 C ATOM 219 N ASN A 41 -28.447 4.621 -16.708 1.00 56.40 N ANISOU 219 N ASN A 41 7721 7114 6592 84 637 69 N ATOM 220 CA ASN A 41 -29.924 4.736 -16.959 1.00 58.26 C ANISOU 220 CA ASN A 41 7933 7335 6865 -17 626 14 C ATOM 221 C ASN A 41 -30.743 4.789 -15.655 1.00 56.10 C ANISOU 221 C ASN A 41 7641 7064 6607 -34 647 -1 C ATOM 222 O ASN A 41 -31.751 4.061 -15.595 1.00 57.41 O ANISOU 222 O ASN A 41 7851 7186 6774 -102 697 -35 O ATOM 223 CB ASN A 41 -30.465 3.612 -17.861 1.00 63.67 C ANISOU 223 CB ASN A 41 8703 7955 7532 -82 683 -11 C ATOM 224 CG ASN A 41 -31.897 3.841 -18.325 1.00 62.77 C ANISOU 224 CG ASN A 41 8546 7848 7453 -189 657 -72 C ATOM 225 N GLN A 42 -30.384 5.642 -14.675 1.00 50.61 N ANISOU 225 N GLN A 42 6883 6421 5923 14 611 15 N ATOM 226 CA GLN A 42 -31.206 5.839 -13.440 1.00 49.87 C ANISOU 226 CA GLN A 42 6763 6335 5847 -5 625 -3 C ATOM 227 C GLN A 42 -32.405 6.735 -13.774 1.00 49.15 C ANISOU 227 C GLN A 42 6587 6272 5816 -84 569 -53 C ATOM 228 O GLN A 42 -32.230 7.720 -14.512 1.00 47.32 O ANISOU 228 O GLN A 42 6286 6081 5612 -86 498 -57 O ATOM 229 CB GLN A 42 -30.429 6.408 -12.259 1.00 49.03 C ANISOU 229 CB GLN A 42 6623 6278 5727 71 610 28 C ATOM 230 CG GLN A 42 -29.278 5.504 -11.832 1.00 52.97 C ANISOU 230 CG GLN A 42 7202 6761 6163 160 664 81 C ATOM 231 CD GLN A 42 -29.715 4.231 -11.132 1.00 53.53 C ANISOU 231 CD GLN A 42 7377 6765 6197 161 758 88 C ATOM 232 OE1 GLN A 42 -30.233 4.266 -10.008 1.00 53.66 O ANISOU 232 OE1 GLN A 42 7391 6784 6212 156 780 82 O ATOM 233 NE2 GLN A 42 -29.488 3.102 -11.792 1.00 48.29 N ANISOU 233 NE2 GLN A 42 6811 6037 5501 166 820 103 N ATOM 234 N GLU A 43 -33.579 6.359 -13.264 1.00 47.88 N ANISOU 234 N GLU A 43 6434 6088 5671 -146 607 -91 N ATOM 235 CA GLU A 43 -34.803 7.186 -13.373 1.00 52.10 C ANISOU 235 CA GLU A 43 6879 6655 6261 -214 560 -140 C ATOM 236 C GLU A 43 -34.480 8.608 -12.823 1.00 46.56 C ANISOU 236 C GLU A 43 6084 6013 5591 -171 493 -128 C ATOM 237 O GLU A 43 -33.828 8.820 -11.720 1.00 45.35 O ANISOU 237 O GLU A 43 5933 5876 5421 -113 505 -101 O ATOM 238 CB GLU A 43 -35.995 6.428 -12.751 1.00 56.83 C ANISOU 238 CB GLU A 43 7507 7219 6865 -282 626 -181 C ATOM 239 CG GLU A 43 -37.357 6.836 -13.321 1.00 61.02 C ANISOU 239 CG GLU A 43 7964 7775 7443 -370 591 -241 C ATOM 240 CD GLU A 43 -37.836 8.184 -12.798 1.00 63.84 C ANISOU 240 CD GLU A 43 8211 8191 7852 -362 528 -253 C ATOM 241 OE1 GLU A 43 -37.503 8.478 -11.630 1.00 67.02 O ANISOU 241 OE1 GLU A 43 8612 8598 8253 -318 544 -233 O ATOM 242 OE2 GLU A 43 -38.528 8.940 -13.539 1.00 59.86 O ANISOU 242 OE2 GLU A 43 7627 7728 7388 -396 466 -282 O ATOM 243 N THR A 44 -34.841 9.619 -13.604 1.00 46.43 N ANISOU 243 N THR A 44 5990 6035 5616 -193 422 -146 N ATOM 244 CA THR A 44 -34.443 11.048 -13.378 1.00 42.68 C ANISOU 244 CA THR A 44 5433 5609 5171 -154 358 -134 C ATOM 245 C THR A 44 -34.887 11.499 -11.966 1.00 40.38 C ANISOU 245 C THR A 44 5106 5335 4901 -151 372 -147 C ATOM 246 O THR A 44 -34.196 12.317 -11.303 1.00 41.27 O ANISOU 246 O THR A 44 5185 5479 5015 -104 351 -130 O ATOM 247 CB THR A 44 -34.997 11.863 -14.562 1.00 45.00 C ANISOU 247 CB THR A 44 5666 5927 5503 -186 292 -154 C ATOM 248 OG1 THR A 44 -34.266 13.071 -14.545 1.00 48.71 O ANISOU 248 OG1 THR A 44 6088 6431 5990 -140 244 -133 O ATOM 249 CG2 THR A 44 -36.500 12.094 -14.525 1.00 42.85 C ANISOU 249 CG2 THR A 44 5339 5667 5272 -247 281 -200 C ATOM 250 N THR A 45 -36.019 11.002 -11.451 1.00 42.53 N ANISOU 250 N THR A 45 5383 5588 5187 -202 412 -181 N ATOM 251 CA THR A 45 -36.606 11.533 -10.187 1.00 42.50 C ANISOU 251 CA THR A 45 5336 5601 5209 -207 424 -200 C ATOM 252 C THR A 45 -35.955 10.850 -8.967 1.00 46.50 C ANISOU 252 C THR A 45 5909 6090 5667 -166 484 -174 C ATOM 253 O THR A 45 -36.224 11.292 -7.873 1.00 46.21 O ANISOU 253 O THR A 45 5845 6070 5642 -161 494 -183 O ATOM 254 CB THR A 45 -38.145 11.440 -10.156 1.00 44.92 C ANISOU 254 CB THR A 45 5606 5905 5556 -281 437 -253 C ATOM 255 OG1 THR A 45 -38.373 10.027 -10.137 1.00 44.09 O ANISOU 255 OG1 THR A 45 5585 5751 5414 -316 508 -260 O ATOM 256 CG2 THR A 45 -38.825 12.098 -11.346 1.00 42.48 C ANISOU 256 CG2 THR A 45 5228 5625 5288 -314 374 -277 C ATOM 257 N ILE A 46 -35.089 9.855 -9.127 1.00 48.26 N ANISOU 257 N ILE A 46 6216 6283 5835 -130 521 -139 N ATOM 258 CA ILE A 46 -34.632 9.055 -7.943 1.00 52.94 C ANISOU 258 CA ILE A 46 6882 6856 6376 -88 587 -112 C ATOM 259 C ILE A 46 -33.238 9.512 -7.450 1.00 49.71 C ANISOU 259 C ILE A 46 6464 6492 5931 -2 561 -68 C ATOM 260 O ILE A 46 -32.960 9.280 -6.259 1.00 51.87 O ANISOU 260 O ILE A 46 6765 6773 6169 35 596 -52 O ATOM 261 CB ILE A 46 -34.739 7.539 -8.233 1.00 55.50 C ANISOU 261 CB ILE A 46 7314 7112 6659 -103 664 -104 C ATOM 262 CG1 ILE A 46 -33.736 7.064 -9.289 1.00 57.19 C ANISOU 262 CG1 ILE A 46 7574 7312 6841 -65 657 -70 C ATOM 263 CG2 ILE A 46 -36.192 7.170 -8.597 1.00 54.36 C ANISOU 263 CG2 ILE A 46 7166 6936 6552 -202 692 -160 C ATOM 264 CD1 ILE A 46 -33.777 5.546 -9.556 1.00 61.98 C ANISOU 264 CD1 ILE A 46 8299 7844 7404 -76 743 -61 C ATOM 265 N GLY A 47 -32.399 10.176 -8.256 1.00 44.51 N ANISOU 265 N GLY A 47 5765 5867 5279 26 504 -53 N ATOM 266 CA GLY A 47 -31.131 10.716 -7.708 1.00 42.95 C ANISOU 266 CA GLY A 47 5545 5724 5050 98 478 -22 C ATOM 267 C GLY A 47 -31.316 11.525 -6.383 1.00 39.64 C ANISOU 267 C GLY A 47 5074 5347 4639 102 471 -38 C ATOM 268 O GLY A 47 -32.219 12.338 -6.324 1.00 36.77 O ANISOU 268 O GLY A 47 4652 4988 4331 51 448 -75 O ATOM 269 N ALA A 48 -30.429 11.352 -5.374 1.00 37.46 N ANISOU 269 N ALA A 48 4815 5107 4307 165 487 -10 N ATOM 270 CA ALA A 48 -30.425 12.154 -4.133 1.00 36.21 C ANISOU 270 CA ALA A 48 4609 4999 4148 172 476 -25 C ATOM 271 C ALA A 48 -30.448 13.653 -4.492 1.00 34.70 C ANISOU 271 C ALA A 48 4322 4846 4013 141 414 -57 C ATOM 272 O ALA A 48 -29.619 14.100 -5.352 1.00 35.46 O ANISOU 272 O ALA A 48 4392 4967 4113 158 374 -46 O ATOM 273 CB ALA A 48 -29.216 11.834 -3.298 1.00 38.19 C ANISOU 273 CB ALA A 48 4883 5302 4324 252 487 11 C ATOM 274 N ALA A 49 -31.323 14.404 -3.856 1.00 33.02 N ANISOU 274 N ALA A 49 4065 4637 3842 99 411 -92 N ATOM 275 CA ALA A 49 -31.477 15.866 -4.053 1.00 29.19 C ANISOU 275 CA ALA A 49 3497 4179 3412 70 364 -124 C ATOM 276 C ALA A 49 -30.299 16.579 -3.409 1.00 30.86 C ANISOU 276 C ALA A 49 3674 4459 3590 107 344 -120 C ATOM 277 O ALA A 49 -29.956 17.694 -3.863 1.00 28.47 O ANISOU 277 O ALA A 49 3317 4180 3321 95 305 -136 O ATOM 278 CB ALA A 49 -32.787 16.280 -3.505 1.00 32.19 C ANISOU 278 CB ALA A 49 3849 4537 3841 20 379 -161 C ATOM 279 N PHE A 50 -29.726 15.999 -2.328 1.00 28.39 N ANISOU 279 N PHE A 50 3393 4181 3212 150 371 -102 N ATOM 280 CA PHE A 50 -28.679 16.662 -1.533 1.00 29.86 C ANISOU 280 CA PHE A 50 3539 4447 3358 181 352 -106 C ATOM 281 C PHE A 50 -27.522 15.690 -1.319 1.00 31.98 C ANISOU 281 C PHE A 50 3850 4755 3544 255 363 -62 C ATOM 282 O PHE A 50 -27.735 14.580 -0.822 1.00 30.96 O ANISOU 282 O PHE A 50 3789 4601 3372 286 405 -35 O ATOM 283 CB PHE A 50 -29.248 17.154 -0.217 1.00 29.49 C ANISOU 283 CB PHE A 50 3473 4419 3312 158 371 -136 C ATOM 284 CG PHE A 50 -30.503 17.981 -0.348 1.00 27.96 C ANISOU 284 CG PHE A 50 3242 4180 3198 93 369 -177 C ATOM 285 CD1 PHE A 50 -30.456 19.301 -0.751 1.00 27.74 C ANISOU 285 CD1 PHE A 50 3151 4166 3223 62 336 -207 C ATOM 286 CD2 PHE A 50 -31.722 17.447 0.012 1.00 28.09 C ANISOU 286 CD2 PHE A 50 3289 4146 3237 64 407 -186 C ATOM 287 CE1 PHE A 50 -31.616 20.046 -0.851 1.00 25.72 C ANISOU 287 CE1 PHE A 50 2863 3870 3038 14 338 -240 C ATOM 288 CE2 PHE A 50 -32.886 18.201 -0.088 1.00 29.43 C ANISOU 288 CE2 PHE A 50 3418 4284 3481 10 406 -224 C ATOM 289 CZ PHE A 50 -32.811 19.509 -0.530 1.00 27.68 C ANISOU 289 CZ PHE A 50 3132 4074 3308 -8 370 -248 C ATOM 290 N LEU A 51 -26.340 16.094 -1.713 1.00 30.08 N ANISOU 290 N LEU A 51 3573 4573 3282 284 330 -56 N ATOM 291 CA ALEU A 51 -25.103 15.283 -1.584 0.54 32.04 C ANISOU 291 CA ALEU A 51 3846 4874 3451 364 334 -14 C ATOM 292 CA BLEU A 51 -25.109 15.273 -1.555 0.46 32.38 C ANISOU 292 CA BLEU A 51 3890 4918 3494 364 335 -14 C ATOM 293 C LEU A 51 -24.042 16.162 -0.934 1.00 35.56 C ANISOU 293 C LEU A 51 4220 5427 3862 380 303 -35 C ATOM 294 O LEU A 51 -24.238 17.440 -0.969 1.00 37.28 O ANISOU 294 O LEU A 51 4374 5658 4130 319 278 -82 O ATOM 295 CB ALEU A 51 -24.678 14.829 -2.978 0.54 31.65 C ANISOU 295 CB ALEU A 51 3820 4791 3415 378 326 10 C ATOM 296 CB BLEU A 51 -24.646 14.754 -2.916 0.46 32.44 C ANISOU 296 CB BLEU A 51 3922 4892 3508 383 328 12 C ATOM 297 CG ALEU A 51 -25.789 14.196 -3.822 0.54 32.11 C ANISOU 297 CG ALEU A 51 3934 4747 3518 341 349 15 C ATOM 298 CG BLEU A 51 -25.571 13.756 -3.615 0.46 33.32 C ANISOU 298 CG BLEU A 51 4110 4905 3643 368 362 31 C ATOM 299 CD1ALEU A 51 -26.341 15.184 -4.846 0.54 29.28 C ANISOU 299 CD1ALEU A 51 3529 4357 3238 274 315 -16 C ATOM 300 CD1BLEU A 51 -25.116 13.547 -5.062 0.46 34.39 C ANISOU 300 CD1BLEU A 51 4255 5013 3795 371 348 47 C ATOM 301 CD2ALEU A 51 -25.281 12.920 -4.485 0.54 34.66 C ANISOU 301 CD2ALEU A 51 4329 5039 3800 394 377 61 C ATOM 302 CD2BLEU A 51 -25.629 12.430 -2.869 0.46 32.73 C ANISOU 302 CD2BLEU A 51 4119 4809 3506 422 417 69 C ATOM 303 N SER A 52 -22.969 15.563 -0.372 1.00 32.99 N ANISOU 303 N SER A 52 3901 5178 3454 456 304 -5 N ATOM 304 CA ASER A 52 -21.929 16.372 0.315 0.33 34.07 C ANISOU 304 CA ASER A 52 3962 5434 3549 469 273 -31 C ATOM 305 CA BSER A 52 -21.909 16.411 0.221 0.67 33.34 C ANISOU 305 CA BSER A 52 3866 5339 3460 466 272 -32 C ATOM 306 C SER A 52 -20.565 15.696 0.198 1.00 35.23 C ANISOU 306 C SER A 52 4104 5660 3621 557 264 6 C ATOM 307 O SER A 52 -20.546 14.486 0.096 1.00 34.49 O ANISOU 307 O SER A 52 4082 5531 3490 622 292 58 O ATOM 308 CB ASER A 52 -22.295 16.605 1.762 0.33 35.36 C ANISOU 308 CB ASER A 52 4117 5637 3678 462 285 -51 C ATOM 309 CB BSER A 52 -22.294 16.864 1.607 0.67 36.02 C ANISOU 309 CB BSER A 52 4188 5721 3777 447 278 -61 C ATOM 310 OG ASER A 52 -21.291 17.360 2.427 0.33 36.14 O ANISOU 310 OG ASER A 52 4142 5859 3731 468 255 -81 O ATOM 311 OG BSER A 52 -22.385 15.762 2.490 0.67 36.25 O ANISOU 311 OG BSER A 52 4280 5755 3736 512 310 -20 O ATOM 312 N LYS A 53 -19.518 16.480 0.276 1.00 37.28 N ANISOU 312 N LYS A 53 4283 6022 3859 556 230 -22 N ATOM 313 CA LYS A 53 -18.146 15.967 0.435 1.00 37.86 C ANISOU 313 CA LYS A 53 4331 6202 3850 643 217 5 C ATOM 314 C LYS A 53 -17.371 17.114 1.062 1.00 40.39 C ANISOU 314 C LYS A 53 4550 6647 4148 610 183 -51 C ATOM 315 O LYS A 53 -17.624 18.302 0.670 1.00 37.50 O ANISOU 315 O LYS A 53 4137 6260 3848 518 170 -105 O ATOM 316 CB LYS A 53 -17.601 15.513 -0.917 1.00 39.81 C ANISOU 316 CB LYS A 53 4593 6416 4117 670 216 33 C ATOM 317 CG LYS A 53 -16.256 14.820 -0.814 1.00 41.93 C ANISOU 317 CG LYS A 53 4843 6786 4303 772 209 69 C ATOM 318 CD LYS A 53 -15.860 14.054 -2.056 1.00 44.38 C ANISOU 318 CD LYS A 53 5194 7043 4623 814 224 110 C ATOM 319 CE LYS A 53 -14.426 14.284 -2.512 1.00 47.69 C ANISOU 319 CE LYS A 53 5538 7570 5012 852 198 103 C ATOM 320 NZ LYS A 53 -14.124 13.752 -3.872 1.00 45.71 N ANISOU 320 NZ LYS A 53 5323 7256 4788 872 213 132 N ATOM 321 N THR A 54 -16.540 16.802 2.064 1.00 39.63 N ANISOU 321 N THR A 54 4425 6674 3959 678 172 -41 N ATOM 322 CA THR A 54 -15.674 17.811 2.705 1.00 42.60 C ANISOU 322 CA THR A 54 4697 7188 4299 649 139 -99 C ATOM 323 C THR A 54 -14.253 17.620 2.185 1.00 45.29 C ANISOU 323 C THR A 54 4980 7634 4595 706 116 -90 C ATOM 324 O THR A 54 -13.793 16.472 2.149 1.00 41.94 O ANISOU 324 O THR A 54 4592 7228 4112 812 123 -28 O ATOM 325 CB THR A 54 -15.747 17.688 4.220 1.00 44.50 C ANISOU 325 CB THR A 54 4935 7509 4463 678 138 -103 C ATOM 326 OG1 THR A 54 -17.119 17.955 4.452 1.00 44.73 O ANISOU 326 OG1 THR A 54 5017 7424 4554 611 164 -117 O ATOM 327 CG2 THR A 54 -14.805 18.640 4.935 1.00 47.71 C ANISOU 327 CG2 THR A 54 5234 8073 4820 649 105 -166 C ATOM 328 N VAL A 55 -13.593 18.698 1.791 1.00 45.87 N ANISOU 328 N VAL A 55 4966 7768 4694 639 95 -151 N ATOM 329 CA VAL A 55 -12.258 18.609 1.137 1.00 48.97 C ANISOU 329 CA VAL A 55 5295 8253 5055 679 76 -151 C ATOM 330 C VAL A 55 -11.300 19.572 1.835 1.00 48.56 C ANISOU 330 C VAL A 55 5128 8364 4957 640 49 -222 C ATOM 331 O VAL A 55 -11.743 20.664 2.200 1.00 45.08 O ANISOU 331 O VAL A 55 4661 7914 4553 539 50 -286 O ATOM 332 CB VAL A 55 -12.408 18.883 -0.373 1.00 50.71 C ANISOU 332 CB VAL A 55 5536 8367 5363 628 88 -152 C ATOM 333 CG1 VAL A 55 -11.094 19.260 -1.059 1.00 54.12 C ANISOU 333 CG1 VAL A 55 5886 8892 5782 627 73 -180 C ATOM 334 CG2 VAL A 55 -13.047 17.681 -1.059 1.00 51.18 C ANISOU 334 CG2 VAL A 55 5700 8300 5442 689 113 -78 C ATOM 335 N MET A 56 -10.022 19.193 1.988 1.00 54.92 N ANISOU 335 N MET A 56 5866 9315 5683 714 27 -216 N ATOM 336 CA MET A 56 -8.996 20.103 2.557 1.00 58.69 C ANISOU 336 CA MET A 56 6221 9964 6113 671 0 -292 C ATOM 337 C MET A 56 -8.460 20.979 1.424 1.00 58.31 C ANISOU 337 C MET A 56 6119 9905 6130 586 5 -344 C ATOM 338 O MET A 56 -7.828 20.455 0.519 1.00 59.19 O ANISOU 338 O MET A 56 6227 10017 6243 638 6 -312 O ATOM 339 CB MET A 56 -7.864 19.306 3.215 1.00 65.64 C ANISOU 339 CB MET A 56 7044 11018 6877 793 -28 -263 C ATOM 340 CG MET A 56 -8.206 18.919 4.645 1.00 72.25 C ANISOU 340 CG MET A 56 7900 11916 7634 845 -39 -244 C ATOM 341 SD MET A 56 -8.670 20.379 5.657 1.00 87.29 S ANISOU 341 SD MET A 56 9751 13862 9550 702 -44 -347 S ATOM 342 CE MET A 56 -7.163 21.374 5.648 1.00 80.91 C ANISOU 342 CE MET A 56 8783 13257 8701 643 -75 -443 C ATOM 343 N ILE A 57 -8.770 22.267 1.410 1.00 60.53 N ANISOU 343 N ILE A 57 6372 10159 6467 459 15 -420 N ATOM 344 CA ILE A 57 -8.250 23.147 0.320 1.00 68.27 C ANISOU 344 CA ILE A 57 7309 11121 7506 374 28 -470 C ATOM 345 C ILE A 57 -7.054 23.910 0.901 1.00 78.36 C ANISOU 345 C ILE A 57 8462 12585 8725 329 13 -554 C ATOM 346 O ILE A 57 -6.512 23.480 1.968 1.00 84.05 O ANISOU 346 O ILE A 57 9128 13455 9350 393 -15 -554 O ATOM 347 CB ILE A 57 -9.349 24.062 -0.235 1.00 66.40 C ANISOU 347 CB ILE A 57 7133 10722 7373 268 58 -495 C ATOM 348 CG1 ILE A 57 -9.892 25.030 0.833 1.00 67.30 C ANISOU 348 CG1 ILE A 57 7229 10851 7489 184 65 -559 C ATOM 349 CG2 ILE A 57 -10.426 23.197 -0.885 1.00 64.00 C ANISOU 349 CG2 ILE A 57 6941 10255 7119 319 69 -414 C ATOM 350 N ASP A 58 -6.603 24.971 0.227 1.00 83.02 N ANISOU 350 N ASP A 58 9005 13175 9362 225 32 -623 N ATOM 351 CA ASP A 58 -5.677 25.920 0.898 1.00 83.90 C ANISOU 351 CA ASP A 58 9001 13449 9426 147 27 -722 C ATOM 352 C ASP A 58 -6.543 26.711 1.893 1.00 81.59 C ANISOU 352 C ASP A 58 8729 13125 9145 68 38 -769 C ATOM 353 O ASP A 58 -7.754 27.051 1.603 1.00 82.97 O ANISOU 353 O ASP A 58 8995 13128 9401 23 65 -752 O ATOM 354 CB ASP A 58 -4.799 26.747 -0.055 1.00 82.56 C ANISOU 354 CB ASP A 58 8772 13305 9292 62 52 -786 C ATOM 355 CG ASP A 58 -3.784 27.573 0.728 1.00 84.23 C ANISOU 355 CG ASP A 58 8858 13704 9441 -12 47 -890 C ATOM 356 OD1 ASP A 58 -2.824 26.971 1.281 1.00 82.23 O ANISOU 356 OD1 ASP A 58 8517 13632 9096 63 10 -890 O ATOM 357 OD2 ASP A 58 -4.005 28.807 0.857 1.00 67.87 O ANISOU 357 OD2 ASP A 58 6778 11599 7409 -143 81 -971 O ATOM 358 N GLY A 59 -6.007 26.863 3.091 1.00 74.79 N ANISOU 358 N GLY A 59 7790 12429 8198 65 16 -818 N ATOM 359 CA GLY A 59 -6.720 27.595 4.137 1.00 72.91 C ANISOU 359 CA GLY A 59 7563 12180 7957 -9 27 -868 C ATOM 360 C GLY A 59 -7.522 26.696 5.058 1.00 71.73 C ANISOU 360 C GLY A 59 7476 12012 7766 81 6 -801 C ATOM 361 O GLY A 59 -7.484 27.003 6.283 1.00 72.01 O ANISOU 361 O GLY A 59 7472 12151 7737 57 -4 -847 O ATOM 362 N ARG A 60 -8.255 25.679 4.563 1.00 61.26 N ANISOU 362 N ARG A 60 6244 10558 6472 171 6 -703 N ATOM 363 CA ARG A 60 -9.466 25.248 5.328 1.00 63.33 C ANISOU 363 CA ARG A 60 6593 10733 6736 203 12 -658 C ATOM 364 C ARG A 60 -10.040 23.894 4.856 1.00 57.50 C ANISOU 364 C ARG A 60 5948 9889 6008 319 10 -549 C ATOM 365 O ARG A 60 -9.791 23.509 3.702 1.00 54.78 O ANISOU 365 O ARG A 60 5622 9487 5703 348 14 -511 O ATOM 366 CB ARG A 60 -10.503 26.383 5.221 1.00 68.57 C ANISOU 366 CB ARG A 60 7299 11261 7494 81 51 -708 C ATOM 367 CG ARG A 60 -11.230 26.413 3.871 1.00 78.21 C ANISOU 367 CG ARG A 60 8594 12297 8822 64 76 -669 C ATOM 368 CD ARG A 60 -11.407 27.774 3.212 1.00 83.94 C ANISOU 368 CD ARG A 60 9314 12946 9634 -58 111 -736 C ATOM 369 NE ARG A 60 -12.314 28.562 4.038 1.00 87.10 N ANISOU 369 NE ARG A 60 9737 13296 10059 -130 136 -779 N ATOM 370 CZ ARG A 60 -12.096 29.794 4.505 1.00 84.59 C ANISOU 370 CZ ARG A 60 9374 13019 9746 -236 161 -871 C ATOM 371 NH1 ARG A 60 -10.999 30.475 4.210 1.00 81.87 N ANISOU 371 NH1 ARG A 60 8956 12766 9385 -297 168 -937 N ATOM 372 NH2 ARG A 60 -13.022 30.352 5.259 1.00 87.71 N ANISOU 372 NH2 ARG A 60 9803 13357 10165 -286 186 -899 N ATOM 373 N ALA A 61 -10.825 23.212 5.717 1.00 52.88 N ANISOU 373 N ALA A 61 5428 9273 5391 375 11 -502 N ATOM 374 CA ALA A 61 -11.795 22.140 5.331 1.00 55.30 C ANISOU 374 CA ALA A 61 5847 9432 5731 447 28 -413 C ATOM 375 C ALA A 61 -13.040 22.799 4.709 1.00 47.33 C ANISOU 375 C ALA A 61 4898 8245 4837 355 60 -427 C ATOM 376 O ALA A 61 -13.652 23.669 5.341 1.00 47.12 O ANISOU 376 O ALA A 61 4867 8199 4836 274 74 -480 O ATOM 377 CB ALA A 61 -12.208 21.302 6.517 1.00 54.52 C ANISOU 377 CB ALA A 61 5794 9362 5557 525 26 -368 C ATOM 378 N LEU A 62 -13.393 22.417 3.498 1.00 46.82 N ANISOU 378 N LEU A 62 4888 8060 4841 367 73 -384 N ATOM 379 CA LEU A 62 -14.582 22.985 2.802 1.00 43.85 C ANISOU 379 CA LEU A 62 4567 7519 4572 291 99 -391 C ATOM 380 C LEU A 62 -15.618 21.873 2.621 1.00 41.20 C ANISOU 380 C LEU A 62 4330 7065 4256 351 114 -317 C ATOM 381 O LEU A 62 -15.250 20.859 2.041 1.00 41.72 O ANISOU 381 O LEU A 62 4428 7123 4301 429 110 -259 O ATOM 382 CB LEU A 62 -14.158 23.497 1.424 1.00 46.16 C ANISOU 382 CB LEU A 62 4842 7769 4926 250 101 -405 C ATOM 383 CG LEU A 62 -15.293 24.004 0.519 1.00 44.34 C ANISOU 383 CG LEU A 62 4669 7375 4801 188 124 -403 C ATOM 384 CD1 LEU A 62 -16.031 25.118 1.219 1.00 46.40 C ANISOU 384 CD1 LEU A 62 4921 7608 5099 102 141 -461 C ATOM 385 CD2 LEU A 62 -14.698 24.493 -0.780 1.00 49.01 C ANISOU 385 CD2 LEU A 62 5241 7943 5437 155 125 -416 C ATOM 386 N LYS A 63 -16.829 22.044 3.146 1.00 37.17 N ANISOU 386 N LYS A 63 3866 6472 3782 315 134 -322 N ATOM 387 CA LYS A 63 -17.910 21.067 2.921 1.00 35.61 C ANISOU 387 CA LYS A 63 3762 6155 3613 353 155 -262 C ATOM 388 C LYS A 63 -18.743 21.518 1.699 1.00 32.92 C ANISOU 388 C LYS A 63 3449 5679 3377 294 166 -265 C ATOM 389 O LYS A 63 -19.410 22.534 1.794 1.00 34.28 O ANISOU 389 O LYS A 63 3608 5808 3607 217 175 -311 O ATOM 390 CB LYS A 63 -18.816 20.945 4.117 1.00 37.75 C ANISOU 390 CB LYS A 63 4066 6409 3866 348 174 -265 C ATOM 391 CG LYS A 63 -19.796 19.793 3.978 1.00 38.91 C ANISOU 391 CG LYS A 63 4307 6449 4026 392 200 -204 C ATOM 392 CD LYS A 63 -20.499 19.445 5.299 1.00 41.30 C ANISOU 392 CD LYS A 63 4648 6754 4288 404 223 -200 C ATOM 393 CE LYS A 63 -21.633 18.475 5.082 1.00 45.14 C ANISOU 393 CE LYS A 63 5226 7117 4805 422 260 -153 C ATOM 394 NZ LYS A 63 -22.341 18.194 6.342 1.00 49.54 N ANISOU 394 NZ LYS A 63 5823 7671 5327 426 288 -153 N ATOM 395 N TYR A 64 -18.611 20.820 0.592 1.00 33.29 N ANISOU 395 N TYR A 64 3531 5674 3442 331 165 -220 N ATOM 396 CA TYR A 64 -19.460 21.040 -0.620 1.00 34.06 C ANISOU 396 CA TYR A 64 3665 5644 3629 287 173 -213 C ATOM 397 C TYR A 64 -20.851 20.504 -0.283 1.00 32.61 C ANISOU 397 C TYR A 64 3548 5368 3474 284 195 -192 C ATOM 398 O TYR A 64 -21.072 19.298 0.034 1.00 32.60 O ANISOU 398 O TYR A 64 3603 5350 3432 344 211 -145 O ATOM 399 CB TYR A 64 -18.885 20.358 -1.847 1.00 33.41 C ANISOU 399 CB TYR A 64 3605 5540 3547 329 166 -173 C ATOM 400 CG TYR A 64 -17.588 20.873 -2.382 1.00 35.55 C ANISOU 400 CG TYR A 64 3815 5890 3802 326 149 -194 C ATOM 401 CD1 TYR A 64 -16.373 20.392 -1.906 1.00 40.11 C ANISOU 401 CD1 TYR A 64 4353 6587 4298 390 137 -185 C ATOM 402 CD2 TYR A 64 -17.548 21.887 -3.336 1.00 35.83 C ANISOU 402 CD2 TYR A 64 3827 5886 3900 259 146 -227 C ATOM 403 CE1 TYR A 64 -15.174 20.883 -2.413 1.00 43.51 C ANISOU 403 CE1 TYR A 64 4718 7096 4714 381 124 -211 C ATOM 404 CE2 TYR A 64 -16.368 22.396 -3.821 1.00 35.98 C ANISOU 404 CE2 TYR A 64 3790 5975 3905 247 137 -252 C ATOM 405 CZ TYR A 64 -15.168 21.862 -3.403 1.00 40.48 C ANISOU 405 CZ TYR A 64 4317 6664 4397 307 126 -245 C ATOM 406 OH TYR A 64 -13.988 22.412 -3.879 1.00 42.76 O ANISOU 406 OH TYR A 64 4542 7030 4674 288 120 -278 O ATOM 407 N GLU A 65 -21.828 21.375 -0.257 1.00 30.54 N ANISOU 407 N GLU A 65 3280 5044 3279 216 203 -227 N ATOM 408 CA GLU A 65 -23.238 20.912 -0.133 1.00 29.54 C ANISOU 408 CA GLU A 65 3209 4822 3192 205 226 -211 C ATOM 409 C GLU A 65 -23.846 20.987 -1.544 1.00 31.45 C ANISOU 409 C GLU A 65 3472 4970 3507 179 221 -199 C ATOM 410 O GLU A 65 -24.315 22.051 -1.940 1.00 28.76 O ANISOU 410 O GLU A 65 3105 4592 3229 125 216 -231 O ATOM 411 CB GLU A 65 -24.041 21.782 0.793 1.00 32.15 C ANISOU 411 CB GLU A 65 3518 5144 3551 151 240 -256 C ATOM 412 CG GLU A 65 -23.529 21.693 2.253 1.00 36.81 C ANISOU 412 CG GLU A 65 4091 5830 4063 173 246 -270 C ATOM 413 CD GLU A 65 -24.060 20.460 3.002 1.00 46.75 C ANISOU 413 CD GLU A 65 5413 7072 5276 223 270 -230 C ATOM 414 OE1 GLU A 65 -24.573 19.514 2.369 1.00 49.38 O ANISOU 414 OE1 GLU A 65 5803 7331 5625 248 284 -188 O ATOM 415 OE2 GLU A 65 -24.008 20.466 4.243 1.00 51.07 O ANISOU 415 OE2 GLU A 65 5956 7676 5771 231 281 -243 O ATOM 416 N ILE A 66 -23.835 19.863 -2.205 1.00 30.60 N ANISOU 416 N ILE A 66 3414 4826 3383 222 225 -153 N ATOM 417 CA ILE A 66 -24.252 19.746 -3.646 1.00 32.42 C ANISOU 417 CA ILE A 66 3670 4979 3668 205 218 -136 C ATOM 418 C ILE A 66 -25.761 19.483 -3.715 1.00 31.02 C ANISOU 418 C ILE A 66 3529 4716 3541 174 234 -137 C ATOM 419 O ILE A 66 -26.270 18.458 -3.186 1.00 33.16 O ANISOU 419 O ILE A 66 3848 4964 3785 196 262 -116 O ATOM 420 CB ILE A 66 -23.485 18.625 -4.364 1.00 33.01 C ANISOU 420 CB ILE A 66 3785 5057 3700 262 219 -91 C ATOM 421 CG1 ILE A 66 -21.955 18.672 -4.269 1.00 37.21 C ANISOU 421 CG1 ILE A 66 4280 5683 4175 306 205 -86 C ATOM 422 CG2 ILE A 66 -23.928 18.644 -5.822 1.00 32.58 C ANISOU 422 CG2 ILE A 66 3752 4928 3700 236 209 -82 C ATOM 423 CD1 ILE A 66 -21.406 20.026 -4.447 1.00 39.38 C ANISOU 423 CD1 ILE A 66 4486 6000 4475 260 184 -130 C ATOM 424 N TRP A 67 -26.455 20.379 -4.400 1.00 27.91 N ANISOU 424 N TRP A 67 3111 4275 3216 125 221 -159 N ATOM 425 CA TRP A 67 -27.897 20.270 -4.661 1.00 24.51 C ANISOU 425 CA TRP A 67 2699 3772 2840 93 230 -165 C ATOM 426 C TRP A 67 -28.100 19.740 -6.084 1.00 25.77 C ANISOU 426 C TRP A 67 2889 3881 3019 94 217 -140 C ATOM 427 O TRP A 67 -27.390 20.180 -6.979 1.00 25.58 O ANISOU 427 O TRP A 67 2852 3865 3000 97 195 -134 O ATOM 428 CB TRP A 67 -28.536 21.628 -4.522 1.00 25.69 C ANISOU 428 CB TRP A 67 2802 3909 3050 48 223 -204 C ATOM 429 CG TRP A 67 -28.705 22.116 -3.107 1.00 25.49 C ANISOU 429 CG TRP A 67 2752 3917 3015 35 242 -235 C ATOM 430 CD1 TRP A 67 -27.792 22.084 -2.100 1.00 28.60 C ANISOU 430 CD1 TRP A 67 3135 4381 3349 54 250 -241 C ATOM 431 CD2 TRP A 67 -29.876 22.702 -2.567 1.00 26.67 C ANISOU 431 CD2 TRP A 67 2883 4034 3213 0 258 -264 C ATOM 432 NE1 TRP A 67 -28.307 22.673 -0.961 1.00 27.06 N ANISOU 432 NE1 TRP A 67 2919 4199 3163 28 269 -276 N ATOM 433 CE2 TRP A 67 -29.599 23.040 -1.219 1.00 26.71 C ANISOU 433 CE2 TRP A 67 2871 4088 3187 -4 277 -290 C ATOM 434 CE3 TRP A 67 -31.135 23.004 -3.100 1.00 27.50 C ANISOU 434 CE3 TRP A 67 2981 4080 3386 -25 257 -273 C ATOM 435 CZ2 TRP A 67 -30.549 23.707 -0.461 1.00 25.67 C ANISOU 435 CZ2 TRP A 67 2721 3937 3095 -37 299 -324 C ATOM 436 CZ3 TRP A 67 -32.101 23.599 -2.337 1.00 27.99 C ANISOU 436 CZ3 TRP A 67 3020 4127 3487 -52 278 -305 C ATOM 437 CH2 TRP A 67 -31.789 23.929 -0.999 1.00 28.01 C ANISOU 437 CH2 TRP A 67 3012 4171 3460 -59 301 -330 C ATOM 438 N ASP A 68 -28.959 18.755 -6.211 1.00 26.50 N ANISOU 438 N ASP A 68 3025 3928 3114 90 236 -127 N ATOM 439 CA ASP A 68 -29.322 18.127 -7.490 1.00 26.30 C ANISOU 439 CA ASP A 68 3033 3854 3103 82 229 -109 C ATOM 440 C ASP A 68 -30.835 18.287 -7.681 1.00 24.94 C ANISOU 440 C ASP A 68 2850 3637 2988 36 229 -132 C ATOM 441 O ASP A 68 -31.596 18.621 -6.729 1.00 25.25 O ANISOU 441 O ASP A 68 2867 3678 3048 17 245 -157 O ATOM 442 CB ASP A 68 -28.772 16.703 -7.586 1.00 25.73 C ANISOU 442 CB ASP A 68 3027 3774 2973 121 256 -74 C ATOM 443 CG ASP A 68 -28.774 16.117 -8.973 1.00 27.99 C ANISOU 443 CG ASP A 68 3349 4021 3263 117 249 -56 C ATOM 444 OD1 ASP A 68 -28.830 16.915 -9.957 1.00 26.22 O ANISOU 444 OD1 ASP A 68 3094 3790 3077 95 213 -65 O ATOM 445 OD2 ASP A 68 -28.865 14.874 -9.054 1.00 27.68 O ANISOU 445 OD2 ASP A 68 3372 3951 3191 130 283 -36 O ATOM 446 N THR A 69 -31.320 18.145 -8.900 1.00 25.17 N ANISOU 446 N THR A 69 2887 3632 3042 18 211 -128 N ATOM 447 CA THR A 69 -32.666 18.596 -9.319 1.00 26.96 C ANISOU 447 CA THR A 69 3083 3833 3327 -21 196 -152 C ATOM 448 C THR A 69 -33.801 17.617 -8.994 1.00 27.77 C ANISOU 448 C THR A 69 3209 3908 3433 -51 228 -166 C ATOM 449 O THR A 69 -34.981 18.029 -9.194 1.00 27.90 O ANISOU 449 O THR A 69 3187 3915 3498 -84 217 -192 O ATOM 450 CB THR A 69 -32.713 18.778 -10.846 1.00 25.72 C ANISOU 450 CB THR A 69 2926 3659 3187 -28 159 -142 C ATOM 451 OG1 THR A 69 -32.508 17.523 -11.486 1.00 25.69 O ANISOU 451 OG1 THR A 69 2979 3635 3146 -27 174 -123 O ATOM 452 CG2 THR A 69 -31.660 19.762 -11.269 1.00 27.86 C ANISOU 452 CG2 THR A 69 3177 3949 3457 -6 134 -130 C ATOM 453 N ALA A 70 -33.512 16.350 -8.687 1.00 28.90 N ANISOU 453 N ALA A 70 3414 4037 3527 -41 268 -150 N ATOM 454 CA ALA A 70 -34.534 15.292 -8.503 1.00 31.02 C ANISOU 454 CA ALA A 70 3719 4273 3795 -76 309 -165 C ATOM 455 C ALA A 70 -35.429 15.255 -9.731 1.00 32.60 C ANISOU 455 C ALA A 70 3902 4455 4029 -119 284 -182 C ATOM 456 O ALA A 70 -36.631 14.918 -9.576 1.00 33.68 O ANISOU 456 O ALA A 70 4028 4578 4190 -165 304 -213 O ATOM 457 CB ALA A 70 -35.355 15.591 -7.271 1.00 34.08 C ANISOU 457 CB ALA A 70 4079 4665 4204 -97 335 -193 C ATOM 458 N GLY A 71 -34.849 15.490 -10.913 1.00 29.56 N ANISOU 458 N GLY A 71 3518 4073 3641 -105 245 -164 N ATOM 459 CA GLY A 71 -35.602 15.307 -12.155 1.00 30.60 C ANISOU 459 CA GLY A 71 3641 4192 3790 -142 221 -177 C ATOM 460 C GLY A 71 -36.540 16.453 -12.470 1.00 29.36 C ANISOU 460 C GLY A 71 3407 4056 3690 -159 176 -201 C ATOM 461 O GLY A 71 -37.158 16.369 -13.521 1.00 27.56 O ANISOU 461 O GLY A 71 3166 3830 3474 -184 148 -211 O ATOM 462 N LEU A 72 -36.619 17.511 -11.675 1.00 28.05 N ANISOU 462 N LEU A 72 3193 3909 3557 -143 167 -208 N ATOM 463 CA LEU A 72 -37.688 18.525 -11.868 1.00 30.18 C ANISOU 463 CA LEU A 72 3390 4193 3882 -155 135 -232 C ATOM 464 C LEU A 72 -37.426 19.424 -13.071 1.00 28.39 C ANISOU 464 C LEU A 72 3142 3974 3671 -133 81 -214 C ATOM 465 O LEU A 72 -38.372 20.191 -13.505 1.00 26.71 O ANISOU 465 O LEU A 72 2874 3775 3499 -135 49 -227 O ATOM 466 CB LEU A 72 -37.882 19.299 -10.554 1.00 30.16 C ANISOU 466 CB LEU A 72 3351 4199 3907 -146 155 -247 C ATOM 467 CG LEU A 72 -38.512 18.466 -9.441 1.00 33.63 C ANISOU 467 CG LEU A 72 3805 4632 4341 -176 208 -271 C ATOM 468 CD1 LEU A 72 -38.441 19.190 -8.141 1.00 34.80 C ANISOU 468 CD1 LEU A 72 3929 4789 4503 -163 229 -282 C ATOM 469 CD2 LEU A 72 -39.946 18.157 -9.762 1.00 37.26 C ANISOU 469 CD2 LEU A 72 4230 5095 4833 -220 208 -306 C ATOM 470 N GLU A 73 -36.211 19.365 -13.640 1.00 26.47 N ANISOU 470 N GLU A 73 2940 3725 3393 -108 72 -183 N ATOM 471 CA GLU A 73 -35.885 20.139 -14.819 1.00 26.15 C ANISOU 471 CA GLU A 73 2890 3685 3358 -89 28 -164 C ATOM 472 C GLU A 73 -36.642 19.564 -16.003 1.00 25.53 C ANISOU 472 C GLU A 73 2815 3608 3274 -114 2 -168 C ATOM 473 O GLU A 73 -36.574 20.204 -17.052 1.00 27.11 O ANISOU 473 O GLU A 73 3008 3813 3479 -98 -37 -153 O ATOM 474 CB GLU A 73 -34.367 20.221 -15.107 1.00 26.66 C ANISOU 474 CB GLU A 73 2995 3745 3388 -61 30 -134 C ATOM 475 CG GLU A 73 -33.753 18.954 -15.630 1.00 26.28 C ANISOU 475 CG GLU A 73 3008 3686 3291 -65 45 -119 C ATOM 476 CD GLU A 73 -33.429 17.819 -14.662 1.00 26.57 C ANISOU 476 CD GLU A 73 3084 3718 3294 -66 94 -119 C ATOM 477 OE1 GLU A 73 -33.976 17.843 -13.494 1.00 28.19 O ANISOU 477 OE1 GLU A 73 3268 3928 3514 -75 118 -138 O ATOM 478 OE2 GLU A 73 -32.620 16.907 -15.050 1.00 25.58 O ANISOU 478 OE2 GLU A 73 3014 3580 3124 -54 113 -99 O ATOM 479 N ARG A 74 -37.278 18.413 -15.889 1.00 28.13 N ANISOU 479 N ARG A 74 3161 3935 3588 -152 26 -189 N ATOM 480 CA ARG A 74 -38.166 17.878 -16.929 1.00 31.82 C ANISOU 480 CA ARG A 74 3623 4415 4051 -187 3 -206 C ATOM 481 C ARG A 74 -39.269 18.913 -17.212 1.00 34.42 C ANISOU 481 C ARG A 74 3874 4776 4426 -181 -41 -221 C ATOM 482 O ARG A 74 -39.785 18.934 -18.371 1.00 33.99 O ANISOU 482 O ARG A 74 3804 4744 4366 -190 -83 -224 O ATOM 483 CB ARG A 74 -38.700 16.463 -16.665 1.00 34.85 C ANISOU 483 CB ARG A 74 4039 4787 4412 -240 47 -235 C ATOM 484 CG ARG A 74 -39.780 16.318 -15.600 1.00 36.07 C ANISOU 484 CG ARG A 74 4154 4951 4597 -271 78 -273 C ATOM 485 CD ARG A 74 -39.903 14.858 -15.237 1.00 41.50 C ANISOU 485 CD ARG A 74 4903 5612 5252 -317 140 -292 C ATOM 486 NE ARG A 74 -40.966 14.566 -14.275 1.00 44.47 N ANISOU 486 NE ARG A 74 5249 5992 5652 -358 178 -332 N ATOM 487 CZ ARG A 74 -40.890 14.710 -12.942 1.00 46.70 C ANISOU 487 CZ ARG A 74 5534 6263 5947 -344 217 -333 C ATOM 488 NH1 ARG A 74 -41.927 14.382 -12.155 1.00 46.99 N ANISOU 488 NH1 ARG A 74 5547 6302 6004 -388 257 -373 N ATOM 489 NH2 ARG A 74 -39.802 15.203 -12.360 1.00 51.25 N ANISOU 489 NH2 ARG A 74 6131 6829 6512 -290 218 -296 N ATOM 490 N PHE A 75 -39.625 19.759 -16.255 1.00 28.91 N ANISOU 490 N PHE A 75 3130 4084 3770 -163 -33 -230 N ATOM 491 CA PHE A 75 -40.730 20.744 -16.427 1.00 29.83 C ANISOU 491 CA PHE A 75 3171 4230 3933 -149 -69 -244 C ATOM 492 C PHE A 75 -40.166 22.086 -16.874 1.00 30.54 C ANISOU 492 C PHE A 75 3254 4311 4037 -94 -100 -210 C ATOM 493 O PHE A 75 -40.925 23.055 -16.999 1.00 29.34 O ANISOU 493 O PHE A 75 3049 4176 3923 -67 -125 -211 O ATOM 494 CB PHE A 75 -41.511 20.882 -15.133 1.00 29.36 C ANISOU 494 CB PHE A 75 3068 4176 3911 -163 -35 -275 C ATOM 495 CG PHE A 75 -42.136 19.596 -14.723 1.00 30.46 C ANISOU 495 CG PHE A 75 3217 4320 4037 -221 2 -311 C ATOM 496 CD1 PHE A 75 -43.008 18.929 -15.539 1.00 29.29 C ANISOU 496 CD1 PHE A 75 3048 4201 3879 -261 -16 -337 C ATOM 497 CD2 PHE A 75 -41.789 19.026 -13.520 1.00 34.33 C ANISOU 497 CD2 PHE A 75 3742 4784 4516 -237 59 -319 C ATOM 498 CE1 PHE A 75 -43.584 17.755 -15.143 1.00 34.96 C ANISOU 498 CE1 PHE A 75 3779 4918 4584 -323 27 -375 C ATOM 499 CE2 PHE A 75 -42.373 17.850 -13.109 1.00 36.22 C ANISOU 499 CE2 PHE A 75 4000 5019 4741 -291 103 -351 C ATOM 500 CZ PHE A 75 -43.240 17.177 -13.947 1.00 37.13 C ANISOU 500 CZ PHE A 75 4098 5158 4851 -338 91 -380 C ATOM 501 N ARG A 76 -38.843 22.142 -17.160 1.00 30.59 N ANISOU 501 N ARG A 76 3317 4291 4013 -77 -95 -179 N ATOM 502 CA ARG A 76 -38.143 23.244 -17.894 1.00 34.33 C ANISOU 502 CA ARG A 76 3802 4751 4488 -35 -121 -146 C ATOM 503 C ARG A 76 -37.952 24.511 -17.067 1.00 37.24 C ANISOU 503 C ARG A 76 4148 5104 4896 -5 -104 -144 C ATOM 504 O ARG A 76 -37.723 25.559 -17.658 1.00 39.37 O ANISOU 504 O ARG A 76 4420 5361 5177 28 -121 -122 O ATOM 505 CB ARG A 76 -38.839 23.807 -19.141 1.00 40.46 C ANISOU 505 CB ARG A 76 4555 5546 5271 -12 -173 -132 C ATOM 506 CG ARG A 76 -39.549 22.834 -20.067 1.00 46.17 C ANISOU 506 CG ARG A 76 5274 6300 5966 -42 -203 -144 C ATOM 507 CD ARG A 76 -38.879 21.508 -20.269 1.00 55.14 C ANISOU 507 CD ARG A 76 6468 7425 7055 -82 -181 -148 C ATOM 508 NE ARG A 76 -37.612 21.653 -20.947 1.00 57.04 N ANISOU 508 NE ARG A 76 6767 7640 7265 -62 -183 -113 N ATOM 509 CZ ARG A 76 -37.426 21.787 -22.261 1.00 61.64 C ANISOU 509 CZ ARG A 76 7373 8227 7820 -51 -219 -92 C ATOM 510 NH1 ARG A 76 -36.183 21.842 -22.704 1.00 60.70 N ANISOU 510 NH1 ARG A 76 7309 8080 7673 -38 -208 -64 N ATOM 511 NH2 ARG A 76 -38.433 21.851 -23.123 1.00 61.90 N ANISOU 511 NH2 ARG A 76 7374 8295 7849 -53 -264 -98 N ATOM 512 N SER A 77 -38.030 24.392 -15.768 1.00 35.95 N ANISOU 512 N SER A 77 3970 4940 4748 -20 -66 -167 N ATOM 513 CA ASER A 77 -38.010 25.476 -14.755 0.50 37.63 C ANISOU 513 CA ASER A 77 4158 5141 4998 -3 -41 -177 C ATOM 514 CA BSER A 77 -38.074 25.478 -14.740 0.50 37.41 C ANISOU 514 CA BSER A 77 4127 5113 4971 -3 -41 -179 C ATOM 515 C SER A 77 -37.539 24.815 -13.468 1.00 36.83 C ANISOU 515 C SER A 77 4071 5042 4880 -29 2 -196 C ATOM 516 O SER A 77 -37.704 23.529 -13.365 1.00 40.77 O ANISOU 516 O SER A 77 4588 5551 5351 -56 11 -204 O ATOM 517 CB ASER A 77 -39.345 25.984 -14.505 0.50 38.20 C ANISOU 517 CB ASER A 77 4172 5225 5117 5 -47 -196 C ATOM 518 CB BSER A 77 -39.460 26.021 -14.447 0.50 38.13 C ANISOU 518 CB BSER A 77 4157 5217 5112 5 -47 -199 C ATOM 519 OG ASER A 77 -40.022 24.958 -13.796 0.50 38.92 O ANISOU 519 OG ASER A 77 4246 5335 5207 -32 -28 -226 O ATOM 520 OG BSER A 77 -39.881 27.095 -15.289 0.50 38.17 O ANISOU 520 OG BSER A 77 4143 5218 5143 48 -77 -179 O ATOM 521 N LEU A 78 -36.929 25.574 -12.582 1.00 34.77 N ANISOU 521 N LEU A 78 3808 4772 4628 -21 29 -203 N ATOM 522 CA LEU A 78 -36.677 25.092 -11.214 1.00 30.85 C ANISOU 522 CA LEU A 78 3316 4286 4117 -41 69 -224 C ATOM 523 C LEU A 78 -37.110 26.196 -10.248 1.00 30.77 C ANISOU 523 C LEU A 78 3270 4270 4150 -37 93 -248 C ATOM 524 O LEU A 78 -37.067 27.389 -10.617 1.00 32.48 O ANISOU 524 O LEU A 78 3474 4469 4395 -16 86 -242 O ATOM 525 CB LEU A 78 -35.196 24.734 -11.103 1.00 32.21 C ANISOU 525 CB LEU A 78 3532 4466 4240 -37 80 -208 C ATOM 526 CG LEU A 78 -34.718 23.558 -11.958 1.00 31.77 C ANISOU 526 CG LEU A 78 3518 4412 4140 -38 66 -185 C ATOM 527 CD1 LEU A 78 -33.193 23.512 -11.954 1.00 33.22 C ANISOU 527 CD1 LEU A 78 3733 4607 4281 -25 73 -169 C ATOM 528 CD2 LEU A 78 -35.286 22.248 -11.463 1.00 30.75 C ANISOU 528 CD2 LEU A 78 3404 4286 3991 -59 87 -195 C ATOM 529 N ALA A 79 -37.375 25.819 -9.021 1.00 32.84 N ANISOU 529 N ALA A 79 3523 4543 4410 -56 126 -272 N ATOM 530 CA ALA A 79 -37.857 26.747 -7.970 1.00 33.92 C ANISOU 530 CA ALA A 79 3628 4675 4585 -58 156 -301 C ATOM 531 C ALA A 79 -36.773 27.767 -7.607 1.00 35.64 C ANISOU 531 C ALA A 79 3857 4888 4796 -52 172 -303 C ATOM 532 O ALA A 79 -35.604 27.424 -7.427 1.00 28.01 O ANISOU 532 O ALA A 79 2919 3939 3783 -58 176 -296 O ATOM 533 CB ALA A 79 -38.282 25.984 -6.767 1.00 32.62 C ANISOU 533 CB ALA A 79 3461 4524 4410 -83 191 -325 C ATOM 534 N PRO A 80 -37.148 29.056 -7.458 1.00 39.22 N ANISOU 534 N PRO A 80 4288 5319 5296 -43 186 -317 N ATOM 535 CA PRO A 80 -36.319 30.057 -6.791 1.00 37.40 C ANISOU 535 CA PRO A 80 4064 5082 5063 -51 217 -335 C ATOM 536 C PRO A 80 -35.480 29.530 -5.630 1.00 33.82 C ANISOU 536 C PRO A 80 3623 4666 4561 -77 241 -355 C ATOM 537 O PRO A 80 -34.293 29.779 -5.519 1.00 30.19 O ANISOU 537 O PRO A 80 3179 4224 4066 -86 247 -358 O ATOM 538 CB PRO A 80 -37.361 31.106 -6.349 1.00 44.40 C ANISOU 538 CB PRO A 80 4919 5940 6009 -43 243 -357 C ATOM 539 CG PRO A 80 -38.422 31.080 -7.503 1.00 43.05 C ANISOU 539 CG PRO A 80 4728 5754 5873 -9 207 -332 C ATOM 540 CD PRO A 80 -38.355 29.673 -8.059 1.00 43.77 C ANISOU 540 CD PRO A 80 4830 5872 5925 -18 172 -313 C ATOM 541 N ILE A 81 -36.096 28.792 -4.761 1.00 36.67 N ANISOU 541 N ILE A 81 3975 5042 4915 -89 256 -369 N ATOM 542 CA ILE A 81 -35.421 28.210 -3.580 1.00 37.41 C ANISOU 542 CA ILE A 81 4082 5173 4956 -106 280 -384 C ATOM 543 C ILE A 81 -34.218 27.344 -3.923 1.00 33.51 C ANISOU 543 C ILE A 81 3620 4712 4399 -97 260 -358 C ATOM 544 O ILE A 81 -33.283 27.264 -3.174 1.00 33.59 O ANISOU 544 O ILE A 81 3638 4761 4363 -102 272 -368 O ATOM 545 CB ILE A 81 -36.478 27.385 -2.834 1.00 50.33 C ANISOU 545 CB ILE A 81 5713 6811 6598 -116 299 -395 C ATOM 546 CG1 ILE A 81 -37.534 28.339 -2.288 1.00 62.11 C ANISOU 546 CG1 ILE A 81 7168 8279 8149 -125 326 -427 C ATOM 547 CG2 ILE A 81 -35.837 26.530 -1.776 1.00 52.75 C ANISOU 547 CG2 ILE A 81 6046 7155 6841 -124 320 -399 C ATOM 548 CD1 ILE A 81 -36.962 29.331 -1.307 1.00 62.07 C ANISOU 548 CD1 ILE A 81 7160 8282 8138 -140 359 -458 C ATOM 549 N TYR A 82 -34.279 26.624 -5.033 1.00 29.43 N ANISOU 549 N TYR A 82 3120 4182 3877 -82 230 -326 N ATOM 550 CA TYR A 82 -33.169 25.777 -5.486 1.00 28.53 C ANISOU 550 CA TYR A 82 3039 4094 3707 -68 214 -299 C ATOM 551 C TYR A 82 -31.953 26.662 -5.642 1.00 27.94 C ANISOU 551 C TYR A 82 2959 4039 3618 -68 210 -304 C ATOM 552 O TYR A 82 -30.879 26.339 -5.223 1.00 27.84 O ANISOU 552 O TYR A 82 2954 4069 3552 -63 214 -303 O ATOM 553 CB TYR A 82 -33.538 25.096 -6.808 1.00 28.43 C ANISOU 553 CB TYR A 82 3044 4056 3702 -57 184 -269 C ATOM 554 CG TYR A 82 -32.513 24.138 -7.332 1.00 27.79 C ANISOU 554 CG TYR A 82 3000 3992 3565 -40 173 -240 C ATOM 555 CD1 TYR A 82 -32.390 22.877 -6.761 1.00 26.65 C ANISOU 555 CD1 TYR A 82 2887 3863 3376 -33 191 -230 C ATOM 556 CD2 TYR A 82 -31.687 24.444 -8.397 1.00 26.06 C ANISOU 556 CD2 TYR A 82 2791 3772 3338 -29 150 -221 C ATOM 557 CE1 TYR A 82 -31.481 21.947 -7.196 1.00 26.88 C ANISOU 557 CE1 TYR A 82 2954 3905 3353 -11 187 -201 C ATOM 558 CE2 TYR A 82 -30.769 23.510 -8.830 1.00 25.02 C ANISOU 558 CE2 TYR A 82 2692 3656 3156 -11 144 -195 C ATOM 559 CZ TYR A 82 -30.656 22.256 -8.262 1.00 24.86 C ANISOU 559 CZ TYR A 82 2702 3651 3092 0 162 -184 C ATOM 560 OH TYR A 82 -29.799 21.309 -8.706 1.00 24.70 O ANISOU 560 OH TYR A 82 2718 3641 3023 24 161 -157 O ATOM 561 N TYR A 83 -32.112 27.776 -6.358 1.00 27.74 N ANISOU 561 N TYR A 83 2921 3981 3636 -71 204 -308 N ATOM 562 CA TYR A 83 -31.010 28.689 -6.701 1.00 28.15 C ANISOU 562 CA TYR A 83 2974 4040 3680 -78 207 -315 C ATOM 563 C TYR A 83 -30.547 29.462 -5.458 1.00 28.51 C ANISOU 563 C TYR A 83 3000 4116 3717 -105 241 -357 C ATOM 564 O TYR A 83 -29.407 29.878 -5.420 1.00 29.63 O ANISOU 564 O TYR A 83 3139 4289 3829 -119 248 -371 O ATOM 565 CB TYR A 83 -31.428 29.721 -7.756 1.00 29.62 C ANISOU 565 CB TYR A 83 3162 4174 3917 -73 200 -306 C ATOM 566 CG TYR A 83 -31.884 29.118 -9.059 1.00 29.54 C ANISOU 566 CG TYR A 83 3169 4139 3914 -49 163 -268 C ATOM 567 CD1 TYR A 83 -30.992 28.580 -9.953 1.00 31.29 C ANISOU 567 CD1 TYR A 83 3416 4372 4100 -41 143 -242 C ATOM 568 CD2 TYR A 83 -33.229 28.990 -9.364 1.00 30.25 C ANISOU 568 CD2 TYR A 83 3247 4203 4043 -37 149 -260 C ATOM 569 CE1 TYR A 83 -31.417 27.997 -11.146 1.00 30.16 C ANISOU 569 CE1 TYR A 83 3291 4208 3958 -24 111 -210 C ATOM 570 CE2 TYR A 83 -33.672 28.462 -10.569 1.00 31.95 C ANISOU 570 CE2 TYR A 83 3474 4405 4260 -20 114 -230 C ATOM 571 CZ TYR A 83 -32.763 27.946 -11.461 1.00 32.41 C ANISOU 571 CZ TYR A 83 3563 4470 4280 -15 95 -205 C ATOM 572 OH TYR A 83 -33.092 27.366 -12.664 1.00 32.26 O ANISOU 572 OH TYR A 83 3561 4441 4255 -3 61 -177 O ATOM 573 N ARG A 84 -31.469 29.873 -4.600 1.00 30.33 N ANISOU 573 N ARG A 84 3213 4329 3978 -117 265 -383 N ATOM 574 CA ARG A 84 -31.151 30.817 -3.513 1.00 30.97 C ANISOU 574 CA ARG A 84 3278 4429 4059 -148 302 -429 C ATOM 575 C ARG A 84 -30.034 30.267 -2.588 1.00 31.04 C ANISOU 575 C ARG A 84 3282 4515 3995 -159 306 -444 C ATOM 576 O ARG A 84 -30.112 29.086 -2.154 1.00 30.47 O ANISOU 576 O ARG A 84 3219 4474 3884 -139 295 -426 O ATOM 577 CB ARG A 84 -32.433 31.089 -2.748 1.00 34.20 C ANISOU 577 CB ARG A 84 3674 4809 4511 -153 327 -449 C ATOM 578 CG ARG A 84 -32.304 32.112 -1.626 1.00 43.34 C ANISOU 578 CG ARG A 84 4818 5974 5674 -188 372 -499 C ATOM 579 CD ARG A 84 -33.748 32.452 -1.171 1.00 51.21 C ANISOU 579 CD ARG A 84 5802 6926 6728 -185 397 -512 C ATOM 580 NE ARG A 84 -34.398 33.023 -2.389 1.00 57.03 N ANISOU 580 NE ARG A 84 6541 7603 7524 -158 384 -487 N ATOM 581 CZ ARG A 84 -35.681 32.885 -2.763 1.00 61.09 C ANISOU 581 CZ ARG A 84 7041 8083 8087 -131 375 -471 C ATOM 582 NH1 ARG A 84 -36.535 32.210 -2.012 1.00 55.47 N ANISOU 582 NH1 ARG A 84 6311 7383 7378 -135 383 -481 N ATOM 583 NH2 ARG A 84 -36.097 33.444 -3.892 1.00 61.07 N ANISOU 583 NH2 ARG A 84 7040 8038 8126 -101 359 -445 N ATOM 584 N GLY A 85 -29.108 31.156 -2.262 1.00 29.84 N ANISOU 584 N GLY A 85 3117 4393 3826 -190 325 -480 N ATOM 585 CA GLY A 85 -27.957 30.967 -1.359 1.00 32.72 C ANISOU 585 CA GLY A 85 3464 4844 4122 -206 329 -506 C ATOM 586 C GLY A 85 -26.836 30.166 -1.948 1.00 29.48 C ANISOU 586 C GLY A 85 3056 4486 3659 -181 298 -478 C ATOM 587 O GLY A 85 -25.890 29.984 -1.233 1.00 32.38 O ANISOU 587 O GLY A 85 3402 4932 3965 -187 298 -498 O ATOM 588 N ALA A 86 -26.869 29.748 -3.254 1.00 28.29 N ANISOU 588 N ALA A 86 2927 4295 3526 -154 273 -435 N ATOM 589 CA ALA A 86 -25.763 29.050 -3.920 1.00 28.86 C ANISOU 589 CA ALA A 86 3002 4410 3551 -130 248 -409 C ATOM 590 C ALA A 86 -24.538 29.958 -3.963 1.00 29.20 C ANISOU 590 C ALA A 86 3019 4499 3576 -166 261 -447 C ATOM 591 O ALA A 86 -24.697 31.175 -4.239 1.00 31.22 O ANISOU 591 O ALA A 86 3274 4709 3876 -204 286 -475 O ATOM 592 CB ALA A 86 -26.200 28.577 -5.304 1.00 27.86 C ANISOU 592 CB ALA A 86 2908 4222 3456 -103 225 -362 C ATOM 593 N SER A 87 -23.367 29.386 -3.678 1.00 29.14 N ANISOU 593 N SER A 87 2990 4579 3502 -152 249 -449 N ATOM 594 CA SER A 87 -22.046 30.023 -3.888 1.00 32.57 C ANISOU 594 CA SER A 87 3392 5072 3909 -183 257 -483 C ATOM 595 C SER A 87 -21.563 29.764 -5.297 1.00 32.00 C ANISOU 595 C SER A 87 3340 4973 3846 -164 242 -448 C ATOM 596 O SER A 87 -20.755 30.578 -5.824 1.00 31.09 O ANISOU 596 O SER A 87 3210 4866 3735 -201 258 -476 O ATOM 597 CB SER A 87 -21.050 29.551 -2.869 1.00 35.58 C ANISOU 597 CB SER A 87 3732 5574 4213 -174 249 -504 C ATOM 598 OG SER A 87 -21.449 29.978 -1.595 1.00 35.08 O ANISOU 598 OG SER A 87 3651 5535 4139 -202 268 -544 O ATOM 599 N GLY A 88 -21.959 28.601 -5.813 1.00 31.34 N ANISOU 599 N GLY A 88 3287 4864 3756 -111 216 -393 N ATOM 600 CA GLY A 88 -21.509 28.105 -7.118 1.00 30.52 C ANISOU 600 CA GLY A 88 3206 4739 3651 -85 199 -355 C ATOM 601 C GLY A 88 -22.593 27.335 -7.845 1.00 28.90 C ANISOU 601 C GLY A 88 3047 4456 3475 -52 182 -305 C ATOM 602 O GLY A 88 -23.561 26.849 -7.229 1.00 26.16 O ANISOU 602 O GLY A 88 2712 4089 3136 -39 180 -295 O ATOM 603 N ALA A 89 -22.387 27.144 -9.164 1.00 28.17 N ANISOU 603 N ALA A 89 2982 4326 3394 -41 170 -275 N ATOM 604 CA ALA A 89 -23.337 26.404 -10.004 1.00 27.35 C ANISOU 604 CA ALA A 89 2922 4156 3313 -16 152 -232 C ATOM 605 C ALA A 89 -22.529 25.689 -11.079 1.00 28.92 C ANISOU 605 C ALA A 89 3143 4360 3483 9 141 -201 C ATOM 606 O ALA A 89 -21.635 26.366 -11.631 1.00 29.98 O ANISOU 606 O ALA A 89 3266 4509 3615 -9 148 -215 O ATOM 607 CB ALA A 89 -24.318 27.396 -10.606 1.00 28.56 C ANISOU 607 CB ALA A 89 3088 4234 3529 -40 153 -237 C ATOM 608 N LEU A 90 -22.831 24.431 -11.337 1.00 26.24 N ANISOU 608 N LEU A 90 2836 4008 3123 45 130 -165 N ATOM 609 CA LEU A 90 -22.306 23.692 -12.504 1.00 27.37 C ANISOU 609 CA LEU A 90 3013 4139 3246 68 122 -132 C ATOM 610 C LEU A 90 -23.438 23.589 -13.520 1.00 27.89 C ANISOU 610 C LEU A 90 3117 4127 3350 60 107 -111 C ATOM 611 O LEU A 90 -24.458 23.008 -13.214 1.00 24.54 O ANISOU 611 O LEU A 90 2708 3677 2936 64 103 -103 O ATOM 612 CB LEU A 90 -21.821 22.291 -12.106 1.00 28.08 C ANISOU 612 CB LEU A 90 3119 4267 3281 117 127 -107 C ATOM 613 CG LEU A 90 -20.386 22.206 -11.559 1.00 31.47 C ANISOU 613 CG LEU A 90 3512 4786 3658 141 135 -117 C ATOM 614 CD1 LEU A 90 -20.189 23.002 -10.302 1.00 32.23 C ANISOU 614 CD1 LEU A 90 3555 4940 3748 121 141 -157 C ATOM 615 CD2 LEU A 90 -20.032 20.746 -11.400 1.00 32.15 C ANISOU 615 CD2 LEU A 90 3629 4892 3692 202 142 -80 C ATOM 616 N VAL A 91 -23.250 24.206 -14.681 1.00 26.49 N ANISOU 616 N VAL A 91 2954 3918 3192 46 100 -105 N ATOM 617 CA VAL A 91 -24.239 24.124 -15.786 1.00 24.86 C ANISOU 617 CA VAL A 91 2782 3647 3013 41 80 -84 C ATOM 618 C VAL A 91 -23.736 23.073 -16.752 1.00 24.38 C ANISOU 618 C VAL A 91 2762 3582 2918 62 76 -54 C ATOM 619 O VAL A 91 -22.628 23.267 -17.253 1.00 25.41 O ANISOU 619 O VAL A 91 2894 3732 3028 65 85 -53 O ATOM 620 CB VAL A 91 -24.400 25.483 -16.492 1.00 26.66 C ANISOU 620 CB VAL A 91 3009 3839 3279 19 77 -91 C ATOM 621 CG1 VAL A 91 -25.363 25.322 -17.639 1.00 28.52 C ANISOU 621 CG1 VAL A 91 3278 4024 3533 23 51 -65 C ATOM 622 CG2 VAL A 91 -24.897 26.561 -15.557 1.00 28.67 C ANISOU 622 CG2 VAL A 91 3230 4092 3571 0 89 -121 C ATOM 623 N VAL A 92 -24.400 21.913 -16.828 1.00 23.27 N ANISOU 623 N VAL A 92 2651 3423 2764 74 71 -37 N ATOM 624 CA VAL A 92 -23.910 20.732 -17.529 1.00 23.39 C ANISOU 624 CA VAL A 92 2710 3434 2741 96 78 -12 C ATOM 625 C VAL A 92 -24.651 20.648 -18.857 1.00 23.81 C ANISOU 625 C VAL A 92 2799 3438 2808 79 57 0 C ATOM 626 O VAL A 92 -25.900 20.821 -18.927 1.00 23.23 O ANISOU 626 O VAL A 92 2722 3338 2765 60 39 -5 O ATOM 627 CB VAL A 92 -24.130 19.457 -16.705 1.00 25.85 C ANISOU 627 CB VAL A 92 3042 3755 3025 118 97 -4 C ATOM 628 CG1 VAL A 92 -23.536 18.210 -17.381 1.00 27.36 C ANISOU 628 CG1 VAL A 92 3285 3936 3172 145 114 22 C ATOM 629 CG2 VAL A 92 -23.565 19.677 -15.288 1.00 26.96 C ANISOU 629 CG2 VAL A 92 3142 3951 3150 136 112 -18 C ATOM 630 N TYR A 93 -23.916 20.358 -19.901 1.00 22.79 N ANISOU 630 N TYR A 93 2702 3300 2655 86 60 17 N ATOM 631 CA TYR A 93 -24.536 19.914 -21.168 1.00 23.64 C ANISOU 631 CA TYR A 93 2853 3367 2759 73 43 32 C ATOM 632 C TYR A 93 -23.892 18.567 -21.540 1.00 24.79 C ANISOU 632 C TYR A 93 3047 3511 2859 92 68 49 C ATOM 633 O TYR A 93 -22.836 18.157 -21.017 1.00 23.87 O ANISOU 633 O TYR A 93 2928 3425 2716 123 94 54 O ATOM 634 CB TYR A 93 -24.422 20.954 -22.269 1.00 23.77 C ANISOU 634 CB TYR A 93 2874 3365 2789 60 24 37 C ATOM 635 CG TYR A 93 -23.019 21.268 -22.715 1.00 22.83 C ANISOU 635 CG TYR A 93 2762 3260 2649 69 43 42 C ATOM 636 CD1 TYR A 93 -22.248 22.187 -22.034 1.00 24.38 C ANISOU 636 CD1 TYR A 93 2917 3487 2857 67 58 25 C ATOM 637 CD2 TYR A 93 -22.456 20.632 -23.822 1.00 25.09 C ANISOU 637 CD2 TYR A 93 3095 3533 2904 74 50 60 C ATOM 638 CE1 TYR A 93 -20.968 22.490 -22.441 1.00 23.99 C ANISOU 638 CE1 TYR A 93 2868 3457 2790 69 79 23 C ATOM 639 CE2 TYR A 93 -21.165 20.958 -24.279 1.00 25.06 C ANISOU 639 CE2 TYR A 93 3094 3544 2883 79 71 62 C ATOM 640 CZ TYR A 93 -20.419 21.874 -23.567 1.00 25.43 C ANISOU 640 CZ TYR A 93 3094 3625 2942 76 86 43 C ATOM 641 OH TYR A 93 -19.157 22.214 -23.997 1.00 24.81 O ANISOU 641 OH TYR A 93 3011 3566 2847 75 110 38 O ATOM 642 N ASP A 94 -24.393 17.959 -22.586 1.00 26.12 N ANISOU 642 N ASP A 94 3261 3646 3017 77 60 57 N ATOM 643 CA ASP A 94 -23.911 16.673 -23.137 1.00 25.08 C ANISOU 643 CA ASP A 94 3187 3498 2843 89 88 72 C ATOM 644 C ASP A 94 -23.218 17.024 -24.483 1.00 24.64 C ANISOU 644 C ASP A 94 3156 3431 2774 86 81 84 C ATOM 645 O ASP A 94 -23.946 17.512 -25.417 1.00 23.35 O ANISOU 645 O ASP A 94 3001 3247 2622 57 50 83 O ATOM 646 CB ASP A 94 -25.161 15.818 -23.336 1.00 27.00 C ANISOU 646 CB ASP A 94 3461 3710 3085 60 86 64 C ATOM 647 CG ASP A 94 -24.976 14.465 -24.007 1.00 25.38 C ANISOU 647 CG ASP A 94 3327 3476 2841 59 118 73 C ATOM 648 OD1 ASP A 94 -23.840 14.157 -24.475 1.00 26.55 O ANISOU 648 OD1 ASP A 94 3504 3624 2960 87 141 90 O ATOM 649 OD2 ASP A 94 -25.937 13.724 -23.982 1.00 28.39 O ANISOU 649 OD2 ASP A 94 3732 3835 3220 31 126 60 O ATOM 650 N ILE A 95 -21.941 16.672 -24.640 1.00 23.96 N ANISOU 650 N ILE A 95 3084 3359 2658 115 111 96 N ATOM 651 CA ILE A 95 -21.172 17.018 -25.865 1.00 25.05 C ANISOU 651 CA ILE A 95 3245 3488 2782 111 112 105 C ATOM 652 C ILE A 95 -21.755 16.262 -27.055 1.00 24.79 C ANISOU 652 C ILE A 95 3276 3413 2728 88 108 112 C ATOM 653 O ILE A 95 -21.483 16.699 -28.166 1.00 27.03 O ANISOU 653 O ILE A 95 3582 3684 3004 75 99 118 O ATOM 654 CB ILE A 95 -19.664 16.746 -25.653 1.00 29.07 C ANISOU 654 CB ILE A 95 3747 4031 3265 149 148 112 C ATOM 655 CG1 ILE A 95 -19.355 15.274 -25.366 1.00 30.60 C ANISOU 655 CG1 ILE A 95 3980 4220 3423 186 186 126 C ATOM 656 CG2 ILE A 95 -19.093 17.683 -24.589 1.00 28.64 C ANISOU 656 CG2 ILE A 95 3622 4028 3229 160 146 97 C ATOM 657 CD1 ILE A 95 -18.655 14.586 -26.498 1.00 35.58 C ANISOU 657 CD1 ILE A 95 4667 4829 4022 196 214 140 C ATOM 658 N THR A 96 -22.506 15.163 -26.822 1.00 24.76 N ANISOU 658 N THR A 96 3303 3390 2713 81 120 109 N ATOM 659 CA THR A 96 -23.178 14.388 -27.903 1.00 24.32 C ANISOU 659 CA THR A 96 3306 3298 2634 48 118 106 C ATOM 660 C THR A 96 -24.535 14.996 -28.316 1.00 27.05 C ANISOU 660 C THR A 96 3633 3641 3003 6 68 92 C ATOM 661 O THR A 96 -25.226 14.397 -29.171 1.00 26.85 O ANISOU 661 O THR A 96 3647 3598 2957 -27 60 83 O ATOM 662 CB THR A 96 -23.357 12.912 -27.505 1.00 26.28 C ANISOU 662 CB THR A 96 3603 3523 2858 52 163 104 C ATOM 663 OG1 THR A 96 -24.455 12.736 -26.603 1.00 26.87 O ANISOU 663 OG1 THR A 96 3656 3599 2954 33 156 87 O ATOM 664 CG2 THR A 96 -22.041 12.325 -27.035 1.00 26.85 C ANISOU 664 CG2 THR A 96 3691 3604 2907 107 212 123 C ATOM 665 N ASN A 97 -24.961 16.114 -27.735 1.00 25.58 N ANISOU 665 N ASN A 97 3388 3476 2855 8 35 87 N ATOM 666 CA ASN A 97 -26.331 16.679 -27.903 1.00 26.02 C ANISOU 666 CA ASN A 97 3414 3536 2935 -19 -10 74 C ATOM 667 C ASN A 97 -26.223 18.211 -28.072 1.00 26.82 C ANISOU 667 C ASN A 97 3478 3646 3064 -6 -41 83 C ATOM 668 O ASN A 97 -26.188 18.987 -27.070 1.00 26.19 O ANISOU 668 O ASN A 97 3350 3580 3018 7 -41 78 O ATOM 669 CB ASN A 97 -27.230 16.290 -26.732 1.00 28.36 C ANISOU 669 CB ASN A 97 3679 3841 3255 -29 -5 54 C ATOM 670 CG ASN A 97 -28.659 16.801 -26.827 1.00 31.52 C ANISOU 670 CG ASN A 97 4039 4253 3681 -54 -50 38 C ATOM 671 OD1 ASN A 97 -28.987 17.597 -27.666 1.00 31.95 O ANISOU 671 OD1 ASN A 97 4085 4313 3740 -56 -89 45 O ATOM 672 ND2 ASN A 97 -29.536 16.224 -26.026 1.00 35.19 N ANISOU 672 ND2 ASN A 97 4487 4723 4160 -74 -41 16 N ATOM 673 N SER A 98 -26.227 18.715 -29.302 1.00 27.05 N ANISOU 673 N SER A 98 3532 3666 3078 -12 -65 96 N ATOM 674 CA SER A 98 -26.116 20.140 -29.601 1.00 26.66 C ANISOU 674 CA SER A 98 3464 3615 3049 0 -86 109 C ATOM 675 C SER A 98 -27.237 20.923 -28.935 1.00 26.41 C ANISOU 675 C SER A 98 3379 3595 3059 4 -117 100 C ATOM 676 O SER A 98 -26.959 22.016 -28.442 1.00 28.22 O ANISOU 676 O SER A 98 3581 3822 3318 20 -112 103 O ATOM 677 CB SER A 98 -26.158 20.318 -31.100 1.00 30.39 C ANISOU 677 CB SER A 98 3982 4074 3489 -6 -108 126 C ATOM 678 OG SER A 98 -26.226 21.664 -31.463 1.00 31.63 O ANISOU 678 OG SER A 98 4131 4222 3662 9 -127 141 O ATOM 679 N GLU A 99 -28.456 20.393 -28.876 1.00 26.20 N ANISOU 679 N GLU A 99 3336 3581 3036 -12 -143 86 N ATOM 680 CA GLU A 99 -29.601 21.072 -28.243 1.00 28.48 C ANISOU 680 CA GLU A 99 3569 3886 3365 -6 -171 76 C ATOM 681 C GLU A 99 -29.267 21.340 -26.760 1.00 27.46 C ANISOU 681 C GLU A 99 3401 3759 3271 2 -141 63 C ATOM 682 O GLU A 99 -29.694 22.378 -26.267 1.00 27.09 O ANISOU 682 O GLU A 99 3316 3714 3262 17 -151 62 O ATOM 683 CB GLU A 99 -30.885 20.247 -28.429 1.00 35.35 C ANISOU 683 CB GLU A 99 4425 4777 4227 -34 -198 55 C ATOM 684 CG GLU A 99 -32.094 20.853 -27.766 1.00 42.40 C ANISOU 684 CG GLU A 99 5255 5693 5162 -28 -224 41 C ATOM 685 CD GLU A 99 -32.477 22.276 -28.143 1.00 49.90 C ANISOU 685 CD GLU A 99 6180 6644 6134 7 -258 61 C ATOM 686 OE1 GLU A 99 -32.136 22.742 -29.291 1.00 47.96 O ANISOU 686 OE1 GLU A 99 5971 6389 5861 22 -277 87 O ATOM 687 OE2 GLU A 99 -33.161 22.911 -27.277 0.80 57.00 O ANISOU 687 OE2 GLU A 99 7027 7552 7077 21 -263 51 O ATOM 688 N SER A 100 -28.566 20.431 -26.079 1.00 25.13 N ANISOU 688 N SER A 100 3119 3465 2962 -1 -103 55 N ATOM 689 CA SER A 100 -28.246 20.536 -24.642 1.00 25.22 C ANISOU 689 CA SER A 100 3096 3488 2997 8 -75 43 C ATOM 690 C SER A 100 -27.342 21.730 -24.410 1.00 25.14 C ANISOU 690 C SER A 100 3069 3477 3003 25 -64 49 C ATOM 691 O SER A 100 -27.482 22.408 -23.356 1.00 25.20 O ANISOU 691 O SER A 100 3035 3495 3042 29 -56 35 O ATOM 692 CB SER A 100 -27.665 19.243 -24.061 1.00 28.23 C ANISOU 692 CB SER A 100 3502 3872 3350 8 -37 39 C ATOM 693 OG SER A 100 -26.326 19.100 -24.440 1.00 29.74 O ANISOU 693 OG SER A 100 3722 4063 3513 25 -13 54 O ATOM 694 N LEU A 101 -26.448 22.030 -25.352 1.00 24.63 N ANISOU 694 N LEU A 101 3038 3401 2917 30 -59 65 N ATOM 695 CA LEU A 101 -25.561 23.209 -25.205 1.00 26.05 C ANISOU 695 CA LEU A 101 3206 3580 3112 37 -41 66 C ATOM 696 C LEU A 101 -26.398 24.507 -25.403 1.00 27.41 C ANISOU 696 C LEU A 101 3363 3732 3319 41 -64 69 C ATOM 697 O LEU A 101 -26.257 25.489 -24.668 1.00 27.24 O ANISOU 697 O LEU A 101 3313 3709 3327 42 -48 58 O ATOM 698 CB LEU A 101 -24.403 23.142 -26.203 1.00 26.86 C ANISOU 698 CB LEU A 101 3350 3673 3180 37 -24 80 C ATOM 699 CG LEU A 101 -23.512 24.386 -26.176 1.00 28.89 C ANISOU 699 CG LEU A 101 3599 3926 3451 34 0 76 C ATOM 700 CD1 LEU A 101 -22.918 24.636 -24.795 1.00 26.76 C ANISOU 700 CD1 LEU A 101 3280 3690 3197 32 26 50 C ATOM 701 CD2 LEU A 101 -22.416 24.331 -27.202 1.00 31.89 C ANISOU 701 CD2 LEU A 101 4019 4297 3800 31 19 87 C ATOM 702 N LYS A 102 -27.314 24.518 -26.353 1.00 28.82 N ANISOU 702 N LYS A 102 3559 3898 3492 45 -99 85 N ATOM 703 CA LYS A 102 -28.216 25.698 -26.566 1.00 30.35 C ANISOU 703 CA LYS A 102 3739 4076 3716 62 -123 94 C ATOM 704 C LYS A 102 -28.989 25.954 -25.291 1.00 31.05 C ANISOU 704 C LYS A 102 3773 4177 3847 64 -122 72 C ATOM 705 O LYS A 102 -29.058 27.048 -24.864 1.00 30.88 O ANISOU 705 O LYS A 102 3734 4140 3856 75 -109 70 O ATOM 706 CB LYS A 102 -29.253 25.403 -27.647 1.00 34.73 C ANISOU 706 CB LYS A 102 4308 4635 4252 69 -170 110 C ATOM 707 CG LYS A 102 -28.668 25.376 -29.044 1.00 45.04 C ANISOU 707 CG LYS A 102 5673 5925 5516 70 -176 135 C ATOM 708 CD LYS A 102 -29.751 25.080 -30.099 1.00 52.06 C ANISOU 708 CD LYS A 102 6571 6829 6379 77 -227 148 C ATOM 709 CE LYS A 102 -29.181 24.521 -31.394 1.00 60.39 C ANISOU 709 CE LYS A 102 7686 7877 7380 65 -231 164 C ATOM 710 NZ LYS A 102 -27.926 25.233 -31.748 1.00 60.82 N ANISOU 710 NZ LYS A 102 7783 7897 7427 72 -194 181 N ATOM 711 N LYS A 103 -29.491 24.912 -24.672 1.00 29.54 N ANISOU 711 N LYS A 103 3560 4010 3654 50 -127 55 N ATOM 712 CA LYS A 103 -30.312 25.071 -23.444 1.00 29.34 C ANISOU 712 CA LYS A 103 3483 3998 3667 49 -123 33 C ATOM 713 C LYS A 103 -29.450 25.464 -22.230 1.00 31.51 C ANISOU 713 C LYS A 103 3739 4276 3956 45 -83 15 C ATOM 714 O LYS A 103 -29.997 26.122 -21.320 1.00 29.62 O ANISOU 714 O LYS A 103 3463 4037 3753 48 -75 0 O ATOM 715 CB LYS A 103 -30.984 23.744 -23.157 1.00 32.79 C ANISOU 715 CB LYS A 103 3911 4455 4091 30 -131 18 C ATOM 716 CG LYS A 103 -32.120 23.371 -24.144 1.00 38.75 C ANISOU 716 CG LYS A 103 4666 5220 4836 24 -173 21 C ATOM 717 CD LYS A 103 -33.075 24.500 -24.396 1.00 43.50 C ANISOU 717 CD LYS A 103 5233 5824 5469 50 -204 28 C ATOM 718 CE LYS A 103 -33.805 24.969 -23.162 1.00 49.29 C ANISOU 718 CE LYS A 103 5913 6565 6251 54 -194 7 C ATOM 719 NZ LYS A 103 -34.978 25.858 -23.445 1.00 54.81 N ANISOU 719 NZ LYS A 103 6573 7273 6980 84 -227 12 N ATOM 720 N ALA A 104 -28.145 25.108 -22.246 1.00 27.66 N ANISOU 720 N ALA A 104 3275 3795 3438 39 -57 17 N ATOM 721 CA ALA A 104 -27.205 25.547 -21.186 1.00 25.33 C ANISOU 721 CA ALA A 104 2958 3517 3149 34 -22 -1 C ATOM 722 C ALA A 104 -27.325 27.075 -21.082 1.00 24.53 C ANISOU 722 C ALA A 104 2844 3392 3084 35 -12 -8 C ATOM 723 O ALA A 104 -27.295 27.617 -19.982 1.00 25.47 O ANISOU 723 O ALA A 104 2930 3520 3225 27 9 -32 O ATOM 724 CB ALA A 104 -25.772 25.118 -21.482 1.00 24.78 C ANISOU 724 CB ALA A 104 2910 3462 3040 33 0 2 C ATOM 725 N GLN A 105 -27.412 27.793 -22.181 1.00 27.76 N ANISOU 725 N GLN A 105 3283 3767 3495 44 -22 12 N ATOM 726 CA GLN A 105 -27.465 29.285 -22.134 1.00 30.16 C ANISOU 726 CA GLN A 105 3588 4038 3832 48 -1 10 C ATOM 727 C GLN A 105 -28.767 29.749 -21.447 1.00 30.74 C ANISOU 727 C GLN A 105 3626 4103 3947 63 -12 1 C ATOM 728 O GLN A 105 -28.751 30.715 -20.670 1.00 33.09 O ANISOU 728 O GLN A 105 3908 4387 4275 58 18 -17 O ATOM 729 CB GLN A 105 -27.334 29.841 -23.543 1.00 32.97 C ANISOU 729 CB GLN A 105 3994 4356 4174 62 -9 41 C ATOM 730 CG GLN A 105 -27.381 31.352 -23.603 1.00 36.02 C ANISOU 730 CG GLN A 105 4398 4696 4590 70 20 43 C ATOM 731 CD GLN A 105 -26.747 31.886 -24.853 1.00 39.36 C ANISOU 731 CD GLN A 105 4881 5083 4990 74 33 69 C ATOM 732 OE1 GLN A 105 -26.920 31.296 -25.908 1.00 43.43 O ANISOU 732 OE1 GLN A 105 5424 5600 5475 89 0 97 O ATOM 733 NE2 GLN A 105 -26.005 32.986 -24.733 1.00 41.84 N ANISOU 733 NE2 GLN A 105 5217 5363 5315 57 85 57 N ATOM 734 N THR A 106 -29.889 29.073 -21.723 1.00 31.91 N ANISOU 734 N THR A 106 3762 4264 4098 78 -52 12 N ATOM 735 CA THR A 106 -31.177 29.313 -21.005 1.00 33.26 C ANISOU 735 CA THR A 106 3888 4439 4307 90 -63 0 C ATOM 736 C THR A 106 -30.992 29.111 -19.515 1.00 32.75 C ANISOU 736 C THR A 106 3789 4396 4257 68 -34 -33 C ATOM 737 O THR A 106 -31.410 30.001 -18.722 1.00 30.84 O ANISOU 737 O THR A 106 3523 4141 4053 72 -13 -50 O ATOM 738 CB THR A 106 -32.280 28.353 -21.474 1.00 36.81 C ANISOU 738 CB THR A 106 4323 4913 4749 96 -108 7 C ATOM 739 OG1 THR A 106 -32.236 28.582 -22.870 1.00 37.54 O ANISOU 739 OG1 THR A 106 4453 4991 4819 115 -134 39 O ATOM 740 CG2 THR A 106 -33.639 28.640 -20.866 1.00 41.05 C ANISOU 740 CG2 THR A 106 4809 5459 5326 110 -120 -5 C ATOM 741 N TRP A 107 -30.326 28.022 -19.091 1.00 29.81 N ANISOU 741 N TRP A 107 3418 4054 3853 47 -27 -43 N ATOM 742 CA TRP A 107 -30.139 27.783 -17.638 1.00 30.22 C ANISOU 742 CA TRP A 107 3440 4132 3910 31 0 -74 C ATOM 743 C TRP A 107 -29.250 28.884 -17.011 1.00 31.32 C ANISOU 743 C TRP A 107 3573 4266 4058 19 37 -94 C ATOM 744 O TRP A 107 -29.485 29.311 -15.833 1.00 35.09 O ANISOU 744 O TRP A 107 4020 4753 4558 8 60 -122 O ATOM 745 CB TRP A 107 -29.586 26.390 -17.399 1.00 30.33 C ANISOU 745 CB TRP A 107 3464 4176 3881 23 1 -73 C ATOM 746 CG TRP A 107 -30.608 25.355 -17.682 1.00 27.77 C ANISOU 746 CG TRP A 107 3142 3854 3553 23 -22 -66 C ATOM 747 CD1 TRP A 107 -30.619 24.464 -18.706 1.00 28.29 C ANISOU 747 CD1 TRP A 107 3239 3917 3590 22 -42 -48 C ATOM 748 CD2 TRP A 107 -31.762 25.089 -16.888 1.00 29.87 C ANISOU 748 CD2 TRP A 107 3377 4127 3845 16 -22 -85 C ATOM 749 NE1 TRP A 107 -31.715 23.665 -18.631 1.00 29.86 N ANISOU 749 NE1 TRP A 107 3429 4121 3793 12 -54 -56 N ATOM 750 CE2 TRP A 107 -32.445 24.024 -17.522 1.00 30.90 C ANISOU 750 CE2 TRP A 107 3521 4260 3960 8 -43 -78 C ATOM 751 CE3 TRP A 107 -32.309 25.680 -15.742 1.00 30.97 C ANISOU 751 CE3 TRP A 107 3478 4269 4018 12 -4 -109 C ATOM 752 CZ2 TRP A 107 -33.629 23.503 -17.005 1.00 31.99 C ANISOU 752 CZ2 TRP A 107 3631 4406 4115 -6 -43 -97 C ATOM 753 CZ3 TRP A 107 -33.456 25.134 -15.202 1.00 32.14 C ANISOU 753 CZ3 TRP A 107 3601 4425 4183 2 -5 -125 C ATOM 754 CH2 TRP A 107 -34.122 24.084 -15.857 1.00 31.13 C ANISOU 754 CH2 TRP A 107 3484 4301 4041 -7 -25 -119 C ATOM 755 N ILE A 108 -28.262 29.364 -17.749 1.00 32.53 N ANISOU 755 N ILE A 108 3754 4407 4195 15 48 -85 N ATOM 756 CA ILE A 108 -27.365 30.453 -17.254 1.00 33.39 C ANISOU 756 CA ILE A 108 3860 4513 4312 -6 90 -110 C ATOM 757 C ILE A 108 -28.246 31.709 -17.021 1.00 37.23 C ANISOU 757 C ILE A 108 4342 4955 4848 0 107 -118 C ATOM 758 O ILE A 108 -28.168 32.275 -15.936 1.00 37.48 O ANISOU 758 O ILE A 108 4350 4994 4897 -19 138 -152 O ATOM 759 CB ILE A 108 -26.179 30.644 -18.223 1.00 33.40 C ANISOU 759 CB ILE A 108 3896 4508 4286 -16 102 -100 C ATOM 760 CG1 ILE A 108 -25.195 29.426 -18.202 1.00 27.09 C ANISOU 760 CG1 ILE A 108 3092 3760 3438 -19 95 -99 C ATOM 761 CG2 ILE A 108 -25.485 31.955 -17.900 1.00 35.76 C ANISOU 761 CG2 ILE A 108 4196 4790 4599 -44 150 -129 C ATOM 762 CD1 ILE A 108 -24.247 29.359 -19.405 1.00 27.12 C ANISOU 762 CD1 ILE A 108 3133 3756 3414 -21 99 -80 C ATOM 763 N LYS A 109 -29.101 32.099 -17.956 1.00 40.74 N ANISOU 763 N LYS A 109 4808 5359 5312 30 86 -88 N ATOM 764 CA LYS A 109 -30.030 33.248 -17.728 1.00 44.81 C ANISOU 764 CA LYS A 109 5318 5832 5874 50 102 -90 C ATOM 765 C LYS A 109 -30.964 32.964 -16.539 1.00 42.75 C ANISOU 765 C LYS A 109 5009 5593 5640 49 100 -113 C ATOM 766 O LYS A 109 -31.084 33.833 -15.673 1.00 45.77 O ANISOU 766 O LYS A 109 5379 5959 6052 39 138 -140 O ATOM 767 CB LYS A 109 -30.711 33.623 -19.040 1.00 50.94 C ANISOU 767 CB LYS A 109 6126 6571 6657 93 75 -46 C ATOM 768 CG LYS A 109 -29.768 33.936 -20.213 1.00 54.80 C ANISOU 768 CG LYS A 109 6670 7032 7116 91 83 -23 C ATOM 769 CD LYS A 109 -30.540 34.446 -21.434 1.00 58.37 C ANISOU 769 CD LYS A 109 7157 7446 7572 142 58 21 C ATOM 770 CE LYS A 109 -29.821 34.364 -22.768 1.00 63.74 C ANISOU 770 CE LYS A 109 7893 8110 8213 145 50 53 C ATOM 771 NZ LYS A 109 -28.611 35.215 -22.809 1.00 65.37 N ANISOU 771 NZ LYS A 109 8142 8280 8415 114 110 40 N ATOM 772 N GLU A 110 -31.563 31.789 -16.392 1.00 39.31 N ANISOU 772 N GLU A 110 4548 5193 5193 53 64 -110 N ATOM 773 CA GLU A 110 -32.437 31.526 -15.224 1.00 39.50 C ANISOU 773 CA GLU A 110 4528 5236 5241 48 70 -135 C ATOM 774 C GLU A 110 -31.601 31.653 -13.955 1.00 44.56 C ANISOU 774 C GLU A 110 5157 5899 5872 14 110 -172 C ATOM 775 O GLU A 110 -32.088 32.153 -12.907 1.00 40.01 O ANISOU 775 O GLU A 110 4556 5321 5325 6 137 -201 O ATOM 776 CB GLU A 110 -33.117 30.161 -15.306 1.00 41.27 C ANISOU 776 CB GLU A 110 4736 5495 5451 49 34 -129 C ATOM 777 CG GLU A 110 -34.247 30.009 -14.290 1.00 47.44 C ANISOU 777 CG GLU A 110 5473 6287 6263 47 40 -152 C ATOM 778 CD GLU A 110 -35.355 28.995 -14.574 1.00 51.73 C ANISOU 778 CD GLU A 110 5994 6852 6807 50 7 -148 C ATOM 779 OE1 GLU A 110 -35.967 29.183 -15.647 1.00 52.30 O ANISOU 779 OE1 GLU A 110 6066 6917 6888 75 -25 -126 O ATOM 780 OE2 GLU A 110 -35.625 28.019 -13.702 1.00 43.27 O ANISOU 780 OE2 GLU A 110 4907 5805 5725 26 18 -169 O ATOM 781 N LEU A 111 -30.344 31.225 -14.004 1.00 40.38 N ANISOU 781 N LEU A 111 4643 5396 5301 -5 116 -175 N ATOM 782 CA LEU A 111 -29.551 31.158 -12.768 1.00 43.28 C ANISOU 782 CA LEU A 111 4992 5804 5648 -35 146 -211 C ATOM 783 C LEU A 111 -29.272 32.602 -12.378 1.00 42.53 C ANISOU 783 C LEU A 111 4897 5682 5580 -56 189 -240 C ATOM 784 O LEU A 111 -29.399 32.914 -11.162 1.00 47.79 O ANISOU 784 O LEU A 111 5538 6364 6255 -76 217 -276 O ATOM 785 CB LEU A 111 -28.277 30.360 -13.068 1.00 40.17 C ANISOU 785 CB LEU A 111 4609 5450 5200 -43 138 -204 C ATOM 786 CG LEU A 111 -27.213 30.371 -12.023 1.00 45.77 C ANISOU 786 CG LEU A 111 5297 6213 5878 -68 164 -238 C ATOM 787 CD1 LEU A 111 -27.757 29.815 -10.706 1.00 47.21 C ANISOU 787 CD1 LEU A 111 5452 6427 6055 -69 168 -256 C ATOM 788 CD2 LEU A 111 -26.022 29.623 -12.633 1.00 44.19 C ANISOU 788 CD2 LEU A 111 5110 6049 5629 -63 153 -222 C ATOM 789 N ARG A 112 -29.058 33.455 -13.362 1.00 42.55 N ANISOU 789 N ARG A 112 4931 5638 5595 -49 199 -224 N ATOM 790 CA ARG A 112 -28.752 34.873 -13.083 1.00 45.97 C ANISOU 790 CA ARG A 112 5377 6033 6053 -72 251 -252 C ATOM 791 C ARG A 112 -29.984 35.648 -12.631 1.00 51.83 C ANISOU 791 C ARG A 112 6112 6731 6846 -53 269 -258 C ATOM 792 O ARG A 112 -29.819 36.538 -11.800 1.00 53.15 O ANISOU 792 O ARG A 112 6277 6885 7031 -81 319 -296 O ATOM 793 CB ARG A 112 -28.142 35.477 -14.331 1.00 48.86 C ANISOU 793 CB ARG A 112 5790 6358 6414 -69 262 -230 C ATOM 794 CG ARG A 112 -26.664 35.083 -14.335 1.00 53.20 C ANISOU 794 CG ARG A 112 6338 6958 6917 -107 270 -249 C ATOM 795 CD ARG A 112 -25.837 35.779 -15.350 1.00 49.04 C ANISOU 795 CD ARG A 112 5855 6396 6382 -121 297 -241 C ATOM 796 NE ARG A 112 -24.405 35.520 -15.119 1.00 45.59 N ANISOU 796 NE ARG A 112 5400 6016 5904 -165 314 -273 N ATOM 797 CZ ARG A 112 -23.550 35.361 -16.097 1.00 42.77 C ANISOU 797 CZ ARG A 112 5068 5661 5521 -170 313 -258 C ATOM 798 NH1 ARG A 112 -22.254 35.218 -15.843 1.00 45.93 N ANISOU 798 NH1 ARG A 112 5445 6120 5886 -210 333 -292 N ATOM 799 NH2 ARG A 112 -24.007 35.248 -17.327 1.00 42.90 N ANISOU 799 NH2 ARG A 112 5127 5628 5542 -133 289 -209 N ATOM 800 N ALA A 113 -31.158 35.354 -13.194 1.00 49.51 N ANISOU 800 N ALA A 113 5814 6419 6576 -7 233 -223 N ATOM 801 CA ALA A 113 -32.454 35.851 -12.662 1.00 49.07 C ANISOU 801 CA ALA A 113 5737 6338 6568 18 243 -228 C ATOM 802 C ALA A 113 -32.613 35.479 -11.184 1.00 50.54 C ANISOU 802 C ALA A 113 5883 6563 6755 -11 260 -270 C ATOM 803 O ALA A 113 -33.195 36.259 -10.497 1.00 47.66 O ANISOU 803 O ALA A 113 5509 6172 6427 -11 296 -292 O ATOM 804 CB ALA A 113 -33.597 35.310 -13.486 1.00 52.06 C ANISOU 804 CB ALA A 113 6103 6716 6960 67 191 -189 C ATOM 805 N ASN A 114 -32.095 34.365 -10.665 1.00 48.78 N ANISOU 805 N ASN A 114 5642 6399 6492 -36 242 -281 N ATOM 806 CA ASN A 114 -32.606 33.821 -9.372 1.00 55.26 C ANISOU 806 CA ASN A 114 6427 7254 7313 -50 249 -310 C ATOM 807 C ASN A 114 -31.558 33.808 -8.283 1.00 58.56 C ANISOU 807 C ASN A 114 6838 7715 7694 -94 278 -349 C ATOM 808 O ASN A 114 -31.961 33.637 -7.118 1.00 66.14 O ANISOU 808 O ASN A 114 7774 8697 8656 -108 295 -377 O ATOM 809 CB ASN A 114 -33.147 32.386 -9.436 1.00 53.30 C ANISOU 809 CB ASN A 114 6163 7040 7045 -37 207 -290 C ATOM 810 CG ASN A 114 -34.487 32.349 -10.127 1.00 59.89 C ANISOU 810 CG ASN A 114 6985 7849 7920 -2 181 -267 C ATOM 811 OD1 ASN A 114 -34.537 32.275 -11.361 1.00 55.28 O ANISOU 811 OD1 ASN A 114 6418 7250 7332 21 149 -233 O ATOM 812 ND2 ASN A 114 -35.556 32.438 -9.346 1.00 60.25 N ANISOU 812 ND2 ASN A 114 6998 7893 7999 0 195 -286 N ATOM 813 N ALA A 115 -30.277 33.874 -8.620 1.00 55.95 N ANISOU 813 N ALA A 115 6523 7406 7327 -114 282 -353 N ATOM 814 CA ALA A 115 -29.256 33.736 -7.565 1.00 59.98 C ANISOU 814 CA ALA A 115 7016 7978 7794 -152 302 -392 C ATOM 815 C ALA A 115 -28.498 35.050 -7.529 1.00 54.38 C ANISOU 815 C ALA A 115 6318 7250 7093 -191 349 -427 C ATOM 816 O ALA A 115 -28.758 35.928 -8.373 1.00 50.22 O ANISOU 816 O ALA A 115 5821 6657 6603 -181 365 -414 O ATOM 817 CB ALA A 115 -28.377 32.521 -7.807 1.00 65.89 C ANISOU 817 CB ALA A 115 7763 8785 8485 -144 268 -372 C ATOM 818 N ASP A 116 -27.597 35.140 -6.572 1.00 56.02 N ANISOU 818 N ASP A 116 6504 7517 7263 -232 371 -472 N ATOM 819 CA ASP A 116 -26.713 36.294 -6.389 1.00 59.14 C ANISOU 819 CA ASP A 116 6904 7910 7654 -285 420 -519 C ATOM 820 C ASP A 116 -25.944 36.541 -7.691 1.00 58.36 C ANISOU 820 C ASP A 116 6833 7788 7552 -286 418 -498 C ATOM 821 O ASP A 116 -25.442 35.610 -8.334 1.00 52.25 O ANISOU 821 O ASP A 116 6057 7049 6746 -263 378 -466 O ATOM 822 CB ASP A 116 -25.817 36.004 -5.189 1.00 62.56 C ANISOU 822 CB ASP A 116 7298 8439 8032 -325 428 -567 C ATOM 823 CG ASP A 116 -24.893 37.148 -4.907 1.00 67.12 C ANISOU 823 CG ASP A 116 7873 9028 8601 -391 481 -627 C ATOM 824 OD1 ASP A 116 -24.519 37.839 -5.880 1.00 66.04 O ANISOU 824 OD1 ASP A 116 7766 8841 8484 -404 503 -623 O ATOM 825 OD2 ASP A 116 -24.599 37.353 -3.731 1.00 75.69 O ANISOU 825 OD2 ASP A 116 8930 10169 9659 -431 503 -679 O ATOM 826 N PRO A 117 -25.822 37.817 -8.114 1.00 63.25 N ANISOU 826 N PRO A 117 7486 8344 8202 -312 468 -516 N ATOM 827 CA PRO A 117 -24.755 38.236 -9.031 1.00 67.18 C ANISOU 827 CA PRO A 117 8007 8833 8683 -338 487 -519 C ATOM 828 C PRO A 117 -23.317 37.751 -8.735 1.00 63.26 C ANISOU 828 C PRO A 117 7472 8435 8126 -378 481 -552 C ATOM 829 O PRO A 117 -22.618 37.591 -9.659 1.00 66.79 O ANISOU 829 O PRO A 117 7933 8884 8557 -377 473 -535 O ATOM 830 CB PRO A 117 -24.795 39.774 -8.916 1.00 71.68 C ANISOU 830 CB PRO A 117 8612 9331 9289 -380 563 -558 C ATOM 831 CG PRO A 117 -26.251 40.084 -8.608 1.00 72.46 C ANISOU 831 CG PRO A 117 8724 9366 9440 -338 568 -539 C ATOM 832 CD PRO A 117 -26.733 38.922 -7.762 1.00 69.17 C ANISOU 832 CD PRO A 117 8257 9017 9004 -316 516 -533 C ATOM 833 N SER A 118 -22.877 37.559 -7.486 1.00 60.90 N ANISOU 833 N SER A 118 7126 8218 7792 -412 486 -601 N ATOM 834 CA SER A 118 -21.491 37.079 -7.165 1.00 62.42 C ANISOU 834 CA SER A 118 7273 8521 7921 -442 476 -633 C ATOM 835 C SER A 118 -21.327 35.555 -7.422 1.00 56.34 C ANISOU 835 C SER A 118 6484 7810 7113 -381 410 -581 C ATOM 836 O SER A 118 -20.254 35.006 -7.160 1.00 53.49 O ANISOU 836 O SER A 118 6082 7544 6697 -389 395 -598 O ATOM 837 CB SER A 118 -21.138 37.374 -5.723 1.00 60.37 C ANISOU 837 CB SER A 118 6968 8338 7631 -492 499 -700 C ATOM 838 OG SER A 118 -21.947 36.553 -4.875 1.00 66.16 O ANISOU 838 OG SER A 118 7685 9095 8356 -450 464 -679 O ATOM 839 N LEU A 119 -22.387 34.832 -7.770 1.00 49.35 N ANISOU 839 N LEU A 119 5622 6877 6251 -323 373 -525 N ATOM 840 CA LEU A 119 -22.287 33.368 -7.952 1.00 41.19 C ANISOU 840 CA LEU A 119 4579 5890 5180 -270 321 -479 C ATOM 841 C LEU A 119 -21.101 33.021 -8.871 1.00 38.18 C ANISOU 841 C LEU A 119 4196 5543 4765 -267 311 -467 C ATOM 842 O LEU A 119 -20.977 33.592 -9.975 1.00 36.38 O ANISOU 842 O LEU A 119 4001 5256 4563 -277 325 -455 O ATOM 843 CB LEU A 119 -23.612 32.952 -8.583 1.00 43.50 C ANISOU 843 CB LEU A 119 4908 6104 5516 -223 296 -426 C ATOM 844 CG LEU A 119 -23.793 31.484 -8.862 1.00 42.62 C ANISOU 844 CG LEU A 119 4802 6015 5377 -172 251 -379 C ATOM 845 CD1 LEU A 119 -23.967 30.727 -7.600 1.00 42.03 C ANISOU 845 CD1 LEU A 119 4701 5998 5270 -160 243 -388 C ATOM 846 CD2 LEU A 119 -25.034 31.256 -9.686 1.00 46.53 C ANISOU 846 CD2 LEU A 119 5330 6433 5915 -140 230 -335 C ATOM 847 N ILE A 120 -20.339 31.995 -8.525 1.00 33.57 N ANISOU 847 N ILE A 120 3581 5048 4125 -243 285 -461 N ATOM 848 CA ILE A 120 -19.363 31.351 -9.450 1.00 34.50 C ANISOU 848 CA ILE A 120 3698 5197 4211 -221 269 -436 C ATOM 849 C ILE A 120 -20.062 30.338 -10.350 1.00 32.40 C ANISOU 849 C ILE A 120 3476 4876 3956 -164 235 -370 C ATOM 850 O ILE A 120 -20.529 29.308 -9.833 1.00 31.38 O ANISOU 850 O ILE A 120 3347 4766 3807 -123 211 -345 O ATOM 851 CB ILE A 120 -18.261 30.674 -8.668 1.00 35.48 C ANISOU 851 CB ILE A 120 3769 5443 4268 -209 258 -456 C ATOM 852 CG1 ILE A 120 -17.620 31.645 -7.683 1.00 38.63 C ANISOU 852 CG1 ILE A 120 4117 5909 4649 -272 289 -528 C ATOM 853 CG2 ILE A 120 -17.245 30.060 -9.596 1.00 38.96 C ANISOU 853 CG2 ILE A 120 4206 5917 4677 -185 246 -433 C ATOM 854 CD1 ILE A 120 -17.094 30.899 -6.527 1.00 46.67 C ANISOU 854 CD1 ILE A 120 5085 7043 5602 -247 269 -541 C ATOM 855 N ILE A 121 -20.040 30.578 -11.671 1.00 28.66 N ANISOU 855 N ILE A 121 3040 4342 3506 -164 236 -346 N ATOM 856 CA ILE A 121 -20.789 29.749 -12.625 1.00 27.92 C ANISOU 856 CA ILE A 121 2991 4191 3424 -120 205 -289 C ATOM 857 C ILE A 121 -19.788 29.014 -13.507 1.00 30.51 C ANISOU 857 C ILE A 121 3328 4549 3716 -99 196 -266 C ATOM 858 O ILE A 121 -19.018 29.695 -14.136 1.00 30.70 O ANISOU 858 O ILE A 121 3353 4569 3740 -128 218 -282 O ATOM 859 CB ILE A 121 -21.754 30.602 -13.471 1.00 29.51 C ANISOU 859 CB ILE A 121 3233 4296 3680 -128 210 -273 C ATOM 860 CG1 ILE A 121 -22.754 31.371 -12.606 1.00 29.47 C ANISOU 860 CG1 ILE A 121 3220 4261 3716 -143 225 -296 C ATOM 861 CG2 ILE A 121 -22.490 29.724 -14.462 1.00 31.26 C ANISOU 861 CG2 ILE A 121 3494 4474 3908 -87 175 -221 C ATOM 862 CD1 ILE A 121 -23.502 32.415 -13.365 1.00 31.41 C ANISOU 862 CD1 ILE A 121 3502 4420 4011 -149 239 -286 C ATOM 863 N VAL A 122 -19.832 27.692 -13.496 1.00 27.49 N ANISOU 863 N VAL A 122 2953 4189 3302 -53 172 -232 N ATOM 864 CA VAL A 122 -18.930 26.834 -14.305 1.00 29.88 C ANISOU 864 CA VAL A 122 3267 4516 3568 -24 165 -206 C ATOM 865 C VAL A 122 -19.746 26.090 -15.377 1.00 26.94 C ANISOU 865 C VAL A 122 2953 4074 3209 2 144 -158 C ATOM 866 O VAL A 122 -20.789 25.486 -15.038 1.00 28.53 O ANISOU 866 O VAL A 122 3170 4249 3420 20 128 -140 O ATOM 867 CB VAL A 122 -18.204 25.872 -13.363 1.00 30.72 C ANISOU 867 CB VAL A 122 3339 4713 3620 11 161 -208 C ATOM 868 CG1 VAL A 122 -17.432 24.857 -14.169 1.00 34.84 C ANISOU 868 CG1 VAL A 122 3879 5252 4106 52 157 -175 C ATOM 869 CG2 VAL A 122 -17.268 26.732 -12.468 1.00 35.61 C ANISOU 869 CG2 VAL A 122 3894 5413 4221 -23 180 -263 C ATOM 870 N LEU A 123 -19.243 26.038 -16.597 1.00 25.20 N ANISOU 870 N LEU A 123 2760 3829 2983 3 146 -141 N ATOM 871 CA LEU A 123 -19.861 25.262 -17.695 1.00 23.29 C ANISOU 871 CA LEU A 123 2573 3531 2743 25 127 -98 C ATOM 872 C LEU A 123 -19.129 23.952 -17.849 1.00 24.77 C ANISOU 872 C LEU A 123 2770 3755 2884 65 128 -77 C ATOM 873 O LEU A 123 -17.886 23.935 -17.962 1.00 24.01 O ANISOU 873 O LEU A 123 2653 3709 2759 70 144 -86 O ATOM 874 CB LEU A 123 -19.819 26.097 -18.975 1.00 23.68 C ANISOU 874 CB LEU A 123 2655 3526 2813 2 131 -92 C ATOM 875 CG LEU A 123 -20.469 25.495 -20.198 1.00 25.03 C ANISOU 875 CG LEU A 123 2882 3643 2985 18 110 -53 C ATOM 876 CD1 LEU A 123 -21.984 25.349 -19.989 1.00 25.10 C ANISOU 876 CD1 LEU A 123 2900 3614 3022 23 83 -42 C ATOM 877 CD2 LEU A 123 -20.114 26.379 -21.439 1.00 27.27 C ANISOU 877 CD2 LEU A 123 3198 3886 3277 -2 120 -47 C ATOM 878 N VAL A 124 -19.872 22.853 -17.880 1.00 24.00 N ANISOU 878 N VAL A 124 2706 3633 2777 92 115 -49 N ATOM 879 CA VAL A 124 -19.268 21.530 -18.042 1.00 24.74 C ANISOU 879 CA VAL A 124 2823 3748 2827 134 124 -24 C ATOM 880 C VAL A 124 -19.891 20.774 -19.215 1.00 24.56 C ANISOU 880 C VAL A 124 2863 3661 2804 138 116 5 C ATOM 881 O VAL A 124 -21.084 20.445 -19.176 1.00 23.26 O ANISOU 881 O VAL A 124 2721 3457 2658 130 102 12 O ATOM 882 CB VAL A 124 -19.413 20.718 -16.759 1.00 26.81 C ANISOU 882 CB VAL A 124 3072 4048 3064 167 129 -22 C ATOM 883 CG1 VAL A 124 -18.791 19.348 -16.957 1.00 27.40 C ANISOU 883 CG1 VAL A 124 3180 4137 3092 219 145 8 C ATOM 884 CG2 VAL A 124 -18.907 21.465 -15.541 1.00 28.26 C ANISOU 884 CG2 VAL A 124 3192 4300 3243 160 134 -55 C ATOM 885 N GLY A 125 -19.081 20.476 -20.219 1.00 25.16 N ANISOU 885 N GLY A 125 2964 3734 2859 147 126 19 N ATOM 886 CA GLY A 125 -19.466 19.550 -21.299 1.00 23.83 C ANISOU 886 CA GLY A 125 2859 3515 2677 154 125 46 C ATOM 887 C GLY A 125 -19.188 18.138 -20.904 1.00 23.21 C ANISOU 887 C GLY A 125 2807 3450 2560 198 147 64 C ATOM 888 O GLY A 125 -17.970 17.718 -20.913 1.00 26.29 O ANISOU 888 O GLY A 125 3190 3881 2917 235 170 72 O ATOM 889 N ASN A 126 -20.225 17.381 -20.566 1.00 21.94 N ANISOU 889 N ASN A 126 2676 3257 2403 198 145 72 N ATOM 890 CA ASN A 126 -20.092 15.991 -20.073 1.00 25.34 C ANISOU 890 CA ASN A 126 3144 3689 2796 241 175 91 C ATOM 891 C ASN A 126 -20.208 14.954 -21.201 1.00 26.08 C ANISOU 891 C ASN A 126 3310 3730 2868 242 194 110 C ATOM 892 O ASN A 126 -20.615 15.265 -22.345 1.00 24.48 O ANISOU 892 O ASN A 126 3129 3490 2681 204 176 107 O ATOM 893 CB ASN A 126 -21.109 15.747 -18.970 1.00 25.23 C ANISOU 893 CB ASN A 126 3124 3667 2793 235 175 84 C ATOM 894 CG ASN A 126 -20.974 14.437 -18.238 1.00 26.86 C ANISOU 894 CG ASN A 126 3369 3874 2959 282 212 104 C ATOM 895 OD1 ASN A 126 -19.827 14.059 -17.900 1.00 25.17 O ANISOU 895 OD1 ASN A 126 3150 3706 2708 337 232 119 O ATOM 896 ND2 ASN A 126 -22.128 13.772 -18.089 1.00 24.57 N ANISOU 896 ND2 ASN A 126 3120 3536 2677 259 223 102 N ATOM 897 N LYS A 127 -19.843 13.738 -20.880 1.00 26.03 N ANISOU 897 N LYS A 127 3344 3719 2824 286 231 130 N ATOM 898 CA LYS A 127 -19.814 12.545 -21.794 1.00 27.34 C ANISOU 898 CA LYS A 127 3590 3835 2963 295 265 149 C ATOM 899 C LYS A 127 -18.768 12.702 -22.876 1.00 27.77 C ANISOU 899 C LYS A 127 3651 3896 3003 306 270 157 C ATOM 900 O LYS A 127 -18.965 12.154 -23.996 1.00 26.29 O ANISOU 900 O LYS A 127 3524 3658 2804 285 283 162 O ATOM 901 CB LYS A 127 -21.172 12.286 -22.442 1.00 28.08 C ANISOU 901 CB LYS A 127 3726 3867 3075 236 254 136 C ATOM 902 CG LYS A 127 -22.347 12.404 -21.481 1.00 29.72 C ANISOU 902 CG LYS A 127 3913 4070 3307 210 242 120 C ATOM 903 CD LYS A 127 -23.654 11.750 -21.980 1.00 28.32 C ANISOU 903 CD LYS A 127 3783 3838 3137 157 246 106 C ATOM 904 CE LYS A 127 -24.808 12.068 -21.069 1.00 28.98 C ANISOU 904 CE LYS A 127 3831 3926 3251 128 230 85 C ATOM 905 NZ LYS A 127 -26.085 11.585 -21.644 1.00 31.73 N ANISOU 905 NZ LYS A 127 4210 4235 3609 69 228 63 N ATOM 906 N LYS A 128 -17.597 13.257 -22.544 1.00 26.92 N ANISOU 906 N LYS A 128 3489 3850 2886 340 270 157 N ATOM 907 CA LYS A 128 -16.520 13.318 -23.543 1.00 28.88 C ANISOU 907 CA LYS A 128 3744 4109 3119 353 284 163 C ATOM 908 C LYS A 128 -15.966 11.957 -23.905 1.00 28.34 C ANISOU 908 C LYS A 128 3739 4017 3009 404 333 190 C ATOM 909 O LYS A 128 -15.288 11.886 -24.947 1.00 27.15 O ANISOU 909 O LYS A 128 3611 3858 2847 405 349 194 O ATOM 910 CB LYS A 128 -15.391 14.258 -23.160 1.00 32.34 C ANISOU 910 CB LYS A 128 4104 4624 3559 368 276 150 C ATOM 911 CG LYS A 128 -14.497 13.828 -22.048 1.00 38.26 C ANISOU 911 CG LYS A 128 4813 5447 4276 437 295 158 C ATOM 912 CD LYS A 128 -13.466 15.000 -22.002 1.00 44.84 C ANISOU 912 CD LYS A 128 5563 6354 5117 424 282 131 C ATOM 913 CE LYS A 128 -12.028 14.631 -21.940 1.00 54.19 C ANISOU 913 CE LYS A 128 6713 7611 6264 484 308 137 C ATOM 914 NZ LYS A 128 -11.740 14.333 -20.520 1.00 55.65 N ANISOU 914 NZ LYS A 128 6852 7870 6421 540 307 141 N ATOM 915 N ASP A 129 -16.320 10.932 -23.169 1.00 28.11 N ANISOU 915 N ASP A 129 3749 3971 2960 440 361 206 N ATOM 916 CA ASP A 129 -15.953 9.554 -23.518 1.00 29.80 C ANISOU 916 CA ASP A 129 4041 4146 3135 488 418 233 C ATOM 917 C ASP A 129 -16.671 9.110 -24.789 1.00 30.91 C ANISOU 917 C ASP A 129 4258 4206 3279 431 428 227 C ATOM 918 O ASP A 129 -16.217 8.092 -25.362 1.00 31.65 O ANISOU 918 O ASP A 129 4420 4263 3342 463 479 244 O ATOM 919 CB ASP A 129 -16.288 8.570 -22.429 1.00 29.40 C ANISOU 919 CB ASP A 129 4027 4083 3061 535 452 252 C ATOM 920 CG ASP A 129 -17.712 8.629 -21.940 1.00 30.12 C ANISOU 920 CG ASP A 129 4130 4134 3177 479 435 235 C ATOM 921 OD1 ASP A 129 -18.060 9.690 -21.282 1.00 29.44 O ANISOU 921 OD1 ASP A 129 3971 4092 3122 451 387 215 O ATOM 922 OD2 ASP A 129 -18.468 7.735 -22.279 1.00 29.76 O ANISOU 922 OD2 ASP A 129 4162 4019 3124 454 467 236 O ATOM 923 N LEU A 130 -17.782 9.748 -25.144 1.00 30.62 N ANISOU 923 N LEU A 130 4213 4143 3275 356 386 203 N ATOM 924 CA LEU A 130 -18.587 9.380 -26.346 1.00 30.93 C ANISOU 924 CA LEU A 130 4318 4119 3314 295 388 192 C ATOM 925 C LEU A 130 -18.082 10.162 -27.576 1.00 31.86 C ANISOU 925 C LEU A 130 4425 4244 3437 269 364 186 C ATOM 926 O LEU A 130 -18.877 10.786 -28.291 1.00 30.68 O ANISOU 926 O LEU A 130 4273 4077 3305 209 324 170 O ATOM 927 CB LEU A 130 -20.071 9.606 -26.062 1.00 31.00 C ANISOU 927 CB LEU A 130 4320 4107 3350 235 355 169 C ATOM 928 CG LEU A 130 -20.672 8.763 -24.928 1.00 34.19 C ANISOU 928 CG LEU A 130 4748 4494 3749 250 387 171 C ATOM 929 CD1 LEU A 130 -22.160 9.031 -24.810 1.00 33.23 C ANISOU 929 CD1 LEU A 130 4614 4355 3656 181 355 143 C ATOM 930 CD2 LEU A 130 -20.425 7.253 -25.158 1.00 35.19 C ANISOU 930 CD2 LEU A 130 4970 4566 3834 277 460 187 C ATOM 931 N GLY A 131 -16.785 10.011 -27.880 1.00 34.76 N ANISOU 931 N GLY A 131 4792 4632 3782 317 394 201 N ATOM 932 CA GLY A 131 -16.087 10.803 -28.907 1.00 33.74 C ANISOU 932 CA GLY A 131 4647 4517 3656 299 381 197 C ATOM 933 C GLY A 131 -16.736 10.660 -30.286 1.00 32.55 C ANISOU 933 C GLY A 131 4560 4309 3497 241 374 189 C ATOM 934 O GLY A 131 -16.872 11.684 -31.000 1.00 30.41 O ANISOU 934 O GLY A 131 4269 4043 3241 200 336 179 O ATOM 935 N SER A 132 -17.212 9.468 -30.620 1.00 30.02 N ANISOU 935 N SER A 132 4316 3936 3152 232 409 191 N ATOM 936 CA ASER A 132 -17.791 9.208 -31.964 0.75 31.38 C ANISOU 936 CA ASER A 132 4553 4060 3307 174 406 179 C ATOM 937 CA BSER A 132 -17.803 9.194 -31.959 0.25 30.54 C ANISOU 937 CA BSER A 132 4447 3953 3200 174 407 179 C ATOM 938 C SER A 132 -19.100 9.973 -32.162 1.00 29.66 C ANISOU 938 C SER A 132 4311 3843 3113 109 343 159 C ATOM 939 O SER A 132 -19.374 10.387 -33.340 1.00 28.62 O ANISOU 939 O SER A 132 4201 3700 2972 66 316 151 O ATOM 940 CB ASER A 132 -17.932 7.703 -32.206 0.75 31.47 C ANISOU 940 CB ASER A 132 4655 4016 3284 178 469 180 C ATOM 941 CB BSER A 132 -18.017 7.723 -32.175 0.25 30.81 C ANISOU 941 CB BSER A 132 4570 3933 3203 175 466 179 C ATOM 942 OG ASER A 132 -18.935 7.155 -31.384 0.75 31.14 O ANISOU 942 OG ASER A 132 4624 3956 3250 162 473 171 O ATOM 943 OG BSER A 132 -16.766 7.070 -32.199 0.25 30.86 O ANISOU 943 OG BSER A 132 4604 3937 3185 240 526 201 O ATOM 944 N LEU A 133 -19.842 10.233 -31.076 1.00 27.84 N ANISOU 944 N LEU A 133 4034 3631 2911 107 317 152 N ATOM 945 CA LEU A 133 -21.204 10.853 -31.145 1.00 28.22 C ANISOU 945 CA LEU A 133 4055 3682 2982 52 260 132 C ATOM 946 C LEU A 133 -21.158 12.354 -30.886 1.00 26.73 C ANISOU 946 C LEU A 133 3791 3533 2829 55 209 134 C ATOM 947 O LEU A 133 -22.181 13.038 -30.998 1.00 26.94 O ANISOU 947 O LEU A 133 3791 3567 2878 21 160 122 O ATOM 948 CB LEU A 133 -22.081 10.151 -30.132 1.00 27.66 C ANISOU 948 CB LEU A 133 3985 3601 2921 45 274 120 C ATOM 949 CG LEU A 133 -22.243 8.650 -30.322 1.00 29.61 C ANISOU 949 CG LEU A 133 4316 3799 3134 35 335 115 C ATOM 950 CD1 LEU A 133 -23.073 8.076 -29.189 1.00 29.85 C ANISOU 950 CD1 LEU A 133 4345 3820 3176 28 353 103 C ATOM 951 CD2 LEU A 133 -22.845 8.315 -31.694 1.00 30.63 C ANISOU 951 CD2 LEU A 133 4498 3900 3237 -28 327 94 C ATOM 952 N ARG A 134 -19.970 12.887 -30.620 1.00 27.11 N ANISOU 952 N ARG A 134 3808 3609 2883 95 222 147 N ATOM 953 CA ARG A 134 -19.806 14.331 -30.325 1.00 27.74 C ANISOU 953 CA ARG A 134 3822 3723 2996 95 185 144 C ATOM 954 C ARG A 134 -20.571 15.194 -31.330 1.00 26.79 C ANISOU 954 C ARG A 134 3708 3587 2883 53 139 141 C ATOM 955 O ARG A 134 -20.294 15.085 -32.543 1.00 27.78 O ANISOU 955 O ARG A 134 3881 3691 2980 38 145 147 O ATOM 956 CB ARG A 134 -18.347 14.738 -30.362 1.00 27.58 C ANISOU 956 CB ARG A 134 3780 3730 2969 127 211 152 C ATOM 957 CG ARG A 134 -18.124 16.209 -30.144 1.00 26.66 C ANISOU 957 CG ARG A 134 3605 3641 2883 117 185 144 C ATOM 958 CD ARG A 134 -16.663 16.572 -30.133 1.00 27.44 C ANISOU 958 CD ARG A 134 3677 3774 2973 140 217 144 C ATOM 959 NE ARG A 134 -15.966 16.108 -28.940 1.00 28.19 N ANISOU 959 NE ARG A 134 3728 3916 3064 185 240 142 N ATOM 960 CZ ARG A 134 -15.758 16.836 -27.875 1.00 30.00 C ANISOU 960 CZ ARG A 134 3890 4192 3315 192 230 128 C ATOM 961 NH1 ARG A 134 -16.300 18.032 -27.798 1.00 28.95 N ANISOU 961 NH1 ARG A 134 3729 4054 3214 155 200 114 N ATOM 962 NH2 ARG A 134 -15.081 16.347 -26.861 1.00 30.07 N ANISOU 962 NH2 ARG A 134 3861 4251 3309 237 251 128 N ATOM 963 N GLN A 135 -21.372 16.143 -30.860 1.00 23.96 N ANISOU 963 N GLN A 135 3302 3241 2559 40 98 134 N ATOM 964 CA GLN A 135 -22.108 17.049 -31.762 1.00 24.26 C ANISOU 964 CA GLN A 135 3345 3270 2604 13 54 136 C ATOM 965 C GLN A 135 -21.596 18.471 -31.615 1.00 28.06 C ANISOU 965 C GLN A 135 3788 3762 3111 23 46 141 C ATOM 966 O GLN A 135 -21.956 19.316 -32.460 1.00 26.91 O ANISOU 966 O GLN A 135 3656 3603 2965 10 18 150 O ATOM 967 CB GLN A 135 -23.615 17.045 -31.514 1.00 23.87 C ANISOU 967 CB GLN A 135 3275 3223 2571 -9 13 124 C ATOM 968 CG GLN A 135 -24.325 15.779 -32.002 1.00 24.81 C ANISOU 968 CG GLN A 135 3439 3327 2659 -37 16 112 C ATOM 969 CD GLN A 135 -25.819 15.758 -31.904 1.00 25.72 C ANISOU 969 CD GLN A 135 3530 3453 2787 -67 -23 94 C ATOM 970 OE1 GLN A 135 -26.419 16.673 -31.392 1.00 25.49 O ANISOU 970 OE1 GLN A 135 3449 3443 2793 -60 -56 93 O ATOM 971 NE2 GLN A 135 -26.456 14.663 -32.308 1.00 27.24 N ANISOU 971 NE2 GLN A 135 3759 3637 2952 -102 -16 76 N ATOM 972 N VAL A 136 -20.953 18.773 -30.495 1.00 25.48 N ANISOU 972 N VAL A 136 3413 3461 2806 43 66 133 N ATOM 973 CA AVAL A 136 -20.423 20.145 -30.343 0.73 27.10 C ANISOU 973 CA AVAL A 136 3585 3676 3036 42 67 131 C ATOM 974 CA BVAL A 136 -20.479 20.130 -30.113 0.27 27.28 C ANISOU 974 CA BVAL A 136 3599 3702 3063 44 66 129 C ATOM 975 C VAL A 136 -18.955 20.069 -29.971 1.00 27.79 C ANISOU 975 C VAL A 136 3653 3791 3112 59 110 124 C ATOM 976 O VAL A 136 -18.470 19.074 -29.416 1.00 29.26 O ANISOU 976 O VAL A 136 3833 3999 3283 83 134 123 O ATOM 977 CB AVAL A 136 -21.229 20.965 -29.320 0.73 28.25 C ANISOU 977 CB AVAL A 136 3678 3832 3224 41 43 119 C ATOM 978 CB BVAL A 136 -21.200 20.532 -28.805 0.27 27.43 C ANISOU 978 CB BVAL A 136 3562 3740 3119 47 49 115 C ATOM 979 CG1AVAL A 136 -22.605 21.311 -29.869 0.73 31.74 C ANISOU 979 CG1AVAL A 136 4132 4251 3676 28 -1 127 C ATOM 980 CG1BVAL A 136 -20.494 21.603 -27.993 0.27 26.82 C ANISOU 980 CG1BVAL A 136 3435 3687 3068 50 66 100 C ATOM 981 CG2AVAL A 136 -21.304 20.219 -27.999 0.73 27.06 C ANISOU 981 CG2AVAL A 136 3491 3709 3080 55 54 107 C ATOM 982 CG2BVAL A 136 -22.629 20.960 -29.091 0.27 28.71 C ANISOU 982 CG2BVAL A 136 3725 3882 3301 33 6 117 C ATOM 983 N SER A 137 -18.243 21.078 -30.425 1.00 27.01 N ANISOU 983 N SER A 137 3551 3690 3018 47 124 122 N ATOM 984 CA SER A 137 -16.786 21.175 -30.275 1.00 27.17 C ANISOU 984 CA SER A 137 3550 3744 3029 55 167 111 C ATOM 985 C SER A 137 -16.474 21.753 -28.910 1.00 26.59 C ANISOU 985 C SER A 137 3404 3717 2980 58 173 87 C ATOM 986 O SER A 137 -17.316 22.436 -28.267 1.00 26.63 O ANISOU 986 O SER A 137 3384 3715 3017 48 149 79 O ATOM 987 CB SER A 137 -16.188 22.028 -31.383 1.00 27.46 C ANISOU 987 CB SER A 137 3618 3756 3058 31 185 113 C ATOM 988 OG SER A 137 -16.604 23.352 -31.192 1.00 26.36 O ANISOU 988 OG SER A 137 3463 3601 2949 10 175 106 O ATOM 989 N PHE A 138 -15.239 21.565 -28.491 1.00 27.32 N ANISOU 989 N PHE A 138 3460 3859 3059 73 206 72 N ATOM 990 CA PHE A 138 -14.713 22.262 -27.310 1.00 28.69 C ANISOU 990 CA PHE A 138 3561 4089 3249 68 216 43 C ATOM 991 C PHE A 138 -14.930 23.768 -27.491 1.00 27.79 C ANISOU 991 C PHE A 138 3443 3948 3167 24 217 26 C ATOM 992 O PHE A 138 -15.384 24.426 -26.580 1.00 26.87 O ANISOU 992 O PHE A 138 3290 3841 3076 12 207 9 O ATOM 993 CB PHE A 138 -13.252 21.887 -27.133 1.00 28.61 C ANISOU 993 CB PHE A 138 3513 4144 3213 87 252 29 C ATOM 994 CG PHE A 138 -12.656 22.458 -25.894 1.00 30.36 C ANISOU 994 CG PHE A 138 3654 4438 3441 83 260 -5 C ATOM 995 CD1 PHE A 138 -12.288 23.790 -25.854 1.00 31.89 C ANISOU 995 CD1 PHE A 138 3819 4639 3656 34 277 -38 C ATOM 996 CD2 PHE A 138 -12.483 21.691 -24.765 1.00 29.92 C ANISOU 996 CD2 PHE A 138 3556 4443 3369 126 254 -6 C ATOM 997 CE1 PHE A 138 -11.773 24.309 -24.687 1.00 32.28 C ANISOU 997 CE1 PHE A 138 3793 4761 3709 22 285 -77 C ATOM 998 CE2 PHE A 138 -11.968 22.234 -23.583 1.00 35.17 C ANISOU 998 CE2 PHE A 138 4142 5183 4034 120 257 -41 C ATOM 999 CZ PHE A 138 -11.597 23.550 -23.572 1.00 32.13 C ANISOU 999 CZ PHE A 138 3725 4810 3670 65 273 -79 C ATOM 1000 N GLU A 139 -14.587 24.305 -28.653 1.00 26.59 N ANISOU 1000 N GLU A 139 3334 3758 3009 0 235 32 N ATOM 1001 CA GLU A 139 -14.733 25.773 -28.895 1.00 28.43 C ANISOU 1001 CA GLU A 139 3577 3956 3268 -38 248 20 C ATOM 1002 C GLU A 139 -16.182 26.234 -28.808 1.00 27.56 C ANISOU 1002 C GLU A 139 3488 3796 3185 -36 210 37 C ATOM 1003 O GLU A 139 -16.357 27.349 -28.382 1.00 29.50 O ANISOU 1003 O GLU A 139 3718 4029 3458 -57 221 20 O ATOM 1004 CB GLU A 139 -14.142 26.109 -30.275 1.00 31.74 C ANISOU 1004 CB GLU A 139 4053 4336 3669 -57 277 30 C ATOM 1005 CG GLU A 139 -12.665 25.840 -30.322 1.00 34.38 C ANISOU 1005 CG GLU A 139 4356 4723 3982 -65 321 6 C ATOM 1006 CD GLU A 139 -12.146 24.473 -30.788 1.00 37.28 C ANISOU 1006 CD GLU A 139 4737 5113 4314 -30 324 23 C ATOM 1007 OE1 GLU A 139 -12.876 23.417 -30.691 0.80 33.42 O ANISOU 1007 OE1 GLU A 139 4266 4615 3814 5 291 48 O ATOM 1008 OE2 GLU A 139 -10.946 24.464 -31.113 0.80 34.88 O ANISOU 1008 OE2 GLU A 139 4418 4841 3994 -39 365 6 O ATOM 1009 N ASP A 140 -17.161 25.408 -29.187 1.00 29.00 N ANISOU 1009 N ASP A 140 3703 3956 3359 -12 171 66 N ATOM 1010 CA ASP A 140 -18.602 25.746 -28.989 1.00 28.79 C ANISOU 1010 CA ASP A 140 3682 3899 3359 -6 131 78 C ATOM 1011 C ASP A 140 -18.787 26.070 -27.493 1.00 30.25 C ANISOU 1011 C ASP A 140 3802 4117 3574 -7 131 51 C ATOM 1012 O ASP A 140 -19.487 27.045 -27.145 1.00 28.32 O ANISOU 1012 O ASP A 140 3549 3849 3361 -15 125 46 O ATOM 1013 CB ASP A 140 -19.549 24.650 -29.485 1.00 30.37 C ANISOU 1013 CB ASP A 140 3912 4085 3540 12 91 102 C ATOM 1014 CG ASP A 140 -19.664 24.546 -31.007 1.00 33.69 C ANISOU 1014 CG ASP A 140 4400 4468 3931 9 83 129 C ATOM 1015 OD1 ASP A 140 -19.364 25.554 -31.659 1.00 33.08 O ANISOU 1015 OD1 ASP A 140 4350 4362 3855 -1 98 135 O ATOM 1016 OD2 ASP A 140 -19.827 23.434 -31.490 1.00 32.81 O ANISOU 1016 OD2 ASP A 140 4315 4358 3791 16 71 139 O ATOM 1017 N GLY A 141 -18.347 25.191 -26.606 1.00 29.31 N ANISOU 1017 N GLY A 141 3643 4050 3443 6 136 38 N ATOM 1018 CA GLY A 141 -18.545 25.428 -25.168 1.00 27.54 C ANISOU 1018 CA GLY A 141 3361 3862 3241 6 135 13 C ATOM 1019 C GLY A 141 -17.763 26.653 -24.674 1.00 29.49 C ANISOU 1019 C GLY A 141 3572 4127 3503 -25 170 -21 C ATOM 1020 O GLY A 141 -18.268 27.433 -23.910 1.00 28.34 O ANISOU 1020 O GLY A 141 3402 3978 3387 -38 170 -38 O ATOM 1021 N GLN A 142 -16.501 26.817 -25.106 1.00 27.98 N ANISOU 1021 N GLN A 142 3378 3959 3291 -40 204 -34 N ATOM 1022 CA GLN A 142 -15.639 27.942 -24.744 1.00 28.77 C ANISOU 1022 CA GLN A 142 3446 4082 3402 -81 245 -75 C ATOM 1023 C GLN A 142 -16.275 29.258 -25.187 1.00 27.88 C ANISOU 1023 C GLN A 142 3373 3897 3322 -109 257 -73 C ATOM 1024 O GLN A 142 -16.211 30.231 -24.432 1.00 28.24 O ANISOU 1024 O GLN A 142 3391 3948 3391 -140 282 -107 O ATOM 1025 CB GLN A 142 -14.314 27.612 -25.428 1.00 33.40 C ANISOU 1025 CB GLN A 142 4032 4700 3956 -87 275 -81 C ATOM 1026 CG GLN A 142 -13.114 28.334 -24.939 1.00 36.20 C ANISOU 1026 CG GLN A 142 4333 5112 4308 -127 319 -131 C ATOM 1027 CD GLN A 142 -11.861 27.912 -25.693 1.00 37.41 C ANISOU 1027 CD GLN A 142 4484 5299 4429 -129 348 -136 C ATOM 1028 OE1 GLN A 142 -11.906 27.752 -26.920 1.00 32.28 O ANISOU 1028 OE1 GLN A 142 3898 4594 3772 -125 353 -107 O ATOM 1029 NE2 GLN A 142 -10.797 27.688 -24.929 1.00 33.93 N ANISOU 1029 NE2 GLN A 142 3969 4954 3969 -130 365 -173 N ATOM 1030 N ARG A 143 -16.854 29.291 -26.369 1.00 30.79 N ANISOU 1030 N ARG A 143 3807 4202 3688 -96 243 -35 N ATOM 1031 CA ARG A 143 -17.545 30.498 -26.885 1.00 31.39 C ANISOU 1031 CA ARG A 143 3931 4205 3791 -107 252 -23 C ATOM 1032 C ARG A 143 -18.692 30.856 -25.945 1.00 32.95 C ANISOU 1032 C ARG A 143 4103 4392 4023 -95 229 -26 C ATOM 1033 O ARG A 143 -18.921 32.047 -25.665 1.00 29.21 O ANISOU 1033 O ARG A 143 3636 3883 3578 -113 257 -41 O ATOM 1034 CB ARG A 143 -17.992 30.309 -28.334 1.00 32.95 C ANISOU 1034 CB ARG A 143 4200 4348 3969 -86 233 22 C ATOM 1035 CG ARG A 143 -16.847 30.523 -29.330 1.00 37.60 C ANISOU 1035 CG ARG A 143 4828 4925 4532 -111 276 20 C ATOM 1036 CD ARG A 143 -17.321 30.554 -30.765 1.00 39.80 C ANISOU 1036 CD ARG A 143 5186 5145 4789 -93 261 65 C ATOM 1037 NE ARG A 143 -17.689 29.246 -31.319 1.00 40.17 N ANISOU 1037 NE ARG A 143 5246 5208 4807 -64 216 92 N ATOM 1038 CZ ARG A 143 -16.865 28.435 -32.050 1.00 43.50 C ANISOU 1038 CZ ARG A 143 5689 5645 5194 -67 228 96 C ATOM 1039 NH1 ARG A 143 -15.618 28.776 -32.291 1.00 43.52 N ANISOU 1039 NH1 ARG A 143 5693 5656 5186 -96 282 75 N ATOM 1040 NH2 ARG A 143 -17.275 27.253 -32.484 1.00 44.34 N ANISOU 1040 NH2 ARG A 143 5811 5761 5275 -44 192 118 N ATOM 1041 N LEU A 144 -19.405 29.866 -25.412 1.00 30.24 N ANISOU 1041 N LEU A 144 3731 4077 3678 -66 185 -16 N ATOM 1042 CA LEU A 144 -20.564 30.197 -24.557 1.00 29.31 C ANISOU 1042 CA LEU A 144 3591 3950 3596 -54 164 -19 C ATOM 1043 C LEU A 144 -20.057 30.759 -23.241 1.00 27.89 C ANISOU 1043 C LEU A 144 3357 3806 3431 -83 197 -65 C ATOM 1044 O LEU A 144 -20.621 31.719 -22.699 1.00 28.63 O ANISOU 1044 O LEU A 144 3445 3872 3559 -93 211 -80 O ATOM 1045 CB LEU A 144 -21.434 28.957 -24.342 1.00 28.09 C ANISOU 1045 CB LEU A 144 3423 3815 3434 -24 116 0 C ATOM 1046 CG LEU A 144 -22.590 29.195 -23.358 1.00 28.84 C ANISOU 1046 CG LEU A 144 3484 3907 3563 -15 98 -9 C ATOM 1047 CD1 LEU A 144 -23.519 30.317 -23.823 1.00 32.07 C ANISOU 1047 CD1 LEU A 144 3920 4259 4004 -5 94 6 C ATOM 1048 CD2 LEU A 144 -23.423 27.929 -23.205 1.00 31.24 C ANISOU 1048 CD2 LEU A 144 3780 4231 3859 7 58 5 C ATOM 1049 N ALA A 145 -18.983 30.163 -22.731 1.00 29.05 N ANISOU 1049 N ALA A 145 3465 4020 3552 -95 210 -90 N ATOM 1050 CA ALA A 145 -18.385 30.606 -21.454 1.00 28.49 C ANISOU 1050 CA ALA A 145 3335 4003 3485 -124 237 -139 C ATOM 1051 C ALA A 145 -17.891 32.048 -21.598 1.00 29.31 C ANISOU 1051 C ALA A 145 3453 4076 3608 -173 290 -171 C ATOM 1052 O ALA A 145 -18.083 32.832 -20.659 1.00 29.03 O ANISOU 1052 O ALA A 145 3391 4043 3595 -199 312 -205 O ATOM 1053 CB ALA A 145 -17.283 29.659 -21.063 1.00 28.16 C ANISOU 1053 CB ALA A 145 3251 4045 3404 -118 238 -154 C ATOM 1054 N ALA A 146 -17.332 32.376 -22.768 1.00 31.16 N ANISOU 1054 N ALA A 146 3733 4274 3832 -186 314 -158 N ATOM 1055 CA ALA A 146 -16.861 33.749 -23.064 1.00 34.16 C ANISOU 1055 CA ALA A 146 4142 4609 4227 -234 374 -185 C ATOM 1056 C ALA A 146 -18.041 34.723 -23.193 1.00 36.92 C ANISOU 1056 C ALA A 146 4540 4873 4615 -223 380 -165 C ATOM 1057 O ALA A 146 -18.052 35.781 -22.515 1.00 35.14 O ANISOU 1057 O ALA A 146 4308 4628 4415 -258 424 -202 O ATOM 1058 CB ALA A 146 -15.990 33.703 -24.306 1.00 35.46 C ANISOU 1058 CB ALA A 146 4347 4757 4366 -247 398 -173 C ATOM 1059 N GLU A 147 -19.037 34.371 -24.013 1.00 37.11 N ANISOU 1059 N GLU A 147 4607 4849 4642 -173 336 -110 N ATOM 1060 CA GLU A 147 -20.247 35.228 -24.220 1.00 37.71 C ANISOU 1060 CA GLU A 147 4725 4849 4750 -146 334 -83 C ATOM 1061 C GLU A 147 -20.914 35.511 -22.875 1.00 40.44 C ANISOU 1061 C GLU A 147 5024 5211 5130 -147 332 -111 C ATOM 1062 O GLU A 147 -21.325 36.659 -22.591 1.00 36.04 O ANISOU 1062 O GLU A 147 4487 4600 4603 -156 371 -121 O ATOM 1063 CB GLU A 147 -21.162 34.503 -25.194 1.00 40.67 C ANISOU 1063 CB GLU A 147 5133 5204 5113 -90 274 -25 C ATOM 1064 CG GLU A 147 -22.463 35.218 -25.541 1.00 49.36 C ANISOU 1064 CG GLU A 147 6270 6242 6240 -48 259 9 C ATOM 1065 CD GLU A 147 -23.314 34.380 -26.505 1.00 58.68 C ANISOU 1065 CD GLU A 147 7472 7424 7401 0 193 59 C ATOM 1066 OE1 GLU A 147 -22.865 33.238 -26.910 1.00 60.87 O ANISOU 1066 OE1 GLU A 147 7741 7741 7644 -3 166 65 O ATOM 1067 OE2 GLU A 147 -24.445 34.823 -26.844 1.00 61.14 O ANISOU 1067 OE2 GLU A 147 7803 7699 7727 43 169 91 O ATOM 1068 N GLU A 148 -20.992 34.519 -21.994 1.00 35.85 N ANISOU 1068 N GLU A 148 4381 4698 4540 -141 296 -124 N ATOM 1069 CA GLU A 148 -21.721 34.694 -20.720 1.00 33.86 C ANISOU 1069 CA GLU A 148 4087 4461 4317 -140 292 -148 C ATOM 1070 C GLU A 148 -20.825 35.132 -19.569 1.00 34.38 C ANISOU 1070 C GLU A 148 4106 4575 4380 -193 336 -210 C ATOM 1071 O GLU A 148 -21.351 35.188 -18.457 1.00 36.22 O ANISOU 1071 O GLU A 148 4302 4828 4630 -195 333 -232 O ATOM 1072 CB GLU A 148 -22.488 33.407 -20.420 1.00 33.73 C ANISOU 1072 CB GLU A 148 4039 4483 4292 -101 231 -125 C ATOM 1073 CG GLU A 148 -23.633 33.255 -21.399 1.00 34.65 C ANISOU 1073 CG GLU A 148 4193 4550 4419 -55 191 -75 C ATOM 1074 CD GLU A 148 -24.787 34.271 -21.282 1.00 39.93 C ANISOU 1074 CD GLU A 148 4877 5163 5131 -33 197 -65 C ATOM 1075 OE1 GLU A 148 -24.780 35.038 -20.297 1.00 40.38 O ANISOU 1075 OE1 GLU A 148 4912 5215 5214 -56 235 -100 O ATOM 1076 OE2 GLU A 148 -25.747 34.234 -22.122 1.00 43.18 O ANISOU 1076 OE2 GLU A 148 5314 5542 5548 8 162 -24 O ATOM 1077 N GLN A 149 -19.520 35.271 -19.813 1.00 35.03 N ANISOU 1077 N GLN A 149 4184 4687 4436 -234 371 -237 N ATOM 1078 CA GLN A 149 -18.525 35.693 -18.814 1.00 35.33 C ANISOU 1078 CA GLN A 149 4172 4787 4464 -293 413 -303 C ATOM 1079 C GLN A 149 -18.620 34.755 -17.611 1.00 33.09 C ANISOU 1079 C GLN A 149 3820 4588 4163 -277 375 -318 C ATOM 1080 O GLN A 149 -18.767 35.208 -16.479 1.00 34.72 O ANISOU 1080 O GLN A 149 3993 4817 4380 -303 392 -358 O ATOM 1081 CB GLN A 149 -18.765 37.174 -18.504 1.00 38.33 C ANISOU 1081 CB GLN A 149 4580 5104 4879 -334 474 -336 C ATOM 1082 CG GLN A 149 -18.634 38.100 -19.716 1.00 44.13 C ANISOU 1082 CG GLN A 149 5393 5748 5624 -345 520 -317 C ATOM 1083 CD GLN A 149 -18.890 39.513 -19.216 1.00 48.95 C ANISOU 1083 CD GLN A 149 6032 6296 6270 -384 588 -353 C ATOM 1084 OE1 GLN A 149 -17.984 40.158 -18.768 1.00 57.59 O ANISOU 1084 OE1 GLN A 149 7112 7412 7357 -454 648 -414 O ATOM 1085 NE2 GLN A 149 -20.138 39.946 -19.125 1.00 50.36 N ANISOU 1085 NE2 GLN A 149 6241 6407 6483 -341 581 -322 N ATOM 1086 N LEU A 150 -18.465 33.454 -17.833 1.00 30.60 N ANISOU 1086 N LEU A 150 3490 4319 3817 -237 329 -287 N ATOM 1087 CA LEU A 150 -18.504 32.471 -16.746 1.00 30.23 C ANISOU 1087 CA LEU A 150 3388 4348 3747 -214 297 -294 C ATOM 1088 C LEU A 150 -17.115 32.393 -16.080 1.00 32.39 C ANISOU 1088 C LEU A 150 3602 4722 3981 -247 318 -343 C ATOM 1089 O LEU A 150 -16.169 33.003 -16.629 1.00 31.01 O ANISOU 1089 O LEU A 150 3430 4551 3798 -287 355 -368 O ATOM 1090 CB LEU A 150 -18.936 31.125 -17.308 1.00 30.22 C ANISOU 1090 CB LEU A 150 3406 4346 3729 -157 248 -240 C ATOM 1091 CG LEU A 150 -20.247 31.081 -18.083 1.00 28.84 C ANISOU 1091 CG LEU A 150 3282 4089 3586 -127 221 -195 C ATOM 1092 CD1 LEU A 150 -20.552 29.627 -18.503 1.00 28.37 C ANISOU 1092 CD1 LEU A 150 3234 4042 3501 -82 179 -154 C ATOM 1093 CD2 LEU A 150 -21.383 31.685 -17.272 1.00 29.84 C ANISOU 1093 CD2 LEU A 150 3399 4185 3751 -128 221 -206 C ATOM 1094 N ALA A 151 -17.022 31.685 -14.946 1.00 29.65 N ANISOU 1094 N ALA A 151 3205 4454 3607 -229 296 -356 N ATOM 1095 CA ALA A 151 -15.812 31.497 -14.120 1.00 31.48 C ANISOU 1095 CA ALA A 151 3367 4799 3792 -247 305 -401 C ATOM 1096 C ALA A 151 -14.913 30.464 -14.779 1.00 33.26 C ANISOU 1096 C ALA A 151 3585 5075 3978 -209 289 -374 C ATOM 1097 O ALA A 151 -13.643 30.543 -14.694 1.00 30.79 O ANISOU 1097 O ALA A 151 3222 4844 3631 -231 307 -411 O ATOM 1098 CB ALA A 151 -16.226 31.075 -12.732 1.00 31.71 C ANISOU 1098 CB ALA A 151 3358 4884 3806 -229 285 -413 C ATOM 1099 N ALA A 152 -15.487 29.449 -15.420 1.00 28.61 N ANISOU 1099 N ALA A 152 3038 4444 3389 -152 256 -315 N ATOM 1100 CA ALA A 152 -14.643 28.347 -15.962 1.00 26.40 C ANISOU 1100 CA ALA A 152 2753 4211 3067 -109 244 -289 C ATOM 1101 C ALA A 152 -15.440 27.484 -16.913 1.00 27.07 C ANISOU 1101 C ALA A 152 2902 4220 3162 -65 219 -228 C ATOM 1102 O ALA A 152 -16.708 27.567 -16.906 1.00 25.72 O ANISOU 1102 O ALA A 152 2767 3981 3025 -60 203 -208 O ATOM 1103 CB ALA A 152 -14.131 27.504 -14.821 1.00 28.22 C ANISOU 1103 CB ALA A 152 2926 4545 3250 -71 228 -297 C ATOM 1104 N PHE A 153 -14.709 26.744 -17.736 1.00 26.76 N ANISOU 1104 N PHE A 153 2876 4196 3095 -37 220 -205 N ATOM 1105 CA PHE A 153 -15.248 25.789 -18.730 1.00 24.29 C ANISOU 1105 CA PHE A 153 2625 3822 2781 1 201 -152 C ATOM 1106 C PHE A 153 -14.398 24.538 -18.695 1.00 27.38 C ANISOU 1106 C PHE A 153 3004 4275 3124 53 200 -134 C ATOM 1107 O PHE A 153 -13.157 24.662 -18.803 1.00 26.43 O ANISOU 1107 O PHE A 153 2844 4219 2979 49 220 -156 O ATOM 1108 CB PHE A 153 -15.229 26.408 -20.118 1.00 25.72 C ANISOU 1108 CB PHE A 153 2856 3935 2982 -27 214 -142 C ATOM 1109 CG PHE A 153 -15.605 25.406 -21.177 1.00 26.17 C ANISOU 1109 CG PHE A 153 2971 3943 3028 7 197 -95 C ATOM 1110 CD1 PHE A 153 -16.845 24.735 -21.137 1.00 26.83 C ANISOU 1110 CD1 PHE A 153 3090 3982 3122 32 167 -64 C ATOM 1111 CD2 PHE A 153 -14.739 25.112 -22.187 1.00 27.73 C ANISOU 1111 CD2 PHE A 153 3189 4141 3203 12 214 -84 C ATOM 1112 CE1 PHE A 153 -17.150 23.740 -22.062 1.00 26.24 C ANISOU 1112 CE1 PHE A 153 3068 3870 3032 57 155 -27 C ATOM 1113 CE2 PHE A 153 -15.062 24.131 -23.121 1.00 28.52 C ANISOU 1113 CE2 PHE A 153 3346 4200 3289 41 202 -44 C ATOM 1114 CZ PHE A 153 -16.306 23.518 -23.104 1.00 26.64 C ANISOU 1114 CZ PHE A 153 3144 3917 3060 60 172 -17 C ATOM 1115 N TYR A 154 -15.050 23.387 -18.723 1.00 26.20 N ANISOU 1115 N TYR A 154 2893 4098 2964 99 182 -94 N ATOM 1116 CA TYR A 154 -14.374 22.069 -18.768 1.00 28.58 C ANISOU 1116 CA TYR A 154 3200 4439 3219 160 187 -67 C ATOM 1117 C TYR A 154 -15.169 21.125 -19.663 1.00 26.59 C ANISOU 1117 C TYR A 154 3025 4108 2970 181 179 -24 C ATOM 1118 O TYR A 154 -16.407 21.178 -19.637 1.00 26.37 O ANISOU 1118 O TYR A 154 3027 4020 2970 165 162 -15 O ATOM 1119 CB TYR A 154 -14.257 21.387 -17.406 1.00 29.55 C ANISOU 1119 CB TYR A 154 3287 4631 3309 206 182 -66 C ATOM 1120 CG TYR A 154 -13.664 22.257 -16.315 1.00 29.70 C ANISOU 1120 CG TYR A 154 3227 4736 3319 182 184 -112 C ATOM 1121 CD1 TYR A 154 -14.479 23.148 -15.636 1.00 28.90 C ANISOU 1121 CD1 TYR A 154 3113 4615 3252 138 176 -139 C ATOM 1122 CD2 TYR A 154 -12.313 22.225 -16.015 1.00 31.76 C ANISOU 1122 CD2 TYR A 154 3426 5099 3540 201 195 -134 C ATOM 1123 CE1 TYR A 154 -13.966 23.929 -14.600 1.00 29.40 C ANISOU 1123 CE1 TYR A 154 3108 4757 3305 111 181 -186 C ATOM 1124 CE2 TYR A 154 -11.793 23.007 -14.981 1.00 32.52 C ANISOU 1124 CE2 TYR A 154 3447 5285 3625 174 196 -183 C ATOM 1125 CZ TYR A 154 -12.611 23.885 -14.310 1.00 29.25 C ANISOU 1125 CZ TYR A 154 3026 4844 3242 124 190 -211 C ATOM 1126 OH TYR A 154 -12.173 24.674 -13.261 1.00 31.89 O ANISOU 1126 OH TYR A 154 3290 5261 3563 89 194 -264 O ATOM 1127 N GLU A 155 -14.467 20.163 -20.263 1.00 24.96 N ANISOU 1127 N GLU A 155 2843 3910 2730 222 195 0 N ATOM 1128 CA GLU A 155 -15.110 18.929 -20.752 1.00 26.26 C ANISOU 1128 CA GLU A 155 3077 4017 2882 253 196 38 C ATOM 1129 C GLU A 155 -14.765 17.828 -19.757 1.00 27.74 C ANISOU 1129 C GLU A 155 3256 4253 3029 318 208 54 C ATOM 1130 O GLU A 155 -13.573 17.780 -19.297 1.00 29.74 O ANISOU 1130 O GLU A 155 3457 4589 3250 354 221 47 O ATOM 1131 CB GLU A 155 -14.703 18.601 -22.187 1.00 26.93 C ANISOU 1131 CB GLU A 155 3211 4062 2958 251 210 55 C ATOM 1132 CG GLU A 155 -15.385 19.507 -23.189 1.00 27.42 C ANISOU 1132 CG GLU A 155 3302 4059 3055 194 194 49 C ATOM 1133 CD GLU A 155 -15.166 19.056 -24.607 1.00 30.53 C ANISOU 1133 CD GLU A 155 3756 4407 3435 192 206 69 C ATOM 1134 OE1 GLU A 155 -14.288 18.179 -24.833 1.00 29.57 O ANISOU 1134 OE1 GLU A 155 3645 4308 3279 232 233 82 O ATOM 1135 OE2 GLU A 155 -15.788 19.673 -25.490 1.00 29.06 O ANISOU 1135 OE2 GLU A 155 3602 4168 3269 153 191 70 O ATOM 1136 N ALA A 156 -15.710 16.929 -19.478 1.00 26.52 N ANISOU 1136 N ALA A 156 3151 4052 2871 336 209 77 N ATOM 1137 CA ALA A 156 -15.543 15.892 -18.451 1.00 26.74 C ANISOU 1137 CA ALA A 156 3185 4114 2860 400 225 97 C ATOM 1138 C ALA A 156 -16.228 14.620 -18.901 1.00 27.14 C ANISOU 1138 C ALA A 156 3321 4090 2899 419 247 129 C ATOM 1139 O ALA A 156 -16.979 14.633 -19.836 1.00 25.33 O ANISOU 1139 O ALA A 156 3135 3792 2694 376 240 129 O ATOM 1140 CB ALA A 156 -16.052 16.371 -17.128 1.00 26.16 C ANISOU 1140 CB ALA A 156 3069 4075 2796 390 209 79 C ATOM 1141 N SER A 157 -15.976 13.544 -18.201 1.00 27.46 N ANISOU 1141 N SER A 157 3386 4146 2898 484 274 155 N ATOM 1142 CA SER A 157 -16.694 12.251 -18.277 1.00 25.95 C ANISOU 1142 CA SER A 157 3282 3885 2691 504 306 182 C ATOM 1143 C SER A 157 -16.957 11.818 -16.830 1.00 27.77 C ANISOU 1143 C SER A 157 3510 4143 2899 545 317 192 C ATOM 1144 O SER A 157 -16.000 11.364 -16.100 1.00 28.46 O ANISOU 1144 O SER A 157 3579 4295 2938 623 335 212 O ATOM 1145 CB SER A 157 -15.998 11.158 -19.059 1.00 27.12 C ANISOU 1145 CB SER A 157 3492 4008 2804 554 348 212 C ATOM 1146 OG SER A 157 -16.748 9.933 -18.982 1.00 27.37 O ANISOU 1146 OG SER A 157 3612 3967 2819 567 387 234 O ATOM 1147 N ALA A 158 -18.216 11.888 -16.414 1.00 26.36 N ANISOU 1147 N ALA A 158 3348 3919 2746 499 310 179 N ATOM 1148 CA ALA A 158 -18.647 11.299 -15.114 1.00 28.07 C ANISOU 1148 CA ALA A 158 3583 4142 2939 532 330 191 C ATOM 1149 C ALA A 158 -18.408 9.788 -15.200 1.00 31.95 C ANISOU 1149 C ALA A 158 4162 4592 3384 596 387 232 C ATOM 1150 O ALA A 158 -17.995 9.170 -14.181 1.00 34.57 O ANISOU 1150 O ALA A 158 4506 4957 3669 668 413 257 O ATOM 1151 CB ALA A 158 -20.076 11.589 -14.791 1.00 28.74 C ANISOU 1151 CB ALA A 158 3675 4179 3065 466 319 168 C ATOM 1152 N LYS A 159 -18.631 9.199 -16.370 1.00 32.20 N ANISOU 1152 N LYS A 159 4259 4553 3423 574 410 238 N ATOM 1153 CA LYS A 159 -18.462 7.744 -16.485 1.00 34.23 C ANISOU 1153 CA LYS A 159 4611 4758 3637 629 474 274 C ATOM 1154 C LYS A 159 -17.016 7.307 -16.270 1.00 35.55 C ANISOU 1154 C LYS A 159 4770 4985 3753 732 496 309 C ATOM 1155 O LYS A 159 -16.809 6.352 -15.571 1.00 36.33 O ANISOU 1155 O LYS A 159 4919 5076 3806 805 542 343 O ATOM 1156 CB LYS A 159 -18.918 7.284 -17.848 1.00 33.84 C ANISOU 1156 CB LYS A 159 4627 4627 3604 577 493 267 C ATOM 1157 CG LYS A 159 -18.824 5.790 -17.975 1.00 37.63 C ANISOU 1157 CG LYS A 159 5215 5042 4042 625 568 299 C ATOM 1158 CD LYS A 159 -19.288 5.383 -19.293 1.00 40.11 C ANISOU 1158 CD LYS A 159 5589 5280 4368 565 586 285 C ATOM 1159 CE LYS A 159 -18.733 4.023 -19.599 1.00 49.75 C ANISOU 1159 CE LYS A 159 6910 6449 5544 627 664 319 C ATOM 1160 NZ LYS A 159 -19.293 3.609 -20.892 1.00 53.77 N ANISOU 1160 NZ LYS A 159 7483 6882 6064 555 684 297 N ATOM 1161 N ASP A 160 -16.054 7.946 -16.904 1.00 36.38 N ANISOU 1161 N ASP A 160 4816 5144 3863 740 469 302 N ATOM 1162 CA ASP A 160 -14.640 7.556 -16.820 1.00 37.80 C ANISOU 1162 CA ASP A 160 4977 5389 3995 837 489 331 C ATOM 1163 C ASP A 160 -13.957 8.314 -15.684 1.00 37.48 C ANISOU 1163 C ASP A 160 4836 5468 3937 875 452 322 C ATOM 1164 O ASP A 160 -12.731 8.166 -15.545 1.00 41.46 O ANISOU 1164 O ASP A 160 5300 6051 4401 953 457 339 O ATOM 1165 CB ASP A 160 -13.950 7.900 -18.136 1.00 39.50 C ANISOU 1165 CB ASP A 160 5175 5605 4225 816 482 320 C ATOM 1166 CG ASP A 160 -14.347 7.050 -19.333 1.00 43.44 C ANISOU 1166 CG ASP A 160 5774 6001 4729 792 524 330 C ATOM 1167 OD1 ASP A 160 -15.038 6.012 -19.137 1.00 43.44 O ANISOU 1167 OD1 ASP A 160 5863 5926 4713 802 570 349 O ATOM 1168 OD2 ASP A 160 -13.907 7.457 -20.475 1.00 47.83 O ANISOU 1168 OD2 ASP A 160 6318 6554 5302 760 514 317 O ATOM 1169 N ASN A 161 -14.670 9.148 -14.948 1.00 34.54 N ANISOU 1169 N ASN A 161 4417 5113 3590 819 414 293 N ATOM 1170 CA ASN A 161 -14.082 10.004 -13.884 1.00 38.71 C ANISOU 1170 CA ASN A 161 4846 5756 4103 838 376 274 C ATOM 1171 C ASN A 161 -12.933 10.845 -14.454 1.00 37.74 C ANISOU 1171 C ASN A 161 4638 5713 3985 832 350 251 C ATOM 1172 O ASN A 161 -11.803 10.868 -13.885 1.00 37.80 O ANISOU 1172 O ASN A 161 4583 5830 3949 900 345 256 O ATOM 1173 CB ASN A 161 -13.530 9.140 -12.739 1.00 41.48 C ANISOU 1173 CB ASN A 161 5209 6165 4386 947 402 314 C ATOM 1174 CG ASN A 161 -13.139 9.965 -11.543 1.00 44.76 C ANISOU 1174 CG ASN A 161 5529 6697 4781 956 362 290 C ATOM 1175 OD1 ASN A 161 -13.547 11.114 -11.386 1.00 43.45 O ANISOU 1175 OD1 ASN A 161 5303 6548 4656 874 323 245 O ATOM 1176 ND2 ASN A 161 -12.369 9.345 -10.666 1.00 47.45 N ANISOU 1176 ND2 ASN A 161 5859 7116 5053 1061 375 323 N ATOM 1177 N ASN A 162 -13.162 11.463 -15.589 1.00 32.81 N ANISOU 1177 N ASN A 162 4014 5041 3409 757 337 227 N ATOM 1178 CA ASN A 162 -12.150 12.322 -16.252 1.00 33.90 C ANISOU 1178 CA ASN A 162 4081 5240 3557 736 319 200 C ATOM 1179 C ASN A 162 -12.524 13.789 -16.048 1.00 33.05 C ANISOU 1179 C ASN A 162 3906 5155 3495 648 279 150 C ATOM 1180 O ASN A 162 -13.632 14.198 -16.464 1.00 31.71 O ANISOU 1180 O ASN A 162 3770 4904 3371 578 266 138 O ATOM 1181 CB ASN A 162 -12.011 11.856 -17.682 1.00 39.10 C ANISOU 1181 CB ASN A 162 4800 5828 4227 728 344 214 C ATOM 1182 CG ASN A 162 -10.934 12.620 -18.418 1.00 45.82 C ANISOU 1182 CG ASN A 162 5588 6735 5084 711 336 190 C ATOM 1183 OD1 ASN A 162 -10.570 13.733 -18.037 1.00 47.35 O ANISOU 1183 OD1 ASN A 162 5698 6999 5292 673 308 152 O ATOM 1184 ND2 ASN A 162 -10.482 12.066 -19.537 1.00 54.57 N ANISOU 1184 ND2 ASN A 162 6742 7805 6187 728 366 207 N ATOM 1185 N ASN A 163 -11.725 14.538 -15.277 1.00 34.16 N ANISOU 1185 N ASN A 163 3955 5405 3619 654 259 122 N ATOM 1186 CA ASN A 163 -11.897 16.004 -15.116 1.00 36.85 C ANISOU 1186 CA ASN A 163 4231 5769 3999 569 230 69 C ATOM 1187 C ASN A 163 -13.065 16.399 -14.227 1.00 36.43 C ANISOU 1187 C ASN A 163 4184 5687 3971 529 213 56 C ATOM 1188 O ASN A 163 -13.383 17.568 -14.209 1.00 42.58 O ANISOU 1188 O ASN A 163 4926 6461 4788 458 196 17 O ATOM 1189 CB ASN A 163 -12.136 16.704 -16.472 1.00 40.92 C ANISOU 1189 CB ASN A 163 4768 6212 4565 495 229 53 C ATOM 1190 CG ASN A 163 -10.988 17.612 -16.816 1.00 45.80 C ANISOU 1190 CG ASN A 163 5315 6904 5184 468 230 16 C ATOM 1191 OD1 ASN A 163 -9.917 17.409 -16.277 1.00 53.15 O ANISOU 1191 OD1 ASN A 163 6185 7937 6071 517 234 10 O ATOM 1192 ND2 ASN A 163 -11.185 18.606 -17.672 1.00 48.00 N ANISOU 1192 ND2 ASN A 163 5596 7134 5506 393 227 -8 N ATOM 1193 N VAL A 164 -13.632 15.513 -13.446 1.00 31.91 N ANISOU 1193 N VAL A 164 3653 5097 3373 575 222 86 N ATOM 1194 CA VAL A 164 -14.752 15.893 -12.544 1.00 32.59 C ANISOU 1194 CA VAL A 164 3742 5157 3482 537 209 70 C ATOM 1195 C VAL A 164 -14.221 16.536 -11.240 1.00 35.97 C ANISOU 1195 C VAL A 164 4088 5696 3881 544 193 40 C ATOM 1196 O VAL A 164 -14.684 17.634 -10.872 1.00 33.20 O ANISOU 1196 O VAL A 164 3699 5348 3566 476 176 -1 O ATOM 1197 CB VAL A 164 -15.609 14.647 -12.261 1.00 34.01 C ANISOU 1197 CB VAL A 164 4006 5268 3646 576 234 111 C ATOM 1198 CG1 VAL A 164 -16.608 14.892 -11.168 1.00 34.68 C ANISOU 1198 CG1 VAL A 164 4090 5343 3743 550 227 97 C ATOM 1199 CG2 VAL A 164 -16.292 14.137 -13.527 1.00 34.98 C ANISOU 1199 CG2 VAL A 164 4205 5282 3801 549 248 129 C ATOM 1200 N GLU A 165 -13.282 15.855 -10.557 1.00 33.29 N ANISOU 1200 N GLU A 165 3725 5448 3475 627 199 60 N ATOM 1201 CA GLU A 165 -12.731 16.380 -9.290 1.00 34.22 C ANISOU 1201 CA GLU A 165 3764 5685 3553 638 181 30 C ATOM 1202 C GLU A 165 -12.243 17.822 -9.514 1.00 34.66 C ANISOU 1202 C GLU A 165 3736 5791 3640 557 163 -31 C ATOM 1203 O GLU A 165 -12.501 18.724 -8.651 1.00 32.96 O ANISOU 1203 O GLU A 165 3474 5614 3433 506 149 -75 O ATOM 1204 CB GLU A 165 -11.608 15.446 -8.805 1.00 40.22 C ANISOU 1204 CB GLU A 165 4502 6545 4233 748 188 64 C ATOM 1205 CG GLU A 165 -11.210 15.739 -7.375 1.00 46.47 C ANISOU 1205 CG GLU A 165 5226 7460 4970 773 169 43 C ATOM 1206 CD GLU A 165 -10.106 14.832 -6.885 1.00 53.22 C ANISOU 1206 CD GLU A 165 6056 8424 5740 892 172 79 C ATOM 1207 OE1 GLU A 165 -9.231 14.426 -7.707 0.70 54.00 O ANISOU 1207 OE1 GLU A 165 6145 8544 5827 938 182 97 O ATOM 1208 OE2 GLU A 165 -10.134 14.531 -5.693 0.70 57.15 O ANISOU 1208 OE2 GLU A 165 6545 8984 6182 942 165 91 O ATOM 1209 N GLN A 166 -11.516 18.061 -10.613 1.00 34.57 N ANISOU 1209 N GLN A 166 3709 5781 3645 542 168 -39 N ATOM 1210 CA GLN A 166 -10.857 19.371 -10.860 1.00 37.62 C ANISOU 1210 CA GLN A 166 4018 6221 4052 467 161 -100 C ATOM 1211 C GLN A 166 -11.919 20.470 -10.878 1.00 34.18 C ANISOU 1211 C GLN A 166 3597 5706 3680 373 157 -133 C ATOM 1212 O GLN A 166 -11.659 21.587 -10.437 1.00 35.48 O ANISOU 1212 O GLN A 166 3702 5922 3855 312 154 -188 O ATOM 1213 CB GLN A 166 -10.074 19.317 -12.183 1.00 43.52 C ANISOU 1213 CB GLN A 166 4768 6956 4810 467 176 -95 C ATOM 1214 CG GLN A 166 -9.089 20.478 -12.376 1.00 55.82 C ANISOU 1214 CG GLN A 166 6242 8593 6374 404 178 -157 C ATOM 1215 CD GLN A 166 -7.990 20.536 -11.322 1.00 63.31 C ANISOU 1215 CD GLN A 166 7090 9703 7259 437 168 -188 C ATOM 1216 OE1 GLN A 166 -7.841 21.513 -10.576 1.00 68.86 O ANISOU 1216 OE1 GLN A 166 7728 10473 7961 377 161 -246 O ATOM 1217 NE2 GLN A 166 -7.222 19.460 -11.215 1.00 65.52 N ANISOU 1217 NE2 GLN A 166 7357 10054 7483 537 169 -151 N ATOM 1218 N VAL A 167 -13.080 20.204 -11.470 1.00 30.57 N ANISOU 1218 N VAL A 167 3219 5126 3267 359 160 -104 N ATOM 1219 CA VAL A 167 -14.164 21.215 -11.564 1.00 31.61 C ANISOU 1219 CA VAL A 167 3366 5179 3462 280 156 -130 C ATOM 1220 C VAL A 167 -14.475 21.749 -10.161 1.00 31.14 C ANISOU 1220 C VAL A 167 3265 5171 3393 260 149 -164 C ATOM 1221 O VAL A 167 -14.624 22.955 -9.998 1.00 32.83 O ANISOU 1221 O VAL A 167 3448 5384 3641 192 151 -210 O ATOM 1222 CB VAL A 167 -15.426 20.621 -12.197 1.00 31.15 C ANISOU 1222 CB VAL A 167 3391 5002 3439 283 155 -90 C ATOM 1223 CG1 VAL A 167 -16.562 21.650 -12.225 1.00 34.88 C ANISOU 1223 CG1 VAL A 167 3873 5404 3974 214 149 -115 C ATOM 1224 CG2 VAL A 167 -15.146 20.130 -13.619 1.00 32.19 C ANISOU 1224 CG2 VAL A 167 3568 5082 3578 296 163 -61 C ATOM 1225 N PHE A 168 -14.654 20.860 -9.225 1.00 33.49 N ANISOU 1225 N PHE A 168 3573 5501 3648 318 145 -138 N ATOM 1226 CA PHE A 168 -15.050 21.238 -7.824 1.00 31.51 C ANISOU 1226 CA PHE A 168 3292 5295 3382 304 140 -166 C ATOM 1227 C PHE A 168 -13.879 21.851 -7.052 1.00 36.41 C ANISOU 1227 C PHE A 168 3824 6052 3957 296 134 -213 C ATOM 1228 O PHE A 168 -14.112 22.846 -6.364 1.00 36.42 O ANISOU 1228 O PHE A 168 3788 6074 3972 235 134 -263 O ATOM 1229 CB PHE A 168 -15.627 20.009 -7.131 1.00 32.74 C ANISOU 1229 CB PHE A 168 3500 5436 3504 371 144 -119 C ATOM 1230 CG PHE A 168 -16.989 19.597 -7.641 1.00 31.65 C ANISOU 1230 CG PHE A 168 3440 5169 3416 356 153 -91 C ATOM 1231 CD1 PHE A 168 -18.129 20.212 -7.157 1.00 32.08 C ANISOU 1231 CD1 PHE A 168 3501 5174 3514 303 154 -114 C ATOM 1232 CD2 PHE A 168 -17.152 18.560 -8.549 1.00 30.99 C ANISOU 1232 CD2 PHE A 168 3421 5020 3332 394 164 -44 C ATOM 1233 CE1 PHE A 168 -19.385 19.752 -7.532 1.00 32.06 C ANISOU 1233 CE1 PHE A 168 3561 5069 3551 292 161 -91 C ATOM 1234 CE2 PHE A 168 -18.410 18.159 -8.985 1.00 32.09 C ANISOU 1234 CE2 PHE A 168 3626 5053 3512 374 173 -25 C ATOM 1235 CZ PHE A 168 -19.531 18.728 -8.460 1.00 31.24 C ANISOU 1235 CZ PHE A 168 3517 4905 3445 324 170 -48 C ATOM 1236 N LEU A 169 -12.668 21.332 -7.213 1.00 36.72 N ANISOU 1236 N LEU A 169 3827 6181 3944 350 130 -203 N ATOM 1237 CA LEU A 169 -11.509 21.881 -6.475 1.00 37.67 C ANISOU 1237 CA LEU A 169 3851 6448 4013 342 121 -253 C ATOM 1238 C LEU A 169 -11.247 23.302 -6.972 1.00 40.88 C ANISOU 1238 C LEU A 169 4214 6849 4466 239 132 -318 C ATOM 1239 O LEU A 169 -11.012 24.171 -6.143 1.00 35.95 O ANISOU 1239 O LEU A 169 3532 6297 3830 186 132 -377 O ATOM 1240 CB LEU A 169 -10.341 20.931 -6.652 1.00 41.44 C ANISOU 1240 CB LEU A 169 4300 7017 4427 431 116 -221 C ATOM 1241 CG LEU A 169 -10.538 19.498 -6.164 1.00 41.58 C ANISOU 1241 CG LEU A 169 4370 7035 4393 542 115 -152 C ATOM 1242 CD1 LEU A 169 -9.225 18.726 -6.311 1.00 46.57 C ANISOU 1242 CD1 LEU A 169 4960 7774 4959 633 112 -128 C ATOM 1243 CD2 LEU A 169 -11.016 19.470 -4.712 1.00 46.84 C ANISOU 1243 CD2 LEU A 169 5028 7746 5020 554 104 -159 C ATOM 1244 N ASP A 170 -11.398 23.568 -8.271 1.00 34.78 N ANISOU 1244 N ASP A 170 3481 5983 3749 206 146 -309 N ATOM 1245 CA ASP A 170 -11.116 24.916 -8.833 1.00 36.17 C ANISOU 1245 CA ASP A 170 3629 6143 3968 111 165 -367 C ATOM 1246 C ASP A 170 -12.140 25.885 -8.281 1.00 37.58 C ANISOU 1246 C ASP A 170 3824 6261 4192 43 173 -399 C ATOM 1247 O ASP A 170 -11.873 27.140 -8.181 1.00 35.95 O ANISOU 1247 O ASP A 170 3581 6069 4006 -40 195 -463 O ATOM 1248 CB ASP A 170 -11.127 24.902 -10.378 1.00 35.19 C ANISOU 1248 CB ASP A 170 3557 5925 3888 101 179 -340 C ATOM 1249 CG ASP A 170 -9.882 24.287 -10.995 1.00 40.44 C ANISOU 1249 CG ASP A 170 4190 6661 4513 146 182 -328 C ATOM 1250 OD1 ASP A 170 -8.915 23.978 -10.190 1.00 40.49 O ANISOU 1250 OD1 ASP A 170 4121 6804 4457 183 172 -347 O ATOM 1251 OD2 ASP A 170 -9.885 24.074 -12.256 1.00 37.68 O ANISOU 1251 OD2 ASP A 170 3889 6235 4190 149 193 -299 O ATOM 1252 N LEU A 171 -13.325 25.369 -7.961 1.00 37.39 N ANISOU 1252 N LEU A 171 3857 6163 4186 72 163 -360 N ATOM 1253 CA LEU A 171 -14.362 26.219 -7.358 1.00 43.90 C ANISOU 1253 CA LEU A 171 4695 6931 5052 16 172 -388 C ATOM 1254 C LEU A 171 -13.868 26.779 -6.034 1.00 47.86 C ANISOU 1254 C LEU A 171 5129 7543 5513 -13 174 -446 C ATOM 1255 O LEU A 171 -14.128 27.982 -5.742 1.00 46.97 O ANISOU 1255 O LEU A 171 5001 7410 5432 -91 196 -501 O ATOM 1256 CB LEU A 171 -15.610 25.375 -7.063 1.00 48.84 C ANISOU 1256 CB LEU A 171 5381 7483 5691 61 160 -338 C ATOM 1257 CG LEU A 171 -16.715 25.401 -8.083 1.00 45.73 C ANISOU 1257 CG LEU A 171 5055 6956 5362 49 163 -305 C ATOM 1258 CD1 LEU A 171 -17.901 24.637 -7.544 1.00 43.99 C ANISOU 1258 CD1 LEU A 171 4878 6684 5148 82 156 -271 C ATOM 1259 CD2 LEU A 171 -17.151 26.804 -8.388 1.00 50.22 C ANISOU 1259 CD2 LEU A 171 5624 7465 5991 -25 181 -345 C ATOM 1260 N ALA A 172 -13.222 25.932 -5.229 1.00 56.28 N ANISOU 1260 N ALA A 172 6157 8719 6505 48 154 -435 N ATOM 1261 CA ALA A 172 -12.862 26.244 -3.829 1.00 60.26 C ANISOU 1261 CA ALA A 172 6600 9340 6956 33 149 -482 C ATOM 1262 C ALA A 172 -12.151 27.581 -3.826 1.00 63.31 C ANISOU 1262 C ALA A 172 6924 9778 7352 -60 170 -564 C ATOM 1263 O ALA A 172 -12.625 28.542 -3.131 1.00 59.45 O ANISOU 1263 O ALA A 172 6427 9276 6883 -130 189 -616 O ATOM 1264 CB ALA A 172 -11.942 25.196 -3.240 1.00 63.12 C ANISOU 1264 CB ALA A 172 6920 9831 7229 120 124 -458 C ATOM 1265 N ALA A 173 -11.025 27.572 -4.538 1.00 61.85 N ANISOU 1265 N ALA A 173 6697 9653 7148 -60 172 -576 N ATOM 1266 CA ALA A 173 -10.188 28.734 -4.874 1.00 65.44 C ANISOU 1266 CA ALA A 173 7098 10149 7615 -150 200 -651 C ATOM 1267 C ALA A 173 -11.069 29.985 -4.873 1.00 65.78 C ANISOU 1267 C ALA A 173 7180 10085 7726 -243 236 -691 C ATOM 1268 O ALA A 173 -10.818 30.894 -4.042 1.00 64.95 O ANISOU 1268 O ALA A 173 7029 10042 7607 -316 256 -765 O ATOM 1269 CB ALA A 173 -9.530 28.480 -6.221 1.00 63.12 C ANISOU 1269 CB ALA A 173 6813 9832 7337 -135 207 -626 C ATOM 1270 N LYS A 174 -12.125 29.984 -5.711 1.00 59.95 N ANISOU 1270 N LYS A 174 6526 9195 7056 -235 243 -642 N ATOM 1271 CA LYS A 174 -12.831 31.213 -6.128 1.00 55.14 C ANISOU 1271 CA LYS A 174 5961 8469 6518 -313 283 -671 C ATOM 1272 C LYS A 174 -13.829 31.589 -5.033 1.00 55.30 C ANISOU 1272 C LYS A 174 5995 8463 6553 -332 288 -688 C ATOM 1273 O LYS A 174 -14.367 32.702 -5.096 1.00 56.88 O ANISOU 1273 O LYS A 174 6222 8585 6805 -398 326 -723 O ATOM 1274 CB LYS A 174 -13.443 31.060 -7.531 1.00 56.12 C ANISOU 1274 CB LYS A 174 6161 8460 6700 -290 285 -612 C ATOM 1275 CG LYS A 174 -12.494 30.792 -8.708 1.00 57.03 C ANISOU 1275 CG LYS A 174 6273 8589 6807 -279 288 -597 C ATOM 1276 N LEU A 175 -14.110 30.686 -4.090 1.00 55.21 N ANISOU 1276 N LEU A 175 5972 8506 6497 -273 256 -663 N ATOM 1277 CA LEU A 175 -15.089 30.918 -2.998 1.00 59.18 C ANISOU 1277 CA LEU A 175 6489 8985 7008 -286 261 -676 C ATOM 1278 C LEU A 175 -14.454 31.893 -2.001 1.00 69.50 C ANISOU 1278 C LEU A 175 7734 10387 8283 -364 285 -764 C ATOM 1279 O LEU A 175 -13.178 32.016 -1.862 1.00 66.63 O ANISOU 1279 O LEU A 175 7301 10147 7865 -387 283 -810 O ATOM 1280 CB LEU A 175 -15.510 29.590 -2.343 1.00 57.49 C ANISOU 1280 CB LEU A 175 6290 8802 6753 -199 225 -619 C ATOM 1281 CG LEU A 175 -16.312 28.632 -3.226 1.00 58.62 C ANISOU 1281 CG LEU A 175 6500 8841 6930 -133 208 -539 C ATOM 1282 CD1 LEU A 175 -16.600 27.308 -2.541 1.00 60.18 C ANISOU 1282 CD1 LEU A 175 6715 9072 7079 -52 183 -489 C ATOM 1283 CD2 LEU A 175 -17.612 29.235 -3.685 1.00 56.36 C ANISOU 1283 CD2 LEU A 175 6270 8418 6726 -165 227 -531 C ATOM 1284 OXT LEU A 175 -15.248 32.605 -1.371 1.00 69.71 O ANISOU 1284 OXT LEU A 175 7781 10365 8340 -408 311 -795 O TER 1285 LEU A 175 HETATM 1286 PB GDP A 201 -29.234 14.212 -15.521 1.00 27.19 P ANISOU 1286 PB GDP A 201 3392 3763 3175 42 198 -17 P HETATM 1287 O1B GDP A 201 -30.594 14.006 -16.100 1.00 26.04 O ANISOU 1287 O1B GDP A 201 3247 3591 3057 -14 189 -42 O HETATM 1288 O2B GDP A 201 -29.146 14.149 -13.973 1.00 24.37 O ANISOU 1288 O2B GDP A 201 3024 3427 2808 65 226 -18 O HETATM 1289 O3B GDP A 201 -28.586 15.484 -16.071 1.00 24.36 O ANISOU 1289 O3B GDP A 201 2985 3432 2836 53 154 -13 O HETATM 1290 O3A GDP A 201 -28.288 13.033 -16.068 1.00 27.98 O ANISOU 1290 O3A GDP A 201 3565 3842 3222 73 234 11 O HETATM 1291 PA GDP A 201 -27.856 11.620 -15.462 1.00 29.02 P ANISOU 1291 PA GDP A 201 3771 3951 3303 110 297 33 P HETATM 1292 O1A GDP A 201 -29.044 10.989 -14.885 1.00 30.19 O ANISOU 1292 O1A GDP A 201 3944 4066 3459 70 330 12 O HETATM 1293 O2A GDP A 201 -26.711 11.798 -14.574 1.00 29.39 O ANISOU 1293 O2A GDP A 201 3802 4042 3320 174 305 56 O HETATM 1294 O5' GDP A 201 -27.288 10.845 -16.717 1.00 27.95 O ANISOU 1294 O5' GDP A 201 3697 3784 3138 116 313 51 O HETATM 1295 C5' GDP A 201 -28.140 10.717 -17.879 1.00 29.67 C ANISOU 1295 C5' GDP A 201 3929 3970 3374 56 298 30 C HETATM 1296 C4' GDP A 201 -27.671 9.465 -18.660 1.00 31.98 C ANISOU 1296 C4' GDP A 201 4309 4217 3623 65 345 46 C HETATM 1297 O4' GDP A 201 -26.373 9.676 -19.206 1.00 32.03 O ANISOU 1297 O4' GDP A 201 4317 4243 3608 114 336 74 O HETATM 1298 C3' GDP A 201 -27.536 8.251 -17.709 1.00 34.12 C ANISOU 1298 C3' GDP A 201 4649 4457 3857 97 419 62 C HETATM 1299 O3' GDP A 201 -27.911 7.087 -18.356 1.00 36.65 O ANISOU 1299 O3' GDP A 201 5051 4717 4154 65 469 55 O HETATM 1300 C2' GDP A 201 -26.100 8.171 -17.354 1.00 33.72 C ANISOU 1300 C2' GDP A 201 4606 4433 3771 182 432 102 C HETATM 1301 O2' GDP A 201 -25.685 6.847 -17.071 1.00 34.87 O ANISOU 1301 O2' GDP A 201 4841 4538 3869 226 505 129 O HETATM 1302 C1' GDP A 201 -25.459 8.736 -18.646 1.00 32.19 C ANISOU 1302 C1' GDP A 201 4391 4254 3584 179 392 105 C HETATM 1303 N9 GDP A 201 -24.161 9.425 -18.402 1.00 30.24 N ANISOU 1303 N9 GDP A 201 4097 4065 3327 241 369 128 N HETATM 1304 C8 GDP A 201 -23.972 10.380 -17.443 1.00 28.29 C ANISOU 1304 C8 GDP A 201 3777 3874 3097 258 337 123 C HETATM 1305 N7 GDP A 201 -22.761 10.839 -17.469 1.00 26.49 N ANISOU 1305 N7 GDP A 201 3514 3695 2853 305 324 138 N HETATM 1306 C5 GDP A 201 -22.117 10.147 -18.503 1.00 26.20 C ANISOU 1306 C5 GDP A 201 3531 3633 2791 324 348 157 C HETATM 1307 C6 GDP A 201 -20.816 10.097 -19.060 1.00 27.39 C ANISOU 1307 C6 GDP A 201 3681 3810 2916 372 355 177 C HETATM 1308 O6 GDP A 201 -19.920 10.875 -18.650 1.00 28.15 O ANISOU 1308 O6 GDP A 201 3711 3973 3010 403 332 178 O HETATM 1309 N1 GDP A 201 -20.634 9.318 -20.115 1.00 28.19 N ANISOU 1309 N1 GDP A 201 3848 3864 2999 371 384 188 N HETATM 1310 C2 GDP A 201 -21.554 8.410 -20.599 1.00 28.56 C ANISOU 1310 C2 GDP A 201 3970 3839 3042 331 415 182 C HETATM 1311 N2 GDP A 201 -21.247 7.625 -21.593 1.00 30.54 N ANISOU 1311 N2 GDP A 201 4287 4045 3269 333 450 192 N HETATM 1312 N3 GDP A 201 -22.798 8.390 -20.136 1.00 27.45 N ANISOU 1312 N3 GDP A 201 3831 3674 2924 280 410 160 N HETATM 1313 C4 GDP A 201 -23.078 9.241 -19.119 1.00 27.14 C ANISOU 1313 C4 GDP A 201 3722 3679 2909 279 377 149 C HETATM 1314 C1 GOL A 202 -16.040 5.944 -29.442 1.00 67.34 C ANISOU 1314 C1 GOL A 202 9193 8594 7797 389 592 243 C HETATM 1315 O1 GOL A 202 -15.472 7.250 -29.394 1.00 59.21 O ANISOU 1315 O1 GOL A 202 8071 7632 6791 391 539 238 O HETATM 1316 C2 GOL A 202 -17.273 5.836 -28.560 1.00 63.87 C ANISOU 1316 C2 GOL A 202 8752 8140 7375 356 574 231 C HETATM 1317 O2 GOL A 202 -16.919 5.661 -27.184 1.00 64.04 O ANISOU 1317 O2 GOL A 202 8740 8197 7393 426 588 252 O HETATM 1318 C3 GOL A 202 -18.184 7.034 -28.709 1.00 54.48 C ANISOU 1318 C3 GOL A 202 7501 6974 6223 284 498 204 C HETATM 1319 O3 GOL A 202 -19.569 6.729 -28.598 1.00 57.57 O ANISOU 1319 O3 GOL A 202 7920 7329 6624 222 488 182 O HETATM 1320 C ACT A 203 -15.494 31.870 -34.156 1.00 63.14 C ANISOU 1320 C ACT A 203 8333 7980 7675 -144 375 100 C HETATM 1321 O ACT A 203 -16.670 31.425 -34.198 1.00 55.88 O ANISOU 1321 O ACT A 203 7419 7057 6756 -103 313 132 O HETATM 1322 OXT ACT A 203 -15.237 33.068 -34.055 1.00 71.59 O ANISOU 1322 OXT ACT A 203 9424 9012 8763 -172 426 85 O HETATM 1323 CH3 ACT A 203 -14.277 30.937 -34.277 1.00 65.30 C ANISOU 1323 CH3 ACT A 203 8577 8308 7923 -163 397 77 C HETATM 1324 MG MG A 204 -30.586 14.033 -12.520 1.00 26.09 MG HETATM 1325 O HOH A 301 -0.984 27.961 2.286 1.00 40.68 O HETATM 1326 O HOH A 302 -12.346 21.205 -31.515 1.00 51.94 O HETATM 1327 O HOH A 303 -26.384 17.885 2.623 1.00 48.33 O HETATM 1328 O HOH A 304 -19.878 22.867 -33.875 1.00 46.25 O HETATM 1329 O HOH A 305 -27.685 29.240 -27.023 1.00 45.03 O HETATM 1330 O HOH A 306 -31.099 22.210 -31.495 1.00 45.37 O HETATM 1331 O HOH A 307 -22.470 35.781 -11.394 1.00 53.45 O HETATM 1332 O HOH A 308 -17.790 5.370 -22.949 1.00 42.04 O HETATM 1333 O HOH A 309 -7.988 27.615 8.714 1.00 46.54 O HETATM 1334 O HOH A 310 -31.952 11.930 -16.766 1.00 34.73 O HETATM 1335 O HOH A 311 -30.985 9.473 -15.938 1.00 34.98 O HETATM 1336 O HOH A 312 -32.031 13.706 -11.068 1.00 26.27 O HETATM 1337 O HOH A 313 -21.517 9.141 -11.489 1.00 33.21 O HETATM 1338 O HOH A 314 -11.903 17.570 -24.024 1.00 42.01 O HETATM 1339 O HOH A 315 -28.282 12.917 -7.429 1.00 31.23 O HETATM 1340 O HOH A 316 -12.342 13.382 -11.890 1.00 40.55 O HETATM 1341 O HOH A 317 -33.931 32.343 -5.954 1.00 52.05 O HETATM 1342 O HOH A 318 -33.007 16.111 -22.670 1.00 44.83 O HETATM 1343 O HOH A 319 -38.798 17.532 -20.375 1.00 43.91 O HETATM 1344 O HOH A 320 -18.151 20.834 -26.007 1.00 26.21 O HETATM 1345 O HOH A 321 -13.999 6.820 -24.673 1.00 51.26 O HETATM 1346 O HOH A 322 -30.354 15.936 -11.891 1.00 25.36 O HETATM 1347 O HOH A 323 -9.554 26.682 -30.678 1.00 39.56 O HETATM 1348 O HOH A 324 -9.820 28.126 -28.521 1.00 35.57 O HETATM 1349 O HOH A 325 -41.164 15.073 -9.701 1.00 58.15 O HETATM 1350 O HOH A 326 -23.413 28.834 -0.210 1.00 29.73 O HETATM 1351 O HOH A 327 -21.319 28.408 -28.513 1.00 34.20 O HETATM 1352 O HOH A 328 -37.716 29.840 -11.429 1.00 53.98 O HETATM 1353 O HOH A 329 -22.514 30.631 -27.358 1.00 59.72 O HETATM 1354 O HOH A 330 -33.184 28.058 -0.628 1.00 40.19 O HETATM 1355 O HOH A 331 -15.723 36.612 -21.505 1.00 44.50 O HETATM 1356 O HOH A 332 -25.770 11.948 -30.127 1.00 37.83 O HETATM 1357 O HOH A 333 -32.066 14.589 -13.811 1.00 27.34 O HETATM 1358 O HOH A 334 -15.502 35.530 -17.275 1.00 45.52 O HETATM 1359 O HOH A 335 -38.941 14.691 -8.211 1.00 44.07 O HETATM 1360 O HOH A 336 -16.451 12.374 -33.569 1.00 45.99 O HETATM 1361 O HOH A 337 -14.441 13.541 -26.903 1.00 42.11 O HETATM 1362 O HOH A 338 -19.346 12.950 -34.188 1.00 27.57 O HETATM 1363 O HOH A 339 -7.797 24.489 -7.780 1.00 51.65 O HETATM 1364 O HOH A 340 -20.573 5.199 -32.325 1.00 35.49 O HETATM 1365 O HOH A 341 -8.509 16.509 -14.118 1.00 52.65 O HETATM 1366 O HOH A 342 -39.917 22.248 -12.372 1.00 31.54 O HETATM 1367 O HOH A 343 -26.762 35.215 -18.404 1.00 43.65 O HETATM 1368 O HOH A 344 -1.885 30.521 0.515 1.00 38.94 O HETATM 1369 O HOH A 345 -26.252 19.055 -0.004 1.00 52.47 O HETATM 1370 O HOH A 346 -19.305 15.974 3.746 1.00 49.61 O HETATM 1371 O HOH A 347 -31.439 14.279 -8.259 1.00 28.82 O HETATM 1372 O HOH A 348 -34.727 19.752 -19.054 1.00 31.40 O HETATM 1373 O HOH A 349 -20.033 32.878 -4.477 1.00 41.10 O HETATM 1374 O HOH A 350 -27.816 21.826 -20.644 1.00 24.67 O HETATM 1375 O HOH A 351 -30.858 12.018 -13.066 1.00 25.89 O HETATM 1376 O HOH A 352 -28.543 14.616 -23.687 1.00 30.27 O HETATM 1377 O HOH A 353 -31.493 22.116 -14.753 1.00 27.19 O HETATM 1378 O HOH A 354 -14.392 25.328 -11.417 1.00 31.80 O HETATM 1379 O HOH A 355 -26.758 32.907 -4.919 1.00 55.60 O HETATM 1380 O HOH A 356 -23.207 21.705 -33.131 1.00 50.83 O HETATM 1381 O HOH A 357 -31.518 10.248 -11.109 1.00 34.56 O HETATM 1382 O HOH A 358 -35.610 15.106 -15.890 1.00 37.19 O HETATM 1383 O HOH A 359 -31.891 19.847 -4.242 1.00 28.67 O HETATM 1384 O HOH A 360 -18.038 33.957 -27.497 1.00 43.29 O HETATM 1385 O HOH A 361 -23.924 8.104 -11.996 1.00 34.78 O HETATM 1386 O HOH A 362 -24.309 12.298 -32.652 1.00 27.03 O HETATM 1387 O HOH A 363 -25.527 27.763 -26.128 1.00 46.24 O HETATM 1388 O HOH A 364 -8.325 31.219 3.667 1.00 45.92 O HETATM 1389 O HOH A 365 -19.278 33.108 -12.682 1.00 34.22 O HETATM 1390 O HOH A 366 -14.950 13.643 -30.276 1.00 44.67 O HETATM 1391 O HOH A 367 -16.535 14.146 3.085 1.00 43.54 O HETATM 1392 O HOH A 368 -28.934 17.930 -30.953 1.00 33.25 O HETATM 1393 O HOH A 369 -28.254 9.263 -12.764 1.00 39.43 O HETATM 1394 O HOH A 370 -24.857 31.402 -27.874 1.00 53.58 O HETATM 1395 O HOH A 371 -9.099 13.700 -14.544 1.00 38.96 O HETATM 1396 O HOH A 372 -29.231 16.806 -22.265 1.00 32.32 O HETATM 1397 O HOH A 373 -23.513 12.797 0.139 1.00 42.65 O HETATM 1398 O HOH A 374 -25.808 10.199 -26.666 1.00 49.12 O HETATM 1399 O HOH A 375 -27.923 7.292 -14.403 1.00 36.45 O HETATM 1400 O HOH A 376 -11.594 20.463 -20.123 1.00 33.73 O HETATM 1401 O HOH A 377 -28.966 33.784 -3.478 1.00 41.69 O HETATM 1402 O HOH A 378 -17.755 3.638 -15.106 1.00 48.45 O HETATM 1403 O HOH A 379 -27.359 12.575 -26.747 1.00 49.54 O HETATM 1404 O HOH A 380 -35.855 8.906 -16.259 1.00 55.96 O HETATM 1405 O HOH A 381 -22.708 5.227 -22.439 1.00 50.11 O HETATM 1406 O HOH A 382 -33.999 3.683 -12.136 1.00 55.33 O HETATM 1407 O HOH A 383 -10.093 16.007 -12.156 1.00 35.31 O HETATM 1408 O HOH A 384 -13.576 19.586 -29.891 1.00 28.06 O HETATM 1409 O HOH A 385 -8.180 27.458 -26.268 1.00 31.32 O HETATM 1410 O HOH A 386 -15.480 25.125 -33.493 1.00 55.45 O HETATM 1411 O HOH A 387 -35.236 20.836 -8.206 1.00 36.35 O HETATM 1412 O HOH A 388 -19.524 2.881 -9.619 1.00 53.48 O HETATM 1413 O HOH A 389 -26.187 18.737 5.369 1.00 49.94 O HETATM 1414 O HOH A 390 -25.151 8.389 -22.017 1.00 43.22 O HETATM 1415 O HOH A 391 -13.971 9.764 -26.767 1.00 52.71 O HETATM 1416 O HOH A 392 -20.634 28.571 -31.016 1.00 44.38 O HETATM 1417 O HOH A 393 -13.783 30.804 -30.916 1.00 61.19 O HETATM 1418 O HOH A 394 -13.217 33.543 -16.024 1.00 53.06 O HETATM 1419 O HOH A 395 -14.502 12.701 -8.942 1.00 48.85 O HETATM 1420 O HOH A 396 -28.208 9.230 -5.826 1.00 41.72 O HETATM 1421 O HOH A 397 -36.377 17.733 -20.517 1.00 38.47 O HETATM 1422 O HOH A 398 -18.196 17.030 -33.812 1.00 41.50 O HETATM 1423 O HOH A 399 -41.279 20.492 -22.770 1.00 57.64 O HETATM 1424 O HOH A 400 -30.943 8.098 -18.149 1.00 51.97 O HETATM 1425 O HOH A 401 -39.317 28.863 -4.985 1.00 49.41 O HETATM 1426 O HOH A 402 -12.590 18.329 -27.586 1.00 44.42 O HETATM 1427 O HOH A 403 -30.845 18.466 -24.071 1.00 47.85 O HETATM 1428 O HOH A 404 -13.167 10.569 -21.162 1.00 45.11 O HETATM 1429 O HOH A 405 -13.781 28.088 -10.687 1.00 41.57 O HETATM 1430 O HOH A 406 -26.216 9.581 -10.907 1.00 42.13 O HETATM 1431 O HOH A 407 -13.379 12.795 -6.983 1.00 60.86 O HETATM 1432 O HOH A 408 -20.159 18.814 -35.342 1.00 53.94 O HETATM 1433 O HOH A 409 -28.366 22.108 -34.121 1.00 48.14 O HETATM 1434 O HOH A 410 -26.048 15.800 1.947 1.00 51.58 O HETATM 1435 O HOH A 411 -31.278 31.862 -23.708 1.00 63.12 O HETATM 1436 O HOH A 412 -33.119 12.025 -19.198 1.00 49.95 O HETATM 1437 O HOH A 413 -29.666 8.902 -10.107 1.00 40.17 O HETATM 1438 O HOH A 414 -24.061 33.128 -0.701 1.00 60.40 O HETATM 1439 O HOH A 415 -12.096 10.661 -23.308 1.00 57.17 O HETATM 1440 O HOH A 416 -30.120 12.611 -23.171 1.00 49.53 O HETATM 1441 O HOH A 417 -29.940 19.991 -32.517 1.00 39.51 O HETATM 1442 O HOH A 418 -34.587 30.039 1.070 1.00 54.21 O HETATM 1443 O HOH A 419 -14.598 18.567 -32.184 1.00 39.90 O HETATM 1444 O HOH A 420 -13.199 31.561 -28.466 1.00 55.91 O HETATM 1445 O HOH A 421 -34.345 20.620 -3.956 1.00 39.92 O HETATM 1446 O HOH A 422 -12.880 12.207 -28.756 1.00 57.92 O HETATM 1447 O HOH A 423 -31.131 10.334 -20.123 1.00 49.61 O HETATM 1448 O HOH A 424 -11.398 32.925 -29.623 1.00 57.27 O CONECT 110 1324 CONECT 1286 1287 1288 1289 1290 CONECT 1287 1286 CONECT 1288 1286 1324 CONECT 1289 1286 CONECT 1290 1286 1291 CONECT 1291 1290 1292 1293 1294 CONECT 1292 1291 CONECT 1293 1291 CONECT 1294 1291 1295 CONECT 1295 1294 1296 CONECT 1296 1295 1297 1298 CONECT 1297 1296 1302 CONECT 1298 1296 1299 1300 CONECT 1299 1298 CONECT 1300 1298 1301 1302 CONECT 1301 1300 CONECT 1302 1297 1300 1303 CONECT 1303 1302 1304 1313 CONECT 1304 1303 1305 CONECT 1305 1304 1306 CONECT 1306 1305 1307 1313 CONECT 1307 1306 1308 1309 CONECT 1308 1307 CONECT 1309 1307 1310 CONECT 1310 1309 1311 1312 CONECT 1311 1310 CONECT 1312 1310 1313 CONECT 1313 1303 1306 1312 CONECT 1314 1315 1316 CONECT 1315 1314 CONECT 1316 1314 1317 1318 CONECT 1317 1316 CONECT 1318 1316 1319 CONECT 1319 1318 CONECT 1320 1321 1322 1323 CONECT 1321 1320 CONECT 1322 1320 CONECT 1323 1320 CONECT 1324 110 1288 MASTER 358 0 4 7 6 0 0 6 1429 1 40 14 END If you find results from this site helpful for your research, please cite one of our papers:
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