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*** TRANSPORT PROTEIN 21-OCT-10 3APV ***elNémo ID: 240110225555577823Job options:ID = 240110225555577823 JOBID = TRANSPORT PROTEIN 21-OCT-10 3APV 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 TRANSPORT PROTEIN 21-OCT-10 3APV TITLE CRYSTAL STRUCTURE OF THE A VARIANT OF HUMAN ALPHA1-ACID GLYCOPROTEIN TITLE 2 AND AMITRIPTYLINE COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: ALPHA-1-ACID GLYCOPROTEIN 2; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: AGP 2, OROSOMUCOID-2, OMD 2; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: AGP2, ORM2; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ORIGAMI B (DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3C KEYWDS BETA BARREL, PLASMA PROTEIN, TRANSPORT PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR K.NISHI,T.ONO,T.NAKAMURA,N.FUKUNAGA,M.IZUMI,H.WATANABE,A.SUENAGA, AUTHOR 2 T.MARUYAMA,Y.YAMAGATA,S.CURRY,M.OTAGIRI REVDAT 3 01-NOV-23 3APV 1 REMARK SEQADV REVDAT 2 07-NOV-18 3APV 1 JRNL REVDAT 1 23-FEB-11 3APV 0 JRNL AUTH K.NISHI,T.ONO,T.NAKAMURA,N.FUKUNAGA,M.IZUMI,H.WATANABE, JRNL AUTH 2 A.SUENAGA,T.MARUYAMA,Y.YAMAGATA,S.CURRY,M.OTAGIRI JRNL TITL STRUCTURAL INSIGHTS INTO DIFFERENCES IN DRUG-BINDING JRNL TITL 2 SELECTIVITY BETWEEN TWO FORMS OF HUMAN ALPHA1-ACID JRNL TITL 3 GLYCOPROTEIN GENETIC VARIANTS, THE A AND F1*S FORMS. JRNL REF J. BIOL. CHEM. V. 286 14427 2011 JRNL REFN ESSN 1083-351X JRNL PMID 21349832 JRNL DOI 10.1074/JBC.M110.208926 REMARK 2 REMARK 2 RESOLUTION. 2.15 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0099 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) : 2.15 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.31 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9 REMARK 3 NUMBER OF REFLECTIONS : 18955 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) : 0.222 REMARK 3 R VALUE (WORKING SET) : 0.219 REMARK 3 FREE R VALUE : 0.267 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 971 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.15 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1314 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.59 REMARK 3 BIN R VALUE (WORKING SET) : 0.2640 REMARK 3 BIN FREE R VALUE SET COUNT : 59 REMARK 3 BIN FREE R VALUE : 0.4160 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2869 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 46 REMARK 3 SOLVENT ATOMS : 96 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.72 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.05000 REMARK 3 B22 (A**2) : 0.07000 REMARK 3 B33 (A**2) : -0.13000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.07000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.318 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.234 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.217 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.509 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.910 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2998 ; 0.013 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4058 ; 1.445 ; 1.959 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 341 ; 6.836 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 164 ;39.816 ;24.146 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 506 ;17.484 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;13.188 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 415 ; 0.098 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2344 ; 0.006 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1715 ; 0.582 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2778 ; 1.086 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1283 ; 1.635 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1280 ; 2.682 ; 4.500 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): 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 : 2 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 3 A 172 REMARK 3 ORIGIN FOR THE GROUP (A): 11.7730 -0.3270 14.1510 REMARK 3 T TENSOR REMARK 3 T11: 0.1483 T22: 0.1163 REMARK 3 T33: 0.4831 T12: 0.0433 REMARK 3 T13: 0.0895 T23: -0.0100 REMARK 3 L TENSOR REMARK 3 L11: 2.3834 L22: 1.5046 REMARK 3 L33: 9.1306 L12: -0.1032 REMARK 3 L13: 0.6006 L23: 0.8995 REMARK 3 S TENSOR REMARK 3 S11: -0.1102 S12: -0.1613 S13: 0.0054 REMARK 3 S21: -0.0711 S22: -0.2260 S23: -0.0618 REMARK 3 S31: 0.4398 S32: -0.3814 S33: 0.3362 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 3 B 175 REMARK 3 ORIGIN FOR THE GROUP (A): 10.2010 3.1260 45.8170 REMARK 3 T TENSOR REMARK 3 T11: 0.0597 T22: 0.3170 REMARK 3 T33: 0.2428 T12: -0.0672 REMARK 3 T13: 0.1021 T23: -0.0705 REMARK 3 L TENSOR REMARK 3 L11: 2.8086 L22: 4.0078 REMARK 3 L33: 8.3797 L12: 1.3429 REMARK 3 L13: 1.8635 L23: 1.3664 REMARK 3 S TENSOR REMARK 3 S11: 0.0724 S12: -0.5546 S13: 0.1063 REMARK 3 S21: 0.1709 S22: -0.2833 S23: -0.0419 REMARK 3 S31: -0.0732 S32: -0.9620 S33: 0.2109 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3APV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-NOV-10. REMARK 100 THE DEPOSITION ID IS D_1000029546. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-FEB-09 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.6 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PHOTON FACTORY REMARK 200 BEAMLINE : BL-5A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20082 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.05900 REMARK 200 R SYM (I) : 0.52400 REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23 REMARK 200 COMPLETENESS FOR SHELL (%) : 93.8 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.17700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 8.100 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS REMARK 200 SOFTWARE USED: CNS REMARK 200 STARTING MODEL: PDB ENTRY 3APU REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 39.57 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000, 0.2M AMMONIUM SULFATE, REMARK 280 0.1M SODIUM ACETATE, PH 4.6, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 33.32500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.97400 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 33.32500 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.97400 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 0 REMARK 465 GLN A 1 REMARK 465 ILE A 2 REMARK 465 GLU A 173 REMARK 465 LYS A 174 REMARK 465 GLU A 175 REMARK 465 ARG A 176 REMARK 465 LYS A 177 REMARK 465 GLN A 178 REMARK 465 GLU A 179 REMARK 465 GLU A 180 REMARK 465 GLY A 181 REMARK 465 GLU A 182 REMARK 465 SER A 183 REMARK 465 HIS A 184 REMARK 465 HIS A 185 REMARK 465 HIS A 186 REMARK 465 HIS A 187 REMARK 465 HIS A 188 REMARK 465 HIS A 189 REMARK 465 MET B 0 REMARK 465 GLN B 1 REMARK 465 ILE B 2 REMARK 465 ARG B 176 REMARK 465 LYS B 177 REMARK 465 GLN B 178 REMARK 465 GLU B 179 REMARK 465 GLU B 180 REMARK 465 GLY B 181 REMARK 465 GLU B 182 REMARK 465 SER B 183 REMARK 465 HIS B 184 REMARK 465 HIS B 185 REMARK 465 HIS B 186 REMARK 465 HIS B 187 REMARK 465 HIS B 188 REMARK 465 HIS B 189 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 GLN A 69 47.84 30.12 REMARK 500 LEU B 4 -29.12 -141.10 REMARK 500 GLN B 69 52.15 36.65 REMARK 500 LYS B 135 -36.88 -39.35 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TP0 A 190 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 191 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TP0 B 190 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3APU RELATED DB: PDB REMARK 900 RELATED ID: 3APW RELATED DB: PDB REMARK 900 RELATED ID: 3APX RELATED DB: PDB DBREF 3APV A 1 183 UNP P19652 A1AG2_HUMAN 19 201 DBREF 3APV B 1 183 UNP P19652 A1AG2_HUMAN 19 201 SEQADV 3APV MET A 0 UNP P19652 EXPRESSION TAG SEQADV 3APV ARG A 149 UNP P19652 CYS 167 ENGINEERED MUTATION SEQADV 3APV HIS A 184 UNP P19652 EXPRESSION TAG SEQADV 3APV HIS A 185 UNP P19652 EXPRESSION TAG SEQADV 3APV HIS A 186 UNP P19652 EXPRESSION TAG SEQADV 3APV HIS A 187 UNP P19652 EXPRESSION TAG SEQADV 3APV HIS A 188 UNP P19652 EXPRESSION TAG SEQADV 3APV HIS A 189 UNP P19652 EXPRESSION TAG SEQADV 3APV MET B 0 UNP P19652 EXPRESSION TAG SEQADV 3APV ARG B 149 UNP P19652 CYS 167 ENGINEERED MUTATION SEQADV 3APV HIS B 184 UNP P19652 EXPRESSION TAG SEQADV 3APV HIS B 185 UNP P19652 EXPRESSION TAG SEQADV 3APV HIS B 186 UNP P19652 EXPRESSION TAG SEQADV 3APV HIS B 187 UNP P19652 EXPRESSION TAG SEQADV 3APV HIS B 188 UNP P19652 EXPRESSION TAG SEQADV 3APV HIS B 189 UNP P19652 EXPRESSION TAG SEQRES 1 A 190 MET GLN ILE PRO LEU CYS ALA ASN LEU VAL PRO VAL PRO SEQRES 2 A 190 ILE THR ASN ALA THR LEU ASP ARG ILE THR GLY LYS TRP SEQRES 3 A 190 PHE TYR ILE ALA SER ALA PHE ARG ASN GLU GLU TYR ASN SEQRES 4 A 190 LYS SER VAL GLN GLU ILE GLN ALA THR PHE PHE TYR PHE SEQRES 5 A 190 THR PRO ASN LYS THR GLU ASP THR ILE PHE LEU ARG GLU SEQRES 6 A 190 TYR GLN THR ARG GLN ASN GLN CYS PHE TYR ASN SER SER SEQRES 7 A 190 TYR LEU ASN VAL GLN ARG GLU ASN GLY THR VAL SER ARG SEQRES 8 A 190 TYR GLU GLY GLY ARG GLU HIS VAL ALA HIS LEU LEU PHE SEQRES 9 A 190 LEU ARG ASP THR LYS THR LEU MET PHE GLY SER TYR LEU SEQRES 10 A 190 ASP ASP GLU LYS ASN TRP GLY LEU SER PHE TYR ALA ASP SEQRES 11 A 190 LYS PRO GLU THR THR LYS GLU GLN LEU GLY GLU PHE TYR SEQRES 12 A 190 GLU ALA LEU ASP CYS LEU ARG ILE PRO ARG SER ASP VAL SEQRES 13 A 190 MET TYR THR ASP TRP LYS LYS ASP LYS CYS GLU PRO LEU SEQRES 14 A 190 GLU LYS GLN HIS GLU LYS GLU ARG LYS GLN GLU GLU GLY SEQRES 15 A 190 GLU SER HIS HIS HIS HIS HIS HIS SEQRES 1 B 190 MET GLN ILE PRO LEU CYS ALA ASN LEU VAL PRO VAL PRO SEQRES 2 B 190 ILE THR ASN ALA THR LEU ASP ARG ILE THR GLY LYS TRP SEQRES 3 B 190 PHE TYR ILE ALA SER ALA PHE ARG ASN GLU GLU TYR ASN SEQRES 4 B 190 LYS SER VAL GLN GLU ILE GLN ALA THR PHE PHE TYR PHE SEQRES 5 B 190 THR PRO ASN LYS THR GLU ASP THR ILE PHE LEU ARG GLU SEQRES 6 B 190 TYR GLN THR ARG GLN ASN GLN CYS PHE TYR ASN SER SER SEQRES 7 B 190 TYR LEU ASN VAL GLN ARG GLU ASN GLY THR VAL SER ARG SEQRES 8 B 190 TYR GLU GLY GLY ARG GLU HIS VAL ALA HIS LEU LEU PHE SEQRES 9 B 190 LEU ARG ASP THR LYS THR LEU MET PHE GLY SER TYR LEU SEQRES 10 B 190 ASP ASP GLU LYS ASN TRP GLY LEU SER PHE TYR ALA ASP SEQRES 11 B 190 LYS PRO GLU THR THR LYS GLU GLN LEU GLY GLU PHE TYR SEQRES 12 B 190 GLU ALA LEU ASP CYS LEU ARG ILE PRO ARG SER ASP VAL SEQRES 13 B 190 MET TYR THR ASP TRP LYS LYS ASP LYS CYS GLU PRO LEU SEQRES 14 B 190 GLU LYS GLN HIS GLU LYS GLU ARG LYS GLN GLU GLU GLY SEQRES 15 B 190 GLU SER HIS HIS HIS HIS HIS HIS HET TP0 A 190 21 HET ACY A 191 4 HET TP0 B 190 21 HETNAM TP0 AMITRIPTYLINE HETNAM ACY ACETIC ACID HETSYN TP0 3-(10,11-DIHYDRO-5H-DIBENZO[A,D][7]ANNULEN-5-YLIDENE)- HETSYN 2 TP0 N,N-DIMETHYLPROPAN-1-AMINE FORMUL 3 TP0 2(C20 H23 N) FORMUL 4 ACY C2 H4 O2 FORMUL 6 HOH *96(H2 O) HELIX 1 1 CYS A 5 VAL A 9 5 5 HELIX 2 2 THR A 14 THR A 22 1 9 HELIX 3 3 ASN A 34 GLN A 42 1 9 HELIX 4 4 THR A 134 LEU A 148 1 15 HELIX 5 5 PRO A 151 VAL A 155 5 5 HELIX 6 6 ASP A 159 ASP A 163 5 5 HELIX 7 7 CYS A 165 HIS A 172 1 8 HELIX 8 8 CYS B 5 VAL B 9 5 5 HELIX 9 9 THR B 14 ILE B 21 1 8 HELIX 10 10 ASN B 34 GLU B 43 1 10 HELIX 11 11 THR B 134 LEU B 148 1 15 HELIX 12 12 PRO B 151 VAL B 155 5 5 HELIX 13 13 ASP B 159 ASP B 163 5 5 HELIX 14 14 CYS B 165 GLU B 175 1 11 SHEET 1 A14 MET A 156 TYR A 157 0 SHEET 2 A14 GLY A 23 PHE A 32 -1 N SER A 30 O MET A 156 SHEET 3 A14 GLY A 123 ALA A 128 -1 O ALA A 128 N PHE A 26 SHEET 4 A14 THR A 109 SER A 114 -1 N LEU A 110 O TYR A 127 SHEET 5 A14 ARG A 95 LEU A 102 -1 N HIS A 100 O GLY A 113 SHEET 6 A14 THR A 87 GLU A 92 -1 N GLU A 92 O ARG A 95 SHEET 7 A14 GLN A 71 GLN A 82 -1 N GLN A 82 O THR A 87 SHEET 8 A14 GLN B 71 GLN B 82 -1 O SER B 76 N SER A 76 SHEET 9 A14 THR B 87 TYR B 91 -1 O SER B 89 N ASN B 80 SHEET 10 A14 GLU B 96 LEU B 102 -1 O HIS B 97 N ARG B 90 SHEET 11 A14 THR B 109 SER B 114 -1 O MET B 111 N LEU B 102 SHEET 12 A14 GLY B 123 ALA B 128 -1 O SER B 125 N PHE B 112 SHEET 13 A14 GLY B 23 PHE B 32 -1 N ALA B 29 O PHE B 126 SHEET 14 A14 MET B 156 TYR B 157 -1 O MET B 156 N SER B 30 SHEET 1 B 8 GLY B 23 PHE B 32 0 SHEET 2 B 8 ILE B 44 ASN B 54 -1 O THR B 47 N TYR B 27 SHEET 3 B 8 THR B 59 ARG B 68 -1 O TYR B 65 N PHE B 48 SHEET 4 B 8 GLN B 71 GLN B 82 -1 O PHE B 73 N GLN B 66 SHEET 5 B 8 THR B 87 TYR B 91 -1 O SER B 89 N ASN B 80 SHEET 6 B 8 GLU B 96 LEU B 102 -1 O HIS B 97 N ARG B 90 SHEET 7 B 8 THR B 109 SER B 114 -1 O MET B 111 N LEU B 102 SHEET 8 B 8 GLY B 123 ALA B 128 -1 O SER B 125 N PHE B 112 SHEET 1 C10 MET B 156 TYR B 157 0 SHEET 2 C10 GLY B 23 PHE B 32 -1 N SER B 30 O MET B 156 SHEET 3 C10 ILE B 44 ASN B 54 -1 O THR B 47 N TYR B 27 SHEET 4 C10 THR B 59 ARG B 68 -1 O TYR B 65 N PHE B 48 SHEET 5 C10 GLN B 71 GLN B 82 -1 O PHE B 73 N GLN B 66 SHEET 6 C10 GLN A 71 GLN A 82 -1 N SER A 76 O SER B 76 SHEET 7 C10 THR A 59 ARG A 68 -1 N LEU A 62 O SER A 77 SHEET 8 C10 ILE A 44 ASN A 54 -1 N ALA A 46 O THR A 67 SHEET 9 C10 GLY A 23 PHE A 32 -1 N GLY A 23 O PHE A 51 SHEET 10 C10 MET A 156 TYR A 157 -1 O MET A 156 N SER A 30 SHEET 1 D 8 GLY A 23 PHE A 32 0 SHEET 2 D 8 ILE A 44 ASN A 54 -1 O PHE A 51 N GLY A 23 SHEET 3 D 8 THR A 59 ARG A 68 -1 O THR A 67 N ALA A 46 SHEET 4 D 8 GLN A 71 GLN A 82 -1 O SER A 77 N LEU A 62 SHEET 5 D 8 THR A 87 GLU A 92 -1 O THR A 87 N GLN A 82 SHEET 6 D 8 ARG A 95 LEU A 102 -1 O ARG A 95 N GLU A 92 SHEET 7 D 8 THR A 109 SER A 114 -1 O GLY A 113 N HIS A 100 SHEET 8 D 8 GLY A 123 ALA A 128 -1 O TYR A 127 N LEU A 110 SSBOND 1 CYS A 5 CYS A 147 1555 1555 2.03 SSBOND 2 CYS A 72 CYS A 165 1555 1555 2.03 SSBOND 3 CYS B 5 CYS B 147 1555 1555 2.04 SSBOND 4 CYS B 72 CYS B 165 1555 1555 2.03 SITE 1 AC1 12 VAL A 41 PHE A 49 PHE A 51 LEU A 62 SITE 2 AC1 12 VAL A 88 ARG A 90 HIS A 97 ALA A 99 SITE 3 AC1 12 PHE A 112 TYR A 127 ACY A 191 HOH A 257 SITE 1 AC2 5 TYR A 27 TYR A 127 TP0 A 190 HOH A 257 SITE 2 AC2 5 HOH A 258 SITE 1 AC3 11 TYR B 37 VAL B 41 PHE B 49 LEU B 62 SITE 2 AC3 11 VAL B 88 HIS B 97 ALA B 99 SER B 125 SITE 3 AC3 11 TYR B 127 HOH B 202 HOH B 208 CRYST1 66.650 45.948 120.732 90.00 92.14 90.00 C 1 2 1 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.015004 0.000000 0.000561 0.00000 SCALE2 0.000000 0.021764 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008289 0.00000 ATOM 1 N PRO A 3 16.417 6.281 -8.843 1.00 60.32 N ANISOU 1 N PRO A 3 8160 6730 8030 436 1227 1325 N ATOM 2 CA PRO A 3 17.057 6.946 -7.704 1.00 59.96 C ANISOU 2 CA PRO A 3 8091 6547 8146 238 1217 1418 C ATOM 3 C PRO A 3 17.077 6.010 -6.491 1.00 57.42 C ANISOU 3 C PRO A 3 7488 6250 8078 339 1251 1230 C ATOM 4 O PRO A 3 16.018 5.800 -5.867 1.00 56.86 O ANISOU 4 O PRO A 3 7430 6030 8144 517 1117 1078 O ATOM 5 CB PRO A 3 16.131 8.117 -7.457 1.00 60.67 C ANISOU 5 CB PRO A 3 8516 6299 8239 298 984 1480 C ATOM 6 CG PRO A 3 14.712 7.519 -7.808 1.00 59.40 C ANISOU 6 CG PRO A 3 8342 6165 8062 643 858 1278 C ATOM 7 CD PRO A 3 14.958 6.511 -8.898 1.00 59.13 C ANISOU 7 CD PRO A 3 8172 6416 7879 670 1011 1221 C ATOM 8 N LEU A 4 18.254 5.475 -6.142 1.00 56.69 N ANISOU 8 N LEU A 4 7143 6376 8021 235 1424 1242 N ATOM 9 CA LEU A 4 18.342 4.259 -5.293 1.00 53.79 C ANISOU 9 CA LEU A 4 6539 6077 7822 403 1486 1058 C ATOM 10 C LEU A 4 18.173 4.479 -3.788 1.00 50.47 C ANISOU 10 C LEU A 4 6062 5479 7635 380 1389 1016 C ATOM 11 O LEU A 4 17.597 3.639 -3.069 1.00 50.19 O ANISOU 11 O LEU A 4 5961 5370 7737 543 1360 853 O ATOM 12 CB LEU A 4 19.676 3.509 -5.551 1.00 55.79 C ANISOU 12 CB LEU A 4 6540 6681 7975 407 1700 1068 C ATOM 13 CG LEU A 4 19.816 2.675 -6.839 1.00 57.56 C ANISOU 13 CG LEU A 4 6757 7125 7986 564 1831 1002 C ATOM 14 CD1 LEU A 4 21.287 2.446 -7.244 1.00 59.78 C ANISOU 14 CD1 LEU A 4 6786 7838 8090 524 2038 1071 C ATOM 15 CD2 LEU A 4 19.049 1.350 -6.709 1.00 56.64 C ANISOU 15 CD2 LEU A 4 6689 6888 7943 842 1815 765 C ATOM 16 N CYS A 5 18.681 5.607 -3.323 1.00 48.58 N ANISOU 16 N CYS A 5 5875 5168 7414 147 1341 1162 N ATOM 17 CA CYS A 5 18.839 5.870 -1.898 1.00 43.91 C ANISOU 17 CA CYS A 5 5203 4472 7010 83 1274 1135 C ATOM 18 C CYS A 5 18.081 7.131 -1.533 1.00 41.01 C ANISOU 18 C CYS A 5 5126 3778 6680 14 1079 1181 C ATOM 19 O CYS A 5 18.336 7.772 -0.512 1.00 40.48 O ANISOU 19 O CYS A 5 5080 3591 6711 -119 1008 1201 O ATOM 20 CB CYS A 5 20.320 6.035 -1.611 1.00 45.13 C ANISOU 20 CB CYS A 5 5138 4892 7116 -156 1399 1244 C ATOM 21 SG CYS A 5 21.206 4.585 -2.234 1.00 48.65 S ANISOU 21 SG CYS A 5 5270 5766 7448 40 1623 1177 S ATOM 22 N ALA A 6 17.144 7.486 -2.397 1.00 38.44 N ANISOU 22 N ALA A 6 5041 3317 6249 139 983 1187 N ATOM 23 CA ALA A 6 16.295 8.623 -2.155 1.00 35.74 C ANISOU 23 CA ALA A 6 5013 2665 5899 194 778 1208 C ATOM 24 C ALA A 6 15.527 8.432 -0.840 1.00 33.62 C ANISOU 24 C ALA A 6 4647 2302 5824 369 670 1028 C ATOM 25 O ALA A 6 15.264 9.395 -0.153 1.00 34.27 O ANISOU 25 O ALA A 6 4927 2153 5941 366 528 1036 O ATOM 26 CB ALA A 6 15.347 8.812 -3.320 1.00 36.81 C ANISOU 26 CB ALA A 6 5364 2757 5864 393 689 1213 C ATOM 27 N ASN A 7 15.220 7.179 -0.452 1.00 31.43 N ANISOU 27 N ASN A 7 4091 2198 5653 501 743 867 N ATOM 28 CA ASN A 7 14.301 7.005 0.688 1.00 29.83 C ANISOU 28 CA ASN A 7 3812 1940 5584 655 640 698 C ATOM 29 C ASN A 7 15.016 7.051 2.025 1.00 28.99 C ANISOU 29 C ASN A 7 3583 1806 5627 527 666 699 C ATOM 30 O ASN A 7 14.393 6.865 3.071 1.00 27.77 O ANISOU 30 O ASN A 7 3345 1632 5573 626 602 568 O ATOM 31 CB ASN A 7 13.437 5.720 0.552 1.00 28.45 C ANISOU 31 CB ASN A 7 3461 1932 5416 804 681 521 C ATOM 32 CG ASN A 7 14.283 4.450 0.492 1.00 27.65 C ANISOU 32 CG ASN A 7 3189 1968 5350 732 870 514 C ATOM 33 OD1 ASN A 7 15.344 4.436 -0.080 1.00 28.54 O ANISOU 33 OD1 ASN A 7 3289 2151 5404 639 981 634 O ATOM 34 ND2 ASN A 7 13.777 3.381 1.042 1.00 27.44 N ANISOU 34 ND2 ASN A 7 3053 1991 5382 785 903 368 N ATOM 35 N LEU A 8 16.323 7.286 1.981 1.00 29.95 N ANISOU 35 N LEU A 8 3668 1979 5734 297 761 840 N ATOM 36 CA LEU A 8 17.132 7.526 3.182 1.00 29.83 C ANISOU 36 CA LEU A 8 3542 1973 5821 137 767 857 C ATOM 37 C LEU A 8 17.169 9.028 3.579 1.00 31.59 C ANISOU 37 C LEU A 8 4051 1933 6019 -23 618 925 C ATOM 38 O LEU A 8 17.749 9.397 4.588 1.00 32.52 O ANISOU 38 O LEU A 8 4123 2032 6202 -182 592 923 O ATOM 39 CB LEU A 8 18.578 7.012 2.996 1.00 30.62 C ANISOU 39 CB LEU A 8 3403 2351 5880 -38 940 954 C ATOM 40 CG LEU A 8 18.933 5.512 3.160 1.00 32.67 C ANISOU 40 CG LEU A 8 3384 2853 6176 136 1081 875 C ATOM 41 CD1 LEU A 8 18.749 5.087 4.630 1.00 32.12 C ANISOU 41 CD1 LEU A 8 3201 2752 6250 223 1033 772 C ATOM 42 CD2 LEU A 8 18.050 4.669 2.278 1.00 30.44 C ANISOU 42 CD2 LEU A 8 3170 2545 5851 347 1112 790 C ATOM 43 N VAL A 9 16.612 9.895 2.761 1.00 33.21 N ANISOU 43 N VAL A 9 4589 1926 6105 16 515 987 N ATOM 44 CA VAL A 9 16.520 11.310 3.128 1.00 35.38 C ANISOU 44 CA VAL A 9 5250 1864 6330 -81 350 1036 C ATOM 45 C VAL A 9 15.358 11.589 4.113 1.00 34.53 C ANISOU 45 C VAL A 9 5223 1595 6301 230 179 848 C ATOM 46 O VAL A 9 14.239 11.159 3.874 1.00 33.50 O ANISOU 46 O VAL A 9 5028 1538 6163 555 131 728 O ATOM 47 CB VAL A 9 16.325 12.194 1.855 1.00 38.13 C ANISOU 47 CB VAL A 9 6016 1997 6475 -108 283 1189 C ATOM 48 CG1 VAL A 9 16.336 13.689 2.216 1.00 41.15 C ANISOU 48 CG1 VAL A 9 6914 1949 6771 -232 106 1256 C ATOM 49 CG2 VAL A 9 17.392 11.866 0.798 1.00 39.21 C ANISOU 49 CG2 VAL A 9 6040 2364 6496 -407 470 1365 C ATOM 50 N PRO A 10 15.621 12.317 5.220 1.00 35.31 N ANISOU 50 N PRO A 10 5448 1518 6450 122 88 809 N ATOM 51 CA PRO A 10 14.566 12.662 6.182 1.00 35.00 C ANISOU 51 CA PRO A 10 5491 1355 6453 434 -71 619 C ATOM 52 C PRO A 10 13.315 13.210 5.499 1.00 36.41 C ANISOU 52 C PRO A 10 5955 1382 6498 819 -227 565 C ATOM 53 O PRO A 10 13.400 13.903 4.471 1.00 38.74 O ANISOU 53 O PRO A 10 6608 1466 6643 791 -281 708 O ATOM 54 CB PRO A 10 15.228 13.723 7.078 1.00 37.02 C ANISOU 54 CB PRO A 10 6019 1343 6704 193 -165 635 C ATOM 55 CG PRO A 10 16.745 13.595 6.838 1.00 37.66 C ANISOU 55 CG PRO A 10 5974 1552 6782 -305 -15 812 C ATOM 56 CD PRO A 10 16.969 12.576 5.765 1.00 36.26 C ANISOU 56 CD PRO A 10 5509 1673 6595 -300 157 902 C ATOM 57 N VAL A 11 12.152 12.862 6.052 1.00 35.33 N ANISOU 57 N VAL A 11 5637 1401 6384 1181 -297 359 N ATOM 58 CA VAL A 11 10.874 13.297 5.520 1.00 36.92 C ANISOU 58 CA VAL A 11 6007 1585 6434 1616 -456 263 C ATOM 59 C VAL A 11 9.945 13.721 6.655 1.00 37.59 C ANISOU 59 C VAL A 11 6089 1688 6503 1956 -602 36 C ATOM 60 O VAL A 11 9.727 12.941 7.601 1.00 35.47 O ANISOU 60 O VAL A 11 5431 1699 6345 1938 -524 -103 O ATOM 61 CB VAL A 11 10.182 12.253 4.678 1.00 35.50 C ANISOU 61 CB VAL A 11 5506 1762 6222 1748 -379 216 C ATOM 62 CG1 VAL A 11 9.077 12.887 3.838 1.00 38.03 C ANISOU 62 CG1 VAL A 11 6054 2067 6330 2165 -558 169 C ATOM 63 CG2 VAL A 11 11.194 11.471 3.790 1.00 36.60 C ANISOU 63 CG2 VAL A 11 5520 1981 6406 1400 -182 393 C ATOM 64 N PRO A 12 9.398 14.959 6.570 1.00 40.93 N ANISOU 64 N PRO A 12 6975 1814 6761 2287 -817 -2 N ATOM 65 CA PRO A 12 8.615 15.438 7.696 1.00 42.06 C ANISOU 65 CA PRO A 12 7138 1979 6865 2638 -955 -234 C ATOM 66 C PRO A 12 7.407 14.570 7.986 1.00 40.76 C ANISOU 66 C PRO A 12 6452 2358 6676 2941 -932 -455 C ATOM 67 O PRO A 12 6.842 13.980 7.091 1.00 40.36 O ANISOU 67 O PRO A 12 6190 2586 6558 3038 -900 -453 O ATOM 68 CB PRO A 12 8.167 16.893 7.280 1.00 46.61 C ANISOU 68 CB PRO A 12 8375 2123 7212 3035 -1206 -230 C ATOM 69 CG PRO A 12 8.918 17.212 6.024 1.00 47.74 C ANISOU 69 CG PRO A 12 8885 1960 7295 2762 -1181 47 C ATOM 70 CD PRO A 12 9.320 15.854 5.408 1.00 44.05 C ANISOU 70 CD PRO A 12 7877 1894 6965 2426 -943 143 C ATOM 71 N ILE A 13 6.995 14.551 9.245 1.00 40.58 N ANISOU 71 N ILE A 13 6241 2500 6676 3071 -955 -653 N ATOM 72 CA ILE A 13 5.866 13.755 9.679 1.00 39.84 C ANISOU 72 CA ILE A 13 5638 2970 6531 3284 -919 -871 C ATOM 73 C ILE A 13 4.619 14.595 9.763 1.00 43.44 C ANISOU 73 C ILE A 13 6195 3570 6742 3907 -1132 -1088 C ATOM 74 O ILE A 13 4.579 15.596 10.495 1.00 45.76 O ANISOU 74 O ILE A 13 6815 3608 6965 4170 -1275 -1188 O ATOM 75 CB ILE A 13 6.175 13.108 11.023 1.00 37.65 C ANISOU 75 CB ILE A 13 5047 2864 6396 3027 -791 -948 C ATOM 76 CG1 ILE A 13 7.431 12.206 10.829 1.00 34.50 C ANISOU 76 CG1 ILE A 13 4542 2359 6207 2482 -589 -729 C ATOM 77 CG2 ILE A 13 4.931 12.389 11.609 1.00 37.68 C ANISOU 77 CG2 ILE A 13 4551 3469 6294 3216 -757 -1185 C ATOM 78 CD1 ILE A 13 7.863 11.462 12.042 1.00 32.42 C ANISOU 78 CD1 ILE A 13 4001 2245 6072 2221 -460 -762 C ATOM 79 N THR A 14 3.602 14.168 9.014 1.00 44.25 N ANISOU 79 N THR A 14 6011 4110 6692 4156 -1158 -1177 N ATOM 80 CA THR A 14 2.271 14.795 9.034 1.00 48.64 C ANISOU 80 CA THR A 14 6522 4993 6968 4810 -1357 -1417 C ATOM 81 C THR A 14 1.326 13.883 9.833 1.00 48.31 C ANISOU 81 C THR A 14 5809 5679 6868 4810 -1259 -1660 C ATOM 82 O THR A 14 1.729 12.799 10.280 1.00 45.16 O ANISOU 82 O THR A 14 5081 5432 6647 4299 -1049 -1612 O ATOM 83 CB THR A 14 1.721 14.953 7.580 1.00 50.74 C ANISOU 83 CB THR A 14 6882 5353 7044 5094 -1469 -1360 C ATOM 84 OG1 THR A 14 1.492 13.654 7.013 1.00 48.17 O ANISOU 84 OG1 THR A 14 6047 5488 6765 4751 -1301 -1347 O ATOM 85 CG2 THR A 14 2.697 15.716 6.677 1.00 51.43 C ANISOU 85 CG2 THR A 14 7626 4747 7168 4989 -1530 -1078 C ATOM 86 N ASN A 15 0.078 14.318 9.993 1.00 51.84 N ANISOU 86 N ASN A 15 6070 6591 7036 5385 -1412 -1917 N ATOM 87 CA ASN A 15 -1.027 13.464 10.466 1.00 52.99 C ANISOU 87 CA ASN A 15 5522 7577 7036 5393 -1330 -2158 C ATOM 88 C ASN A 15 -1.301 12.226 9.601 1.00 51.43 C ANISOU 88 C ASN A 15 4909 7784 6847 4987 -1189 -2105 C ATOM 89 O ASN A 15 -1.600 11.142 10.134 1.00 50.65 O ANISOU 89 O ASN A 15 4335 8140 6770 4585 -1014 -2184 O ATOM 90 CB ASN A 15 -2.327 14.267 10.543 1.00 56.64 C ANISOU 90 CB ASN A 15 5857 8528 7136 6166 -1548 -2446 C ATOM 91 CG ASN A 15 -2.352 15.221 11.719 1.00 59.85 C ANISOU 91 CG ASN A 15 6503 8762 7476 6568 -1655 -2606 C ATOM 92 OD1 ASN A 15 -1.414 15.277 12.520 1.00 57.74 O ANISOU 92 OD1 ASN A 15 6476 8028 7436 6229 -1567 -2507 O ATOM 93 ND2 ASN A 15 -3.450 15.977 11.838 1.00 63.71 N ANISOU 93 ND2 ASN A 15 6915 9668 7623 7329 -1855 -2877 N ATOM 94 N ALA A 16 -1.276 12.427 8.281 1.00 52.41 N ANISOU 94 N ALA A 16 5244 7757 6912 5112 -1278 -1986 N ATOM 95 CA ALA A 16 -1.251 11.321 7.315 1.00 51.68 C ANISOU 95 CA ALA A 16 4910 7865 6861 4679 -1147 -1892 C ATOM 96 C ALA A 16 -0.144 10.302 7.609 1.00 47.11 C ANISOU 96 C ALA A 16 4341 6965 6593 3981 -900 -1703 C ATOM 97 O ALA A 16 -0.405 9.092 7.610 1.00 46.89 O ANISOU 97 O ALA A 16 3940 7300 6577 3567 -742 -1748 O ATOM 98 CB ALA A 16 -1.138 11.860 5.870 1.00 53.14 C ANISOU 98 CB ALA A 16 5448 7791 6951 4927 -1287 -1748 C ATOM 99 N THR A 17 1.084 10.767 7.865 1.00 45.77 N ANISOU 99 N THR A 17 4606 6135 6648 3845 -870 -1500 N ATOM 100 CA THR A 17 2.192 9.847 8.268 1.00 41.20 C ANISOU 100 CA THR A 17 4020 5293 6342 3261 -649 -1334 C ATOM 101 C THR A 17 1.815 9.053 9.510 1.00 40.45 C ANISOU 101 C THR A 17 3538 5568 6264 3039 -524 -1478 C ATOM 102 O THR A 17 2.014 7.834 9.558 1.00 38.49 O ANISOU 102 O THR A 17 3091 5434 6099 2596 -346 -1432 O ATOM 103 CB THR A 17 3.493 10.580 8.640 1.00 39.92 C ANISOU 103 CB THR A 17 4301 4494 6373 3171 -653 -1145 C ATOM 104 OG1 THR A 17 3.812 11.525 7.638 1.00 42.01 O ANISOU 104 OG1 THR A 17 4997 4384 6580 3381 -786 -1011 O ATOM 105 CG2 THR A 17 4.664 9.593 8.735 1.00 37.09 C ANISOU 105 CG2 THR A 17 3911 3933 6249 2635 -441 -961 C ATOM 106 N LEU A 18 1.292 9.763 10.512 1.00 42.40 N ANISOU 106 N LEU A 18 3727 5975 6409 3357 -621 -1649 N ATOM 107 CA LEU A 18 0.864 9.165 11.783 1.00 42.53 C ANISOU 107 CA LEU A 18 3384 6383 6393 3187 -514 -1796 C ATOM 108 C LEU A 18 -0.259 8.153 11.598 1.00 44.34 C ANISOU 108 C LEU A 18 3114 7303 6430 3010 -433 -1953 C ATOM 109 O LEU A 18 -0.229 7.067 12.204 1.00 44.24 O ANISOU 109 O LEU A 18 2883 7470 6457 2550 -255 -1944 O ATOM 110 CB LEU A 18 0.490 10.237 12.813 1.00 44.26 C ANISOU 110 CB LEU A 18 3656 6661 6499 3628 -649 -1972 C ATOM 111 CG LEU A 18 1.637 11.155 13.269 1.00 41.62 C ANISOU 111 CG LEU A 18 3823 5648 6343 3680 -714 -1841 C ATOM 112 CD1 LEU A 18 1.095 12.325 14.118 1.00 44.04 C ANISOU 112 CD1 LEU A 18 4249 6006 6478 4214 -887 -2061 C ATOM 113 CD2 LEU A 18 2.748 10.399 14.027 1.00 37.45 C ANISOU 113 CD2 LEU A 18 3300 4872 6058 3150 -532 -1678 C ATOM 114 N ASP A 19 -1.220 8.487 10.742 1.00 46.54 N ANISOU 114 N ASP A 19 3239 7964 6479 3347 -566 -2088 N ATOM 115 CA ASP A 19 -2.253 7.538 10.344 1.00 48.21 C ANISOU 115 CA ASP A 19 2980 8856 6483 3121 -502 -2234 C ATOM 116 C ASP A 19 -1.629 6.304 9.694 1.00 46.09 C ANISOU 116 C ASP A 19 2786 8352 6376 2523 -328 -2056 C ATOM 117 O ASP A 19 -2.026 5.169 9.981 1.00 46.94 O ANISOU 117 O ASP A 19 2615 8804 6415 2054 -179 -2117 O ATOM 118 CB ASP A 19 -3.232 8.198 9.359 1.00 51.92 C ANISOU 118 CB ASP A 19 3319 9732 6678 3633 -704 -2385 C ATOM 119 CG ASP A 19 -4.349 9.008 10.059 1.00 55.58 C ANISOU 119 CG ASP A 19 3474 10801 6843 4202 -850 -2672 C ATOM 120 OD1 ASP A 19 -5.100 9.712 9.341 1.00 60.56 O ANISOU 120 OD1 ASP A 19 4046 11739 7227 4756 -1050 -2799 O ATOM 121 OD2 ASP A 19 -4.492 8.941 11.304 1.00 53.33 O ANISOU 121 OD2 ASP A 19 3004 10718 6542 4133 -772 -2778 O ATOM 122 N ARG A 20 -0.641 6.516 8.825 1.00 43.58 N ANISOU 122 N ARG A 20 2872 7441 6244 2529 -345 -1840 N ATOM 123 CA ARG A 20 0.003 5.410 8.117 1.00 41.16 C ANISOU 123 CA ARG A 20 2674 6898 6069 2054 -193 -1685 C ATOM 124 C ARG A 20 0.678 4.401 9.069 1.00 38.32 C ANISOU 124 C ARG A 20 2339 6343 5878 1576 8 -1594 C ATOM 125 O ARG A 20 0.610 3.200 8.845 1.00 37.49 O ANISOU 125 O ARG A 20 2170 6323 5753 1150 143 -1586 O ATOM 126 CB ARG A 20 0.998 5.942 7.082 1.00 39.41 C ANISOU 126 CB ARG A 20 2866 6118 5991 2188 -243 -1471 C ATOM 127 CG ARG A 20 1.961 4.878 6.535 1.00 38.61 C ANISOU 127 CG ARG A 20 2929 5685 6054 1751 -70 -1295 C ATOM 128 CD ARG A 20 2.635 5.442 5.318 1.00 37.98 C ANISOU 128 CD ARG A 20 3159 5256 6016 1913 -132 -1131 C ATOM 129 NE ARG A 20 3.522 4.511 4.628 1.00 36.76 N ANISOU 129 NE ARG A 20 3149 4843 5973 1584 21 -987 N ATOM 130 CZ ARG A 20 4.095 4.836 3.479 1.00 36.63 C ANISOU 130 CZ ARG A 20 3364 4595 5957 1665 -3 -848 C ATOM 131 NH1 ARG A 20 3.842 6.042 2.961 1.00 33.96 N ANISOU 131 NH1 ARG A 20 3169 4217 5517 2031 -176 -822 N ATOM 132 NH2 ARG A 20 4.922 4.001 2.872 1.00 34.82 N ANISOU 132 NH2 ARG A 20 3253 4169 5807 1410 140 -736 N ATOM 133 N ILE A 21 1.299 4.889 10.137 1.00 36.84 N ANISOU 133 N ILE A 21 2276 5894 5829 1659 16 -1533 N ATOM 134 CA ILE A 21 1.991 4.019 11.098 1.00 34.29 C ANISOU 134 CA ILE A 21 2001 5382 5646 1276 184 -1432 C ATOM 135 C ILE A 21 1.156 3.537 12.290 1.00 35.40 C ANISOU 135 C ILE A 21 1832 5985 5634 1096 254 -1587 C ATOM 136 O ILE A 21 1.671 2.809 13.150 1.00 33.29 O ANISOU 136 O ILE A 21 1631 5569 5447 790 386 -1497 O ATOM 137 CB ILE A 21 3.287 4.662 11.607 1.00 32.57 C ANISOU 137 CB ILE A 21 2086 4635 5656 1381 172 -1260 C ATOM 138 CG1 ILE A 21 2.957 5.893 12.490 1.00 34.61 C ANISOU 138 CG1 ILE A 21 2318 4974 5858 1751 34 -1381 C ATOM 139 CG2 ILE A 21 4.219 4.983 10.408 1.00 31.85 C ANISOU 139 CG2 ILE A 21 2292 4117 5693 1443 143 -1082 C ATOM 140 CD1 ILE A 21 4.170 6.473 13.146 1.00 31.28 C ANISOU 140 CD1 ILE A 21 2172 4086 5628 1769 23 -1242 C ATOM 141 N THR A 22 -0.120 3.942 12.342 1.00 38.51 N ANISOU 141 N THR A 22 1884 6971 5778 1299 166 -1817 N ATOM 142 CA THR A 22 -1.041 3.479 13.383 1.00 40.48 C ANISOU 142 CA THR A 22 1770 7792 5819 1097 243 -1985 C ATOM 143 C THR A 22 -1.271 1.950 13.276 1.00 41.12 C ANISOU 143 C THR A 22 1784 8016 5823 455 423 -1953 C ATOM 144 O THR A 22 -1.493 1.415 12.189 1.00 42.07 O ANISOU 144 O THR A 22 1916 8177 5893 279 429 -1957 O ATOM 145 CB THR A 22 -2.369 4.272 13.301 1.00 44.81 C ANISOU 145 CB THR A 22 1920 9031 6073 1506 100 -2259 C ATOM 146 OG1 THR A 22 -2.052 5.662 13.372 1.00 43.98 O ANISOU 146 OG1 THR A 22 2019 8651 6039 2110 -75 -2269 O ATOM 147 CG2 THR A 22 -3.299 3.918 14.433 1.00 46.23 C ANISOU 147 CG2 THR A 22 1679 9880 6005 1323 185 -2446 C ATOM 148 N GLY A 23 -1.183 1.243 14.401 1.00 41.03 N ANISOU 148 N GLY A 23 1761 8041 5787 96 564 -1915 N ATOM 149 CA GLY A 23 -1.414 -0.205 14.415 1.00 41.01 C ANISOU 149 CA GLY A 23 1790 8115 5675 -541 731 -1876 C ATOM 150 C GLY A 23 -0.254 -1.054 14.926 1.00 38.24 C ANISOU 150 C GLY A 23 1869 7143 5516 -824 860 -1634 C ATOM 151 O GLY A 23 0.707 -0.549 15.523 1.00 35.87 O ANISOU 151 O GLY A 23 1758 6452 5418 -569 836 -1505 O ATOM 152 N LYS A 24 -0.382 -2.353 14.670 1.00 39.20 N ANISOU 152 N LYS A 24 2156 7198 5541 -1349 986 -1586 N ATOM 153 CA LYS A 24 0.505 -3.410 15.125 1.00 38.24 C ANISOU 153 CA LYS A 24 2471 6550 5508 -1658 1114 -1379 C ATOM 154 C LYS A 24 1.610 -3.544 14.086 1.00 35.75 C ANISOU 154 C LYS A 24 2519 5636 5428 -1467 1088 -1232 C ATOM 155 O LYS A 24 1.351 -3.578 12.881 1.00 36.09 O ANISOU 155 O LYS A 24 2546 5717 5449 -1456 1044 -1300 O ATOM 156 CB LYS A 24 -0.300 -4.737 15.246 1.00 41.94 C ANISOU 156 CB LYS A 24 3000 7237 5699 -2335 1249 -1424 C ATOM 157 CG LYS A 24 0.384 -5.880 16.032 1.00 41.87 C ANISOU 157 CG LYS A 24 3473 6750 5686 -2685 1384 -1220 C ATOM 158 CD LYS A 24 -0.481 -7.159 16.078 1.00 47.41 C ANISOU 158 CD LYS A 24 4310 7631 6072 -3417 1511 -1267 C ATOM 159 CE LYS A 24 0.155 -8.240 16.957 1.00 48.16 C ANISOU 159 CE LYS A 24 4953 7224 6122 -3727 1631 -1050 C ATOM 160 NZ LYS A 24 -0.527 -9.584 16.878 1.00 54.22 N ANISOU 160 NZ LYS A 24 6037 7983 6580 -4485 1751 -1061 N ATOM 161 N TRP A 25 2.851 -3.588 14.543 1.00 33.51 N ANISOU 161 N TRP A 25 2531 4854 5346 -1298 1111 -1039 N ATOM 162 CA TRP A 25 3.958 -3.804 13.637 1.00 31.63 C ANISOU 162 CA TRP A 25 2611 4114 5294 -1129 1108 -900 C ATOM 163 C TRP A 25 4.819 -4.911 14.192 1.00 31.85 C ANISOU 163 C TRP A 25 3047 3713 5343 -1294 1216 -726 C ATOM 164 O TRP A 25 4.781 -5.181 15.406 1.00 32.87 O ANISOU 164 O TRP A 25 3207 3882 5402 -1431 1265 -675 O ATOM 165 CB TRP A 25 4.772 -2.535 13.503 1.00 29.17 C ANISOU 165 CB TRP A 25 2221 3662 5199 -653 999 -842 C ATOM 166 CG TRP A 25 3.996 -1.443 12.837 1.00 30.76 C ANISOU 166 CG TRP A 25 2132 4192 5363 -422 874 -994 C ATOM 167 CD1 TRP A 25 3.283 -0.463 13.449 1.00 31.20 C ANISOU 167 CD1 TRP A 25 1895 4611 5350 -229 784 -1127 C ATOM 168 CD2 TRP A 25 3.840 -1.237 11.424 1.00 33.07 C ANISOU 168 CD2 TRP A 25 2428 4485 5651 -316 815 -1034 C ATOM 169 NE1 TRP A 25 2.689 0.348 12.510 1.00 34.10 N ANISOU 169 NE1 TRP A 25 2102 5191 5665 24 662 -1243 N ATOM 170 CE2 TRP A 25 3.032 -0.090 11.259 1.00 35.30 C ANISOU 170 CE2 TRP A 25 2430 5125 5860 -35 678 -1178 C ATOM 171 CE3 TRP A 25 4.329 -1.891 10.282 1.00 34.58 C ANISOU 171 CE3 TRP A 25 2852 4410 5876 -393 860 -966 C ATOM 172 CZ2 TRP A 25 2.684 0.412 9.988 1.00 36.89 C ANISOU 172 CZ2 TRP A 25 2582 5422 6013 159 578 -1237 C ATOM 173 CZ3 TRP A 25 3.988 -1.387 9.015 1.00 34.84 C ANISOU 173 CZ3 TRP A 25 2811 4557 5868 -233 772 -1032 C ATOM 174 CH2 TRP A 25 3.198 -0.242 8.884 1.00 35.99 C ANISOU 174 CH2 TRP A 25 2688 5047 5940 39 630 -1153 C ATOM 175 N PHE A 26 5.578 -5.563 13.317 1.00 31.28 N ANISOU 175 N PHE A 26 3303 3248 5336 -1254 1249 -639 N ATOM 176 CA PHE A 26 6.485 -6.586 13.772 1.00 31.70 C ANISOU 176 CA PHE A 26 3784 2870 5392 -1293 1330 -476 C ATOM 177 C PHE A 26 7.915 -6.173 13.439 1.00 29.48 C ANISOU 177 C PHE A 26 3582 2297 5321 -850 1296 -344 C ATOM 178 O PHE A 26 8.196 -5.765 12.323 1.00 28.50 O ANISOU 178 O PHE A 26 3400 2146 5282 -670 1260 -370 O ATOM 179 CB PHE A 26 6.127 -7.949 13.124 1.00 34.31 C ANISOU 179 CB PHE A 26 4510 2983 5543 -1653 1412 -506 C ATOM 180 CG PHE A 26 4.761 -8.500 13.536 1.00 37.30 C ANISOU 180 CG PHE A 26 4838 3670 5664 -2210 1465 -625 C ATOM 181 CD1 PHE A 26 3.597 -8.119 12.868 1.00 38.30 C ANISOU 181 CD1 PHE A 26 4606 4265 5680 -2412 1427 -824 C ATOM 182 CD2 PHE A 26 4.651 -9.440 14.563 1.00 39.63 C ANISOU 182 CD2 PHE A 26 5456 3810 5790 -2549 1553 -535 C ATOM 183 CE1 PHE A 26 2.340 -8.657 13.246 1.00 41.65 C ANISOU 183 CE1 PHE A 26 4930 5071 5826 -2975 1484 -948 C ATOM 184 CE2 PHE A 26 3.394 -9.977 14.941 1.00 42.96 C ANISOU 184 CE2 PHE A 26 5833 4558 5934 -3149 1618 -638 C ATOM 185 CZ PHE A 26 2.254 -9.578 14.291 1.00 43.98 C ANISOU 185 CZ PHE A 26 5541 5217 5954 -3372 1587 -851 C ATOM 186 N TYR A 27 8.808 -6.252 14.416 1.00 28.99 N ANISOU 186 N TYR A 27 3625 2074 5315 -688 1305 -205 N ATOM 187 CA TYR A 27 10.230 -6.009 14.184 1.00 27.60 C ANISOU 187 CA TYR A 27 3507 1690 5291 -309 1283 -81 C ATOM 188 C TYR A 27 10.793 -7.159 13.373 1.00 28.97 C ANISOU 188 C TYR A 27 4076 1531 5398 -256 1351 -32 C ATOM 189 O TYR A 27 10.696 -8.319 13.813 1.00 31.13 O ANISOU 189 O TYR A 27 4734 1572 5520 -408 1412 12 O ATOM 190 CB TYR A 27 10.976 -5.807 15.512 1.00 27.22 C ANISOU 190 CB TYR A 27 3428 1634 5280 -158 1262 36 C ATOM 191 CG TYR A 27 12.504 -5.846 15.417 1.00 26.76 C ANISOU 191 CG TYR A 27 3445 1413 5311 199 1252 167 C ATOM 192 CD1 TYR A 27 13.255 -6.632 16.291 1.00 28.09 C ANISOU 192 CD1 TYR A 27 3852 1422 5397 329 1273 295 C ATOM 193 CD2 TYR A 27 13.178 -5.108 14.470 1.00 25.49 C ANISOU 193 CD2 TYR A 27 3107 1301 5276 401 1220 165 C ATOM 194 CE1 TYR A 27 14.633 -6.686 16.196 1.00 30.32 C ANISOU 194 CE1 TYR A 27 4144 1654 5721 687 1257 395 C ATOM 195 CE2 TYR A 27 14.577 -5.134 14.371 1.00 25.58 C ANISOU 195 CE2 TYR A 27 3118 1272 5331 698 1220 272 C ATOM 196 CZ TYR A 27 15.294 -5.922 15.231 1.00 28.23 C ANISOU 196 CZ TYR A 27 3637 1507 5581 857 1236 375 C ATOM 197 OH TYR A 27 16.657 -5.962 15.129 1.00 29.28 O ANISOU 197 OH TYR A 27 3713 1692 5719 1182 1230 460 O ATOM 198 N ILE A 28 11.274 -6.866 12.166 1.00 28.17 N ANISOU 198 N ILE A 28 3926 1403 5375 -64 1342 -52 N ATOM 199 CA ILE A 28 11.823 -7.871 11.259 1.00 29.64 C ANISOU 199 CA ILE A 28 4468 1308 5484 46 1403 -39 C ATOM 200 C ILE A 28 13.355 -8.092 11.320 1.00 29.81 C ANISOU 200 C ILE A 28 4592 1190 5545 467 1420 89 C ATOM 201 O ILE A 28 13.846 -9.263 11.320 1.00 32.05 O ANISOU 201 O ILE A 28 5297 1180 5700 602 1470 130 O ATOM 202 CB ILE A 28 11.427 -7.627 9.773 1.00 29.39 C ANISOU 202 CB ILE A 28 4361 1353 5452 7 1399 -153 C ATOM 203 CG1 ILE A 28 9.911 -7.446 9.577 1.00 29.78 C ANISOU 203 CG1 ILE A 28 4270 1624 5423 -371 1370 -302 C ATOM 204 CG2 ILE A 28 12.015 -8.751 8.824 1.00 31.33 C ANISOU 204 CG2 ILE A 28 5020 1297 5588 143 1468 -163 C ATOM 205 CD1 ILE A 28 9.016 -8.567 10.109 1.00 32.32 C ANISOU 205 CD1 ILE A 28 4882 1845 5551 -781 1423 -359 C ATOM 206 N ALA A 29 14.109 -6.998 11.341 1.00 28.01 N ANISOU 206 N ALA A 29 4001 1180 5460 677 1374 142 N ATOM 207 CA ALA A 29 15.563 -7.042 11.133 1.00 28.44 C ANISOU 207 CA ALA A 29 4027 1249 5531 1054 1392 234 C ATOM 208 C ALA A 29 16.198 -5.636 11.263 1.00 26.65 C ANISOU 208 C ALA A 29 3361 1316 5449 1127 1333 282 C ATOM 209 O ALA A 29 15.484 -4.638 11.231 1.00 25.12 O ANISOU 209 O ALA A 29 2958 1242 5344 931 1276 233 O ATOM 210 CB ALA A 29 15.881 -7.654 9.744 1.00 29.69 C ANISOU 210 CB ALA A 29 4376 1298 5607 1202 1457 183 C ATOM 211 N SER A 30 17.510 -5.585 11.516 1.00 27.34 N ANISOU 211 N SER A 30 3334 1525 5531 1402 1336 372 N ATOM 212 CA SER A 30 18.254 -4.322 11.600 1.00 26.39 C ANISOU 212 CA SER A 30 2831 1686 5509 1412 1287 420 C ATOM 213 C SER A 30 19.720 -4.615 11.415 1.00 28.13 C ANISOU 213 C SER A 30 2944 2095 5649 1725 1326 489 C ATOM 214 O SER A 30 20.154 -5.817 11.448 1.00 30.11 O ANISOU 214 O SER A 30 3437 2238 5767 2013 1374 502 O ATOM 215 CB SER A 30 18.041 -3.623 12.938 1.00 25.43 C ANISOU 215 CB SER A 30 2559 1645 5459 1281 1200 437 C ATOM 216 OG SER A 30 18.539 -4.391 14.012 1.00 29.14 O ANISOU 216 OG SER A 30 3130 2095 5845 1448 1196 499 O ATOM 217 N ALA A 31 20.493 -3.549 11.199 1.00 27.94 N ANISOU 217 N ALA A 31 2581 2362 5673 1679 1305 528 N ATOM 218 CA ALA A 31 21.964 -3.628 11.130 1.00 30.00 C ANISOU 218 CA ALA A 31 2608 2957 5832 1929 1337 587 C ATOM 219 C ALA A 31 22.469 -2.214 11.457 1.00 29.55 C ANISOU 219 C ALA A 31 2197 3181 5849 1677 1272 627 C ATOM 220 O ALA A 31 21.797 -1.239 11.097 1.00 28.02 O ANISOU 220 O ALA A 31 2003 2884 5760 1382 1236 609 O ATOM 221 CB ALA A 31 22.378 -4.022 9.772 1.00 31.27 C ANISOU 221 CB ALA A 31 2791 3195 5896 2088 1437 566 C ATOM 222 N PHE A 32 23.622 -2.088 12.123 1.00 31.27 N ANISOU 222 N PHE A 32 2143 3747 5989 1789 1247 673 N ATOM 223 CA PHE A 32 24.107 -0.757 12.536 1.00 31.34 C ANISOU 223 CA PHE A 32 1856 4006 6045 1479 1175 699 C ATOM 224 C PHE A 32 25.626 -0.731 12.494 1.00 34.44 C ANISOU 224 C PHE A 32 1871 4938 6277 1598 1206 739 C ATOM 225 O PHE A 32 26.267 -1.784 12.615 1.00 36.21 O ANISOU 225 O PHE A 32 2056 5342 6359 2011 1245 741 O ATOM 226 CB PHE A 32 23.730 -0.421 13.992 1.00 30.41 C ANISOU 226 CB PHE A 32 1756 3800 5998 1374 1058 683 C ATOM 227 CG PHE A 32 22.276 -0.623 14.338 1.00 30.20 C ANISOU 227 CG PHE A 32 2043 3353 6078 1307 1029 631 C ATOM 228 CD1 PHE A 32 21.798 -1.888 14.753 1.00 33.71 C ANISOU 228 CD1 PHE A 32 2741 3597 6472 1537 1060 628 C ATOM 229 CD2 PHE A 32 21.406 0.436 14.296 1.00 28.98 C ANISOU 229 CD2 PHE A 32 1943 3030 6039 1020 966 582 C ATOM 230 CE1 PHE A 32 20.473 -2.056 15.087 1.00 31.34 C ANISOU 230 CE1 PHE A 32 2679 2997 6232 1405 1044 576 C ATOM 231 CE2 PHE A 32 20.094 0.288 14.628 1.00 29.11 C ANISOU 231 CE2 PHE A 32 2168 2776 6116 972 940 515 C ATOM 232 CZ PHE A 32 19.614 -0.953 15.021 1.00 29.01 C ANISOU 232 CZ PHE A 32 2345 2629 6051 1130 986 511 C ATOM 233 N ARG A 33 26.203 0.469 12.392 1.00 35.17 N ANISOU 233 N ARG A 33 1697 5303 6363 1239 1178 764 N ATOM 234 CA ARG A 33 27.644 0.629 12.586 1.00 38.78 C ANISOU 234 CA ARG A 33 1718 6374 6643 1254 1189 788 C ATOM 235 C ARG A 33 27.948 0.959 14.054 1.00 39.40 C ANISOU 235 C ARG A 33 1649 6601 6721 1179 1058 774 C ATOM 236 O ARG A 33 29.077 0.775 14.527 1.00 41.90 O ANISOU 236 O ARG A 33 1603 7452 6866 1315 1040 776 O ATOM 237 CB ARG A 33 28.215 1.681 11.620 1.00 40.87 C ANISOU 237 CB ARG A 33 1772 6914 6843 840 1245 829 C ATOM 238 CG ARG A 33 28.280 1.195 10.159 1.00 41.19 C ANISOU 238 CG ARG A 33 1847 7004 6799 997 1393 845 C ATOM 239 CD ARG A 33 28.948 2.193 9.265 1.00 44.08 C ANISOU 239 CD ARG A 33 1991 7707 7052 569 1460 906 C ATOM 240 NE ARG A 33 29.206 1.678 7.915 1.00 44.54 N ANISOU 240 NE ARG A 33 2008 7943 6974 750 1613 916 N ATOM 241 CZ ARG A 33 29.656 2.428 6.908 1.00 48.84 C ANISOU 241 CZ ARG A 33 2420 8743 7393 390 1701 983 C ATOM 242 NH1 ARG A 33 29.899 3.721 7.102 1.00 48.79 N ANISOU 242 NH1 ARG A 33 2356 8799 7381 -191 1646 1053 N ATOM 243 NH2 ARG A 33 29.887 1.891 5.706 1.00 50.16 N ANISOU 243 NH2 ARG A 33 2542 9103 7414 593 1846 981 N ATOM 244 N ASN A 34 26.939 1.461 14.754 1.00 36.42 N ANISOU 244 N ASN A 34 1532 5798 6509 977 964 746 N ATOM 245 CA ASN A 34 26.993 1.751 16.191 1.00 37.77 C ANISOU 245 CA ASN A 34 1641 6023 6688 913 835 716 C ATOM 246 C ASN A 34 27.006 0.465 17.082 1.00 39.05 C ANISOU 246 C ASN A 34 1871 6191 6775 1389 817 725 C ATOM 247 O ASN A 34 26.048 -0.324 17.085 1.00 35.11 O ANISOU 247 O ASN A 34 1720 5276 6344 1586 848 726 O ATOM 248 CB ASN A 34 25.780 2.627 16.566 1.00 34.92 C ANISOU 248 CB ASN A 34 1577 5187 6505 613 753 665 C ATOM 249 CG ASN A 34 25.744 2.973 18.041 1.00 36.38 C ANISOU 249 CG ASN A 34 1728 5408 6687 541 623 614 C ATOM 250 OD1 ASN A 34 24.990 2.380 18.812 1.00 36.65 O ANISOU 250 OD1 ASN A 34 1947 5218 6759 737 596 592 O ATOM 251 ND2 ASN A 34 26.577 3.924 18.445 1.00 37.81 N ANISOU 251 ND2 ASN A 34 1674 5894 6797 229 543 591 N ATOM 252 N GLU A 35 28.080 0.272 17.845 1.00 43.15 N ANISOU 252 N GLU A 35 2077 7192 7128 1552 760 734 N ATOM 253 CA GLU A 35 28.252 -1.008 18.554 1.00 46.34 C ANISOU 253 CA GLU A 35 2577 7625 7406 2075 742 766 C ATOM 254 C GLU A 35 27.314 -1.274 19.723 1.00 44.39 C ANISOU 254 C GLU A 35 2645 6993 7227 2097 664 769 C ATOM 255 O GLU A 35 26.847 -2.406 19.918 1.00 44.11 O ANISOU 255 O GLU A 35 2942 6669 7150 2433 693 812 O ATOM 256 CB GLU A 35 29.706 -1.278 18.913 1.00 50.76 C ANISOU 256 CB GLU A 35 2697 8873 7718 2357 702 776 C ATOM 257 CG GLU A 35 30.510 -1.914 17.740 1.00 58.75 C ANISOU 257 CG GLU A 35 3532 10216 8575 2698 820 784 C ATOM 258 CD GLU A 35 29.634 -2.806 16.810 1.00 62.12 C ANISOU 258 CD GLU A 35 4433 10082 9087 2937 933 798 C ATOM 259 OE1 GLU A 35 29.390 -2.407 15.641 1.00 61.99 O ANISOU 259 OE1 GLU A 35 4429 9970 9155 2703 1032 783 O ATOM 260 OE2 GLU A 35 29.174 -3.892 17.252 1.00 63.67 O ANISOU 260 OE2 GLU A 35 5019 9923 9248 3325 918 825 O ATOM 261 N GLU A 36 27.032 -0.229 20.483 1.00 44.41 N ANISOU 261 N GLU A 36 2576 6986 7313 1720 569 718 N ATOM 262 CA GLU A 36 25.990 -0.258 21.509 1.00 43.62 C ANISOU 262 CA GLU A 36 2754 6535 7283 1657 510 698 C ATOM 263 C GLU A 36 24.632 -0.806 21.026 1.00 40.72 C ANISOU 263 C GLU A 36 2802 5632 7038 1672 596 701 C ATOM 264 O GLU A 36 24.029 -1.656 21.673 1.00 40.66 O ANISOU 264 O GLU A 36 3062 5404 6982 1838 602 735 O ATOM 265 CB GLU A 36 25.780 1.157 22.034 1.00 43.57 C ANISOU 265 CB GLU A 36 2642 6547 7365 1213 411 606 C ATOM 266 CG GLU A 36 25.509 1.228 23.514 1.00 48.32 C ANISOU 266 CG GLU A 36 3287 7161 7912 1214 303 571 C ATOM 267 CD GLU A 36 26.612 0.558 24.304 1.00 57.69 C ANISOU 267 CD GLU A 36 4248 8788 8884 1522 242 630 C ATOM 268 OE1 GLU A 36 27.795 0.955 24.151 1.00 64.57 O ANISOU 268 OE1 GLU A 36 4742 10143 9651 1469 201 617 O ATOM 269 OE2 GLU A 36 26.304 -0.385 25.067 1.00 61.91 O ANISOU 269 OE2 GLU A 36 4984 9214 9325 1818 233 692 O ATOM 270 N TYR A 37 24.130 -0.289 19.915 1.00 38.36 N ANISOU 270 N TYR A 37 2559 5144 6872 1460 658 664 N ATOM 271 CA TYR A 37 22.869 -0.788 19.367 1.00 35.52 C ANISOU 271 CA TYR A 37 2537 4358 6601 1454 733 649 C ATOM 272 C TYR A 37 23.021 -2.246 18.881 1.00 36.44 C ANISOU 272 C TYR A 37 2865 4368 6613 1810 826 716 C ATOM 273 O TYR A 37 22.138 -3.065 19.117 1.00 35.07 O ANISOU 273 O TYR A 37 3020 3885 6422 1859 860 726 O ATOM 274 CB TYR A 37 22.390 0.114 18.234 1.00 34.49 C ANISOU 274 CB TYR A 37 2405 4097 6601 1192 762 599 C ATOM 275 CG TYR A 37 21.573 1.333 18.652 1.00 34.62 C ANISOU 275 CG TYR A 37 2453 3977 6724 893 674 509 C ATOM 276 CD1 TYR A 37 21.059 1.472 19.948 1.00 37.03 C ANISOU 276 CD1 TYR A 37 2803 4251 7017 861 597 457 C ATOM 277 CD2 TYR A 37 21.240 2.317 17.712 1.00 34.20 C ANISOU 277 CD2 TYR A 37 2431 3806 6759 681 666 472 C ATOM 278 CE1 TYR A 37 20.250 2.608 20.300 1.00 36.18 C ANISOU 278 CE1 TYR A 37 2748 4017 6981 651 513 345 C ATOM 279 CE2 TYR A 37 20.446 3.441 18.060 1.00 32.61 C ANISOU 279 CE2 TYR A 37 2324 3440 6626 486 570 377 C ATOM 280 CZ TYR A 37 19.971 3.589 19.341 1.00 33.66 C ANISOU 280 CZ TYR A 37 2482 3564 6745 487 494 303 C ATOM 281 OH TYR A 37 19.184 4.707 19.646 1.00 35.38 O ANISOU 281 OH TYR A 37 2811 3629 7005 360 396 184 O ATOM 282 N ASN A 38 24.134 -2.586 18.215 1.00 36.81 N ANISOU 282 N ASN A 38 2745 4680 6562 2052 867 754 N ATOM 283 CA ASN A 38 24.388 -4.017 17.851 1.00 39.33 C ANISOU 283 CA ASN A 38 3316 4889 6737 2483 937 801 C ATOM 284 C ASN A 38 24.301 -4.975 19.049 1.00 40.79 C ANISOU 284 C ASN A 38 3767 4942 6788 2740 887 865 C ATOM 285 O ASN A 38 23.628 -5.997 19.001 1.00 39.98 O ANISOU 285 O ASN A 38 4108 4449 6633 2852 934 892 O ATOM 286 CB ASN A 38 25.739 -4.186 17.126 1.00 41.54 C ANISOU 286 CB ASN A 38 3307 5596 6881 2783 975 813 C ATOM 287 CG ASN A 38 25.614 -3.954 15.624 1.00 42.19 C ANISOU 287 CG ASN A 38 3370 5634 7026 2667 1080 774 C ATOM 288 OD1 ASN A 38 24.547 -4.141 15.062 1.00 44.35 O ANISOU 288 OD1 ASN A 38 3954 5496 7403 2522 1128 745 O ATOM 289 ND2 ASN A 38 26.694 -3.561 14.975 1.00 44.49 N ANISOU 289 ND2 ASN A 38 3283 6391 7229 2718 1116 772 N ATOM 290 N LYS A 39 24.997 -4.600 20.115 1.00 43.37 N ANISOU 290 N LYS A 39 3835 5605 7040 2795 786 890 N ATOM 291 CA LYS A 39 24.993 -5.277 21.405 1.00 46.30 C ANISOU 291 CA LYS A 39 4403 5924 7266 3005 714 962 C ATOM 292 C LYS A 39 23.591 -5.487 22.006 1.00 44.39 C ANISOU 292 C LYS A 39 4540 5239 7086 2734 730 968 C ATOM 293 O LYS A 39 23.246 -6.595 22.423 1.00 46.11 O ANISOU 293 O LYS A 39 5187 5168 7166 2916 749 1049 O ATOM 294 CB LYS A 39 25.789 -4.425 22.393 1.00 47.78 C ANISOU 294 CB LYS A 39 4163 6587 7404 2943 592 948 C ATOM 295 CG LYS A 39 27.099 -4.942 22.759 1.00 53.24 C ANISOU 295 CG LYS A 39 4650 7718 7862 3408 527 1000 C ATOM 296 CD LYS A 39 26.996 -5.838 23.966 1.00 58.70 C ANISOU 296 CD LYS A 39 5658 8277 8369 3710 454 1097 C ATOM 297 CE LYS A 39 28.312 -6.568 24.153 1.00 63.75 C ANISOU 297 CE LYS A 39 6158 9334 8728 4326 386 1152 C ATOM 298 NZ LYS A 39 28.088 -7.969 24.595 1.00 67.94 N ANISOU 298 NZ LYS A 39 7283 9475 9058 4788 376 1275 N ATOM 299 N SER A 40 22.786 -4.436 22.091 1.00 41.57 N ANISOU 299 N SER A 40 4046 4847 6903 2303 721 883 N ATOM 300 CA SER A 40 21.485 -4.619 22.737 1.00 40.06 C ANISOU 300 CA SER A 40 4135 4361 6726 2063 739 872 C ATOM 301 C SER A 40 20.498 -5.363 21.849 1.00 38.66 C ANISOU 301 C SER A 40 4316 3798 6576 1966 850 862 C ATOM 302 O SER A 40 19.719 -6.201 22.333 1.00 39.66 O ANISOU 302 O SER A 40 4807 3666 6597 1896 889 907 O ATOM 303 CB SER A 40 20.893 -3.287 23.216 1.00 38.21 C ANISOU 303 CB SER A 40 3654 4241 6624 1707 681 761 C ATOM 304 OG SER A 40 20.665 -2.411 22.131 1.00 38.63 O ANISOU 304 OG SER A 40 3555 4277 6848 1515 703 672 O ATOM 305 N VAL A 41 20.556 -5.083 20.554 1.00 36.38 N ANISOU 305 N VAL A 41 3935 3488 6400 1934 901 805 N ATOM 306 CA VAL A 41 19.564 -5.605 19.621 1.00 34.93 C ANISOU 306 CA VAL A 41 4033 2989 6249 1786 994 763 C ATOM 307 C VAL A 41 19.812 -7.094 19.297 1.00 37.83 C ANISOU 307 C VAL A 41 4842 3083 6449 2067 1055 838 C ATOM 308 O VAL A 41 18.873 -7.819 18.949 1.00 37.81 O ANISOU 308 O VAL A 41 5205 2759 6402 1897 1122 818 O ATOM 309 CB VAL A 41 19.496 -4.739 18.356 1.00 33.47 C ANISOU 309 CB VAL A 41 3619 2878 6221 1655 1017 677 C ATOM 310 CG1 VAL A 41 18.766 -5.456 17.220 1.00 33.24 C ANISOU 310 CG1 VAL A 41 3874 2573 6183 1597 1108 636 C ATOM 311 CG2 VAL A 41 18.869 -3.332 18.690 1.00 28.88 C ANISOU 311 CG2 VAL A 41 2770 2424 5779 1349 950 589 C ATOM 312 N GLN A 42 21.066 -7.521 19.416 1.00 39.50 N ANISOU 312 N GLN A 42 5025 3441 6542 2494 1024 910 N ATOM 313 CA GLN A 42 21.473 -8.937 19.327 1.00 43.52 C ANISOU 313 CA GLN A 42 6004 3690 6840 2887 1050 986 C ATOM 314 C GLN A 42 20.609 -9.909 20.113 1.00 44.69 C ANISOU 314 C GLN A 42 6706 3429 6845 2759 1063 1061 C ATOM 315 O GLN A 42 20.333 -11.015 19.653 1.00 45.97 O ANISOU 315 O GLN A 42 7398 3191 6876 2843 1118 1080 O ATOM 316 CB GLN A 42 22.843 -9.083 19.933 1.00 45.83 C ANISOU 316 CB GLN A 42 6122 4307 6986 3372 969 1062 C ATOM 317 CG GLN A 42 23.966 -9.130 18.961 1.00 50.99 C ANISOU 317 CG GLN A 42 6546 5236 7591 3762 989 1025 C ATOM 318 CD GLN A 42 25.194 -9.632 19.650 1.00 56.76 C ANISOU 318 CD GLN A 42 7216 6259 8092 4324 904 1100 C ATOM 319 OE1 GLN A 42 25.531 -9.164 20.740 1.00 58.39 O ANISOU 319 OE1 GLN A 42 7166 6750 8269 4305 810 1146 O ATOM 320 NE2 GLN A 42 25.852 -10.616 19.051 1.00 63.21 N ANISOU 320 NE2 GLN A 42 8287 7015 8716 4863 928 1103 N ATOM 321 N GLU A 43 20.226 -9.478 21.313 1.00 43.73 N ANISOU 321 N GLU A 43 6473 3419 6723 2542 1014 1100 N ATOM 322 CA GLU A 43 19.557 -10.301 22.280 1.00 45.62 C ANISOU 322 CA GLU A 43 7179 3370 6784 2407 1022 1198 C ATOM 323 C GLU A 43 18.073 -10.412 21.969 1.00 43.72 C ANISOU 323 C GLU A 43 7136 2889 6586 1864 1113 1127 C ATOM 324 O GLU A 43 17.365 -11.259 22.547 1.00 45.33 O ANISOU 324 O GLU A 43 7808 2806 6609 1648 1153 1203 O ATOM 325 CB GLU A 43 19.735 -9.689 23.664 1.00 46.02 C ANISOU 325 CB GLU A 43 6963 3720 6804 2375 937 1249 C ATOM 326 CG GLU A 43 21.179 -9.465 24.088 1.00 50.32 C ANISOU 326 CG GLU A 43 7222 4615 7284 2858 828 1301 C ATOM 327 CD GLU A 43 21.298 -9.027 25.543 1.00 54.47 C ANISOU 327 CD GLU A 43 7572 5398 7727 2816 736 1354 C ATOM 328 OE1 GLU A 43 22.275 -9.445 26.203 1.00 60.31 O ANISOU 328 OE1 GLU A 43 8350 6288 8275 3243 646 1456 O ATOM 329 OE2 GLU A 43 20.417 -8.282 26.038 1.00 55.66 O ANISOU 329 OE2 GLU A 43 7549 5623 7975 2392 748 1285 O ATOM 330 N ILE A 44 17.597 -9.553 21.069 1.00 39.73 N ANISOU 330 N ILE A 44 6275 2531 6289 1629 1144 984 N ATOM 331 CA ILE A 44 16.174 -9.557 20.689 1.00 37.60 C ANISOU 331 CA ILE A 44 6091 2146 6048 1136 1218 887 C ATOM 332 C ILE A 44 15.827 -10.806 19.869 1.00 40.23 C ANISOU 332 C ILE A 44 6984 2056 6246 1077 1295 892 C ATOM 333 O ILE A 44 16.341 -11.003 18.761 1.00 40.66 O ANISOU 333 O ILE A 44 7088 2015 6345 1311 1311 849 O ATOM 334 CB ILE A 44 15.722 -8.251 19.973 1.00 33.72 C ANISOU 334 CB ILE A 44 5087 1938 5786 951 1207 733 C ATOM 335 CG1 ILE A 44 15.782 -7.075 20.940 1.00 31.12 C ANISOU 335 CG1 ILE A 44 4333 1947 5545 912 1129 707 C ATOM 336 CG2 ILE A 44 14.269 -8.374 19.499 1.00 32.46 C ANISOU 336 CG2 ILE A 44 5007 1717 5609 506 1274 621 C ATOM 337 CD1 ILE A 44 15.661 -5.686 20.248 1.00 28.49 C ANISOU 337 CD1 ILE A 44 3556 1846 5423 848 1087 577 C ATOM 338 N GLN A 45 14.964 -11.660 20.414 1.00 41.37 N ANISOU 338 N GLN A 45 7572 1949 6198 740 1347 941 N ATOM 339 CA GLN A 45 14.539 -12.826 19.638 1.00 43.38 C ANISOU 339 CA GLN A 45 8412 1767 6302 590 1415 927 C ATOM 340 C GLN A 45 13.362 -12.502 18.742 1.00 41.71 C ANISOU 340 C GLN A 45 8017 1660 6171 114 1474 756 C ATOM 341 O GLN A 45 13.301 -12.980 17.605 1.00 42.49 O ANISOU 341 O GLN A 45 8344 1543 6258 114 1506 677 O ATOM 342 CB GLN A 45 14.238 -14.047 20.530 1.00 47.24 C ANISOU 342 CB GLN A 45 9594 1862 6492 416 1444 1074 C ATOM 343 CG GLN A 45 15.462 -14.597 21.205 1.00 49.50 C ANISOU 343 CG GLN A 45 10195 1967 6645 991 1372 1246 C ATOM 344 CD GLN A 45 15.093 -15.545 22.295 1.00 55.23 C ANISOU 344 CD GLN A 45 11542 2369 7074 784 1387 1415 C ATOM 345 OE1 GLN A 45 14.596 -15.131 23.336 1.00 57.81 O ANISOU 345 OE1 GLN A 45 11656 2944 7366 490 1393 1466 O ATOM 346 NE2 GLN A 45 15.326 -16.833 22.070 1.00 57.81 N ANISOU 346 NE2 GLN A 45 12684 2122 7158 936 1393 1504 N ATOM 347 N ALA A 46 12.420 -11.736 19.266 1.00 40.13 N ANISOU 347 N ALA A 46 7421 1808 6019 -264 1482 688 N ATOM 348 CA ALA A 46 11.280 -11.285 18.491 1.00 38.96 C ANISOU 348 CA ALA A 46 6998 1878 5929 -659 1516 511 C ATOM 349 C ALA A 46 10.685 -10.057 19.162 1.00 36.69 C ANISOU 349 C ALA A 46 6121 2078 5742 -790 1482 434 C ATOM 350 O ALA A 46 10.918 -9.817 20.348 1.00 37.02 O ANISOU 350 O ALA A 46 6081 2236 5748 -725 1457 519 O ATOM 351 CB ALA A 46 10.241 -12.368 18.356 1.00 42.24 C ANISOU 351 CB ALA A 46 7872 2074 6104 -1189 1599 482 C ATOM 352 N THR A 47 9.929 -9.268 18.412 1.00 35.03 N ANISOU 352 N THR A 47 5519 2157 5634 -934 1470 267 N ATOM 353 CA THR A 47 9.201 -8.156 19.010 1.00 33.62 C ANISOU 353 CA THR A 47 4839 2433 5502 -1040 1433 162 C ATOM 354 C THR A 47 8.034 -7.814 18.139 1.00 33.58 C ANISOU 354 C THR A 47 4582 2697 5478 -1302 1441 -25 C ATOM 355 O THR A 47 8.201 -7.704 16.921 1.00 32.69 O ANISOU 355 O THR A 47 4461 2495 5463 -1183 1420 -81 O ATOM 356 CB THR A 47 10.080 -6.887 19.100 1.00 30.75 C ANISOU 356 CB THR A 47 4108 2209 5368 -617 1332 165 C ATOM 357 OG1 THR A 47 11.162 -7.133 20.008 1.00 32.75 O ANISOU 357 OG1 THR A 47 4515 2315 5614 -373 1310 323 O ATOM 358 CG2 THR A 47 9.298 -5.703 19.599 1.00 29.69 C ANISOU 358 CG2 THR A 47 3527 2488 5267 -676 1279 28 C ATOM 359 N PHE A 48 6.856 -7.645 18.748 1.00 34.85 N ANISOU 359 N PHE A 48 4516 3238 5487 -1642 1469 -130 N ATOM 360 CA PHE A 48 5.814 -6.864 18.097 1.00 34.48 C ANISOU 360 CA PHE A 48 4043 3619 5441 -1729 1432 -336 C ATOM 361 C PHE A 48 5.363 -5.697 18.972 1.00 33.72 C ANISOU 361 C PHE A 48 3491 3966 5355 -1596 1373 -434 C ATOM 362 O PHE A 48 5.653 -5.655 20.157 1.00 33.91 O ANISOU 362 O PHE A 48 3535 4007 5341 -1568 1385 -355 O ATOM 363 CB PHE A 48 4.643 -7.737 17.664 1.00 37.51 C ANISOU 363 CB PHE A 48 4513 4159 5581 -2260 1513 -440 C ATOM 364 CG PHE A 48 3.918 -8.411 18.792 1.00 40.56 C ANISOU 364 CG PHE A 48 4984 4729 5697 -2730 1611 -417 C ATOM 365 CD1 PHE A 48 4.209 -9.732 19.131 1.00 45.01 C ANISOU 365 CD1 PHE A 48 6137 4862 6102 -3034 1701 -257 C ATOM 366 CD2 PHE A 48 2.909 -7.750 19.484 1.00 42.87 C ANISOU 366 CD2 PHE A 48 4798 5636 5855 -2872 1614 -558 C ATOM 367 CE1 PHE A 48 3.520 -10.389 20.156 1.00 47.62 C ANISOU 367 CE1 PHE A 48 6601 5348 6144 -3536 1800 -213 C ATOM 368 CE2 PHE A 48 2.220 -8.395 20.518 1.00 44.91 C ANISOU 368 CE2 PHE A 48 5116 6123 5824 -3358 1723 -533 C ATOM 369 CZ PHE A 48 2.530 -9.723 20.842 1.00 49.47 C ANISOU 369 CZ PHE A 48 6309 6242 6246 -3723 1820 -348 C ATOM 370 N PHE A 49 4.657 -4.744 18.390 1.00 33.17 N ANISOU 370 N PHE A 49 3037 4252 5316 -1478 1300 -614 N ATOM 371 CA PHE A 49 4.309 -3.543 19.121 1.00 32.67 C ANISOU 371 CA PHE A 49 2595 4554 5263 -1245 1221 -728 C ATOM 372 C PHE A 49 3.103 -2.831 18.499 1.00 33.72 C ANISOU 372 C PHE A 49 2334 5181 5296 -1208 1160 -960 C ATOM 373 O PHE A 49 2.717 -3.112 17.364 1.00 34.20 O ANISOU 373 O PHE A 49 2396 5265 5332 -1307 1156 -1018 O ATOM 374 CB PHE A 49 5.540 -2.594 19.307 1.00 29.96 C ANISOU 374 CB PHE A 49 2285 3928 5170 -795 1119 -638 C ATOM 375 CG PHE A 49 6.091 -2.052 18.027 1.00 29.87 C ANISOU 375 CG PHE A 49 2307 3693 5348 -537 1042 -628 C ATOM 376 CD1 PHE A 49 7.177 -2.660 17.411 1.00 30.02 C ANISOU 376 CD1 PHE A 49 2620 3296 5489 -491 1075 -467 C ATOM 377 CD2 PHE A 49 5.535 -0.926 17.421 1.00 30.12 C ANISOU 377 CD2 PHE A 49 2093 3942 5408 -312 933 -777 C ATOM 378 CE1 PHE A 49 7.696 -2.146 16.217 1.00 27.05 C ANISOU 378 CE1 PHE A 49 2257 2760 5259 -278 1018 -453 C ATOM 379 CE2 PHE A 49 6.037 -0.447 16.215 1.00 26.64 C ANISOU 379 CE2 PHE A 49 1725 3286 5112 -108 867 -745 C ATOM 380 CZ PHE A 49 7.108 -1.068 15.618 1.00 25.53 C ANISOU 380 CZ PHE A 49 1845 2766 5088 -120 919 -582 C ATOM 381 N TYR A 50 2.528 -1.906 19.259 1.00 34.37 N ANISOU 381 N TYR A 50 2085 5674 5301 -1027 1103 -1102 N ATOM 382 CA TYR A 50 1.413 -1.079 18.794 1.00 35.81 C ANISOU 382 CA TYR A 50 1870 6375 5360 -854 1017 -1339 C ATOM 383 C TYR A 50 1.768 0.418 18.844 1.00 34.37 C ANISOU 383 C TYR A 50 1603 6128 5328 -288 855 -1406 C ATOM 384 O TYR A 50 2.243 0.912 19.874 1.00 33.77 O ANISOU 384 O TYR A 50 1558 5971 5301 -129 831 -1380 O ATOM 385 CB TYR A 50 0.193 -1.318 19.682 1.00 39.13 C ANISOU 385 CB TYR A 50 1949 7456 5462 -1129 1094 -1500 C ATOM 386 CG TYR A 50 -0.371 -2.713 19.559 1.00 42.64 C ANISOU 386 CG TYR A 50 2473 8034 5695 -1768 1246 -1466 C ATOM 387 CD1 TYR A 50 0.264 -3.809 20.161 1.00 42.72 C ANISOU 387 CD1 TYR A 50 2891 7638 5702 -2135 1370 -1253 C ATOM 388 CD2 TYR A 50 -1.542 -2.939 18.842 1.00 45.66 C ANISOU 388 CD2 TYR A 50 2552 8946 5850 -2012 1256 -1651 C ATOM 389 CE1 TYR A 50 -0.262 -5.098 20.039 1.00 47.83 C ANISOU 389 CE1 TYR A 50 3713 8334 6125 -2759 1503 -1218 C ATOM 390 CE2 TYR A 50 -2.067 -4.216 18.712 1.00 49.21 C ANISOU 390 CE2 TYR A 50 3113 9505 6080 -2676 1392 -1631 C ATOM 391 CZ TYR A 50 -1.425 -5.289 19.312 1.00 49.26 C ANISOU 391 CZ TYR A 50 3597 9031 6088 -3061 1517 -1410 C ATOM 392 OH TYR A 50 -1.960 -6.549 19.179 1.00 56.24 O ANISOU 392 OH TYR A 50 4682 9960 6727 -3752 1645 -1389 O ATOM 393 N PHE A 51 1.531 1.123 17.735 1.00 34.20 N ANISOU 393 N PHE A 51 1514 6127 5353 -3 738 -1490 N ATOM 394 CA PHE A 51 1.565 2.593 17.746 1.00 34.04 C ANISOU 394 CA PHE A 51 1438 6104 5390 523 570 -1592 C ATOM 395 C PHE A 51 0.168 3.109 17.808 1.00 37.17 C ANISOU 395 C PHE A 51 1439 7165 5518 717 504 -1859 C ATOM 396 O PHE A 51 -0.668 2.686 17.016 1.00 38.81 O ANISOU 396 O PHE A 51 1445 7729 5573 584 516 -1952 O ATOM 397 CB PHE A 51 2.218 3.172 16.486 1.00 32.41 C ANISOU 397 CB PHE A 51 1462 5480 5371 771 464 -1502 C ATOM 398 CG PHE A 51 3.728 3.076 16.468 1.00 29.65 C ANISOU 398 CG PHE A 51 1460 4525 5281 722 492 -1266 C ATOM 399 CD1 PHE A 51 4.409 3.084 15.257 1.00 28.29 C ANISOU 399 CD1 PHE A 51 1494 4006 5249 756 472 -1139 C ATOM 400 CD2 PHE A 51 4.460 2.989 17.644 1.00 28.79 C ANISOU 400 CD2 PHE A 51 1439 4256 5242 651 535 -1181 C ATOM 401 CE1 PHE A 51 5.835 3.007 15.219 1.00 26.77 C ANISOU 401 CE1 PHE A 51 1561 3348 5261 718 503 -934 C ATOM 402 CE2 PHE A 51 5.875 2.903 17.604 1.00 26.71 C ANISOU 402 CE2 PHE A 51 1438 3525 5186 624 551 -978 C ATOM 403 CZ PHE A 51 6.542 2.926 16.398 1.00 25.55 C ANISOU 403 CZ PHE A 51 1459 3080 5169 659 538 -862 C ATOM 404 N THR A 52 -0.075 4.015 18.754 1.00 38.69 N ANISOU 404 N THR A 52 1513 7556 5630 1044 428 -1996 N ATOM 405 CA THR A 52 -1.336 4.777 18.826 1.00 42.91 C ANISOU 405 CA THR A 52 1678 8734 5893 1416 327 -2282 C ATOM 406 C THR A 52 -0.911 6.230 18.982 1.00 43.07 C ANISOU 406 C THR A 52 1925 8432 6006 2009 139 -2337 C ATOM 407 O THR A 52 -0.686 6.691 20.089 1.00 42.59 O ANISOU 407 O THR A 52 1905 8343 5933 2140 126 -2390 O ATOM 408 CB THR A 52 -2.219 4.338 20.023 1.00 45.73 C ANISOU 408 CB THR A 52 1646 9764 5964 1202 444 -2439 C ATOM 409 OG1 THR A 52 -2.416 2.925 19.948 1.00 47.98 O ANISOU 409 OG1 THR A 52 1859 10197 6175 546 628 -2336 O ATOM 410 CG2 THR A 52 -3.601 5.021 19.999 1.00 51.00 C ANISOU 410 CG2 THR A 52 1845 11237 6296 1599 349 -2761 C ATOM 411 N PRO A 53 -0.748 6.941 17.859 1.00 43.72 N ANISOU 411 N PRO A 53 2214 8224 6174 2338 -8 -2314 N ATOM 412 CA PRO A 53 -0.386 8.347 17.858 1.00 45.15 C ANISOU 412 CA PRO A 53 2707 8036 6411 2875 -202 -2358 C ATOM 413 C PRO A 53 -1.476 9.241 18.474 1.00 50.46 C ANISOU 413 C PRO A 53 3149 9235 6790 3416 -327 -2669 C ATOM 414 O PRO A 53 -2.669 8.970 18.297 1.00 52.81 O ANISOU 414 O PRO A 53 3005 10244 6816 3506 -317 -2861 O ATOM 415 CB PRO A 53 -0.257 8.661 16.365 1.00 45.07 C ANISOU 415 CB PRO A 53 2908 7747 6469 3035 -307 -2266 C ATOM 416 CG PRO A 53 0.006 7.320 15.706 1.00 42.79 C ANISOU 416 CG PRO A 53 2532 7442 6283 2482 -137 -2096 C ATOM 417 CD PRO A 53 -0.860 6.404 16.491 1.00 43.34 C ANISOU 417 CD PRO A 53 2169 8142 6157 2179 3 -2229 C ATOM 418 N ASN A 54 -1.035 10.254 19.227 1.00 52.18 N ANISOU 418 N ASN A 54 3657 9128 7041 3749 -438 -2726 N ATOM 419 CA ASN A 54 -1.833 11.399 19.625 1.00 57.54 C ANISOU 419 CA ASN A 54 4316 10080 7465 4419 -614 -3012 C ATOM 420 C ASN A 54 -1.328 12.585 18.828 1.00 58.59 C ANISOU 420 C ASN A 54 5017 9553 7689 4847 -831 -2952 C ATOM 421 O ASN A 54 -0.368 13.253 19.240 1.00 58.71 O ANISOU 421 O ASN A 54 5501 8940 7866 4853 -896 -2866 O ATOM 422 CB ASN A 54 -1.684 11.708 21.123 1.00 58.25 C ANISOU 422 CB ASN A 54 4405 10231 7494 4477 -590 -3138 C ATOM 423 CG ASN A 54 -2.662 12.803 21.591 1.00 64.92 C ANISOU 423 CG ASN A 54 5178 11476 8014 5222 -761 -3486 C ATOM 424 OD1 ASN A 54 -3.384 13.395 20.784 1.00 68.69 O ANISOU 424 OD1 ASN A 54 5651 12131 8319 5739 -916 -3619 O ATOM 425 ND2 ASN A 54 -2.683 13.071 22.897 1.00 66.59 N ANISOU 425 ND2 ASN A 54 5343 11843 8116 5317 -739 -3642 N ATOM 426 N LYS A 55 -1.960 12.816 17.681 1.00 60.70 N ANISOU 426 N LYS A 55 5255 9974 7835 5158 -940 -2989 N ATOM 427 CA LYS A 55 -1.635 13.910 16.763 1.00 62.72 C ANISOU 427 CA LYS A 55 6069 9645 8116 5582 -1154 -2920 C ATOM 428 C LYS A 55 -1.649 15.292 17.432 1.00 66.50 C ANISOU 428 C LYS A 55 6987 9814 8466 6183 -1359 -3095 C ATOM 429 O LYS A 55 -0.877 16.179 17.051 1.00 67.37 O ANISOU 429 O LYS A 55 7744 9170 8683 6299 -1497 -2965 O ATOM 430 CB LYS A 55 -2.639 13.932 15.607 1.00 65.08 C ANISOU 430 CB LYS A 55 6155 10379 8192 5943 -1256 -3006 C ATOM 431 CG LYS A 55 -2.828 12.606 14.889 1.00 63.94 C ANISOU 431 CG LYS A 55 5575 10615 8106 5398 -1079 -2893 C ATOM 432 CD LYS A 55 -4.200 12.581 14.195 1.00 69.01 C ANISOU 432 CD LYS A 55 5778 12037 8407 5799 -1176 -3111 C ATOM 433 CE LYS A 55 -4.148 11.694 12.958 1.00 66.89 C ANISOU 433 CE LYS A 55 5384 11819 8213 5385 -1098 -2946 C ATOM 434 NZ LYS A 55 -5.508 11.439 12.408 1.00 69.77 N ANISOU 434 NZ LYS A 55 5198 13084 8227 5626 -1159 -3176 N ATOM 435 N THR A 56 -2.550 15.496 18.393 1.00 69.45 N ANISOU 435 N THR A 56 7035 10776 8576 6567 -1383 -3400 N ATOM 436 CA THR A 56 -2.624 16.793 19.065 1.00 72.87 C ANISOU 436 CA THR A 56 7909 10930 8850 7191 -1584 -3607 C ATOM 437 C THR A 56 -1.366 17.048 19.918 1.00 70.56 C ANISOU 437 C THR A 56 8059 9944 8807 6800 -1546 -3478 C ATOM 438 O THR A 56 -0.900 18.201 20.044 1.00 72.82 O ANISOU 438 O THR A 56 9008 9581 9080 7111 -1733 -3510 O ATOM 439 CB THR A 56 -3.959 16.985 19.880 1.00 77.81 C ANISOU 439 CB THR A 56 8041 12447 9078 7782 -1623 -4005 C ATOM 440 OG1 THR A 56 -3.969 16.161 21.047 1.00 77.24 O ANISOU 440 OG1 THR A 56 7491 12836 9023 7327 -1406 -4061 O ATOM 441 CG2 THR A 56 -5.192 16.654 19.029 1.00 78.40 C ANISOU 441 CG2 THR A 56 7582 13328 8880 8107 -1655 -4138 C ATOM 442 N GLU A 57 -0.799 15.963 20.462 1.00 65.80 N ANISOU 442 N GLU A 57 7124 9466 8411 6104 -1314 -3327 N ATOM 443 CA GLU A 57 0.328 16.078 21.383 1.00 63.50 C ANISOU 443 CA GLU A 57 7125 8685 8316 5729 -1268 -3229 C ATOM 444 C GLU A 57 1.687 15.788 20.756 1.00 58.59 C ANISOU 444 C GLU A 57 6823 7406 8032 5145 -1206 -2877 C ATOM 445 O GLU A 57 2.720 15.971 21.401 1.00 57.47 O ANISOU 445 O GLU A 57 6949 6844 8044 4833 -1192 -2786 O ATOM 446 CB GLU A 57 0.109 15.176 22.605 1.00 62.72 C ANISOU 446 CB GLU A 57 6496 9164 8172 5420 -1073 -3313 C ATOM 447 CG GLU A 57 -0.831 15.783 23.638 1.00 68.97 C ANISOU 447 CG GLU A 57 7127 10444 8633 5974 -1150 -3678 C ATOM 448 CD GLU A 57 -0.088 16.661 24.623 1.00 72.59 C ANISOU 448 CD GLU A 57 8068 10394 9119 6066 -1255 -3759 C ATOM 449 OE1 GLU A 57 0.837 16.138 25.295 1.00 71.16 O ANISOU 449 OE1 GLU A 57 7885 10023 9132 5513 -1132 -3598 O ATOM 450 OE2 GLU A 57 -0.414 17.862 24.708 1.00 74.03 O ANISOU 450 OE2 GLU A 57 8657 10359 9114 6694 -1471 -3984 O ATOM 451 N ASP A 58 1.709 15.339 19.508 1.00 55.96 N ANISOU 451 N ASP A 58 6443 7028 7791 4995 -1169 -2692 N ATOM 452 CA ASP A 58 2.982 14.935 18.905 1.00 51.26 C ANISOU 452 CA ASP A 58 6064 5925 7489 4435 -1079 -2368 C ATOM 453 C ASP A 58 3.673 13.897 19.767 1.00 46.64 C ANISOU 453 C ASP A 58 5184 5468 7071 3881 -877 -2257 C ATOM 454 O ASP A 58 4.862 14.001 20.091 1.00 44.08 O ANISOU 454 O ASP A 58 5107 4718 6922 3545 -857 -2104 O ATOM 455 CB ASP A 58 3.879 16.153 18.723 1.00 53.50 C ANISOU 455 CB ASP A 58 7041 5453 7832 4496 -1248 -2287 C ATOM 456 CG ASP A 58 3.419 17.016 17.568 1.00 57.48 C ANISOU 456 CG ASP A 58 7936 5704 8202 4941 -1432 -2289 C ATOM 457 OD1 ASP A 58 2.402 16.675 16.912 1.00 60.56 O ANISOU 457 OD1 ASP A 58 8011 6548 8451 5238 -1437 -2366 O ATOM 458 OD2 ASP A 58 4.082 18.032 17.311 1.00 63.47 O ANISOU 458 OD2 ASP A 58 9331 5814 8972 4971 -1575 -2208 O ATOM 459 N THR A 59 2.895 12.911 20.180 1.00 44.92 N ANISOU 459 N THR A 59 4439 5871 6759 3790 -734 -2343 N ATOM 460 CA THR A 59 3.446 11.740 20.796 1.00 41.84 C ANISOU 460 CA THR A 59 3790 5609 6498 3266 -533 -2202 C ATOM 461 C THR A 59 2.795 10.501 20.183 1.00 40.60 C ANISOU 461 C THR A 59 3230 5891 6306 3029 -378 -2147 C ATOM 462 O THR A 59 1.762 10.576 19.510 1.00 41.86 O ANISOU 462 O THR A 59 3204 6400 6300 3287 -426 -2276 O ATOM 463 CB THR A 59 3.189 11.706 22.285 1.00 42.61 C ANISOU 463 CB THR A 59 3702 6023 6466 3292 -495 -2368 C ATOM 464 OG1 THR A 59 1.779 11.616 22.488 1.00 44.41 O ANISOU 464 OG1 THR A 59 3544 6911 6417 3588 -487 -2613 O ATOM 465 CG2 THR A 59 3.769 12.955 22.988 1.00 45.73 C ANISOU 465 CG2 THR A 59 4515 6003 6860 3526 -661 -2468 C ATOM 466 N ILE A 60 3.399 9.354 20.462 1.00 37.21 N ANISOU 466 N ILE A 60 2681 5452 6006 2541 -202 -1968 N ATOM 467 CA ILE A 60 2.876 8.081 20.014 1.00 36.58 C ANISOU 467 CA ILE A 60 2298 5717 5882 2230 -44 -1910 C ATOM 468 C ILE A 60 2.921 7.160 21.220 1.00 35.58 C ANISOU 468 C ILE A 60 1980 5835 5703 1893 112 -1887 C ATOM 469 O ILE A 60 3.995 6.896 21.788 1.00 34.92 O ANISOU 469 O ILE A 60 2073 5424 5770 1681 159 -1724 O ATOM 470 CB ILE A 60 3.759 7.498 18.881 1.00 34.83 C ANISOU 470 CB ILE A 60 2271 5088 5876 1958 13 -1659 C ATOM 471 CG1 ILE A 60 3.766 8.433 17.660 1.00 35.70 C ANISOU 471 CG1 ILE A 60 2609 4938 6017 2265 -138 -1654 C ATOM 472 CG2 ILE A 60 3.300 6.105 18.492 1.00 33.95 C ANISOU 472 CG2 ILE A 60 1928 5260 5711 1595 177 -1604 C ATOM 473 CD1 ILE A 60 4.819 8.058 16.615 1.00 34.24 C ANISOU 473 CD1 ILE A 60 2649 4324 6037 2022 -88 -1405 C ATOM 474 N PHE A 61 1.768 6.652 21.598 1.00 37.26 N ANISOU 474 N PHE A 61 1829 6652 5675 1830 191 -2041 N ATOM 475 CA PHE A 61 1.717 5.657 22.646 1.00 37.11 C ANISOU 475 CA PHE A 61 1655 6882 5564 1443 358 -1993 C ATOM 476 C PHE A 61 2.247 4.326 22.128 1.00 35.12 C ANISOU 476 C PHE A 61 1514 6398 5433 963 504 -1749 C ATOM 477 O PHE A 61 1.772 3.827 21.129 1.00 35.36 O ANISOU 477 O PHE A 61 1470 6531 5434 833 537 -1743 O ATOM 478 CB PHE A 61 0.283 5.491 23.179 1.00 40.53 C ANISOU 478 CB PHE A 61 1646 8098 5656 1453 416 -2233 C ATOM 479 CG PHE A 61 0.217 4.624 24.397 1.00 41.55 C ANISOU 479 CG PHE A 61 1654 8488 5645 1061 580 -2185 C ATOM 480 CD1 PHE A 61 -0.671 3.559 24.455 1.00 43.59 C ANISOU 480 CD1 PHE A 61 1631 9260 5672 629 742 -2203 C ATOM 481 CD2 PHE A 61 1.109 4.841 25.462 1.00 40.55 C ANISOU 481 CD2 PHE A 61 1733 8068 5607 1079 573 -2101 C ATOM 482 CE1 PHE A 61 -0.716 2.750 25.588 1.00 45.29 C ANISOU 482 CE1 PHE A 61 1798 9682 5728 231 898 -2131 C ATOM 483 CE2 PHE A 61 1.085 4.043 26.586 1.00 41.77 C ANISOU 483 CE2 PHE A 61 1815 8442 5611 735 717 -2035 C ATOM 484 CZ PHE A 61 0.161 2.992 26.649 1.00 45.93 C ANISOU 484 CZ PHE A 61 2093 9463 5895 309 884 -2040 C ATOM 485 N LEU A 62 3.243 3.766 22.805 1.00 33.49 N ANISOU 485 N LEU A 62 1508 5877 5341 733 578 -1558 N ATOM 486 CA LEU A 62 3.860 2.498 22.375 1.00 31.99 C ANISOU 486 CA LEU A 62 1503 5404 5250 355 703 -1324 C ATOM 487 C LEU A 62 3.544 1.364 23.348 1.00 33.34 C ANISOU 487 C LEU A 62 1630 5804 5232 -37 861 -1264 C ATOM 488 O LEU A 62 3.843 1.482 24.519 1.00 33.66 O ANISOU 488 O LEU A 62 1682 5886 5220 -23 869 -1248 O ATOM 489 CB LEU A 62 5.391 2.675 22.210 1.00 29.47 C ANISOU 489 CB LEU A 62 1491 4512 5192 437 654 -1124 C ATOM 490 CG LEU A 62 6.291 1.457 21.978 1.00 28.19 C ANISOU 490 CG LEU A 62 1561 4024 5124 172 763 -884 C ATOM 491 CD1 LEU A 62 6.000 0.725 20.663 1.00 28.01 C ANISOU 491 CD1 LEU A 62 1601 3924 5119 20 823 -843 C ATOM 492 CD2 LEU A 62 7.815 1.821 22.131 1.00 26.43 C ANISOU 492 CD2 LEU A 62 1535 3406 5103 312 700 -729 C ATOM 493 N ARG A 63 2.915 0.290 22.878 1.00 34.51 N ANISOU 493 N ARG A 63 1755 6105 5253 -408 980 -1235 N ATOM 494 CA ARG A 63 2.809 -0.927 23.672 1.00 35.96 C ANISOU 494 CA ARG A 63 2049 6351 5264 -853 1135 -1114 C ATOM 495 C ARG A 63 3.735 -1.948 23.037 1.00 34.55 C ANISOU 495 C ARG A 63 2279 5618 5231 -1031 1188 -878 C ATOM 496 O ARG A 63 3.473 -2.410 21.930 1.00 34.64 O ANISOU 496 O ARG A 63 2350 5551 5259 -1168 1211 -882 O ATOM 497 CB ARG A 63 1.354 -1.447 23.702 1.00 39.65 C ANISOU 497 CB ARG A 63 2225 7429 5413 -1222 1239 -1267 C ATOM 498 CG ARG A 63 0.331 -0.348 24.004 1.00 44.22 C ANISOU 498 CG ARG A 63 2331 8643 5828 -931 1166 -1553 C ATOM 499 CD ARG A 63 -1.072 -0.860 24.355 1.00 50.41 C ANISOU 499 CD ARG A 63 2740 10185 6229 -1321 1288 -1714 C ATOM 500 NE ARG A 63 -1.765 -1.341 23.160 1.00 56.97 N ANISOU 500 NE ARG A 63 3459 11199 6986 -1563 1306 -1781 N ATOM 501 CZ ARG A 63 -2.524 -0.590 22.353 1.00 59.38 C ANISOU 501 CZ ARG A 63 3418 11907 7237 -1256 1198 -2004 C ATOM 502 NH1 ARG A 63 -2.710 0.707 22.586 1.00 60.87 N ANISOU 502 NH1 ARG A 63 3377 12318 7434 -660 1058 -2185 N ATOM 503 NH2 ARG A 63 -3.098 -1.135 21.296 1.00 59.33 N ANISOU 503 NH2 ARG A 63 3327 12069 7148 -1527 1217 -2052 N ATOM 504 N GLU A 64 4.831 -2.282 23.723 1.00 33.54 N ANISOU 504 N GLU A 64 2428 5128 5188 -988 1199 -686 N ATOM 505 CA GLU A 64 5.882 -3.123 23.146 1.00 32.79 C ANISOU 505 CA GLU A 64 2722 4507 5231 -1011 1224 -474 C ATOM 506 C GLU A 64 6.002 -4.485 23.794 1.00 34.69 C ANISOU 506 C GLU A 64 3309 4579 5292 -1346 1345 -297 C ATOM 507 O GLU A 64 6.047 -4.602 25.025 1.00 35.53 O ANISOU 507 O GLU A 64 3438 4799 5261 -1410 1373 -240 O ATOM 508 CB GLU A 64 7.244 -2.414 23.210 1.00 30.57 C ANISOU 508 CB GLU A 64 2507 3920 5189 -621 1116 -383 C ATOM 509 CG GLU A 64 8.349 -3.208 22.559 1.00 31.01 C ANISOU 509 CG GLU A 64 2894 3527 5362 -567 1138 -192 C ATOM 510 CD GLU A 64 9.725 -2.581 22.790 1.00 33.17 C ANISOU 510 CD GLU A 64 3175 3615 5812 -238 1043 -102 C ATOM 511 OE1 GLU A 64 10.289 -2.048 21.816 1.00 35.29 O ANISOU 511 OE1 GLU A 64 3407 3748 6255 -58 986 -106 O ATOM 512 OE2 GLU A 64 10.224 -2.620 23.937 1.00 33.02 O ANISOU 512 OE2 GLU A 64 3188 3626 5732 -188 1026 -29 O ATOM 513 N TYR A 65 6.110 -5.510 22.952 1.00 35.23 N ANISOU 513 N TYR A 65 3701 4338 5348 -1537 1408 -205 N ATOM 514 CA TYR A 65 6.175 -6.904 23.411 1.00 37.64 C ANISOU 514 CA TYR A 65 4465 4386 5451 -1872 1517 -33 C ATOM 515 C TYR A 65 7.422 -7.567 22.853 1.00 37.32 C ANISOU 515 C TYR A 65 4859 3778 5541 -1630 1495 144 C ATOM 516 O TYR A 65 7.435 -8.040 21.707 1.00 36.74 O ANISOU 516 O TYR A 65 4969 3477 5515 -1675 1512 127 O ATOM 517 CB TYR A 65 4.967 -7.668 22.922 1.00 40.52 C ANISOU 517 CB TYR A 65 4885 4917 5594 -2402 1620 -119 C ATOM 518 CG TYR A 65 3.644 -7.273 23.537 1.00 42.22 C ANISOU 518 CG TYR A 65 4673 5784 5585 -2714 1671 -291 C ATOM 519 CD1 TYR A 65 2.936 -6.167 23.073 1.00 41.23 C ANISOU 519 CD1 TYR A 65 4010 6134 5521 -2536 1601 -528 C ATOM 520 CD2 TYR A 65 3.090 -8.029 24.548 1.00 47.22 C ANISOU 520 CD2 TYR A 65 5454 6579 5910 -3176 1789 -219 C ATOM 521 CE1 TYR A 65 1.710 -5.812 23.622 1.00 44.60 C ANISOU 521 CE1 TYR A 65 4006 7236 5705 -2759 1645 -711 C ATOM 522 CE2 TYR A 65 1.846 -7.693 25.114 1.00 51.43 C ANISOU 522 CE2 TYR A 65 5541 7810 6191 -3483 1853 -393 C ATOM 523 CZ TYR A 65 1.167 -6.579 24.635 1.00 49.86 C ANISOU 523 CZ TYR A 65 4760 8126 6058 -3243 1778 -651 C ATOM 524 OH TYR A 65 -0.053 -6.230 25.183 1.00 54.48 O ANISOU 524 OH TYR A 65 4862 9472 6365 -3471 1835 -846 O ATOM 525 N GLN A 66 8.466 -7.577 23.672 1.00 37.06 N ANISOU 525 N GLN A 66 4967 3569 5545 -1347 1452 296 N ATOM 526 CA GLN A 66 9.787 -8.035 23.285 1.00 36.48 C ANISOU 526 CA GLN A 66 5209 3072 5581 -995 1411 448 C ATOM 527 C GLN A 66 10.094 -9.408 23.890 1.00 39.91 C ANISOU 527 C GLN A 66 6233 3147 5784 -1098 1470 649 C ATOM 528 O GLN A 66 9.791 -9.647 25.067 1.00 40.71 O ANISOU 528 O GLN A 66 6422 3355 5691 -1282 1502 726 O ATOM 529 CB GLN A 66 10.787 -7.014 23.795 1.00 35.46 C ANISOU 529 CB GLN A 66 4785 3066 5622 -581 1300 463 C ATOM 530 CG GLN A 66 12.176 -7.254 23.313 1.00 37.62 C ANISOU 530 CG GLN A 66 5222 3062 6010 -184 1248 580 C ATOM 531 CD GLN A 66 12.955 -6.004 23.246 1.00 37.75 C ANISOU 531 CD GLN A 66 4840 3270 6234 110 1143 523 C ATOM 532 OE1 GLN A 66 14.080 -5.948 23.715 1.00 41.51 O ANISOU 532 OE1 GLN A 66 5311 3735 6726 394 1081 621 O ATOM 533 NE2 GLN A 66 12.367 -4.971 22.685 1.00 40.22 N ANISOU 533 NE2 GLN A 66 4826 3775 6682 38 1114 361 N ATOM 534 N THR A 67 10.647 -10.308 23.071 1.00 40.85 N ANISOU 534 N THR A 67 6788 2836 5895 -976 1485 729 N ATOM 535 CA THR A 67 11.119 -11.620 23.529 1.00 44.39 C ANISOU 535 CA THR A 67 7906 2842 6119 -947 1514 928 C ATOM 536 C THR A 67 12.644 -11.646 23.526 1.00 44.72 C ANISOU 536 C THR A 67 8035 2703 6255 -313 1421 1043 C ATOM 537 O THR A 67 13.270 -11.442 22.489 1.00 43.44 O ANISOU 537 O THR A 67 7767 2476 6261 -11 1390 984 O ATOM 538 CB THR A 67 10.568 -12.762 22.649 1.00 46.83 C ANISOU 538 CB THR A 67 8750 2762 6279 -1274 1596 918 C ATOM 539 OG1 THR A 67 9.133 -12.726 22.676 1.00 46.95 O ANISOU 539 OG1 THR A 67 8616 3052 6173 -1910 1681 797 O ATOM 540 CG2 THR A 67 11.079 -14.141 23.135 1.00 50.58 C ANISOU 540 CG2 THR A 67 10042 2687 6488 -1207 1610 1132 C ATOM 541 N ARG A 68 13.230 -11.841 24.704 1.00 47.28 N ANISOU 541 N ARG A 68 8497 3019 6447 -113 1376 1198 N ATOM 542 CA ARG A 68 14.678 -12.048 24.852 1.00 48.64 C ANISOU 542 CA ARG A 68 8788 3069 6625 498 1281 1320 C ATOM 543 C ARG A 68 14.823 -13.147 25.889 1.00 53.15 C ANISOU 543 C ARG A 68 9980 3339 6877 530 1280 1533 C ATOM 544 O ARG A 68 13.917 -13.342 26.691 1.00 54.37 O ANISOU 544 O ARG A 68 10270 3529 6860 78 1342 1578 O ATOM 545 CB ARG A 68 15.425 -10.779 25.315 1.00 46.00 C ANISOU 545 CB ARG A 68 7814 3187 6475 791 1180 1270 C ATOM 546 CG ARG A 68 14.945 -9.431 24.733 1.00 42.66 C ANISOU 546 CG ARG A 68 6772 3115 6320 611 1175 1066 C ATOM 547 CD ARG A 68 15.865 -8.264 25.155 1.00 40.50 C ANISOU 547 CD ARG A 68 5993 3197 6197 901 1062 1029 C ATOM 548 NE ARG A 68 15.730 -7.958 26.584 1.00 43.10 N ANISOU 548 NE ARG A 68 6224 3744 6407 827 1020 1067 N ATOM 549 CZ ARG A 68 14.745 -7.227 27.106 1.00 43.45 C ANISOU 549 CZ ARG A 68 6014 4030 6465 505 1038 949 C ATOM 550 NH1 ARG A 68 13.799 -6.730 26.321 1.00 41.45 N ANISOU 550 NH1 ARG A 68 5574 3842 6335 249 1089 791 N ATOM 551 NH2 ARG A 68 14.687 -7.005 28.414 1.00 44.35 N ANISOU 551 NH2 ARG A 68 6060 4350 6443 469 1002 980 N ATOM 552 N GLN A 69 15.957 -13.857 25.864 1.00 56.73 N ANISOU 552 N GLN A 69 10811 3522 7222 1079 1210 1664 N ATOM 553 CA GLN A 69 16.206 -15.090 26.671 1.00 62.13 C ANISOU 553 CA GLN A 69 12260 3788 7558 1221 1191 1890 C ATOM 554 C GLN A 69 14.948 -15.899 26.961 1.00 64.63 C ANISOU 554 C GLN A 69 13140 3779 7640 554 1307 1955 C ATOM 555 O GLN A 69 14.699 -16.291 28.105 1.00 67.25 O ANISOU 555 O GLN A 69 13782 4054 7717 378 1313 2119 O ATOM 556 CB GLN A 69 16.939 -14.785 27.989 1.00 63.26 C ANISOU 556 CB GLN A 69 12233 4211 7594 1555 1084 2021 C ATOM 557 CG GLN A 69 18.178 -13.881 27.854 1.00 63.76 C ANISOU 557 CG GLN A 69 11658 4711 7857 2120 965 1947 C ATOM 558 CD GLN A 69 17.942 -12.469 28.371 1.00 61.44 C ANISOU 558 CD GLN A 69 10598 4978 7769 1882 941 1818 C ATOM 559 OE1 GLN A 69 17.751 -12.259 29.578 1.00 63.56 O ANISOU 559 OE1 GLN A 69 10807 5436 7906 1760 912 1887 O ATOM 560 NE2 GLN A 69 17.981 -11.493 27.469 1.00 59.41 N ANISOU 560 NE2 GLN A 69 9791 4972 7811 1835 948 1632 N ATOM 561 N ASN A 70 14.158 -16.132 25.916 1.00 64.26 N ANISOU 561 N ASN A 70 13205 3555 7655 155 1399 1825 N ATOM 562 CA ASN A 70 12.879 -16.830 26.018 1.00 67.18 C ANISOU 562 CA ASN A 70 14023 3699 7802 -591 1520 1843 C ATOM 563 C ASN A 70 11.982 -16.390 27.190 1.00 67.46 C ANISOU 563 C ASN A 70 13772 4139 7720 -1113 1581 1874 C ATOM 564 O ASN A 70 11.435 -17.225 27.921 1.00 71.57 O ANISOU 564 O ASN A 70 14863 4421 7910 -1534 1647 2031 O ATOM 565 CB ASN A 70 13.116 -18.341 26.004 1.00 72.67 C ANISOU 565 CB ASN A 70 15787 3656 8168 -533 1521 2024 C ATOM 566 CG ASN A 70 14.002 -18.767 24.839 1.00 72.86 C ANISOU 566 CG ASN A 70 16081 3320 8281 44 1462 1962 C ATOM 567 OD1 ASN A 70 15.058 -19.379 25.045 1.00 76.22 O ANISOU 567 OD1 ASN A 70 16969 3425 8566 693 1368 2100 O ATOM 568 ND2 ASN A 70 13.587 -18.417 23.610 1.00 66.01 N ANISOU 568 ND2 ASN A 70 14897 2554 7628 -148 1511 1746 N ATOM 569 N GLN A 71 11.864 -15.069 27.349 1.00 63.20 N ANISOU 569 N GLN A 71 12378 4204 7432 -1069 1557 1721 N ATOM 570 CA GLN A 71 10.914 -14.420 28.262 1.00 62.78 C ANISOU 570 CA GLN A 71 11893 4653 7309 -1527 1618 1667 C ATOM 571 C GLN A 71 10.177 -13.327 27.494 1.00 58.42 C ANISOU 571 C GLN A 71 10611 4565 7021 -1721 1644 1394 C ATOM 572 O GLN A 71 10.702 -12.814 26.515 1.00 55.60 O ANISOU 572 O GLN A 71 9986 4201 6939 -1373 1582 1281 O ATOM 573 CB GLN A 71 11.641 -13.729 29.415 1.00 61.59 C ANISOU 573 CB GLN A 71 11415 4808 7177 -1134 1523 1739 C ATOM 574 CG GLN A 71 12.481 -14.593 30.314 1.00 66.27 C ANISOU 574 CG GLN A 71 12608 5062 7508 -816 1461 2006 C ATOM 575 CD GLN A 71 12.477 -14.049 31.724 1.00 67.27 C ANISOU 575 CD GLN A 71 12453 5595 7510 -823 1431 2067 C ATOM 576 OE1 GLN A 71 11.558 -14.329 32.493 1.00 72.14 O ANISOU 576 OE1 GLN A 71 13220 6323 7866 -1345 1534 2127 O ATOM 577 NE2 GLN A 71 13.496 -13.270 32.073 1.00 62.48 N ANISOU 577 NE2 GLN A 71 11431 5247 7063 -277 1295 2042 N ATOM 578 N CYS A 72 8.981 -12.953 27.949 1.00 58.70 N ANISOU 578 N CYS A 72 10323 5034 6945 -2246 1732 1289 N ATOM 579 CA CYS A 72 8.280 -11.791 27.395 1.00 55.21 C ANISOU 579 CA CYS A 72 9154 5104 6718 -2329 1731 1024 C ATOM 580 C CYS A 72 8.460 -10.532 28.271 1.00 52.14 C ANISOU 580 C CYS A 72 8173 5197 6442 -2055 1658 942 C ATOM 581 O CYS A 72 8.046 -10.500 29.440 1.00 54.34 O ANISOU 581 O CYS A 72 8400 5744 6502 -2261 1701 985 O ATOM 582 CB CYS A 72 6.791 -12.092 27.145 1.00 57.36 C ANISOU 582 CB CYS A 72 9360 5643 6789 -3029 1862 900 C ATOM 583 SG CYS A 72 5.860 -10.697 26.394 1.00 54.60 S ANISOU 583 SG CYS A 72 8135 5956 6654 -3048 1840 561 S ATOM 584 N PHE A 73 9.085 -9.509 27.692 1.00 48.11 N ANISOU 584 N PHE A 73 7254 4779 6247 -1614 1550 821 N ATOM 585 CA PHE A 73 9.243 -8.204 28.335 1.00 45.03 C ANISOU 585 CA PHE A 73 6329 4797 5982 -1366 1465 702 C ATOM 586 C PHE A 73 8.241 -7.247 27.691 1.00 43.05 C ANISOU 586 C PHE A 73 5579 4933 5846 -1497 1472 441 C ATOM 587 O PHE A 73 8.266 -7.014 26.482 1.00 41.30 O ANISOU 587 O PHE A 73 5272 4605 5815 -1404 1446 354 O ATOM 588 CB PHE A 73 10.704 -7.714 28.233 1.00 42.76 C ANISOU 588 CB PHE A 73 5984 4344 5920 -814 1329 761 C ATOM 589 CG PHE A 73 11.710 -8.679 28.843 1.00 45.05 C ANISOU 589 CG PHE A 73 6743 4310 6062 -599 1303 1007 C ATOM 590 CD1 PHE A 73 12.041 -8.602 30.200 1.00 46.26 C ANISOU 590 CD1 PHE A 73 6902 4622 6052 -510 1261 1103 C ATOM 591 CD2 PHE A 73 12.295 -9.682 28.073 1.00 43.70 C ANISOU 591 CD2 PHE A 73 7033 3689 5881 -453 1314 1135 C ATOM 592 CE1 PHE A 73 12.954 -9.519 30.773 1.00 48.76 C ANISOU 592 CE1 PHE A 73 7676 4655 6193 -261 1220 1338 C ATOM 593 CE2 PHE A 73 13.215 -10.585 28.636 1.00 45.51 C ANISOU 593 CE2 PHE A 73 7731 3622 5938 -169 1274 1356 C ATOM 594 CZ PHE A 73 13.544 -10.507 29.977 1.00 46.46 C ANISOU 594 CZ PHE A 73 7852 3908 5892 -66 1223 1465 C ATOM 595 N TYR A 74 7.308 -6.761 28.493 1.00 43.92 N ANISOU 595 N TYR A 74 5380 5512 5797 -1707 1512 318 N ATOM 596 CA TYR A 74 6.277 -5.860 28.012 1.00 43.28 C ANISOU 596 CA TYR A 74 4818 5866 5759 -1772 1509 57 C ATOM 597 C TYR A 74 6.551 -4.509 28.607 1.00 42.03 C ANISOU 597 C TYR A 74 4284 5966 5718 -1398 1393 -80 C ATOM 598 O TYR A 74 6.848 -4.423 29.805 1.00 44.02 O ANISOU 598 O TYR A 74 4552 6324 5851 -1347 1382 -22 O ATOM 599 CB TYR A 74 4.876 -6.329 28.446 1.00 46.23 C ANISOU 599 CB TYR A 74 5084 6679 5802 -2299 1649 -22 C ATOM 600 CG TYR A 74 3.807 -5.264 28.239 1.00 45.56 C ANISOU 600 CG TYR A 74 4419 7192 5701 -2258 1628 -318 C ATOM 601 CD1 TYR A 74 3.440 -4.390 29.267 1.00 47.80 C ANISOU 601 CD1 TYR A 74 4345 7945 5873 -2110 1604 -460 C ATOM 602 CD2 TYR A 74 3.199 -5.097 27.007 1.00 44.99 C ANISOU 602 CD2 TYR A 74 4166 7220 5708 -2302 1616 -466 C ATOM 603 CE1 TYR A 74 2.459 -3.386 29.067 1.00 46.06 C ANISOU 603 CE1 TYR A 74 3613 8280 5608 -1974 1569 -752 C ATOM 604 CE2 TYR A 74 2.229 -4.106 26.798 1.00 45.30 C ANISOU 604 CE2 TYR A 74 3684 7824 5704 -2178 1576 -741 C ATOM 605 CZ TYR A 74 1.871 -3.255 27.821 1.00 45.55 C ANISOU 605 CZ TYR A 74 3384 8306 5618 -1990 1550 -885 C ATOM 606 OH TYR A 74 0.915 -2.293 27.583 1.00 46.33 O ANISOU 606 OH TYR A 74 3000 8957 5645 -1788 1497 -1169 O ATOM 607 N ASN A 75 6.409 -3.463 27.793 1.00 39.77 N ANISOU 607 N ASN A 75 3699 5776 5635 -1151 1303 -265 N ATOM 608 CA ASN A 75 6.563 -2.082 28.235 1.00 39.30 C ANISOU 608 CA ASN A 75 3339 5919 5673 -807 1179 -430 C ATOM 609 C ASN A 75 5.620 -1.169 27.477 1.00 38.24 C ANISOU 609 C ASN A 75 2877 6075 5579 -698 1133 -680 C ATOM 610 O ASN A 75 5.490 -1.282 26.265 1.00 37.04 O ANISOU 610 O ASN A 75 2749 5782 5544 -708 1128 -690 O ATOM 611 CB ASN A 75 7.999 -1.579 27.957 1.00 37.39 C ANISOU 611 CB ASN A 75 3218 5287 5701 -465 1051 -337 C ATOM 612 CG ASN A 75 9.034 -2.206 28.873 1.00 41.14 C ANISOU 612 CG ASN A 75 3937 5574 6120 -436 1050 -127 C ATOM 613 OD1 ASN A 75 9.722 -3.163 28.489 1.00 44.79 O ANISOU 613 OD1 ASN A 75 4699 5708 6611 -455 1085 69 O ATOM 614 ND2 ASN A 75 9.147 -1.685 30.090 1.00 42.08 N ANISOU 614 ND2 ASN A 75 3944 5913 6132 -355 1001 -177 N ATOM 615 N SER A 76 4.992 -0.231 28.165 1.00 39.23 N ANISOU 615 N SER A 76 2710 6604 5592 -542 1086 -888 N ATOM 616 CA SER A 76 4.353 0.868 27.434 1.00 39.11 C ANISOU 616 CA SER A 76 2441 6781 5640 -264 986 -1126 C ATOM 617 C SER A 76 5.023 2.209 27.763 1.00 38.17 C ANISOU 617 C SER A 76 2327 6509 5667 154 818 -1224 C ATOM 618 O SER A 76 5.637 2.385 28.816 1.00 37.77 O ANISOU 618 O SER A 76 2346 6415 5590 203 790 -1186 O ATOM 619 CB SER A 76 2.842 0.892 27.631 1.00 42.38 C ANISOU 619 CB SER A 76 2498 7842 5762 -384 1058 -1343 C ATOM 620 OG SER A 76 2.461 1.673 28.741 1.00 45.31 O ANISOU 620 OG SER A 76 2657 8594 5964 -177 1021 -1525 O ATOM 621 N SER A 77 4.927 3.143 26.833 1.00 37.17 N ANISOU 621 N SER A 77 2167 6278 5678 436 700 -1345 N ATOM 622 CA SER A 77 5.643 4.390 26.944 1.00 36.29 C ANISOU 622 CA SER A 77 2169 5909 5712 769 534 -1416 C ATOM 623 C SER A 77 5.168 5.256 25.811 1.00 36.77 C ANISOU 623 C SER A 77 2209 5921 5842 1038 427 -1552 C ATOM 624 O SER A 77 4.426 4.799 24.934 1.00 36.32 O ANISOU 624 O SER A 77 2033 6027 5740 960 483 -1569 O ATOM 625 CB SER A 77 7.163 4.161 26.793 1.00 34.58 C ANISOU 625 CB SER A 77 2213 5204 5722 692 508 -1180 C ATOM 626 OG SER A 77 7.446 3.523 25.557 1.00 30.94 O ANISOU 626 OG SER A 77 1852 4502 5403 576 558 -1029 O ATOM 627 N TYR A 78 5.603 6.513 25.842 1.00 37.56 N ANISOU 627 N TYR A 78 2459 5785 6025 1344 264 -1648 N ATOM 628 CA TYR A 78 5.321 7.455 24.786 1.00 37.78 C ANISOU 628 CA TYR A 78 2582 5659 6113 1636 134 -1747 C ATOM 629 C TYR A 78 6.620 7.787 24.055 1.00 36.19 C ANISOU 629 C TYR A 78 2687 4899 6163 1578 66 -1560 C ATOM 630 O TYR A 78 7.671 7.989 24.661 1.00 35.41 O ANISOU 630 O TYR A 78 2733 4566 6153 1485 33 -1476 O ATOM 631 CB TYR A 78 4.667 8.713 25.357 1.00 40.80 C ANISOU 631 CB TYR A 78 2965 6202 6334 2056 -11 -2029 C ATOM 632 CG TYR A 78 3.245 8.509 25.828 1.00 41.90 C ANISOU 632 CG TYR A 78 2735 7000 6184 2185 49 -2251 C ATOM 633 CD1 TYR A 78 2.971 8.056 27.121 1.00 43.13 C ANISOU 633 CD1 TYR A 78 2687 7542 6158 2045 151 -2313 C ATOM 634 CD2 TYR A 78 2.165 8.789 24.988 1.00 42.83 C ANISOU 634 CD2 TYR A 78 2684 7415 6173 2452 3 -2407 C ATOM 635 CE1 TYR A 78 1.649 7.872 27.554 1.00 43.00 C ANISOU 635 CE1 TYR A 78 2284 8218 5835 2125 223 -2525 C ATOM 636 CE2 TYR A 78 0.849 8.619 25.416 1.00 43.85 C ANISOU 636 CE2 TYR A 78 2403 8260 5997 2567 59 -2633 C ATOM 637 CZ TYR A 78 0.599 8.146 26.691 1.00 45.31 C ANISOU 637 CZ TYR A 78 2368 8846 6002 2379 179 -2689 C ATOM 638 OH TYR A 78 -0.715 7.973 27.103 1.00 49.79 O ANISOU 638 OH TYR A 78 2485 10204 6229 2454 251 -2918 O ATOM 639 N LEU A 79 6.535 7.761 22.731 1.00 35.35 N ANISOU 639 N LEU A 79 2643 4644 6146 1601 56 -1492 N ATOM 640 CA LEU A 79 7.534 8.349 21.863 1.00 33.02 C ANISOU 640 CA LEU A 79 2630 3884 6033 1604 -26 -1359 C ATOM 641 C LEU A 79 7.141 9.819 21.604 1.00 35.27 C ANISOU 641 C LEU A 79 3133 4015 6255 1971 -216 -1530 C ATOM 642 O LEU A 79 5.945 10.134 21.509 1.00 37.02 O ANISOU 642 O LEU A 79 3237 4520 6309 2269 -267 -1723 O ATOM 643 CB LEU A 79 7.552 7.531 20.572 1.00 30.95 C ANISOU 643 CB LEU A 79 2336 3569 5853 1456 66 -1209 C ATOM 644 CG LEU A 79 7.795 6.009 20.743 1.00 28.96 C ANISOU 644 CG LEU A 79 1950 3432 5622 1135 245 -1059 C ATOM 645 CD1 LEU A 79 7.993 5.331 19.405 1.00 26.36 C ANISOU 645 CD1 LEU A 79 1671 2966 5378 1017 315 -923 C ATOM 646 CD2 LEU A 79 9.020 5.731 21.619 1.00 25.98 C ANISOU 646 CD2 LEU A 79 1649 2894 5327 982 275 -921 C ATOM 647 N ASN A 80 8.110 10.729 21.532 1.00 35.14 N ANISOU 647 N ASN A 80 3443 3572 6335 1957 -328 -1472 N ATOM 648 CA ASN A 80 7.816 12.080 21.025 1.00 37.99 C ANISOU 648 CA ASN A 80 4142 3659 6632 2278 -513 -1587 C ATOM 649 C ASN A 80 8.090 12.170 19.548 1.00 36.91 C ANISOU 649 C ASN A 80 4180 3261 6584 2231 -525 -1423 C ATOM 650 O ASN A 80 9.026 11.552 19.072 1.00 33.88 O ANISOU 650 O ASN A 80 3768 2756 6348 1899 -422 -1209 O ATOM 651 CB ASN A 80 8.664 13.129 21.728 1.00 40.34 C ANISOU 651 CB ASN A 80 4790 3596 6943 2241 -644 -1627 C ATOM 652 CG ASN A 80 8.247 13.334 23.149 1.00 44.33 C ANISOU 652 CG ASN A 80 5198 4336 7310 2393 -677 -1844 C ATOM 653 OD1 ASN A 80 7.075 13.230 23.483 1.00 47.72 O ANISOU 653 OD1 ASN A 80 5411 5144 7574 2696 -670 -2033 O ATOM 654 ND2 ASN A 80 9.204 13.640 24.000 1.00 48.72 N ANISOU 654 ND2 ASN A 80 5889 4718 7904 2177 -714 -1829 N ATOM 655 N VAL A 81 7.290 12.967 18.842 1.00 38.76 N ANISOU 655 N VAL A 81 4603 3423 6700 2600 -657 -1529 N ATOM 656 CA VAL A 81 7.406 13.166 17.401 1.00 38.14 C ANISOU 656 CA VAL A 81 4726 3109 6657 2614 -689 -1385 C ATOM 657 C VAL A 81 8.023 14.560 17.165 1.00 41.06 C ANISOU 657 C VAL A 81 5673 2921 7007 2682 -865 -1353 C ATOM 658 O VAL A 81 7.562 15.554 17.717 1.00 43.39 O ANISOU 658 O VAL A 81 6240 3085 7161 3021 -1027 -1541 O ATOM 659 CB VAL A 81 5.986 13.135 16.754 1.00 40.56 C ANISOU 659 CB VAL A 81 4868 3753 6789 3024 -741 -1533 C ATOM 660 CG1 VAL A 81 6.053 13.298 15.242 1.00 40.57 C ANISOU 660 CG1 VAL A 81 5070 3545 6800 3057 -779 -1384 C ATOM 661 CG2 VAL A 81 5.233 11.877 17.160 1.00 38.88 C ANISOU 661 CG2 VAL A 81 4113 4126 6535 2919 -582 -1612 C ATOM 662 N GLN A 82 9.050 14.640 16.330 1.00 40.36 N ANISOU 662 N GLN A 82 5800 2506 7030 2355 -833 -1120 N ATOM 663 CA GLN A 82 9.556 15.942 15.909 1.00 42.98 C ANISOU 663 CA GLN A 82 6728 2298 7303 2356 -993 -1063 C ATOM 664 C GLN A 82 9.270 15.990 14.412 1.00 43.50 C ANISOU 664 C GLN A 82 6935 2269 7325 2464 -1008 -928 C ATOM 665 O GLN A 82 9.993 15.379 13.588 1.00 40.60 O ANISOU 665 O GLN A 82 6451 1910 7065 2117 -874 -712 O ATOM 666 CB GLN A 82 11.046 16.079 16.217 1.00 42.70 C ANISOU 666 CB GLN A 82 6822 2016 7384 1819 -943 -904 C ATOM 667 CG GLN A 82 11.427 15.947 17.698 1.00 42.41 C ANISOU 667 CG GLN A 82 6613 2117 7383 1681 -928 -1025 C ATOM 668 CD GLN A 82 11.474 14.502 18.211 1.00 38.91 C ANISOU 668 CD GLN A 82 5572 2162 7051 1550 -736 -996 C ATOM 669 OE1 GLN A 82 11.958 13.560 17.532 1.00 35.49 O ANISOU 669 OE1 GLN A 82 4888 1873 6725 1323 -585 -812 O ATOM 670 NE2 GLN A 82 10.992 14.322 19.438 1.00 36.72 N ANISOU 670 NE2 GLN A 82 5102 2126 6722 1699 -742 -1178 N ATOM 671 N ARG A 83 8.175 16.673 14.084 1.00 45.35 N ANISOU 671 N ARG A 83 7389 2467 7374 2990 -1170 -1071 N ATOM 672 CA ARG A 83 7.551 16.623 12.770 1.00 46.60 C ANISOU 672 CA ARG A 83 7588 2680 7439 3229 -1204 -1002 C ATOM 673 C ARG A 83 8.392 17.196 11.631 1.00 48.06 C ANISOU 673 C ARG A 83 8252 2389 7621 2983 -1234 -744 C ATOM 674 O ARG A 83 8.440 16.617 10.550 1.00 46.85 O ANISOU 674 O ARG A 83 7949 2362 7490 2874 -1143 -595 O ATOM 675 CB ARG A 83 6.203 17.339 12.783 1.00 50.38 C ANISOU 675 CB ARG A 83 8209 3259 7673 3923 -1404 -1235 C ATOM 676 CG ARG A 83 5.102 16.660 13.574 1.00 49.55 C ANISOU 676 CG ARG A 83 7525 3799 7502 4208 -1358 -1492 C ATOM 677 CD ARG A 83 3.814 17.482 13.419 1.00 52.94 C ANISOU 677 CD ARG A 83 8106 4369 7640 4957 -1575 -1722 C ATOM 678 NE ARG A 83 2.704 16.851 14.133 1.00 54.75 N ANISOU 678 NE ARG A 83 7723 5324 7757 5214 -1523 -1982 N ATOM 679 CZ ARG A 83 1.626 16.257 13.535 1.00 57.68 C ANISOU 679 CZ ARG A 83 7635 6298 7981 5449 -1506 -2080 C ATOM 680 NH1 ARG A 83 1.473 16.339 12.189 1.00 58.78 N ANISOU 680 NH1 ARG A 83 7920 6353 8060 5563 -1571 -1952 N ATOM 681 NH2 ARG A 83 0.691 15.702 14.292 1.00 58.40 N ANISOU 681 NH2 ARG A 83 7163 7079 7949 5587 -1443 -2316 N ATOM 682 N GLU A 84 9.020 18.348 11.842 1.00 51.45 N ANISOU 682 N GLU A 84 9284 2275 7991 2882 -1364 -697 N ATOM 683 CA GLU A 84 9.823 18.965 10.768 1.00 53.02 C ANISOU 683 CA GLU A 84 9988 2017 8142 2584 -1389 -439 C ATOM 684 C GLU A 84 10.964 18.019 10.395 1.00 48.83 C ANISOU 684 C GLU A 84 9075 1680 7797 1968 -1153 -222 C ATOM 685 O GLU A 84 11.269 17.827 9.215 1.00 48.09 O ANISOU 685 O GLU A 84 9026 1565 7681 1808 -1084 -24 O ATOM 686 CB GLU A 84 10.396 20.317 11.179 1.00 57.31 C ANISOU 686 CB GLU A 84 11269 1932 8576 2454 -1555 -427 C ATOM 687 CG GLU A 84 9.355 21.386 11.502 1.00 62.85 C ANISOU 687 CG GLU A 84 12490 2340 9051 3121 -1816 -643 C ATOM 688 CD GLU A 84 8.717 21.193 12.875 1.00 64.40 C ANISOU 688 CD GLU A 84 12348 2853 9267 3447 -1843 -952 C ATOM 689 OE1 GLU A 84 7.652 21.795 13.135 1.00 71.35 O ANISOU 689 OE1 GLU A 84 13446 3713 9952 4116 -2026 -1178 O ATOM 690 OE2 GLU A 84 9.283 20.454 13.703 1.00 62.49 O ANISOU 690 OE2 GLU A 84 11630 2902 9210 3060 -1684 -973 O ATOM 691 N ASN A 85 11.578 17.440 11.423 1.00 45.68 N ANISOU 691 N ASN A 85 8308 1494 7555 1667 -1036 -271 N ATOM 692 CA ASN A 85 12.765 16.594 11.263 1.00 42.58 C ANISOU 692 CA ASN A 85 7562 1302 7314 1132 -829 -93 C ATOM 693 C ASN A 85 12.493 15.192 10.779 1.00 38.65 C ANISOU 693 C ASN A 85 6504 1266 6916 1180 -651 -63 C ATOM 694 O ASN A 85 13.440 14.462 10.405 1.00 36.80 O ANISOU 694 O ASN A 85 6018 1193 6772 821 -483 92 O ATOM 695 CB ASN A 85 13.546 16.530 12.577 1.00 41.45 C ANISOU 695 CB ASN A 85 7262 1221 7265 836 -796 -160 C ATOM 696 CG ASN A 85 14.115 17.893 12.967 1.00 45.58 C ANISOU 696 CG ASN A 85 8376 1260 7681 616 -954 -161 C ATOM 697 OD1 ASN A 85 14.222 18.219 14.149 1.00 45.90 O ANISOU 697 OD1 ASN A 85 8456 1257 7725 592 -1024 -315 O ATOM 698 ND2 ASN A 85 14.499 18.679 11.966 1.00 47.98 N ANISOU 698 ND2 ASN A 85 9169 1193 7868 420 -1007 12 N ATOM 699 N GLY A 86 11.222 14.794 10.794 1.00 37.71 N ANISOU 699 N GLY A 86 6187 1384 6757 1613 -687 -225 N ATOM 700 CA GLY A 86 10.892 13.386 10.498 1.00 34.78 C ANISOU 700 CA GLY A 86 5302 1449 6466 1609 -521 -231 C ATOM 701 C GLY A 86 11.470 12.368 11.463 1.00 32.07 C ANISOU 701 C GLY A 86 4557 1357 6270 1358 -367 -244 C ATOM 702 O GLY A 86 11.814 11.248 11.059 1.00 29.98 O ANISOU 702 O GLY A 86 4002 1307 6080 1193 -205 -158 O ATOM 703 N THR A 87 11.589 12.744 12.739 1.00 32.54 N ANISOU 703 N THR A 87 4632 1381 6349 1352 -425 -355 N ATOM 704 CA THR A 87 12.100 11.823 13.751 1.00 30.70 C ANISOU 704 CA THR A 87 4050 1390 6224 1155 -300 -367 C ATOM 705 C THR A 87 11.087 11.534 14.829 1.00 30.64 C ANISOU 705 C THR A 87 3835 1630 6176 1396 -325 -576 C ATOM 706 O THR A 87 10.080 12.238 14.995 1.00 31.90 O ANISOU 706 O THR A 87 4123 1779 6217 1730 -458 -744 O ATOM 707 CB THR A 87 13.349 12.346 14.474 1.00 32.12 C ANISOU 707 CB THR A 87 4346 1410 6450 844 -319 -303 C ATOM 708 OG1 THR A 87 13.004 13.503 15.246 1.00 33.59 O ANISOU 708 OG1 THR A 87 4838 1370 6553 984 -493 -453 O ATOM 709 CG2 THR A 87 14.469 12.699 13.504 1.00 34.21 C ANISOU 709 CG2 THR A 87 4783 1496 6718 523 -283 -95 C ATOM 710 N VAL A 88 11.382 10.485 15.578 1.00 28.28 N ANISOU 710 N VAL A 88 3222 1575 5948 1239 -195 -564 N ATOM 711 CA VAL A 88 10.646 10.131 16.768 1.00 29.47 C ANISOU 711 CA VAL A 88 3165 1986 6048 1362 -189 -730 C ATOM 712 C VAL A 88 11.714 9.883 17.829 1.00 29.00 C ANISOU 712 C VAL A 88 3032 1929 6058 1123 -144 -670 C ATOM 713 O VAL A 88 12.855 9.514 17.523 1.00 27.84 O ANISOU 713 O VAL A 88 2861 1720 5997 881 -70 -500 O ATOM 714 CB VAL A 88 9.733 8.892 16.527 1.00 29.73 C ANISOU 714 CB VAL A 88 2894 2358 6044 1394 -66 -765 C ATOM 715 CG1 VAL A 88 8.924 8.608 17.743 1.00 33.72 C ANISOU 715 CG1 VAL A 88 3192 3168 6454 1479 -54 -933 C ATOM 716 CG2 VAL A 88 8.749 9.130 15.388 1.00 29.30 C ANISOU 716 CG2 VAL A 88 2874 2358 5900 1612 -121 -825 C ATOM 717 N SER A 89 11.388 10.108 19.082 1.00 30.50 N ANISOU 717 N SER A 89 3170 2233 6185 1207 -194 -817 N ATOM 718 CA SER A 89 12.380 9.917 20.120 1.00 32.30 C ANISOU 718 CA SER A 89 3329 2493 6450 1001 -171 -769 C ATOM 719 C SER A 89 11.749 9.277 21.365 1.00 33.88 C ANISOU 719 C SER A 89 3304 3001 6568 1074 -122 -883 C ATOM 720 O SER A 89 10.520 9.232 21.507 1.00 33.66 O ANISOU 720 O SER A 89 3188 3165 6436 1278 -124 -1033 O ATOM 721 CB SER A 89 13.085 11.240 20.464 1.00 33.52 C ANISOU 721 CB SER A 89 3775 2371 6591 923 -322 -813 C ATOM 722 OG SER A 89 12.186 12.181 21.010 1.00 36.69 O ANISOU 722 OG SER A 89 4362 2703 6876 1195 -460 -1033 O ATOM 723 N ARG A 90 12.605 8.791 22.251 1.00 35.31 N ANISOU 723 N ARG A 90 3380 3269 6767 903 -78 -809 N ATOM 724 CA ARG A 90 12.211 8.175 23.512 1.00 38.28 C ANISOU 724 CA ARG A 90 3582 3919 7045 924 -29 -878 C ATOM 725 C ARG A 90 13.446 8.156 24.402 1.00 40.37 C ANISOU 725 C ARG A 90 3828 4190 7322 763 -54 -803 C ATOM 726 O ARG A 90 14.527 7.756 23.977 1.00 39.46 O ANISOU 726 O ARG A 90 3682 4022 7288 615 -14 -632 O ATOM 727 CB ARG A 90 11.706 6.779 23.240 1.00 37.26 C ANISOU 727 CB ARG A 90 3284 3974 6898 873 131 -785 C ATOM 728 CG ARG A 90 11.374 5.933 24.461 1.00 42.10 C ANISOU 728 CG ARG A 90 3757 4855 7385 820 211 -797 C ATOM 729 CD ARG A 90 11.884 4.531 24.161 1.00 43.61 C ANISOU 729 CD ARG A 90 3932 5029 7608 671 348 -588 C ATOM 730 NE ARG A 90 11.268 3.501 24.983 1.00 50.62 N ANISOU 730 NE ARG A 90 4757 6131 8346 582 454 -571 N ATOM 731 CZ ARG A 90 11.220 2.228 24.624 1.00 53.19 C ANISOU 731 CZ ARG A 90 5141 6425 8645 456 578 -432 C ATOM 732 NH1 ARG A 90 11.741 1.858 23.467 1.00 52.53 N ANISOU 732 NH1 ARG A 90 5146 6134 8680 453 610 -321 N ATOM 733 NH2 ARG A 90 10.644 1.325 25.412 1.00 59.33 N ANISOU 733 NH2 ARG A 90 5923 7368 9252 320 673 -406 N ATOM 734 N TYR A 91 13.300 8.688 25.603 1.00 44.54 N ANISOU 734 N TYR A 91 4365 4812 7745 814 -136 -951 N ATOM 735 CA TYR A 91 14.331 8.616 26.594 1.00 47.95 C ANISOU 735 CA TYR A 91 4743 5331 8146 676 -169 -906 C ATOM 736 C TYR A 91 14.182 7.228 27.217 1.00 48.30 C ANISOU 736 C TYR A 91 4598 5634 8120 671 -35 -798 C ATOM 737 O TYR A 91 13.066 6.820 27.578 1.00 48.74 O ANISOU 737 O TYR A 91 4590 5855 8073 759 32 -877 O ATOM 738 CB TYR A 91 14.126 9.720 27.633 1.00 50.20 C ANISOU 738 CB TYR A 91 5148 5610 8317 744 -312 -1130 C ATOM 739 CG TYR A 91 15.208 9.800 28.692 1.00 55.38 C ANISOU 739 CG TYR A 91 5752 6375 8915 582 -376 -1115 C ATOM 740 CD1 TYR A 91 16.224 10.759 28.610 1.00 60.49 C ANISOU 740 CD1 TYR A 91 6548 6845 9589 383 -504 -1137 C ATOM 741 CD2 TYR A 91 15.214 8.919 29.785 1.00 58.25 C ANISOU 741 CD2 TYR A 91 5929 7040 9165 600 -313 -1078 C ATOM 742 CE1 TYR A 91 17.218 10.844 29.594 1.00 63.89 C ANISOU 742 CE1 TYR A 91 6891 7444 9938 212 -576 -1144 C ATOM 743 CE2 TYR A 91 16.202 8.991 30.769 1.00 62.17 C ANISOU 743 CE2 TYR A 91 6362 7680 9580 481 -387 -1069 C ATOM 744 CZ TYR A 91 17.194 9.957 30.670 1.00 63.98 C ANISOU 744 CZ TYR A 91 6691 7777 9840 291 -522 -1113 C ATOM 745 OH TYR A 91 18.165 10.022 31.641 1.00 66.73 O ANISOU 745 OH TYR A 91 6937 8333 10083 153 -605 -1121 O ATOM 746 N GLU A 92 15.281 6.491 27.324 1.00 49.09 N ANISOU 746 N GLU A 92 4621 5786 8244 570 6 -617 N ATOM 747 CA GLU A 92 15.222 5.180 27.985 1.00 50.49 C ANISOU 747 CA GLU A 92 4716 6147 8321 587 113 -496 C ATOM 748 C GLU A 92 16.548 4.738 28.574 1.00 52.13 C ANISOU 748 C GLU A 92 4851 6469 8487 560 85 -358 C ATOM 749 O GLU A 92 17.603 4.808 27.917 1.00 52.03 O ANISOU 749 O GLU A 92 4795 6417 8560 520 63 -262 O ATOM 750 CB GLU A 92 14.640 4.067 27.087 1.00 49.36 C ANISOU 750 CB GLU A 92 4603 5941 8210 592 260 -378 C ATOM 751 CG GLU A 92 15.043 4.123 25.614 1.00 49.36 C ANISOU 751 CG GLU A 92 4644 5742 8367 581 281 -300 C ATOM 752 CD GLU A 92 15.385 2.750 25.014 1.00 49.20 C ANISOU 752 CD GLU A 92 4666 5674 8355 592 406 -113 C ATOM 753 OE1 GLU A 92 15.594 1.787 25.793 1.00 51.39 O ANISOU 753 OE1 GLU A 92 4976 6033 8517 617 454 -13 O ATOM 754 OE2 GLU A 92 15.466 2.652 23.761 1.00 45.88 O ANISOU 754 OE2 GLU A 92 4283 5115 8033 593 447 -67 O ATOM 755 N GLY A 93 16.463 4.281 29.825 1.00 53.93 N ANISOU 755 N GLY A 93 5050 6890 8552 593 86 -353 N ATOM 756 CA GLY A 93 17.605 3.812 30.577 1.00 55.87 C ANISOU 756 CA GLY A 93 5222 7307 8701 625 42 -233 C ATOM 757 C GLY A 93 18.738 4.799 30.486 1.00 57.06 C ANISOU 757 C GLY A 93 5266 7506 8907 535 -92 -288 C ATOM 758 O GLY A 93 19.832 4.454 30.038 1.00 58.08 O ANISOU 758 O GLY A 93 5291 7715 9062 546 -96 -158 O ATOM 759 N GLY A 94 18.462 6.039 30.883 1.00 58.06 N ANISOU 759 N GLY A 94 5433 7598 9029 437 -202 -492 N ATOM 760 CA GLY A 94 19.495 7.068 30.964 1.00 59.23 C ANISOU 760 CA GLY A 94 5533 7785 9185 262 -344 -569 C ATOM 761 C GLY A 94 19.558 8.051 29.807 1.00 59.09 C ANISOU 761 C GLY A 94 5637 7499 9315 109 -380 -624 C ATOM 762 O GLY A 94 19.779 9.244 30.030 1.00 60.84 O ANISOU 762 O GLY A 94 5976 7625 9514 -62 -511 -778 O ATOM 763 N ARG A 95 19.351 7.568 28.580 1.00 56.68 N ANISOU 763 N ARG A 95 5350 7049 9137 158 -269 -502 N ATOM 764 CA ARG A 95 19.656 8.354 27.375 1.00 56.04 C ANISOU 764 CA ARG A 95 5368 6752 9170 -4 -290 -495 C ATOM 765 C ARG A 95 18.433 8.656 26.487 1.00 53.15 C ANISOU 765 C ARG A 95 5211 6088 8897 105 -250 -553 C ATOM 766 O ARG A 95 17.488 7.863 26.433 1.00 52.13 O ANISOU 766 O ARG A 95 5061 5975 8770 291 -152 -538 O ATOM 767 CB ARG A 95 20.779 7.645 26.578 1.00 56.33 C ANISOU 767 CB ARG A 95 5207 6955 9242 -57 -212 -298 C ATOM 768 CG ARG A 95 20.533 7.542 25.069 1.00 57.34 C ANISOU 768 CG ARG A 95 5416 6876 9494 -52 -117 -210 C ATOM 769 CD ARG A 95 21.574 6.740 24.326 1.00 60.40 C ANISOU 769 CD ARG A 95 5596 7470 9883 -39 -25 -37 C ATOM 770 NE ARG A 95 22.865 7.417 24.280 1.00 67.33 N ANISOU 770 NE ARG A 95 6312 8573 10699 -310 -94 -24 N ATOM 771 CZ ARG A 95 23.854 7.064 23.467 1.00 71.27 C ANISOU 771 CZ ARG A 95 6603 9303 11173 -358 -24 97 C ATOM 772 NH1 ARG A 95 23.683 6.043 22.628 1.00 70.83 N ANISOU 772 NH1 ARG A 95 6527 9222 11162 -112 109 208 N ATOM 773 NH2 ARG A 95 25.011 7.731 23.484 1.00 74.76 N ANISOU 773 NH2 ARG A 95 6856 10029 11522 -666 -86 93 N ATOM 774 N GLU A 96 18.452 9.795 25.794 1.00 52.03 N ANISOU 774 N GLU A 96 5282 5686 8802 -25 -332 -619 N ATOM 775 CA GLU A 96 17.452 10.062 24.758 1.00 49.65 C ANISOU 775 CA GLU A 96 5168 5127 8571 107 -305 -645 C ATOM 776 C GLU A 96 17.831 9.341 23.459 1.00 46.40 C ANISOU 776 C GLU A 96 4661 4714 8253 71 -181 -451 C ATOM 777 O GLU A 96 18.979 9.420 23.019 1.00 48.49 O ANISOU 777 O GLU A 96 4852 5040 8533 -140 -172 -337 O ATOM 778 CB GLU A 96 17.286 11.558 24.489 1.00 51.77 C ANISOU 778 CB GLU A 96 5788 5065 8819 31 -453 -777 C ATOM 779 CG GLU A 96 15.829 11.899 24.176 1.00 54.12 C ANISOU 779 CG GLU A 96 6270 5192 9100 344 -478 -913 C ATOM 780 CD GLU A 96 15.654 12.997 23.139 1.00 58.24 C ANISOU 780 CD GLU A 96 7167 5331 9631 338 -573 -930 C ATOM 781 OE1 GLU A 96 16.676 13.597 22.703 1.00 60.41 O ANISOU 781 OE1 GLU A 96 7602 5432 9918 20 -618 -838 O ATOM 782 OE2 GLU A 96 14.479 13.247 22.757 1.00 57.78 O ANISOU 782 OE2 GLU A 96 7240 5174 9540 650 -602 -1033 O ATOM 783 N HIS A 97 16.891 8.614 22.870 1.00 41.27 N ANISOU 783 N HIS A 97 3994 4045 7643 261 -82 -426 N ATOM 784 CA HIS A 97 17.119 7.952 21.595 1.00 37.17 C ANISOU 784 CA HIS A 97 3428 3500 7196 252 30 -273 C ATOM 785 C HIS A 97 16.264 8.615 20.516 1.00 35.25 C ANISOU 785 C HIS A 97 3392 3016 6985 323 0 -321 C ATOM 786 O HIS A 97 15.090 8.880 20.732 1.00 34.21 O ANISOU 786 O HIS A 97 3340 2842 6815 502 -43 -461 O ATOM 787 CB HIS A 97 16.767 6.461 21.708 1.00 36.72 C ANISOU 787 CB HIS A 97 3223 3601 7129 388 166 -199 C ATOM 788 CG HIS A 97 17.574 5.735 22.739 1.00 38.50 C ANISOU 788 CG HIS A 97 3294 4043 7290 385 186 -131 C ATOM 789 ND1 HIS A 97 18.690 4.979 22.425 1.00 43.09 N ANISOU 789 ND1 HIS A 97 3750 4757 7867 388 251 21 N ATOM 790 CD2 HIS A 97 17.455 5.694 24.087 1.00 39.29 C ANISOU 790 CD2 HIS A 97 3349 4278 7301 413 139 -199 C ATOM 791 CE1 HIS A 97 19.203 4.481 23.539 1.00 43.53 C ANISOU 791 CE1 HIS A 97 3699 5010 7831 441 233 49 C ATOM 792 NE2 HIS A 97 18.478 4.915 24.562 1.00 41.70 N ANISOU 792 NE2 HIS A 97 3518 4775 7550 434 166 -77 N ATOM 793 N VAL A 98 16.852 8.872 19.355 1.00 32.62 N ANISOU 793 N VAL A 98 3131 2571 6694 199 22 -207 N ATOM 794 CA VAL A 98 16.146 9.489 18.247 1.00 29.58 C ANISOU 794 CA VAL A 98 2968 1957 6315 273 -13 -223 C ATOM 795 C VAL A 98 16.314 8.625 17.003 1.00 26.67 C ANISOU 795 C VAL A 98 2504 1644 5987 274 121 -81 C ATOM 796 O VAL A 98 17.367 7.991 16.808 1.00 25.83 O ANISOU 796 O VAL A 98 2229 1688 5896 152 214 46 O ATOM 797 CB VAL A 98 16.709 10.889 17.987 1.00 32.31 C ANISOU 797 CB VAL A 98 3604 2045 6626 76 -138 -219 C ATOM 798 CG1 VAL A 98 15.895 11.598 16.945 1.00 32.09 C ANISOU 798 CG1 VAL A 98 3878 1745 6570 215 -202 -236 C ATOM 799 CG2 VAL A 98 16.683 11.735 19.281 1.00 34.49 C ANISOU 799 CG2 VAL A 98 4012 2248 6844 52 -278 -377 C ATOM 800 N ALA A 99 15.260 8.550 16.188 1.00 25.44 N ANISOU 800 N ALA A 99 2435 1409 5824 443 127 -120 N ATOM 801 CA ALA A 99 15.334 7.816 14.926 1.00 24.60 C ANISOU 801 CA ALA A 99 2279 1333 5734 446 240 -9 C ATOM 802 C ALA A 99 14.516 8.533 13.904 1.00 25.28 C ANISOU 802 C ALA A 99 2578 1249 5780 557 168 -40 C ATOM 803 O ALA A 99 13.402 8.956 14.205 1.00 25.70 O ANISOU 803 O ALA A 99 2704 1276 5784 755 75 -185 O ATOM 804 CB ALA A 99 14.793 6.366 15.093 1.00 23.05 C ANISOU 804 CB ALA A 99 1901 1317 5542 549 359 -28 C ATOM 805 N HIS A 100 15.036 8.598 12.684 1.00 25.65 N ANISOU 805 N HIS A 100 2700 1229 5817 461 216 91 N ATOM 806 CA HIS A 100 14.229 8.986 11.513 1.00 26.21 C ANISOU 806 CA HIS A 100 2951 1183 5827 598 170 87 C ATOM 807 C HIS A 100 13.240 7.909 11.062 1.00 24.88 C ANISOU 807 C HIS A 100 2618 1193 5641 764 243 17 C ATOM 808 O HIS A 100 13.646 6.762 10.814 1.00 23.73 O ANISOU 808 O HIS A 100 2309 1180 5527 690 382 76 O ATOM 809 CB HIS A 100 15.145 9.307 10.364 1.00 27.22 C ANISOU 809 CB HIS A 100 3198 1221 5922 409 216 260 C ATOM 810 CG HIS A 100 15.919 10.557 10.580 1.00 29.40 C ANISOU 810 CG HIS A 100 3720 1288 6161 185 124 326 C ATOM 811 ND1 HIS A 100 17.080 10.587 11.322 1.00 29.92 N ANISOU 811 ND1 HIS A 100 3657 1454 6257 -82 160 374 N ATOM 812 CD2 HIS A 100 15.653 11.842 10.236 1.00 31.70 C ANISOU 812 CD2 HIS A 100 4415 1265 6365 183 -20 338 C ATOM 813 CE1 HIS A 100 17.524 11.839 11.377 1.00 32.38 C ANISOU 813 CE1 HIS A 100 4274 1529 6501 -309 53 412 C ATOM 814 NE2 HIS A 100 16.683 12.607 10.721 1.00 33.56 N ANISOU 814 NE2 HIS A 100 4786 1387 6580 -150 -56 398 N ATOM 815 N LEU A 101 11.973 8.295 10.933 1.00 25.51 N ANISOU 815 N LEU A 101 2760 1287 5646 990 141 -115 N ATOM 816 CA LEU A 101 10.989 7.501 10.258 1.00 25.04 C ANISOU 816 CA LEU A 101 2572 1417 5526 1101 184 -186 C ATOM 817 C LEU A 101 11.142 7.577 8.724 1.00 25.56 C ANISOU 817 C LEU A 101 2765 1407 5538 1099 200 -79 C ATOM 818 O LEU A 101 10.952 8.628 8.115 1.00 27.16 O ANISOU 818 O LEU A 101 3205 1451 5664 1219 80 -51 O ATOM 819 CB LEU A 101 9.608 7.948 10.702 1.00 26.13 C ANISOU 819 CB LEU A 101 2667 1700 5561 1358 61 -383 C ATOM 820 CG LEU A 101 8.414 7.263 10.051 1.00 26.37 C ANISOU 820 CG LEU A 101 2523 2018 5480 1458 78 -495 C ATOM 821 CD1 LEU A 101 8.340 5.771 10.457 1.00 24.98 C ANISOU 821 CD1 LEU A 101 2112 2046 5333 1230 241 -516 C ATOM 822 CD2 LEU A 101 7.159 7.973 10.476 1.00 28.23 C ANISOU 822 CD2 LEU A 101 2698 2452 5574 1766 -68 -695 C ATOM 823 N LEU A 102 11.462 6.427 8.107 1.00 24.50 N ANISOU 823 N LEU A 102 2509 1378 5421 981 345 -23 N ATOM 824 CA LEU A 102 11.715 6.340 6.678 1.00 24.97 C ANISOU 824 CA LEU A 102 2664 1407 5418 962 387 75 C ATOM 825 C LEU A 102 10.788 5.318 6.054 1.00 24.69 C ANISOU 825 C LEU A 102 2508 1565 5306 1010 435 -31 C ATOM 826 O LEU A 102 10.360 4.385 6.727 1.00 23.93 O ANISOU 826 O LEU A 102 2259 1604 5229 956 494 -131 O ATOM 827 CB LEU A 102 13.171 5.948 6.472 1.00 24.58 C ANISOU 827 CB LEU A 102 2593 1320 5427 770 523 232 C ATOM 828 CG LEU A 102 14.210 6.950 6.993 1.00 26.28 C ANISOU 828 CG LEU A 102 2900 1400 5684 629 484 341 C ATOM 829 CD1 LEU A 102 15.628 6.398 6.825 1.00 25.40 C ANISOU 829 CD1 LEU A 102 2660 1397 5593 453 631 469 C ATOM 830 CD2 LEU A 102 14.040 8.288 6.285 1.00 27.32 C ANISOU 830 CD2 LEU A 102 3328 1329 5724 643 358 407 C ATOM 831 N PHE A 103 10.528 5.417 4.765 1.00 25.55 N ANISOU 831 N PHE A 103 2704 1694 5310 1069 417 -5 N ATOM 832 CA PHE A 103 9.589 4.511 4.147 1.00 25.72 C ANISOU 832 CA PHE A 103 2617 1923 5231 1086 442 -129 C ATOM 833 C PHE A 103 10.170 3.738 2.976 1.00 25.71 C ANISOU 833 C PHE A 103 2670 1913 5185 993 563 -56 C ATOM 834 O PHE A 103 11.168 4.117 2.384 1.00 26.61 O ANISOU 834 O PHE A 103 2899 1906 5305 962 608 98 O ATOM 835 CB PHE A 103 8.285 5.242 3.740 1.00 27.43 C ANISOU 835 CB PHE A 103 2827 2297 5298 1314 272 -249 C ATOM 836 CG PHE A 103 7.449 5.673 4.923 1.00 29.68 C ANISOU 836 CG PHE A 103 2986 2712 5580 1443 171 -394 C ATOM 837 CD1 PHE A 103 6.761 4.722 5.683 1.00 31.23 C ANISOU 837 CD1 PHE A 103 2937 3165 5764 1320 234 -544 C ATOM 838 CD2 PHE A 103 7.407 6.990 5.317 1.00 32.48 C ANISOU 838 CD2 PHE A 103 3497 2919 5923 1664 24 -380 C ATOM 839 CE1 PHE A 103 6.050 5.087 6.797 1.00 31.65 C ANISOU 839 CE1 PHE A 103 2845 3390 5791 1424 163 -678 C ATOM 840 CE2 PHE A 103 6.667 7.388 6.433 1.00 33.36 C ANISOU 840 CE2 PHE A 103 3493 3170 6011 1824 -65 -535 C ATOM 841 CZ PHE A 103 5.988 6.441 7.173 1.00 33.43 C ANISOU 841 CZ PHE A 103 3196 3500 6004 1709 10 -685 C ATOM 842 N LEU A 104 9.564 2.601 2.678 1.00 26.46 N ANISOU 842 N LEU A 104 2687 2153 5213 919 624 -178 N ATOM 843 CA LEU A 104 9.915 1.851 1.486 1.00 27.80 C ANISOU 843 CA LEU A 104 2937 2328 5299 868 720 -156 C ATOM 844 C LEU A 104 8.729 1.962 0.591 1.00 29.55 C ANISOU 844 C LEU A 104 3130 2749 5349 934 617 -276 C ATOM 845 O LEU A 104 7.700 2.535 0.981 1.00 30.03 O ANISOU 845 O LEU A 104 3081 2969 5358 1034 483 -378 O ATOM 846 CB LEU A 104 10.151 0.348 1.806 1.00 26.46 C ANISOU 846 CB LEU A 104 2779 2127 5149 721 862 -222 C ATOM 847 CG LEU A 104 11.281 0.006 2.768 1.00 28.02 C ANISOU 847 CG LEU A 104 2991 2173 5481 701 961 -122 C ATOM 848 CD1 LEU A 104 12.563 0.720 2.352 1.00 26.35 C ANISOU 848 CD1 LEU A 104 2800 1904 5310 774 997 52 C ATOM 849 CD2 LEU A 104 10.910 0.307 4.226 1.00 29.23 C ANISOU 849 CD2 LEU A 104 3040 2334 5730 668 902 -153 C ATOM 850 N ARG A 105 8.854 1.365 -0.586 1.00 32.17 N ANISOU 850 N ARG A 105 3539 3117 5566 897 678 -285 N ATOM 851 CA ARG A 105 7.814 1.372 -1.579 1.00 35.99 C ANISOU 851 CA ARG A 105 3992 3827 5856 947 582 -402 C ATOM 852 C ARG A 105 6.619 0.564 -1.099 1.00 37.79 C ANISOU 852 C ARG A 105 4052 4295 6011 796 556 -624 C ATOM 853 O ARG A 105 5.473 0.954 -1.319 1.00 39.69 O ANISOU 853 O ARG A 105 4141 4835 6106 878 418 -750 O ATOM 854 CB ARG A 105 8.360 0.828 -2.900 1.00 37.42 C ANISOU 854 CB ARG A 105 4311 3984 5925 917 673 -366 C ATOM 855 CG ARG A 105 9.290 1.818 -3.632 1.00 40.94 C ANISOU 855 CG ARG A 105 4894 4310 6352 1043 675 -151 C ATOM 856 CD ARG A 105 9.478 1.425 -5.098 1.00 48.30 C ANISOU 856 CD ARG A 105 5928 5328 7097 1050 729 -147 C ATOM 857 NE ARG A 105 9.410 -0.027 -5.252 1.00 49.57 N ANISOU 857 NE ARG A 105 6092 5520 7220 917 841 -311 N ATOM 858 CZ ARG A 105 10.432 -0.861 -5.070 1.00 51.61 C ANISOU 858 CZ ARG A 105 6425 5635 7550 869 1007 -285 C ATOM 859 NH1 ARG A 105 11.634 -0.402 -4.724 1.00 51.23 N ANISOU 859 NH1 ARG A 105 6372 5480 7612 920 1090 -105 N ATOM 860 NH2 ARG A 105 10.246 -2.167 -5.228 1.00 51.84 N ANISOU 860 NH2 ARG A 105 6546 5638 7512 771 1083 -449 N ATOM 861 N ASP A 106 6.891 -0.540 -0.412 1.00 37.76 N ANISOU 861 N ASP A 106 4081 4183 6083 577 684 -668 N ATOM 862 CA ASP A 106 5.825 -1.278 0.267 1.00 39.28 C ANISOU 862 CA ASP A 106 4138 4583 6202 347 676 -852 C ATOM 863 C ASP A 106 5.225 -0.497 1.420 1.00 38.38 C ANISOU 863 C ASP A 106 3809 4635 6139 429 585 -883 C ATOM 864 O ASP A 106 5.844 -0.235 2.438 1.00 37.67 O ANISOU 864 O ASP A 106 3742 4360 6212 467 621 -785 O ATOM 865 CB ASP A 106 6.303 -2.644 0.758 1.00 39.24 C ANISOU 865 CB ASP A 106 4319 4350 6239 91 831 -866 C ATOM 866 CG ASP A 106 5.162 -3.615 1.002 1.00 43.31 C ANISOU 866 CG ASP A 106 4789 5074 6593 -261 839 -1065 C ATOM 867 OD1 ASP A 106 4.009 -3.198 1.299 1.00 45.85 O ANISOU 867 OD1 ASP A 106 4828 5785 6809 -321 738 -1193 O ATOM 868 OD2 ASP A 106 5.434 -4.824 0.894 1.00 46.31 O ANISOU 868 OD2 ASP A 106 5433 5236 6924 -483 947 -1100 O ATOM 869 N THR A 107 3.958 -0.205 1.254 1.00 39.92 N ANISOU 869 N THR A 107 3774 5233 6160 454 464 -1047 N ATOM 870 CA THR A 107 3.151 0.444 2.256 1.00 40.03 C ANISOU 870 CA THR A 107 3538 5523 6150 557 370 -1138 C ATOM 871 C THR A 107 2.965 -0.389 3.548 1.00 38.76 C ANISOU 871 C THR A 107 3298 5402 6028 244 478 -1198 C ATOM 872 O THR A 107 2.601 0.145 4.600 1.00 37.84 O ANISOU 872 O THR A 107 3008 5440 5930 334 435 -1238 O ATOM 873 CB THR A 107 1.831 0.867 1.573 1.00 43.43 C ANISOU 873 CB THR A 107 3709 6469 6325 699 211 -1320 C ATOM 874 OG1 THR A 107 1.719 2.291 1.639 1.00 45.40 O ANISOU 874 OG1 THR A 107 3936 6741 6572 1154 50 -1275 O ATOM 875 CG2 THR A 107 0.570 0.152 2.133 1.00 46.54 C ANISOU 875 CG2 THR A 107 3770 7387 6527 401 218 -1556 C ATOM 876 N LYS A 108 3.309 -1.674 3.485 1.00 37.18 N ANISOU 876 N LYS A 108 3284 5013 5830 -98 620 -1191 N ATOM 877 CA LYS A 108 3.106 -2.580 4.614 1.00 36.60 C ANISOU 877 CA LYS A 108 3219 4940 5746 -438 724 -1230 C ATOM 878 C LYS A 108 4.354 -2.709 5.480 1.00 32.91 C ANISOU 878 C LYS A 108 2979 4029 5497 -374 819 -1041 C ATOM 879 O LYS A 108 4.391 -3.491 6.432 1.00 33.18 O ANISOU 879 O LYS A 108 3104 3977 5529 -618 910 -1030 O ATOM 880 CB LYS A 108 2.638 -3.946 4.102 1.00 39.46 C ANISOU 880 CB LYS A 108 3723 5338 5932 -876 806 -1346 C ATOM 881 CG LYS A 108 1.146 -4.008 3.757 1.00 45.07 C ANISOU 881 CG LYS A 108 4104 6650 6371 -1099 726 -1580 C ATOM 882 CD LYS A 108 0.856 -5.171 2.799 1.00 51.51 C ANISOU 882 CD LYS A 108 5121 7445 7007 -1488 776 -1692 C ATOM 883 CE LYS A 108 -0.642 -5.521 2.739 1.00 56.50 C ANISOU 883 CE LYS A 108 5419 8720 7329 -1891 728 -1940 C ATOM 884 NZ LYS A 108 -1.047 -6.503 3.788 1.00 59.50 N ANISOU 884 NZ LYS A 108 5872 9132 7604 -2440 847 -1986 N ATOM 885 N THR A 109 5.372 -1.927 5.149 1.00 29.27 N ANISOU 885 N THR A 109 2608 3318 5195 -58 792 -891 N ATOM 886 CA THR A 109 6.631 -1.933 5.900 1.00 27.17 C ANISOU 886 CA THR A 109 2499 2711 5115 30 865 -718 C ATOM 887 C THR A 109 6.994 -0.510 6.319 1.00 25.99 C ANISOU 887 C THR A 109 2233 2555 5086 312 765 -640 C ATOM 888 O THR A 109 6.405 0.449 5.802 1.00 26.67 O ANISOU 888 O THR A 109 2206 2815 5114 490 642 -694 O ATOM 889 CB THR A 109 7.774 -2.526 5.097 1.00 26.72 C ANISOU 889 CB THR A 109 2700 2346 5108 79 957 -606 C ATOM 890 OG1 THR A 109 8.021 -1.718 3.942 1.00 26.55 O ANISOU 890 OG1 THR A 109 2657 2349 5083 277 898 -564 O ATOM 891 CG2 THR A 109 7.449 -3.991 4.656 1.00 28.40 C ANISOU 891 CG2 THR A 109 3130 2482 5177 -187 1049 -700 C ATOM 892 N LEU A 110 7.916 -0.404 7.283 1.00 24.75 N ANISOU 892 N LEU A 110 2132 2202 5069 351 806 -522 N ATOM 893 CA LEU A 110 8.579 0.855 7.604 1.00 23.84 C ANISOU 893 CA LEU A 110 1995 1991 5072 560 728 -426 C ATOM 894 C LEU A 110 9.954 0.573 8.153 1.00 22.80 C ANISOU 894 C LEU A 110 1964 1634 5067 551 813 -274 C ATOM 895 O LEU A 110 10.318 -0.599 8.464 1.00 22.84 O ANISOU 895 O LEU A 110 2061 1553 5063 443 922 -249 O ATOM 896 CB LEU A 110 7.773 1.696 8.589 1.00 24.51 C ANISOU 896 CB LEU A 110 1917 2259 5135 648 620 -528 C ATOM 897 CG LEU A 110 7.386 1.117 9.950 1.00 25.00 C ANISOU 897 CG LEU A 110 1876 2445 5177 498 670 -593 C ATOM 898 CD1 LEU A 110 8.501 1.396 10.927 1.00 23.16 C ANISOU 898 CD1 LEU A 110 1712 2005 5084 541 687 -469 C ATOM 899 CD2 LEU A 110 6.138 1.835 10.389 1.00 26.83 C ANISOU 899 CD2 LEU A 110 1889 3015 5291 607 561 -767 C ATOM 900 N MET A 111 10.741 1.635 8.221 1.00 22.36 N ANISOU 900 N MET A 111 1914 1482 5097 667 756 -175 N ATOM 901 CA MET A 111 12.103 1.552 8.673 1.00 21.82 C ANISOU 901 CA MET A 111 1876 1291 5121 663 819 -39 C ATOM 902 C MET A 111 12.303 2.699 9.680 1.00 21.66 C ANISOU 902 C MET A 111 1803 1256 5170 696 717 -28 C ATOM 903 O MET A 111 11.674 3.782 9.524 1.00 22.18 O ANISOU 903 O MET A 111 1892 1323 5212 777 595 -84 O ATOM 904 CB MET A 111 12.949 1.732 7.430 1.00 22.15 C ANISOU 904 CB MET A 111 1988 1277 5152 696 861 67 C ATOM 905 CG MET A 111 14.309 1.302 7.404 1.00 26.06 C ANISOU 905 CG MET A 111 2476 1751 5673 705 961 184 C ATOM 906 SD MET A 111 14.772 0.900 5.679 1.00 27.11 S ANISOU 906 SD MET A 111 2688 1906 5707 748 1055 233 S ATOM 907 CE MET A 111 14.745 2.492 4.918 1.00 23.71 C ANISOU 907 CE MET A 111 2287 1466 5257 706 954 310 C ATOM 908 N PHE A 112 13.115 2.473 10.709 1.00 21.32 N ANISOU 908 N PHE A 112 1717 1197 5186 661 751 29 N ATOM 909 CA PHE A 112 13.635 3.563 11.527 1.00 21.48 C ANISOU 909 CA PHE A 112 1713 1185 5262 657 661 55 C ATOM 910 C PHE A 112 15.132 3.670 11.264 1.00 21.84 C ANISOU 910 C PHE A 112 1740 1216 5340 597 712 200 C ATOM 911 O PHE A 112 15.838 2.637 11.182 1.00 21.81 O ANISOU 911 O PHE A 112 1688 1276 5325 621 822 263 O ATOM 912 CB PHE A 112 13.296 3.395 13.032 1.00 21.25 C ANISOU 912 CB PHE A 112 1607 1230 5239 651 635 -19 C ATOM 913 CG PHE A 112 11.859 3.760 13.347 1.00 21.59 C ANISOU 913 CG PHE A 112 1617 1367 5218 712 558 -181 C ATOM 914 CD1 PHE A 112 11.488 5.101 13.464 1.00 22.33 C ANISOU 914 CD1 PHE A 112 1762 1421 5302 823 418 -256 C ATOM 915 CD2 PHE A 112 10.877 2.788 13.462 1.00 21.64 C ANISOU 915 CD2 PHE A 112 1559 1520 5143 661 621 -267 C ATOM 916 CE1 PHE A 112 10.171 5.449 13.726 1.00 23.13 C ANISOU 916 CE1 PHE A 112 1802 1676 5309 958 341 -426 C ATOM 917 CE2 PHE A 112 9.534 3.139 13.705 1.00 22.93 C ANISOU 917 CE2 PHE A 112 1618 1886 5207 717 555 -434 C ATOM 918 CZ PHE A 112 9.193 4.461 13.860 1.00 24.24 C ANISOU 918 CZ PHE A 112 1788 2061 5361 903 414 -519 C ATOM 919 N GLY A 113 15.607 4.905 11.087 1.00 22.66 N ANISOU 919 N GLY A 113 1901 1253 5456 521 632 248 N ATOM 920 CA GLY A 113 17.020 5.180 10.845 1.00 23.63 C ANISOU 920 CA GLY A 113 1966 1440 5572 388 676 378 C ATOM 921 C GLY A 113 17.674 5.773 12.075 1.00 24.24 C ANISOU 921 C GLY A 113 1975 1558 5675 277 606 375 C ATOM 922 O GLY A 113 17.199 6.743 12.631 1.00 24.63 O ANISOU 922 O GLY A 113 2148 1474 5737 242 483 305 O ATOM 923 N SER A 114 18.764 5.171 12.516 1.00 24.64 N ANISOU 923 N SER A 114 1835 1814 5713 253 676 438 N ATOM 924 CA SER A 114 19.484 5.638 13.712 1.00 25.50 C ANISOU 924 CA SER A 114 1836 2033 5822 138 608 430 C ATOM 925 C SER A 114 20.812 6.256 13.276 1.00 27.57 C ANISOU 925 C SER A 114 1988 2471 6018 -104 626 532 C ATOM 926 O SER A 114 21.486 5.723 12.372 1.00 28.21 O ANISOU 926 O SER A 114 1943 2733 6040 -83 740 617 O ATOM 927 CB SER A 114 19.751 4.445 14.659 1.00 25.00 C ANISOU 927 CB SER A 114 1612 2140 5746 310 660 424 C ATOM 928 OG SER A 114 18.501 3.799 14.974 1.00 25.96 O ANISOU 928 OG SER A 114 1849 2120 5895 457 667 344 O ATOM 929 N TYR A 115 21.178 7.347 13.946 1.00 28.98 N ANISOU 929 N TYR A 115 2210 2620 6180 -346 515 509 N ATOM 930 CA TYR A 115 22.416 8.079 13.707 1.00 32.40 C ANISOU 930 CA TYR A 115 2545 3245 6519 -690 516 590 C ATOM 931 C TYR A 115 22.689 8.321 12.243 1.00 33.78 C ANISOU 931 C TYR A 115 2788 3417 6629 -827 600 702 C ATOM 932 O TYR A 115 23.837 8.237 11.831 1.00 35.75 O ANISOU 932 O TYR A 115 2798 4015 6771 -1009 686 788 O ATOM 933 CB TYR A 115 23.645 7.363 14.304 1.00 34.08 C ANISOU 933 CB TYR A 115 2361 3929 6659 -679 575 620 C ATOM 934 CG TYR A 115 23.484 7.055 15.750 1.00 35.05 C ANISOU 934 CG TYR A 115 2410 4096 6813 -540 496 531 C ATOM 935 CD1 TYR A 115 23.526 5.744 16.207 1.00 32.78 C ANISOU 935 CD1 TYR A 115 1956 3978 6522 -196 559 534 C ATOM 936 CD2 TYR A 115 23.283 8.088 16.671 1.00 37.78 C ANISOU 936 CD2 TYR A 115 2900 4286 7166 -748 351 441 C ATOM 937 CE1 TYR A 115 23.338 5.464 17.556 1.00 36.92 C ANISOU 937 CE1 TYR A 115 2446 4534 7049 -78 486 469 C ATOM 938 CE2 TYR A 115 23.095 7.826 18.008 1.00 39.48 C ANISOU 938 CE2 TYR A 115 3052 4558 7390 -619 280 353 C ATOM 939 CZ TYR A 115 23.117 6.516 18.449 1.00 39.03 C ANISOU 939 CZ TYR A 115 2812 4690 7327 -293 351 377 C ATOM 940 OH TYR A 115 22.936 6.279 19.792 1.00 41.30 O ANISOU 940 OH TYR A 115 3060 5036 7594 -185 280 307 O ATOM 941 N LEU A 116 21.658 8.633 11.465 1.00 33.53 N ANISOU 941 N LEU A 116 3058 3049 6634 -735 574 698 N ATOM 942 CA LEU A 116 21.805 8.767 10.001 1.00 35.44 C ANISOU 942 CA LEU A 116 3388 3282 6795 -823 657 811 C ATOM 943 C LEU A 116 22.854 9.760 9.543 1.00 38.75 C ANISOU 943 C LEU A 116 3846 3800 7076 -1279 665 929 C ATOM 944 O LEU A 116 23.250 9.745 8.378 1.00 40.83 O ANISOU 944 O LEU A 116 4097 4182 7235 -1391 768 1042 O ATOM 945 CB LEU A 116 20.480 9.168 9.332 1.00 34.25 C ANISOU 945 CB LEU A 116 3594 2747 6675 -660 584 781 C ATOM 946 CG LEU A 116 19.444 8.123 9.002 1.00 32.95 C ANISOU 946 CG LEU A 116 3390 2556 6572 -294 629 705 C ATOM 947 CD1 LEU A 116 18.338 8.768 8.188 1.00 33.87 C ANISOU 947 CD1 LEU A 116 3828 2385 6658 -193 541 691 C ATOM 948 CD2 LEU A 116 20.019 6.919 8.269 1.00 36.30 C ANISOU 948 CD2 LEU A 116 3575 3260 6959 -195 800 758 C ATOM 949 N ASP A 117 23.298 10.636 10.435 1.00 41.05 N ANISOU 949 N ASP A 117 4203 4052 7342 -1579 559 902 N ATOM 950 CA ASP A 117 24.135 11.730 10.005 1.00 45.21 C ANISOU 950 CA ASP A 117 4874 4590 7713 -2104 547 1010 C ATOM 951 C ASP A 117 25.602 11.344 10.186 1.00 46.90 C ANISOU 951 C ASP A 117 4593 5421 7807 -2367 659 1057 C ATOM 952 O ASP A 117 26.505 12.144 9.904 1.00 49.22 O ANISOU 952 O ASP A 117 4892 5878 7931 -2893 674 1144 O ATOM 953 CB ASP A 117 23.727 13.061 10.705 1.00 47.69 C ANISOU 953 CB ASP A 117 5657 4440 8022 -2333 351 948 C ATOM 954 CG ASP A 117 24.444 13.316 12.063 1.00 51.80 C ANISOU 954 CG ASP A 117 5997 5156 8529 -2575 275 853 C ATOM 955 OD1 ASP A 117 23.759 13.503 13.085 1.00 54.59 O ANISOU 955 OD1 ASP A 117 6501 5267 8975 -2377 145 708 O ATOM 956 OD2 ASP A 117 25.688 13.421 12.124 1.00 58.57 O ANISOU 956 OD2 ASP A 117 6569 6432 9254 -2991 335 911 O ATOM 957 N ASP A 118 25.820 10.098 10.621 1.00 44.06 N ANISOU 957 N ASP A 118 3817 5419 7504 -1996 736 998 N ATOM 958 CA ASP A 118 27.130 9.679 11.098 1.00 45.80 C ANISOU 958 CA ASP A 118 3535 6263 7604 -2116 801 1000 C ATOM 959 C ASP A 118 27.568 8.366 10.453 1.00 45.11 C ANISOU 959 C ASP A 118 3077 6600 7463 -1735 969 1028 C ATOM 960 O ASP A 118 27.135 7.297 10.881 1.00 41.75 O ANISOU 960 O ASP A 118 2581 6144 7139 -1252 980 960 O ATOM 961 CB ASP A 118 27.079 9.543 12.631 1.00 44.84 C ANISOU 961 CB ASP A 118 3313 6163 7561 -1997 679 876 C ATOM 962 CG ASP A 118 28.434 9.231 13.246 1.00 47.40 C ANISOU 962 CG ASP A 118 3117 7162 7730 -2120 708 865 C ATOM 963 OD1 ASP A 118 28.500 9.197 14.490 1.00 48.43 O ANISOU 963 OD1 ASP A 118 3156 7356 7889 -2065 600 772 O ATOM 964 OD2 ASP A 118 29.407 8.986 12.506 1.00 48.02 O ANISOU 964 OD2 ASP A 118 2856 7751 7640 -2235 835 938 O ATOM 965 N GLU A 119 28.441 8.445 9.446 1.00 47.38 N ANISOU 965 N GLU A 119 3153 7286 7563 -1959 1101 1124 N ATOM 966 CA GLU A 119 28.915 7.234 8.743 1.00 47.97 C ANISOU 966 CA GLU A 119 2892 7788 7546 -1563 1265 1132 C ATOM 967 C GLU A 119 29.530 6.170 9.664 1.00 47.36 C ANISOU 967 C GLU A 119 2412 8143 7439 -1155 1271 1047 C ATOM 968 O GLU A 119 29.541 5.003 9.332 1.00 46.43 O ANISOU 968 O GLU A 119 2186 8154 7302 -659 1360 1020 O ATOM 969 CB GLU A 119 29.879 7.577 7.606 1.00 50.67 C ANISOU 969 CB GLU A 119 3008 8605 7641 -1905 1412 1237 C ATOM 970 CG GLU A 119 31.176 8.220 8.033 1.00 56.54 C ANISOU 970 CG GLU A 119 3356 9956 8169 -2407 1417 1258 C ATOM 971 CD GLU A 119 32.066 8.518 6.841 1.00 61.21 C ANISOU 971 CD GLU A 119 3711 11064 8483 -2773 1585 1365 C ATOM 972 OE1 GLU A 119 33.307 8.525 6.994 1.00 66.90 O ANISOU 972 OE1 GLU A 119 3898 12561 8961 -3004 1655 1357 O ATOM 973 OE2 GLU A 119 31.515 8.732 5.740 1.00 60.81 O ANISOU 973 OE2 GLU A 119 3988 10685 8431 -2825 1650 1455 O ATOM 974 N LYS A 120 30.004 6.599 10.827 1.00 48.62 N ANISOU 974 N LYS A 120 2406 8488 7581 -1356 1161 1004 N ATOM 975 CA LYS A 120 30.599 5.707 11.812 1.00 49.17 C ANISOU 975 CA LYS A 120 2116 8970 7595 -977 1135 933 C ATOM 976 C LYS A 120 29.577 4.965 12.660 1.00 45.19 C ANISOU 976 C LYS A 120 1891 7989 7291 -525 1051 869 C ATOM 977 O LYS A 120 29.896 3.906 13.200 1.00 45.19 O ANISOU 977 O LYS A 120 1706 8226 7238 -63 1058 835 O ATOM 978 CB LYS A 120 31.569 6.483 12.703 1.00 52.80 C ANISOU 978 CB LYS A 120 2254 9892 7915 -1410 1045 906 C ATOM 979 CG LYS A 120 32.793 7.035 11.948 1.00 58.57 C ANISOU 979 CG LYS A 120 2586 11294 8374 -1878 1148 962 C ATOM 980 CD LYS A 120 33.767 5.929 11.530 1.00 61.37 C ANISOU 980 CD LYS A 120 2402 12407 8509 -1422 1284 948 C ATOM 981 CE LYS A 120 34.842 6.456 10.580 1.00 67.50 C ANISOU 981 CE LYS A 120 2784 13869 8996 -1891 1421 1006 C ATOM 982 NZ LYS A 120 35.692 7.458 11.246 1.00 70.33 N ANISOU 982 NZ LYS A 120 2852 14686 9184 -2562 1342 990 N ATOM 983 N ASN A 121 28.358 5.505 12.765 1.00 41.52 N ANISOU 983 N ASN A 121 1874 6879 7022 -645 972 854 N ATOM 984 CA ASN A 121 27.334 4.921 13.631 1.00 38.62 C ANISOU 984 CA ASN A 121 1751 6107 6816 -311 896 788 C ATOM 985 C ASN A 121 25.986 4.534 13.009 1.00 35.27 C ANISOU 985 C ASN A 121 1712 5147 6541 -105 927 777 C ATOM 986 O ASN A 121 25.185 3.815 13.641 1.00 33.16 O ANISOU 986 O ASN A 121 1603 4632 6365 181 897 726 O ATOM 987 CB ASN A 121 27.079 5.831 14.845 1.00 39.00 C ANISOU 987 CB ASN A 121 1900 5991 6927 -581 737 724 C ATOM 988 CG ASN A 121 28.205 5.771 15.843 1.00 42.87 C ANISOU 988 CG ASN A 121 2005 7009 7277 -625 681 699 C ATOM 989 OD1 ASN A 121 28.333 4.799 16.580 1.00 43.11 O ANISOU 989 OD1 ASN A 121 1904 7197 7278 -230 671 679 O ATOM 990 ND2 ASN A 121 29.032 6.809 15.874 1.00 44.35 N ANISOU 990 ND2 ASN A 121 2025 7478 7347 -1123 639 702 N ATOM 991 N TRP A 122 25.728 4.961 11.773 1.00 35.26 N ANISOU 991 N TRP A 122 1856 5003 6537 -260 989 826 N ATOM 992 CA TRP A 122 24.388 4.745 11.231 1.00 32.59 C ANISOU 992 CA TRP A 122 1866 4195 6322 -107 990 798 C ATOM 993 C TRP A 122 23.897 3.279 11.170 1.00 31.02 C ANISOU 993 C TRP A 122 1718 3919 6148 332 1062 758 C ATOM 994 O TRP A 122 24.682 2.347 11.146 1.00 32.27 O ANISOU 994 O TRP A 122 1685 4371 6205 584 1141 771 O ATOM 995 CB TRP A 122 24.212 5.468 9.899 1.00 33.20 C ANISOU 995 CB TRP A 122 2104 4149 6362 -330 1030 865 C ATOM 996 CG TRP A 122 25.125 5.053 8.780 1.00 35.16 C ANISOU 996 CG TRP A 122 2139 4767 6455 -314 1181 939 C ATOM 997 CD1 TRP A 122 25.544 3.790 8.484 1.00 35.44 C ANISOU 997 CD1 TRP A 122 1991 5057 6417 55 1296 919 C ATOM 998 CD2 TRP A 122 25.644 5.902 7.746 1.00 37.43 C ANISOU 998 CD2 TRP A 122 2425 5183 6613 -665 1236 1040 C ATOM 999 NE1 TRP A 122 26.325 3.811 7.359 1.00 39.73 N ANISOU 999 NE1 TRP A 122 2366 5937 6793 -20 1422 983 N ATOM 1000 CE2 TRP A 122 26.399 5.094 6.885 1.00 38.94 C ANISOU 1000 CE2 TRP A 122 2360 5782 6654 -489 1395 1068 C ATOM 1001 CE3 TRP A 122 25.550 7.273 7.472 1.00 39.59 C ANISOU 1001 CE3 TRP A 122 2932 5253 6859 -1112 1165 1113 C ATOM 1002 CZ2 TRP A 122 27.054 5.602 5.774 1.00 41.91 C ANISOU 1002 CZ2 TRP A 122 2649 6426 6851 -770 1499 1167 C ATOM 1003 CZ3 TRP A 122 26.219 7.779 6.366 1.00 41.49 C ANISOU 1003 CZ3 TRP A 122 3136 5711 6918 -1423 1263 1233 C ATOM 1004 CH2 TRP A 122 26.959 6.949 5.536 1.00 43.61 C ANISOU 1004 CH2 TRP A 122 3091 6443 7038 -1266 1435 1260 C ATOM 1005 N GLY A 123 22.577 3.115 11.134 1.00 28.74 N ANISOU 1005 N GLY A 123 1711 3240 5968 413 1026 700 N ATOM 1006 CA GLY A 123 21.918 1.820 11.029 1.00 27.53 C ANISOU 1006 CA GLY A 123 1694 2939 5826 716 1086 654 C ATOM 1007 C GLY A 123 20.456 2.014 10.681 1.00 25.66 C ANISOU 1007 C GLY A 123 1715 2360 5674 666 1044 588 C ATOM 1008 O GLY A 123 19.954 3.145 10.730 1.00 25.28 O ANISOU 1008 O GLY A 123 1742 2183 5679 476 951 572 O ATOM 1009 N LEU A 124 19.794 0.917 10.304 1.00 24.98 N ANISOU 1009 N LEU A 124 1778 2142 5572 843 1107 542 N ATOM 1010 CA LEU A 124 18.394 0.891 9.896 1.00 23.69 C ANISOU 1010 CA LEU A 124 1808 1749 5446 803 1078 461 C ATOM 1011 C LEU A 124 17.735 -0.270 10.572 1.00 23.25 C ANISOU 1011 C LEU A 124 1876 1581 5376 903 1102 398 C ATOM 1012 O LEU A 124 18.372 -1.362 10.704 1.00 24.21 O ANISOU 1012 O LEU A 124 2045 1724 5428 1078 1177 429 O ATOM 1013 CB LEU A 124 18.251 0.662 8.393 1.00 24.06 C ANISOU 1013 CB LEU A 124 1938 1774 5429 832 1149 463 C ATOM 1014 CG LEU A 124 18.855 1.765 7.534 1.00 24.94 C ANISOU 1014 CG LEU A 124 1978 1985 5512 698 1143 547 C ATOM 1015 CD1 LEU A 124 18.967 1.321 6.064 1.00 25.71 C ANISOU 1015 CD1 LEU A 124 2132 2130 5507 765 1241 562 C ATOM 1016 CD2 LEU A 124 17.973 3.047 7.678 1.00 24.35 C ANISOU 1016 CD2 LEU A 124 2007 1747 5496 546 1006 524 C ATOM 1017 N SER A 125 16.490 -0.089 10.992 1.00 22.31 N ANISOU 1017 N SER A 125 1830 1356 5290 804 1041 310 N ATOM 1018 CA SER A 125 15.673 -1.207 11.521 1.00 22.31 C ANISOU 1018 CA SER A 125 1977 1260 5240 801 1076 248 C ATOM 1019 C SER A 125 14.446 -1.268 10.669 1.00 22.09 C ANISOU 1019 C SER A 125 2029 1185 5178 700 1072 147 C ATOM 1020 O SER A 125 13.881 -0.221 10.282 1.00 21.63 O ANISOU 1020 O SER A 125 1887 1180 5151 655 993 101 O ATOM 1021 CB SER A 125 15.212 -0.952 12.959 1.00 21.93 C ANISOU 1021 CB SER A 125 1875 1246 5213 730 1011 216 C ATOM 1022 OG SER A 125 16.360 -0.809 13.777 1.00 22.45 O ANISOU 1022 OG SER A 125 1842 1394 5296 818 995 302 O ATOM 1023 N PHE A 126 14.028 -2.505 10.425 1.00 22.84 N ANISOU 1023 N PHE A 126 2314 1179 5184 669 1147 107 N ATOM 1024 CA PHE A 126 12.991 -2.841 9.456 1.00 23.21 C ANISOU 1024 CA PHE A 126 2451 1212 5157 552 1159 1 C ATOM 1025 C PHE A 126 11.839 -3.539 10.167 1.00 23.88 C ANISOU 1025 C PHE A 126 2618 1300 5154 338 1167 -93 C ATOM 1026 O PHE A 126 12.065 -4.437 11.020 1.00 24.67 O ANISOU 1026 O PHE A 126 2889 1278 5205 303 1219 -48 O ATOM 1027 CB PHE A 126 13.656 -3.733 8.380 1.00 24.23 C ANISOU 1027 CB PHE A 126 2770 1221 5215 662 1251 25 C ATOM 1028 CG PHE A 126 12.761 -4.128 7.233 1.00 25.77 C ANISOU 1028 CG PHE A 126 3076 1403 5313 545 1264 -88 C ATOM 1029 CD1 PHE A 126 12.118 -3.166 6.470 1.00 26.49 C ANISOU 1029 CD1 PHE A 126 3005 1646 5412 504 1191 -139 C ATOM 1030 CD2 PHE A 126 12.676 -5.479 6.848 1.00 31.69 C ANISOU 1030 CD2 PHE A 126 4135 1969 5937 504 1343 -141 C ATOM 1031 CE1 PHE A 126 11.327 -3.508 5.408 1.00 28.37 C ANISOU 1031 CE1 PHE A 126 3316 1925 5539 410 1190 -247 C ATOM 1032 CE2 PHE A 126 11.900 -5.850 5.755 1.00 34.41 C ANISOU 1032 CE2 PHE A 126 4585 2318 6173 368 1350 -262 C ATOM 1033 CZ PHE A 126 11.211 -4.840 5.035 1.00 33.71 C ANISOU 1033 CZ PHE A 126 4259 2453 6096 319 1271 -316 C ATOM 1034 N TYR A 127 10.620 -3.119 9.801 1.00 23.98 N ANISOU 1034 N TYR A 127 2510 1481 5119 199 1113 -218 N ATOM 1035 CA TYR A 127 9.381 -3.497 10.461 1.00 24.94 C ANISOU 1035 CA TYR A 127 2592 1753 5131 -48 1110 -331 C ATOM 1036 C TYR A 127 8.393 -3.781 9.404 1.00 26.06 C ANISOU 1036 C TYR A 127 2730 2022 5151 -204 1105 -464 C ATOM 1037 O TYR A 127 8.447 -3.142 8.370 1.00 25.61 O ANISOU 1037 O TYR A 127 2596 2014 5121 -60 1053 -479 O ATOM 1038 CB TYR A 127 8.828 -2.339 11.308 1.00 24.32 C ANISOU 1038 CB TYR A 127 2234 1918 5090 2 1015 -387 C ATOM 1039 CG TYR A 127 9.790 -1.975 12.378 1.00 23.39 C ANISOU 1039 CG TYR A 127 2107 1700 5078 132 1005 -274 C ATOM 1040 CD1 TYR A 127 10.826 -1.083 12.106 1.00 22.31 C ANISOU 1040 CD1 TYR A 127 1930 1475 5071 341 956 -183 C ATOM 1041 CD2 TYR A 127 9.782 -2.645 13.612 1.00 23.97 C ANISOU 1041 CD2 TYR A 127 2249 1759 5097 14 1054 -241 C ATOM 1042 CE1 TYR A 127 11.744 -0.789 13.028 1.00 21.83 C ANISOU 1042 CE1 TYR A 127 1844 1366 5084 424 942 -93 C ATOM 1043 CE2 TYR A 127 10.724 -2.332 14.586 1.00 23.31 C ANISOU 1043 CE2 TYR A 127 2151 1614 5093 149 1034 -140 C ATOM 1044 CZ TYR A 127 11.697 -1.378 14.267 1.00 22.23 C ANISOU 1044 CZ TYR A 127 1926 1433 5089 352 973 -77 C ATOM 1045 OH TYR A 127 12.657 -0.996 15.172 1.00 22.87 O ANISOU 1045 OH TYR A 127 1956 1504 5230 454 941 6 O ATOM 1046 N ALA A 128 7.490 -4.731 9.669 1.00 27.86 N ANISOU 1046 N ALA A 128 3047 2320 5220 -528 1155 -557 N ATOM 1047 CA ALA A 128 6.409 -5.084 8.781 1.00 29.88 C ANISOU 1047 CA ALA A 128 3265 2775 5315 -762 1145 -714 C ATOM 1048 C ALA A 128 5.109 -5.417 9.546 1.00 33.20 C ANISOU 1048 C ALA A 128 3530 3530 5553 -1134 1156 -846 C ATOM 1049 O ALA A 128 5.125 -5.753 10.740 1.00 33.94 O ANISOU 1049 O ALA A 128 3678 3593 5623 -1273 1207 -793 O ATOM 1050 CB ALA A 128 6.812 -6.298 7.866 1.00 30.83 C ANISOU 1050 CB ALA A 128 3776 2580 5356 -876 1228 -708 C ATOM 1051 N ASP A 129 3.981 -5.362 8.844 1.00 35.52 N ANISOU 1051 N ASP A 129 3621 4189 5686 -1313 1111 -1019 N ATOM 1052 CA ASP A 129 2.704 -5.719 9.456 1.00 38.68 C ANISOU 1052 CA ASP A 129 3818 5017 5863 -1717 1131 -1167 C ATOM 1053 C ASP A 129 2.442 -7.239 9.633 1.00 40.87 C ANISOU 1053 C ASP A 129 4458 5117 5954 -2267 1253 -1177 C ATOM 1054 O ASP A 129 1.420 -7.612 10.180 1.00 43.11 O ANISOU 1054 O ASP A 129 4593 5766 6021 -2694 1289 -1286 O ATOM 1055 CB ASP A 129 1.520 -4.994 8.778 1.00 40.53 C ANISOU 1055 CB ASP A 129 3612 5836 5950 -1681 1020 -1369 C ATOM 1056 CG ASP A 129 1.272 -5.436 7.328 1.00 45.50 C ANISOU 1056 CG ASP A 129 4339 6474 6477 -1793 996 -1460 C ATOM 1057 OD1 ASP A 129 1.780 -6.484 6.865 1.00 46.67 O ANISOU 1057 OD1 ASP A 129 4900 6218 6614 -2010 1081 -1410 O ATOM 1058 OD2 ASP A 129 0.518 -4.712 6.636 1.00 51.78 O ANISOU 1058 OD2 ASP A 129 4797 7704 7173 -1634 880 -1596 O ATOM 1059 N LYS A 130 3.375 -8.069 9.175 1.00 40.18 N ANISOU 1059 N LYS A 130 4857 4482 5927 -2242 1313 -1069 N ATOM 1060 CA LYS A 130 3.441 -9.496 9.445 1.00 43.12 C ANISOU 1060 CA LYS A 130 5746 4491 6146 -2653 1419 -1031 C ATOM 1061 C LYS A 130 4.789 -9.799 10.083 1.00 41.38 C ANISOU 1061 C LYS A 130 5901 3739 6082 -2338 1465 -816 C ATOM 1062 O LYS A 130 5.766 -9.070 9.835 1.00 37.88 O ANISOU 1062 O LYS A 130 5355 3182 5856 -1838 1422 -724 O ATOM 1063 CB LYS A 130 3.326 -10.316 8.145 1.00 45.44 C ANISOU 1063 CB LYS A 130 6359 4592 6316 -2846 1430 -1135 C ATOM 1064 CG LYS A 130 1.908 -10.469 7.601 1.00 50.30 C ANISOU 1064 CG LYS A 130 6719 5713 6678 -3338 1402 -1363 C ATOM 1065 CD LYS A 130 1.887 -11.155 6.215 1.00 54.08 C ANISOU 1065 CD LYS A 130 7501 6001 7044 -3472 1394 -1478 C ATOM 1066 CE LYS A 130 0.514 -11.038 5.532 1.00 59.59 C ANISOU 1066 CE LYS A 130 7811 7331 7502 -3866 1330 -1723 C ATOM 1067 NZ LYS A 130 0.253 -12.092 4.479 1.00 64.40 N ANISOU 1067 NZ LYS A 130 8822 7752 7896 -4266 1345 -1867 N ATOM 1068 N PRO A 131 4.866 -10.887 10.881 1.00 43.52 N ANISOU 1068 N PRO A 131 6624 3698 6214 -2634 1549 -732 N ATOM 1069 CA PRO A 131 6.119 -11.342 11.512 1.00 42.90 C ANISOU 1069 CA PRO A 131 6955 3121 6223 -2317 1583 -532 C ATOM 1070 C PRO A 131 7.111 -11.931 10.511 1.00 43.32 C ANISOU 1070 C PRO A 131 7427 2715 6318 -2000 1591 -500 C ATOM 1071 O PRO A 131 8.279 -12.215 10.837 1.00 41.86 O ANISOU 1071 O PRO A 131 7519 2182 6205 -1608 1603 -352 O ATOM 1072 CB PRO A 131 5.641 -12.435 12.487 1.00 46.60 C ANISOU 1072 CB PRO A 131 7853 3404 6449 -2809 1662 -476 C ATOM 1073 CG PRO A 131 4.330 -12.883 11.970 1.00 49.09 C ANISOU 1073 CG PRO A 131 8148 3974 6531 -3433 1689 -660 C ATOM 1074 CD PRO A 131 3.700 -11.653 11.374 1.00 47.70 C ANISOU 1074 CD PRO A 131 7259 4405 6460 -3306 1610 -817 C ATOM 1075 N GLU A 132 6.634 -12.142 9.298 1.00 45.48 N ANISOU 1075 N GLU A 132 7736 3030 6513 -2158 1583 -652 N ATOM 1076 CA GLU A 132 7.472 -12.692 8.244 1.00 48.07 C ANISOU 1076 CA GLU A 132 8440 2978 6844 -1866 1595 -660 C ATOM 1077 C GLU A 132 7.352 -11.794 7.057 1.00 46.69 C ANISOU 1077 C GLU A 132 7842 3127 6770 -1686 1539 -766 C ATOM 1078 O GLU A 132 6.288 -11.228 6.789 1.00 48.11 O ANISOU 1078 O GLU A 132 7631 3739 6908 -1953 1492 -893 O ATOM 1079 CB GLU A 132 7.028 -14.095 7.842 1.00 51.03 C ANISOU 1079 CB GLU A 132 9461 2975 6953 -2284 1645 -754 C ATOM 1080 CG GLU A 132 6.594 -14.942 8.992 1.00 57.28 C ANISOU 1080 CG GLU A 132 10652 3551 7560 -2719 1696 -683 C ATOM 1081 CD GLU A 132 5.072 -15.035 9.124 1.00 62.27 C ANISOU 1081 CD GLU A 132 11089 4577 7993 -3465 1709 -829 C ATOM 1082 OE1 GLU A 132 4.317 -14.244 8.484 1.00 60.55 O ANISOU 1082 OE1 GLU A 132 10300 4899 7808 -3567 1659 -983 O ATOM 1083 OE2 GLU A 132 4.644 -15.909 9.899 1.00 65.81 O ANISOU 1083 OE2 GLU A 132 11964 4818 8224 -3945 1767 -783 O ATOM 1084 N THR A 133 8.441 -11.664 6.328 1.00 46.66 N ANISOU 1084 N THR A 133 7912 2949 6870 -1217 1542 -714 N ATOM 1085 CA THR A 133 8.459 -10.711 5.235 1.00 45.01 C ANISOU 1085 CA THR A 133 7313 3036 6754 -1014 1492 -773 C ATOM 1086 C THR A 133 8.621 -11.467 3.900 1.00 46.15 C ANISOU 1086 C THR A 133 7802 2974 6758 -989 1520 -888 C ATOM 1087 O THR A 133 9.213 -12.543 3.870 1.00 47.29 O ANISOU 1087 O THR A 133 8475 2693 6800 -904 1578 -878 O ATOM 1088 CB THR A 133 9.518 -9.621 5.515 1.00 42.16 C ANISOU 1088 CB THR A 133 6619 2779 6619 -543 1469 -616 C ATOM 1089 OG1 THR A 133 8.924 -8.313 5.398 1.00 44.20 O ANISOU 1089 OG1 THR A 133 6374 3446 6975 -553 1386 -642 O ATOM 1090 CG2 THR A 133 10.738 -9.760 4.640 1.00 41.51 C ANISOU 1090 CG2 THR A 133 6680 2530 6563 -134 1510 -567 C ATOM 1091 N THR A 134 8.035 -10.915 2.830 1.00 44.85 N ANISOU 1091 N THR A 134 7365 3115 6560 -1055 1467 -1007 N ATOM 1092 CA THR A 134 8.228 -11.414 1.476 1.00 44.73 C ANISOU 1092 CA THR A 134 7594 2982 6418 -983 1484 -1121 C ATOM 1093 C THR A 134 9.634 -11.098 0.995 1.00 42.50 C ANISOU 1093 C THR A 134 7311 2592 6246 -432 1527 -1002 C ATOM 1094 O THR A 134 10.307 -10.218 1.553 1.00 40.16 O ANISOU 1094 O THR A 134 6705 2419 6136 -158 1520 -843 O ATOM 1095 CB THR A 134 7.186 -10.831 0.455 1.00 45.88 C ANISOU 1095 CB THR A 134 7408 3552 6472 -1187 1401 -1275 C ATOM 1096 OG1 THR A 134 7.394 -9.411 0.248 1.00 39.91 O ANISOU 1096 OG1 THR A 134 6160 3125 5880 -875 1338 -1177 O ATOM 1097 CG2 THR A 134 5.736 -11.138 0.896 1.00 46.53 C ANISOU 1097 CG2 THR A 134 7404 3878 6398 -1761 1359 -1422 C ATOM 1098 N LYS A 135 10.077 -11.799 -0.047 1.00 42.39 N ANISOU 1098 N LYS A 135 7628 2384 6093 -288 1572 -1092 N ATOM 1099 CA LYS A 135 11.393 -11.546 -0.602 1.00 41.03 C ANISOU 1099 CA LYS A 135 7416 2200 5972 223 1627 -1004 C ATOM 1100 C LYS A 135 11.475 -10.148 -1.238 1.00 38.48 C ANISOU 1100 C LYS A 135 6566 2295 5762 350 1585 -932 C ATOM 1101 O LYS A 135 12.550 -9.576 -1.295 1.00 37.29 O ANISOU 1101 O LYS A 135 6229 2236 5703 693 1626 -797 O ATOM 1102 CB LYS A 135 11.830 -12.648 -1.583 1.00 44.22 C ANISOU 1102 CB LYS A 135 8313 2324 6164 385 1689 -1141 C ATOM 1103 CG LYS A 135 11.525 -12.369 -3.015 1.00 44.69 C ANISOU 1103 CG LYS A 135 8262 2608 6111 359 1674 -1266 C ATOM 1104 CD LYS A 135 11.646 -13.599 -3.869 1.00 48.45 C ANISOU 1104 CD LYS A 135 9300 2771 6339 403 1719 -1456 C ATOM 1105 CE LYS A 135 11.054 -13.327 -5.229 1.00 49.56 C ANISOU 1105 CE LYS A 135 9316 3173 6342 261 1681 -1604 C ATOM 1106 NZ LYS A 135 9.739 -13.969 -5.254 1.00 52.83 N ANISOU 1106 NZ LYS A 135 9966 3502 6605 -300 1613 -1792 N ATOM 1107 N GLU A 136 10.345 -9.622 -1.711 1.00 38.16 N ANISOU 1107 N GLU A 136 6305 2514 5681 67 1501 -1022 N ATOM 1108 CA GLU A 136 10.255 -8.252 -2.231 1.00 36.20 C ANISOU 1108 CA GLU A 136 5625 2618 5511 175 1434 -945 C ATOM 1109 C GLU A 136 10.488 -7.200 -1.136 1.00 33.63 C ANISOU 1109 C GLU A 136 4980 2397 5400 260 1394 -776 C ATOM 1110 O GLU A 136 11.288 -6.255 -1.318 1.00 32.24 O ANISOU 1110 O GLU A 136 4602 2326 5321 497 1398 -630 O ATOM 1111 CB GLU A 136 8.902 -7.993 -2.917 1.00 37.05 C ANISOU 1111 CB GLU A 136 5589 3003 5486 -100 1328 -1097 C ATOM 1112 CG GLU A 136 8.712 -8.762 -4.257 1.00 39.61 C ANISOU 1112 CG GLU A 136 6169 3302 5578 -165 1346 -1269 C ATOM 1113 CD GLU A 136 8.562 -10.297 -4.105 1.00 43.06 C ANISOU 1113 CD GLU A 136 7100 3393 5870 -400 1409 -1427 C ATOM 1114 OE1 GLU A 136 8.148 -10.753 -3.008 1.00 42.70 O ANISOU 1114 OE1 GLU A 136 7155 3208 5860 -653 1411 -1431 O ATOM 1115 OE2 GLU A 136 8.843 -11.036 -5.097 1.00 44.62 O ANISOU 1115 OE2 GLU A 136 7616 3445 5893 -340 1453 -1548 O ATOM 1116 N GLN A 137 9.831 -7.376 0.006 1.00 33.50 N ANISOU 1116 N GLN A 137 4941 2354 5435 40 1362 -797 N ATOM 1117 CA GLN A 137 10.016 -6.427 1.130 1.00 31.37 C ANISOU 1117 CA GLN A 137 4397 2174 5350 118 1320 -661 C ATOM 1118 C GLN A 137 11.435 -6.460 1.619 1.00 30.93 C ANISOU 1118 C GLN A 137 4398 1948 5405 396 1397 -505 C ATOM 1119 O GLN A 137 12.038 -5.422 1.896 1.00 28.83 O ANISOU 1119 O GLN A 137 3891 1795 5268 552 1371 -374 O ATOM 1120 CB GLN A 137 9.093 -6.754 2.286 1.00 31.48 C ANISOU 1120 CB GLN A 137 4394 2211 5358 -169 1292 -723 C ATOM 1121 CG GLN A 137 7.644 -6.673 1.938 1.00 34.21 C ANISOU 1121 CG GLN A 137 4588 2846 5565 -461 1213 -892 C ATOM 1122 CD GLN A 137 6.773 -7.279 3.028 1.00 39.49 C ANISOU 1122 CD GLN A 137 5280 3559 6164 -823 1222 -968 C ATOM 1123 OE1 GLN A 137 7.226 -8.132 3.777 1.00 40.89 O ANISOU 1123 OE1 GLN A 137 5751 3437 6346 -902 1303 -911 O ATOM 1124 NE2 GLN A 137 5.520 -6.854 3.101 1.00 40.81 N ANISOU 1124 NE2 GLN A 137 5143 4129 6233 -1034 1140 -1097 N ATOM 1125 N LEU A 138 12.003 -7.666 1.684 1.00 32.41 N ANISOU 1125 N LEU A 138 4930 1872 5514 469 1485 -526 N ATOM 1126 CA LEU A 138 13.334 -7.807 2.204 1.00 31.91 C ANISOU 1126 CA LEU A 138 4902 1708 5514 778 1549 -396 C ATOM 1127 C LEU A 138 14.389 -7.207 1.255 1.00 31.74 C ANISOU 1127 C LEU A 138 4705 1863 5491 1059 1593 -323 C ATOM 1128 O LEU A 138 15.449 -6.696 1.693 1.00 31.10 O ANISOU 1128 O LEU A 138 4428 1896 5493 1263 1618 -190 O ATOM 1129 CB LEU A 138 13.570 -9.295 2.548 1.00 34.87 C ANISOU 1129 CB LEU A 138 5752 1734 5762 832 1613 -448 C ATOM 1130 CG LEU A 138 14.795 -9.845 3.281 1.00 35.70 C ANISOU 1130 CG LEU A 138 6013 1686 5865 1188 1665 -344 C ATOM 1131 CD1 LEU A 138 14.950 -9.373 4.734 1.00 36.55 C ANISOU 1131 CD1 LEU A 138 5926 1849 6110 1166 1623 -214 C ATOM 1132 CD2 LEU A 138 14.785 -11.396 3.227 1.00 39.83 C ANISOU 1132 CD2 LEU A 138 7151 1791 6191 1244 1710 -436 C ATOM 1133 N GLY A 139 14.133 -7.255 -0.045 1.00 32.64 N ANISOU 1133 N GLY A 139 4872 2043 5486 1046 1607 -409 N ATOM 1134 CA GLY A 139 15.048 -6.629 -1.000 1.00 32.78 C ANISOU 1134 CA GLY A 139 4713 2274 5468 1256 1658 -332 C ATOM 1135 C GLY A 139 15.097 -5.088 -0.875 1.00 30.85 C ANISOU 1135 C GLY A 139 4113 2257 5352 1180 1591 -189 C ATOM 1136 O GLY A 139 16.173 -4.493 -0.954 1.00 30.86 O ANISOU 1136 O GLY A 139 3934 2418 5375 1313 1640 -59 O ATOM 1137 N GLU A 140 13.941 -4.461 -0.673 1.00 29.70 N ANISOU 1137 N GLU A 140 3886 2137 5263 966 1476 -221 N ATOM 1138 CA GLU A 140 13.855 -3.002 -0.442 1.00 28.31 C ANISOU 1138 CA GLU A 140 3470 2095 5192 920 1385 -103 C ATOM 1139 C GLU A 140 14.674 -2.633 0.790 1.00 27.33 C ANISOU 1139 C GLU A 140 3219 1950 5216 965 1395 15 C ATOM 1140 O GLU A 140 15.420 -1.706 0.744 1.00 27.16 O ANISOU 1140 O GLU A 140 3056 2030 5232 988 1393 145 O ATOM 1141 CB GLU A 140 12.376 -2.542 -0.273 1.00 27.78 C ANISOU 1141 CB GLU A 140 3349 2076 5130 761 1248 -198 C ATOM 1142 CG GLU A 140 11.470 -3.042 -1.421 1.00 31.16 C ANISOU 1142 CG GLU A 140 3879 2580 5382 687 1225 -346 C ATOM 1143 CD GLU A 140 10.020 -2.682 -1.210 1.00 39.70 C ANISOU 1143 CD GLU A 140 4844 3812 6426 551 1089 -463 C ATOM 1144 OE1 GLU A 140 9.770 -1.591 -0.695 1.00 37.19 O ANISOU 1144 OE1 GLU A 140 4370 3570 6190 610 991 -399 O ATOM 1145 OE2 GLU A 140 9.122 -3.512 -1.557 1.00 46.54 O ANISOU 1145 OE2 GLU A 140 5780 4746 7159 383 1078 -636 O ATOM 1146 N PHE A 141 14.574 -3.418 1.868 1.00 27.10 N ANISOU 1146 N PHE A 141 3265 1791 5239 954 1408 -29 N ATOM 1147 CA PHE A 141 15.410 -3.212 3.039 1.00 26.50 C ANISOU 1147 CA PHE A 141 3077 1719 5272 1023 1416 73 C ATOM 1148 C PHE A 141 16.898 -3.357 2.762 1.00 27.61 C ANISOU 1148 C PHE A 141 3145 1979 5366 1231 1515 166 C ATOM 1149 O PHE A 141 17.662 -2.562 3.242 1.00 27.31 O ANISOU 1149 O PHE A 141 2901 2082 5394 1229 1501 275 O ATOM 1150 CB PHE A 141 15.035 -4.150 4.202 1.00 26.51 C ANISOU 1150 CB PHE A 141 3222 1555 5295 989 1417 19 C ATOM 1151 CG PHE A 141 15.849 -3.904 5.464 1.00 26.38 C ANISOU 1151 CG PHE A 141 3079 1571 5372 1072 1407 122 C ATOM 1152 CD1 PHE A 141 16.557 -4.949 6.076 1.00 27.20 C ANISOU 1152 CD1 PHE A 141 3335 1576 5425 1254 1467 145 C ATOM 1153 CD2 PHE A 141 15.935 -2.605 6.023 1.00 24.75 C ANISOU 1153 CD2 PHE A 141 2633 1490 5281 991 1326 192 C ATOM 1154 CE1 PHE A 141 17.313 -4.739 7.237 1.00 27.03 C ANISOU 1154 CE1 PHE A 141 3179 1630 5462 1350 1445 236 C ATOM 1155 CE2 PHE A 141 16.716 -2.390 7.174 1.00 24.57 C ANISOU 1155 CE2 PHE A 141 2489 1525 5324 1047 1310 270 C ATOM 1156 CZ PHE A 141 17.386 -3.477 7.783 1.00 25.65 C ANISOU 1156 CZ PHE A 141 2730 1612 5405 1226 1370 292 C ATOM 1157 N TYR A 142 17.304 -4.394 2.022 1.00 29.29 N ANISOU 1157 N TYR A 142 3526 2161 5442 1410 1611 107 N ATOM 1158 CA TYR A 142 18.714 -4.618 1.661 1.00 31.00 C ANISOU 1158 CA TYR A 142 3638 2579 5562 1671 1715 165 C ATOM 1159 C TYR A 142 19.241 -3.506 0.796 1.00 31.20 C ANISOU 1159 C TYR A 142 3422 2881 5553 1585 1740 262 C ATOM 1160 O TYR A 142 20.382 -3.111 0.932 1.00 32.17 O ANISOU 1160 O TYR A 142 3307 3272 5646 1653 1791 357 O ATOM 1161 CB TYR A 142 18.926 -5.928 0.851 1.00 33.26 C ANISOU 1161 CB TYR A 142 4201 2771 5665 1924 1809 48 C ATOM 1162 CG TYR A 142 18.880 -7.204 1.650 1.00 34.38 C ANISOU 1162 CG TYR A 142 4663 2631 5769 2096 1814 -21 C ATOM 1163 CD1 TYR A 142 18.855 -8.448 1.004 1.00 36.76 C ANISOU 1163 CD1 TYR A 142 5351 2724 5894 2296 1872 -153 C ATOM 1164 CD2 TYR A 142 18.856 -7.186 3.046 1.00 33.46 C ANISOU 1164 CD2 TYR A 142 4521 2427 5765 2058 1754 44 C ATOM 1165 CE1 TYR A 142 18.826 -9.643 1.736 1.00 38.42 C ANISOU 1165 CE1 TYR A 142 5961 2601 6036 2453 1868 -203 C ATOM 1166 CE2 TYR A 142 18.810 -8.393 3.796 1.00 34.95 C ANISOU 1166 CE2 TYR A 142 5075 2319 5885 2211 1756 4 C ATOM 1167 CZ TYR A 142 18.795 -9.613 3.126 1.00 37.52 C ANISOU 1167 CZ TYR A 142 5830 2398 6029 2404 1811 -113 C ATOM 1168 OH TYR A 142 18.735 -10.809 3.836 1.00 39.57 O ANISOU 1168 OH TYR A 142 6553 2292 6189 2542 1803 -141 O ATOM 1169 N GLU A 143 18.395 -3.049 -0.123 1.00 31.68 N ANISOU 1169 N GLU A 143 3556 2896 5586 1426 1701 234 N ATOM 1170 CA GLU A 143 18.742 -1.978 -1.015 1.00 33.14 C ANISOU 1170 CA GLU A 143 3601 3284 5709 1313 1714 342 C ATOM 1171 C GLU A 143 18.974 -0.717 -0.210 1.00 31.59 C ANISOU 1171 C GLU A 143 3235 3130 5639 1120 1634 476 C ATOM 1172 O GLU A 143 19.813 0.086 -0.588 1.00 32.41 O ANISOU 1172 O GLU A 143 3192 3444 5677 1016 1675 602 O ATOM 1173 CB GLU A 143 17.677 -1.787 -2.101 1.00 34.28 C ANISOU 1173 CB GLU A 143 3900 3350 5775 1221 1662 282 C ATOM 1174 CG GLU A 143 17.814 -2.804 -3.228 1.00 39.61 C ANISOU 1174 CG GLU A 143 4715 4074 6261 1385 1766 172 C ATOM 1175 CD GLU A 143 16.772 -2.680 -4.366 1.00 47.03 C ANISOU 1175 CD GLU A 143 5797 4984 7088 1295 1708 97 C ATOM 1176 OE1 GLU A 143 15.589 -2.371 -4.098 1.00 47.93 O ANISOU 1176 OE1 GLU A 143 5960 4977 7274 1158 1577 46 O ATOM 1177 OE2 GLU A 143 17.142 -2.963 -5.541 1.00 52.29 O ANISOU 1177 OE2 GLU A 143 6511 5792 7564 1388 1796 71 O ATOM 1178 N ALA A 144 18.263 -0.554 0.909 1.00 29.29 N ANISOU 1178 N ALA A 144 2975 2652 5502 1050 1525 443 N ATOM 1179 CA ALA A 144 18.520 0.611 1.802 1.00 28.85 C ANISOU 1179 CA ALA A 144 2793 2609 5558 885 1440 544 C ATOM 1180 C ALA A 144 19.830 0.476 2.612 1.00 29.46 C ANISOU 1180 C ALA A 144 2659 2887 5647 928 1502 609 C ATOM 1181 O ALA A 144 20.504 1.447 2.848 1.00 29.51 O ANISOU 1181 O ALA A 144 2527 3026 5658 752 1482 713 O ATOM 1182 CB ALA A 144 17.322 0.932 2.711 1.00 26.28 C ANISOU 1182 CB ALA A 144 2550 2072 5363 821 1301 473 C ATOM 1183 N LEU A 145 20.163 -0.751 3.018 1.00 30.69 N ANISOU 1183 N LEU A 145 2817 3064 5779 1164 1569 541 N ATOM 1184 CA LEU A 145 21.482 -1.061 3.569 1.00 31.64 C ANISOU 1184 CA LEU A 145 2718 3459 5844 1309 1635 588 C ATOM 1185 C LEU A 145 22.586 -0.793 2.574 1.00 34.57 C ANISOU 1185 C LEU A 145 2882 4204 6047 1315 1748 656 C ATOM 1186 O LEU A 145 23.565 -0.133 2.927 1.00 36.44 O ANISOU 1186 O LEU A 145 2845 4751 6248 1187 1761 743 O ATOM 1187 CB LEU A 145 21.558 -2.518 4.057 1.00 32.50 C ANISOU 1187 CB LEU A 145 2965 3472 5914 1640 1674 500 C ATOM 1188 CG LEU A 145 20.625 -2.906 5.214 1.00 30.18 C ANISOU 1188 CG LEU A 145 2860 2864 5745 1607 1583 451 C ATOM 1189 CD1 LEU A 145 20.619 -4.404 5.365 1.00 32.08 C ANISOU 1189 CD1 LEU A 145 3366 2931 5890 1898 1633 375 C ATOM 1190 CD2 LEU A 145 21.039 -2.228 6.518 1.00 31.04 C ANISOU 1190 CD2 LEU A 145 2764 3081 5948 1513 1505 519 C ATOM 1191 N ASP A 146 22.445 -1.305 1.347 1.00 35.06 N ANISOU 1191 N ASP A 146 3061 4279 5982 1436 1834 608 N ATOM 1192 CA ASP A 146 23.409 -1.052 0.293 1.00 38.09 C ANISOU 1192 CA ASP A 146 3248 5054 6170 1430 1957 667 C ATOM 1193 C ASP A 146 23.731 0.434 0.247 1.00 38.19 C ANISOU 1193 C ASP A 146 3107 5213 6191 1015 1923 819 C ATOM 1194 O ASP A 146 24.888 0.814 0.133 1.00 39.15 O ANISOU 1194 O ASP A 146 2934 5764 6177 912 2006 898 O ATOM 1195 CB ASP A 146 22.900 -1.545 -1.087 1.00 39.65 C ANISOU 1195 CB ASP A 146 3652 5174 6239 1533 2024 595 C ATOM 1196 CG ASP A 146 22.693 -3.092 -1.151 1.00 41.87 C ANISOU 1196 CG ASP A 146 4157 5291 6460 1929 2067 427 C ATOM 1197 OD1 ASP A 146 22.118 -3.558 -2.153 1.00 44.32 O ANISOU 1197 OD1 ASP A 146 4688 5476 6677 1989 2097 338 O ATOM 1198 OD2 ASP A 146 23.048 -3.838 -0.208 1.00 43.99 O ANISOU 1198 OD2 ASP A 146 4434 5522 6758 2169 2058 383 O ATOM 1199 N CYS A 147 22.703 1.269 0.378 1.00 36.20 N ANISOU 1199 N CYS A 147 3069 4611 6075 778 1795 852 N ATOM 1200 CA CYS A 147 22.867 2.727 0.346 1.00 38.11 C ANISOU 1200 CA CYS A 147 3306 4861 6314 388 1735 995 C ATOM 1201 C CYS A 147 23.739 3.261 1.458 1.00 37.92 C ANISOU 1201 C CYS A 147 3053 5023 6332 204 1705 1050 C ATOM 1202 O CYS A 147 24.419 4.287 1.279 1.00 39.40 O ANISOU 1202 O CYS A 147 3159 5389 6424 -154 1717 1174 O ATOM 1203 CB CYS A 147 21.491 3.410 0.449 1.00 36.92 C ANISOU 1203 CB CYS A 147 3469 4265 6295 295 1573 983 C ATOM 1204 SG CYS A 147 20.504 3.116 -1.018 1.00 41.62 S ANISOU 1204 SG CYS A 147 4305 4725 6783 417 1583 941 S ATOM 1205 N LEU A 148 23.698 2.580 2.612 1.00 34.98 N ANISOU 1205 N LEU A 148 2606 4604 6082 414 1662 960 N ATOM 1206 CA LEU A 148 24.471 3.036 3.770 1.00 35.74 C ANISOU 1206 CA LEU A 148 2477 4891 6213 262 1614 992 C ATOM 1207 C LEU A 148 25.802 2.321 3.815 1.00 38.26 C ANISOU 1207 C LEU A 148 2421 5747 6368 448 1736 985 C ATOM 1208 O LEU A 148 26.581 2.485 4.756 1.00 39.40 O ANISOU 1208 O LEU A 148 2307 6165 6498 387 1707 994 O ATOM 1209 CB LEU A 148 23.687 2.845 5.073 1.00 33.28 C ANISOU 1209 CB LEU A 148 2290 4261 6095 368 1484 912 C ATOM 1210 CG LEU A 148 22.458 3.774 5.294 1.00 31.41 C ANISOU 1210 CG LEU A 148 2353 3586 5995 185 1338 902 C ATOM 1211 CD1 LEU A 148 21.949 3.591 6.680 1.00 29.71 C ANISOU 1211 CD1 LEU A 148 2163 3204 5922 273 1235 821 C ATOM 1212 CD2 LEU A 148 22.847 5.257 5.057 1.00 33.16 C ANISOU 1212 CD2 LEU A 148 2629 3810 6161 -224 1285 1015 C ATOM 1213 N ARG A 149 26.026 1.505 2.790 1.00 39.38 N ANISOU 1213 N ARG A 149 2536 6059 6367 711 1866 951 N ATOM 1214 CA ARG A 149 27.224 0.631 2.664 1.00 42.25 C ANISOU 1214 CA ARG A 149 2565 6960 6530 1038 1992 909 C ATOM 1215 C ARG A 149 27.383 -0.317 3.876 1.00 41.85 C ANISOU 1215 C ARG A 149 2474 6890 6538 1429 1934 825 C ATOM 1216 O ARG A 149 28.464 -0.494 4.416 1.00 44.29 O ANISOU 1216 O ARG A 149 2430 7677 6719 1565 1957 822 O ATOM 1217 CB ARG A 149 28.464 1.484 2.412 1.00 45.68 C ANISOU 1217 CB ARG A 149 2589 7999 6767 699 2069 1006 C ATOM 1218 CG ARG A 149 28.271 2.484 1.243 1.00 48.64 C ANISOU 1218 CG ARG A 149 3089 8334 7061 260 2120 1121 C ATOM 1219 CD ARG A 149 29.482 3.401 1.006 1.00 58.33 C ANISOU 1219 CD ARG A 149 3945 10155 8061 -203 2204 1236 C ATOM 1220 NE ARG A 149 29.922 4.169 2.186 1.00 63.50 N ANISOU 1220 NE ARG A 149 4442 10907 8778 -551 2098 1271 N ATOM 1221 CZ ARG A 149 29.568 5.428 2.472 1.00 64.01 C ANISOU 1221 CZ ARG A 149 4751 10641 8929 -1080 1987 1368 C ATOM 1222 NH1 ARG A 149 28.741 6.098 1.677 1.00 63.78 N ANISOU 1222 NH1 ARG A 149 5146 10153 8936 -1295 1958 1455 N ATOM 1223 NH2 ARG A 149 30.048 6.029 3.562 1.00 63.18 N ANISOU 1223 NH2 ARG A 149 4493 10661 8850 -1376 1893 1371 N ATOM 1224 N ILE A 150 26.261 -0.874 4.309 1.00 39.05 N ANISOU 1224 N ILE A 150 2487 5996 6355 1578 1853 762 N ATOM 1225 CA ILE A 150 26.211 -1.872 5.381 1.00 38.71 C ANISOU 1225 CA ILE A 150 2536 5820 6352 1938 1800 698 C ATOM 1226 C ILE A 150 25.959 -3.247 4.732 1.00 39.43 C ANISOU 1226 C ILE A 150 2911 5728 6343 2382 1875 598 C ATOM 1227 O ILE A 150 24.874 -3.469 4.163 1.00 37.65 O ANISOU 1227 O ILE A 150 3026 5087 6193 2306 1869 551 O ATOM 1228 CB ILE A 150 25.096 -1.586 6.407 1.00 35.60 C ANISOU 1228 CB ILE A 150 2387 4956 6184 1749 1663 695 C ATOM 1229 CG1 ILE A 150 25.287 -0.211 7.091 1.00 35.14 C ANISOU 1229 CG1 ILE A 150 2127 5010 6214 1330 1572 768 C ATOM 1230 CG2 ILE A 150 25.033 -2.704 7.437 1.00 35.67 C ANISOU 1230 CG2 ILE A 150 2544 4816 6193 2104 1623 647 C ATOM 1231 CD1 ILE A 150 24.112 0.238 8.005 1.00 32.30 C ANISOU 1231 CD1 ILE A 150 2003 4214 6056 1146 1438 745 C ATOM 1232 N PRO A 151 26.948 -4.163 4.807 1.00 42.45 N ANISOU 1232 N PRO A 151 3170 6428 6530 2855 1935 553 N ATOM 1233 CA PRO A 151 26.767 -5.444 4.120 1.00 43.79 C ANISOU 1233 CA PRO A 151 3679 6389 6570 3293 2003 443 C ATOM 1234 C PRO A 151 25.531 -6.190 4.630 1.00 41.65 C ANISOU 1234 C PRO A 151 3938 5451 6436 3306 1924 394 C ATOM 1235 O PRO A 151 25.180 -6.110 5.835 1.00 40.18 O ANISOU 1235 O PRO A 151 3814 5073 6381 3206 1824 438 O ATOM 1236 CB PRO A 151 28.076 -6.204 4.427 1.00 47.77 C ANISOU 1236 CB PRO A 151 3961 7357 6834 3855 2043 406 C ATOM 1237 CG PRO A 151 29.102 -5.124 4.709 1.00 49.02 C ANISOU 1237 CG PRO A 151 3507 8176 6940 3609 2051 492 C ATOM 1238 CD PRO A 151 28.238 -4.120 5.522 1.00 45.20 C ANISOU 1238 CD PRO A 151 3095 7339 6740 3050 1931 580 C ATOM 1239 N ARG A 152 24.849 -6.874 3.714 1.00 41.71 N ANISOU 1239 N ARG A 152 4317 5134 6395 3378 1971 299 N ATOM 1240 CA ARG A 152 23.677 -7.684 4.104 1.00 40.45 C ANISOU 1240 CA ARG A 152 4678 4378 6315 3335 1910 237 C ATOM 1241 C ARG A 152 23.984 -8.740 5.159 1.00 42.27 C ANISOU 1241 C ARG A 152 5176 4420 6465 3712 1867 232 C ATOM 1242 O ARG A 152 23.082 -9.130 5.893 1.00 41.06 O ANISOU 1242 O ARG A 152 5362 3840 6398 3549 1801 234 O ATOM 1243 CB ARG A 152 23.054 -8.365 2.889 1.00 41.18 C ANISOU 1243 CB ARG A 152 5132 4206 6308 3371 1970 112 C ATOM 1244 CG ARG A 152 22.373 -7.399 1.909 1.00 39.12 C ANISOU 1244 CG ARG A 152 4729 4004 6131 2958 1980 118 C ATOM 1245 CD ARG A 152 22.346 -8.088 0.534 1.00 41.14 C ANISOU 1245 CD ARG A 152 5212 4224 6196 3143 2069 -10 C ATOM 1246 NE ARG A 152 21.938 -7.151 -0.484 1.00 42.36 N ANISOU 1246 NE ARG A 152 5192 4528 6374 2827 2086 15 N ATOM 1247 CZ ARG A 152 21.550 -7.479 -1.706 1.00 45.74 C ANISOU 1247 CZ ARG A 152 5807 4899 6673 2834 2134 -89 C ATOM 1248 NH1 ARG A 152 21.464 -8.753 -2.073 1.00 47.20 N ANISOU 1248 NH1 ARG A 152 6393 4839 6700 3117 2171 -246 N ATOM 1249 NH2 ARG A 152 21.209 -6.516 -2.553 1.00 45.59 N ANISOU 1249 NH2 ARG A 152 5618 5038 6665 2552 2134 -36 N ATOM 1250 N SER A 153 25.239 -9.218 5.217 1.00 45.59 N ANISOU 1250 N SER A 153 5452 5184 6688 4226 1905 225 N ATOM 1251 CA SER A 153 25.603 -10.240 6.204 1.00 47.96 C ANISOU 1251 CA SER A 153 6046 5308 6868 4671 1848 231 C ATOM 1252 C SER A 153 25.656 -9.721 7.649 1.00 46.48 C ANISOU 1252 C SER A 153 5653 5200 6808 4510 1745 351 C ATOM 1253 O SER A 153 25.709 -10.509 8.597 1.00 47.98 O ANISOU 1253 O SER A 153 6152 5157 6919 4785 1680 381 O ATOM 1254 CB SER A 153 26.921 -10.945 5.835 1.00 52.58 C ANISOU 1254 CB SER A 153 6542 6277 7160 5369 1903 169 C ATOM 1255 OG SER A 153 27.955 -10.015 5.541 1.00 53.26 O ANISOU 1255 OG SER A 153 5930 7108 7198 5359 1955 203 O ATOM 1256 N ASP A 154 25.658 -8.398 7.813 1.00 43.93 N ANISOU 1256 N ASP A 154 4848 5187 6655 4072 1726 419 N ATOM 1257 CA ASP A 154 25.638 -7.779 9.152 1.00 42.42 C ANISOU 1257 CA ASP A 154 4459 5071 6589 3862 1623 511 C ATOM 1258 C ASP A 154 24.264 -7.733 9.798 1.00 39.47 C ANISOU 1258 C ASP A 154 4417 4184 6395 3476 1559 525 C ATOM 1259 O ASP A 154 24.155 -7.398 10.980 1.00 39.17 O ANISOU 1259 O ASP A 154 4298 4154 6432 3349 1475 586 O ATOM 1260 CB ASP A 154 26.175 -6.346 9.092 1.00 41.38 C ANISOU 1260 CB ASP A 154 3744 5435 6543 3515 1618 562 C ATOM 1261 CG ASP A 154 27.681 -6.272 9.131 1.00 44.77 C ANISOU 1261 CG ASP A 154 3709 6530 6773 3834 1643 575 C ATOM 1262 OD1 ASP A 154 28.342 -7.312 9.327 1.00 48.47 O ANISOU 1262 OD1 ASP A 154 4276 7104 7037 4406 1646 544 O ATOM 1263 OD2 ASP A 154 28.200 -5.146 8.950 1.00 44.67 O ANISOU 1263 OD2 ASP A 154 3238 6951 6785 3500 1655 613 O ATOM 1264 N VAL A 155 23.216 -8.011 9.018 1.00 38.42 N ANISOU 1264 N VAL A 155 4612 3674 6312 3269 1599 456 N ATOM 1265 CA VAL A 155 21.822 -7.937 9.486 1.00 35.83 C ANISOU 1265 CA VAL A 155 4536 2954 6122 2862 1551 445 C ATOM 1266 C VAL A 155 21.487 -8.969 10.555 1.00 37.75 C ANISOU 1266 C VAL A 155 5205 2853 6286 2976 1511 473 C ATOM 1267 O VAL A 155 21.718 -10.170 10.383 1.00 40.23 O ANISOU 1267 O VAL A 155 5944 2918 6422 3310 1541 449 O ATOM 1268 CB VAL A 155 20.810 -8.010 8.284 1.00 34.84 C ANISOU 1268 CB VAL A 155 4614 2598 6024 2613 1600 347 C ATOM 1269 CG1 VAL A 155 19.373 -7.950 8.713 1.00 32.95 C ANISOU 1269 CG1 VAL A 155 4566 2071 5884 2202 1553 313 C ATOM 1270 CG2 VAL A 155 21.079 -6.919 7.277 1.00 33.74 C ANISOU 1270 CG2 VAL A 155 4096 2776 5946 2476 1630 347 C ATOM 1271 N MET A 156 20.965 -8.475 11.672 1.00 36.85 N ANISOU 1271 N MET A 156 5003 2721 6279 2706 1442 526 N ATOM 1272 CA MET A 156 20.432 -9.291 12.761 1.00 38.69 C ANISOU 1272 CA MET A 156 5628 2634 6438 2678 1407 569 C ATOM 1273 C MET A 156 18.943 -9.475 12.507 1.00 36.62 C ANISOU 1273 C MET A 156 5635 2058 6220 2228 1431 496 C ATOM 1274 O MET A 156 18.251 -8.491 12.231 1.00 33.09 O ANISOU 1274 O MET A 156 4893 1756 5923 1892 1417 446 O ATOM 1275 CB MET A 156 20.589 -8.503 14.078 1.00 38.90 C ANISOU 1275 CB MET A 156 5341 2894 6547 2571 1325 646 C ATOM 1276 CG MET A 156 22.046 -8.538 14.672 1.00 43.07 C ANISOU 1276 CG MET A 156 5642 3754 6969 3017 1279 725 C ATOM 1277 SD MET A 156 22.207 -7.154 15.847 1.00 42.55 S ANISOU 1277 SD MET A 156 5068 4059 7042 2755 1180 764 S ATOM 1278 CE MET A 156 21.815 -5.751 14.788 1.00 39.04 C ANISOU 1278 CE MET A 156 4262 3770 6802 2356 1204 685 C ATOM 1279 N TYR A 157 18.434 -10.694 12.641 1.00 37.27 N ANISOU 1279 N TYR A 157 6279 1732 6149 2207 1457 488 N ATOM 1280 CA TYR A 157 17.014 -10.950 12.371 1.00 36.81 C ANISOU 1280 CA TYR A 157 6461 1439 6088 1723 1485 404 C ATOM 1281 C TYR A 157 16.241 -11.416 13.596 1.00 37.66 C ANISOU 1281 C TYR A 157 6840 1357 6113 1432 1469 462 C ATOM 1282 O TYR A 157 16.803 -12.089 14.468 1.00 39.79 O ANISOU 1282 O TYR A 157 7403 1463 6254 1673 1449 573 O ATOM 1283 CB TYR A 157 16.846 -12.033 11.298 1.00 39.28 C ANISOU 1283 CB TYR A 157 7270 1408 6247 1777 1543 313 C ATOM 1284 CG TYR A 157 17.450 -11.680 9.977 1.00 38.82 C ANISOU 1284 CG TYR A 157 6988 1535 6228 2017 1576 238 C ATOM 1285 CD1 TYR A 157 18.801 -11.959 9.713 1.00 42.72 C ANISOU 1285 CD1 TYR A 157 7468 2126 6636 2577 1592 271 C ATOM 1286 CD2 TYR A 157 16.680 -11.128 8.959 1.00 37.13 C ANISOU 1286 CD2 TYR A 157 6584 1429 6094 1711 1594 128 C ATOM 1287 CE1 TYR A 157 19.374 -11.644 8.465 1.00 42.01 C ANISOU 1287 CE1 TYR A 157 7152 2264 6547 2780 1640 201 C ATOM 1288 CE2 TYR A 157 17.234 -10.800 7.729 1.00 36.95 C ANISOU 1288 CE2 TYR A 157 6375 1585 6079 1915 1630 73 C ATOM 1289 CZ TYR A 157 18.582 -11.038 7.485 1.00 38.62 C ANISOU 1289 CZ TYR A 157 6549 1913 6211 2426 1662 111 C ATOM 1290 OH TYR A 157 19.146 -10.744 6.254 1.00 38.86 O ANISOU 1290 OH TYR A 157 6385 2168 6212 2612 1715 56 O ATOM 1291 N THR A 158 14.943 -11.118 13.636 1.00 36.50 N ANISOU 1291 N THR A 158 6615 1253 6002 926 1480 385 N ATOM 1292 CA THR A 158 14.075 -11.852 14.539 1.00 38.36 C ANISOU 1292 CA THR A 158 7216 1277 6084 567 1499 419 C ATOM 1293 C THR A 158 13.767 -13.317 14.001 1.00 42.11 C ANISOU 1293 C THR A 158 8417 1254 6330 448 1555 389 C ATOM 1294 O THR A 158 13.833 -13.586 12.812 1.00 42.63 O ANISOU 1294 O THR A 158 8606 1208 6382 521 1579 287 O ATOM 1295 CB THR A 158 12.789 -11.118 14.756 1.00 36.66 C ANISOU 1295 CB THR A 158 6654 1344 5929 75 1498 327 C ATOM 1296 OG1 THR A 158 12.235 -10.810 13.485 1.00 35.74 O ANISOU 1296 OG1 THR A 158 6382 1328 5870 -69 1510 181 O ATOM 1297 CG2 THR A 158 13.018 -9.814 15.572 1.00 33.88 C ANISOU 1297 CG2 THR A 158 5744 1382 5746 178 1433 359 C ATOM 1298 N ASP A 159 13.426 -14.225 14.912 1.00 44.99 N ANISOU 1298 N ASP A 159 9284 1315 6494 243 1571 480 N ATOM 1299 CA ASP A 159 12.952 -15.571 14.572 1.00 49.08 C ANISOU 1299 CA ASP A 159 10565 1321 6763 -10 1618 454 C ATOM 1300 C ASP A 159 11.526 -15.567 15.130 1.00 49.61 C ANISOU 1300 C ASP A 159 10598 1514 6739 -753 1660 419 C ATOM 1301 O ASP A 159 11.316 -15.697 16.349 1.00 50.61 O ANISOU 1301 O ASP A 159 10819 1645 6766 -928 1665 544 O ATOM 1302 CB ASP A 159 13.862 -16.592 15.276 1.00 52.67 C ANISOU 1302 CB ASP A 159 11669 1323 7018 406 1594 620 C ATOM 1303 CG ASP A 159 13.724 -18.052 14.745 1.00 57.65 C ANISOU 1303 CG ASP A 159 13240 1294 7370 337 1622 592 C ATOM 1304 OD1 ASP A 159 14.214 -18.957 15.455 1.00 61.35 O ANISOU 1304 OD1 ASP A 159 14358 1331 7620 584 1596 739 O ATOM 1305 OD2 ASP A 159 13.175 -18.312 13.651 1.00 58.27 O ANISOU 1305 OD2 ASP A 159 13458 1261 7422 69 1659 428 O ATOM 1306 N TRP A 160 10.531 -15.358 14.277 1.00 49.10 N ANISOU 1306 N TRP A 160 10335 1632 6688 -1189 1688 245 N ATOM 1307 CA TRP A 160 9.162 -15.459 14.775 1.00 50.48 C ANISOU 1307 CA TRP A 160 10466 1997 6718 -1908 1735 192 C ATOM 1308 C TRP A 160 8.883 -16.846 15.456 1.00 55.61 C ANISOU 1308 C TRP A 160 11955 2133 7040 -2292 1788 302 C ATOM 1309 O TRP A 160 7.943 -16.961 16.253 1.00 57.23 O ANISOU 1309 O TRP A 160 12145 2514 7086 -2867 1837 323 O ATOM 1310 CB TRP A 160 8.126 -15.133 13.682 1.00 49.97 C ANISOU 1310 CB TRP A 160 10081 2241 6664 -2307 1745 -29 C ATOM 1311 CG TRP A 160 6.687 -15.216 14.176 1.00 55.47 C ANISOU 1311 CG TRP A 160 10639 3264 7172 -3056 1794 -110 C ATOM 1312 CD1 TRP A 160 5.724 -16.133 13.797 1.00 63.29 C ANISOU 1312 CD1 TRP A 160 12016 4138 7891 -3719 1849 -215 C ATOM 1313 CD2 TRP A 160 6.075 -14.386 15.173 1.00 57.38 C ANISOU 1313 CD2 TRP A 160 10323 4037 7442 -3231 1798 -101 C ATOM 1314 NE1 TRP A 160 4.550 -15.904 14.493 1.00 65.22 N ANISOU 1314 NE1 TRP A 160 11916 4876 7989 -4311 1893 -268 N ATOM 1315 CE2 TRP A 160 4.737 -14.836 15.336 1.00 61.69 C ANISOU 1315 CE2 TRP A 160 10885 4833 7720 -3990 1864 -204 C ATOM 1316 CE3 TRP A 160 6.522 -13.288 15.934 1.00 56.53 C ANISOU 1316 CE3 TRP A 160 9699 4243 7539 -2829 1750 -32 C ATOM 1317 CZ2 TRP A 160 3.845 -14.230 16.235 1.00 61.78 C ANISOU 1317 CZ2 TRP A 160 10382 5437 7656 -4306 1891 -243 C ATOM 1318 CZ3 TRP A 160 5.631 -12.687 16.835 1.00 56.76 C ANISOU 1318 CZ3 TRP A 160 9275 4791 7502 -3131 1767 -76 C ATOM 1319 CH2 TRP A 160 4.311 -13.168 16.975 1.00 60.50 C ANISOU 1319 CH2 TRP A 160 9747 5540 7700 -3838 1841 -181 C ATOM 1320 N LYS A 161 9.697 -17.875 15.170 1.00 59.32 N ANISOU 1320 N LYS A 161 13171 1984 7384 -1966 1777 375 N ATOM 1321 CA LYS A 161 9.569 -19.183 15.902 1.00 66.08 C ANISOU 1321 CA LYS A 161 14946 2255 7906 -2253 1809 517 C ATOM 1322 C LYS A 161 9.781 -18.995 17.411 1.00 66.56 C ANISOU 1322 C LYS A 161 14943 2423 7925 -2189 1803 728 C ATOM 1323 O LYS A 161 9.169 -19.694 18.227 1.00 70.25 O ANISOU 1323 O LYS A 161 15891 2682 8120 -2709 1853 836 O ATOM 1324 CB LYS A 161 10.573 -20.239 15.412 1.00 69.44 C ANISOU 1324 CB LYS A 161 16209 1979 8196 -1724 1773 564 C ATOM 1325 CG LYS A 161 10.242 -20.949 14.107 1.00 72.48 C ANISOU 1325 CG LYS A 161 17060 2016 8464 -1933 1791 375 C ATOM 1326 CD LYS A 161 11.212 -22.128 13.817 1.00 77.32 C ANISOU 1326 CD LYS A 161 18650 1860 8870 -1381 1751 428 C ATOM 1327 CE LYS A 161 11.168 -23.226 14.889 1.00 84.05 C ANISOU 1327 CE LYS A 161 20454 2095 9386 -1570 1750 632 C ATOM 1328 NZ LYS A 161 11.783 -24.541 14.494 1.00 88.47 N ANISOU 1328 NZ LYS A 161 22161 1797 9658 -1193 1707 642 N ATOM 1329 N LYS A 162 10.647 -18.041 17.766 1.00 63.45 N ANISOU 1329 N LYS A 162 13959 2369 7778 -1585 1742 784 N ATOM 1330 CA LYS A 162 11.085 -17.857 19.154 1.00 64.07 C ANISOU 1330 CA LYS A 162 13987 2538 7818 -1385 1712 980 C ATOM 1331 C LYS A 162 10.185 -16.960 20.034 1.00 62.13 C ANISOU 1331 C LYS A 162 13101 2882 7623 -1843 1748 962 C ATOM 1332 O LYS A 162 10.507 -16.738 21.201 1.00 62.74 O ANISOU 1332 O LYS A 162 13094 3081 7663 -1697 1723 1108 O ATOM 1333 CB LYS A 162 12.556 -17.391 19.210 1.00 61.69 C ANISOU 1333 CB LYS A 162 13439 2305 7697 -512 1619 1052 C ATOM 1334 CG LYS A 162 13.580 -18.340 18.573 1.00 65.48 C ANISOU 1334 CG LYS A 162 14566 2251 8063 71 1579 1088 C ATOM 1335 CD LYS A 162 13.833 -19.596 19.434 1.00 73.43 C ANISOU 1335 CD LYS A 162 16516 2660 8722 158 1559 1291 C ATOM 1336 CE LYS A 162 14.387 -20.759 18.593 1.00 79.08 C ANISOU 1336 CE LYS A 162 18076 2724 9245 541 1537 1266 C ATOM 1337 NZ LYS A 162 14.365 -22.070 19.329 1.00 84.49 N ANISOU 1337 NZ LYS A 162 19850 2711 9543 487 1520 1453 N ATOM 1338 N ASP A 163 9.052 -16.490 19.514 1.00 61.15 N ANISOU 1338 N ASP A 163 12549 3140 7545 -2373 1799 777 N ATOM 1339 CA ASP A 163 8.215 -15.508 20.245 1.00 59.58 C ANISOU 1339 CA ASP A 163 11655 3586 7396 -2693 1823 715 C ATOM 1340 C ASP A 163 7.531 -16.024 21.521 1.00 62.91 C ANISOU 1340 C ASP A 163 12340 4046 7517 -3219 1897 841 C ATOM 1341 O ASP A 163 6.857 -17.036 21.489 1.00 67.35 O ANISOU 1341 O ASP A 163 13461 4336 7793 -3796 1975 867 O ATOM 1342 CB ASP A 163 7.152 -14.908 19.314 1.00 58.46 C ANISOU 1342 CB ASP A 163 10987 3890 7334 -3065 1847 471 C ATOM 1343 CG ASP A 163 6.133 -14.052 20.062 1.00 57.51 C ANISOU 1343 CG ASP A 163 10225 4444 7183 -3415 1876 381 C ATOM 1344 OD1 ASP A 163 6.469 -12.910 20.430 1.00 51.78 O ANISOU 1344 OD1 ASP A 163 8934 4071 6671 -3018 1812 357 O ATOM 1345 OD2 ASP A 163 4.997 -14.535 20.290 1.00 62.47 O ANISOU 1345 OD2 ASP A 163 10927 5264 7545 -4096 1964 326 O ATOM 1346 N LYS A 164 7.672 -15.297 22.632 1.00 61.22 N ANISOU 1346 N LYS A 164 11719 4194 7347 -3062 1877 910 N ATOM 1347 CA LYS A 164 7.016 -15.688 23.893 1.00 64.00 C ANISOU 1347 CA LYS A 164 12252 4667 7397 -3555 1956 1029 C ATOM 1348 C LYS A 164 5.936 -14.716 24.399 1.00 62.81 C ANISOU 1348 C LYS A 164 11333 5293 7237 -3917 2005 872 C ATOM 1349 O LYS A 164 5.485 -14.843 25.553 1.00 65.21 O ANISOU 1349 O LYS A 164 11658 5814 7303 -4243 2070 964 O ATOM 1350 CB LYS A 164 8.053 -15.903 25.006 1.00 64.59 C ANISOU 1350 CB LYS A 164 12646 4485 7410 -3103 1898 1272 C ATOM 1351 CG LYS A 164 9.148 -16.920 24.712 1.00 67.45 C ANISOU 1351 CG LYS A 164 13804 4117 7708 -2659 1839 1441 C ATOM 1352 CD LYS A 164 8.601 -18.338 24.692 1.00 74.91 C ANISOU 1352 CD LYS A 164 15676 4505 8283 -3215 1921 1552 C ATOM 1353 CE LYS A 164 9.707 -19.375 24.732 1.00 79.25 C ANISOU 1353 CE LYS A 164 17115 4307 8690 -2695 1847 1754 C ATOM 1354 NZ LYS A 164 10.063 -19.702 26.131 1.00 83.58 N ANISOU 1354 NZ LYS A 164 18013 4745 8999 -2587 1825 2011 N ATOM 1355 N CYS A 165 5.505 -13.774 23.553 1.00 59.45 N ANISOU 1355 N CYS A 165 10259 5295 7034 -3843 1973 638 N ATOM 1356 CA CYS A 165 4.620 -12.680 23.995 1.00 58.32 C ANISOU 1356 CA CYS A 165 9345 5909 6906 -3980 1986 463 C ATOM 1357 C CYS A 165 3.161 -12.800 23.606 1.00 61.38 C ANISOU 1357 C CYS A 165 9468 6774 7081 -4648 2078 272 C ATOM 1358 O CYS A 165 2.308 -12.208 24.277 1.00 62.71 O ANISOU 1358 O CYS A 165 9119 7588 7119 -4867 2121 160 O ATOM 1359 CB CYS A 165 5.124 -11.309 23.514 1.00 53.16 C ANISOU 1359 CB CYS A 165 8083 5496 6618 -3360 1864 326 C ATOM 1360 SG CYS A 165 6.470 -10.642 24.455 1.00 49.51 S ANISOU 1360 SG CYS A 165 7552 4915 6346 -2701 1761 472 S ATOM 1361 N GLU A 166 2.859 -13.525 22.530 1.00 63.73 N ANISOU 1361 N GLU A 166 10077 6818 7320 -4956 2103 213 N ATOM 1362 CA GLU A 166 1.457 -13.792 22.171 1.00 68.11 C ANISOU 1362 CA GLU A 166 10415 7852 7609 -5685 2192 32 C ATOM 1363 C GLU A 166 0.603 -14.012 23.427 1.00 72.23 C ANISOU 1363 C GLU A 166 10837 8831 7776 -6264 2314 72 C ATOM 1364 O GLU A 166 -0.396 -13.306 23.623 1.00 72.87 O ANISOU 1364 O GLU A 166 10219 9717 7753 -6462 2345 -126 O ATOM 1365 CB GLU A 166 1.324 -15.009 21.252 1.00 71.34 C ANISOU 1365 CB GLU A 166 11485 7754 7866 -6135 2231 43 C ATOM 1366 CG GLU A 166 1.786 -14.826 19.816 1.00 70.36 C ANISOU 1366 CG GLU A 166 11356 7369 8006 -5736 2137 -71 C ATOM 1367 CD GLU A 166 2.091 -16.160 19.130 1.00 74.43 C ANISOU 1367 CD GLU A 166 12754 7142 8385 -5997 2162 2 C ATOM 1368 OE1 GLU A 166 1.749 -17.229 19.697 1.00 81.78 O ANISOU 1368 OE1 GLU A 166 14300 7790 8983 -6600 2253 120 O ATOM 1369 OE2 GLU A 166 2.680 -16.156 18.029 1.00 72.25 O ANISOU 1369 OE2 GLU A 166 12603 6542 8306 -5605 2090 -57 O ATOM 1370 N PRO A 167 1.003 -14.971 24.297 1.00 75.75 N ANISOU 1370 N PRO A 167 11980 8792 8009 -6499 2380 330 N ATOM 1371 CA PRO A 167 0.134 -15.344 25.429 1.00 80.46 C ANISOU 1371 CA PRO A 167 12572 9800 8200 -7179 2520 390 C ATOM 1372 C PRO A 167 -0.090 -14.240 26.462 1.00 79.15 C ANISOU 1372 C PRO A 167 11682 10336 8054 -6909 2520 322 C ATOM 1373 O PRO A 167 -1.064 -14.316 27.205 1.00 83.28 O ANISOU 1373 O PRO A 167 11950 11459 8235 -7482 2644 277 O ATOM 1374 CB PRO A 167 0.869 -16.533 26.058 1.00 83.12 C ANISOU 1374 CB PRO A 167 13911 9320 8352 -7303 2553 714 C ATOM 1375 CG PRO A 167 1.659 -17.109 24.937 1.00 81.94 C ANISOU 1375 CG PRO A 167 14342 8398 8393 -6993 2467 749 C ATOM 1376 CD PRO A 167 2.165 -15.877 24.217 1.00 76.23 C ANISOU 1376 CD PRO A 167 12922 7920 8121 -6218 2338 573 C ATOM 1377 N LEU A 168 0.794 -13.239 26.510 1.00 74.58 N ANISOU 1377 N LEU A 168 10792 9701 7844 -6078 2387 305 N ATOM 1378 CA LEU A 168 0.590 -12.063 27.367 1.00 72.97 C ANISOU 1378 CA LEU A 168 9898 10143 7684 -5758 2362 191 C ATOM 1379 C LEU A 168 -0.306 -11.009 26.708 1.00 72.05 C ANISOU 1379 C LEU A 168 8965 10758 7651 -5659 2324 -139 C ATOM 1380 O LEU A 168 -1.184 -10.433 27.360 1.00 73.93 O ANISOU 1380 O LEU A 168 8643 11758 7690 -5802 2377 -297 O ATOM 1381 CB LEU A 168 1.925 -11.425 27.803 1.00 68.21 C ANISOU 1381 CB LEU A 168 9347 9175 7394 -4964 2228 310 C ATOM 1382 CG LEU A 168 1.771 -10.248 28.785 1.00 66.10 C ANISOU 1382 CG LEU A 168 8468 9502 7143 -4650 2194 192 C ATOM 1383 CD1 LEU A 168 0.957 -10.668 30.040 1.00 70.07 C ANISOU 1383 CD1 LEU A 168 8955 10461 7209 -5210 2345 246 C ATOM 1384 CD2 LEU A 168 3.087 -9.612 29.193 1.00 60.77 C ANISOU 1384 CD2 LEU A 168 7842 8492 6755 -3941 2054 291 C ATOM 1385 N GLU A 169 -0.086 -10.765 25.419 1.00 70.06 N ANISOU 1385 N GLU A 169 8660 10296 7666 -5384 2229 -243 N ATOM 1386 CA GLU A 169 -0.889 -9.804 24.666 1.00 69.82 C ANISOU 1386 CA GLU A 169 7930 10892 7705 -5232 2169 -540 C ATOM 1387 C GLU A 169 -2.375 -10.170 24.645 1.00 75.38 C ANISOU 1387 C GLU A 169 8292 12341 8009 -5955 2290 -718 C ATOM 1388 O GLU A 169 -3.241 -9.286 24.594 1.00 76.02 O ANISOU 1388 O GLU A 169 7665 13206 8012 -5835 2264 -974 O ATOM 1389 CB GLU A 169 -0.366 -9.683 23.244 1.00 66.59 C ANISOU 1389 CB GLU A 169 7640 10060 7601 -4896 2059 -580 C ATOM 1390 CG GLU A 169 -1.265 -8.905 22.328 1.00 66.76 C ANISOU 1390 CG GLU A 169 7052 10680 7635 -4814 1996 -864 C ATOM 1391 CD GLU A 169 -1.096 -9.330 20.908 1.00 68.71 C ANISOU 1391 CD GLU A 169 7542 10561 8005 -4848 1951 -888 C ATOM 1392 OE1 GLU A 169 -1.138 -10.552 20.638 1.00 74.20 O ANISOU 1392 OE1 GLU A 169 8756 10895 8539 -5379 2037 -792 O ATOM 1393 OE2 GLU A 169 -0.908 -8.444 20.051 1.00 67.89 O ANISOU 1393 OE2 GLU A 169 7155 10500 8140 -4345 1826 -1002 O ATOM 1394 N LYS A 170 -2.667 -11.467 24.687 1.00 80.14 N ANISOU 1394 N LYS A 170 9407 12713 8328 -6701 2418 -590 N ATOM 1395 CA LYS A 170 -4.051 -11.919 24.716 1.00 86.21 C ANISOU 1395 CA LYS A 170 9880 14210 8666 -7516 2549 -745 C ATOM 1396 C LYS A 170 -4.575 -11.836 26.136 1.00 89.51 C ANISOU 1396 C LYS A 170 10048 15205 8759 -7807 2674 -716 C ATOM 1397 O LYS A 170 -5.727 -11.473 26.352 1.00 92.95 O ANISOU 1397 O LYS A 170 9815 16600 8901 -8111 2743 -943 O ATOM 1398 CB LYS A 170 -4.183 -13.327 24.127 1.00 89.90 C ANISOU 1398 CB LYS A 170 11044 14180 8932 -8270 2632 -636 C ATOM 1399 CG LYS A 170 -5.197 -13.415 22.967 1.00 93.43 C ANISOU 1399 CG LYS A 170 11122 15136 9240 -8693 2626 -903 C ATOM 1400 CD LYS A 170 -4.916 -12.347 21.868 1.00 87.84 C ANISOU 1400 CD LYS A 170 9959 14492 8923 -7887 2446 -1089 C ATOM 1401 CE LYS A 170 -4.230 -12.915 20.632 1.00 85.69 C ANISOU 1401 CE LYS A 170 10261 13425 8872 -7787 2370 -1030 C ATOM 1402 NZ LYS A 170 -3.511 -11.825 19.888 1.00 81.61 N ANISOU 1402 NZ LYS A 170 9467 12750 8793 -6860 2202 -1093 N ATOM 1403 N GLN A 171 -3.711 -12.147 27.099 1.00 89.27 N ANISOU 1403 N GLN A 171 10527 14631 8761 -7671 2697 -447 N ATOM 1404 CA GLN A 171 -3.992 -11.956 28.526 1.00 91.68 C ANISOU 1404 CA GLN A 171 10630 15407 8799 -7803 2796 -394 C ATOM 1405 C GLN A 171 -4.231 -10.469 28.861 1.00 89.12 C ANISOU 1405 C GLN A 171 9461 15794 8606 -7132 2710 -646 C ATOM 1406 O GLN A 171 -4.680 -10.138 29.957 1.00 91.45 O ANISOU 1406 O GLN A 171 9416 16685 8645 -7210 2792 -692 O ATOM 1407 CB GLN A 171 -2.829 -12.530 29.352 1.00 91.07 C ANISOU 1407 CB GLN A 171 11317 14503 8784 -7638 2792 -45 C ATOM 1408 CG GLN A 171 -2.817 -12.209 30.844 1.00 93.09 C ANISOU 1408 CG GLN A 171 11418 15114 8838 -7580 2855 38 C ATOM 1409 CD GLN A 171 -3.151 -13.412 31.713 1.00101.25 C ANISOU 1409 CD GLN A 171 13016 16057 9396 -8412 3035 285 C ATOM 1410 OE1 GLN A 171 -2.270 -13.961 32.384 1.00102.49 O ANISOU 1410 OE1 GLN A 171 13843 15558 9540 -8298 3023 584 O ATOM 1411 NE2 GLN A 171 -4.426 -13.829 31.712 1.00106.66 N ANISOU 1411 NE2 GLN A 171 13441 17425 9658 -9264 3201 166 N ATOM 1412 N HIS A 172 -3.920 -9.579 27.916 1.00 85.22 N ANISOU 1412 N HIS A 172 8680 15214 8487 -6469 2544 -809 N ATOM 1413 CA HIS A 172 -4.150 -8.136 28.083 1.00 82.92 C ANISOU 1413 CA HIS A 172 7682 15505 8320 -5795 2436 -1063 C ATOM 1414 C HIS A 172 -5.520 -7.705 27.544 1.00 86.05 C ANISOU 1414 C HIS A 172 7347 16873 8476 -5964 2453 -1398 C ATOM 1415 O HIS A 172 -6.504 -8.419 27.707 1.00 91.48 O ANISOU 1415 O HIS A 172 7884 18122 8751 -6718 2608 -1449 O ATOM 1416 CB HIS A 172 -3.023 -7.324 27.435 1.00 76.61 C ANISOU 1416 CB HIS A 172 7010 14073 8025 -4970 2237 -1041 C ATOM 1417 CG HIS A 172 -1.858 -7.065 28.344 1.00 73.75 C ANISOU 1417 CG HIS A 172 6965 13205 7853 -4545 2183 -847 C ATOM 1418 ND1 HIS A 172 -2.002 -6.528 29.605 1.00 74.08 N ANISOU 1418 ND1 HIS A 172 6748 13665 7732 -4409 2210 -893 N ATOM 1419 CD2 HIS A 172 -0.525 -7.239 28.161 1.00 70.56 C ANISOU 1419 CD2 HIS A 172 7074 11970 7765 -4206 2095 -627 C ATOM 1420 CE1 HIS A 172 -0.813 -6.397 30.165 1.00 71.67 C ANISOU 1420 CE1 HIS A 172 6799 12795 7639 -4035 2135 -704 C ATOM 1421 NE2 HIS A 172 0.101 -6.822 29.311 1.00 69.49 N ANISOU 1421 NE2 HIS A 172 6974 11779 7649 -3903 2065 -541 N TER 1422 HIS A 172 ATOM 1423 N PRO B 3 17.702 -4.969 66.960 1.00 88.15 N ANISOU 1423 N PRO B 3 13907 11905 7682 -4029 -2423 1867 N ATOM 1424 CA PRO B 3 16.480 -4.690 67.710 1.00 89.98 C ANISOU 1424 CA PRO B 3 14261 12568 7358 -4530 -2067 1770 C ATOM 1425 C PRO B 3 15.834 -3.368 67.302 1.00 86.78 C ANISOU 1425 C PRO B 3 13335 12572 7066 -4411 -1587 1360 C ATOM 1426 O PRO B 3 14.753 -3.031 67.801 1.00 88.62 O ANISOU 1426 O PRO B 3 13556 13235 6882 -4742 -1234 1198 O ATOM 1427 CB PRO B 3 16.987 -4.577 69.144 1.00 94.07 C ANISOU 1427 CB PRO B 3 15151 13147 7445 -4753 -2388 1890 C ATOM 1428 CG PRO B 3 18.414 -4.076 69.005 1.00 93.21 C ANISOU 1428 CG PRO B 3 14824 12810 7781 -4270 -2768 1861 C ATOM 1429 CD PRO B 3 18.881 -4.345 67.584 1.00 88.93 C ANISOU 1429 CD PRO B 3 13939 11973 7877 -3808 -2775 1845 C ATOM 1430 N LEU B 4 16.500 -2.660 66.386 1.00 82.50 N ANISOU 1430 N LEU B 4 12382 11894 7070 -3937 -1588 1193 N ATOM 1431 CA LEU B 4 16.263 -1.252 66.078 1.00 79.48 C ANISOU 1431 CA LEU B 4 11590 11769 6840 -3736 -1284 823 C ATOM 1432 C LEU B 4 16.396 -1.097 64.574 1.00 74.59 C ANISOU 1432 C LEU B 4 10596 10969 6775 -3362 -1152 735 C ATOM 1433 O LEU B 4 15.788 -0.225 63.967 1.00 72.25 O ANISOU 1433 O LEU B 4 9994 10857 6601 -3225 -826 463 O ATOM 1434 CB LEU B 4 17.341 -0.392 66.758 1.00 80.49 C ANISOU 1434 CB LEU B 4 11715 11857 7011 -3602 -1562 750 C ATOM 1435 CG LEU B 4 17.225 1.092 67.174 1.00 80.78 C ANISOU 1435 CG LEU B 4 11596 12146 6951 -3552 -1388 400 C ATOM 1436 CD1 LEU B 4 16.719 2.017 66.064 1.00 76.83 C ANISOU 1436 CD1 LEU B 4 10709 11704 6780 -3269 -1035 103 C ATOM 1437 CD2 LEU B 4 16.400 1.278 68.466 1.00 85.34 C ANISOU 1437 CD2 LEU B 4 12444 13094 6887 -3926 -1237 296 C ATOM 1438 N CYS B 5 17.221 -1.953 63.989 1.00 73.39 N ANISOU 1438 N CYS B 5 10494 10450 6940 -3176 -1428 959 N ATOM 1439 CA CYS B 5 17.395 -2.028 62.553 1.00 69.20 C ANISOU 1439 CA CYS B 5 9667 9733 6892 -2856 -1319 908 C ATOM 1440 C CYS B 5 16.820 -3.343 62.067 1.00 69.46 C ANISOU 1440 C CYS B 5 9917 9598 6877 -2988 -1298 1104 C ATOM 1441 O CYS B 5 17.184 -3.864 61.012 1.00 67.76 O ANISOU 1441 O CYS B 5 9610 9117 7018 -2738 -1340 1155 O ATOM 1442 CB CYS B 5 18.872 -1.910 62.242 1.00 68.88 C ANISOU 1442 CB CYS B 5 9473 9444 7256 -2513 -1639 955 C ATOM 1443 SG CYS B 5 19.482 -0.322 62.843 1.00 68.88 S ANISOU 1443 SG CYS B 5 9265 9644 7260 -2471 -1667 722 S ATOM 1444 N ALA B 6 15.895 -3.862 62.867 1.00 71.88 N ANISOU 1444 N ALA B 6 10531 10079 6699 -3422 -1220 1202 N ATOM 1445 CA ALA B 6 15.248 -5.140 62.621 1.00 73.23 C ANISOU 1445 CA ALA B 6 11011 10107 6707 -3693 -1218 1411 C ATOM 1446 C ALA B 6 14.494 -5.128 61.295 1.00 69.87 C ANISOU 1446 C ALA B 6 10283 9737 6528 -3597 -889 1264 C ATOM 1447 O ALA B 6 14.409 -6.148 60.607 1.00 69.98 O ANISOU 1447 O ALA B 6 10478 9465 6645 -3619 -960 1414 O ATOM 1448 CB ALA B 6 14.309 -5.481 63.781 1.00 76.92 C ANISOU 1448 CB ALA B 6 11813 10868 6544 -4273 -1126 1503 C ATOM 1449 N ASN B 7 13.973 -3.964 60.928 1.00 66.88 N ANISOU 1449 N ASN B 7 9477 9695 6239 -3471 -561 965 N ATOM 1450 CA ASN B 7 13.118 -3.859 59.754 1.00 64.34 C ANISOU 1450 CA ASN B 7 8865 9494 6087 -3405 -255 812 C ATOM 1451 C ASN B 7 13.891 -3.718 58.431 1.00 60.63 C ANISOU 1451 C ASN B 7 8181 8703 6151 -2954 -308 771 C ATOM 1452 O ASN B 7 13.302 -3.494 57.367 1.00 58.47 O ANISOU 1452 O ASN B 7 7662 8506 6049 -2847 -80 633 O ATOM 1453 CB ASN B 7 12.026 -2.788 59.960 1.00 64.41 C ANISOU 1453 CB ASN B 7 8550 10028 5893 -3476 105 508 C ATOM 1454 CG ASN B 7 12.558 -1.362 59.916 1.00 63.06 C ANISOU 1454 CG ASN B 7 8116 9898 5947 -3095 133 265 C ATOM 1455 OD1 ASN B 7 12.021 -0.529 59.185 1.00 62.62 O ANISOU 1455 OD1 ASN B 7 7748 10001 6045 -2876 357 24 O ATOM 1456 ND2 ASN B 7 13.600 -1.067 60.701 1.00 65.15 N ANISOU 1456 ND2 ASN B 7 8534 10009 6213 -3029 -120 330 N ATOM 1457 N LEU B 8 15.216 -3.866 58.523 1.00 59.85 N ANISOU 1457 N LEU B 8 8171 8281 6290 -2703 -617 886 N ATOM 1458 CA LEU B 8 16.092 -3.967 57.361 1.00 56.65 C ANISOU 1458 CA LEU B 8 7598 7581 6347 -2315 -692 873 C ATOM 1459 C LEU B 8 16.329 -5.406 56.895 1.00 57.81 C ANISOU 1459 C LEU B 8 8042 7353 6569 -2292 -883 1077 C ATOM 1460 O LEU B 8 17.006 -5.625 55.890 1.00 56.22 O ANISOU 1460 O LEU B 8 7716 6921 6725 -1963 -924 1046 O ATOM 1461 CB LEU B 8 17.436 -3.319 57.665 1.00 56.51 C ANISOU 1461 CB LEU B 8 7434 7483 6556 -2043 -914 844 C ATOM 1462 CG LEU B 8 17.486 -1.829 57.400 1.00 53.48 C ANISOU 1462 CG LEU B 8 6704 7311 6304 -1918 -716 598 C ATOM 1463 CD1 LEU B 8 18.807 -1.314 57.873 1.00 56.25 C ANISOU 1463 CD1 LEU B 8 6959 7603 6808 -1767 -973 600 C ATOM 1464 CD2 LEU B 8 17.308 -1.582 55.925 1.00 50.71 C ANISOU 1464 CD2 LEU B 8 6107 6906 6255 -1716 -488 477 C ATOM 1465 N VAL B 9 15.783 -6.367 57.635 1.00 60.49 N ANISOU 1465 N VAL B 9 8804 7630 6548 -2652 -999 1275 N ATOM 1466 CA VAL B 9 15.882 -7.790 57.303 1.00 62.95 C ANISOU 1466 CA VAL B 9 9531 7530 6859 -2687 -1213 1482 C ATOM 1467 C VAL B 9 14.859 -8.155 56.233 1.00 61.64 C ANISOU 1467 C VAL B 9 9323 7396 6703 -2840 -936 1411 C ATOM 1468 O VAL B 9 13.674 -7.849 56.394 1.00 61.56 O ANISOU 1468 O VAL B 9 9213 7758 6420 -3206 -660 1337 O ATOM 1469 CB VAL B 9 15.654 -8.690 58.565 1.00 67.33 C ANISOU 1469 CB VAL B 9 10659 7968 6956 -3103 -1475 1756 C ATOM 1470 CG1 VAL B 9 15.549 -10.167 58.194 1.00 70.33 C ANISOU 1470 CG1 VAL B 9 11567 7880 7276 -3211 -1688 1969 C ATOM 1471 CG2 VAL B 9 16.763 -8.484 59.589 1.00 69.35 C ANISOU 1471 CG2 VAL B 9 11015 8134 7201 -2923 -1834 1855 C ATOM 1472 N PRO B 10 15.304 -8.827 55.151 1.00 61.05 N ANISOU 1472 N PRO B 10 9313 6958 6924 -2558 -1013 1414 N ATOM 1473 CA PRO B 10 14.378 -9.277 54.127 1.00 60.24 C ANISOU 1473 CA PRO B 10 9232 6846 6810 -2724 -799 1359 C ATOM 1474 C PRO B 10 13.167 -9.989 54.725 1.00 63.14 C ANISOU 1474 C PRO B 10 9952 7329 6709 -3350 -754 1505 C ATOM 1475 O PRO B 10 13.303 -10.828 55.630 1.00 66.77 O ANISOU 1475 O PRO B 10 10916 7556 6897 -3603 -1023 1741 O ATOM 1476 CB PRO B 10 15.218 -10.251 53.300 1.00 61.44 C ANISOU 1476 CB PRO B 10 9632 6475 7238 -2374 -1023 1408 C ATOM 1477 CG PRO B 10 16.594 -9.725 53.423 1.00 60.69 C ANISOU 1477 CG PRO B 10 9289 6313 7459 -1875 -1188 1348 C ATOM 1478 CD PRO B 10 16.684 -9.250 54.851 1.00 62.04 C ANISOU 1478 CD PRO B 10 9497 6689 7384 -2070 -1315 1450 C ATOM 1479 N VAL B 11 11.992 -9.606 54.230 1.00 61.61 N ANISOU 1479 N VAL B 11 9479 7525 6406 -3608 -423 1361 N ATOM 1480 CA VAL B 11 10.724 -10.165 54.653 1.00 64.32 C ANISOU 1480 CA VAL B 11 10016 8119 6305 -4248 -306 1446 C ATOM 1481 C VAL B 11 10.137 -10.829 53.429 1.00 63.87 C ANISOU 1481 C VAL B 11 10016 7925 6327 -4352 -226 1411 C ATOM 1482 O VAL B 11 10.037 -10.202 52.384 1.00 60.77 O ANISOU 1482 O VAL B 11 9218 7658 6213 -4049 -44 1206 O ATOM 1483 CB VAL B 11 9.748 -9.086 55.212 1.00 64.13 C ANISOU 1483 CB VAL B 11 9528 8793 6045 -4471 20 1258 C ATOM 1484 CG1 VAL B 11 8.428 -9.716 55.690 1.00 67.04 C ANISOU 1484 CG1 VAL B 11 10040 9516 5915 -5191 166 1331 C ATOM 1485 CG2 VAL B 11 10.388 -8.324 56.371 1.00 64.71 C ANISOU 1485 CG2 VAL B 11 9551 8986 6050 -4331 -57 1253 C ATOM 1486 N PRO B 12 9.768 -12.115 53.547 1.00 67.71 N ANISOU 1486 N PRO B 12 11062 8119 6545 -4801 -386 1620 N ATOM 1487 CA PRO B 12 9.172 -12.793 52.405 1.00 68.09 C ANISOU 1487 CA PRO B 12 11215 8026 6629 -4960 -328 1583 C ATOM 1488 C PRO B 12 7.934 -12.063 51.891 1.00 66.40 C ANISOU 1488 C PRO B 12 10430 8461 6337 -5181 36 1364 C ATOM 1489 O PRO B 12 7.247 -11.383 52.653 1.00 66.75 O ANISOU 1489 O PRO B 12 10143 9077 6143 -5427 234 1291 O ATOM 1490 CB PRO B 12 8.782 -14.159 52.977 1.00 73.38 C ANISOU 1490 CB PRO B 12 12610 8383 6890 -5581 -547 1861 C ATOM 1491 CG PRO B 12 9.680 -14.342 54.144 1.00 75.16 C ANISOU 1491 CG PRO B 12 13209 8322 7027 -5475 -838 2064 C ATOM 1492 CD PRO B 12 9.859 -12.996 54.728 1.00 72.12 C ANISOU 1492 CD PRO B 12 12235 8445 6723 -5221 -647 1908 C ATOM 1493 N ILE B 13 7.653 -12.210 50.605 1.00 64.94 N ANISOU 1493 N ILE B 13 10133 8200 6341 -5070 109 1244 N ATOM 1494 CA ILE B 13 6.455 -11.620 50.034 1.00 64.17 C ANISOU 1494 CA ILE B 13 9518 8695 6167 -5263 392 1044 C ATOM 1495 C ILE B 13 5.339 -12.656 49.945 1.00 68.01 C ANISOU 1495 C ILE B 13 10265 9296 6280 -5998 401 1139 C ATOM 1496 O ILE B 13 5.485 -13.698 49.294 1.00 69.88 O ANISOU 1496 O ILE B 13 10985 9035 6530 -6127 227 1244 O ATOM 1497 CB ILE B 13 6.761 -10.920 48.683 1.00 59.82 C ANISOU 1497 CB ILE B 13 8611 8095 6024 -4701 479 834 C ATOM 1498 CG1 ILE B 13 7.468 -9.595 48.948 1.00 56.53 C ANISOU 1498 CG1 ILE B 13 7795 7820 5862 -4157 555 705 C ATOM 1499 CG2 ILE B 13 5.497 -10.625 47.919 1.00 61.05 C ANISOU 1499 CG2 ILE B 13 8367 8746 6083 -4926 677 663 C ATOM 1500 CD1 ILE B 13 8.197 -9.012 47.748 1.00 51.63 C ANISOU 1500 CD1 ILE B 13 6990 6981 5645 -3590 576 567 C ATOM 1501 N THR B 14 4.235 -12.387 50.640 1.00 70.25 N ANISOU 1501 N THR B 14 10242 10245 6205 -6502 603 1092 N ATOM 1502 CA THR B 14 3.029 -13.222 50.507 1.00 73.87 C ANISOU 1502 CA THR B 14 10801 10982 6285 -7274 664 1142 C ATOM 1503 C THR B 14 1.936 -12.499 49.728 1.00 72.67 C ANISOU 1503 C THR B 14 9931 11516 6166 -7273 913 861 C ATOM 1504 O THR B 14 2.127 -11.371 49.267 1.00 67.68 O ANISOU 1504 O THR B 14 8798 11071 5848 -6653 1017 645 O ATOM 1505 CB THR B 14 2.439 -13.635 51.873 1.00 78.92 C ANISOU 1505 CB THR B 14 11624 11965 6398 -8006 719 1300 C ATOM 1506 OG1 THR B 14 2.106 -12.458 52.623 1.00 78.48 O ANISOU 1506 OG1 THR B 14 10949 12597 6273 -7849 975 1105 O ATOM 1507 CG2 THR B 14 3.414 -14.513 52.655 1.00 80.64 C ANISOU 1507 CG2 THR B 14 12662 11467 6510 -8096 405 1620 C ATOM 1508 N ASN B 15 0.775 -13.148 49.605 1.00 76.76 N ANISOU 1508 N ASN B 15 10410 12419 6336 -7992 987 869 N ATOM 1509 CA ASN B 15 -0.369 -12.530 48.941 1.00 76.94 C ANISOU 1509 CA ASN B 15 9711 13179 6344 -8039 1192 599 C ATOM 1510 C ASN B 15 -0.936 -11.309 49.697 1.00 76.96 C ANISOU 1510 C ASN B 15 8981 13998 6263 -7857 1459 359 C ATOM 1511 O ASN B 15 -1.314 -10.301 49.070 1.00 74.53 O ANISOU 1511 O ASN B 15 8059 14084 6174 -7375 1564 88 O ATOM 1512 CB ASN B 15 -1.444 -13.572 48.600 1.00 81.68 C ANISOU 1512 CB ASN B 15 10434 14014 6587 -8893 1184 660 C ATOM 1513 CG ASN B 15 -1.139 -14.336 47.293 1.00 80.68 C ANISOU 1513 CG ASN B 15 10751 13242 6660 -8830 963 721 C ATOM 1514 OD1 ASN B 15 -0.121 -14.116 46.624 1.00 75.92 O ANISOU 1514 OD1 ASN B 15 10347 12043 6456 -8144 838 711 O ATOM 1515 ND2 ASN B 15 -2.037 -15.224 46.929 1.00 84.82 N ANISOU 1515 ND2 ASN B 15 11418 13926 6883 -9575 927 766 N ATOM 1516 N ALA B 16 -0.953 -11.384 51.028 1.00 79.42 N ANISOU 1516 N ALA B 16 9402 14522 6252 -8203 1545 451 N ATOM 1517 CA ALA B 16 -1.337 -10.233 51.860 1.00 80.08 C ANISOU 1517 CA ALA B 16 8878 15305 6243 -7975 1793 207 C ATOM 1518 C ALA B 16 -0.375 -9.057 51.635 1.00 74.40 C ANISOU 1518 C ALA B 16 8008 14275 5986 -7029 1743 75 C ATOM 1519 O ALA B 16 -0.810 -7.919 51.465 1.00 73.54 O ANISOU 1519 O ALA B 16 7290 14650 6001 -6584 1893 -225 O ATOM 1520 CB ALA B 16 -1.413 -10.617 53.351 1.00 83.97 C ANISOU 1520 CB ALA B 16 9631 16010 6265 -8557 1881 356 C ATOM 1521 N THR B 17 0.923 -9.340 51.588 1.00 71.41 N ANISOU 1521 N THR B 17 8189 13087 5858 -6724 1516 289 N ATOM 1522 CA THR B 17 1.936 -8.309 51.285 1.00 66.12 C ANISOU 1522 CA THR B 17 7418 12080 5626 -5904 1451 190 C ATOM 1523 C THR B 17 1.591 -7.606 49.972 1.00 64.10 C ANISOU 1523 C THR B 17 6729 11949 5675 -5453 1492 -35 C ATOM 1524 O THR B 17 1.534 -6.372 49.900 1.00 62.17 O ANISOU 1524 O THR B 17 6060 11966 5597 -4946 1583 -267 O ATOM 1525 CB THR B 17 3.351 -8.919 51.189 1.00 63.54 C ANISOU 1525 CB THR B 17 7719 10888 5535 -5685 1182 447 C ATOM 1526 OG1 THR B 17 3.680 -9.557 52.425 1.00 65.76 O ANISOU 1526 OG1 THR B 17 8442 11025 5519 -6073 1088 671 O ATOM 1527 CG2 THR B 17 4.381 -7.858 50.882 1.00 58.46 C ANISOU 1527 CG2 THR B 17 6926 9976 5310 -4931 1137 340 C ATOM 1528 N LEU B 18 1.338 -8.418 48.949 1.00 64.99 N ANISOU 1528 N LEU B 18 7009 11854 5830 -5664 1402 40 N ATOM 1529 CA LEU B 18 0.961 -7.949 47.630 1.00 63.24 C ANISOU 1529 CA LEU B 18 6463 11724 5839 -5335 1403 -135 C ATOM 1530 C LEU B 18 -0.314 -7.106 47.657 1.00 66.13 C ANISOU 1530 C LEU B 18 6124 12936 6068 -5317 1581 -423 C ATOM 1531 O LEU B 18 -0.457 -6.159 46.879 1.00 64.44 O ANISOU 1531 O LEU B 18 5563 12836 6086 -4794 1576 -618 O ATOM 1532 CB LEU B 18 0.842 -9.140 46.672 1.00 63.70 C ANISOU 1532 CB LEU B 18 6894 11434 5876 -5691 1269 3 C ATOM 1533 CG LEU B 18 2.166 -9.880 46.436 1.00 60.62 C ANISOU 1533 CG LEU B 18 7171 10176 5688 -5527 1073 223 C ATOM 1534 CD1 LEU B 18 1.962 -11.216 45.774 1.00 62.27 C ANISOU 1534 CD1 LEU B 18 7851 10034 5774 -5983 936 358 C ATOM 1535 CD2 LEU B 18 3.150 -9.008 45.608 1.00 54.63 C ANISOU 1535 CD2 LEU B 18 6330 9068 5359 -4770 1039 128 C ATOM 1536 N ASP B 19 -1.216 -7.429 48.577 1.00 71.15 N ANISOU 1536 N ASP B 19 6554 14171 6311 -5873 1731 -457 N ATOM 1537 CA ASP B 19 -2.397 -6.604 48.810 1.00 75.37 C ANISOU 1537 CA ASP B 19 6355 15596 6687 -5818 1924 -775 C ATOM 1538 C ASP B 19 -2.037 -5.294 49.489 1.00 73.93 C ANISOU 1538 C ASP B 19 5929 15536 6625 -5205 2011 -971 C ATOM 1539 O ASP B 19 -2.614 -4.254 49.182 1.00 74.66 O ANISOU 1539 O ASP B 19 5497 16056 6816 -4737 2066 -1269 O ATOM 1540 CB ASP B 19 -3.435 -7.350 49.661 1.00 81.45 C ANISOU 1540 CB ASP B 19 6952 17037 6956 -6649 2100 -771 C ATOM 1541 CG ASP B 19 -4.289 -8.288 48.848 1.00 85.64 C ANISOU 1541 CG ASP B 19 7429 17776 7334 -7230 2050 -725 C ATOM 1542 OD1 ASP B 19 -4.674 -7.921 47.715 1.00 86.31 O ANISOU 1542 OD1 ASP B 19 7195 17965 7635 -6900 1968 -878 O ATOM 1543 OD2 ASP B 19 -4.598 -9.391 49.350 1.00 91.91 O ANISOU 1543 OD2 ASP B 19 8526 18633 7764 -8052 2078 -531 O ATOM 1544 N ARG B 20 -1.083 -5.354 50.412 1.00 72.90 N ANISOU 1544 N ARG B 20 6213 15009 6476 -5203 1993 -808 N ATOM 1545 CA ARG B 20 -0.697 -4.191 51.184 1.00 72.06 C ANISOU 1545 CA ARG B 20 5956 14991 6433 -4714 2065 -981 C ATOM 1546 C ARG B 20 -0.147 -3.110 50.261 1.00 68.19 C ANISOU 1546 C ARG B 20 5385 14148 6376 -3939 1944 -1107 C ATOM 1547 O ARG B 20 -0.394 -1.928 50.483 1.00 68.46 O ANISOU 1547 O ARG B 20 5084 14467 6460 -3470 2010 -1380 O ATOM 1548 CB ARG B 20 0.318 -4.581 52.265 1.00 71.77 C ANISOU 1548 CB ARG B 20 6443 14530 6296 -4902 2009 -741 C ATOM 1549 CG ARG B 20 0.673 -3.488 53.269 1.00 71.31 C ANISOU 1549 CG ARG B 20 6277 14610 6209 -4534 2090 -914 C ATOM 1550 CD ARG B 20 1.807 -3.945 54.189 1.00 70.93 C ANISOU 1550 CD ARG B 20 6793 14058 6098 -4702 1960 -637 C ATOM 1551 NE ARG B 20 2.350 -2.848 55.002 1.00 69.06 N ANISOU 1551 NE ARG B 20 6518 13827 5894 -4299 1981 -790 N ATOM 1552 CZ ARG B 20 2.893 -2.999 56.209 1.00 69.54 C ANISOU 1552 CZ ARG B 20 6890 13808 5724 -4514 1951 -669 C ATOM 1553 NH1 ARG B 20 2.976 -4.200 56.775 1.00 71.41 N ANISOU 1553 NH1 ARG B 20 7526 13935 5672 -5117 1887 -376 N ATOM 1554 NH2 ARG B 20 3.335 -1.938 56.869 1.00 68.41 N ANISOU 1554 NH2 ARG B 20 6698 13685 5610 -4141 1964 -842 N ATOM 1555 N ILE B 21 0.567 -3.525 49.210 1.00 65.32 N ANISOU 1555 N ILE B 21 5355 13168 6295 -3823 1767 -918 N ATOM 1556 CA ILE B 21 1.284 -2.597 48.327 1.00 61.17 C ANISOU 1556 CA ILE B 21 4868 12223 6153 -3178 1648 -977 C ATOM 1557 C ILE B 21 0.524 -2.248 47.046 1.00 61.17 C ANISOU 1557 C ILE B 21 4561 12413 6269 -2948 1601 -1129 C ATOM 1558 O ILE B 21 0.994 -1.442 46.234 1.00 58.73 O ANISOU 1558 O ILE B 21 4294 11790 6232 -2448 1499 -1178 O ATOM 1559 CB ILE B 21 2.717 -3.117 47.981 1.00 57.98 C ANISOU 1559 CB ILE B 21 5005 11030 5996 -3115 1495 -705 C ATOM 1560 CG1 ILE B 21 2.664 -4.312 47.023 1.00 58.21 C ANISOU 1560 CG1 ILE B 21 5278 10794 6044 -3425 1410 -536 C ATOM 1561 CG2 ILE B 21 3.474 -3.484 49.256 1.00 58.64 C ANISOU 1561 CG2 ILE B 21 5395 10927 5960 -3318 1483 -545 C ATOM 1562 CD1 ILE B 21 4.040 -4.811 46.582 1.00 57.34 C ANISOU 1562 CD1 ILE B 21 5645 9954 6186 -3278 1270 -330 C ATOM 1563 N THR B 22 -0.635 -2.880 46.862 1.00 64.36 N ANISOU 1563 N THR B 22 4679 13333 6443 -3355 1660 -1189 N ATOM 1564 CA THR B 22 -1.513 -2.611 45.725 1.00 64.95 C ANISOU 1564 CA THR B 22 4404 13699 6574 -3188 1592 -1348 C ATOM 1565 C THR B 22 -2.006 -1.175 45.857 1.00 65.49 C ANISOU 1565 C THR B 22 4028 14151 6703 -2584 1608 -1665 C ATOM 1566 O THR B 22 -2.533 -0.791 46.920 1.00 68.21 O ANISOU 1566 O THR B 22 4052 15016 6846 -2597 1762 -1857 O ATOM 1567 CB THR B 22 -2.736 -3.577 45.718 1.00 69.84 C ANISOU 1567 CB THR B 22 4733 14924 6880 -3830 1663 -1375 C ATOM 1568 OG1 THR B 22 -2.282 -4.935 45.711 1.00 70.27 O ANISOU 1568 OG1 THR B 22 5295 14563 6840 -4418 1626 -1079 O ATOM 1569 CG2 THR B 22 -3.635 -3.347 44.503 1.00 71.02 C ANISOU 1569 CG2 THR B 22 4509 15393 7084 -3670 1548 -1534 C ATOM 1570 N GLY B 23 -1.822 -0.381 44.801 1.00 62.30 N ANISOU 1570 N GLY B 23 3647 13474 6550 -2054 1443 -1726 N ATOM 1571 CA GLY B 23 -2.404 0.957 44.758 1.00 63.20 C ANISOU 1571 CA GLY B 23 3390 13908 6716 -1443 1391 -2034 C ATOM 1572 C GLY B 23 -1.503 2.095 44.346 1.00 59.73 C ANISOU 1572 C GLY B 23 3268 12880 6546 -841 1246 -2031 C ATOM 1573 O GLY B 23 -0.418 1.874 43.763 1.00 55.96 O ANISOU 1573 O GLY B 23 3258 11751 6253 -870 1174 -1788 O ATOM 1574 N LYS B 24 -1.966 3.314 44.625 1.00 61.23 N ANISOU 1574 N LYS B 24 3210 13311 6743 -299 1200 -2318 N ATOM 1575 CA LYS B 24 -1.221 4.537 44.311 1.00 59.36 C ANISOU 1575 CA LYS B 24 3303 12532 6718 266 1042 -2345 C ATOM 1576 C LYS B 24 -0.164 4.865 45.386 1.00 57.64 C ANISOU 1576 C LYS B 24 3405 11964 6530 253 1141 -2284 C ATOM 1577 O LYS B 24 -0.479 4.921 46.591 1.00 59.92 O ANISOU 1577 O LYS B 24 3490 12640 6638 178 1299 -2443 O ATOM 1578 CB LYS B 24 -2.185 5.720 44.099 1.00 62.94 C ANISOU 1578 CB LYS B 24 3431 13322 7162 900 890 -2688 C ATOM 1579 CG LYS B 24 -1.524 6.936 43.440 1.00 60.94 C ANISOU 1579 CG LYS B 24 3612 12433 7110 1447 650 -2675 C ATOM 1580 CD LYS B 24 -2.523 7.998 42.984 1.00 64.06 C ANISOU 1580 CD LYS B 24 3762 13078 7501 2106 414 -2982 C ATOM 1581 CE LYS B 24 -1.778 9.290 42.638 1.00 62.85 C ANISOU 1581 CE LYS B 24 4155 12228 7497 2604 184 -2969 C ATOM 1582 NZ LYS B 24 -2.648 10.459 42.312 1.00 64.90 N ANISOU 1582 NZ LYS B 24 4303 12605 7750 3337 -100 -3276 N ATOM 1583 N TRP B 25 1.083 5.060 44.945 1.00 53.61 N ANISOU 1583 N TRP B 25 3379 10767 6224 294 1054 -2062 N ATOM 1584 CA TRP B 25 2.187 5.430 45.834 1.00 52.01 C ANISOU 1584 CA TRP B 25 3487 10200 6072 287 1099 -1992 C ATOM 1585 C TRP B 25 2.967 6.603 45.259 1.00 50.54 C ANISOU 1585 C TRP B 25 3661 9464 6079 685 926 -1983 C ATOM 1586 O TRP B 25 3.074 6.759 44.041 1.00 49.69 O ANISOU 1586 O TRP B 25 3701 9087 6091 803 795 -1890 O ATOM 1587 CB TRP B 25 3.164 4.266 46.075 1.00 49.28 C ANISOU 1587 CB TRP B 25 3385 9580 5760 -208 1184 -1689 C ATOM 1588 CG TRP B 25 2.540 3.078 46.708 1.00 52.51 C ANISOU 1588 CG TRP B 25 3581 10419 5950 -679 1329 -1647 C ATOM 1589 CD1 TRP B 25 2.002 2.006 46.064 1.00 54.06 C ANISOU 1589 CD1 TRP B 25 3681 10773 6085 -1015 1346 -1542 C ATOM 1590 CD2 TRP B 25 2.381 2.830 48.111 1.00 56.06 C ANISOU 1590 CD2 TRP B 25 3939 11191 6172 -923 1470 -1702 C ATOM 1591 NE1 TRP B 25 1.500 1.105 46.975 1.00 57.53 N ANISOU 1591 NE1 TRP B 25 3984 11604 6271 -1482 1484 -1518 N ATOM 1592 CE2 TRP B 25 1.717 1.584 48.240 1.00 59.66 C ANISOU 1592 CE2 TRP B 25 4251 11994 6424 -1438 1570 -1610 C ATOM 1593 CE3 TRP B 25 2.721 3.542 49.274 1.00 57.47 C ANISOU 1593 CE3 TRP B 25 4174 11397 6266 -790 1516 -1823 C ATOM 1594 CZ2 TRP B 25 1.375 1.031 49.495 1.00 63.19 C ANISOU 1594 CZ2 TRP B 25 4614 12828 6568 -1845 1725 -1618 C ATOM 1595 CZ3 TRP B 25 2.396 2.984 50.527 1.00 60.45 C ANISOU 1595 CZ3 TRP B 25 4454 12168 6346 -1164 1673 -1844 C ATOM 1596 CH2 TRP B 25 1.728 1.742 50.621 1.00 63.75 C ANISOU 1596 CH2 TRP B 25 4735 12938 6550 -1695 1780 -1733 C ATOM 1597 N PHE B 26 3.521 7.415 46.152 1.00 50.07 N ANISOU 1597 N PHE B 26 3776 9233 6016 842 924 -2072 N ATOM 1598 CA PHE B 26 4.324 8.564 45.771 1.00 48.15 C ANISOU 1598 CA PHE B 26 3927 8450 5917 1134 760 -2059 C ATOM 1599 C PHE B 26 5.742 8.323 46.223 1.00 44.79 C ANISOU 1599 C PHE B 26 3794 7641 5585 828 806 -1840 C ATOM 1600 O PHE B 26 5.972 7.827 47.320 1.00 44.12 O ANISOU 1600 O PHE B 26 3635 7724 5406 590 921 -1826 O ATOM 1601 CB PHE B 26 3.784 9.842 46.441 1.00 51.25 C ANISOU 1601 CB PHE B 26 4319 8938 6217 1604 676 -2388 C ATOM 1602 CG PHE B 26 2.430 10.285 45.935 1.00 53.63 C ANISOU 1602 CG PHE B 26 4330 9596 6453 2043 571 -2648 C ATOM 1603 CD1 PHE B 26 1.247 9.741 46.458 1.00 55.30 C ANISOU 1603 CD1 PHE B 26 3998 10524 6488 2024 716 -2859 C ATOM 1604 CD2 PHE B 26 2.331 11.264 44.947 1.00 54.33 C ANISOU 1604 CD2 PHE B 26 4684 9326 6634 2469 310 -2688 C ATOM 1605 CE1 PHE B 26 0.005 10.154 45.998 1.00 57.17 C ANISOU 1605 CE1 PHE B 26 3892 11158 6672 2456 603 -3126 C ATOM 1606 CE2 PHE B 26 1.076 11.688 44.483 1.00 56.18 C ANISOU 1606 CE2 PHE B 26 4640 9895 6811 2938 159 -2938 C ATOM 1607 CZ PHE B 26 -0.081 11.133 45.008 1.00 58.41 C ANISOU 1607 CZ PHE B 26 4311 10935 6947 2951 305 -3170 C ATOM 1608 N TYR B 27 6.698 8.681 45.379 1.00 43.11 N ANISOU 1608 N TYR B 27 3904 6940 5537 821 710 -1671 N ATOM 1609 CA TYR B 27 8.102 8.606 45.762 1.00 40.87 C ANISOU 1609 CA TYR B 27 3851 6323 5354 571 731 -1496 C ATOM 1610 C TYR B 27 8.456 9.842 46.609 1.00 42.76 C ANISOU 1610 C TYR B 27 4310 6388 5550 750 639 -1651 C ATOM 1611 O TYR B 27 8.124 10.989 46.243 1.00 45.14 O ANISOU 1611 O TYR B 27 4809 6505 5838 1080 495 -1796 O ATOM 1612 CB TYR B 27 8.998 8.354 44.521 1.00 39.28 C ANISOU 1612 CB TYR B 27 3839 5768 5319 423 712 -1268 C ATOM 1613 CG TYR B 27 10.470 8.649 44.714 1.00 38.53 C ANISOU 1613 CG TYR B 27 3968 5334 5339 242 699 -1137 C ATOM 1614 CD1 TYR B 27 11.117 9.581 43.899 1.00 38.88 C ANISOU 1614 CD1 TYR B 27 4310 5015 5450 276 611 -1086 C ATOM 1615 CD2 TYR B 27 11.204 8.039 45.735 1.00 37.13 C ANISOU 1615 CD2 TYR B 27 3712 5219 5178 17 756 -1066 C ATOM 1616 CE1 TYR B 27 12.457 9.901 44.082 1.00 39.40 C ANISOU 1616 CE1 TYR B 27 4532 4836 5602 59 605 -984 C ATOM 1617 CE2 TYR B 27 12.550 8.357 45.933 1.00 39.83 C ANISOU 1617 CE2 TYR B 27 4199 5309 5625 -140 719 -968 C ATOM 1618 CZ TYR B 27 13.168 9.293 45.099 1.00 40.19 C ANISOU 1618 CZ TYR B 27 4483 5045 5741 -133 657 -936 C ATOM 1619 OH TYR B 27 14.488 9.637 45.287 1.00 39.29 O ANISOU 1619 OH TYR B 27 4468 4747 5713 -343 629 -854 O ATOM 1620 N ILE B 28 9.044 9.607 47.787 1.00 41.95 N ANISOU 1620 N ILE B 28 4201 6341 5396 547 695 -1635 N ATOM 1621 CA ILE B 28 9.308 10.700 48.742 1.00 43.25 C ANISOU 1621 CA ILE B 28 4573 6383 5476 682 612 -1811 C ATOM 1622 C ILE B 28 10.799 11.096 48.815 1.00 41.96 C ANISOU 1622 C ILE B 28 4703 5806 5432 457 524 -1652 C ATOM 1623 O ILE B 28 11.154 12.283 48.729 1.00 42.97 O ANISOU 1623 O ILE B 28 5154 5606 5567 578 385 -1734 O ATOM 1624 CB ILE B 28 8.834 10.367 50.180 1.00 44.64 C ANISOU 1624 CB ILE B 28 4560 6962 5439 620 718 -1963 C ATOM 1625 CG1 ILE B 28 7.394 9.818 50.205 1.00 46.79 C ANISOU 1625 CG1 ILE B 28 4456 7760 5561 731 849 -2117 C ATOM 1626 CG2 ILE B 28 8.978 11.605 51.105 1.00 46.86 C ANISOU 1626 CG2 ILE B 28 5091 7113 5601 817 625 -2204 C ATOM 1627 CD1 ILE B 28 6.278 10.887 50.136 1.00 50.09 C ANISOU 1627 CD1 ILE B 28 4810 8339 5882 1234 794 -2468 C ATOM 1628 N ALA B 29 11.660 10.104 49.005 1.00 39.04 N ANISOU 1628 N ALA B 29 4224 5463 5145 127 586 -1436 N ATOM 1629 CA ALA B 29 13.056 10.374 49.257 1.00 38.69 C ANISOU 1629 CA ALA B 29 4346 5156 5199 -99 505 -1314 C ATOM 1630 C ALA B 29 13.849 9.098 49.118 1.00 37.16 C ANISOU 1630 C ALA B 29 3966 5021 5133 -359 566 -1081 C ATOM 1631 O ALA B 29 13.297 7.994 49.243 1.00 35.29 O ANISOU 1631 O ALA B 29 3536 5019 4851 -401 653 -1026 O ATOM 1632 CB ALA B 29 13.241 10.962 50.659 1.00 40.90 C ANISOU 1632 CB ALA B 29 4741 5474 5324 -123 432 -1459 C ATOM 1633 N SER B 30 15.148 9.260 48.856 1.00 36.79 N ANISOU 1633 N SER B 30 3985 4762 5232 -538 508 -956 N ATOM 1634 CA SER B 30 16.083 8.136 48.812 1.00 35.88 C ANISOU 1634 CA SER B 30 3687 4693 5254 -722 529 -771 C ATOM 1635 C SER B 30 17.511 8.618 49.040 1.00 37.17 C ANISOU 1635 C SER B 30 3879 4725 5521 -912 427 -716 C ATOM 1636 O SER B 30 17.801 9.837 48.984 1.00 38.43 O ANISOU 1636 O SER B 30 4242 4708 5651 -961 359 -792 O ATOM 1637 CB SER B 30 15.970 7.361 47.481 1.00 34.49 C ANISOU 1637 CB SER B 30 3411 4492 5203 -693 646 -669 C ATOM 1638 OG SER B 30 16.600 8.063 46.411 1.00 37.38 O ANISOU 1638 OG SER B 30 3876 4657 5670 -737 665 -643 O ATOM 1639 N ALA B 31 18.392 7.653 49.312 1.00 37.01 N ANISOU 1639 N ALA B 31 3663 4789 5608 -1021 395 -589 N ATOM 1640 CA ALA B 31 19.814 7.891 49.486 1.00 38.35 C ANISOU 1640 CA ALA B 31 3741 4931 5898 -1201 295 -535 C ATOM 1641 C ALA B 31 20.474 6.553 49.235 1.00 38.78 C ANISOU 1641 C ALA B 31 3540 5084 6113 -1174 306 -410 C ATOM 1642 O ALA B 31 19.863 5.479 49.458 1.00 36.79 O ANISOU 1642 O ALA B 31 3268 4889 5820 -1066 318 -356 O ATOM 1643 CB ALA B 31 20.116 8.384 50.891 1.00 40.15 C ANISOU 1643 CB ALA B 31 4053 5203 6000 -1306 116 -589 C ATOM 1644 N PHE B 32 21.694 6.608 48.708 1.00 39.64 N ANISOU 1644 N PHE B 32 3461 5211 6389 -1274 306 -377 N ATOM 1645 CA PHE B 32 22.376 5.390 48.292 1.00 40.71 C ANISOU 1645 CA PHE B 32 3339 5432 6695 -1172 326 -305 C ATOM 1646 C PHE B 32 23.848 5.617 48.438 1.00 43.54 C ANISOU 1646 C PHE B 32 3428 5924 7192 -1301 231 -310 C ATOM 1647 O PHE B 32 24.324 6.735 48.252 1.00 43.66 O ANISOU 1647 O PHE B 32 3457 5942 7189 -1530 249 -357 O ATOM 1648 CB PHE B 32 22.120 5.069 46.808 1.00 39.81 C ANISOU 1648 CB PHE B 32 3203 5265 6657 -1095 550 -312 C ATOM 1649 CG PHE B 32 20.667 4.891 46.435 1.00 36.90 C ANISOU 1649 CG PHE B 32 3057 4804 6162 -988 646 -319 C ATOM 1650 CD1 PHE B 32 19.930 5.972 45.955 1.00 36.87 C ANISOU 1650 CD1 PHE B 32 3256 4705 6049 -1026 715 -379 C ATOM 1651 CD2 PHE B 32 20.069 3.646 46.491 1.00 37.07 C ANISOU 1651 CD2 PHE B 32 3088 4829 6169 -856 649 -269 C ATOM 1652 CE1 PHE B 32 18.591 5.842 45.572 1.00 33.39 C ANISOU 1652 CE1 PHE B 32 2955 4235 5496 -902 782 -406 C ATOM 1653 CE2 PHE B 32 18.720 3.478 46.110 1.00 36.98 C ANISOU 1653 CE2 PHE B 32 3228 4792 6030 -806 738 -286 C ATOM 1654 CZ PHE B 32 17.978 4.595 45.649 1.00 35.42 C ANISOU 1654 CZ PHE B 32 3159 4562 5737 -813 805 -364 C ATOM 1655 N ARG B 33 24.581 4.557 48.747 1.00 45.89 N ANISOU 1655 N ARG B 33 3484 6335 7618 -1159 113 -265 N ATOM 1656 CA ARG B 33 26.034 4.643 48.634 1.00 49.90 C ANISOU 1656 CA ARG B 33 3616 7052 8292 -1230 51 -300 C ATOM 1657 C ARG B 33 26.463 4.444 47.180 1.00 50.74 C ANISOU 1657 C ARG B 33 3512 7236 8531 -1195 310 -359 C ATOM 1658 O ARG B 33 27.473 4.979 46.745 1.00 53.01 O ANISOU 1658 O ARG B 33 3519 7726 8895 -1383 379 -421 O ATOM 1659 CB ARG B 33 26.721 3.689 49.603 1.00 52.08 C ANISOU 1659 CB ARG B 33 3703 7435 8649 -1047 -231 -251 C ATOM 1660 CG ARG B 33 26.951 4.338 50.959 1.00 54.11 C ANISOU 1660 CG ARG B 33 4035 7742 8781 -1234 -495 -227 C ATOM 1661 CD ARG B 33 27.419 3.342 51.974 1.00 56.04 C ANISOU 1661 CD ARG B 33 4198 8043 9052 -1039 -816 -146 C ATOM 1662 NE ARG B 33 27.676 3.986 53.255 1.00 59.32 N ANISOU 1662 NE ARG B 33 4695 8526 9319 -1245 -1078 -128 N ATOM 1663 CZ ARG B 33 27.982 3.337 54.373 1.00 61.87 C ANISOU 1663 CZ ARG B 33 5047 8880 9580 -1147 -1412 -39 C ATOM 1664 NH1 ARG B 33 28.064 2.016 54.376 1.00 63.23 N ANISOU 1664 NH1 ARG B 33 5204 8984 9836 -829 -1543 50 N ATOM 1665 NH2 ARG B 33 28.204 4.008 55.492 1.00 62.96 N ANISOU 1665 NH2 ARG B 33 5282 9088 9552 -1369 -1638 -37 N ATOM 1666 N ASN B 34 25.658 3.691 46.438 1.00 49.66 N ANISOU 1666 N ASN B 34 3523 6958 8388 -996 461 -347 N ATOM 1667 CA ASN B 34 25.858 3.468 45.005 1.00 51.16 C ANISOU 1667 CA ASN B 34 3599 7191 8648 -958 727 -412 C ATOM 1668 C ASN B 34 25.651 4.752 44.173 1.00 50.94 C ANISOU 1668 C ASN B 34 3723 7128 8505 -1268 922 -432 C ATOM 1669 O ASN B 34 24.519 5.221 44.027 1.00 47.98 O ANISOU 1669 O ASN B 34 3702 6543 7986 -1299 954 -396 O ATOM 1670 CB ASN B 34 24.892 2.369 44.518 1.00 49.11 C ANISOU 1670 CB ASN B 34 3548 6746 8366 -703 798 -389 C ATOM 1671 CG ASN B 34 25.076 2.040 43.056 1.00 50.92 C ANISOU 1671 CG ASN B 34 3694 7012 8640 -646 1063 -472 C ATOM 1672 OD1 ASN B 34 24.382 2.583 42.195 1.00 52.73 O ANISOU 1672 OD1 ASN B 34 4133 7150 8751 -779 1239 -470 O ATOM 1673 ND2 ASN B 34 26.022 1.158 42.761 1.00 52.55 N ANISOU 1673 ND2 ASN B 34 3602 7359 9005 -425 1082 -561 N ATOM 1674 N GLU B 35 26.737 5.281 43.605 1.00 54.10 N ANISOU 1674 N GLU B 35 3856 7744 8954 -1493 1041 -491 N ATOM 1675 CA GLU B 35 26.712 6.551 42.858 1.00 55.20 C ANISOU 1675 CA GLU B 35 4189 7831 8953 -1864 1191 -485 C ATOM 1676 C GLU B 35 25.888 6.563 41.567 1.00 53.39 C ANISOU 1676 C GLU B 35 4237 7435 8612 -1842 1413 -472 C ATOM 1677 O GLU B 35 25.286 7.568 41.228 1.00 51.96 O ANISOU 1677 O GLU B 35 4425 7048 8270 -2035 1426 -425 O ATOM 1678 CB GLU B 35 28.136 7.036 42.562 1.00 59.74 C ANISOU 1678 CB GLU B 35 4384 8738 9576 -2191 1281 -547 C ATOM 1679 CG GLU B 35 28.265 8.573 42.503 1.00 64.21 C ANISOU 1679 CG GLU B 35 5221 9207 9968 -2691 1273 -503 C ATOM 1680 CD GLU B 35 27.452 9.302 43.607 1.00 66.80 C ANISOU 1680 CD GLU B 35 5967 9218 10195 -2694 1010 -447 C ATOM 1681 OE1 GLU B 35 27.348 8.796 44.759 1.00 66.20 O ANISOU 1681 OE1 GLU B 35 5797 9162 10192 -2469 799 -450 O ATOM 1682 OE2 GLU B 35 26.915 10.398 43.318 1.00 68.88 O ANISOU 1682 OE2 GLU B 35 6683 9204 10283 -2915 1006 -409 O ATOM 1683 N GLU B 36 25.891 5.448 40.847 1.00 53.42 N ANISOU 1683 N GLU B 36 4091 7515 8693 -1595 1559 -523 N ATOM 1684 CA GLU B 36 25.061 5.262 39.654 1.00 53.10 C ANISOU 1684 CA GLU B 36 4312 7327 8538 -1542 1742 -517 C ATOM 1685 C GLU B 36 23.576 5.554 39.949 1.00 50.46 C ANISOU 1685 C GLU B 36 4398 6694 8082 -1448 1608 -437 C ATOM 1686 O GLU B 36 22.927 6.300 39.202 1.00 50.03 O ANISOU 1686 O GLU B 36 4654 6484 7869 -1571 1666 -402 O ATOM 1687 CB GLU B 36 25.260 3.841 39.087 1.00 53.51 C ANISOU 1687 CB GLU B 36 4158 7476 8698 -1236 1863 -607 C ATOM 1688 CG GLU B 36 26.774 3.468 38.885 1.00 58.31 C ANISOU 1688 CG GLU B 36 4259 8447 9449 -1229 1985 -741 C ATOM 1689 CD GLU B 36 27.516 3.209 40.207 1.00 60.73 C ANISOU 1689 CD GLU B 36 4251 8893 9931 -1103 1733 -749 C ATOM 1690 OE1 GLU B 36 26.998 2.466 41.055 1.00 62.83 O ANISOU 1690 OE1 GLU B 36 4630 8984 10260 -827 1512 -696 O ATOM 1691 OE2 GLU B 36 28.619 3.742 40.417 1.00 66.87 O ANISOU 1691 OE2 GLU B 36 4675 9968 10763 -1310 1742 -802 O ATOM 1692 N TYR B 37 23.071 5.007 41.060 1.00 49.16 N ANISOU 1692 N TYR B 37 4233 6475 7971 -1241 1418 -415 N ATOM 1693 CA TYR B 37 21.734 5.343 41.567 1.00 47.90 C ANISOU 1693 CA TYR B 37 4377 6133 7688 -1167 1293 -375 C ATOM 1694 C TYR B 37 21.578 6.793 42.016 1.00 48.47 C ANISOU 1694 C TYR B 37 4666 6099 7651 -1349 1189 -368 C ATOM 1695 O TYR B 37 20.519 7.391 41.805 1.00 47.51 O ANISOU 1695 O TYR B 37 4835 5819 7398 -1297 1155 -370 O ATOM 1696 CB TYR B 37 21.306 4.407 42.706 1.00 46.71 C ANISOU 1696 CB TYR B 37 4173 5998 7577 -975 1137 -353 C ATOM 1697 CG TYR B 37 20.694 3.097 42.253 1.00 47.18 C ANISOU 1697 CG TYR B 37 4258 6020 7647 -789 1190 -345 C ATOM 1698 CD1 TYR B 37 20.341 2.881 40.917 1.00 48.31 C ANISOU 1698 CD1 TYR B 37 4489 6116 7749 -773 1361 -372 C ATOM 1699 CD2 TYR B 37 20.431 2.083 43.172 1.00 49.48 C ANISOU 1699 CD2 TYR B 37 4544 6303 7955 -667 1051 -303 C ATOM 1700 CE1 TYR B 37 19.770 1.675 40.503 1.00 47.93 C ANISOU 1700 CE1 TYR B 37 4506 6013 7692 -637 1392 -375 C ATOM 1701 CE2 TYR B 37 19.846 0.868 42.776 1.00 50.02 C ANISOU 1701 CE2 TYR B 37 4707 6292 8006 -551 1077 -288 C ATOM 1702 CZ TYR B 37 19.514 0.669 41.447 1.00 50.05 C ANISOU 1702 CZ TYR B 37 4784 6248 7983 -535 1246 -332 C ATOM 1703 OH TYR B 37 18.943 -0.543 41.071 1.00 48.63 O ANISOU 1703 OH TYR B 37 4735 5972 7772 -452 1251 -327 O ATOM 1704 N ASN B 38 22.603 7.358 42.649 1.00 50.62 N ANISOU 1704 N ASN B 38 4809 6452 7970 -1544 1114 -375 N ATOM 1705 CA ASN B 38 22.521 8.772 43.054 1.00 52.41 C ANISOU 1705 CA ASN B 38 5314 6525 8075 -1747 998 -381 C ATOM 1706 C ASN B 38 22.415 9.692 41.846 1.00 53.43 C ANISOU 1706 C ASN B 38 5734 6489 8080 -1941 1102 -355 C ATOM 1707 O ASN B 38 21.608 10.618 41.840 1.00 53.24 O ANISOU 1707 O ASN B 38 6098 6214 7915 -1917 998 -360 O ATOM 1708 CB ASN B 38 23.685 9.182 43.957 1.00 54.36 C ANISOU 1708 CB ASN B 38 5376 6900 8378 -1979 878 -393 C ATOM 1709 CG ASN B 38 23.463 8.770 45.393 1.00 55.25 C ANISOU 1709 CG ASN B 38 5422 7060 8509 -1816 682 -409 C ATOM 1710 OD1 ASN B 38 22.326 8.744 45.879 1.00 55.34 O ANISOU 1710 OD1 ASN B 38 5648 6956 8422 -1621 620 -429 O ATOM 1711 ND2 ASN B 38 24.541 8.441 46.085 1.00 56.94 N ANISOU 1711 ND2 ASN B 38 5326 7479 8830 -1901 579 -408 N ATOM 1712 N LYS B 39 23.195 9.378 40.814 1.00 54.72 N ANISOU 1712 N LYS B 39 5718 6796 8277 -2102 1301 -337 N ATOM 1713 CA LYS B 39 23.246 10.150 39.572 1.00 56.85 C ANISOU 1713 CA LYS B 39 6266 6944 8391 -2358 1424 -290 C ATOM 1714 C LYS B 39 21.882 10.176 38.889 1.00 54.93 C ANISOU 1714 C LYS B 39 6375 6469 8028 -2120 1402 -265 C ATOM 1715 O LYS B 39 21.427 11.225 38.446 1.00 56.58 O ANISOU 1715 O LYS B 39 7017 6413 8067 -2224 1316 -220 O ATOM 1716 CB LYS B 39 24.293 9.553 38.621 1.00 58.48 C ANISOU 1716 CB LYS B 39 6136 7441 8642 -2535 1689 -310 C ATOM 1717 CG LYS B 39 25.063 10.555 37.775 1.00 63.20 C ANISOU 1717 CG LYS B 39 6887 8055 9071 -3035 1818 -264 C ATOM 1718 CD LYS B 39 26.474 10.728 38.292 1.00 66.80 C ANISOU 1718 CD LYS B 39 6935 8833 9614 -3360 1855 -309 C ATOM 1719 CE LYS B 39 27.449 10.944 37.148 1.00 71.53 C ANISOU 1719 CE LYS B 39 7388 9701 10089 -3798 2143 -318 C ATOM 1720 NZ LYS B 39 28.856 11.026 37.635 1.00 74.23 N ANISOU 1720 NZ LYS B 39 7213 10465 10525 -4114 2192 -392 N ATOM 1721 N SER B 40 21.219 9.031 38.827 1.00 52.18 N ANISOU 1721 N SER B 40 5862 6209 7757 -1803 1445 -295 N ATOM 1722 CA SER B 40 19.954 8.940 38.111 1.00 50.91 C ANISOU 1722 CA SER B 40 5958 5903 7484 -1600 1424 -282 C ATOM 1723 C SER B 40 18.766 9.530 38.916 1.00 49.50 C ANISOU 1723 C SER B 40 6000 5564 7244 -1370 1198 -316 C ATOM 1724 O SER B 40 18.048 10.420 38.424 1.00 50.29 O ANISOU 1724 O SER B 40 6463 5448 7198 -1321 1089 -305 O ATOM 1725 CB SER B 40 19.704 7.494 37.637 1.00 49.39 C ANISOU 1725 CB SER B 40 5533 5866 7366 -1412 1559 -309 C ATOM 1726 OG SER B 40 19.162 6.688 38.666 1.00 49.76 O ANISOU 1726 OG SER B 40 5414 5983 7511 -1180 1459 -342 O ATOM 1727 N VAL B 41 18.596 9.058 40.151 1.00 47.31 N ANISOU 1727 N VAL B 41 5514 5401 7059 -1223 1119 -368 N ATOM 1728 CA VAL B 41 17.539 9.530 41.053 1.00 46.46 C ANISOU 1728 CA VAL B 41 5539 5233 6881 -1006 947 -443 C ATOM 1729 C VAL B 41 17.576 11.040 41.321 1.00 47.87 C ANISOU 1729 C VAL B 41 6073 5161 6952 -1071 789 -478 C ATOM 1730 O VAL B 41 16.530 11.660 41.435 1.00 48.14 O ANISOU 1730 O VAL B 41 6334 5073 6883 -833 655 -558 O ATOM 1731 CB VAL B 41 17.540 8.756 42.385 1.00 45.06 C ANISOU 1731 CB VAL B 41 5095 5248 6780 -925 912 -481 C ATOM 1732 CG1 VAL B 41 16.569 9.378 43.357 1.00 46.78 C ANISOU 1732 CG1 VAL B 41 5439 5450 6887 -744 770 -591 C ATOM 1733 CG2 VAL B 41 17.168 7.310 42.141 1.00 44.24 C ANISOU 1733 CG2 VAL B 41 4768 5308 6733 -824 1011 -451 C ATOM 1734 N GLN B 42 18.777 11.608 41.424 1.00 49.44 N ANISOU 1734 N GLN B 42 6319 5295 7172 -1389 794 -433 N ATOM 1735 CA GLN B 42 18.992 13.062 41.521 1.00 51.98 C ANISOU 1735 CA GLN B 42 7065 5316 7369 -1554 640 -444 C ATOM 1736 C GLN B 42 18.037 13.879 40.652 1.00 53.04 C ANISOU 1736 C GLN B 42 7658 5149 7346 -1390 526 -442 C ATOM 1737 O GLN B 42 17.462 14.848 41.134 1.00 54.43 O ANISOU 1737 O GLN B 42 8181 5077 7424 -1221 320 -532 O ATOM 1738 CB GLN B 42 20.443 13.420 41.168 1.00 53.97 C ANISOU 1738 CB GLN B 42 7296 5580 7631 -2035 724 -355 C ATOM 1739 CG GLN B 42 20.734 14.918 41.026 1.00 59.35 C ANISOU 1739 CG GLN B 42 8507 5901 8142 -2324 569 -329 C ATOM 1740 CD GLN B 42 21.286 15.552 42.295 1.00 62.52 C ANISOU 1740 CD GLN B 42 8960 6250 8544 -2486 410 -401 C ATOM 1741 OE1 GLN B 42 22.481 15.849 42.377 1.00 65.52 O ANISOU 1741 OE1 GLN B 42 9257 6710 8927 -2940 440 -353 O ATOM 1742 NE2 GLN B 42 20.420 15.761 43.292 1.00 61.21 N ANISOU 1742 NE2 GLN B 42 8913 5988 8355 -2135 245 -534 N ATOM 1743 N GLU B 43 17.865 13.490 39.385 1.00 52.64 N ANISOU 1743 N GLU B 43 7629 5113 7260 -1411 639 -353 N ATOM 1744 CA GLU B 43 17.061 14.288 38.440 1.00 55.28 C ANISOU 1744 CA GLU B 43 8437 5145 7422 -1283 493 -321 C ATOM 1745 C GLU B 43 15.525 14.189 38.562 1.00 53.88 C ANISOU 1745 C GLU B 43 8272 4981 7218 -767 341 -437 C ATOM 1746 O GLU B 43 14.800 14.979 37.951 1.00 56.45 O ANISOU 1746 O GLU B 43 9005 5039 7406 -577 144 -439 O ATOM 1747 CB GLU B 43 17.527 14.067 36.995 1.00 56.19 C ANISOU 1747 CB GLU B 43 8644 5256 7449 -1562 651 -176 C ATOM 1748 CG GLU B 43 18.547 15.150 36.533 1.00 64.21 C ANISOU 1748 CG GLU B 43 10071 6014 8312 -2054 636 -59 C ATOM 1749 CD GLU B 43 18.864 15.113 35.027 1.00 70.46 C ANISOU 1749 CD GLU B 43 11061 6780 8931 -2351 780 83 C ATOM 1750 OE1 GLU B 43 20.030 15.393 34.664 1.00 74.47 O ANISOU 1750 OE1 GLU B 43 11597 7338 9361 -2865 939 167 O ATOM 1751 OE2 GLU B 43 17.959 14.813 34.201 1.00 72.07 O ANISOU 1751 OE2 GLU B 43 11383 6947 9053 -2100 739 105 O ATOM 1752 N ILE B 44 15.051 13.238 39.364 1.00 50.78 N ANISOU 1752 N ILE B 44 7440 4912 6943 -559 418 -535 N ATOM 1753 CA ILE B 44 13.621 12.981 39.558 1.00 49.44 C ANISOU 1753 CA ILE B 44 7149 4890 6745 -132 325 -665 C ATOM 1754 C ILE B 44 13.078 14.038 40.473 1.00 51.32 C ANISOU 1754 C ILE B 44 7608 4977 6916 142 114 -834 C ATOM 1755 O ILE B 44 13.466 14.122 41.636 1.00 51.76 O ANISOU 1755 O ILE B 44 7565 5095 7008 86 130 -913 O ATOM 1756 CB ILE B 44 13.357 11.598 40.212 1.00 46.46 C ANISOU 1756 CB ILE B 44 6259 4918 6474 -96 489 -705 C ATOM 1757 CG1 ILE B 44 13.896 10.466 39.344 1.00 43.80 C ANISOU 1757 CG1 ILE B 44 5729 4703 6209 -318 685 -571 C ATOM 1758 CG2 ILE B 44 11.877 11.389 40.471 1.00 46.32 C ANISOU 1758 CG2 ILE B 44 6081 5122 6396 267 409 -853 C ATOM 1759 CD1 ILE B 44 13.797 9.068 39.992 1.00 39.60 C ANISOU 1759 CD1 ILE B 44 4793 4481 5774 -327 815 -584 C ATOM 1760 N GLN B 45 12.176 14.849 39.946 1.00 53.12 N ANISOU 1760 N GLN B 45 8152 5001 7030 464 -102 -904 N ATOM 1761 CA GLN B 45 11.570 15.924 40.727 1.00 55.41 C ANISOU 1761 CA GLN B 45 8698 5112 7242 823 -330 -1111 C ATOM 1762 C GLN B 45 10.397 15.411 41.555 1.00 54.74 C ANISOU 1762 C GLN B 45 8176 5454 7168 1216 -301 -1340 C ATOM 1763 O GLN B 45 10.224 15.816 42.693 1.00 56.37 O ANISOU 1763 O GLN B 45 8363 5711 7343 1380 -338 -1533 O ATOM 1764 CB GLN B 45 11.148 17.061 39.803 1.00 58.37 C ANISOU 1764 CB GLN B 45 9650 5045 7483 1045 -621 -1096 C ATOM 1765 CG GLN B 45 12.293 17.531 38.916 1.00 59.10 C ANISOU 1765 CG GLN B 45 10195 4750 7511 560 -622 -847 C ATOM 1766 CD GLN B 45 11.849 18.477 37.834 1.00 61.06 C ANISOU 1766 CD GLN B 45 11051 4559 7588 723 -914 -774 C ATOM 1767 OE1 GLN B 45 11.271 18.067 36.828 1.00 59.77 O ANISOU 1767 OE1 GLN B 45 10837 4492 7382 840 -939 -697 O ATOM 1768 NE2 GLN B 45 12.111 19.766 38.039 1.00 66.15 N ANISOU 1768 NE2 GLN B 45 12330 4690 8114 725 -1169 -795 N ATOM 1769 N ALA B 46 9.600 14.523 40.971 1.00 53.28 N ANISOU 1769 N ALA B 46 7648 5597 7000 1327 -228 -1326 N ATOM 1770 CA ALA B 46 8.453 13.918 41.634 1.00 52.72 C ANISOU 1770 CA ALA B 46 7106 6012 6912 1606 -171 -1526 C ATOM 1771 C ALA B 46 8.181 12.607 40.935 1.00 50.29 C ANISOU 1771 C ALA B 46 6441 6021 6648 1418 -12 -1396 C ATOM 1772 O ALA B 46 8.635 12.390 39.802 1.00 49.70 O ANISOU 1772 O ALA B 46 6532 5758 6593 1222 -3 -1202 O ATOM 1773 CB ALA B 46 7.246 14.813 41.552 1.00 56.81 C ANISOU 1773 CB ALA B 46 7722 6529 7333 2169 -419 -1766 C ATOM 1774 N THR B 47 7.463 11.721 41.615 1.00 49.05 N ANISOU 1774 N THR B 47 5820 6340 6475 1438 120 -1504 N ATOM 1775 CA THR B 47 7.034 10.451 41.032 1.00 46.58 C ANISOU 1775 CA THR B 47 5188 6335 6173 1258 244 -1410 C ATOM 1776 C THR B 47 5.840 9.893 41.796 1.00 47.58 C ANISOU 1776 C THR B 47 4855 7013 6213 1375 309 -1604 C ATOM 1777 O THR B 47 5.852 9.815 43.031 1.00 47.58 O ANISOU 1777 O THR B 47 4699 7208 6170 1335 410 -1711 O ATOM 1778 CB THR B 47 8.198 9.400 40.953 1.00 43.48 C ANISOU 1778 CB THR B 47 4778 5859 5884 800 445 -1182 C ATOM 1779 OG1 THR B 47 9.139 9.819 39.964 1.00 41.80 O ANISOU 1779 OG1 THR B 47 4912 5250 5721 673 414 -1020 O ATOM 1780 CG2 THR B 47 7.710 8.009 40.558 1.00 41.54 C ANISOU 1780 CG2 THR B 47 4244 5911 5628 612 565 -1116 C ATOM 1781 N PHE B 48 4.802 9.541 41.046 1.00 48.27 N ANISOU 1781 N PHE B 48 4725 7372 6244 1495 244 -1654 N ATOM 1782 CA PHE B 48 3.783 8.622 41.546 1.00 48.42 C ANISOU 1782 CA PHE B 48 4253 7976 6169 1404 362 -1770 C ATOM 1783 C PHE B 48 3.587 7.414 40.612 1.00 46.33 C ANISOU 1783 C PHE B 48 3871 7830 5902 1085 419 -1605 C ATOM 1784 O PHE B 48 3.894 7.496 39.418 1.00 44.81 O ANISOU 1784 O PHE B 48 3931 7340 5756 1085 320 -1471 O ATOM 1785 CB PHE B 48 2.470 9.338 41.858 1.00 51.87 C ANISOU 1785 CB PHE B 48 4399 8811 6497 1865 237 -2085 C ATOM 1786 CG PHE B 48 1.844 10.048 40.689 1.00 54.30 C ANISOU 1786 CG PHE B 48 4814 9011 6805 2261 -41 -2141 C ATOM 1787 CD1 PHE B 48 2.157 11.386 40.414 1.00 56.59 C ANISOU 1787 CD1 PHE B 48 5548 8826 7127 2657 -276 -2185 C ATOM 1788 CD2 PHE B 48 0.875 9.416 39.912 1.00 55.73 C ANISOU 1788 CD2 PHE B 48 4673 9575 6928 2243 -103 -2160 C ATOM 1789 CE1 PHE B 48 1.552 12.068 39.357 1.00 58.05 C ANISOU 1789 CE1 PHE B 48 5893 8878 7285 3049 -584 -2224 C ATOM 1790 CE2 PHE B 48 0.258 10.087 38.847 1.00 58.07 C ANISOU 1790 CE2 PHE B 48 5070 9789 7206 2637 -407 -2213 C ATOM 1791 CZ PHE B 48 0.599 11.417 38.569 1.00 59.40 C ANISOU 1791 CZ PHE B 48 5717 9448 7405 3058 -657 -2238 C ATOM 1792 N PHE B 49 3.098 6.303 41.169 1.00 45.71 N ANISOU 1792 N PHE B 49 3459 8167 5743 782 575 -1616 N ATOM 1793 CA PHE B 49 2.917 5.056 40.410 1.00 45.15 C ANISOU 1793 CA PHE B 49 3322 8186 5647 425 628 -1470 C ATOM 1794 C PHE B 49 1.827 4.155 41.006 1.00 47.21 C ANISOU 1794 C PHE B 49 3150 9045 5743 171 727 -1571 C ATOM 1795 O PHE B 49 1.383 4.381 42.129 1.00 49.24 O ANISOU 1795 O PHE B 49 3156 9652 5902 216 810 -1732 O ATOM 1796 CB PHE B 49 4.255 4.287 40.293 1.00 41.92 C ANISOU 1796 CB PHE B 49 3223 7354 5350 93 747 -1225 C ATOM 1797 CG PHE B 49 4.791 3.815 41.607 1.00 41.46 C ANISOU 1797 CG PHE B 49 3135 7331 5285 -125 888 -1185 C ATOM 1798 CD1 PHE B 49 5.687 4.598 42.324 1.00 41.01 C ANISOU 1798 CD1 PHE B 49 3246 7027 5311 6 892 -1186 C ATOM 1799 CD2 PHE B 49 4.383 2.602 42.136 1.00 40.36 C ANISOU 1799 CD2 PHE B 49 2838 7466 5032 -490 992 -1140 C ATOM 1800 CE1 PHE B 49 6.174 4.164 43.548 1.00 42.59 C ANISOU 1800 CE1 PHE B 49 3431 7270 5482 -195 988 -1144 C ATOM 1801 CE2 PHE B 49 4.851 2.167 43.348 1.00 40.16 C ANISOU 1801 CE2 PHE B 49 2839 7457 4965 -699 1086 -1084 C ATOM 1802 CZ PHE B 49 5.742 2.935 44.057 1.00 43.83 C ANISOU 1802 CZ PHE B 49 3445 7693 5514 -538 1080 -1087 C ATOM 1803 N TYR B 50 1.387 3.152 40.244 1.00 47.51 N ANISOU 1803 N TYR B 50 3117 9213 5721 -127 723 -1487 N ATOM 1804 CA TYR B 50 0.416 2.154 40.713 1.00 49.51 C ANISOU 1804 CA TYR B 50 3010 10009 5790 -507 818 -1543 C ATOM 1805 C TYR B 50 1.029 0.751 40.698 1.00 47.67 C ANISOU 1805 C TYR B 50 3033 9537 5542 -1035 925 -1310 C ATOM 1806 O TYR B 50 1.709 0.399 39.753 1.00 44.47 O ANISOU 1806 O TYR B 50 2951 8703 5242 -1078 878 -1160 O ATOM 1807 CB TYR B 50 -0.826 2.141 39.813 1.00 52.61 C ANISOU 1807 CB TYR B 50 3081 10823 6086 -439 673 -1673 C ATOM 1808 CG TYR B 50 -1.626 3.412 39.836 1.00 56.05 C ANISOU 1808 CG TYR B 50 3213 11570 6514 123 525 -1939 C ATOM 1809 CD1 TYR B 50 -1.264 4.500 39.043 1.00 55.38 C ANISOU 1809 CD1 TYR B 50 3411 11072 6559 610 317 -1940 C ATOM 1810 CD2 TYR B 50 -2.759 3.528 40.639 1.00 59.39 C ANISOU 1810 CD2 TYR B 50 3079 12706 6780 173 585 -2202 C ATOM 1811 CE1 TYR B 50 -1.999 5.679 39.071 1.00 58.42 C ANISOU 1811 CE1 TYR B 50 3587 11677 6934 1185 131 -2191 C ATOM 1812 CE2 TYR B 50 -3.500 4.699 40.676 1.00 62.80 C ANISOU 1812 CE2 TYR B 50 3220 13430 7212 776 432 -2490 C ATOM 1813 CZ TYR B 50 -3.115 5.769 39.888 1.00 62.50 C ANISOU 1813 CZ TYR B 50 3526 12902 7321 1304 184 -2480 C ATOM 1814 OH TYR B 50 -3.839 6.934 39.913 1.00 64.03 O ANISOU 1814 OH TYR B 50 3506 13311 7513 1953 -18 -2767 O ATOM 1815 N PHE B 51 0.758 -0.054 41.730 1.00 49.46 N ANISOU 1815 N PHE B 51 3137 10042 5613 -1432 1059 -1290 N ATOM 1816 CA PHE B 51 1.119 -1.479 41.722 1.00 49.18 C ANISOU 1816 CA PHE B 51 3370 9799 5516 -1949 1110 -1082 C ATOM 1817 C PHE B 51 -0.133 -2.327 41.518 1.00 52.91 C ANISOU 1817 C PHE B 51 3576 10773 5757 -2385 1112 -1132 C ATOM 1818 O PHE B 51 -1.075 -2.246 42.317 1.00 55.68 O ANISOU 1818 O PHE B 51 3523 11723 5909 -2538 1196 -1277 O ATOM 1819 CB PHE B 51 1.756 -1.908 43.045 1.00 48.70 C ANISOU 1819 CB PHE B 51 3471 9633 5401 -2177 1219 -974 C ATOM 1820 CG PHE B 51 3.234 -1.606 43.176 1.00 47.98 C ANISOU 1820 CG PHE B 51 3740 8957 5534 -1936 1199 -845 C ATOM 1821 CD1 PHE B 51 3.761 -1.261 44.418 1.00 49.44 C ANISOU 1821 CD1 PHE B 51 3957 9126 5702 -1896 1253 -838 C ATOM 1822 CD2 PHE B 51 4.099 -1.693 42.091 1.00 46.84 C ANISOU 1822 CD2 PHE B 51 3881 8326 5589 -1783 1133 -744 C ATOM 1823 CE1 PHE B 51 5.127 -1.011 44.577 1.00 48.54 C ANISOU 1823 CE1 PHE B 51 4127 8529 5786 -1712 1216 -725 C ATOM 1824 CE2 PHE B 51 5.461 -1.445 42.243 1.00 47.66 C ANISOU 1824 CE2 PHE B 51 4241 7981 5886 -1599 1131 -646 C ATOM 1825 CZ PHE B 51 5.973 -1.097 43.487 1.00 47.95 C ANISOU 1825 CZ PHE B 51 4278 8018 5922 -1564 1159 -635 C ATOM 1826 N THR B 52 -0.146 -3.142 40.462 1.00 53.32 N ANISOU 1826 N THR B 52 3843 10609 5809 -2611 1028 -1029 N ATOM 1827 CA THR B 52 -1.230 -4.116 40.259 1.00 57.68 C ANISOU 1827 CA THR B 52 4222 11572 6120 -3144 1014 -1045 C ATOM 1828 C THR B 52 -0.663 -5.545 40.318 1.00 57.68 C ANISOU 1828 C THR B 52 4729 11137 6051 -3657 1026 -821 C ATOM 1829 O THR B 52 -0.160 -6.061 39.325 1.00 56.58 O ANISOU 1829 O THR B 52 4958 10540 6000 -3663 939 -730 O ATOM 1830 CB THR B 52 -2.031 -3.860 38.949 1.00 59.16 C ANISOU 1830 CB THR B 52 4196 11982 6300 -3015 854 -1161 C ATOM 1831 OG1 THR B 52 -2.666 -2.572 39.011 1.00 59.26 O ANISOU 1831 OG1 THR B 52 3740 12424 6351 -2518 803 -1383 O ATOM 1832 CG2 THR B 52 -3.090 -4.940 38.740 1.00 62.85 C ANISOU 1832 CG2 THR B 52 4503 12870 6507 -3643 826 -1169 C ATOM 1833 N PRO B 53 -0.698 -6.167 41.505 1.00 59.56 N ANISOU 1833 N PRO B 53 5031 11484 6115 -4064 1124 -735 N ATOM 1834 CA PRO B 53 -0.114 -7.488 41.643 1.00 60.10 C ANISOU 1834 CA PRO B 53 5659 11064 6113 -4499 1088 -514 C ATOM 1835 C PRO B 53 -0.831 -8.512 40.790 1.00 63.13 C ANISOU 1835 C PRO B 53 6174 11490 6324 -4991 996 -488 C ATOM 1836 O PRO B 53 -2.058 -8.449 40.622 1.00 66.04 O ANISOU 1836 O PRO B 53 6103 12487 6502 -5262 1003 -619 O ATOM 1837 CB PRO B 53 -0.314 -7.801 43.122 1.00 62.68 C ANISOU 1837 CB PRO B 53 5956 11650 6208 -4883 1193 -448 C ATOM 1838 CG PRO B 53 -0.289 -6.475 43.763 1.00 61.88 C ANISOU 1838 CG PRO B 53 5443 11869 6200 -4409 1295 -609 C ATOM 1839 CD PRO B 53 -1.056 -5.602 42.811 1.00 61.40 C ANISOU 1839 CD PRO B 53 4920 12185 6223 -4062 1260 -831 C ATOM 1840 N ASN B 54 -0.039 -9.411 40.215 1.00 62.63 N ANISOU 1840 N ASN B 54 6699 10764 6333 -5066 900 -345 N ATOM 1841 CA ASN B 54 -0.540 -10.640 39.623 1.00 66.36 C ANISOU 1841 CA ASN B 54 7493 11117 6602 -5632 796 -282 C ATOM 1842 C ASN B 54 0.035 -11.781 40.447 1.00 67.87 C ANISOU 1842 C ASN B 54 8279 10835 6675 -6016 754 -71 C ATOM 1843 O ASN B 54 1.188 -12.195 40.255 1.00 65.54 O ANISOU 1843 O ASN B 54 8495 9850 6559 -5743 680 26 O ATOM 1844 CB ASN B 54 -0.141 -10.754 38.151 1.00 65.17 C ANISOU 1844 CB ASN B 54 7599 10557 6606 -5365 692 -327 C ATOM 1845 CG ASN B 54 -1.000 -11.747 37.382 1.00 70.14 C ANISOU 1845 CG ASN B 54 8403 11255 6992 -5941 574 -338 C ATOM 1846 OD1 ASN B 54 -1.662 -12.627 37.954 1.00 75.28 O ANISOU 1846 OD1 ASN B 54 9165 12075 7364 -6609 550 -260 O ATOM 1847 ND2 ASN B 54 -0.987 -11.612 36.064 1.00 71.97 N ANISOU 1847 ND2 ASN B 54 8693 11354 7300 -5726 491 -431 N ATOM 1848 N LYS B 55 -0.790 -12.264 41.378 1.00 71.74 N ANISOU 1848 N LYS B 55 8686 11729 6843 -6648 797 -8 N ATOM 1849 CA LYS B 55 -0.374 -13.218 42.402 1.00 74.32 C ANISOU 1849 CA LYS B 55 9559 11691 6990 -7062 747 214 C ATOM 1850 C LYS B 55 -0.004 -14.559 41.789 1.00 76.42 C ANISOU 1850 C LYS B 55 10594 11248 7194 -7359 548 351 C ATOM 1851 O LYS B 55 0.990 -15.190 42.176 1.00 76.19 O ANISOU 1851 O LYS B 55 11172 10547 7230 -7246 426 512 O ATOM 1852 CB LYS B 55 -1.471 -13.382 43.465 1.00 78.49 C ANISOU 1852 CB LYS B 55 9794 12906 7122 -7755 864 237 C ATOM 1853 CG LYS B 55 -1.927 -12.067 44.107 1.00 77.79 C ANISOU 1853 CG LYS B 55 8929 13566 7060 -7443 1072 48 C ATOM 1854 CD LYS B 55 -2.675 -12.298 45.406 1.00 84.99 C ANISOU 1854 CD LYS B 55 9668 15055 7570 -8084 1218 90 C ATOM 1855 CE LYS B 55 -3.552 -11.111 45.784 1.00 87.11 C ANISOU 1855 CE LYS B 55 9051 16255 7790 -7878 1436 -190 C ATOM 1856 NZ LYS B 55 -4.730 -10.978 44.860 1.00 90.47 N ANISOU 1856 NZ LYS B 55 8921 17300 8152 -8033 1442 -399 N ATOM 1857 N THR B 56 -0.811 -14.971 40.819 1.00 79.11 N ANISOU 1857 N THR B 56 10908 11744 7407 -7706 492 268 N ATOM 1858 CA THR B 56 -0.617 -16.226 40.114 1.00 82.16 C ANISOU 1858 CA THR B 56 12027 11491 7699 -8023 297 351 C ATOM 1859 C THR B 56 0.706 -16.260 39.331 1.00 78.60 C ANISOU 1859 C THR B 56 11989 10279 7594 -7304 216 319 C ATOM 1860 O THR B 56 1.364 -17.300 39.252 1.00 80.57 O ANISOU 1860 O THR B 56 12981 9807 7824 -7362 50 422 O ATOM 1861 CB THR B 56 -1.776 -16.434 39.160 1.00 84.73 C ANISOU 1861 CB THR B 56 12122 12238 7834 -8480 262 224 C ATOM 1862 OG1 THR B 56 -2.994 -16.434 39.916 1.00 90.74 O ANISOU 1862 OG1 THR B 56 12438 13779 8259 -9173 355 231 O ATOM 1863 CG2 THR B 56 -1.623 -17.741 38.389 1.00 88.47 C ANISOU 1863 CG2 THR B 56 13404 12031 8180 -8842 49 285 C ATOM 1864 N GLU B 57 1.094 -15.122 38.764 1.00 74.01 N ANISOU 1864 N GLU B 57 10939 9869 7312 -6629 329 167 N ATOM 1865 CA GLU B 57 2.268 -15.073 37.894 1.00 70.98 C ANISOU 1865 CA GLU B 57 10847 8898 7225 -5996 299 101 C ATOM 1866 C GLU B 57 3.569 -14.598 38.577 1.00 67.60 C ANISOU 1866 C GLU B 57 10444 8162 7077 -5400 345 156 C ATOM 1867 O GLU B 57 4.627 -14.576 37.934 1.00 65.38 O ANISOU 1867 O GLU B 57 10366 7437 7038 -4882 339 91 O ATOM 1868 CB GLU B 57 1.963 -14.230 36.645 1.00 68.87 C ANISOU 1868 CB GLU B 57 10169 8926 7071 -5687 367 -89 C ATOM 1869 CG GLU B 57 0.722 -14.678 35.858 1.00 72.76 C ANISOU 1869 CG GLU B 57 10614 9735 7297 -6236 283 -161 C ATOM 1870 CD GLU B 57 0.958 -15.935 35.040 1.00 76.99 C ANISOU 1870 CD GLU B 57 11875 9657 7721 -6477 131 -163 C ATOM 1871 OE1 GLU B 57 2.123 -16.192 34.675 1.00 77.05 O ANISOU 1871 OE1 GLU B 57 12306 9049 7923 -6016 123 -184 O ATOM 1872 OE2 GLU B 57 -0.019 -16.663 34.754 1.00 81.04 O ANISOU 1872 OE2 GLU B 57 12529 10320 7945 -7127 19 -163 O ATOM 1873 N ASP B 58 3.498 -14.239 39.863 1.00 67.08 N ANISOU 1873 N ASP B 58 10165 8363 6960 -5496 393 261 N ATOM 1874 CA ASP B 58 4.652 -13.664 40.587 1.00 64.10 C ANISOU 1874 CA ASP B 58 9735 7792 6829 -4966 423 307 C ATOM 1875 C ASP B 58 5.254 -12.428 39.903 1.00 60.15 C ANISOU 1875 C ASP B 58 8808 7403 6642 -4317 554 151 C ATOM 1876 O ASP B 58 6.497 -12.283 39.787 1.00 58.41 O ANISOU 1876 O ASP B 58 8718 6798 6677 -3823 545 142 O ATOM 1877 CB ASP B 58 5.744 -14.715 40.826 1.00 65.77 C ANISOU 1877 CB ASP B 58 10623 7260 7108 -4834 239 428 C ATOM 1878 CG ASP B 58 5.446 -15.619 42.025 1.00 69.59 C ANISOU 1878 CG ASP B 58 11529 7612 7300 -5379 91 647 C ATOM 1879 OD1 ASP B 58 4.331 -15.557 42.579 1.00 70.27 O ANISOU 1879 OD1 ASP B 58 11398 8205 7096 -5953 162 697 O ATOM 1880 OD2 ASP B 58 6.345 -16.388 42.414 1.00 70.30 O ANISOU 1880 OD2 ASP B 58 12170 7102 7438 -5224 -104 765 O ATOM 1881 N THR B 59 4.370 -11.540 39.446 1.00 58.63 N ANISOU 1881 N THR B 59 8112 7749 6415 -4328 660 26 N ATOM 1882 CA THR B 59 4.783 -10.242 38.909 1.00 54.79 C ANISOU 1882 CA THR B 59 7241 7407 6169 -3783 764 -98 C ATOM 1883 C THR B 59 3.907 -9.114 39.463 1.00 54.17 C ANISOU 1883 C THR B 59 6587 7968 6029 -3776 851 -174 C ATOM 1884 O THR B 59 2.821 -9.362 39.996 1.00 56.22 O ANISOU 1884 O THR B 59 6662 8656 6044 -4213 857 -174 O ATOM 1885 CB THR B 59 4.694 -10.193 37.378 1.00 54.31 C ANISOU 1885 CB THR B 59 7228 7254 6154 -3646 760 -215 C ATOM 1886 OG1 THR B 59 3.321 -10.302 36.982 1.00 57.19 O ANISOU 1886 OG1 THR B 59 7390 8051 6289 -4041 720 -274 O ATOM 1887 CG2 THR B 59 5.528 -11.311 36.730 1.00 55.71 C ANISOU 1887 CG2 THR B 59 7976 6815 6375 -3611 692 -199 C ATOM 1888 N ILE B 60 4.384 -7.881 39.325 1.00 50.77 N ANISOU 1888 N ILE B 60 5883 7604 5802 -3287 918 -255 N ATOM 1889 CA ILE B 60 3.600 -6.698 39.670 1.00 50.73 C ANISOU 1889 CA ILE B 60 5371 8141 5764 -3154 974 -373 C ATOM 1890 C ILE B 60 3.556 -5.767 38.465 1.00 49.19 C ANISOU 1890 C ILE B 60 5025 7973 5693 -2779 956 -489 C ATOM 1891 O ILE B 60 4.607 -5.417 37.902 1.00 46.86 O ANISOU 1891 O ILE B 60 4919 7295 5592 -2452 973 -470 O ATOM 1892 CB ILE B 60 4.203 -5.928 40.870 1.00 49.33 C ANISOU 1892 CB ILE B 60 5068 7996 5679 -2917 1037 -357 C ATOM 1893 CG1 ILE B 60 4.293 -6.825 42.105 1.00 50.44 C ANISOU 1893 CG1 ILE B 60 5409 8094 5664 -3293 1031 -220 C ATOM 1894 CG2 ILE B 60 3.385 -4.669 41.176 1.00 49.72 C ANISOU 1894 CG2 ILE B 60 4632 8569 5689 -2713 1085 -524 C ATOM 1895 CD1 ILE B 60 5.097 -6.225 43.235 1.00 51.18 C ANISOU 1895 CD1 ILE B 60 5480 8120 5846 -3070 1058 -182 C ATOM 1896 N PHE B 61 2.352 -5.355 38.085 1.00 50.37 N ANISOU 1896 N PHE B 61 4830 8595 5713 -2835 913 -609 N ATOM 1897 CA PHE B 61 2.188 -4.415 36.989 1.00 49.84 C ANISOU 1897 CA PHE B 61 4643 8571 5724 -2477 844 -707 C ATOM 1898 C PHE B 61 2.383 -2.992 37.502 1.00 48.64 C ANISOU 1898 C PHE B 61 4254 8532 5695 -2028 864 -785 C ATOM 1899 O PHE B 61 1.681 -2.533 38.406 1.00 50.38 O ANISOU 1899 O PHE B 61 4127 9180 5837 -2008 886 -883 O ATOM 1900 CB PHE B 61 0.828 -4.602 36.310 1.00 53.00 C ANISOU 1900 CB PHE B 61 4786 9418 5932 -2690 732 -807 C ATOM 1901 CG PHE B 61 0.627 -3.741 35.096 1.00 52.51 C ANISOU 1901 CG PHE B 61 4673 9364 5914 -2341 605 -885 C ATOM 1902 CD1 PHE B 61 -0.468 -2.868 35.026 1.00 55.44 C ANISOU 1902 CD1 PHE B 61 4594 10252 6217 -2135 484 -1038 C ATOM 1903 CD2 PHE B 61 1.526 -3.800 34.021 1.00 49.66 C ANISOU 1903 CD2 PHE B 61 4719 8509 5641 -2205 596 -816 C ATOM 1904 CE1 PHE B 61 -0.678 -2.070 33.897 1.00 56.53 C ANISOU 1904 CE1 PHE B 61 4744 10363 6372 -1798 310 -1090 C ATOM 1905 CE2 PHE B 61 1.337 -3.017 32.884 1.00 50.12 C ANISOU 1905 CE2 PHE B 61 4795 8560 5690 -1934 466 -864 C ATOM 1906 CZ PHE B 61 0.231 -2.136 32.820 1.00 54.07 C ANISOU 1906 CZ PHE B 61 4899 9525 6120 -1724 300 -985 C ATOM 1907 N LEU B 62 3.381 -2.326 36.938 1.00 46.15 N ANISOU 1907 N LEU B 62 4155 7825 5553 -1694 866 -750 N ATOM 1908 CA LEU B 62 3.802 -1.003 37.370 1.00 44.74 C ANISOU 1908 CA LEU B 62 3890 7612 5497 -1303 869 -798 C ATOM 1909 C LEU B 62 3.381 0.047 36.350 1.00 45.49 C ANISOU 1909 C LEU B 62 3946 7748 5590 -983 733 -879 C ATOM 1910 O LEU B 62 3.650 -0.106 35.171 1.00 44.59 O ANISOU 1910 O LEU B 62 4065 7404 5474 -989 691 -827 O ATOM 1911 CB LEU B 62 5.333 -0.984 37.528 1.00 41.37 C ANISOU 1911 CB LEU B 62 3759 6710 5249 -1216 960 -685 C ATOM 1912 CG LEU B 62 6.009 0.358 37.769 1.00 39.33 C ANISOU 1912 CG LEU B 62 3517 6309 5119 -878 956 -709 C ATOM 1913 CD1 LEU B 62 5.529 0.960 39.095 1.00 38.16 C ANISOU 1913 CD1 LEU B 62 3117 6451 4930 -789 954 -803 C ATOM 1914 CD2 LEU B 62 7.578 0.260 37.708 1.00 34.36 C ANISOU 1914 CD2 LEU B 62 3140 5259 4657 -857 1048 -601 C ATOM 1915 N ARG B 63 2.715 1.104 36.807 1.00 47.12 N ANISOU 1915 N ARG B 63 3890 8237 5777 -691 650 -1015 N ATOM 1916 CA ARG B 63 2.400 2.239 35.944 1.00 48.32 C ANISOU 1916 CA ARG B 63 4080 8349 5931 -314 467 -1083 C ATOM 1917 C ARG B 63 2.958 3.489 36.605 1.00 47.64 C ANISOU 1917 C ARG B 63 4075 8077 5950 32 456 -1126 C ATOM 1918 O ARG B 63 2.326 4.020 37.527 1.00 49.58 O ANISOU 1918 O ARG B 63 4042 8635 6163 221 434 -1284 O ATOM 1919 CB ARG B 63 0.877 2.350 35.752 1.00 52.59 C ANISOU 1919 CB ARG B 63 4222 9432 6329 -223 304 -1251 C ATOM 1920 CG ARG B 63 0.320 1.403 34.675 1.00 55.20 C ANISOU 1920 CG ARG B 63 4560 9875 6537 -519 227 -1207 C ATOM 1921 CD ARG B 63 -1.211 1.276 34.657 1.00 62.26 C ANISOU 1921 CD ARG B 63 4957 11423 7276 -545 86 -1381 C ATOM 1922 NE ARG B 63 -1.901 2.464 35.152 1.00 66.84 N ANISOU 1922 NE ARG B 63 5200 12330 7867 -59 -40 -1583 N ATOM 1923 CZ ARG B 63 -2.309 3.484 34.395 1.00 70.86 C ANISOU 1923 CZ ARG B 63 5725 12819 8377 409 -312 -1664 C ATOM 1924 NH1 ARG B 63 -2.109 3.483 33.077 1.00 69.55 N ANISOU 1924 NH1 ARG B 63 5900 12345 8180 411 -480 -1540 N ATOM 1925 NH2 ARG B 63 -2.933 4.515 34.966 1.00 74.21 N ANISOU 1925 NH2 ARG B 63 5853 13528 8815 894 -430 -1880 N ATOM 1926 N GLU B 64 4.139 3.950 36.182 1.00 45.34 N ANISOU 1926 N GLU B 64 4158 7307 5763 88 482 -1003 N ATOM 1927 CA GLU B 64 4.738 5.128 36.831 1.00 44.87 C ANISOU 1927 CA GLU B 64 4226 7036 5787 343 460 -1035 C ATOM 1928 C GLU B 64 4.702 6.411 36.050 1.00 45.85 C ANISOU 1928 C GLU B 64 4616 6914 5889 668 254 -1050 C ATOM 1929 O GLU B 64 4.840 6.424 34.820 1.00 45.35 O ANISOU 1929 O GLU B 64 4798 6657 5777 629 178 -951 O ATOM 1930 CB GLU B 64 6.161 4.910 37.397 1.00 42.75 C ANISOU 1930 CB GLU B 64 4138 6459 5646 152 635 -911 C ATOM 1931 CG GLU B 64 7.132 4.179 36.566 1.00 42.00 C ANISOU 1931 CG GLU B 64 4260 6093 5606 -87 749 -758 C ATOM 1932 CD GLU B 64 8.598 4.579 36.861 1.00 40.35 C ANISOU 1932 CD GLU B 64 4242 5564 5527 -134 849 -672 C ATOM 1933 OE1 GLU B 64 9.068 4.509 38.023 1.00 38.38 O ANISOU 1933 OE1 GLU B 64 3892 5338 5352 -175 909 -678 O ATOM 1934 OE2 GLU B 64 9.278 4.957 35.900 1.00 40.82 O ANISOU 1934 OE2 GLU B 64 4544 5374 5590 -161 865 -598 O ATOM 1935 N TYR B 65 4.542 7.484 36.826 1.00 46.54 N ANISOU 1935 N TYR B 65 4699 6990 5992 978 158 -1178 N ATOM 1936 CA TYR B 65 4.466 8.857 36.352 1.00 48.85 C ANISOU 1936 CA TYR B 65 5308 6999 6254 1341 -85 -1216 C ATOM 1937 C TYR B 65 5.538 9.683 37.065 1.00 48.71 C ANISOU 1937 C TYR B 65 5580 6615 6313 1343 -39 -1186 C ATOM 1938 O TYR B 65 5.416 10.051 38.244 1.00 49.24 O ANISOU 1938 O TYR B 65 5509 6800 6401 1486 -15 -1334 O ATOM 1939 CB TYR B 65 3.088 9.456 36.635 1.00 52.30 C ANISOU 1939 CB TYR B 65 5475 7780 6616 1798 -303 -1463 C ATOM 1940 CG TYR B 65 1.919 8.717 36.032 1.00 51.62 C ANISOU 1940 CG TYR B 65 5021 8150 6441 1797 -379 -1528 C ATOM 1941 CD1 TYR B 65 1.466 7.514 36.582 1.00 48.44 C ANISOU 1941 CD1 TYR B 65 4171 8220 6016 1485 -176 -1570 C ATOM 1942 CD2 TYR B 65 1.231 9.248 34.944 1.00 53.97 C ANISOU 1942 CD2 TYR B 65 5437 8414 6655 2092 -684 -1548 C ATOM 1943 CE1 TYR B 65 0.369 6.851 36.047 1.00 49.95 C ANISOU 1943 CE1 TYR B 65 4015 8857 6104 1423 -257 -1638 C ATOM 1944 CE2 TYR B 65 0.130 8.589 34.399 1.00 53.81 C ANISOU 1944 CE2 TYR B 65 5044 8857 6543 2078 -785 -1621 C ATOM 1945 CZ TYR B 65 -0.289 7.391 34.958 1.00 51.03 C ANISOU 1945 CZ TYR B 65 4223 8991 6174 1723 -559 -1671 C ATOM 1946 OH TYR B 65 -1.359 6.724 34.418 1.00 51.84 O ANISOU 1946 OH TYR B 65 3962 9566 6170 1633 -661 -1741 O ATOM 1947 N GLN B 66 6.576 9.990 36.305 1.00 48.03 N ANISOU 1947 N GLN B 66 5900 6108 6241 1155 -26 -1002 N ATOM 1948 CA GLN B 66 7.791 10.538 36.824 1.00 47.43 C ANISOU 1948 CA GLN B 66 6075 5712 6235 998 56 -930 C ATOM 1949 C GLN B 66 8.022 11.892 36.172 1.00 49.75 C ANISOU 1949 C GLN B 66 6896 5563 6443 1141 -174 -881 C ATOM 1950 O GLN B 66 7.870 12.035 34.952 1.00 50.74 O ANISOU 1950 O GLN B 66 7276 5537 6467 1131 -288 -776 O ATOM 1951 CB GLN B 66 8.903 9.561 36.459 1.00 44.47 C ANISOU 1951 CB GLN B 66 5673 5291 5933 570 308 -756 C ATOM 1952 CG GLN B 66 10.221 9.811 37.110 1.00 46.55 C ANISOU 1952 CG GLN B 66 6033 5362 6291 346 433 -691 C ATOM 1953 CD GLN B 66 11.181 8.698 36.830 1.00 46.07 C ANISOU 1953 CD GLN B 66 5835 5353 6318 18 672 -574 C ATOM 1954 OE1 GLN B 66 12.198 8.902 36.188 1.00 47.03 O ANISOU 1954 OE1 GLN B 66 6148 5280 6442 -200 758 -467 O ATOM 1955 NE2 GLN B 66 10.832 7.487 37.261 1.00 48.34 N ANISOU 1955 NE2 GLN B 66 5800 5912 6656 -21 776 -603 N ATOM 1956 N THR B 67 8.378 12.884 36.980 1.00 50.34 N ANISOU 1956 N THR B 67 7188 5409 6532 1250 -260 -954 N ATOM 1957 CA THR B 67 8.689 14.202 36.449 1.00 53.35 C ANISOU 1957 CA THR B 67 8168 5293 6811 1327 -497 -893 C ATOM 1958 C THR B 67 10.193 14.461 36.535 1.00 52.60 C ANISOU 1958 C THR B 67 8335 4907 6744 860 -346 -731 C ATOM 1959 O THR B 67 10.797 14.333 37.598 1.00 50.70 O ANISOU 1959 O THR B 67 7916 4747 6602 722 -210 -781 O ATOM 1960 CB THR B 67 7.897 15.313 37.160 1.00 56.61 C ANISOU 1960 CB THR B 67 8744 5585 7179 1835 -777 -1120 C ATOM 1961 OG1 THR B 67 6.520 14.936 37.243 1.00 57.55 O ANISOU 1961 OG1 THR B 67 8452 6126 7290 2256 -864 -1314 O ATOM 1962 CG2 THR B 67 8.004 16.632 36.394 1.00 60.93 C ANISOU 1962 CG2 THR B 67 10007 5558 7586 1966 -1103 -1042 C ATOM 1963 N ARG B 68 10.786 14.788 35.390 1.00 54.08 N ANISOU 1963 N ARG B 68 8924 4803 6821 591 -369 -537 N ATOM 1964 CA ARG B 68 12.198 15.150 35.286 1.00 54.81 C ANISOU 1964 CA ARG B 68 9277 4653 6895 102 -234 -384 C ATOM 1965 C ARG B 68 12.303 16.270 34.273 1.00 59.02 C ANISOU 1965 C ARG B 68 10502 4715 7210 12 -465 -244 C ATOM 1966 O ARG B 68 11.542 16.288 33.299 1.00 60.55 O ANISOU 1966 O ARG B 68 10875 4855 7277 201 -625 -197 O ATOM 1967 CB ARG B 68 13.046 13.974 34.797 1.00 51.86 C ANISOU 1967 CB ARG B 68 8565 4549 6591 -297 109 -269 C ATOM 1968 CG ARG B 68 12.859 12.668 35.573 1.00 48.93 C ANISOU 1968 CG ARG B 68 7576 4608 6406 -213 307 -370 C ATOM 1969 CD ARG B 68 13.872 11.633 35.154 1.00 47.65 C ANISOU 1969 CD ARG B 68 7160 4626 6317 -569 610 -277 C ATOM 1970 NE ARG B 68 13.930 11.504 33.703 1.00 48.76 N ANISOU 1970 NE ARG B 68 7518 4698 6310 -723 664 -167 N ATOM 1971 CZ ARG B 68 13.135 10.703 33.002 1.00 50.80 C ANISOU 1971 CZ ARG B 68 7664 5114 6525 -589 673 -180 C ATOM 1972 NH1 ARG B 68 12.219 9.959 33.630 1.00 50.13 N ANISOU 1972 NH1 ARG B 68 7233 5277 6538 -329 637 -293 N ATOM 1973 NH2 ARG B 68 13.252 10.642 31.678 1.00 51.38 N ANISOU 1973 NH2 ARG B 68 7980 5114 6428 -757 718 -83 N ATOM 1974 N GLN B 69 13.261 17.175 34.472 1.00 61.12 N ANISOU 1974 N GLN B 69 11177 4642 7406 -321 -497 -164 N ATOM 1975 CA GLN B 69 13.371 18.361 33.625 1.00 66.32 C ANISOU 1975 CA GLN B 69 12607 4775 7815 -454 -757 -17 C ATOM 1976 C GLN B 69 11.969 18.850 33.261 1.00 68.56 C ANISOU 1976 C GLN B 69 13173 4870 8007 157 -1144 -99 C ATOM 1977 O GLN B 69 11.645 18.998 32.083 1.00 70.88 O ANISOU 1977 O GLN B 69 13815 5002 8115 150 -1290 43 O ATOM 1978 CB GLN B 69 14.226 18.092 32.367 1.00 66.96 C ANISOU 1978 CB GLN B 69 12849 4860 7733 -1021 -546 218 C ATOM 1979 CG GLN B 69 15.686 18.606 32.450 1.00 69.82 C ANISOU 1979 CG GLN B 69 13429 5083 8019 -1691 -377 345 C ATOM 1980 CD GLN B 69 15.872 20.064 31.965 1.00 76.41 C ANISOU 1980 CD GLN B 69 15180 5296 8558 -1936 -686 499 C ATOM 1981 OE1 GLN B 69 16.223 20.955 32.749 1.00 78.36 O ANISOU 1981 OE1 GLN B 69 15745 5232 8795 -2034 -844 461 O ATOM 1982 NE2 GLN B 69 15.655 20.297 30.665 1.00 78.93 N ANISOU 1982 NE2 GLN B 69 15970 5411 8608 -2069 -785 680 N ATOM 1983 N ASN B 70 11.142 19.033 34.295 1.00 68.26 N ANISOU 1983 N ASN B 70 12929 4913 8093 691 -1299 -345 N ATOM 1984 CA ASN B 70 9.837 19.706 34.217 1.00 71.30 C ANISOU 1984 CA ASN B 70 13558 5122 8409 1366 -1708 -498 C ATOM 1985 C ASN B 70 8.830 19.200 33.174 1.00 71.48 C ANISOU 1985 C ASN B 70 13442 5351 8368 1656 -1836 -468 C ATOM 1986 O ASN B 70 8.104 19.996 32.575 1.00 75.85 O ANISOU 1986 O ASN B 70 14472 5577 8770 2042 -2243 -467 O ATOM 1987 CB ASN B 70 10.038 21.220 34.049 1.00 76.78 C ANISOU 1987 CB ASN B 70 15165 5098 8910 1407 -2091 -439 C ATOM 1988 CG ASN B 70 11.155 21.765 34.924 1.00 77.14 C ANISOU 1988 CG ASN B 70 15434 4901 8976 986 -1980 -433 C ATOM 1989 OD1 ASN B 70 12.163 22.275 34.421 1.00 78.45 O ANISOU 1989 OD1 ASN B 70 16111 4710 8986 403 -1962 -205 O ATOM 1990 ND2 ASN B 70 10.990 21.646 36.238 1.00 75.31 N ANISOU 1990 ND2 ASN B 70 14810 4896 8908 1235 -1900 -685 N ATOM 1991 N GLN B 71 8.787 17.892 32.950 1.00 67.05 N ANISOU 1991 N GLN B 71 12265 5305 7906 1477 -1524 -444 N ATOM 1992 CA GLN B 71 7.829 17.299 32.011 1.00 66.94 C ANISOU 1992 CA GLN B 71 12065 5542 7827 1699 -1630 -432 C ATOM 1993 C GLN B 71 7.539 15.872 32.448 1.00 61.87 C ANISOU 1993 C GLN B 71 10618 5528 7362 1648 -1305 -539 C ATOM 1994 O GLN B 71 8.309 15.304 33.212 1.00 59.03 O ANISOU 1994 O GLN B 71 9950 5335 7143 1345 -982 -548 O ATOM 1995 CB GLN B 71 8.340 17.357 30.558 1.00 68.28 C ANISOU 1995 CB GLN B 71 12721 5450 7771 1297 -1651 -151 C ATOM 1996 CG GLN B 71 9.745 16.801 30.332 1.00 66.20 C ANISOU 1996 CG GLN B 71 12413 5229 7509 597 -1223 24 C ATOM 1997 CD GLN B 71 10.406 17.373 29.089 1.00 70.71 C ANISOU 1997 CD GLN B 71 13661 5414 7790 169 -1280 285 C ATOM 1998 OE1 GLN B 71 10.650 16.658 28.108 1.00 70.37 O ANISOU 1998 OE1 GLN B 71 13561 5546 7632 -138 -1087 404 O ATOM 1999 NE2 GLN B 71 10.691 18.675 29.118 1.00 73.68 N ANISOU 1999 NE2 GLN B 71 14730 5251 8015 126 -1550 372 N ATOM 2000 N CYS B 72 6.424 15.312 31.995 1.00 61.49 N ANISOU 2000 N CYS B 72 10256 5815 7293 1935 -1421 -620 N ATOM 2001 CA CYS B 72 5.981 13.997 32.469 1.00 57.80 C ANISOU 2001 CA CYS B 72 9067 5931 6962 1889 -1161 -736 C ATOM 2002 C CYS B 72 6.472 12.840 31.600 1.00 54.79 C ANISOU 2002 C CYS B 72 8567 5697 6552 1424 -897 -568 C ATOM 2003 O CYS B 72 6.295 12.846 30.385 1.00 56.09 O ANISOU 2003 O CYS B 72 9008 5752 6552 1362 -1028 -446 O ATOM 2004 CB CYS B 72 4.455 13.943 32.574 1.00 60.24 C ANISOU 2004 CB CYS B 72 9008 6619 7262 2412 -1410 -955 C ATOM 2005 SG CYS B 72 3.813 12.415 33.301 1.00 56.06 S ANISOU 2005 SG CYS B 72 7625 6821 6856 2293 -1110 -1108 S ATOM 2006 N PHE B 73 7.080 11.848 32.244 1.00 51.40 N ANISOU 2006 N PHE B 73 7756 5504 6268 1120 -544 -576 N ATOM 2007 CA PHE B 73 7.468 10.595 31.577 1.00 48.88 C ANISOU 2007 CA PHE B 73 7268 5359 5945 751 -286 -477 C ATOM 2008 C PHE B 73 6.670 9.432 32.147 1.00 46.54 C ANISOU 2008 C PHE B 73 6411 5533 5739 796 -186 -610 C ATOM 2009 O PHE B 73 6.770 9.152 33.341 1.00 45.54 O ANISOU 2009 O PHE B 73 5981 5575 5747 800 -53 -701 O ATOM 2010 CB PHE B 73 8.979 10.334 31.730 1.00 47.27 C ANISOU 2010 CB PHE B 73 7141 5000 5819 336 29 -364 C ATOM 2011 CG PHE B 73 9.849 11.435 31.164 1.00 49.80 C ANISOU 2011 CG PHE B 73 8002 4903 6017 164 -27 -222 C ATOM 2012 CD1 PHE B 73 10.288 11.381 29.839 1.00 51.29 C ANISOU 2012 CD1 PHE B 73 8516 4954 6019 -113 29 -73 C ATOM 2013 CD2 PHE B 73 10.209 12.535 31.949 1.00 50.78 C ANISOU 2013 CD2 PHE B 73 8346 4771 6176 239 -140 -241 C ATOM 2014 CE1 PHE B 73 11.092 12.399 29.303 1.00 53.63 C ANISOU 2014 CE1 PHE B 73 9338 4884 6153 -359 -9 74 C ATOM 2015 CE2 PHE B 73 11.008 13.549 31.431 1.00 53.22 C ANISOU 2015 CE2 PHE B 73 9200 4680 6342 0 -203 -97 C ATOM 2016 CZ PHE B 73 11.451 13.486 30.101 1.00 54.76 C ANISOU 2016 CZ PHE B 73 9710 4759 6337 -320 -133 71 C ATOM 2017 N TYR B 74 5.885 8.766 31.294 1.00 45.81 N ANISOU 2017 N TYR B 74 6214 5647 5544 786 -263 -612 N ATOM 2018 CA TYR B 74 5.094 7.613 31.689 1.00 43.72 C ANISOU 2018 CA TYR B 74 5467 5824 5318 732 -182 -719 C ATOM 2019 C TYR B 74 5.675 6.295 31.137 1.00 42.04 C ANISOU 2019 C TYR B 74 5245 5628 5101 326 69 -627 C ATOM 2020 O TYR B 74 6.096 6.245 29.979 1.00 41.84 O ANISOU 2020 O TYR B 74 5536 5403 4960 178 80 -521 O ATOM 2021 CB TYR B 74 3.636 7.787 31.222 1.00 46.14 C ANISOU 2021 CB TYR B 74 5605 6422 5505 1023 -488 -831 C ATOM 2022 CG TYR B 74 2.774 6.550 31.430 1.00 43.71 C ANISOU 2022 CG TYR B 74 4820 6602 5186 858 -413 -925 C ATOM 2023 CD1 TYR B 74 2.550 5.644 30.395 1.00 43.30 C ANISOU 2023 CD1 TYR B 74 4811 6624 5017 595 -414 -861 C ATOM 2024 CD2 TYR B 74 2.211 6.271 32.670 1.00 42.33 C ANISOU 2024 CD2 TYR B 74 4187 6811 5084 911 -333 -1079 C ATOM 2025 CE1 TYR B 74 1.761 4.510 30.585 1.00 42.87 C ANISOU 2025 CE1 TYR B 74 4371 6990 4928 378 -365 -941 C ATOM 2026 CE2 TYR B 74 1.435 5.131 32.872 1.00 42.35 C ANISOU 2026 CE2 TYR B 74 3789 7263 5039 668 -259 -1148 C ATOM 2027 CZ TYR B 74 1.212 4.266 31.832 1.00 43.15 C ANISOU 2027 CZ TYR B 74 3959 7403 5034 396 -286 -1075 C ATOM 2028 OH TYR B 74 0.450 3.154 32.036 1.00 44.65 O ANISOU 2028 OH TYR B 74 3802 8008 5154 100 -231 -1137 O ATOM 2029 N ASN B 75 5.695 5.254 31.975 1.00 40.29 N ANISOU 2029 N ASN B 75 4700 5627 4981 155 258 -675 N ATOM 2030 CA ASN B 75 6.118 3.888 31.579 1.00 39.73 C ANISOU 2030 CA ASN B 75 4624 5562 4908 -178 458 -623 C ATOM 2031 C ASN B 75 5.287 2.878 32.316 1.00 39.74 C ANISOU 2031 C ASN B 75 4269 5914 4917 -295 481 -705 C ATOM 2032 O ASN B 75 5.024 3.032 33.513 1.00 39.92 O ANISOU 2032 O ASN B 75 4037 6121 5010 -218 497 -772 O ATOM 2033 CB ASN B 75 7.589 3.586 31.912 1.00 37.45 C ANISOU 2033 CB ASN B 75 4452 5024 4755 -344 714 -549 C ATOM 2034 CG ASN B 75 8.535 4.008 30.815 1.00 39.55 C ANISOU 2034 CG ASN B 75 5068 5004 4955 -426 789 -460 C ATOM 2035 OD1 ASN B 75 9.251 5.008 30.960 1.00 46.26 O ANISOU 2035 OD1 ASN B 75 6076 5663 5839 -379 798 -410 O ATOM 2036 ND2 ASN B 75 8.537 3.279 29.705 1.00 36.77 N ANISOU 2036 ND2 ASN B 75 4863 4630 4478 -583 846 -447 N ATOM 2037 N SER B 76 4.864 1.844 31.616 1.00 39.78 N ANISOU 2037 N SER B 76 4280 6015 4818 -519 483 -703 N ATOM 2038 CA SER B 76 4.298 0.689 32.300 1.00 40.21 C ANISOU 2038 CA SER B 76 4086 6332 4859 -762 542 -746 C ATOM 2039 C SER B 76 5.173 -0.477 31.945 1.00 39.39 C ANISOU 2039 C SER B 76 4228 5959 4778 -1027 714 -677 C ATOM 2040 O SER B 76 5.711 -0.530 30.837 1.00 39.16 O ANISOU 2040 O SER B 76 4483 5697 4701 -1045 748 -645 O ATOM 2041 CB SER B 76 2.832 0.417 31.909 1.00 42.41 C ANISOU 2041 CB SER B 76 4123 7019 4972 -830 352 -836 C ATOM 2042 OG SER B 76 2.710 -0.079 30.593 1.00 42.57 O ANISOU 2042 OG SER B 76 4375 6941 4858 -979 282 -807 O ATOM 2043 N SER B 77 5.335 -1.378 32.902 1.00 38.77 N ANISOU 2043 N SER B 77 4066 5907 4758 -1214 816 -664 N ATOM 2044 CA SER B 77 6.190 -2.532 32.762 1.00 39.30 C ANISOU 2044 CA SER B 77 4379 5687 4867 -1400 948 -617 C ATOM 2045 C SER B 77 5.767 -3.502 33.839 1.00 40.32 C ANISOU 2045 C SER B 77 4404 5945 4971 -1650 950 -601 C ATOM 2046 O SER B 77 4.869 -3.197 34.657 1.00 41.28 O ANISOU 2046 O SER B 77 4228 6421 5034 -1695 890 -633 O ATOM 2047 CB SER B 77 7.656 -2.140 33.009 1.00 37.00 C ANISOU 2047 CB SER B 77 4202 5098 4757 -1223 1094 -572 C ATOM 2048 OG SER B 77 7.794 -1.664 34.350 1.00 38.06 O ANISOU 2048 OG SER B 77 4135 5328 4998 -1139 1098 -552 O ATOM 2049 N TYR B 78 6.436 -4.653 33.856 1.00 40.51 N ANISOU 2049 N TYR B 78 4689 5681 5023 -1805 1018 -559 N ATOM 2050 CA TYR B 78 6.301 -5.615 34.943 1.00 41.61 C ANISOU 2050 CA TYR B 78 4856 5821 5135 -2053 1007 -503 C ATOM 2051 C TYR B 78 7.556 -5.693 35.787 1.00 41.07 C ANISOU 2051 C TYR B 78 4876 5480 5248 -1891 1080 -438 C ATOM 2052 O TYR B 78 8.682 -5.621 35.265 1.00 40.50 O ANISOU 2052 O TYR B 78 4948 5127 5315 -1670 1158 -452 O ATOM 2053 CB TYR B 78 5.989 -6.996 34.388 1.00 42.60 C ANISOU 2053 CB TYR B 78 5287 5779 5119 -2374 956 -501 C ATOM 2054 CG TYR B 78 4.605 -7.039 33.839 1.00 44.35 C ANISOU 2054 CG TYR B 78 5360 6358 5132 -2633 851 -556 C ATOM 2055 CD1 TYR B 78 4.339 -6.594 32.549 1.00 41.63 C ANISOU 2055 CD1 TYR B 78 5032 6057 4730 -2524 807 -628 C ATOM 2056 CD2 TYR B 78 3.549 -7.497 34.624 1.00 43.41 C ANISOU 2056 CD2 TYR B 78 5064 6579 4850 -3007 789 -538 C ATOM 2057 CE1 TYR B 78 3.057 -6.609 32.050 1.00 45.73 C ANISOU 2057 CE1 TYR B 78 5375 6942 5058 -2741 669 -685 C ATOM 2058 CE2 TYR B 78 2.268 -7.538 34.127 1.00 49.14 C ANISOU 2058 CE2 TYR B 78 5577 7710 5382 -3260 685 -609 C ATOM 2059 CZ TYR B 78 2.024 -7.096 32.834 1.00 47.91 C ANISOU 2059 CZ TYR B 78 5422 7586 5196 -3106 609 -685 C ATOM 2060 OH TYR B 78 0.735 -7.135 32.341 1.00 51.04 O ANISOU 2060 OH TYR B 78 5573 8421 5397 -3344 465 -761 O ATOM 2061 N LEU B 79 7.338 -5.855 37.088 1.00 41.56 N ANISOU 2061 N LEU B 79 4835 5671 5285 -2021 1052 -377 N ATOM 2062 CA LEU B 79 8.384 -6.239 38.017 1.00 41.42 C ANISOU 2062 CA LEU B 79 4950 5398 5389 -1947 1057 -295 C ATOM 2063 C LEU B 79 8.208 -7.713 38.362 1.00 43.89 C ANISOU 2063 C LEU B 79 5587 5511 5580 -2262 969 -214 C ATOM 2064 O LEU B 79 7.081 -8.177 38.566 1.00 45.82 O ANISOU 2064 O LEU B 79 5821 5980 5611 -2636 921 -194 O ATOM 2065 CB LEU B 79 8.304 -5.397 39.286 1.00 40.39 C ANISOU 2065 CB LEU B 79 4557 5515 5273 -1893 1063 -271 C ATOM 2066 CG LEU B 79 8.373 -3.875 39.160 1.00 39.40 C ANISOU 2066 CG LEU B 79 4167 5563 5239 -1604 1111 -352 C ATOM 2067 CD1 LEU B 79 7.970 -3.253 40.484 1.00 40.59 C ANISOU 2067 CD1 LEU B 79 4095 5998 5327 -1621 1103 -363 C ATOM 2068 CD2 LEU B 79 9.766 -3.363 38.699 1.00 37.65 C ANISOU 2068 CD2 LEU B 79 4025 5050 5229 -1318 1167 -350 C ATOM 2069 N ASN B 80 9.312 -8.452 38.412 1.00 44.49 N ANISOU 2069 N ASN B 80 5957 5170 5778 -2118 934 -175 N ATOM 2070 CA ASN B 80 9.274 -9.840 38.837 1.00 47.51 C ANISOU 2070 CA ASN B 80 6746 5259 6047 -2369 800 -84 C ATOM 2071 C ASN B 80 9.400 -9.919 40.351 1.00 48.10 C ANISOU 2071 C ASN B 80 6822 5373 6080 -2479 716 55 C ATOM 2072 O ASN B 80 10.239 -9.235 40.956 1.00 45.70 O ANISOU 2072 O ASN B 80 6341 5081 5942 -2191 733 67 O ATOM 2073 CB ASN B 80 10.359 -10.654 38.146 1.00 49.23 C ANISOU 2073 CB ASN B 80 7314 4991 6402 -2102 766 -137 C ATOM 2074 CG ASN B 80 10.308 -10.522 36.624 1.00 50.73 C ANISOU 2074 CG ASN B 80 7513 5160 6600 -1995 877 -290 C ATOM 2075 OD1 ASN B 80 9.305 -10.843 35.987 1.00 54.52 O ANISOU 2075 OD1 ASN B 80 8090 5733 6892 -2295 856 -319 O ATOM 2076 ND2 ASN B 80 11.395 -10.044 36.041 1.00 51.52 N ANISOU 2076 ND2 ASN B 80 7508 5171 6895 -1599 994 -390 N ATOM 2077 N VAL B 81 8.536 -10.724 40.964 1.00 50.14 N ANISOU 2077 N VAL B 81 7287 5679 6085 -2945 624 159 N ATOM 2078 CA VAL B 81 8.553 -10.915 42.407 1.00 51.40 C ANISOU 2078 CA VAL B 81 7524 5881 6126 -3140 539 309 C ATOM 2079 C VAL B 81 9.293 -12.210 42.737 1.00 54.31 C ANISOU 2079 C VAL B 81 8476 5677 6482 -3159 323 441 C ATOM 2080 O VAL B 81 8.980 -13.264 42.198 1.00 56.86 O ANISOU 2080 O VAL B 81 9214 5707 6683 -3393 227 461 O ATOM 2081 CB VAL B 81 7.125 -10.972 43.010 1.00 52.98 C ANISOU 2081 CB VAL B 81 7586 6547 5997 -3704 583 350 C ATOM 2082 CG1 VAL B 81 7.192 -10.928 44.521 1.00 54.29 C ANISOU 2082 CG1 VAL B 81 7774 6833 6020 -3880 542 482 C ATOM 2083 CG2 VAL B 81 6.266 -9.832 42.493 1.00 50.63 C ANISOU 2083 CG2 VAL B 81 6736 6796 5705 -3639 752 182 C ATOM 2084 N GLN B 82 10.292 -12.105 43.607 1.00 54.78 N ANISOU 2084 N GLN B 82 8584 5562 6667 -2888 220 521 N ATOM 2085 CA GLN B 82 10.977 -13.267 44.170 1.00 58.38 C ANISOU 2085 CA GLN B 82 9598 5493 7091 -2871 -46 668 C ATOM 2086 C GLN B 82 10.466 -13.423 45.598 1.00 60.21 C ANISOU 2086 C GLN B 82 9961 5880 7036 -3308 -143 867 C ATOM 2087 O GLN B 82 10.907 -12.716 46.501 1.00 58.59 O ANISOU 2087 O GLN B 82 9520 5862 6880 -3159 -144 906 O ATOM 2088 CB GLN B 82 12.494 -13.070 44.141 1.00 57.83 C ANISOU 2088 CB GLN B 82 9466 5156 7352 -2242 -129 611 C ATOM 2089 CG GLN B 82 13.081 -12.874 42.738 1.00 57.59 C ANISOU 2089 CG GLN B 82 9276 5031 7576 -1824 9 395 C ATOM 2090 CD GLN B 82 12.794 -11.489 42.144 1.00 55.66 C ANISOU 2090 CD GLN B 82 8457 5266 7426 -1754 289 260 C ATOM 2091 OE1 GLN B 82 12.926 -10.465 42.819 1.00 54.18 O ANISOU 2091 OE1 GLN B 82 7909 5386 7290 -1697 354 278 O ATOM 2092 NE2 GLN B 82 12.402 -11.463 40.872 1.00 55.88 N ANISOU 2092 NE2 GLN B 82 8453 5323 7455 -1759 430 125 N ATOM 2093 N ARG B 83 9.522 -14.344 45.785 1.00 63.57 N ANISOU 2093 N ARG B 83 10777 6245 7132 -3894 -217 989 N ATOM 2094 CA ARG B 83 8.712 -14.388 46.996 1.00 65.86 C ANISOU 2094 CA ARG B 83 11107 6855 7063 -4463 -216 1148 C ATOM 2095 C ARG B 83 9.520 -14.625 48.272 1.00 67.99 C ANISOU 2095 C ARG B 83 11685 6872 7277 -4384 -444 1342 C ATOM 2096 O ARG B 83 9.450 -13.818 49.202 1.00 66.53 O ANISOU 2096 O ARG B 83 11179 7086 7015 -4425 -352 1358 O ATOM 2097 CB ARG B 83 7.582 -15.430 46.867 1.00 70.37 C ANISOU 2097 CB ARG B 83 12079 7397 7261 -5186 -258 1249 C ATOM 2098 CG ARG B 83 6.392 -14.992 45.996 1.00 69.42 C ANISOU 2098 CG ARG B 83 11499 7809 7068 -5459 -10 1073 C ATOM 2099 CD ARG B 83 5.198 -15.949 46.128 1.00 74.41 C ANISOU 2099 CD ARG B 83 12450 8552 7269 -6307 -44 1186 C ATOM 2100 NE ARG B 83 4.036 -15.485 45.368 1.00 74.43 N ANISOU 2100 NE ARG B 83 11929 9154 7196 -6561 170 1006 N ATOM 2101 CZ ARG B 83 2.873 -15.114 45.904 1.00 75.82 C ANISOU 2101 CZ ARG B 83 11671 10055 7082 -7070 349 973 C ATOM 2102 NH1 ARG B 83 2.683 -15.156 47.215 1.00 77.67 N ANISOU 2102 NH1 ARG B 83 11955 10518 7039 -7438 376 1111 N ATOM 2103 NH2 ARG B 83 1.888 -14.705 45.116 1.00 76.44 N ANISOU 2103 NH2 ARG B 83 11252 10662 7131 -7207 497 788 N ATOM 2104 N GLU B 84 10.284 -15.718 48.321 1.00 71.49 N ANISOU 2104 N GLU B 84 12767 6647 7750 -4245 -762 1475 N ATOM 2105 CA GLU B 84 10.974 -16.110 49.567 1.00 74.85 C ANISOU 2105 CA GLU B 84 13591 6784 8065 -4220 -1057 1696 C ATOM 2106 C GLU B 84 12.114 -15.161 49.925 1.00 71.49 C ANISOU 2106 C GLU B 84 12735 6464 7962 -3592 -1071 1615 C ATOM 2107 O GLU B 84 12.443 -15.015 51.104 1.00 72.44 O ANISOU 2107 O GLU B 84 12944 6628 7952 -3646 -1220 1763 O ATOM 2108 CB GLU B 84 11.499 -17.562 49.538 1.00 79.94 C ANISOU 2108 CB GLU B 84 15094 6630 8650 -4181 -1460 1859 C ATOM 2109 CG GLU B 84 10.469 -18.645 49.228 1.00 85.70 C ANISOU 2109 CG GLU B 84 16404 7132 9028 -4859 -1515 1968 C ATOM 2110 CD GLU B 84 10.444 -19.020 47.747 1.00 87.24 C ANISOU 2110 CD GLU B 84 16647 7071 9431 -4632 -1452 1761 C ATOM 2111 OE1 GLU B 84 9.979 -20.136 47.430 1.00 92.18 O ANISOU 2111 OE1 GLU B 84 17934 7262 9827 -5032 -1621 1846 O ATOM 2112 OE2 GLU B 84 10.901 -18.210 46.899 1.00 84.98 O ANISOU 2112 OE2 GLU B 84 15782 6997 9508 -4082 -1242 1514 O ATOM 2113 N ASN B 85 12.715 -14.537 48.908 1.00 67.91 N ANISOU 2113 N ASN B 85 11845 6059 7899 -3045 -924 1385 N ATOM 2114 CA ASN B 85 13.779 -13.546 49.123 1.00 65.05 C ANISOU 2114 CA ASN B 85 11017 5856 7845 -2508 -903 1284 C ATOM 2115 C ASN B 85 13.188 -12.190 49.473 1.00 61.78 C ANISOU 2115 C ASN B 85 10024 6075 7376 -2668 -609 1194 C ATOM 2116 O ASN B 85 13.895 -11.297 49.950 1.00 59.59 O ANISOU 2116 O ASN B 85 9414 5975 7253 -2382 -604 1146 O ATOM 2117 CB ASN B 85 14.664 -13.385 47.883 1.00 63.14 C ANISOU 2117 CB ASN B 85 10535 5454 8001 -1921 -834 1068 C ATOM 2118 CG ASN B 85 15.422 -14.649 47.512 1.00 66.96 C ANISOU 2118 CG ASN B 85 11542 5312 8587 -1605 -1129 1088 C ATOM 2119 OD1 ASN B 85 16.237 -14.629 46.594 1.00 66.72 O ANISOU 2119 OD1 ASN B 85 11339 5156 8856 -1104 -1085 897 O ATOM 2120 ND2 ASN B 85 15.150 -15.751 48.199 1.00 71.03 N ANISOU 2120 ND2 ASN B 85 12719 5432 8835 -1897 -1427 1305 N ATOM 2121 N GLY B 86 11.890 -12.041 49.212 1.00 61.43 N ANISOU 2121 N GLY B 86 9860 6373 7109 -3113 -381 1152 N ATOM 2122 CA GLY B 86 11.190 -10.777 49.422 1.00 59.58 C ANISOU 2122 CA GLY B 86 9079 6743 6817 -3215 -102 1020 C ATOM 2123 C GLY B 86 11.807 -9.628 48.647 1.00 56.15 C ANISOU 2123 C GLY B 86 8162 6433 6740 -2705 49 816 C ATOM 2124 O GLY B 86 11.875 -8.506 49.159 1.00 55.02 O ANISOU 2124 O GLY B 86 7667 6612 6626 -2600 151 737 O ATOM 2125 N THR B 87 12.281 -9.927 47.432 1.00 55.40 N ANISOU 2125 N THR B 87 8099 6062 6889 -2414 55 730 N ATOM 2126 CA THR B 87 12.800 -8.932 46.493 1.00 52.49 C ANISOU 2126 CA THR B 87 7328 5799 6816 -2013 219 545 C ATOM 2127 C THR B 87 11.849 -8.762 45.315 1.00 51.95 C ANISOU 2127 C THR B 87 7125 5901 6714 -2128 414 420 C ATOM 2128 O THR B 87 10.974 -9.610 45.064 1.00 53.70 O ANISOU 2128 O THR B 87 7586 6083 6734 -2473 396 466 O ATOM 2129 CB THR B 87 14.191 -9.304 45.904 1.00 52.57 C ANISOU 2129 CB THR B 87 7418 5430 7127 -1554 110 504 C ATOM 2130 OG1 THR B 87 14.111 -10.547 45.198 1.00 54.36 O ANISOU 2130 OG1 THR B 87 8043 5284 7327 -1578 20 518 O ATOM 2131 CG2 THR B 87 15.247 -9.408 46.975 1.00 53.18 C ANISOU 2131 CG2 THR B 87 7563 5365 7279 -1362 -121 605 C ATOM 2132 N VAL B 88 12.012 -7.646 44.616 1.00 49.40 N ANISOU 2132 N VAL B 88 6439 5767 6564 -1873 576 272 N ATOM 2133 CA VAL B 88 11.401 -7.459 43.318 1.00 49.10 C ANISOU 2133 CA VAL B 88 6300 5814 6540 -1873 715 153 C ATOM 2134 C VAL B 88 12.482 -7.022 42.325 1.00 48.16 C ANISOU 2134 C VAL B 88 6082 5526 6689 -1479 785 50 C ATOM 2135 O VAL B 88 13.503 -6.449 42.712 1.00 46.73 O ANISOU 2135 O VAL B 88 5759 5319 6679 -1235 771 43 O ATOM 2136 CB VAL B 88 10.227 -6.466 43.354 1.00 48.32 C ANISOU 2136 CB VAL B 88 5875 6181 6305 -2015 844 68 C ATOM 2137 CG1 VAL B 88 9.684 -6.259 41.962 1.00 48.98 C ANISOU 2137 CG1 VAL B 88 5874 6327 6408 -1973 935 -45 C ATOM 2138 CG2 VAL B 88 9.110 -6.989 44.228 1.00 49.24 C ANISOU 2138 CG2 VAL B 88 6039 6548 6123 -2451 819 137 C ATOM 2139 N SER B 89 12.254 -7.311 41.049 1.00 49.24 N ANISOU 2139 N SER B 89 6296 5577 6835 -1459 862 -34 N ATOM 2140 CA SER B 89 13.257 -7.092 40.024 1.00 50.47 C ANISOU 2140 CA SER B 89 6405 5581 7189 -1145 955 -140 C ATOM 2141 C SER B 89 12.667 -6.604 38.706 1.00 50.36 C ANISOU 2141 C SER B 89 6321 5691 7122 -1170 1094 -244 C ATOM 2142 O SER B 89 11.481 -6.773 38.439 1.00 49.74 O ANISOU 2142 O SER B 89 6285 5750 6865 -1416 1081 -242 O ATOM 2143 CB SER B 89 14.072 -8.357 39.791 1.00 52.28 C ANISOU 2143 CB SER B 89 6941 5426 7497 -994 862 -150 C ATOM 2144 OG SER B 89 13.225 -9.404 39.363 1.00 55.47 O ANISOU 2144 OG SER B 89 7686 5668 7724 -1239 801 -136 O ATOM 2145 N ARG B 90 13.529 -6.016 37.883 1.00 51.49 N ANISOU 2145 N ARG B 90 6355 5804 7403 -936 1219 -333 N ATOM 2146 CA ARG B 90 13.132 -5.431 36.604 1.00 52.73 C ANISOU 2146 CA ARG B 90 6483 6059 7495 -946 1340 -416 C ATOM 2147 C ARG B 90 14.386 -5.155 35.817 1.00 53.50 C ANISOU 2147 C ARG B 90 6533 6068 7728 -724 1486 -506 C ATOM 2148 O ARG B 90 15.406 -4.768 36.369 1.00 53.12 O ANISOU 2148 O ARG B 90 6316 6032 7836 -575 1506 -502 O ATOM 2149 CB ARG B 90 12.366 -4.135 36.833 1.00 51.45 C ANISOU 2149 CB ARG B 90 6105 6176 7269 -1001 1337 -395 C ATOM 2150 CG ARG B 90 11.833 -3.425 35.585 1.00 54.06 C ANISOU 2150 CG ARG B 90 6440 6600 7501 -1002 1395 -454 C ATOM 2151 CD ARG B 90 12.117 -1.931 35.766 1.00 54.88 C ANISOU 2151 CD ARG B 90 6382 6808 7662 -879 1417 -448 C ATOM 2152 NE ARG B 90 10.957 -1.090 35.490 1.00 58.60 N ANISOU 2152 NE ARG B 90 6800 7466 8001 -889 1335 -465 N ATOM 2153 CZ ARG B 90 10.978 0.240 35.526 1.00 58.52 C ANISOU 2153 CZ ARG B 90 6738 7499 7999 -768 1305 -470 C ATOM 2154 NH1 ARG B 90 12.105 0.872 35.813 1.00 57.73 N ANISOU 2154 NH1 ARG B 90 6631 7283 8020 -705 1370 -447 N ATOM 2155 NH2 ARG B 90 9.876 0.941 35.265 1.00 59.86 N ANISOU 2155 NH2 ARG B 90 6871 7823 8049 -708 1189 -505 N ATOM 2156 N TYR B 91 14.304 -5.394 34.522 1.00 56.08 N ANISOU 2156 N TYR B 91 7000 6338 7969 -730 1589 -598 N ATOM 2157 CA TYR B 91 15.414 -5.190 33.627 1.00 58.60 C ANISOU 2157 CA TYR B 91 7277 6630 8357 -569 1773 -711 C ATOM 2158 C TYR B 91 15.205 -3.825 33.012 1.00 58.48 C ANISOU 2158 C TYR B 91 7164 6794 8261 -653 1861 -688 C ATOM 2159 O TYR B 91 14.094 -3.506 32.564 1.00 58.18 O ANISOU 2159 O TYR B 91 7222 6822 8061 -788 1794 -654 O ATOM 2160 CB TYR B 91 15.387 -6.277 32.553 1.00 60.85 C ANISOU 2160 CB TYR B 91 7837 6739 8544 -547 1836 -839 C ATOM 2161 CG TYR B 91 16.598 -6.375 31.638 1.00 63.18 C ANISOU 2161 CG TYR B 91 8095 7021 8888 -353 2057 -1010 C ATOM 2162 CD1 TYR B 91 16.778 -5.485 30.571 1.00 63.63 C ANISOU 2162 CD1 TYR B 91 8105 7241 8831 -433 2249 -1056 C ATOM 2163 CD2 TYR B 91 17.529 -7.401 31.804 1.00 66.79 C ANISOU 2163 CD2 TYR B 91 8588 7311 9477 -88 2066 -1138 C ATOM 2164 CE1 TYR B 91 17.874 -5.589 29.717 1.00 66.43 C ANISOU 2164 CE1 TYR B 91 8403 7653 9186 -305 2493 -1231 C ATOM 2165 CE2 TYR B 91 18.630 -7.525 30.950 1.00 70.42 C ANISOU 2165 CE2 TYR B 91 8956 7831 9971 119 2296 -1344 C ATOM 2166 CZ TYR B 91 18.798 -6.618 29.911 1.00 69.89 C ANISOU 2166 CZ TYR B 91 8799 7985 9770 -17 2532 -1394 C ATOM 2167 OH TYR B 91 19.894 -6.756 29.086 1.00 72.53 O ANISOU 2167 OH TYR B 91 9013 8444 10102 147 2796 -1615 O ATOM 2168 N GLU B 92 16.248 -3.000 33.059 1.00 59.91 N ANISOU 2168 N GLU B 92 7160 7058 8546 -584 1976 -701 N ATOM 2169 CA GLU B 92 16.353 -1.777 32.230 1.00 61.14 C ANISOU 2169 CA GLU B 92 7320 7314 8597 -686 2086 -688 C ATOM 2170 C GLU B 92 17.793 -1.257 32.147 1.00 62.78 C ANISOU 2170 C GLU B 92 7333 7613 8907 -663 2265 -738 C ATOM 2171 O GLU B 92 18.486 -1.148 33.159 1.00 62.83 O ANISOU 2171 O GLU B 92 7119 7665 9089 -591 2220 -721 O ATOM 2172 CB GLU B 92 15.350 -0.680 32.636 1.00 59.66 C ANISOU 2172 CB GLU B 92 7149 7185 8332 -767 1926 -576 C ATOM 2173 CG GLU B 92 15.397 -0.221 34.080 1.00 60.19 C ANISOU 2173 CG GLU B 92 7037 7298 8533 -722 1802 -512 C ATOM 2174 CD GLU B 92 15.896 1.219 34.249 1.00 62.08 C ANISOU 2174 CD GLU B 92 7231 7569 8786 -766 1811 -470 C ATOM 2175 OE1 GLU B 92 15.773 1.732 35.384 1.00 62.93 O ANISOU 2175 OE1 GLU B 92 7241 7708 8962 -736 1691 -432 O ATOM 2176 OE2 GLU B 92 16.384 1.839 33.269 1.00 60.88 O ANISOU 2176 OE2 GLU B 92 7179 7402 8550 -861 1930 -474 O ATOM 2177 N GLY B 93 18.236 -0.972 30.925 1.00 64.80 N ANISOU 2177 N GLY B 93 7665 7926 9028 -757 2467 -806 N ATOM 2178 CA GLY B 93 19.579 -0.443 30.681 1.00 67.07 C ANISOU 2178 CA GLY B 93 7745 8377 9359 -819 2681 -869 C ATOM 2179 C GLY B 93 20.614 -1.545 30.548 1.00 69.64 C ANISOU 2179 C GLY B 93 7870 8779 9809 -611 2842 -1060 C ATOM 2180 O GLY B 93 21.753 -1.399 31.012 1.00 71.21 O ANISOU 2180 O GLY B 93 7742 9151 10164 -554 2922 -1121 O ATOM 2181 N GLY B 94 20.209 -2.649 29.913 1.00 70.10 N ANISOU 2181 N GLY B 94 8129 8712 9795 -483 2867 -1170 N ATOM 2182 CA GLY B 94 21.046 -3.835 29.770 1.00 72.42 C ANISOU 2182 CA GLY B 94 8314 9004 10198 -200 2975 -1384 C ATOM 2183 C GLY B 94 21.327 -4.568 31.072 1.00 72.05 C ANISOU 2183 C GLY B 94 8124 8844 10406 66 2758 -1370 C ATOM 2184 O GLY B 94 22.139 -5.503 31.099 1.00 74.91 O ANISOU 2184 O GLY B 94 8378 9189 10894 373 2794 -1550 O ATOM 2185 N ARG B 95 20.634 -4.168 32.139 1.00 68.76 N ANISOU 2185 N ARG B 95 7734 8346 10045 -32 2518 -1168 N ATOM 2186 CA ARG B 95 20.939 -4.624 33.493 1.00 68.16 C ANISOU 2186 CA ARG B 95 7529 8196 10172 149 2297 -1111 C ATOM 2187 C ARG B 95 19.662 -4.939 34.281 1.00 64.60 C ANISOU 2187 C ARG B 95 7336 7545 9664 46 2044 -943 C ATOM 2188 O ARG B 95 18.637 -4.265 34.130 1.00 62.27 O ANISOU 2188 O ARG B 95 7155 7281 9225 -183 2021 -838 O ATOM 2189 CB ARG B 95 21.790 -3.555 34.204 1.00 68.64 C ANISOU 2189 CB ARG B 95 7227 8494 10358 84 2307 -1056 C ATOM 2190 CG ARG B 95 22.598 -4.051 35.407 1.00 72.33 C ANISOU 2190 CG ARG B 95 7469 8967 11048 325 2119 -1060 C ATOM 2191 CD ARG B 95 22.080 -3.435 36.712 1.00 73.73 C ANISOU 2191 CD ARG B 95 7656 9114 11243 179 1888 -860 C ATOM 2192 NE ARG B 95 22.438 -4.237 37.888 1.00 77.15 N ANISOU 2192 NE ARG B 95 8055 9442 11817 398 1633 -821 N ATOM 2193 CZ ARG B 95 22.112 -3.924 39.142 1.00 76.47 C ANISOU 2193 CZ ARG B 95 7989 9332 11734 304 1416 -667 C ATOM 2194 NH1 ARG B 95 21.416 -2.817 39.403 1.00 74.78 N ANISOU 2194 NH1 ARG B 95 7805 9197 11410 35 1433 -566 N ATOM 2195 NH2 ARG B 95 22.478 -4.720 40.140 1.00 77.33 N ANISOU 2195 NH2 ARG B 95 8117 9328 11937 496 1169 -622 N ATOM 2196 N GLU B 96 19.718 -5.978 35.108 1.00 64.16 N ANISOU 2196 N GLU B 96 7378 7299 9701 214 1847 -924 N ATOM 2197 CA GLU B 96 18.579 -6.318 35.958 1.00 61.14 C ANISOU 2197 CA GLU B 96 7222 6775 9233 54 1625 -761 C ATOM 2198 C GLU B 96 18.745 -5.600 37.290 1.00 58.65 C ANISOU 2198 C GLU B 96 6698 6583 9002 8 1491 -627 C ATOM 2199 O GLU B 96 19.838 -5.558 37.838 1.00 59.71 O ANISOU 2199 O GLU B 96 6616 6769 9302 191 1448 -654 O ATOM 2200 CB GLU B 96 18.473 -7.827 36.163 1.00 63.52 C ANISOU 2200 CB GLU B 96 7846 6759 9530 182 1459 -783 C ATOM 2201 CG GLU B 96 17.158 -8.277 36.793 1.00 63.00 C ANISOU 2201 CG GLU B 96 8065 6572 9300 -101 1274 -623 C ATOM 2202 CD GLU B 96 17.185 -9.729 37.214 1.00 67.67 C ANISOU 2202 CD GLU B 96 9036 6800 9877 -19 1061 -603 C ATOM 2203 OE1 GLU B 96 18.258 -10.359 37.118 1.00 69.55 O ANISOU 2203 OE1 GLU B 96 9303 6860 10263 339 1021 -721 O ATOM 2204 OE2 GLU B 96 16.132 -10.243 37.649 1.00 69.18 O ANISOU 2204 OE2 GLU B 96 9505 6885 9895 -316 921 -477 O ATOM 2205 N HIS B 97 17.664 -5.021 37.802 1.00 54.72 N ANISOU 2205 N HIS B 97 6247 6164 8381 -227 1421 -504 N ATOM 2206 CA HIS B 97 17.730 -4.315 39.081 1.00 52.37 C ANISOU 2206 CA HIS B 97 5792 5985 8123 -282 1302 -401 C ATOM 2207 C HIS B 97 16.941 -5.134 40.079 1.00 51.50 C ANISOU 2207 C HIS B 97 5887 5771 7909 -394 1109 -287 C ATOM 2208 O HIS B 97 15.832 -5.554 39.775 1.00 51.05 O ANISOU 2208 O HIS B 97 6018 5688 7690 -572 1106 -264 O ATOM 2209 CB HIS B 97 17.175 -2.887 38.954 1.00 49.89 C ANISOU 2209 CB HIS B 97 5364 5863 7729 -432 1382 -384 C ATOM 2210 CG HIS B 97 18.002 -1.989 38.075 1.00 50.58 C ANISOU 2210 CG HIS B 97 5306 6035 7877 -403 1553 -459 C ATOM 2211 ND1 HIS B 97 18.538 -0.797 38.519 1.00 49.89 N ANISOU 2211 ND1 HIS B 97 5052 6064 7838 -458 1557 -440 N ATOM 2212 CD2 HIS B 97 18.393 -2.113 36.783 1.00 50.96 C ANISOU 2212 CD2 HIS B 97 5379 6073 7910 -373 1732 -554 C ATOM 2213 CE1 HIS B 97 19.227 -0.231 37.541 1.00 51.08 C ANISOU 2213 CE1 HIS B 97 5134 6274 7998 -497 1729 -503 C ATOM 2214 NE2 HIS B 97 19.145 -1.004 36.474 1.00 51.34 N ANISOU 2214 NE2 HIS B 97 5269 6251 7986 -443 1850 -575 N ATOM 2215 N VAL B 98 17.528 -5.376 41.252 1.00 51.31 N ANISOU 2215 N VAL B 98 5835 5706 7955 -324 939 -211 N ATOM 2216 CA VAL B 98 16.866 -6.087 42.360 1.00 50.66 C ANISOU 2216 CA VAL B 98 5980 5537 7731 -486 744 -75 C ATOM 2217 C VAL B 98 16.691 -5.116 43.548 1.00 48.34 C ANISOU 2217 C VAL B 98 5521 5466 7379 -609 691 -5 C ATOM 2218 O VAL B 98 17.532 -4.249 43.754 1.00 46.95 O ANISOU 2218 O VAL B 98 5107 5397 7334 -490 709 -43 O ATOM 2219 CB VAL B 98 17.703 -7.303 42.810 1.00 53.87 C ANISOU 2219 CB VAL B 98 6592 5654 8223 -288 532 -32 C ATOM 2220 CG1 VAL B 98 16.885 -8.238 43.690 1.00 55.86 C ANISOU 2220 CG1 VAL B 98 7218 5742 8264 -535 335 129 C ATOM 2221 CG2 VAL B 98 18.270 -8.067 41.597 1.00 56.37 C ANISOU 2221 CG2 VAL B 98 7000 5763 8655 -34 604 -175 C ATOM 2222 N ALA B 99 15.602 -5.263 44.308 1.00 47.07 N ANISOU 2222 N ALA B 99 5487 5396 7000 -871 637 81 N ATOM 2223 CA ALA B 99 15.352 -4.447 45.511 1.00 45.73 C ANISOU 2223 CA ALA B 99 5201 5447 6726 -988 593 120 C ATOM 2224 C ALA B 99 14.505 -5.197 46.529 1.00 46.59 C ANISOU 2224 C ALA B 99 5535 5589 6578 -1277 485 241 C ATOM 2225 O ALA B 99 13.612 -5.943 46.160 1.00 47.34 O ANISOU 2225 O ALA B 99 5799 5662 6527 -1483 513 268 O ATOM 2226 CB ALA B 99 14.686 -3.122 45.156 1.00 43.74 C ANISOU 2226 CB ALA B 99 4730 5452 6436 -1013 758 9 C ATOM 2227 N HIS B 100 14.794 -4.988 47.809 1.00 46.78 N ANISOU 2227 N HIS B 100 5573 5682 6520 -1335 359 316 N ATOM 2228 CA HIS B 100 14.067 -5.654 48.882 1.00 48.63 C ANISOU 2228 CA HIS B 100 6043 5974 6460 -1661 262 445 C ATOM 2229 C HIS B 100 12.907 -4.772 49.343 1.00 48.00 C ANISOU 2229 C HIS B 100 5767 6314 6158 -1875 432 353 C ATOM 2230 O HIS B 100 13.122 -3.622 49.751 1.00 47.19 O ANISOU 2230 O HIS B 100 5448 6387 6092 -1750 479 254 O ATOM 2231 CB HIS B 100 15.000 -5.943 50.067 1.00 50.56 C ANISOU 2231 CB HIS B 100 6445 6077 6688 -1617 11 578 C ATOM 2232 CG HIS B 100 15.910 -7.116 49.863 1.00 51.70 C ANISOU 2232 CG HIS B 100 6864 5811 6970 -1429 -222 685 C ATOM 2233 ND1 HIS B 100 17.203 -6.986 49.399 1.00 51.38 N ANISOU 2233 ND1 HIS B 100 6655 5623 7242 -1028 -299 618 N ATOM 2234 CD2 HIS B 100 15.721 -8.439 50.086 1.00 53.27 C ANISOU 2234 CD2 HIS B 100 7507 5712 7021 -1576 -410 841 C ATOM 2235 CE1 HIS B 100 17.767 -8.181 49.332 1.00 53.54 C ANISOU 2235 CE1 HIS B 100 7228 5540 7577 -867 -526 702 C ATOM 2236 NE2 HIS B 100 16.888 -9.079 49.742 1.00 54.49 N ANISOU 2236 NE2 HIS B 100 7767 5518 7420 -1193 -614 848 N ATOM 2237 N LEU B 101 11.681 -5.298 49.255 1.00 48.74 N ANISOU 2237 N LEU B 101 5925 6579 6014 -2192 520 363 N ATOM 2238 CA LEU B 101 10.511 -4.620 49.813 1.00 48.54 C ANISOU 2238 CA LEU B 101 5680 7023 5738 -2399 677 253 C ATOM 2239 C LEU B 101 10.594 -4.698 51.332 1.00 50.42 C ANISOU 2239 C LEU B 101 6052 7379 5728 -2615 595 344 C ATOM 2240 O LEU B 101 10.627 -5.783 51.898 1.00 52.73 O ANISOU 2240 O LEU B 101 6681 7516 5837 -2902 460 533 O ATOM 2241 CB LEU B 101 9.204 -5.242 49.287 1.00 49.58 C ANISOU 2241 CB LEU B 101 5793 7371 5673 -2721 788 232 C ATOM 2242 CG LEU B 101 7.883 -4.888 49.989 1.00 50.93 C ANISOU 2242 CG LEU B 101 5727 8108 5516 -3022 947 123 C ATOM 2243 CD1 LEU B 101 7.648 -3.388 50.073 1.00 49.70 C ANISOU 2243 CD1 LEU B 101 5191 8267 5427 -2698 1071 -114 C ATOM 2244 CD2 LEU B 101 6.688 -5.561 49.312 1.00 53.20 C ANISOU 2244 CD2 LEU B 101 5950 8624 5639 -3355 1035 99 C ATOM 2245 N LEU B 102 10.653 -3.548 51.989 1.00 49.76 N ANISOU 2245 N LEU B 102 5759 7532 5615 -2482 656 211 N ATOM 2246 CA LEU B 102 10.735 -3.515 53.452 1.00 52.31 C ANISOU 2246 CA LEU B 102 6211 7997 5668 -2686 587 271 C ATOM 2247 C LEU B 102 9.647 -2.621 54.026 1.00 53.77 C ANISOU 2247 C LEU B 102 6127 8710 5595 -2783 805 53 C ATOM 2248 O LEU B 102 9.182 -1.702 53.338 1.00 53.26 O ANISOU 2248 O LEU B 102 5761 8817 5657 -2531 946 -162 O ATOM 2249 CB LEU B 102 12.109 -3.001 53.891 1.00 51.13 C ANISOU 2249 CB LEU B 102 6115 7595 5717 -2411 401 308 C ATOM 2250 CG LEU B 102 13.352 -3.761 53.409 1.00 50.16 C ANISOU 2250 CG LEU B 102 6176 7009 5875 -2219 172 473 C ATOM 2251 CD1 LEU B 102 14.597 -2.855 53.437 1.00 45.85 C ANISOU 2251 CD1 LEU B 102 5471 6350 5598 -1891 71 409 C ATOM 2252 CD2 LEU B 102 13.557 -5.062 54.208 1.00 52.06 C ANISOU 2252 CD2 LEU B 102 6831 7038 5909 -2470 -62 721 C ATOM 2253 N PHE B 103 9.271 -2.854 55.284 1.00 56.64 N ANISOU 2253 N PHE B 103 6609 9326 5585 -3118 820 94 N ATOM 2254 CA PHE B 103 8.255 -2.037 55.939 1.00 58.65 C ANISOU 2254 CA PHE B 103 6591 10136 5556 -3196 1047 -153 C ATOM 2255 C PHE B 103 8.718 -1.285 57.175 1.00 59.92 C ANISOU 2255 C PHE B 103 6823 10390 5555 -3148 1006 -229 C ATOM 2256 O PHE B 103 9.634 -1.710 57.863 1.00 60.57 O ANISOU 2256 O PHE B 103 7221 10195 5597 -3247 790 -25 O ATOM 2257 CB PHE B 103 6.997 -2.873 56.241 1.00 62.01 C ANISOU 2257 CB PHE B 103 6985 10988 5588 -3714 1213 -129 C ATOM 2258 CG PHE B 103 6.315 -3.336 55.009 1.00 62.01 C ANISOU 2258 CG PHE B 103 6823 11019 5719 -3750 1286 -143 C ATOM 2259 CD1 PHE B 103 6.420 -4.657 54.595 1.00 63.45 C ANISOU 2259 CD1 PHE B 103 7329 10891 5887 -4068 1162 116 C ATOM 2260 CD2 PHE B 103 5.633 -2.427 54.199 1.00 60.85 C ANISOU 2260 CD2 PHE B 103 6245 11153 5724 -3425 1438 -418 C ATOM 2261 CE1 PHE B 103 5.814 -5.078 53.415 1.00 62.95 C ANISOU 2261 CE1 PHE B 103 7144 10839 5937 -4112 1214 91 C ATOM 2262 CE2 PHE B 103 5.024 -2.841 53.021 1.00 59.95 C ANISOU 2262 CE2 PHE B 103 5988 11068 5723 -3455 1473 -429 C ATOM 2263 CZ PHE B 103 5.116 -4.165 52.628 1.00 60.88 C ANISOU 2263 CZ PHE B 103 6414 10906 5810 -3816 1371 -178 C ATOM 2264 N LEU B 104 8.067 -0.155 57.426 1.00 60.89 N ANISOU 2264 N LEU B 104 6657 10899 5580 -2965 1194 -542 N ATOM 2265 CA LEU B 104 8.234 0.621 58.642 1.00 63.48 C ANISOU 2265 CA LEU B 104 7038 11410 5671 -2949 1208 -687 C ATOM 2266 C LEU B 104 7.024 0.330 59.536 1.00 68.39 C ANISOU 2266 C LEU B 104 7552 12647 5787 -3348 1451 -805 C ATOM 2267 O LEU B 104 6.150 -0.445 59.149 1.00 69.76 O ANISOU 2267 O LEU B 104 7600 13071 5834 -3639 1583 -756 O ATOM 2268 CB LEU B 104 8.319 2.101 58.279 1.00 61.85 C ANISOU 2268 CB LEU B 104 6630 11186 5685 -2448 1247 -990 C ATOM 2269 CG LEU B 104 9.292 2.402 57.125 1.00 58.73 C ANISOU 2269 CG LEU B 104 6271 10271 5772 -2113 1075 -895 C ATOM 2270 CD1 LEU B 104 9.048 3.760 56.489 1.00 57.15 C ANISOU 2270 CD1 LEU B 104 5891 10068 5757 -1673 1135 -1182 C ATOM 2271 CD2 LEU B 104 10.731 2.278 57.599 1.00 58.52 C ANISOU 2271 CD2 LEU B 104 6523 9846 5866 -2139 816 -688 C ATOM 2272 N ARG B 105 6.965 0.938 60.718 1.00 71.88 N ANISOU 2272 N ARG B 105 8038 13359 5914 -3398 1519 -970 N ATOM 2273 CA ARG B 105 5.799 0.784 61.607 1.00 77.58 C ANISOU 2273 CA ARG B 105 8607 14758 6112 -3771 1803 -1141 C ATOM 2274 C ARG B 105 4.488 1.252 60.955 1.00 78.97 C ANISOU 2274 C ARG B 105 8249 15467 6289 -3585 2090 -1483 C ATOM 2275 O ARG B 105 3.455 0.596 61.094 1.00 82.18 O ANISOU 2275 O ARG B 105 8451 16394 6379 -3997 2306 -1509 O ATOM 2276 CB ARG B 105 6.012 1.511 62.938 1.00 80.34 C ANISOU 2276 CB ARG B 105 9094 15302 6129 -3780 1836 -1319 C ATOM 2277 CG ARG B 105 6.524 0.645 64.081 1.00 83.62 C ANISOU 2277 CG ARG B 105 9969 15641 6164 -4309 1695 -1012 C ATOM 2278 CD ARG B 105 6.177 1.297 65.407 1.00 88.26 C ANISOU 2278 CD ARG B 105 10580 16697 6259 -4433 1869 -1280 C ATOM 2279 NE ARG B 105 6.656 0.545 66.569 1.00 92.90 N ANISOU 2279 NE ARG B 105 11650 17225 6423 -4953 1717 -989 N ATOM 2280 CZ ARG B 105 5.979 -0.422 67.191 1.00 97.65 C ANISOU 2280 CZ ARG B 105 12391 18193 6517 -5598 1859 -832 C ATOM 2281 NH1 ARG B 105 4.777 -0.794 66.765 1.00 99.91 N ANISOU 2281 NH1 ARG B 105 12320 18982 6660 -5838 2177 -946 N ATOM 2282 NH2 ARG B 105 6.512 -1.028 68.245 1.00100.49 N ANISOU 2282 NH2 ARG B 105 13268 18423 6490 -6036 1662 -548 N ATOM 2283 N ASP B 106 4.552 2.374 60.234 1.00 77.28 N ANISOU 2283 N ASP B 106 7824 15119 6421 -2980 2067 -1736 N ATOM 2284 CA ASP B 106 3.393 2.959 59.545 1.00 78.64 C ANISOU 2284 CA ASP B 106 7499 15737 6646 -2667 2264 -2080 C ATOM 2285 C ASP B 106 2.958 2.127 58.337 1.00 77.16 C ANISOU 2285 C ASP B 106 7143 15518 6657 -2799 2250 -1906 C ATOM 2286 O ASP B 106 3.795 1.777 57.485 1.00 73.60 O ANISOU 2286 O ASP B 106 6931 14473 6563 -2719 2033 -1636 O ATOM 2287 CB ASP B 106 3.710 4.398 59.100 1.00 76.82 C ANISOU 2287 CB ASP B 106 7227 15235 6726 -1974 2165 -2354 C ATOM 2288 CG ASP B 106 2.459 5.230 58.859 1.00 79.79 C ANISOU 2288 CG ASP B 106 7125 16161 7031 -1574 2358 -2808 C ATOM 2289 OD1 ASP B 106 1.641 4.855 58.000 1.00 80.63 O ANISOU 2289 OD1 ASP B 106 6887 16533 7214 -1572 2426 -2832 O ATOM 2290 OD2 ASP B 106 2.286 6.268 59.527 1.00 81.95 O ANISOU 2290 OD2 ASP B 106 7368 16606 7166 -1235 2422 -3160 O ATOM 2291 N THR B 107 1.653 1.840 58.263 1.00 80.39 N ANISOU 2291 N THR B 107 7123 16598 6822 -2999 2486 -2089 N ATOM 2292 CA THR B 107 1.048 1.094 57.138 1.00 79.75 C ANISOU 2292 CA THR B 107 6831 16596 6874 -3160 2485 -1978 C ATOM 2293 C THR B 107 1.019 1.901 55.842 1.00 76.44 C ANISOU 2293 C THR B 107 6219 15939 6886 -2534 2363 -2123 C ATOM 2294 O THR B 107 1.018 1.332 54.754 1.00 74.80 O ANISOU 2294 O THR B 107 6024 15500 6898 -2590 2260 -1945 O ATOM 2295 CB THR B 107 -0.415 0.642 57.444 1.00 85.24 C ANISOU 2295 CB THR B 107 7041 18186 7159 -3579 2776 -2173 C ATOM 2296 OG1 THR B 107 -0.487 0.020 58.732 1.00 89.10 O ANISOU 2296 OG1 THR B 107 7710 18975 7168 -4190 2925 -2074 O ATOM 2297 CG2 THR B 107 -0.927 -0.344 56.385 1.00 85.29 C ANISOU 2297 CG2 THR B 107 6932 18222 7253 -3909 2738 -1988 C ATOM 2298 N LYS B 108 1.011 3.224 55.964 1.00 76.38 N ANISOU 2298 N LYS B 108 6092 15954 6974 -1949 2357 -2442 N ATOM 2299 CA LYS B 108 0.836 4.119 54.815 1.00 74.41 C ANISOU 2299 CA LYS B 108 5680 15527 7065 -1338 2232 -2615 C ATOM 2300 C LYS B 108 2.153 4.401 54.081 1.00 68.87 C ANISOU 2300 C LYS B 108 5426 13981 6762 -1102 1973 -2366 C ATOM 2301 O LYS B 108 2.209 5.243 53.184 1.00 67.01 O ANISOU 2301 O LYS B 108 5183 13488 6791 -618 1841 -2472 O ATOM 2302 CB LYS B 108 0.143 5.424 55.255 1.00 78.23 C ANISOU 2302 CB LYS B 108 5871 16408 7446 -790 2318 -3096 C ATOM 2303 CG LYS B 108 -1.235 5.210 55.889 1.00 84.23 C ANISOU 2303 CG LYS B 108 6071 18119 7812 -968 2606 -3410 C ATOM 2304 CD LYS B 108 -1.743 6.451 56.612 1.00 90.05 C ANISOU 2304 CD LYS B 108 6590 19231 8396 -427 2711 -3911 C ATOM 2305 CE LYS B 108 -2.462 7.410 55.673 1.00 91.96 C ANISOU 2305 CE LYS B 108 6501 19575 8864 305 2590 -4242 C ATOM 2306 NZ LYS B 108 -2.847 8.650 56.392 1.00 97.18 N ANISOU 2306 NZ LYS B 108 7046 20487 9390 906 2650 -4743 N ATOM 2307 N THR B 109 3.202 3.681 54.471 1.00 66.35 N ANISOU 2307 N THR B 109 5493 13257 6462 -1459 1894 -2038 N ATOM 2308 CA THR B 109 4.529 3.846 53.895 1.00 62.20 C ANISOU 2308 CA THR B 109 5337 12016 6280 -1300 1677 -1808 C ATOM 2309 C THR B 109 5.130 2.502 53.482 1.00 59.76 C ANISOU 2309 C THR B 109 5246 11398 6063 -1698 1597 -1431 C ATOM 2310 O THR B 109 4.680 1.446 53.918 1.00 61.92 O ANISOU 2310 O THR B 109 5509 11925 6091 -2155 1680 -1310 O ATOM 2311 CB THR B 109 5.510 4.530 54.901 1.00 62.23 C ANISOU 2311 CB THR B 109 5631 11760 6255 -1215 1594 -1826 C ATOM 2312 OG1 THR B 109 5.857 3.616 55.956 1.00 63.34 O ANISOU 2312 OG1 THR B 109 5950 11969 6148 -1685 1612 -1628 O ATOM 2313 CG2 THR B 109 4.910 5.806 55.499 1.00 65.03 C ANISOU 2313 CG2 THR B 109 5843 12407 6457 -843 1675 -2229 C ATOM 2314 N LEU B 110 6.157 2.551 52.644 1.00 56.06 N ANISOU 2314 N LEU B 110 4996 10376 5928 -1528 1434 -1259 N ATOM 2315 CA LEU B 110 7.001 1.386 52.385 1.00 53.67 C ANISOU 2315 CA LEU B 110 4958 9700 5736 -1802 1326 -934 C ATOM 2316 C LEU B 110 8.393 1.833 51.944 1.00 50.69 C ANISOU 2316 C LEU B 110 4791 8788 5683 -1551 1164 -827 C ATOM 2317 O LEU B 110 8.599 3.012 51.606 1.00 49.98 O ANISOU 2317 O LEU B 110 4661 8593 5737 -1214 1140 -981 O ATOM 2318 CB LEU B 110 6.356 0.432 51.365 1.00 53.46 C ANISOU 2318 CB LEU B 110 4851 9725 5737 -1983 1361 -841 C ATOM 2319 CG LEU B 110 6.136 0.778 49.886 1.00 51.08 C ANISOU 2319 CG LEU B 110 4429 9301 5679 -1701 1341 -904 C ATOM 2320 CD1 LEU B 110 7.444 0.799 49.104 1.00 46.05 C ANISOU 2320 CD1 LEU B 110 4041 8095 5362 -1521 1211 -745 C ATOM 2321 CD2 LEU B 110 5.191 -0.255 49.250 1.00 51.15 C ANISOU 2321 CD2 LEU B 110 4327 9533 5574 -2007 1395 -853 C ATOM 2322 N MET B 111 9.344 0.905 51.958 1.00 49.15 N ANISOU 2322 N MET B 111 4823 8265 5586 -1717 1044 -575 N ATOM 2323 CA MET B 111 10.684 1.185 51.437 1.00 46.03 C ANISOU 2323 CA MET B 111 4551 7437 5501 -1509 909 -482 C ATOM 2324 C MET B 111 11.123 0.102 50.467 1.00 44.76 C ANISOU 2324 C MET B 111 4490 6998 5520 -1559 859 -301 C ATOM 2325 O MET B 111 10.693 -1.049 50.567 1.00 45.93 O ANISOU 2325 O MET B 111 4741 7178 5531 -1817 855 -180 O ATOM 2326 CB MET B 111 11.734 1.241 52.547 1.00 46.56 C ANISOU 2326 CB MET B 111 4780 7369 5543 -1566 762 -391 C ATOM 2327 CG MET B 111 11.537 2.267 53.649 1.00 48.40 C ANISOU 2327 CG MET B 111 4993 7816 5580 -1536 780 -566 C ATOM 2328 SD MET B 111 13.012 2.371 54.705 1.00 50.20 S ANISOU 2328 SD MET B 111 5419 7817 5836 -1589 546 -440 S ATOM 2329 CE MET B 111 13.231 0.665 55.229 1.00 49.16 C ANISOU 2329 CE MET B 111 5493 7612 5575 -1893 413 -146 C ATOM 2330 N PHE B 112 12.006 0.481 49.545 1.00 42.61 N ANISOU 2330 N PHE B 112 4215 6445 5528 -1333 822 -291 N ATOM 2331 CA PHE B 112 12.766 -0.479 48.778 1.00 41.33 C ANISOU 2331 CA PHE B 112 4161 5991 5551 -1323 761 -147 C ATOM 2332 C PHE B 112 14.232 -0.259 49.100 1.00 41.25 C ANISOU 2332 C PHE B 112 4180 5766 5727 -1199 630 -87 C ATOM 2333 O PHE B 112 14.715 0.879 49.099 1.00 41.05 O ANISOU 2333 O PHE B 112 4064 5740 5792 -1076 635 -178 O ATOM 2334 CB PHE B 112 12.481 -0.348 47.282 1.00 39.73 C ANISOU 2334 CB PHE B 112 3892 5720 5483 -1197 863 -209 C ATOM 2335 CG PHE B 112 11.188 -0.992 46.866 1.00 39.83 C ANISOU 2335 CG PHE B 112 3888 5915 5331 -1362 940 -227 C ATOM 2336 CD1 PHE B 112 11.087 -2.381 46.761 1.00 40.91 C ANISOU 2336 CD1 PHE B 112 4202 5934 5407 -1572 897 -96 C ATOM 2337 CD2 PHE B 112 10.063 -0.218 46.605 1.00 40.97 C ANISOU 2337 CD2 PHE B 112 3849 6351 5369 -1310 1029 -383 C ATOM 2338 CE1 PHE B 112 9.877 -2.990 46.399 1.00 42.91 C ANISOU 2338 CE1 PHE B 112 4444 6379 5482 -1804 958 -111 C ATOM 2339 CE2 PHE B 112 8.851 -0.819 46.239 1.00 42.40 C ANISOU 2339 CE2 PHE B 112 3949 6774 5388 -1492 1088 -413 C ATOM 2340 CZ PHE B 112 8.760 -2.205 46.146 1.00 42.04 C ANISOU 2340 CZ PHE B 112 4075 6630 5268 -1778 1060 -271 C ATOM 2341 N GLY B 113 14.926 -1.346 49.416 1.00 41.86 N ANISOU 2341 N GLY B 113 4397 5664 5844 -1241 487 63 N ATOM 2342 CA GLY B 113 16.355 -1.282 49.709 1.00 42.56 C ANISOU 2342 CA GLY B 113 4455 5596 6119 -1099 330 113 C ATOM 2343 C GLY B 113 17.175 -1.889 48.595 1.00 42.25 C ANISOU 2343 C GLY B 113 4378 5345 6330 -913 332 128 C ATOM 2344 O GLY B 113 16.900 -2.996 48.163 1.00 43.53 O ANISOU 2344 O GLY B 113 4699 5364 6478 -923 318 189 O ATOM 2345 N SER B 114 18.191 -1.163 48.136 1.00 42.23 N ANISOU 2345 N SER B 114 4176 5333 6535 -765 355 57 N ATOM 2346 CA SER B 114 19.009 -1.616 47.014 1.00 41.93 C ANISOU 2346 CA SER B 114 4042 5173 6718 -583 411 23 C ATOM 2347 C SER B 114 20.384 -2.049 47.476 1.00 43.47 C ANISOU 2347 C SER B 114 4120 5318 7078 -418 218 55 C ATOM 2348 O SER B 114 20.943 -1.451 48.381 1.00 44.12 O ANISOU 2348 O SER B 114 4100 5503 7160 -461 85 71 O ATOM 2349 CB SER B 114 19.122 -0.502 45.994 1.00 40.47 C ANISOU 2349 CB SER B 114 3699 5064 6615 -577 610 -91 C ATOM 2350 OG SER B 114 17.836 -0.211 45.482 1.00 41.13 O ANISOU 2350 OG SER B 114 3891 5183 6554 -663 743 -125 O ATOM 2351 N TYR B 115 20.906 -3.107 46.861 1.00 44.66 N ANISOU 2351 N TYR B 115 4291 5317 7362 -212 183 48 N ATOM 2352 CA TYR B 115 22.188 -3.691 47.244 1.00 47.50 C ANISOU 2352 CA TYR B 115 4522 5634 7892 35 -35 53 C ATOM 2353 C TYR B 115 22.364 -3.800 48.760 1.00 48.89 C ANISOU 2353 C TYR B 115 4805 5808 7964 -25 -339 187 C ATOM 2354 O TYR B 115 23.442 -3.478 49.290 1.00 49.98 O ANISOU 2354 O TYR B 115 4702 6068 8221 78 -506 170 O ATOM 2355 CB TYR B 115 23.354 -2.873 46.673 1.00 47.93 C ANISOU 2355 CB TYR B 115 4155 5903 8153 128 76 -84 C ATOM 2356 CG TYR B 115 23.270 -2.559 45.201 1.00 48.23 C ANISOU 2356 CG TYR B 115 4087 5988 8249 126 393 -212 C ATOM 2357 CD1 TYR B 115 23.112 -1.239 44.768 1.00 47.61 C ANISOU 2357 CD1 TYR B 115 3899 6064 8128 -101 590 -258 C ATOM 2358 CD2 TYR B 115 23.359 -3.573 44.230 1.00 50.87 C ANISOU 2358 CD2 TYR B 115 4484 6187 8656 347 479 -290 C ATOM 2359 CE1 TYR B 115 23.044 -0.928 43.423 1.00 46.80 C ANISOU 2359 CE1 TYR B 115 3751 5994 8037 -135 858 -352 C ATOM 2360 CE2 TYR B 115 23.284 -3.266 42.866 1.00 50.38 C ANISOU 2360 CE2 TYR B 115 4349 6187 8605 316 775 -410 C ATOM 2361 CZ TYR B 115 23.132 -1.934 42.479 1.00 49.63 C ANISOU 2361 CZ TYR B 115 4143 6261 8451 61 960 -427 C ATOM 2362 OH TYR B 115 23.067 -1.584 41.152 1.00 50.83 O ANISOU 2362 OH TYR B 115 4273 6465 8574 -5 1230 -520 O ATOM 2363 N LEU B 116 21.329 -4.268 49.456 1.00 48.56 N ANISOU 2363 N LEU B 116 5114 5660 7677 -220 -416 316 N ATOM 2364 CA LEU B 116 21.385 -4.370 50.924 1.00 50.60 C ANISOU 2364 CA LEU B 116 5537 5927 7763 -337 -691 455 C ATOM 2365 C LEU B 116 22.489 -5.325 51.376 1.00 54.53 C ANISOU 2365 C LEU B 116 6089 6248 8383 -51 -1046 533 C ATOM 2366 O LEU B 116 22.906 -5.340 52.543 1.00 56.42 O ANISOU 2366 O LEU B 116 6403 6508 8528 -80 -1333 640 O ATOM 2367 CB LEU B 116 20.030 -4.797 51.474 1.00 50.11 C ANISOU 2367 CB LEU B 116 5844 5819 7377 -645 -665 571 C ATOM 2368 CG LEU B 116 19.134 -3.769 52.171 1.00 48.80 C ANISOU 2368 CG LEU B 116 5652 5920 6969 -944 -524 540 C ATOM 2369 CD1 LEU B 116 19.352 -2.353 51.704 1.00 45.92 C ANISOU 2369 CD1 LEU B 116 4957 5751 6739 -895 -331 368 C ATOM 2370 CD2 LEU B 116 17.677 -4.182 51.991 1.00 47.93 C ANISOU 2370 CD2 LEU B 116 5746 5847 6616 -1203 -349 565 C ATOM 2371 N ASP B 117 22.965 -6.101 50.409 1.00 56.22 N ANISOU 2371 N ASP B 117 6266 6294 8800 254 -1033 459 N ATOM 2372 CA ASP B 117 24.053 -7.048 50.574 1.00 60.78 C ANISOU 2372 CA ASP B 117 6854 6694 9546 652 -1358 471 C ATOM 2373 C ASP B 117 25.352 -6.329 50.949 1.00 62.18 C ANISOU 2373 C ASP B 117 6549 7158 9918 826 -1491 386 C ATOM 2374 O ASP B 117 25.885 -6.587 52.010 1.00 64.93 O ANISOU 2374 O ASP B 117 6967 7478 10225 907 -1859 496 O ATOM 2375 CB ASP B 117 24.209 -7.877 49.286 1.00 61.94 C ANISOU 2375 CB ASP B 117 7025 6645 9864 957 -1234 337 C ATOM 2376 CG ASP B 117 22.848 -8.165 48.595 1.00 61.62 C ANISOU 2376 CG ASP B 117 7321 6448 9643 680 -979 363 C ATOM 2377 OD1 ASP B 117 22.451 -9.355 48.545 1.00 66.24 O ANISOU 2377 OD1 ASP B 117 8364 6672 10133 725 -1131 444 O ATOM 2378 OD2 ASP B 117 22.165 -7.216 48.111 1.00 57.70 O ANISOU 2378 OD2 ASP B 117 6656 6178 9088 413 -657 302 O ATOM 2379 N ASP B 118 25.835 -5.407 50.111 1.00 60.91 N ANISOU 2379 N ASP B 118 5922 7284 9936 830 -1209 203 N ATOM 2380 CA ASP B 118 27.167 -4.818 50.324 1.00 63.72 C ANISOU 2380 CA ASP B 118 5771 7950 10489 970 -1325 99 C ATOM 2381 C ASP B 118 27.218 -3.395 50.895 1.00 61.91 C ANISOU 2381 C ASP B 118 5344 8005 10176 599 -1260 101 C ATOM 2382 O ASP B 118 26.532 -2.480 50.433 1.00 58.00 O ANISOU 2382 O ASP B 118 4868 7575 9594 308 -950 60 O ATOM 2383 CB ASP B 118 28.064 -4.940 49.079 1.00 65.80 C ANISOU 2383 CB ASP B 118 5598 8381 11024 1271 -1129 -127 C ATOM 2384 CG ASP B 118 27.618 -4.051 47.952 1.00 62.86 C ANISOU 2384 CG ASP B 118 5095 8151 10639 1008 -670 -237 C ATOM 2385 OD1 ASP B 118 26.402 -3.773 47.868 1.00 61.79 O ANISOU 2385 OD1 ASP B 118 5304 7862 10312 729 -509 -148 O ATOM 2386 OD2 ASP B 118 28.473 -3.627 47.152 1.00 63.32 O ANISOU 2386 OD2 ASP B 118 4705 8493 10860 1071 -478 -414 O ATOM 2387 N GLU B 119 28.097 -3.234 51.881 1.00 65.07 N ANISOU 2387 N GLU B 119 5562 8556 10605 643 -1589 136 N ATOM 2388 CA GLU B 119 28.223 -2.004 52.651 1.00 64.50 C ANISOU 2388 CA GLU B 119 5380 8706 10421 295 -1624 146 C ATOM 2389 C GLU B 119 28.599 -0.802 51.771 1.00 63.15 C ANISOU 2389 C GLU B 119 4829 8800 10363 87 -1298 -20 C ATOM 2390 O GLU B 119 28.280 0.339 52.105 1.00 61.10 O ANISOU 2390 O GLU B 119 4636 8615 9966 -263 -1210 -24 O ATOM 2391 CB GLU B 119 29.250 -2.217 53.767 1.00 68.78 C ANISOU 2391 CB GLU B 119 5766 9374 10993 423 -2084 202 C ATOM 2392 CG GLU B 119 29.025 -1.389 55.029 1.00 69.23 C ANISOU 2392 CG GLU B 119 6003 9503 10800 66 -2255 292 C ATOM 2393 CD GLU B 119 29.815 -1.899 56.238 1.00 75.50 C ANISOU 2393 CD GLU B 119 6801 10334 11552 212 -2782 403 C ATOM 2394 OE1 GLU B 119 30.980 -2.343 56.070 1.00 79.10 O ANISOU 2394 OE1 GLU B 119 6851 10948 12255 547 -3015 335 O ATOM 2395 OE2 GLU B 119 29.268 -1.848 57.365 1.00 76.31 O ANISOU 2395 OE2 GLU B 119 7305 10332 11356 -2 -2970 547 O ATOM 2396 N LYS B 120 29.254 -1.070 50.641 1.00 64.28 N ANISOU 2396 N LYS B 120 4623 9071 10731 294 -1119 -161 N ATOM 2397 CA LYS B 120 29.778 -0.008 49.780 1.00 64.06 C ANISOU 2397 CA LYS B 120 4225 9326 10789 60 -825 -307 C ATOM 2398 C LYS B 120 28.742 0.625 48.841 1.00 59.89 C ANISOU 2398 C LYS B 120 3956 8654 10144 -180 -438 -320 C ATOM 2399 O LYS B 120 28.961 1.716 48.307 1.00 59.42 O ANISOU 2399 O LYS B 120 3757 8750 10072 -479 -229 -391 O ATOM 2400 CB LYS B 120 31.005 -0.501 48.996 1.00 68.14 C ANISOU 2400 CB LYS B 120 4198 10131 11560 351 -778 -479 C ATOM 2401 CG LYS B 120 30.857 -1.850 48.293 1.00 69.33 C ANISOU 2401 CG LYS B 120 4438 10087 11818 816 -736 -533 C ATOM 2402 CD LYS B 120 32.203 -2.270 47.684 1.00 76.89 C ANISOU 2402 CD LYS B 120 4784 11407 13024 1155 -721 -755 C ATOM 2403 CE LYS B 120 32.068 -3.421 46.667 1.00 78.58 C ANISOU 2403 CE LYS B 120 5081 11444 13332 1594 -568 -881 C ATOM 2404 NZ LYS B 120 32.137 -4.787 47.280 1.00 80.59 N ANISOU 2404 NZ LYS B 120 5572 11393 13655 2118 -970 -832 N ATOM 2405 N ASN B 121 27.614 -0.049 48.658 1.00 56.89 N ANISOU 2405 N ASN B 121 3975 7978 9664 -71 -371 -245 N ATOM 2406 CA ASN B 121 26.636 0.369 47.652 1.00 53.62 C ANISOU 2406 CA ASN B 121 3771 7445 9157 -219 -37 -270 C ATOM 2407 C ASN B 121 25.198 0.508 48.114 1.00 50.42 C ANISOU 2407 C ASN B 121 3807 6825 8527 -356 -27 -168 C ATOM 2408 O ASN B 121 24.360 1.031 47.378 1.00 47.93 O ANISOU 2408 O ASN B 121 3644 6443 8123 -481 206 -195 O ATOM 2409 CB ASN B 121 26.678 -0.604 46.472 1.00 54.11 C ANISOU 2409 CB ASN B 121 3786 7440 9332 49 138 -349 C ATOM 2410 CG ASN B 121 27.823 -0.327 45.547 1.00 55.55 C ANISOU 2410 CG ASN B 121 3519 7911 9678 78 322 -511 C ATOM 2411 OD1 ASN B 121 27.910 0.755 44.963 1.00 52.25 O ANISOU 2411 OD1 ASN B 121 3011 7631 9209 -226 543 -555 O ATOM 2412 ND2 ASN B 121 28.723 -1.301 45.407 1.00 59.06 N ANISOU 2412 ND2 ASN B 121 3685 8454 10300 445 226 -612 N ATOM 2413 N TRP B 122 24.914 0.044 49.330 1.00 51.42 N ANISOU 2413 N TRP B 122 4127 6869 8539 -335 -287 -57 N ATOM 2414 CA TRP B 122 23.539 -0.075 49.828 1.00 49.10 C ANISOU 2414 CA TRP B 122 4215 6434 8008 -455 -270 27 C ATOM 2415 C TRP B 122 22.811 1.265 49.882 1.00 47.03 C ANISOU 2415 C TRP B 122 4038 6234 7599 -696 -114 -33 C ATOM 2416 O TRP B 122 23.444 2.317 50.008 1.00 47.55 O ANISOU 2416 O TRP B 122 3961 6406 7701 -824 -125 -97 O ATOM 2417 CB TRP B 122 23.500 -0.790 51.190 1.00 50.87 C ANISOU 2417 CB TRP B 122 4638 6596 8095 -444 -583 162 C ATOM 2418 CG TRP B 122 24.215 -0.099 52.366 1.00 53.74 C ANISOU 2418 CG TRP B 122 4906 7106 8406 -559 -821 176 C ATOM 2419 CD1 TRP B 122 24.475 1.242 52.520 1.00 53.49 C ANISOU 2419 CD1 TRP B 122 4744 7224 8356 -757 -760 83 C ATOM 2420 CD2 TRP B 122 24.700 -0.733 53.561 1.00 57.34 C ANISOU 2420 CD2 TRP B 122 5459 7542 8786 -505 -1185 298 C ATOM 2421 NE1 TRP B 122 25.108 1.470 53.718 1.00 55.64 N ANISOU 2421 NE1 TRP B 122 4997 7593 8552 -840 -1051 123 N ATOM 2422 CE2 TRP B 122 25.254 0.279 54.380 1.00 58.39 C ANISOU 2422 CE2 TRP B 122 5472 7853 8861 -682 -1320 259 C ATOM 2423 CE3 TRP B 122 24.719 -2.060 54.017 1.00 60.06 C ANISOU 2423 CE3 TRP B 122 6032 7703 9084 -336 -1440 443 C ATOM 2424 CZ2 TRP B 122 25.823 0.006 55.635 1.00 62.28 C ANISOU 2424 CZ2 TRP B 122 6031 8385 9250 -690 -1697 359 C ATOM 2425 CZ3 TRP B 122 25.286 -2.334 55.267 1.00 64.27 C ANISOU 2425 CZ3 TRP B 122 6661 8247 9512 -330 -1830 559 C ATOM 2426 CH2 TRP B 122 25.833 -1.304 56.057 1.00 65.82 C ANISOU 2426 CH2 TRP B 122 6695 8662 9651 -504 -1953 515 C ATOM 2427 N GLY B 123 21.486 1.216 49.783 1.00 44.57 N ANISOU 2427 N GLY B 123 3964 5856 7115 -754 14 -25 N ATOM 2428 CA GLY B 123 20.666 2.426 49.826 1.00 43.21 C ANISOU 2428 CA GLY B 123 3891 5729 6797 -892 140 -111 C ATOM 2429 C GLY B 123 19.193 2.153 50.023 1.00 41.37 C ANISOU 2429 C GLY B 123 3857 5510 6350 -926 225 -110 C ATOM 2430 O GLY B 123 18.766 1.013 49.962 1.00 41.62 O ANISOU 2430 O GLY B 123 3973 5499 6343 -904 216 -27 O ATOM 2431 N LEU B 124 18.410 3.202 50.247 1.00 41.47 N ANISOU 2431 N LEU B 124 3947 5593 6216 -982 302 -218 N ATOM 2432 CA LEU B 124 16.977 3.049 50.578 1.00 41.33 C ANISOU 2432 CA LEU B 124 4039 5696 5969 -1014 388 -261 C ATOM 2433 C LEU B 124 16.093 4.094 49.923 1.00 41.05 C ANISOU 2433 C LEU B 124 4016 5694 5888 -931 531 -414 C ATOM 2434 O LEU B 124 16.416 5.291 49.931 1.00 41.46 O ANISOU 2434 O LEU B 124 4111 5681 5962 -899 507 -511 O ATOM 2435 CB LEU B 124 16.763 3.160 52.089 1.00 42.59 C ANISOU 2435 CB LEU B 124 4295 5994 5894 -1133 278 -270 C ATOM 2436 CG LEU B 124 17.203 1.974 52.937 1.00 44.71 C ANISOU 2436 CG LEU B 124 4645 6248 6096 -1237 105 -98 C ATOM 2437 CD1 LEU B 124 17.442 2.402 54.366 1.00 46.70 C ANISOU 2437 CD1 LEU B 124 4995 6604 6144 -1359 -46 -111 C ATOM 2438 CD2 LEU B 124 16.175 0.839 52.870 1.00 40.95 C ANISOU 2438 CD2 LEU B 124 4272 5826 5461 -1341 180 -15 C ATOM 2439 N SER B 125 14.951 3.641 49.411 1.00 40.49 N ANISOU 2439 N SER B 125 3931 5721 5732 -903 648 -438 N ATOM 2440 CA SER B 125 13.978 4.525 48.775 1.00 40.37 C ANISOU 2440 CA SER B 125 3910 5765 5662 -770 744 -589 C ATOM 2441 C SER B 125 12.683 4.482 49.546 1.00 41.46 C ANISOU 2441 C SER B 125 4001 6202 5551 -783 798 -703 C ATOM 2442 O SER B 125 12.195 3.400 49.878 1.00 41.87 O ANISOU 2442 O SER B 125 4013 6410 5485 -945 833 -625 O ATOM 2443 CB SER B 125 13.738 4.099 47.329 1.00 39.10 C ANISOU 2443 CB SER B 125 3719 5521 5616 -714 831 -545 C ATOM 2444 OG SER B 125 14.965 4.043 46.655 1.00 40.54 O ANISOU 2444 OG SER B 125 3914 5492 6000 -724 818 -458 O ATOM 2445 N PHE B 126 12.135 5.672 49.809 1.00 42.11 N ANISOU 2445 N PHE B 126 4101 6363 5537 -618 804 -902 N ATOM 2446 CA PHE B 126 11.021 5.869 50.732 1.00 43.81 C ANISOU 2446 CA PHE B 126 4232 6921 5492 -590 867 -1080 C ATOM 2447 C PHE B 126 9.755 6.306 49.978 1.00 44.19 C ANISOU 2447 C PHE B 126 4141 7154 5495 -358 940 -1258 C ATOM 2448 O PHE B 126 9.796 7.241 49.153 1.00 44.34 O ANISOU 2448 O PHE B 126 4252 6963 5632 -114 879 -1333 O ATOM 2449 CB PHE B 126 11.444 6.899 51.796 1.00 44.72 C ANISOU 2449 CB PHE B 126 4485 6994 5512 -532 789 -1216 C ATOM 2450 CG PHE B 126 10.397 7.209 52.836 1.00 48.29 C ANISOU 2450 CG PHE B 126 4858 7820 5669 -478 874 -1449 C ATOM 2451 CD1 PHE B 126 9.621 6.205 53.410 1.00 47.99 C ANISOU 2451 CD1 PHE B 126 4657 8164 5411 -695 996 -1423 C ATOM 2452 CD2 PHE B 126 10.246 8.509 53.293 1.00 50.75 C ANISOU 2452 CD2 PHE B 126 5289 8098 5896 -238 832 -1702 C ATOM 2453 CE1 PHE B 126 8.688 6.502 54.387 1.00 52.66 C ANISOU 2453 CE1 PHE B 126 5140 9170 5697 -678 1113 -1660 C ATOM 2454 CE2 PHE B 126 9.309 8.817 54.283 1.00 54.72 C ANISOU 2454 CE2 PHE B 126 5702 8981 6108 -152 932 -1965 C ATOM 2455 CZ PHE B 126 8.525 7.808 54.826 1.00 55.00 C ANISOU 2455 CZ PHE B 126 5509 9470 5919 -379 1092 -1949 C ATOM 2456 N TYR B 127 8.652 5.622 50.268 1.00 44.91 N ANISOU 2456 N TYR B 127 4020 7646 5397 -457 1052 -1318 N ATOM 2457 CA TYR B 127 7.378 5.783 49.559 1.00 46.14 C ANISOU 2457 CA TYR B 127 3952 8081 5500 -275 1112 -1479 C ATOM 2458 C TYR B 127 6.202 5.925 50.513 1.00 49.57 C ANISOU 2458 C TYR B 127 4130 9054 5649 -250 1230 -1727 C ATOM 2459 O TYR B 127 6.151 5.254 51.540 1.00 50.47 O ANISOU 2459 O TYR B 127 4211 9404 5561 -559 1320 -1683 O ATOM 2460 CB TYR B 127 7.140 4.583 48.630 1.00 44.93 C ANISOU 2460 CB TYR B 127 3719 7947 5407 -494 1148 -1297 C ATOM 2461 CG TYR B 127 8.250 4.410 47.606 1.00 42.84 C ANISOU 2461 CG TYR B 127 3670 7207 5399 -493 1067 -1095 C ATOM 2462 CD1 TYR B 127 9.324 3.562 47.853 1.00 42.50 C ANISOU 2462 CD1 TYR B 127 3774 6931 5442 -724 1044 -881 C ATOM 2463 CD2 TYR B 127 8.229 5.121 46.412 1.00 40.94 C ANISOU 2463 CD2 TYR B 127 3489 6772 5296 -248 1007 -1133 C ATOM 2464 CE1 TYR B 127 10.367 3.431 46.917 1.00 42.20 C ANISOU 2464 CE1 TYR B 127 3875 6527 5633 -695 999 -743 C ATOM 2465 CE2 TYR B 127 9.225 4.990 45.486 1.00 41.49 C ANISOU 2465 CE2 TYR B 127 3737 6472 5556 -282 974 -971 C ATOM 2466 CZ TYR B 127 10.294 4.155 45.739 1.00 39.85 C ANISOU 2466 CZ TYR B 127 3611 6089 5441 -499 988 -794 C ATOM 2467 OH TYR B 127 11.271 4.052 44.803 1.00 41.77 O ANISOU 2467 OH TYR B 127 3973 6035 5861 -507 983 -679 O ATOM 2468 N ALA B 128 5.252 6.788 50.153 1.00 51.89 N ANISOU 2468 N ALA B 128 4246 9558 5911 123 1224 -1995 N ATOM 2469 CA ALA B 128 4.061 7.045 50.969 1.00 55.82 C ANISOU 2469 CA ALA B 128 4421 10646 6141 233 1353 -2305 C ATOM 2470 C ALA B 128 2.823 7.150 50.088 1.00 58.09 C ANISOU 2470 C ALA B 128 4358 11288 6426 482 1352 -2481 C ATOM 2471 O ALA B 128 2.934 7.331 48.867 1.00 56.77 O ANISOU 2471 O ALA B 128 4285 10821 6465 660 1209 -2389 O ATOM 2472 CB ALA B 128 4.234 8.303 51.780 1.00 57.79 C ANISOU 2472 CB ALA B 128 4819 10818 6322 574 1310 -2565 C ATOM 2473 N ASP B 129 1.650 7.024 50.700 1.00 61.69 N ANISOU 2473 N ASP B 129 4394 12416 6628 476 1509 -2738 N ATOM 2474 CA ASP B 129 0.385 7.057 49.961 1.00 64.61 C ANISOU 2474 CA ASP B 129 4327 13251 6969 694 1503 -2935 C ATOM 2475 C ASP B 129 -0.037 8.508 49.721 1.00 67.47 C ANISOU 2475 C ASP B 129 4664 13569 7402 1417 1348 -3274 C ATOM 2476 O ASP B 129 -1.089 8.782 49.142 1.00 70.80 O ANISOU 2476 O ASP B 129 4723 14367 7813 1751 1285 -3495 O ATOM 2477 CB ASP B 129 -0.697 6.255 50.704 1.00 67.81 C ANISOU 2477 CB ASP B 129 4239 14472 7053 327 1750 -3075 C ATOM 2478 CG ASP B 129 -1.232 6.973 51.959 1.00 72.79 C ANISOU 2478 CG ASP B 129 4640 15592 7423 549 1911 -3460 C ATOM 2479 OD1 ASP B 129 -0.457 7.618 52.697 1.00 72.56 O ANISOU 2479 OD1 ASP B 129 4960 15220 7392 690 1888 -3496 O ATOM 2480 OD2 ASP B 129 -2.448 6.892 52.211 1.00 76.00 O ANISOU 2480 OD2 ASP B 129 4498 16770 7609 574 2068 -3752 O ATOM 2481 N LYS B 130 0.797 9.429 50.198 1.00 66.96 N ANISOU 2481 N LYS B 130 5008 13035 7399 1654 1261 -3317 N ATOM 2482 CA LYS B 130 0.593 10.861 50.020 1.00 69.22 C ANISOU 2482 CA LYS B 130 5446 13104 7750 2330 1067 -3610 C ATOM 2483 C LYS B 130 1.912 11.473 49.543 1.00 66.45 C ANISOU 2483 C LYS B 130 5726 11902 7622 2361 860 -3368 C ATOM 2484 O LYS B 130 2.978 10.888 49.768 1.00 62.38 O ANISOU 2484 O LYS B 130 5446 11092 7164 1901 918 -3067 O ATOM 2485 CB LYS B 130 0.116 11.506 51.329 1.00 73.67 C ANISOU 2485 CB LYS B 130 5865 14057 8071 2586 1196 -4014 C ATOM 2486 CG LYS B 130 -1.409 11.419 51.577 1.00 76.59 C ANISOU 2486 CG LYS B 130 5559 15311 8231 2826 1345 -4406 C ATOM 2487 CD LYS B 130 -1.731 11.477 53.069 1.00 78.92 C ANISOU 2487 CD LYS B 130 5650 16136 8202 2744 1616 -4707 C ATOM 2488 CE LYS B 130 -3.226 11.649 53.341 1.00 82.82 C ANISOU 2488 CE LYS B 130 5447 17541 8479 3097 1767 -5189 C ATOM 2489 NZ LYS B 130 -3.441 11.939 54.782 1.00 88.95 N ANISOU 2489 NZ LYS B 130 6111 18761 8924 3105 2024 -5534 N ATOM 2490 N PRO B 131 1.847 12.637 48.858 1.00 68.57 N ANISOU 2490 N PRO B 131 6270 11780 8002 2892 602 -3495 N ATOM 2491 CA PRO B 131 3.074 13.284 48.356 1.00 66.64 C ANISOU 2491 CA PRO B 131 6642 10748 7932 2860 409 -3267 C ATOM 2492 C PRO B 131 3.959 13.858 49.471 1.00 67.01 C ANISOU 2492 C PRO B 131 7036 10511 7914 2766 427 -3321 C ATOM 2493 O PRO B 131 5.152 14.124 49.254 1.00 65.15 O ANISOU 2493 O PRO B 131 7237 9717 7800 2537 329 -3084 O ATOM 2494 CB PRO B 131 2.538 14.411 47.462 1.00 69.66 C ANISOU 2494 CB PRO B 131 7240 10854 8376 3468 112 -3434 C ATOM 2495 CG PRO B 131 1.148 14.659 47.941 1.00 74.00 C ANISOU 2495 CG PRO B 131 7320 12025 8771 3954 142 -3863 C ATOM 2496 CD PRO B 131 0.634 13.331 48.385 1.00 72.88 C ANISOU 2496 CD PRO B 131 6576 12596 8519 3516 451 -3825 C ATOM 2497 N GLU B 132 3.375 14.034 50.650 1.00 70.25 N ANISOU 2497 N GLU B 132 7232 11346 8113 2914 559 -3642 N ATOM 2498 CA GLU B 132 4.101 14.485 51.826 1.00 71.28 C ANISOU 2498 CA GLU B 132 7655 11300 8129 2796 590 -3724 C ATOM 2499 C GLU B 132 3.876 13.482 52.951 1.00 71.16 C ANISOU 2499 C GLU B 132 7265 11877 7895 2400 879 -3740 C ATOM 2500 O GLU B 132 2.790 12.911 53.087 1.00 73.14 O ANISOU 2500 O GLU B 132 7016 12770 8004 2429 1056 -3895 O ATOM 2501 CB GLU B 132 3.618 15.889 52.261 1.00 76.77 C ANISOU 2501 CB GLU B 132 8586 11869 8713 3420 442 -4162 C ATOM 2502 CG GLU B 132 3.977 17.011 51.271 1.00 78.66 C ANISOU 2502 CG GLU B 132 9375 11388 9125 3773 101 -4126 C ATOM 2503 CD GLU B 132 2.855 18.038 51.084 1.00 85.47 C ANISOU 2503 CD GLU B 132 10246 12304 9924 4566 -83 -4556 C ATOM 2504 OE1 GLU B 132 2.651 18.872 51.992 1.00 89.81 O ANISOU 2504 OE1 GLU B 132 10975 12834 10314 4921 -115 -4929 O ATOM 2505 OE2 GLU B 132 2.195 18.020 50.014 1.00 86.62 O ANISOU 2505 OE2 GLU B 132 10242 12496 10176 4857 -221 -4531 O ATOM 2506 N THR B 133 4.907 13.282 53.759 1.00 69.39 N ANISOU 2506 N THR B 133 7293 11449 7623 2005 909 -3576 N ATOM 2507 CA THR B 133 4.798 12.474 54.964 1.00 69.79 C ANISOU 2507 CA THR B 133 7124 11979 7415 1626 1136 -3587 C ATOM 2508 C THR B 133 4.809 13.392 56.178 1.00 73.83 C ANISOU 2508 C THR B 133 7839 12527 7686 1823 1146 -3930 C ATOM 2509 O THR B 133 5.192 14.564 56.082 1.00 75.03 O ANISOU 2509 O THR B 133 8390 12205 7913 2159 946 -4079 O ATOM 2510 CB THR B 133 5.964 11.463 55.077 1.00 65.82 C ANISOU 2510 CB THR B 133 6763 11245 7000 1033 1131 -3145 C ATOM 2511 OG1 THR B 133 7.212 12.140 54.876 1.00 63.33 O ANISOU 2511 OG1 THR B 133 6893 10295 6873 1020 917 -3003 O ATOM 2512 CG2 THR B 133 5.820 10.361 54.048 1.00 62.04 C ANISOU 2512 CG2 THR B 133 6055 10828 6688 808 1171 -2853 C ATOM 2513 N THR B 134 4.369 12.857 57.314 1.00 76.26 N ANISOU 2513 N THR B 134 7910 13393 7672 1587 1378 -4058 N ATOM 2514 CA THR B 134 4.475 13.552 58.593 1.00 80.02 C ANISOU 2514 CA THR B 134 8597 13943 7863 1667 1419 -4359 C ATOM 2515 C THR B 134 5.836 13.288 59.246 1.00 77.66 C ANISOU 2515 C THR B 134 8692 13262 7552 1182 1310 -4053 C ATOM 2516 O THR B 134 6.526 12.317 58.904 1.00 74.05 O ANISOU 2516 O THR B 134 8226 12661 7247 750 1272 -3628 O ATOM 2517 CB THR B 134 3.353 13.133 59.567 1.00 84.21 C ANISOU 2517 CB THR B 134 8692 15316 7990 1607 1742 -4666 C ATOM 2518 OG1 THR B 134 3.146 11.713 59.491 1.00 81.33 O ANISOU 2518 OG1 THR B 134 8004 15336 7562 1058 1911 -4349 O ATOM 2519 CG2 THR B 134 2.050 13.878 59.255 1.00 89.52 C ANISOU 2519 CG2 THR B 134 9015 16382 8614 2266 1813 -5156 C ATOM 2520 N LYS B 135 6.209 14.170 60.175 1.00 80.34 N ANISOU 2520 N LYS B 135 9376 13441 7708 1286 1241 -4292 N ATOM 2521 CA LYS B 135 7.396 14.026 61.023 1.00 79.21 C ANISOU 2521 CA LYS B 135 9581 13041 7476 848 1127 -4083 C ATOM 2522 C LYS B 135 7.595 12.582 61.469 1.00 77.51 C ANISOU 2522 C LYS B 135 9160 13154 7136 275 1249 -3737 C ATOM 2523 O LYS B 135 8.726 12.105 61.570 1.00 74.91 O ANISOU 2523 O LYS B 135 9031 12512 6919 -94 1082 -3383 O ATOM 2524 CB LYS B 135 7.256 14.908 62.276 1.00 83.95 C ANISOU 2524 CB LYS B 135 10432 13750 7715 999 1156 -4495 C ATOM 2525 CG LYS B 135 6.877 16.353 62.006 1.00 86.58 C ANISOU 2525 CG LYS B 135 11016 13788 8094 1628 1039 -4920 C ATOM 2526 CD LYS B 135 5.979 16.921 63.107 1.00 91.14 C ANISOU 2526 CD LYS B 135 11552 14826 8250 1939 1231 -5469 C ATOM 2527 CE LYS B 135 5.754 18.416 62.924 1.00 93.42 C ANISOU 2527 CE LYS B 135 12221 14697 8578 2597 1048 -5903 C ATOM 2528 NZ LYS B 135 5.491 18.808 61.506 1.00 90.87 N ANISOU 2528 NZ LYS B 135 11881 14013 8633 3015 873 -5839 N ATOM 2529 N GLU B 136 6.481 11.905 61.735 1.00 79.79 N ANISOU 2529 N GLU B 136 9055 14081 7182 205 1524 -3852 N ATOM 2530 CA GLU B 136 6.467 10.543 62.262 1.00 79.83 C ANISOU 2530 CA GLU B 136 8919 14436 6977 -362 1654 -3560 C ATOM 2531 C GLU B 136 6.945 9.497 61.236 1.00 75.31 C ANISOU 2531 C GLU B 136 8276 13598 6739 -612 1549 -3096 C ATOM 2532 O GLU B 136 7.926 8.778 61.477 1.00 73.64 O ANISOU 2532 O GLU B 136 8277 13129 6575 -987 1400 -2736 O ATOM 2533 CB GLU B 136 5.067 10.204 62.798 1.00 84.04 C ANISOU 2533 CB GLU B 136 9046 15767 7120 -405 1999 -3849 C ATOM 2534 CG GLU B 136 4.570 11.129 63.925 1.00 90.63 C ANISOU 2534 CG GLU B 136 9925 16951 7558 -173 2150 -4346 C ATOM 2535 CD GLU B 136 3.833 12.379 63.425 1.00 94.18 C ANISOU 2535 CD GLU B 136 10238 17418 8128 564 2163 -4832 C ATOM 2536 OE1 GLU B 136 2.630 12.520 63.736 1.00 98.67 O ANISOU 2536 OE1 GLU B 136 10403 18658 8429 783 2437 -5237 O ATOM 2537 OE2 GLU B 136 4.447 13.221 62.728 1.00 92.02 O ANISOU 2537 OE2 GLU B 136 10264 16501 8198 924 1891 -4818 O ATOM 2538 N GLN B 137 6.269 9.425 60.090 1.00 73.86 N ANISOU 2538 N GLN B 137 7807 13474 6781 -374 1606 -3122 N ATOM 2539 CA GLN B 137 6.661 8.512 59.007 1.00 69.18 C ANISOU 2539 CA GLN B 137 7163 12620 6502 -557 1517 -2736 C ATOM 2540 C GLN B 137 8.084 8.787 58.542 1.00 65.70 C ANISOU 2540 C GLN B 137 7057 11511 6395 -544 1246 -2485 C ATOM 2541 O GLN B 137 8.871 7.851 58.364 1.00 63.76 O ANISOU 2541 O GLN B 137 6893 11056 6276 -857 1148 -2128 O ATOM 2542 CB GLN B 137 5.680 8.609 57.836 1.00 69.08 C ANISOU 2542 CB GLN B 137 6818 12771 6656 -250 1595 -2860 C ATOM 2543 CG GLN B 137 4.219 8.339 58.243 1.00 72.85 C ANISOU 2543 CG GLN B 137 6860 14011 6807 -269 1871 -3140 C ATOM 2544 CD GLN B 137 3.185 8.697 57.173 1.00 74.43 C ANISOU 2544 CD GLN B 137 6695 14427 7157 146 1905 -3354 C ATOM 2545 OE1 GLN B 137 3.398 9.586 56.344 1.00 73.46 O ANISOU 2545 OE1 GLN B 137 6703 13896 7311 603 1723 -3429 O ATOM 2546 NE2 GLN B 137 2.042 8.011 57.207 1.00 77.47 N ANISOU 2546 NE2 GLN B 137 6628 15476 7330 -39 2124 -3452 N ATOM 2547 N LEU B 138 8.421 10.066 58.367 1.00 65.35 N ANISOU 2547 N LEU B 138 7213 11142 6474 -190 1119 -2683 N ATOM 2548 CA LEU B 138 9.765 10.476 57.943 1.00 62.21 C ANISOU 2548 CA LEU B 138 7116 10162 6360 -221 877 -2482 C ATOM 2549 C LEU B 138 10.861 9.962 58.894 1.00 61.62 C ANISOU 2549 C LEU B 138 7224 9992 6195 -616 754 -2258 C ATOM 2550 O LEU B 138 11.929 9.546 58.447 1.00 58.53 O ANISOU 2550 O LEU B 138 6900 9289 6051 -785 599 -1966 O ATOM 2551 CB LEU B 138 9.831 12.002 57.822 1.00 64.05 C ANISOU 2551 CB LEU B 138 7607 10089 6639 159 759 -2768 C ATOM 2552 CG LEU B 138 10.991 12.658 57.076 1.00 61.77 C ANISOU 2552 CG LEU B 138 7614 9212 6645 155 531 -2610 C ATOM 2553 CD1 LEU B 138 10.825 12.487 55.574 1.00 60.91 C ANISOU 2553 CD1 LEU B 138 7387 8934 6821 291 531 -2463 C ATOM 2554 CD2 LEU B 138 11.083 14.132 57.427 1.00 64.94 C ANISOU 2554 CD2 LEU B 138 8389 9323 6960 413 394 -2909 C ATOM 2555 N GLY B 139 10.573 9.996 60.198 1.00 64.33 N ANISOU 2555 N GLY B 139 7634 10638 6170 -744 820 -2414 N ATOM 2556 CA GLY B 139 11.458 9.466 61.237 1.00 64.81 C ANISOU 2556 CA GLY B 139 7882 10675 6067 -1121 686 -2215 C ATOM 2557 C GLY B 139 11.812 7.995 61.078 1.00 62.83 C ANISOU 2557 C GLY B 139 7543 10445 5884 -1451 646 -1822 C ATOM 2558 O GLY B 139 12.980 7.615 61.201 1.00 61.76 O ANISOU 2558 O GLY B 139 7544 10037 5885 -1625 415 -1563 O ATOM 2559 N GLU B 140 10.810 7.161 60.806 1.00 62.72 N ANISOU 2559 N GLU B 140 7308 10754 5769 -1533 849 -1789 N ATOM 2560 CA GLU B 140 11.043 5.737 60.549 1.00 61.24 C ANISOU 2560 CA GLU B 140 7101 10528 5641 -1833 801 -1427 C ATOM 2561 C GLU B 140 12.030 5.562 59.378 1.00 57.61 C ANISOU 2561 C GLU B 140 6637 9606 5648 -1703 626 -1204 C ATOM 2562 O GLU B 140 12.943 4.728 59.435 1.00 56.59 O ANISOU 2562 O GLU B 140 6618 9260 5625 -1875 438 -917 O ATOM 2563 CB GLU B 140 9.715 5.007 60.301 1.00 62.16 C ANISOU 2563 CB GLU B 140 6978 11063 5576 -1958 1058 -1466 C ATOM 2564 CG GLU B 140 8.943 4.676 61.591 1.00 67.22 C ANISOU 2564 CG GLU B 140 7641 12208 5690 -2287 1226 -1564 C ATOM 2565 CD GLU B 140 7.444 4.459 61.389 1.00 71.10 C ANISOU 2565 CD GLU B 140 7786 13259 5968 -2338 1541 -1766 C ATOM 2566 OE1 GLU B 140 7.011 4.107 60.281 1.00 70.64 O ANISOU 2566 OE1 GLU B 140 7513 13183 6144 -2252 1590 -1714 O ATOM 2567 OE2 GLU B 140 6.677 4.640 62.357 1.00 76.14 O ANISOU 2567 OE2 GLU B 140 8345 14407 6180 -2483 1747 -1997 O ATOM 2568 N PHE B 141 11.850 6.371 58.334 1.00 55.57 N ANISOU 2568 N PHE B 141 6263 9208 5645 -1386 679 -1353 N ATOM 2569 CA PHE B 141 12.768 6.401 57.211 1.00 52.45 C ANISOU 2569 CA PHE B 141 5865 8417 5647 -1274 552 -1191 C ATOM 2570 C PHE B 141 14.168 6.760 57.684 1.00 52.62 C ANISOU 2570 C PHE B 141 6056 8168 5769 -1352 315 -1095 C ATOM 2571 O PHE B 141 15.129 6.076 57.340 1.00 51.99 O ANISOU 2571 O PHE B 141 5958 7896 5900 -1440 175 -856 O ATOM 2572 CB PHE B 141 12.305 7.384 56.132 1.00 50.94 C ANISOU 2572 CB PHE B 141 5600 8120 5635 -948 629 -1382 C ATOM 2573 CG PHE B 141 13.248 7.493 54.966 1.00 48.27 C ANISOU 2573 CG PHE B 141 5281 7406 5653 -885 528 -1226 C ATOM 2574 CD1 PHE B 141 13.656 8.742 54.502 1.00 48.58 C ANISOU 2574 CD1 PHE B 141 5457 7179 5823 -714 454 -1346 C ATOM 2575 CD2 PHE B 141 13.748 6.354 54.347 1.00 45.42 C ANISOU 2575 CD2 PHE B 141 4835 6952 5470 -1012 507 -969 C ATOM 2576 CE1 PHE B 141 14.523 8.857 53.429 1.00 46.51 C ANISOU 2576 CE1 PHE B 141 5210 6621 5840 -722 391 -1204 C ATOM 2577 CE2 PHE B 141 14.617 6.452 53.262 1.00 44.29 C ANISOU 2577 CE2 PHE B 141 4677 6525 5626 -956 453 -859 C ATOM 2578 CZ PHE B 141 15.011 7.707 52.798 1.00 44.20 C ANISOU 2578 CZ PHE B 141 4767 6305 5722 -838 409 -971 C ATOM 2579 N TYR B 142 14.279 7.815 58.484 1.00 54.40 N ANISOU 2579 N TYR B 142 6435 8401 5833 -1315 260 -1300 N ATOM 2580 CA TYR B 142 15.587 8.259 58.961 1.00 54.94 C ANISOU 2580 CA TYR B 142 6655 8244 5974 -1430 17 -1233 C ATOM 2581 C TYR B 142 16.263 7.225 59.857 1.00 56.00 C ANISOU 2581 C TYR B 142 6834 8449 5996 -1692 -157 -996 C ATOM 2582 O TYR B 142 17.466 7.022 59.749 1.00 56.13 O ANISOU 2582 O TYR B 142 6828 8282 6217 -1762 -374 -823 O ATOM 2583 CB TYR B 142 15.500 9.604 59.679 1.00 56.83 C ANISOU 2583 CB TYR B 142 7114 8456 6022 -1359 -20 -1522 C ATOM 2584 CG TYR B 142 15.322 10.819 58.788 1.00 55.57 C ANISOU 2584 CG TYR B 142 7036 8051 6027 -1102 13 -1716 C ATOM 2585 CD1 TYR B 142 15.082 12.072 59.358 1.00 57.53 C ANISOU 2585 CD1 TYR B 142 7547 8220 6090 -975 -24 -2019 C ATOM 2586 CD2 TYR B 142 15.372 10.726 57.392 1.00 51.78 C ANISOU 2586 CD2 TYR B 142 6428 7392 5853 -983 63 -1605 C ATOM 2587 CE1 TYR B 142 14.917 13.202 58.583 1.00 57.56 C ANISOU 2587 CE1 TYR B 142 7721 7931 6217 -732 -44 -2188 C ATOM 2588 CE2 TYR B 142 15.200 11.858 56.592 1.00 52.89 C ANISOU 2588 CE2 TYR B 142 6720 7273 6102 -769 58 -1760 C ATOM 2589 CZ TYR B 142 14.967 13.099 57.206 1.00 56.68 C ANISOU 2589 CZ TYR B 142 7500 7639 6399 -638 -10 -2045 C ATOM 2590 OH TYR B 142 14.797 14.255 56.468 1.00 57.53 O ANISOU 2590 OH TYR B 142 7854 7420 6585 -416 -66 -2195 O ATOM 2591 N GLU B 143 15.495 6.575 60.728 1.00 57.57 N ANISOU 2591 N GLU B 143 7091 8927 5855 -1841 -74 -989 N ATOM 2592 CA GLU B 143 16.002 5.443 61.519 1.00 59.34 C ANISOU 2592 CA GLU B 143 7426 9185 5935 -2098 -261 -723 C ATOM 2593 C GLU B 143 16.685 4.393 60.631 1.00 56.79 C ANISOU 2593 C GLU B 143 6994 8638 5946 -2063 -382 -439 C ATOM 2594 O GLU B 143 17.780 3.931 60.928 1.00 57.54 O ANISOU 2594 O GLU B 143 7138 8585 6141 -2116 -662 -250 O ATOM 2595 CB GLU B 143 14.859 4.747 62.265 1.00 61.70 C ANISOU 2595 CB GLU B 143 7802 9823 5816 -2309 -87 -728 C ATOM 2596 CG GLU B 143 14.400 5.405 63.537 1.00 66.56 C ANISOU 2596 CG GLU B 143 8579 10719 5993 -2433 -22 -952 C ATOM 2597 CD GLU B 143 13.458 4.499 64.306 1.00 72.27 C ANISOU 2597 CD GLU B 143 9383 11805 6273 -2748 132 -890 C ATOM 2598 OE1 GLU B 143 12.271 4.386 63.918 1.00 73.37 O ANISOU 2598 OE1 GLU B 143 9326 12233 6316 -2732 434 -1029 O ATOM 2599 OE2 GLU B 143 13.913 3.883 65.297 1.00 76.24 O ANISOU 2599 OE2 GLU B 143 10147 12316 6504 -3041 -64 -691 O ATOM 2600 N ALA B 144 16.016 4.022 59.545 1.00 54.28 N ANISOU 2600 N ALA B 144 6524 8310 5789 -1950 -182 -435 N ATOM 2601 CA ALA B 144 16.515 3.007 58.626 1.00 52.16 C ANISOU 2601 CA ALA B 144 6176 7834 5810 -1892 -255 -213 C ATOM 2602 C ALA B 144 17.810 3.454 57.934 1.00 50.75 C ANISOU 2602 C ALA B 144 5859 7417 6007 -1724 -402 -189 C ATOM 2603 O ALA B 144 18.705 2.642 57.686 1.00 50.68 O ANISOU 2603 O ALA B 144 5806 7257 6192 -1682 -582 -7 O ATOM 2604 CB ALA B 144 15.450 2.669 57.611 1.00 49.80 C ANISOU 2604 CB ALA B 144 5756 7600 5565 -1828 0 -256 C ATOM 2605 N LEU B 145 17.906 4.744 57.636 1.00 50.22 N ANISOU 2605 N LEU B 145 5734 7325 6023 -1634 -331 -384 N ATOM 2606 CA LEU B 145 19.129 5.311 57.059 1.00 50.28 C ANISOU 2606 CA LEU B 145 5618 7159 6328 -1575 -451 -376 C ATOM 2607 C LEU B 145 20.297 5.276 58.025 1.00 53.25 C ANISOU 2607 C LEU B 145 6016 7538 6679 -1699 -755 -290 C ATOM 2608 O LEU B 145 21.431 4.987 57.627 1.00 53.95 O ANISOU 2608 O LEU B 145 5921 7556 7023 -1663 -907 -188 O ATOM 2609 CB LEU B 145 18.900 6.754 56.598 1.00 49.41 C ANISOU 2609 CB LEU B 145 5545 6980 6251 -1512 -333 -593 C ATOM 2610 CG LEU B 145 18.201 7.007 55.266 1.00 46.59 C ANISOU 2610 CG LEU B 145 5120 6544 6037 -1344 -110 -661 C ATOM 2611 CD1 LEU B 145 18.207 8.478 54.976 1.00 45.96 C ANISOU 2611 CD1 LEU B 145 5173 6322 5966 -1298 -93 -846 C ATOM 2612 CD2 LEU B 145 18.823 6.241 54.101 1.00 43.13 C ANISOU 2612 CD2 LEU B 145 4492 6003 5891 -1296 -82 -502 C ATOM 2613 N ASP B 146 20.013 5.602 59.286 1.00 56.12 N ANISOU 2613 N ASP B 146 6584 8019 6719 -1840 -841 -356 N ATOM 2614 CA ASP B 146 21.005 5.582 60.361 1.00 59.70 C ANISOU 2614 CA ASP B 146 7106 8503 7076 -1986 -1163 -279 C ATOM 2615 C ASP B 146 21.528 4.179 60.528 1.00 60.17 C ANISOU 2615 C ASP B 146 7129 8536 7197 -1961 -1377 -20 C ATOM 2616 O ASP B 146 22.725 3.968 60.701 1.00 62.01 O ANISOU 2616 O ASP B 146 7235 8739 7588 -1943 -1666 80 O ATOM 2617 CB ASP B 146 20.389 6.054 61.679 1.00 62.58 C ANISOU 2617 CB ASP B 146 7750 9015 7010 -2149 -1177 -403 C ATOM 2618 CG ASP B 146 20.009 7.524 61.655 1.00 65.00 C ANISOU 2618 CG ASP B 146 8151 9302 7243 -2127 -1035 -695 C ATOM 2619 OD1 ASP B 146 19.199 7.934 62.524 1.00 68.80 O ANISOU 2619 OD1 ASP B 146 8844 9929 7369 -2181 -944 -868 O ATOM 2620 OD2 ASP B 146 20.519 8.266 60.772 1.00 66.19 O ANISOU 2620 OD2 ASP B 146 8193 9287 7669 -2059 -1019 -759 O ATOM 2621 N CYS B 147 20.605 3.232 60.473 1.00 59.35 N ANISOU 2621 N CYS B 147 7146 8446 6959 -1960 -1250 76 N ATOM 2622 CA CYS B 147 20.903 1.805 60.434 1.00 60.29 C ANISOU 2622 CA CYS B 147 7320 8453 7136 -1909 -1431 323 C ATOM 2623 C CYS B 147 21.929 1.424 59.369 1.00 58.85 C ANISOU 2623 C CYS B 147 6854 8117 7388 -1660 -1521 381 C ATOM 2624 O CYS B 147 22.839 0.652 59.643 1.00 60.67 O ANISOU 2624 O CYS B 147 7069 8267 7715 -1558 -1835 533 O ATOM 2625 CB CYS B 147 19.612 1.031 60.196 1.00 59.60 C ANISOU 2625 CB CYS B 147 7389 8387 6868 -1987 -1196 373 C ATOM 2626 SG CYS B 147 18.540 1.008 61.619 1.00 63.87 S ANISOU 2626 SG CYS B 147 8258 9175 6834 -2327 -1137 362 S ATOM 2627 N LEU B 148 21.780 1.961 58.159 1.00 55.92 N ANISOU 2627 N LEU B 148 6265 7721 7260 -1547 -1254 250 N ATOM 2628 CA LEU B 148 22.765 1.713 57.099 1.00 55.48 C ANISOU 2628 CA LEU B 148 5910 7583 7587 -1338 -1283 264 C ATOM 2629 C LEU B 148 23.928 2.705 57.103 1.00 56.57 C ANISOU 2629 C LEU B 148 5788 7816 7892 -1374 -1397 167 C ATOM 2630 O LEU B 148 24.743 2.724 56.176 1.00 57.23 O ANISOU 2630 O LEU B 148 5565 7910 8268 -1255 -1360 134 O ATOM 2631 CB LEU B 148 22.100 1.649 55.721 1.00 52.51 C ANISOU 2631 CB LEU B 148 5452 7134 7365 -1232 -955 198 C ATOM 2632 CG LEU B 148 21.147 0.464 55.530 1.00 51.94 C ANISOU 2632 CG LEU B 148 5588 6965 7183 -1208 -877 308 C ATOM 2633 CD1 LEU B 148 20.486 0.515 54.167 1.00 49.77 C ANISOU 2633 CD1 LEU B 148 5225 6645 7041 -1126 -572 225 C ATOM 2634 CD2 LEU B 148 21.860 -0.879 55.716 1.00 54.62 C ANISOU 2634 CD2 LEU B 148 5999 7147 7606 -1061 -1159 485 C ATOM 2635 N ARG B 149 24.015 3.513 58.160 1.00 57.73 N ANISOU 2635 N ARG B 149 6060 8052 7824 -1572 -1531 113 N ATOM 2636 CA ARG B 149 25.051 4.549 58.296 1.00 58.85 C ANISOU 2636 CA ARG B 149 6011 8285 8063 -1702 -1661 15 C ATOM 2637 C ARG B 149 25.121 5.474 57.071 1.00 56.67 C ANISOU 2637 C ARG B 149 5572 7974 7988 -1730 -1390 -121 C ATOM 2638 O ARG B 149 26.197 5.875 56.633 1.00 57.93 O ANISOU 2638 O ARG B 149 5443 8218 8350 -1798 -1452 -154 O ATOM 2639 CB ARG B 149 26.420 3.932 58.642 1.00 62.07 C ANISOU 2639 CB ARG B 149 6152 8798 8636 -1622 -2023 119 C ATOM 2640 CG ARG B 149 26.359 2.875 59.737 1.00 64.87 C ANISOU 2640 CG ARG B 149 6733 9123 8792 -1557 -2334 295 C ATOM 2641 CD ARG B 149 27.709 2.573 60.352 1.00 70.02 C ANISOU 2641 CD ARG B 149 7159 9902 9542 -1494 -2776 368 C ATOM 2642 NE ARG B 149 27.540 1.709 61.525 1.00 74.38 N ANISOU 2642 NE ARG B 149 8052 10387 9823 -1481 -3107 550 N ATOM 2643 CZ ARG B 149 28.466 1.460 62.451 1.00 78.28 C ANISOU 2643 CZ ARG B 149 8509 10973 10262 -1465 -3570 641 C ATOM 2644 NH1 ARG B 149 29.675 2.013 62.380 1.00 81.80 N ANISOU 2644 NH1 ARG B 149 8523 11635 10922 -1467 -3765 550 N ATOM 2645 NH2 ARG B 149 28.175 0.652 63.466 1.00 80.06 N ANISOU 2645 NH2 ARG B 149 9139 11091 10189 -1479 -3856 831 N ATOM 2646 N ILE B 150 23.964 5.805 56.513 1.00 53.74 N ANISOU 2646 N ILE B 150 5382 7499 7538 -1696 -1100 -198 N ATOM 2647 CA ILE B 150 23.911 6.839 55.487 1.00 52.57 C ANISOU 2647 CA ILE B 150 5203 7271 7502 -1750 -886 -320 C ATOM 2648 C ILE B 150 23.475 8.137 56.172 1.00 53.60 C ANISOU 2648 C ILE B 150 5628 7339 7397 -1913 -903 -475 C ATOM 2649 O ILE B 150 22.428 8.164 56.818 1.00 53.23 O ANISOU 2649 O ILE B 150 5822 7294 7108 -1858 -849 -539 O ATOM 2650 CB ILE B 150 22.979 6.468 54.313 1.00 49.79 C ANISOU 2650 CB ILE B 150 4868 6825 7227 -1574 -598 -320 C ATOM 2651 CG1 ILE B 150 23.445 5.157 53.651 1.00 49.33 C ANISOU 2651 CG1 ILE B 150 4568 6793 7383 -1402 -593 -194 C ATOM 2652 CG2 ILE B 150 22.935 7.599 53.287 1.00 47.97 C ANISOU 2652 CG2 ILE B 150 4676 6482 7070 -1644 -423 -427 C ATOM 2653 CD1 ILE B 150 22.391 4.479 52.791 1.00 46.59 C ANISOU 2653 CD1 ILE B 150 4300 6361 7041 -1246 -367 -172 C ATOM 2654 N PRO B 151 24.293 9.207 56.061 1.00 55.55 N ANISOU 2654 N PRO B 151 5866 7545 7696 -2129 -982 -551 N ATOM 2655 CA PRO B 151 23.913 10.459 56.732 1.00 57.14 C ANISOU 2655 CA PRO B 151 6424 7626 7662 -2270 -1032 -719 C ATOM 2656 C PRO B 151 22.647 11.018 56.109 1.00 55.12 C ANISOU 2656 C PRO B 151 6424 7193 7327 -2091 -793 -845 C ATOM 2657 O PRO B 151 22.353 10.702 54.952 1.00 53.52 O ANISOU 2657 O PRO B 151 6104 6942 7289 -1959 -606 -790 O ATOM 2658 CB PRO B 151 25.104 11.400 56.485 1.00 59.42 C ANISOU 2658 CB PRO B 151 6654 7875 8048 -2586 -1157 -748 C ATOM 2659 CG PRO B 151 26.201 10.551 55.916 1.00 60.49 C ANISOU 2659 CG PRO B 151 6310 8218 8455 -2608 -1194 -603 C ATOM 2660 CD PRO B 151 25.556 9.329 55.310 1.00 56.65 C ANISOU 2660 CD PRO B 151 5685 7757 8082 -2275 -1017 -506 C ATOM 2661 N ARG B 152 21.898 11.814 56.871 1.00 56.06 N ANISOU 2661 N ARG B 152 6879 7233 7187 -2059 -810 -1028 N ATOM 2662 CA ARG B 152 20.651 12.423 56.376 1.00 55.11 C ANISOU 2662 CA ARG B 152 6991 6970 6980 -1819 -624 -1191 C ATOM 2663 C ARG B 152 20.885 13.553 55.364 1.00 55.52 C ANISOU 2663 C ARG B 152 7243 6717 7134 -1877 -611 -1247 C ATOM 2664 O ARG B 152 19.961 13.926 54.620 1.00 54.60 O ANISOU 2664 O ARG B 152 7273 6459 7013 -1640 -479 -1332 O ATOM 2665 CB ARG B 152 19.775 12.911 57.534 1.00 57.01 C ANISOU 2665 CB ARG B 152 7506 7258 6897 -1714 -641 -1416 C ATOM 2666 CG ARG B 152 19.149 11.783 58.347 1.00 56.83 C ANISOU 2666 CG ARG B 152 7336 7548 6708 -1648 -575 -1367 C ATOM 2667 CD ARG B 152 18.598 12.316 59.647 1.00 59.62 C ANISOU 2667 CD ARG B 152 7948 8004 6702 -1642 -609 -1595 C ATOM 2668 NE ARG B 152 18.448 11.281 60.665 1.00 58.66 N ANISOU 2668 NE ARG B 152 7742 8177 6370 -1751 -628 -1495 N ATOM 2669 CZ ARG B 152 17.799 11.469 61.807 1.00 60.35 C ANISOU 2669 CZ ARG B 152 8135 8580 6214 -1762 -593 -1679 C ATOM 2670 NH1 ARG B 152 17.235 12.646 62.055 1.00 61.82 N ANISOU 2670 NH1 ARG B 152 8570 8689 6231 -1606 -535 -2002 N ATOM 2671 NH2 ARG B 152 17.706 10.482 62.690 1.00 60.67 N ANISOU 2671 NH2 ARG B 152 8141 8878 6035 -1922 -620 -1548 N ATOM 2672 N SER B 153 22.111 14.084 55.342 1.00 56.66 N ANISOU 2672 N SER B 153 7401 6776 7352 -2213 -765 -1194 N ATOM 2673 CA SER B 153 22.538 15.046 54.318 1.00 57.53 C ANISOU 2673 CA SER B 153 7700 6611 7547 -2394 -758 -1189 C ATOM 2674 C SER B 153 22.629 14.478 52.888 1.00 55.05 C ANISOU 2674 C SER B 153 7132 6330 7456 -2348 -565 -1033 C ATOM 2675 O SER B 153 22.636 15.243 51.929 1.00 55.58 O ANISOU 2675 O SER B 153 7427 6150 7539 -2438 -519 -1030 O ATOM 2676 CB SER B 153 23.869 15.709 54.714 1.00 61.11 C ANISOU 2676 CB SER B 153 8193 7035 7990 -2858 -965 -1171 C ATOM 2677 OG SER B 153 24.865 14.736 54.990 1.00 61.08 O ANISOU 2677 OG SER B 153 7697 7378 8134 -3005 -1027 -1024 O ATOM 2678 N ASP B 154 22.686 13.152 52.741 1.00 52.61 N ANISOU 2678 N ASP B 154 6407 6293 7289 -2215 -465 -906 N ATOM 2679 CA ASP B 154 22.774 12.530 51.416 1.00 50.60 C ANISOU 2679 CA ASP B 154 5919 6082 7226 -2156 -276 -784 C ATOM 2680 C ASP B 154 21.412 12.215 50.819 1.00 48.13 C ANISOU 2680 C ASP B 154 5706 5703 6880 -1812 -113 -815 C ATOM 2681 O ASP B 154 21.309 11.715 49.698 1.00 46.94 O ANISOU 2681 O ASP B 154 5421 5564 6850 -1741 42 -731 O ATOM 2682 CB ASP B 154 23.643 11.274 51.456 1.00 50.34 C ANISOU 2682 CB ASP B 154 5412 6341 7375 -2175 -277 -652 C ATOM 2683 CG ASP B 154 25.118 11.592 51.606 1.00 53.52 C ANISOU 2683 CG ASP B 154 5596 6874 7863 -2523 -406 -621 C ATOM 2684 OD1 ASP B 154 25.505 12.753 51.426 1.00 56.99 O ANISOU 2684 OD1 ASP B 154 6254 7166 8232 -2825 -449 -671 O ATOM 2685 OD2 ASP B 154 25.902 10.681 51.919 1.00 56.08 O ANISOU 2685 OD2 ASP B 154 5534 7455 8318 -2503 -486 -551 O ATOM 2686 N VAL B 155 20.356 12.511 51.556 1.00 47.85 N ANISOU 2686 N VAL B 155 5888 5630 6664 -1601 -145 -955 N ATOM 2687 CA VAL B 155 19.021 12.217 51.064 1.00 46.17 C ANISOU 2687 CA VAL B 155 5704 5433 6408 -1280 -5 -1009 C ATOM 2688 C VAL B 155 18.626 13.159 49.915 1.00 46.84 C ANISOU 2688 C VAL B 155 6067 5235 6497 -1199 24 -1052 C ATOM 2689 O VAL B 155 18.878 14.380 49.992 1.00 47.81 O ANISOU 2689 O VAL B 155 6548 5084 6536 -1299 -103 -1136 O ATOM 2690 CB VAL B 155 17.970 12.262 52.194 1.00 46.64 C ANISOU 2690 CB VAL B 155 5852 5621 6250 -1074 -23 -1182 C ATOM 2691 CG1 VAL B 155 16.633 11.777 51.687 1.00 44.34 C ANISOU 2691 CG1 VAL B 155 5466 5459 5923 -782 131 -1233 C ATOM 2692 CG2 VAL B 155 18.416 11.387 53.342 1.00 47.18 C ANISOU 2692 CG2 VAL B 155 5730 5931 6264 -1211 -84 -1110 C ATOM 2693 N MET B 156 18.036 12.572 48.857 1.00 44.63 N ANISOU 2693 N MET B 156 5665 4997 6294 -1040 165 -984 N ATOM 2694 CA MET B 156 17.397 13.346 47.774 1.00 45.98 C ANISOU 2694 CA MET B 156 6116 4922 6432 -890 168 -1022 C ATOM 2695 C MET B 156 15.861 13.328 47.945 1.00 45.90 C ANISOU 2695 C MET B 156 6124 5009 6306 -483 181 -1186 C ATOM 2696 O MET B 156 15.268 12.271 48.172 1.00 43.64 O ANISOU 2696 O MET B 156 5529 5026 6026 -381 292 -1176 O ATOM 2697 CB MET B 156 17.786 12.816 46.393 1.00 44.93 C ANISOU 2697 CB MET B 156 5860 4783 6430 -1005 299 -852 C ATOM 2698 CG MET B 156 19.291 12.899 46.076 1.00 46.87 C ANISOU 2698 CG MET B 156 6032 5003 6775 -1407 321 -724 C ATOM 2699 SD MET B 156 19.843 11.619 44.907 1.00 48.85 S ANISOU 2699 SD MET B 156 5904 5464 7195 -1487 542 -571 S ATOM 2700 CE MET B 156 19.409 10.087 45.756 1.00 43.60 C ANISOU 2700 CE MET B 156 4869 5094 6604 -1258 575 -571 C ATOM 2701 N TYR B 157 15.225 14.500 47.848 1.00 47.97 N ANISOU 2701 N TYR B 157 6752 5022 6453 -254 55 -1347 N ATOM 2702 CA TYR B 157 13.785 14.601 48.101 1.00 48.84 C ANISOU 2702 CA TYR B 157 6827 5282 6447 179 51 -1560 C ATOM 2703 C TYR B 157 12.998 14.950 46.843 1.00 49.41 C ANISOU 2703 C TYR B 157 7040 5204 6528 446 3 -1564 C ATOM 2704 O TYR B 157 13.478 15.707 45.998 1.00 51.52 O ANISOU 2704 O TYR B 157 7671 5093 6811 350 -107 -1471 O ATOM 2705 CB TYR B 157 13.534 15.641 49.175 1.00 52.27 C ANISOU 2705 CB TYR B 157 7546 5597 6719 353 -86 -1814 C ATOM 2706 CG TYR B 157 14.164 15.309 50.505 1.00 52.75 C ANISOU 2706 CG TYR B 157 7484 5839 6719 111 -61 -1833 C ATOM 2707 CD1 TYR B 157 15.465 15.725 50.812 1.00 54.02 C ANISOU 2707 CD1 TYR B 157 7836 5778 6913 -262 -166 -1733 C ATOM 2708 CD2 TYR B 157 13.460 14.582 51.461 1.00 52.08 C ANISOU 2708 CD2 TYR B 157 7097 6173 6518 220 56 -1948 C ATOM 2709 CE1 TYR B 157 16.039 15.419 52.042 1.00 55.08 C ANISOU 2709 CE1 TYR B 157 7861 6089 6976 -474 -186 -1747 C ATOM 2710 CE2 TYR B 157 14.022 14.275 52.689 1.00 52.65 C ANISOU 2710 CE2 TYR B 157 7109 6401 6496 -12 52 -1949 C ATOM 2711 CZ TYR B 157 15.305 14.692 52.974 1.00 54.26 C ANISOU 2711 CZ TYR B 157 7505 6365 6746 -334 -84 -1849 C ATOM 2712 OH TYR B 157 15.846 14.385 54.198 1.00 56.85 O ANISOU 2712 OH TYR B 157 7776 6858 6966 -551 -127 -1849 O ATOM 2713 N THR B 158 11.804 14.394 46.689 1.00 48.28 N ANISOU 2713 N THR B 158 6619 5371 6353 743 72 -1660 N ATOM 2714 CA THR B 158 10.941 14.840 45.600 1.00 49.34 C ANISOU 2714 CA THR B 158 6894 5382 6469 1062 -34 -1703 C ATOM 2715 C THR B 158 10.243 16.098 46.048 1.00 53.54 C ANISOU 2715 C THR B 158 7741 5729 6873 1494 -236 -1984 C ATOM 2716 O THR B 158 10.102 16.336 47.250 1.00 55.03 O ANISOU 2716 O THR B 158 7890 6048 6969 1590 -223 -2189 O ATOM 2717 CB THR B 158 9.845 13.824 45.207 1.00 48.13 C ANISOU 2717 CB THR B 158 6303 5664 6320 1226 83 -1725 C ATOM 2718 OG1 THR B 158 9.097 13.446 46.369 1.00 47.78 O ANISOU 2718 OG1 THR B 158 5929 6049 6175 1360 179 -1930 O ATOM 2719 CG2 THR B 158 10.446 12.614 44.536 1.00 42.96 C ANISOU 2719 CG2 THR B 158 5431 5108 5785 861 246 -1463 C ATOM 2720 N ASP B 159 9.812 16.900 45.082 1.00 55.91 N ANISOU 2720 N ASP B 159 8385 5709 7148 1770 -439 -2001 N ATOM 2721 CA ASP B 159 9.023 18.075 45.382 1.00 60.99 C ANISOU 2721 CA ASP B 159 9349 6148 7674 2294 -677 -2294 C ATOM 2722 C ASP B 159 7.726 18.051 44.598 1.00 62.76 C ANISOU 2722 C ASP B 159 9413 6552 7880 2787 -787 -2408 C ATOM 2723 O ASP B 159 7.722 18.232 43.383 1.00 62.89 O ANISOU 2723 O ASP B 159 9674 6303 7919 2795 -928 -2235 O ATOM 2724 CB ASP B 159 9.811 19.353 45.079 1.00 63.71 C ANISOU 2724 CB ASP B 159 10435 5803 7970 2196 -928 -2229 C ATOM 2725 CG ASP B 159 9.041 20.607 45.430 1.00 69.57 C ANISOU 2725 CG ASP B 159 11607 6243 8585 2782 -1216 -2551 C ATOM 2726 OD1 ASP B 159 9.478 21.700 45.011 1.00 74.87 O ANISOU 2726 OD1 ASP B 159 12977 6283 9189 2763 -1483 -2498 O ATOM 2727 OD2 ASP B 159 8.000 20.506 46.120 1.00 70.79 O ANISOU 2727 OD2 ASP B 159 11418 6791 8688 3259 -1180 -2868 O ATOM 2728 N TRP B 160 6.623 17.873 45.316 1.00 65.02 N ANISOU 2728 N TRP B 160 9290 7314 8102 3192 -731 -2714 N ATOM 2729 CA TRP B 160 5.305 17.747 44.693 1.00 67.51 C ANISOU 2729 CA TRP B 160 9304 7948 8398 3667 -824 -2865 C ATOM 2730 C TRP B 160 4.888 18.960 43.848 1.00 71.69 C ANISOU 2730 C TRP B 160 10366 7983 8891 4175 -1217 -2945 C ATOM 2731 O TRP B 160 4.059 18.844 42.944 1.00 73.31 O ANISOU 2731 O TRP B 160 10427 8326 9102 4471 -1359 -2949 O ATOM 2732 CB TRP B 160 4.234 17.406 45.742 1.00 69.24 C ANISOU 2732 CB TRP B 160 8947 8838 8522 3977 -668 -3221 C ATOM 2733 CG TRP B 160 2.910 16.984 45.123 1.00 72.75 C ANISOU 2733 CG TRP B 160 8898 9788 8955 4335 -703 -3354 C ATOM 2734 CD1 TRP B 160 1.675 17.567 45.323 1.00 77.95 C ANISOU 2734 CD1 TRP B 160 9333 10758 9529 5011 -847 -3752 C ATOM 2735 CD2 TRP B 160 2.698 15.915 44.184 1.00 71.10 C ANISOU 2735 CD2 TRP B 160 8358 9844 8814 4043 -615 -3110 C ATOM 2736 NE1 TRP B 160 0.718 16.914 44.580 1.00 78.64 N ANISOU 2736 NE1 TRP B 160 8923 11325 9630 5124 -857 -3757 N ATOM 2737 CE2 TRP B 160 1.313 15.899 43.873 1.00 75.37 C ANISOU 2737 CE2 TRP B 160 8465 10871 9301 4520 -720 -3362 C ATOM 2738 CE3 TRP B 160 3.540 14.966 43.582 1.00 66.65 C ANISOU 2738 CE3 TRP B 160 7812 9167 8343 3444 -464 -2729 C ATOM 2739 CZ2 TRP B 160 0.753 14.966 42.979 1.00 74.49 C ANISOU 2739 CZ2 TRP B 160 7968 11118 9215 4356 -689 -3223 C ATOM 2740 CZ3 TRP B 160 2.981 14.044 42.688 1.00 66.67 C ANISOU 2740 CZ3 TRP B 160 7476 9486 8368 3320 -425 -2606 C ATOM 2741 CH2 TRP B 160 1.602 14.056 42.395 1.00 69.94 C ANISOU 2741 CH2 TRP B 160 7492 10364 8717 3747 -543 -2842 C ATOM 2742 N LYS B 161 5.471 20.117 44.136 1.00 74.17 N ANISOU 2742 N LYS B 161 11332 7698 9150 4256 -1424 -2999 N ATOM 2743 CA LYS B 161 5.131 21.350 43.427 1.00 78.71 C ANISOU 2743 CA LYS B 161 12549 7696 9660 4739 -1847 -3071 C ATOM 2744 C LYS B 161 5.675 21.337 41.998 1.00 77.30 C ANISOU 2744 C LYS B 161 12761 7106 9503 4402 -1977 -2675 C ATOM 2745 O LYS B 161 5.196 22.059 41.124 1.00 80.23 O ANISOU 2745 O LYS B 161 13565 7109 9810 4784 -2333 -2668 O ATOM 2746 CB LYS B 161 5.639 22.565 44.209 1.00 82.05 C ANISOU 2746 CB LYS B 161 13630 7556 9990 4856 -2033 -3243 C ATOM 2747 CG LYS B 161 4.713 22.993 45.342 1.00 86.46 C ANISOU 2747 CG LYS B 161 13977 8407 10466 5503 -2057 -3745 C ATOM 2748 CD LYS B 161 4.618 21.956 46.477 1.00 83.87 C ANISOU 2748 CD LYS B 161 12892 8836 10141 5257 -1627 -3869 C ATOM 2749 CE LYS B 161 5.630 22.222 47.589 1.00 82.91 C ANISOU 2749 CE LYS B 161 13052 8497 9955 4856 -1513 -3886 C ATOM 2750 NZ LYS B 161 5.630 23.645 48.004 1.00 87.99 N ANISOU 2750 NZ LYS B 161 14412 8544 10475 5284 -1829 -4170 N ATOM 2751 N LYS B 162 6.671 20.484 41.774 1.00 72.41 N ANISOU 2751 N LYS B 162 11981 6575 8958 3697 -1690 -2355 N ATOM 2752 CA LYS B 162 7.323 20.383 40.481 1.00 71.44 C ANISOU 2752 CA LYS B 162 12183 6131 8829 3286 -1733 -1990 C ATOM 2753 C LYS B 162 6.634 19.345 39.579 1.00 69.63 C ANISOU 2753 C LYS B 162 11459 6353 8644 3320 -1639 -1892 C ATOM 2754 O LYS B 162 6.967 19.224 38.393 1.00 69.11 O ANISOU 2754 O LYS B 162 11641 6077 8541 3058 -1687 -1623 O ATOM 2755 CB LYS B 162 8.804 20.041 40.675 1.00 68.22 C ANISOU 2755 CB LYS B 162 11843 5608 8470 2536 -1475 -1736 C ATOM 2756 CG LYS B 162 9.561 21.000 41.611 1.00 70.11 C ANISOU 2756 CG LYS B 162 12540 5443 8655 2402 -1563 -1825 C ATOM 2757 CD LYS B 162 10.266 22.109 40.850 1.00 73.54 C ANISOU 2757 CD LYS B 162 13825 5156 8961 2154 -1826 -1632 C ATOM 2758 CE LYS B 162 10.973 23.068 41.810 1.00 76.80 C ANISOU 2758 CE LYS B 162 14718 5161 9301 1990 -1937 -1738 C ATOM 2759 NZ LYS B 162 12.012 23.859 41.107 1.00 78.65 N ANISOU 2759 NZ LYS B 162 15677 4795 9409 1439 -2079 -1468 N ATOM 2760 N ASP B 163 5.673 18.612 40.146 1.00 68.87 N ANISOU 2760 N ASP B 163 10685 6885 8597 3605 -1503 -2116 N ATOM 2761 CA ASP B 163 4.973 17.543 39.439 1.00 67.11 C ANISOU 2761 CA ASP B 163 9944 7149 8406 3586 -1402 -2052 C ATOM 2762 C ASP B 163 4.310 18.018 38.150 1.00 70.14 C ANISOU 2762 C ASP B 163 10625 7316 8709 3918 -1750 -1993 C ATOM 2763 O ASP B 163 3.755 19.121 38.091 1.00 75.09 O ANISOU 2763 O ASP B 163 11628 7640 9262 4469 -2112 -2163 O ATOM 2764 CB ASP B 163 3.916 16.896 40.338 1.00 67.46 C ANISOU 2764 CB ASP B 163 9263 7901 8466 3862 -1250 -2348 C ATOM 2765 CG ASP B 163 3.027 15.922 39.578 1.00 67.12 C ANISOU 2765 CG ASP B 163 8720 8358 8426 3872 -1213 -2316 C ATOM 2766 OD1 ASP B 163 3.495 14.816 39.263 1.00 61.30 O ANISOU 2766 OD1 ASP B 163 7769 7784 7737 3357 -966 -2090 O ATOM 2767 OD2 ASP B 163 1.865 16.283 39.276 1.00 72.12 O ANISOU 2767 OD2 ASP B 163 9186 9209 9006 4413 -1457 -2529 O ATOM 2768 N LYS B 164 4.360 17.177 37.119 1.00 67.61 N ANISOU 2768 N LYS B 164 10165 7136 8388 3605 -1663 -1762 N ATOM 2769 CA LYS B 164 3.693 17.496 35.857 1.00 70.39 C ANISOU 2769 CA LYS B 164 10765 7343 8637 3881 -1998 -1690 C ATOM 2770 C LYS B 164 2.764 16.391 35.364 1.00 68.80 C ANISOU 2770 C LYS B 164 9939 7755 8446 3907 -1927 -1722 C ATOM 2771 O LYS B 164 2.118 16.546 34.337 1.00 72.06 O ANISOU 2771 O LYS B 164 10477 8137 8767 4138 -2215 -1678 O ATOM 2772 CB LYS B 164 4.728 17.841 34.775 1.00 70.19 C ANISOU 2772 CB LYS B 164 11423 6733 8512 3440 -2058 -1341 C ATOM 2773 CG LYS B 164 5.411 19.194 34.966 1.00 74.16 C ANISOU 2773 CG LYS B 164 12701 6542 8934 3470 -2279 -1300 C ATOM 2774 CD LYS B 164 4.441 20.365 34.794 1.00 81.00 C ANISOU 2774 CD LYS B 164 13986 7091 9698 4203 -2796 -1482 C ATOM 2775 CE LYS B 164 4.981 21.640 35.438 1.00 85.36 C ANISOU 2775 CE LYS B 164 15218 7019 10197 4308 -2990 -1551 C ATOM 2776 NZ LYS B 164 6.298 22.065 34.874 1.00 85.38 N ANISOU 2776 NZ LYS B 164 15920 6439 10082 3635 -2953 -1207 N ATOM 2777 N CYS B 165 2.677 15.293 36.103 1.00 64.63 N ANISOU 2777 N CYS B 165 8776 7772 8009 3654 -1575 -1796 N ATOM 2778 CA CYS B 165 2.098 14.066 35.566 1.00 62.28 C ANISOU 2778 CA CYS B 165 7977 7979 7707 3447 -1448 -1750 C ATOM 2779 C CYS B 165 0.603 13.904 35.762 1.00 65.10 C ANISOU 2779 C CYS B 165 7754 8947 8032 3898 -1591 -2038 C ATOM 2780 O CYS B 165 -0.028 13.102 35.071 1.00 64.82 O ANISOU 2780 O CYS B 165 7396 9278 7955 3782 -1607 -2001 O ATOM 2781 CB CYS B 165 2.841 12.847 36.110 1.00 57.29 C ANISOU 2781 CB CYS B 165 7040 7565 7162 2859 -1016 -1633 C ATOM 2782 SG CYS B 165 4.378 12.533 35.245 1.00 55.32 S ANISOU 2782 SG CYS B 165 7275 6818 6928 2271 -844 -1271 S ATOM 2783 N GLU B 166 0.039 14.673 36.688 1.00 67.81 N ANISOU 2783 N GLU B 166 7959 9424 8382 4405 -1697 -2344 N ATOM 2784 CA GLU B 166 -1.368 14.549 37.047 1.00 70.98 C ANISOU 2784 CA GLU B 166 7705 10515 8750 4850 -1785 -2681 C ATOM 2785 C GLU B 166 -2.356 14.665 35.882 1.00 74.47 C ANISOU 2785 C GLU B 166 8057 11116 9122 5206 -2162 -2708 C ATOM 2786 O GLU B 166 -3.324 13.910 35.849 1.00 75.15 O ANISOU 2786 O GLU B 166 7480 11896 9177 5198 -2116 -2848 O ATOM 2787 CB GLU B 166 -1.729 15.546 38.147 1.00 74.92 C ANISOU 2787 CB GLU B 166 8169 11052 9247 5423 -1866 -3038 C ATOM 2788 CG GLU B 166 -1.141 15.221 39.498 1.00 71.98 C ANISOU 2788 CG GLU B 166 7634 10814 8902 5099 -1476 -3104 C ATOM 2789 CD GLU B 166 -1.237 16.397 40.445 1.00 76.68 C ANISOU 2789 CD GLU B 166 8430 11233 9472 5643 -1593 -3421 C ATOM 2790 OE1 GLU B 166 -0.169 16.876 40.895 1.00 75.54 O ANISOU 2790 OE1 GLU B 166 8808 10541 9352 5443 -1533 -3308 O ATOM 2791 OE2 GLU B 166 -2.376 16.852 40.725 1.00 80.29 O ANISOU 2791 OE2 GLU B 166 8520 12108 9877 6280 -1754 -3802 O ATOM 2792 N PRO B 167 -2.128 15.608 34.936 1.00 76.85 N ANISOU 2792 N PRO B 167 9036 10790 9375 5488 -2552 -2570 N ATOM 2793 CA PRO B 167 -3.004 15.679 33.761 1.00 80.88 C ANISOU 2793 CA PRO B 167 9517 11419 9796 5793 -2948 -2556 C ATOM 2794 C PRO B 167 -2.996 14.429 32.863 1.00 77.94 C ANISOU 2794 C PRO B 167 8923 11315 9375 5200 -2796 -2316 C ATOM 2795 O PRO B 167 -4.067 13.964 32.467 1.00 80.53 O ANISOU 2795 O PRO B 167 8732 12211 9653 5348 -2946 -2445 O ATOM 2796 CB PRO B 167 -2.483 16.914 33.007 1.00 83.54 C ANISOU 2796 CB PRO B 167 10791 10895 10055 6067 -3354 -2382 C ATOM 2797 CG PRO B 167 -1.901 17.765 34.071 1.00 83.49 C ANISOU 2797 CG PRO B 167 11102 10511 10111 6243 -3279 -2510 C ATOM 2798 CD PRO B 167 -1.230 16.778 34.989 1.00 77.51 C ANISOU 2798 CD PRO B 167 9937 10063 9452 5618 -2712 -2470 C ATOM 2799 N LEU B 168 -1.812 13.898 32.549 1.00 73.39 N ANISOU 2799 N LEU B 168 8722 10356 8806 4549 -2512 -1998 N ATOM 2800 CA LEU B 168 -1.686 12.640 31.794 1.00 70.48 C ANISOU 2800 CA LEU B 168 8185 10203 8391 3966 -2317 -1798 C ATOM 2801 C LEU B 168 -2.440 11.507 32.493 1.00 70.28 C ANISOU 2801 C LEU B 168 7340 10955 8407 3769 -2060 -1981 C ATOM 2802 O LEU B 168 -3.197 10.772 31.856 1.00 71.38 O ANISOU 2802 O LEU B 168 7142 11514 8467 3640 -2141 -1992 O ATOM 2803 CB LEU B 168 -0.208 12.258 31.576 1.00 65.30 C ANISOU 2803 CB LEU B 168 7997 9055 7758 3354 -1996 -1494 C ATOM 2804 CG LEU B 168 0.136 11.144 30.574 1.00 61.65 C ANISOU 2804 CG LEU B 168 7581 8624 7219 2803 -1835 -1273 C ATOM 2805 CD1 LEU B 168 -0.432 11.402 29.186 1.00 64.49 C ANISOU 2805 CD1 LEU B 168 8215 8893 7394 2955 -2217 -1184 C ATOM 2806 CD2 LEU B 168 1.633 10.965 30.479 1.00 57.63 C ANISOU 2806 CD2 LEU B 168 7502 7651 6743 2322 -1525 -1039 C ATOM 2807 N GLU B 169 -2.236 11.391 33.804 1.00 69.57 N ANISOU 2807 N GLU B 169 6969 11053 8412 3712 -1766 -2121 N ATOM 2808 CA GLU B 169 -2.934 10.414 34.644 1.00 70.56 C ANISOU 2808 CA GLU B 169 6362 11911 8538 3494 -1506 -2300 C ATOM 2809 C GLU B 169 -4.459 10.571 34.558 1.00 76.55 C ANISOU 2809 C GLU B 169 6515 13349 9220 3943 -1766 -2603 C ATOM 2810 O GLU B 169 -5.189 9.575 34.517 1.00 77.41 O ANISOU 2810 O GLU B 169 6076 14075 9263 3630 -1664 -2661 O ATOM 2811 CB GLU B 169 -2.454 10.555 36.094 1.00 69.17 C ANISOU 2811 CB GLU B 169 6090 11756 8434 3456 -1212 -2414 C ATOM 2812 CG GLU B 169 -3.193 9.699 37.124 1.00 71.57 C ANISOU 2812 CG GLU B 169 5681 12822 8689 3241 -942 -2616 C ATOM 2813 CD GLU B 169 -3.237 10.346 38.509 1.00 74.79 C ANISOU 2813 CD GLU B 169 5930 13382 9106 3533 -814 -2876 C ATOM 2814 OE1 GLU B 169 -3.380 11.592 38.591 1.00 79.95 O ANISOU 2814 OE1 GLU B 169 6791 13805 9781 4154 -1059 -3057 O ATOM 2815 OE2 GLU B 169 -3.142 9.610 39.520 1.00 72.80 O ANISOU 2815 OE2 GLU B 169 5385 13462 8815 3142 -483 -2906 O ATOM 2816 N LYS B 170 -4.922 11.822 34.519 1.00 81.42 N ANISOU 2816 N LYS B 170 7248 13848 9841 4671 -2120 -2800 N ATOM 2817 CA LYS B 170 -6.342 12.138 34.384 1.00 88.18 C ANISOU 2817 CA LYS B 170 7534 15331 10638 5235 -2432 -3122 C ATOM 2818 C LYS B 170 -6.855 11.738 32.993 1.00 89.93 C ANISOU 2818 C LYS B 170 7755 15647 10768 5148 -2739 -2977 C ATOM 2819 O LYS B 170 -7.937 11.156 32.858 1.00 93.10 O ANISOU 2819 O LYS B 170 7473 16799 11102 5131 -2805 -3150 O ATOM 2820 CB LYS B 170 -6.579 13.635 34.632 1.00 93.16 C ANISOU 2820 CB LYS B 170 8426 15669 11300 6105 -2784 -3361 C ATOM 2821 CG LYS B 170 -7.878 13.966 35.364 1.00 99.84 C ANISOU 2821 CG LYS B 170 8492 17315 12130 6727 -2879 -3850 C ATOM 2822 CD LYS B 170 -7.666 14.062 36.882 1.00100.14 C ANISOU 2822 CD LYS B 170 8289 17564 12196 6718 -2486 -4087 C ATOM 2823 CE LYS B 170 -7.604 15.512 37.364 1.00103.98 C ANISOU 2823 CE LYS B 170 9175 17613 12720 7529 -2740 -4342 C ATOM 2824 NZ LYS B 170 -6.806 15.598 38.621 1.00100.34 N ANISOU 2824 NZ LYS B 170 8877 16965 12280 7288 -2348 -4385 N ATOM 2825 N GLN B 171 -6.066 12.057 31.967 1.00 88.20 N ANISOU 2825 N GLN B 171 8304 14687 10521 5054 -2922 -2662 N ATOM 2826 CA GLN B 171 -6.320 11.622 30.596 1.00 89.11 C ANISOU 2826 CA GLN B 171 8567 14778 10513 4858 -3173 -2467 C ATOM 2827 C GLN B 171 -6.422 10.093 30.507 1.00 85.88 C ANISOU 2827 C GLN B 171 7732 14839 10061 4112 -2841 -2383 C ATOM 2828 O GLN B 171 -7.284 9.565 29.806 1.00 88.35 O ANISOU 2828 O GLN B 171 7698 15607 10265 4031 -3040 -2423 O ATOM 2829 CB GLN B 171 -5.235 12.185 29.662 1.00 87.44 C ANISOU 2829 CB GLN B 171 9316 13662 10246 4758 -3310 -2127 C ATOM 2830 CG GLN B 171 -4.894 11.335 28.428 1.00 86.39 C ANISOU 2830 CG GLN B 171 9461 13387 9976 4187 -3287 -1836 C ATOM 2831 CD GLN B 171 -4.559 12.171 27.195 1.00 89.76 C ANISOU 2831 CD GLN B 171 10686 13174 10244 4368 -3686 -1607 C ATOM 2832 OE1 GLN B 171 -5.098 11.934 26.114 1.00 92.85 O ANISOU 2832 OE1 GLN B 171 11127 13683 10471 4346 -3983 -1533 O ATOM 2833 NE2 GLN B 171 -3.676 13.157 27.355 1.00 90.14 N ANISOU 2833 NE2 GLN B 171 11390 12545 10314 4509 -3708 -1489 N ATOM 2834 N HIS B 172 -5.556 9.398 31.245 1.00 80.80 N ANISOU 2834 N HIS B 172 7132 14074 9493 3578 -2366 -2274 N ATOM 2835 CA HIS B 172 -5.560 7.932 31.292 1.00 78.03 C ANISOU 2835 CA HIS B 172 6475 14072 9101 2865 -2046 -2190 C ATOM 2836 C HIS B 172 -6.848 7.326 31.846 1.00 81.56 C ANISOU 2836 C HIS B 172 6060 15443 9487 2806 -2016 -2463 C ATOM 2837 O HIS B 172 -7.407 6.421 31.230 1.00 82.66 O ANISOU 2837 O HIS B 172 5952 15944 9512 2418 -2062 -2430 O ATOM 2838 CB HIS B 172 -4.351 7.396 32.057 1.00 72.28 C ANISOU 2838 CB HIS B 172 6000 12993 8472 2396 -1595 -2030 C ATOM 2839 CG HIS B 172 -3.081 7.409 31.262 1.00 68.69 C ANISOU 2839 CG HIS B 172 6274 11795 8031 2156 -1536 -1728 C ATOM 2840 ND1 HIS B 172 -3.004 6.927 29.973 1.00 68.10 N ANISOU 2840 ND1 HIS B 172 6482 11558 7837 1902 -1653 -1557 N ATOM 2841 CD2 HIS B 172 -1.838 7.842 31.576 1.00 64.46 C ANISOU 2841 CD2 HIS B 172 6213 10686 7593 2109 -1360 -1585 C ATOM 2842 CE1 HIS B 172 -1.769 7.063 29.528 1.00 64.93 C ANISOU 2842 CE1 HIS B 172 6681 10536 7453 1718 -1525 -1334 C ATOM 2843 NE2 HIS B 172 -1.043 7.620 30.479 1.00 62.99 N ANISOU 2843 NE2 HIS B 172 6543 10043 7345 1832 -1352 -1343 N ATOM 2844 N GLU B 173 -7.308 7.825 32.996 1.00 83.88 N ANISOU 2844 N GLU B 173 5906 16132 9832 3156 -1931 -2741 N ATOM 2845 CA GLU B 173 -8.560 7.363 33.619 1.00 88.17 C ANISOU 2845 CA GLU B 173 5561 17647 10291 3116 -1871 -3045 C ATOM 2846 C GLU B 173 -9.720 7.474 32.642 1.00 94.04 C ANISOU 2846 C GLU B 173 5925 18869 10938 3398 -2300 -3179 C ATOM 2847 O GLU B 173 -10.536 6.559 32.527 1.00 96.62 O ANISOU 2847 O GLU B 173 5687 19878 11144 2977 -2261 -3255 O ATOM 2848 CB GLU B 173 -8.859 8.143 34.907 1.00 90.45 C ANISOU 2848 CB GLU B 173 5487 18250 10629 3600 -1755 -3368 C ATOM 2849 CG GLU B 173 -7.829 7.921 36.035 1.00 85.02 C ANISOU 2849 CG GLU B 173 5069 17233 10003 3254 -1321 -3264 C ATOM 2850 CD GLU B 173 -8.014 8.853 37.235 1.00 87.59 C ANISOU 2850 CD GLU B 173 5175 17748 10356 3788 -1241 -3584 C ATOM 2851 OE1 GLU B 173 -9.162 8.981 37.735 1.00 96.20 O ANISOU 2851 OE1 GLU B 173 5531 19661 11361 4069 -1254 -3951 O ATOM 2852 OE2 GLU B 173 -7.019 9.462 37.683 1.00 83.23 O ANISOU 2852 OE2 GLU B 173 5168 16556 9901 3921 -1162 -3492 O ATOM 2853 N LYS B 174 -9.768 8.584 31.913 1.00 96.85 N ANISOU 2853 N LYS B 174 6633 18838 11327 4079 -2736 -3191 N ATOM 2854 CA LYS B 174 -10.844 8.840 30.963 1.00103.05 C ANISOU 2854 CA LYS B 174 7109 20023 12021 4464 -3230 -3318 C ATOM 2855 C LYS B 174 -10.762 7.919 29.738 1.00101.76 C ANISOU 2855 C LYS B 174 7190 19745 11729 3871 -3331 -3040 C ATOM 2856 O LYS B 174 -11.783 7.585 29.136 1.00106.63 O ANISOU 2856 O LYS B 174 7324 20961 12228 3861 -3611 -3155 O ATOM 2857 CB LYS B 174 -10.851 10.319 30.564 1.00106.38 C ANISOU 2857 CB LYS B 174 7962 19961 12496 5379 -3706 -3386 C ATOM 2858 CG LYS B 174 -12.179 10.825 29.997 1.00114.43 C ANISOU 2858 CG LYS B 174 8466 21563 13451 6045 -4256 -3659 C ATOM 2859 CD LYS B 174 -12.433 12.309 30.324 1.00119.74 C ANISOU 2859 CD LYS B 174 9270 22016 14209 7096 -4619 -3919 C ATOM 2860 CE LYS B 174 -11.201 13.205 30.104 1.00116.13 C ANISOU 2860 CE LYS B 174 9931 20389 13803 7266 -4697 -3635 C ATOM 2861 NZ LYS B 174 -10.564 13.026 28.756 1.00113.58 N ANISOU 2861 NZ LYS B 174 10384 19405 13366 6887 -4902 -3205 N ATOM 2862 N GLU B 175 -9.551 7.506 29.381 1.00 96.21 N ANISOU 2862 N GLU B 175 7215 18304 11036 3382 -3102 -2698 N ATOM 2863 CA GLU B 175 -9.351 6.525 28.310 1.00 94.68 C ANISOU 2863 CA GLU B 175 7300 17969 10706 2765 -3114 -2454 C ATOM 2864 C GLU B 175 -9.750 5.127 28.792 1.00 93.97 C ANISOU 2864 C GLU B 175 6676 18477 10550 2029 -2783 -2506 C ATOM 2865 O GLU B 175 -10.471 4.396 28.116 1.00 96.46 O ANISOU 2865 O GLU B 175 6722 19215 10714 1688 -2941 -2521 O ATOM 2866 CB GLU B 175 -7.890 6.522 27.837 1.00 89.18 C ANISOU 2866 CB GLU B 175 7509 16340 10035 2498 -2932 -2118 C ATOM 2867 CG GLU B 175 -7.469 7.740 27.009 1.00 90.67 C ANISOU 2867 CG GLU B 175 8373 15881 10197 3020 -3298 -1987 C ATOM 2868 CD GLU B 175 -5.953 7.900 26.911 1.00 86.45 C ANISOU 2868 CD GLU B 175 8619 14517 9712 2775 -3022 -1712 C ATOM 2869 OE1 GLU B 175 -5.209 7.027 27.411 1.00 82.27 O ANISOU 2869 OE1 GLU B 175 8104 13904 9251 2244 -2572 -1625 O ATOM 2870 OE2 GLU B 175 -5.497 8.905 26.329 1.00 87.93 O ANISOU 2870 OE2 GLU B 175 9414 14141 9855 3105 -3271 -1582 O TER 2871 GLU B 175 HETATM 2872 N1 TP0 A 190 16.345 0.880 18.393 1.00 35.33 N HETATM 2873 C3 TP0 A 190 12.801 2.422 17.647 1.00 39.08 C HETATM 2874 C4 TP0 A 190 13.079 3.652 19.751 1.00 39.75 C HETATM 2875 C5 TP0 A 190 10.932 1.416 19.068 1.00 36.84 C HETATM 2876 C6 TP0 A 190 13.012 3.714 18.372 1.00 38.84 C HETATM 2877 C7 TP0 A 190 11.454 1.762 17.812 1.00 37.83 C HETATM 2878 C8 TP0 A 190 13.749 1.810 16.894 1.00 38.51 C HETATM 2879 C10 TP0 A 190 13.262 4.827 20.494 1.00 39.86 C HETATM 2880 C11 TP0 A 190 9.688 0.793 19.134 1.00 36.36 C HETATM 2881 C12 TP0 A 190 13.075 4.932 17.692 1.00 38.74 C HETATM 2882 C13 TP0 A 190 10.743 1.458 16.661 1.00 35.79 C HETATM 2883 C14 TP0 A 190 16.238 1.304 16.967 1.00 36.21 C HETATM 2884 C15 TP0 A 190 13.340 6.045 19.809 1.00 39.46 C HETATM 2885 C16 TP0 A 190 8.989 0.501 17.992 1.00 33.74 C HETATM 2886 C17 TP0 A 190 13.261 6.107 18.422 1.00 36.85 C HETATM 2887 C18 TP0 A 190 9.502 0.839 16.749 1.00 36.34 C HETATM 2888 C19 TP0 A 190 17.590 0.090 18.576 1.00 36.70 C HETATM 2889 C20 TP0 A 190 16.321 1.920 19.440 1.00 29.86 C HETATM 2890 C21 TP0 A 190 12.972 2.298 20.437 1.00 40.07 C HETATM 2891 C22 TP0 A 190 11.560 1.686 20.417 1.00 36.15 C HETATM 2892 C29 TP0 A 190 15.146 2.348 16.668 1.00 38.81 C HETATM 2893 C ACY A 191 14.062 -2.171 18.412 1.00 48.11 C HETATM 2894 O ACY A 191 14.927 -1.698 17.653 1.00 45.95 O HETATM 2895 OXT ACY A 191 13.974 -1.811 19.614 1.00 52.33 O HETATM 2896 CH3 ACY A 191 13.089 -3.164 17.864 1.00 44.24 C HETATM 2897 N1 TP0 B 190 15.533 2.777 42.318 1.00 54.97 N HETATM 2898 C3 TP0 B 190 12.230 0.644 42.426 1.00 58.96 C HETATM 2899 C4 TP0 B 190 12.980 -0.484 40.354 1.00 60.91 C HETATM 2900 C5 TP0 B 190 10.418 1.270 40.735 1.00 59.72 C HETATM 2901 C6 TP0 B 190 12.734 -0.587 41.719 1.00 59.82 C HETATM 2902 C7 TP0 B 190 10.831 1.053 42.057 1.00 59.40 C HETATM 2903 C8 TP0 B 190 12.931 1.393 43.326 1.00 55.89 C HETATM 2904 C10 TP0 B 190 13.439 -1.594 39.631 1.00 61.31 C HETATM 2905 C11 TP0 B 190 9.096 1.639 40.522 1.00 60.63 C HETATM 2906 C12 TP0 B 190 12.907 -1.805 42.373 1.00 60.66 C HETATM 2907 C13 TP0 B 190 9.928 1.200 43.107 1.00 58.99 C HETATM 2908 C14 TP0 B 190 15.276 2.344 43.717 1.00 53.66 C HETATM 2909 C15 TP0 B 190 13.639 -2.807 40.291 1.00 60.64 C HETATM 2910 C16 TP0 B 190 8.203 1.792 41.576 1.00 60.65 C HETATM 2911 C17 TP0 B 190 13.374 -2.913 41.658 1.00 60.15 C HETATM 2912 C18 TP0 B 190 8.621 1.574 42.875 1.00 59.72 C HETATM 2913 C19 TP0 B 190 16.561 3.835 42.280 1.00 54.71 C HETATM 2914 C20 TP0 B 190 15.970 1.679 41.428 1.00 54.88 C HETATM 2915 C21 TP0 B 190 12.759 0.857 39.668 1.00 60.74 C HETATM 2916 C22 TP0 B 190 11.270 1.137 39.476 1.00 59.37 C HETATM 2917 C29 TP0 B 190 14.339 1.126 43.828 1.00 54.74 C HETATM 2918 O HOH A 192 17.206 2.015 13.617 1.00 2.06 O HETATM 2919 O HOH A 193 20.922 -12.070 2.152 1.00 2.00 O HETATM 2920 O HOH A 194 7.987 -10.802 21.089 1.00 2.00 O HETATM 2921 O HOH A 195 17.788 5.375 17.111 1.00 8.51 O HETATM 2922 O HOH A 196 17.650 -13.399 23.962 1.00 2.00 O HETATM 2923 O HOH A 197 7.036 1.947 3.632 1.00 7.46 O HETATM 2924 O HOH A 198 18.856 9.417 12.703 1.00 5.72 O HETATM 2925 O HOH A 199 5.776 14.773 4.838 1.00 4.28 O HETATM 2926 O HOH A 200 12.161 -5.504 -3.667 1.00 2.00 O HETATM 2927 O HOH A 201 11.808 7.477 3.355 1.00 4.63 O HETATM 2928 O HOH A 202 -2.515 14.849 6.988 1.00 2.00 O HETATM 2929 O HOH A 203 9.408 -10.066 15.717 1.00 2.00 O HETATM 2930 O HOH A 204 19.624 7.378 19.358 1.00 11.99 O HETATM 2931 O HOH A 205 12.331 10.878 8.189 1.00 2.00 O HETATM 2932 O HOH A 206 24.737 -4.776 12.490 1.00 2.00 O HETATM 2933 O HOH A 207 13.006 -11.878 10.591 1.00 2.00 O HETATM 2934 O HOH A 208 21.650 -11.463 6.116 1.00 12.27 O HETATM 2935 O HOH A 209 7.543 0.841 25.758 1.00 2.00 O HETATM 2936 O HOH A 210 24.944 -4.299 1.434 1.00 10.79 O HETATM 2937 O HOH A 211 16.769 2.520 -0.813 1.00 11.61 O HETATM 2938 O HOH A 212 14.937 0.778 -0.387 1.00 3.46 O HETATM 2939 O HOH A 213 27.773 -3.134 10.128 1.00 5.79 O HETATM 2940 O HOH A 214 8.168 -13.979 -1.238 1.00 4.91 O HETATM 2941 O HOH A 215 4.254 2.246 5.685 1.00 2.00 O HETATM 2942 O HOH A 216 9.062 10.466 8.389 1.00 2.00 O HETATM 2943 O HOH A 217 6.336 4.617 0.375 1.00 15.99 O HETATM 2944 O HOH A 218 6.945 11.392 6.851 1.00 7.40 O HETATM 2945 O HOH A 219 25.904 -6.847 1.097 1.00 13.09 O HETATM 2946 O HOH A 220 12.135 8.196 -1.536 1.00 3.81 O HETATM 2947 O HOH A 221 5.742 -17.965 17.205 1.00 12.72 O HETATM 2948 O HOH A 222 28.877 -1.247 8.105 1.00 2.00 O HETATM 2949 O HOH A 223 15.184 15.309 15.862 1.00 7.04 O HETATM 2950 O HOH A 224 9.533 -4.320 25.986 1.00 3.13 O HETATM 2951 O HOH A 225 19.718 10.990 5.544 1.00 2.00 O HETATM 2952 O HOH A 226 15.955 15.625 10.579 1.00 7.28 O HETATM 2953 O HOH A 227 13.080 9.952 1.796 1.00 8.54 O HETATM 2954 O HOH A 228 20.917 11.956 12.533 1.00 24.92 O HETATM 2955 O HOH A 229 5.801 -11.577 31.162 1.00 9.07 O HETATM 2956 O HOH A 230 11.919 -4.524 26.699 1.00 10.63 O HETATM 2957 O HOH A 231 20.657 -11.442 16.346 1.00 5.10 O HETATM 2958 O HOH A 232 22.858 -11.919 8.782 1.00 3.36 O HETATM 2959 O HOH A 233 10.463 7.589 0.424 1.00 4.96 O HETATM 2960 O HOH A 234 13.770 5.770 -3.248 1.00 29.04 O HETATM 2961 O HOH A 235 16.288 -6.046 -4.941 1.00 35.69 O HETATM 2962 O HOH A 236 0.324 19.303 13.238 1.00 33.47 O HETATM 2963 O HOH A 237 -0.301 -1.550 10.528 1.00 15.45 O HETATM 2964 O HOH A 238 18.408 -5.713 24.708 1.00 22.65 O HETATM 2965 O HOH A 239 21.799 -13.945 22.045 1.00 43.02 O HETATM 2966 O HOH A 240 14.900 15.859 18.847 1.00 19.99 O HETATM 2967 O HOH A 241 25.504 15.613 7.952 1.00 2.87 O HETATM 2968 O HOH A 242 28.906 10.578 8.375 1.00 4.29 O HETATM 2969 O HOH A 243 27.087 -2.550 0.929 1.00 16.57 O HETATM 2970 O HOH A 244 17.143 -18.163 12.301 1.00 37.83 O HETATM 2971 O HOH A 245 11.462 -22.271 18.911 1.00 17.95 O HETATM 2972 O HOH A 246 -1.789 15.115 4.467 1.00 12.15 O HETATM 2973 O HOH A 247 -2.645 0.070 17.402 1.00 19.99 O HETATM 2974 O HOH A 248 -0.097 -5.838 11.713 1.00 12.79 O HETATM 2975 O HOH A 249 17.702 -8.064 16.404 1.00 9.59 O HETATM 2976 O HOH A 250 31.359 4.372 5.178 1.00 4.94 O HETATM 2977 O HOH A 251 17.257 -15.422 17.662 1.00 45.56 O HETATM 2978 O HOH A 252 0.549 -11.599 18.826 1.00 20.49 O HETATM 2979 O HOH A 253 -0.298 0.481 29.627 1.00 2.00 O HETATM 2980 O HOH A 254 3.034 -7.458 4.671 1.00 17.61 O HETATM 2981 O HOH A 255 20.301 0.181 -3.119 1.00 20.86 O HETATM 2982 O HOH A 256 21.557 -11.259 -0.355 1.00 11.66 O HETATM 2983 O HOH A 257 10.567 -1.995 19.158 1.00 9.62 O HETATM 2984 O HOH A 258 16.645 -2.243 15.927 1.00 7.09 O HETATM 2985 O HOH A 259 12.552 0.751 -1.435 1.00 2.92 O HETATM 2986 O HOH A 260 -0.002 -1.660 7.166 1.00 19.58 O HETATM 2987 O HOH A 261 23.594 3.806 20.755 1.00 10.41 O HETATM 2988 O HOH A 262 0.662 11.914 25.431 1.00 12.89 O HETATM 2989 O HOH A 263 11.103 18.807 14.468 1.00 6.17 O HETATM 2990 O HOH A 264 23.468 -12.058 3.729 1.00 2.00 O HETATM 2991 O HOH B 191 16.065 1.488 46.811 1.00 18.06 O HETATM 2992 O HOH B 192 0.746 15.327 32.331 1.00 7.70 O HETATM 2993 O HOH B 193 12.153 -7.821 52.077 1.00 16.43 O HETATM 2994 O HOH B 194 -3.173 10.573 48.396 1.00 13.83 O HETATM 2995 O HOH B 195 10.818 18.795 48.220 1.00 13.51 O HETATM 2996 O HOH B 196 6.099 -16.020 50.428 1.00 16.01 O HETATM 2997 O HOH B 197 15.209 17.274 36.510 1.00 12.62 O HETATM 2998 O HOH B 198 6.991 7.426 27.927 1.00 20.50 O HETATM 2999 O HOH B 199 0.824 -15.862 50.054 1.00 25.17 O HETATM 3000 O HOH B 200 -1.393 3.500 48.818 1.00 41.66 O HETATM 3001 O HOH B 201 15.737 14.468 43.998 1.00 31.60 O HETATM 3002 O HOH B 202 9.214 4.712 40.725 1.00 37.70 O HETATM 3003 O HOH B 203 8.288 20.943 36.870 1.00 15.25 O HETATM 3004 O HOH B 204 18.994 -5.147 48.031 1.00 26.51 O HETATM 3005 O HOH B 205 -4.428 16.757 37.367 1.00 7.18 O HETATM 3006 O HOH B 206 -4.015 6.681 35.819 1.00 15.16 O HETATM 3007 O HOH B 207 -2.909 5.709 25.746 1.00 14.94 O HETATM 3008 O HOH B 208 13.682 4.009 40.512 1.00 44.71 O HETATM 3009 O HOH B 209 10.861 5.733 42.122 1.00 24.50 O HETATM 3010 O HOH B 210 14.204 -8.892 34.419 1.00 27.08 O HETATM 3011 O HOH B 211 -2.826 0.076 36.914 1.00 34.67 O HETATM 3012 O HOH B 212 17.599 -1.835 43.567 1.00 19.72 O HETATM 3013 O HOH B 213 6.861 18.417 54.441 1.00 47.71 O CONECT 21 1204 CONECT 583 1360 CONECT 1204 21 CONECT 1360 583 CONECT 1443 2626 CONECT 2005 2782 CONECT 2626 1443 CONECT 2782 2005 CONECT 2872 2883 2888 2889 CONECT 2873 2876 2877 2878 CONECT 2874 2876 2879 2890 CONECT 2875 2877 2880 2891 CONECT 2876 2873 2874 2881 CONECT 2877 2873 2875 2882 CONECT 2878 2873 2892 CONECT 2879 2874 2884 CONECT 2880 2875 2885 CONECT 2881 2876 2886 CONECT 2882 2877 2887 CONECT 2883 2872 2892 CONECT 2884 2879 2886 CONECT 2885 2880 2887 CONECT 2886 2881 2884 CONECT 2887 2882 2885 CONECT 2888 2872 CONECT 2889 2872 CONECT 2890 2874 2891 CONECT 2891 2875 2890 CONECT 2892 2878 2883 CONECT 2893 2894 2895 2896 CONECT 2894 2893 CONECT 2895 2893 CONECT 2896 2893 CONECT 2897 2908 2913 2914 CONECT 2898 2901 2902 2903 CONECT 2899 2901 2904 2915 CONECT 2900 2902 2905 2916 CONECT 2901 2898 2899 2906 CONECT 2902 2898 2900 2907 CONECT 2903 2898 2917 CONECT 2904 2899 2909 CONECT 2905 2900 2910 CONECT 2906 2901 2911 CONECT 2907 2902 2912 CONECT 2908 2897 2917 CONECT 2909 2904 2911 CONECT 2910 2905 2912 CONECT 2911 2906 2909 CONECT 2912 2907 2910 CONECT 2913 2897 CONECT 2914 2897 CONECT 2915 2899 2916 CONECT 2916 2900 2915 CONECT 2917 2903 2908 MASTER 365 0 3 14 40 0 8 6 3011 2 54 30 END If you find results from this site helpful for your research, please cite one of our papers:
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