HEADER HYDROLASE 26-OCT-01 1GOU TITLE RIBONUCLEASE BINASE (G SPECIFIC ENDONUCLEASE) UNLIGANDED TITLE 2 FORM COMPND MOL_ID: 1; COMPND 2 MOLECULE: RIBONUCLEASE; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: BINASE, G SPECIFIC ENDONUCLEASE; COMPND 5 EC: 3.1.27.3; COMPND 6 ENGINEERED: YES; COMPND 7 OTHER_DETAILS: UNLIGANDED FORM SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS INTERMEDIUS; SOURCE 3 ORGANISM_TAXID: 1400; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS HYDROLASE, ENDORIBONUCLEASE, NUCLEASE EXPDTA X-RAY DIFFRACTION AUTHOR K.M.POLYAKOV,A.A.LEBEDEV,G.G.DODSON REVDAT 3 24-FEB-09 1GOU 1 VERSN REVDAT 2 03-MAY-02 1GOU 1 JRNL REVDAT 1 29-NOV-01 1GOU 0 JRNL AUTH K.M.POLYAKOV,A.A.LEBEDEV,A.L.OKOROKOV,K.I.PANOV, JRNL AUTH 2 A.A.SCHULGA,A.G.PAVLOVSKY,M.Y.A.KARPEISKY, JRNL AUTH 3 G.G.DODSON JRNL TITL THE STRUCTURE OF SUBSTRATE-FREE MICROBIAL JRNL TITL 2 RIBONUCLEASE BINASE AND OF ITS COMPLEXES WITH JRNL TITL 3 3'GMP AND SULFATE IONS JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 58 744 2002 JRNL REFN ISSN 0907-4449 JRNL PMID 11976484 JRNL DOI 10.1107/S0907444902003207 REMARK 2 REMARK 2 RESOLUTION. 1.65 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.1.00 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3 REMARK 3 NUMBER OF REFLECTIONS : 28989 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.140 REMARK 3 FREE R VALUE : 0.176 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1546 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.65 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2029 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.1440 REMARK 3 BIN FREE R VALUE SET COUNT : 114 REMARK 3 BIN FREE R VALUE : 0.1750 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1773 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 255 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.103 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.079 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.048 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.390 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1816 ; 0.018 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): 1625 ; 0.003 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL REMARK 3 BOND ANGLES OTHERS (DEGREES): 2465 ; 2.077 ; 1.929 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3741 ; 2.555 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 261 ; 0.149 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2074 ; 0.011 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 434 ; 0.005 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 276 ; 0.189 ; 0.100 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1477 ; 0.154 ; 0.100 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): 1039 ; 0.081 ; 0.100 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 121 ; 0.177 ; 0.100 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): 5 ; 0.129 ; 0.100 REMARK 3 SYMMETRY VDW OTHERS (A): 18 ; 0.198 ; 0.100 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 23 ; 0.111 ; 0.100 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): 1103 ; 1.822 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1768 ; 2.771 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 713 ; 3.269 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 697 ; 4.803 ; 4.500 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL PLUS 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 REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 1GOU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-OCT-01. REMARK 100 THE PDBE ID CODE IS EBI-8770. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 287.0 REMARK 200 PH : 9.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.98 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28989 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650 REMARK 200 RESOLUTION RANGE LOW (A) : 10.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3 REMARK 200 DATA REDUNDANCY : 4.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: BLANC REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL 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 57.51500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 16.64500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 57.51500 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 16.64500 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 GENERATING THE BIOMOLECULE 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: PQS 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 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PQS 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 PHE A -7 REMARK 465 THR A -6 REMARK 465 PRO A -5 REMARK 465 VAL A -4 REMARK 465 THR A -3 REMARK 465 LYS A -2 REMARK 465 ALA A -1 REMARK 465 PHE B -7 REMARK 465 THR B -6 REMARK 465 PRO B -5 REMARK 465 VAL B -4 REMARK 465 THR B -3 REMARK 465 LYS B -2 REMARK 465 ALA B -1 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 SER A 67 CB OG REMARK 470 LYS B 38 CE NZ REMARK 470 SER B 67 CB OG REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O HOH B 2050 - O HOH B 2102 2.17 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ASP A 92 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES REMARK 500 ARG B 15 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES REMARK 500 ARG B 15 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 ASP B 53 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES REMARK 500 ARG B 61 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 GLY B 66 N - CA - C ANGL. DEV. = -21.7 DEGREES REMARK 500 SER B 67 C - N - CA ANGL. DEV. = 19.7 DEGREES REMARK 500 ARG B 68 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES REMARK 500 ARG B 71 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 ASP B 92 CB - CG - OD2 ANGL. DEV. = 7.8 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 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 VAL A 2 96.33 50.03 REMARK 500 ASN A 4 20.61 -142.32 REMARK 500 VAL A 78 -60.16 -120.45 REMARK 500 ASN B 4 20.40 -143.91 REMARK 500 VAL B 78 -56.55 -122.70 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 GLY B 66 SER B 67 -67.08 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 GLY B 66 10.44 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 SER A 56 20.9 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1BUJ RELATED DB: PDB REMARK 900 STRUCTURE OF BINASE IN SOLUTION REMARK 900 RELATED ID: 2RBI RELATED DB: PDB REMARK 900 STRUCTURE OF BINASE MUTANT HIS 101 ASN REMARK 900 RELATED ID: 1GOV RELATED DB: PDB REMARK 900 STRUCTURE OF RIBONUCLEASE BI(G SPECIFIC ENDONUCLEASE) REMARK 900 COMPLEXED WITH SULFATE IONS REMARK 900 RELATED ID: 1GOY RELATED DB: PDB REMARK 900 STRUCTURE OF RIBONUCLEASE BI(G SPECIFIC ENDONUCLEASE) REMARK 900 COMPLEXED WITH GUANOSINE-3'-PHOSPHATE (3'-GMP) DBREF 1GOU A -7 -1 PDB 1GOU 1GOU -7 -1 DBREF 1GOU A 1 109 UNP P00649 RN_BACIN 54 162 DBREF 1GOU B -7 -1 PDB 1GOU 1GOU -7 -1 DBREF 1GOU B 1 109 UNP P00649 RN_BACIN 54 162 SEQADV 1GOU ASN A 21 UNP P00649 ASP 74 CONFLICT SEQADV 1GOU ASP A 22 UNP P00649 ASN 75 CONFLICT SEQADV 1GOU ASP A 40 UNP P00649 ASN 93 CONFLICT SEQADV 1GOU GLY A 66 UNP P00649 SER 119 CONFLICT SEQADV 1GOU SER A 67 UNP P00649 GLY 120 CONFLICT SEQADV 1GOU ASN B 21 UNP P00649 ASP 74 CONFLICT SEQADV 1GOU ASP B 22 UNP P00649 ASN 75 CONFLICT SEQADV 1GOU ASP B 40 UNP P00649 ASN 93 CONFLICT SEQADV 1GOU GLY B 66 UNP P00649 SER 119 CONFLICT SEQADV 1GOU SER B 67 UNP P00649 GLY 120 CONFLICT SEQRES 1 A 116 PHE THR PRO VAL THR LYS ALA ALA VAL ILE ASN THR PHE SEQRES 2 A 116 ASP GLY VAL ALA ASP TYR LEU ILE ARG TYR LYS ARG LEU SEQRES 3 A 116 PRO ASN ASP TYR ILE THR LYS SER GLN ALA SER ALA LEU SEQRES 4 A 116 GLY TRP VAL ALA SER LYS GLY ASP LEU ALA GLU VAL ALA SEQRES 5 A 116 PRO GLY LYS SER ILE GLY GLY ASP VAL PHE SER ASN ARG SEQRES 6 A 116 GLU GLY ARG LEU PRO SER ALA GLY SER ARG THR TRP ARG SEQRES 7 A 116 GLU ALA ASP ILE ASN TYR VAL SER GLY PHE ARG ASN ALA SEQRES 8 A 116 ASP ARG LEU VAL TYR SER SER ASP TRP LEU ILE TYR LYS SEQRES 9 A 116 THR THR ASP HIS TYR ALA THR PHE THR ARG ILE ARG SEQRES 1 B 116 PHE THR PRO VAL THR LYS ALA ALA VAL ILE ASN THR PHE SEQRES 2 B 116 ASP GLY VAL ALA ASP TYR LEU ILE ARG TYR LYS ARG LEU SEQRES 3 B 116 PRO ASN ASP TYR ILE THR LYS SER GLN ALA SER ALA LEU SEQRES 4 B 116 GLY TRP VAL ALA SER LYS GLY ASP LEU ALA GLU VAL ALA SEQRES 5 B 116 PRO GLY LYS SER ILE GLY GLY ASP VAL PHE SER ASN ARG SEQRES 6 B 116 GLU GLY ARG LEU PRO SER ALA GLY SER ARG THR TRP ARG SEQRES 7 B 116 GLU ALA ASP ILE ASN TYR VAL SER GLY PHE ARG ASN ALA SEQRES 8 B 116 ASP ARG LEU VAL TYR SER SER ASP TRP LEU ILE TYR LYS SEQRES 9 B 116 THR THR ASP HIS TYR ALA THR PHE THR ARG ILE ARG FORMUL 3 HOH *255(H2 O1) HELIX 1 1 THR A 5 LYS A 17 1 13 HELIX 2 2 THR A 25 LEU A 32 1 8 HELIX 3 3 VAL A 35 GLY A 39 5 5 HELIX 4 4 ASP A 40 ALA A 45 1 6 HELIX 5 5 THR B 5 LYS B 17 1 13 HELIX 6 6 THR B 25 LEU B 32 1 8 HELIX 7 7 VAL B 35 GLY B 39 5 5 HELIX 8 8 ASP B 40 ALA B 45 1 6 SHEET 1 AA 6 TYR A 23 ILE A 24 0 SHEET 2 AA 6 SER A 49 PHE A 55 1 O SER A 49 N ILE A 24 SHEET 3 AA 6 TRP A 70 ASP A 74 -1 O TRP A 70 N PHE A 55 SHEET 4 AA 6 ARG A 86 SER A 90 -1 O LEU A 87 N ALA A 73 SHEET 5 AA 6 ILE A 95 THR A 98 -1 O TYR A 96 N VAL A 88 SHEET 6 AA 6 THR A 106 ARG A 109 -1 O THR A 106 N LYS A 97 SHEET 1 BA 6 TYR B 23 ILE B 24 0 SHEET 2 BA 6 SER B 49 PHE B 55 1 O SER B 49 N ILE B 24 SHEET 3 BA 6 TRP B 70 ASP B 74 -1 O TRP B 70 N PHE B 55 SHEET 4 BA 6 ARG B 86 SER B 90 -1 O LEU B 87 N ALA B 73 SHEET 5 BA 6 ILE B 95 THR B 98 -1 O TYR B 96 N VAL B 88 SHEET 6 BA 6 THR B 106 ARG B 107 -1 O THR B 106 N LYS B 97 CRYST1 115.030 33.290 78.700 90.00 119.08 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 0.008693 0.000000 0.004835 0.00000 SCALE2 0.000000 0.030039 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014539 0.00000 ATOM 1 N ALA A 1 -8.178 22.154 36.483 1.00 49.01 N ANISOU 1 N ALA A 1 6176 6195 6248 -14 -10 55 N ATOM 2 CA ALA A 1 -7.596 22.741 35.202 1.00 47.98 C ANISOU 2 CA ALA A 1 6071 6046 6111 0 2 -2 C ATOM 3 C ALA A 1 -6.721 21.708 34.474 1.00 46.09 C ANISOU 3 C ALA A 1 5859 5736 5913 -53 -21 21 C ATOM 4 O ALA A 1 -5.594 21.981 34.020 1.00 47.48 O ANISOU 4 O ALA A 1 5977 6045 6018 -47 30 64 O ATOM 5 CB ALA A 1 -6.788 24.028 35.531 1.00 48.74 C ANISOU 5 CB ALA A 1 6176 6124 6218 -41 -34 -9 C ATOM 6 N VAL A 2 -7.325 20.537 34.285 1.00 43.02 N ANISOU 6 N VAL A 2 5483 5372 5488 21 -31 -22 N ATOM 7 CA VAL A 2 -6.623 19.255 34.038 1.00 38.70 C ANISOU 7 CA VAL A 2 4957 4825 4920 28 -60 49 C ATOM 8 C VAL A 2 -5.499 18.992 35.080 1.00 33.44 C ANISOU 8 C VAL A 2 4360 4006 4338 -32 60 -1 C ATOM 9 O VAL A 2 -4.382 19.423 34.949 1.00 33.59 O ANISOU 9 O VAL A 2 4448 3814 4501 -99 -70 68 O ATOM 10 CB VAL A 2 -6.202 18.958 32.582 1.00 39.51 C ANISOU 10 CB VAL A 2 5050 4952 5010 26 -7 -3 C ATOM 11 CG1 VAL A 2 -5.505 17.585 32.486 1.00 39.75 C ANISOU 11 CG1 VAL A 2 5103 5033 4967 41 -33 11 C ATOM 12 CG2 VAL A 2 -7.447 18.921 31.675 1.00 40.80 C ANISOU 12 CG2 VAL A 2 5221 5099 5180 48 -76 18 C ATOM 13 N ILE A 3 -5.858 18.219 36.092 1.00 28.02 N ANISOU 13 N ILE A 3 3699 3203 3743 76 -105 -84 N ATOM 14 CA ILE A 3 -4.938 17.733 37.102 1.00 22.77 C ANISOU 14 CA ILE A 3 3185 2222 3243 -6 -66 -98 C ATOM 15 C ILE A 3 -4.754 16.259 36.681 1.00 20.41 C ANISOU 15 C ILE A 3 2806 2001 2947 113 -9 -81 C ATOM 16 O ILE A 3 -5.725 15.511 36.812 1.00 19.96 O ANISOU 16 O ILE A 3 2844 1430 3308 260 -167 -99 O ATOM 17 CB ILE A 3 -5.583 17.797 38.449 1.00 22.29 C ANISOU 17 CB ILE A 3 3129 2192 3148 91 -115 -189 C ATOM 18 CG1 ILE A 3 -5.758 19.306 38.855 1.00 23.84 C ANISOU 18 CG1 ILE A 3 3416 2244 3397 38 -8 -115 C ATOM 19 CG2 ILE A 3 -4.706 17.123 39.488 1.00 21.97 C ANISOU 19 CG2 ILE A 3 3120 2145 3082 -44 -121 -121 C ATOM 20 CD1 ILE A 3 -6.562 19.491 40.076 1.00 25.99 C ANISOU 20 CD1 ILE A 3 3658 2640 3574 27 99 -62 C ATOM 21 N ASN A 4 -3.588 15.902 36.177 1.00 17.74 N ANISOU 21 N ASN A 4 2595 1503 2641 9 -95 99 N ATOM 22 CA ASN A 4 -3.383 14.504 35.711 1.00 17.70 C ANISOU 22 CA ASN A 4 2493 1816 2414 17 -70 -60 C ATOM 23 C ASN A 4 -2.015 13.971 36.007 1.00 16.96 C ANISOU 23 C ASN A 4 2432 1693 2319 -30 -59 57 C ATOM 24 O ASN A 4 -1.595 13.008 35.373 1.00 19.49 O ANISOU 24 O ASN A 4 2799 2084 2522 -18 -126 -217 O ATOM 25 CB ASN A 4 -3.711 14.380 34.200 1.00 17.65 C ANISOU 25 CB ASN A 4 2417 1696 2592 62 -134 -127 C ATOM 26 CG ASN A 4 -2.656 14.993 33.305 1.00 21.27 C ANISOU 26 CG ASN A 4 3097 2547 2436 -51 -54 110 C ATOM 27 OD1 ASN A 4 -1.834 15.797 33.771 1.00 23.03 O ANISOU 27 OD1 ASN A 4 3814 1789 3147 -194 -60 184 O ATOM 28 ND2 ASN A 4 -2.608 14.564 32.024 1.00 22.57 N ANISOU 28 ND2 ASN A 4 3641 2042 2891 168 -164 -218 N ATOM 29 N THR A 5 -1.293 14.556 36.966 1.00 16.79 N ANISOU 29 N THR A 5 2507 1576 2296 6 -85 -28 N ATOM 30 CA THR A 5 0.024 14.077 37.347 1.00 17.51 C ANISOU 30 CA THR A 5 2319 1932 2400 -75 -13 18 C ATOM 31 C THR A 5 -0.087 13.201 38.580 1.00 15.55 C ANISOU 31 C THR A 5 2111 1619 2175 -79 -26 -21 C ATOM 32 O THR A 5 -1.070 13.250 39.305 1.00 14.45 O ANISOU 32 O THR A 5 2189 1112 2186 -20 3 -56 O ATOM 33 CB THR A 5 0.977 15.230 37.694 1.00 19.16 C ANISOU 33 CB THR A 5 2457 2202 2621 -161 3 3 C ATOM 34 OG1 THR A 5 0.431 16.039 38.747 1.00 20.01 O ANISOU 34 OG1 THR A 5 3098 1517 2986 -131 9 -23 O ATOM 35 CG2 THR A 5 1.144 16.160 36.461 1.00 22.01 C ANISOU 35 CG2 THR A 5 2801 2743 2820 -50 -82 195 C ATOM 36 N PHE A 6 0.944 12.427 38.853 1.00 15.53 N ANISOU 36 N PHE A 6 2039 1729 2130 -55 53 -138 N ATOM 37 CA PHE A 6 0.924 11.587 40.071 1.00 15.79 C ANISOU 37 CA PHE A 6 2103 1823 2070 -32 -58 0 C ATOM 38 C PHE A 6 0.700 12.398 41.355 1.00 15.36 C ANISOU 38 C PHE A 6 1981 1628 2227 48 24 -38 C ATOM 39 O PHE A 6 -0.167 12.127 42.138 1.00 14.99 O ANISOU 39 O PHE A 6 2413 1207 2073 21 138 -87 O ATOM 40 CB PHE A 6 2.193 10.775 40.248 1.00 16.21 C ANISOU 40 CB PHE A 6 2106 1923 2129 15 98 -24 C ATOM 41 CG PHE A 6 2.350 9.655 39.251 1.00 16.53 C ANISOU 41 CG PHE A 6 2182 1907 2192 33 -93 -27 C ATOM 42 CD1 PHE A 6 3.328 9.704 38.255 1.00 18.21 C ANISOU 42 CD1 PHE A 6 2479 1929 2510 -55 -67 -162 C ATOM 43 CD2 PHE A 6 1.463 8.575 39.297 1.00 16.65 C ANISOU 43 CD2 PHE A 6 2403 1839 2083 129 -84 -92 C ATOM 44 CE1 PHE A 6 3.452 8.638 37.350 1.00 20.83 C ANISOU 44 CE1 PHE A 6 2710 2666 2538 139 -92 -203 C ATOM 45 CE2 PHE A 6 1.599 7.505 38.383 1.00 17.46 C ANISOU 45 CE2 PHE A 6 2559 1742 2331 -31 -238 -111 C ATOM 46 CZ PHE A 6 2.575 7.565 37.440 1.00 18.59 C ANISOU 46 CZ PHE A 6 2679 2110 2272 161 -126 -135 C ATOM 47 N ASP A 7 1.492 13.451 41.531 1.00 16.96 N ANISOU 47 N ASP A 7 2289 1830 2325 -98 45 -79 N ATOM 48 CA ASP A 7 1.331 14.275 42.736 1.00 16.18 C ANISOU 48 CA ASP A 7 2178 1775 2194 -182 -26 -100 C ATOM 49 C ASP A 7 0.057 15.055 42.743 1.00 15.62 C ANISOU 49 C ASP A 7 2112 1668 2152 -273 -72 -87 C ATOM 50 O ASP A 7 -0.532 15.194 43.782 1.00 17.74 O ANISOU 50 O ASP A 7 2338 1834 2568 -130 10 -90 O ATOM 51 CB ASP A 7 2.529 15.219 42.904 1.00 18.34 C ANISOU 51 CB ASP A 7 2275 2125 2567 -307 -56 -83 C ATOM 52 CG ASP A 7 3.743 14.497 43.355 1.00 19.37 C ANISOU 52 CG ASP A 7 2544 2163 2651 -109 -26 -74 C ATOM 53 OD1 ASP A 7 4.783 14.612 42.678 1.00 26.54 O ANISOU 53 OD1 ASP A 7 2841 3567 3673 -18 152 73 O ATOM 54 OD2 ASP A 7 3.743 13.756 44.349 1.00 19.26 O ANISOU 54 OD2 ASP A 7 2723 1809 2784 -21 -337 -168 O ATOM 55 N GLY A 8 -0.322 15.633 41.605 1.00 15.33 N ANISOU 55 N GLY A 8 2128 1501 2193 -132 -130 -149 N ATOM 56 CA GLY A 8 -1.547 16.423 41.511 1.00 16.13 C ANISOU 56 CA GLY A 8 2146 1732 2250 -34 -18 -130 C ATOM 57 C GLY A 8 -2.781 15.668 41.897 1.00 16.15 C ANISOU 57 C GLY A 8 2189 1701 2246 8 29 -168 C ATOM 58 O GLY A 8 -3.611 16.117 42.698 1.00 16.30 O ANISOU 58 O GLY A 8 2255 1413 2525 -23 80 -258 O ATOM 59 N VAL A 9 -2.888 14.436 41.346 1.00 15.39 N ANISOU 59 N VAL A 9 2144 1504 2197 17 7 -271 N ATOM 60 CA VAL A 9 -4.065 13.633 41.604 1.00 14.66 C ANISOU 60 CA VAL A 9 2040 1491 2040 48 0 -166 C ATOM 61 C VAL A 9 -4.024 13.086 43.033 1.00 14.23 C ANISOU 61 C VAL A 9 2078 1286 2040 -5 2 -287 C ATOM 62 O VAL A 9 -5.053 13.054 43.704 1.00 14.88 O ANISOU 62 O VAL A 9 2280 1190 2182 -33 43 -172 O ATOM 63 CB VAL A 9 -4.231 12.537 40.528 1.00 14.36 C ANISOU 63 CB VAL A 9 1969 1617 1870 11 35 -200 C ATOM 64 CG1 VAL A 9 -5.454 11.633 40.881 1.00 17.24 C ANISOU 64 CG1 VAL A 9 2319 1817 2412 -106 57 -157 C ATOM 65 CG2 VAL A 9 -4.392 13.160 39.124 1.00 15.01 C ANISOU 65 CG2 VAL A 9 1982 1531 2188 -145 -43 -152 C ATOM 66 N ALA A 10 -2.835 12.648 43.486 1.00 14.62 N ANISOU 66 N ALA A 10 2055 1444 2053 49 40 -201 N ATOM 67 CA ALA A 10 -2.695 12.114 44.835 1.00 14.94 C ANISOU 67 CA ALA A 10 2060 1635 1982 -52 83 -188 C ATOM 68 C ALA A 10 -3.100 13.161 45.883 1.00 16.13 C ANISOU 68 C ALA A 10 2257 1735 2138 -51 120 -217 C ATOM 69 O ALA A 10 -3.878 12.869 46.743 1.00 16.47 O ANISOU 69 O ALA A 10 2532 1559 2167 -48 158 -256 O ATOM 70 CB ALA A 10 -1.343 11.602 45.104 1.00 15.63 C ANISOU 70 CB ALA A 10 2261 1668 2009 -77 -63 -59 C ATOM 71 N ASP A 11 -2.623 14.382 45.709 1.00 17.16 N ANISOU 71 N ASP A 11 2460 1782 2278 108 132 -89 N ATOM 72 CA ASP A 11 -2.925 15.464 46.676 1.00 17.84 C ANISOU 72 CA ASP A 11 2483 1961 2334 0 77 -202 C ATOM 73 C ASP A 11 -4.380 15.883 46.594 1.00 17.80 C ANISOU 73 C ASP A 11 2518 1847 2398 -38 44 -143 C ATOM 74 O ASP A 11 -5.007 16.181 47.619 1.00 20.18 O ANISOU 74 O ASP A 11 2821 2324 2521 -31 111 -412 O ATOM 75 CB ASP A 11 -2.006 16.638 46.415 1.00 19.60 C ANISOU 75 CB ASP A 11 2547 2218 2682 4 49 -190 C ATOM 76 CG ASP A 11 -0.592 16.385 46.852 1.00 22.18 C ANISOU 76 CG ASP A 11 2918 2681 2826 10 -124 -198 C ATOM 77 OD1 ASP A 11 -0.298 15.431 47.589 1.00 22.19 O ANISOU 77 OD1 ASP A 11 2978 2573 2877 375 -503 -499 O ATOM 78 OD2 ASP A 11 0.279 17.158 46.476 1.00 28.46 O ANISOU 78 OD2 ASP A 11 3263 3751 3799 -289 140 -266 O ATOM 79 N TYR A 12 -4.952 15.863 45.404 1.00 16.38 N ANISOU 79 N TYR A 12 2381 1497 2346 26 70 -117 N ATOM 80 CA TYR A 12 -6.374 16.118 45.264 1.00 17.45 C ANISOU 80 CA TYR A 12 2413 1782 2434 118 3 -98 C ATOM 81 C TYR A 12 -7.238 15.095 45.974 1.00 18.62 C ANISOU 81 C TYR A 12 2489 2119 2466 109 77 -146 C ATOM 82 O TYR A 12 -8.184 15.414 46.670 1.00 18.21 O ANISOU 82 O TYR A 12 2608 1829 2478 336 83 -410 O ATOM 83 CB TYR A 12 -6.729 16.237 43.810 1.00 17.38 C ANISOU 83 CB TYR A 12 2328 1885 2390 1 -53 -175 C ATOM 84 CG TYR A 12 -8.083 16.848 43.551 1.00 17.49 C ANISOU 84 CG TYR A 12 2241 1895 2506 177 -51 -14 C ATOM 85 CD1 TYR A 12 -8.212 18.150 43.116 1.00 20.17 C ANISOU 85 CD1 TYR A 12 2541 2101 3020 -191 -126 -55 C ATOM 86 CD2 TYR A 12 -9.223 16.090 43.613 1.00 17.82 C ANISOU 86 CD2 TYR A 12 2452 1495 2821 90 1 -262 C ATOM 87 CE1 TYR A 12 -9.451 18.686 42.885 1.00 20.73 C ANISOU 87 CE1 TYR A 12 2686 2088 3099 69 -135 40 C ATOM 88 CE2 TYR A 12 -10.470 16.593 43.347 1.00 20.78 C ANISOU 88 CE2 TYR A 12 2658 2248 2987 109 -126 10 C ATOM 89 CZ TYR A 12 -10.584 17.911 42.964 1.00 20.90 C ANISOU 89 CZ TYR A 12 2593 2312 3033 95 104 41 C ATOM 90 OH TYR A 12 -11.836 18.451 42.701 1.00 24.86 O ANISOU 90 OH TYR A 12 2997 2905 3541 411 -52 23 O ATOM 91 N LEU A 13 -6.918 13.821 45.783 1.00 18.21 N ANISOU 91 N LEU A 13 2527 1948 2442 188 150 -209 N ATOM 92 CA LEU A 13 -7.628 12.754 46.467 1.00 18.63 C ANISOU 92 CA LEU A 13 2525 2153 2399 115 132 -75 C ATOM 93 C LEU A 13 -7.567 12.914 47.986 1.00 20.22 C ANISOU 93 C LEU A 13 2753 2267 2660 31 142 -126 C ATOM 94 O LEU A 13 -8.591 12.736 48.652 1.00 20.62 O ANISOU 94 O LEU A 13 2897 2234 2704 103 430 -408 O ATOM 95 CB LEU A 13 -7.058 11.375 46.066 1.00 18.78 C ANISOU 95 CB LEU A 13 2539 2102 2493 83 65 -178 C ATOM 96 CG LEU A 13 -7.502 10.861 44.702 1.00 18.62 C ANISOU 96 CG LEU A 13 2345 2207 2522 310 -16 -87 C ATOM 97 CD1 LEU A 13 -6.514 9.746 44.244 1.00 19.80 C ANISOU 97 CD1 LEU A 13 2683 1988 2850 228 94 -156 C ATOM 98 CD2 LEU A 13 -8.936 10.352 44.781 1.00 18.99 C ANISOU 98 CD2 LEU A 13 2487 2113 2615 45 69 -251 C ATOM 99 N ILE A 14 -6.405 13.239 48.519 1.00 20.81 N ANISOU 99 N ILE A 14 2776 2469 2659 70 94 18 N ATOM 100 CA ILE A 14 -6.249 13.363 49.967 1.00 22.00 C ANISOU 100 CA ILE A 14 3021 2605 2731 77 112 -149 C ATOM 101 C ILE A 14 -7.125 14.522 50.493 1.00 23.54 C ANISOU 101 C ILE A 14 3149 2810 2982 91 137 -159 C ATOM 102 O ILE A 14 -7.798 14.370 51.532 1.00 25.91 O ANISOU 102 O ILE A 14 3668 3095 3081 176 286 -345 O ATOM 103 CB ILE A 14 -4.760 13.487 50.387 1.00 22.47 C ANISOU 103 CB ILE A 14 3018 2735 2784 125 103 -131 C ATOM 104 CG1 ILE A 14 -3.901 12.213 50.137 1.00 23.69 C ANISOU 104 CG1 ILE A 14 3276 2933 2789 100 -11 -5 C ATOM 105 CG2 ILE A 14 -4.613 13.876 51.875 1.00 24.80 C ANISOU 105 CG2 ILE A 14 3282 3191 2948 51 7 -8 C ATOM 106 CD1AILE A 14 -4.578 10.918 50.557 0.50 23.91 C ANISOU 106 CD1AILE A 14 3121 2931 3030 -78 45 -18 C ATOM 107 CD1BILE A 14 -2.436 12.593 49.975 0.50 23.80 C ANISOU 107 CD1BILE A 14 3168 2915 2958 50 15 -24 C ATOM 108 N ARG A 15 -7.080 15.635 49.794 1.00 24.51 N ANISOU 108 N ARG A 15 3346 2858 3107 150 76 -206 N ATOM 109 CA ARG A 15 -7.840 16.838 50.212 1.00 25.84 C ANISOU 109 CA ARG A 15 3431 3081 3304 161 83 -177 C ATOM 110 C ARG A 15 -9.348 16.713 50.043 1.00 26.20 C ANISOU 110 C ARG A 15 3493 3159 3301 156 90 -137 C ATOM 111 O ARG A 15 -10.126 17.088 50.949 1.00 26.87 O ANISOU 111 O ARG A 15 3747 3072 3388 354 236 -350 O ATOM 112 CB ARG A 15 -7.326 18.016 49.388 1.00 27.16 C ANISOU 112 CB ARG A 15 3632 3229 3459 53 26 -162 C ATOM 113 CG ARG A 15 -7.844 19.380 49.851 1.00 32.82 C ANISOU 113 CG ARG A 15 4256 3898 4312 248 33 -191 C ATOM 114 CD ARG A 15 -7.192 20.543 49.071 1.00 40.91 C ANISOU 114 CD ARG A 15 5323 4946 5272 -63 96 78 C ATOM 115 NE ARG A 15 -5.810 20.896 49.409 1.00 47.54 N ANISOU 115 NE ARG A 15 5758 6079 6223 -26 -52 -42 N ATOM 116 CZ ARG A 15 -5.340 21.421 50.571 1.00 52.04 C ANISOU 116 CZ ARG A 15 6599 6654 6517 -33 -73 -84 C ATOM 117 NH1 ARG A 15 -6.120 21.655 51.640 1.00 53.15 N ANISOU 117 NH1 ARG A 15 6726 6792 6674 -5 51 -58 N ATOM 118 NH2 ARG A 15 -4.029 21.700 50.659 1.00 53.30 N ANISOU 118 NH2 ARG A 15 6600 6814 6834 -61 -42 -20 N ATOM 119 N TYR A 16 -9.793 16.195 48.896 1.00 25.12 N ANISOU 119 N TYR A 16 3333 2944 3265 174 19 -218 N ATOM 120 CA TYR A 16 -11.224 16.185 48.547 1.00 25.94 C ANISOU 120 CA TYR A 16 3320 3153 3381 43 70 -128 C ATOM 121 C TYR A 16 -11.927 14.842 48.575 1.00 26.50 C ANISOU 121 C TYR A 16 3314 3305 3450 23 33 -128 C ATOM 122 O TYR A 16 -13.162 14.810 48.429 1.00 27.04 O ANISOU 122 O TYR A 16 3299 3392 3583 78 120 -274 O ATOM 123 CB TYR A 16 -11.410 16.826 47.192 1.00 25.85 C ANISOU 123 CB TYR A 16 3300 3136 3383 75 39 -116 C ATOM 124 CG TYR A 16 -10.919 18.256 47.162 1.00 27.55 C ANISOU 124 CG TYR A 16 3496 3233 3736 19 72 -133 C ATOM 125 CD1 TYR A 16 -9.780 18.612 46.474 1.00 27.79 C ANISOU 125 CD1 TYR A 16 3540 3317 3701 224 155 -206 C ATOM 126 CD2 TYR A 16 -11.631 19.285 47.844 1.00 31.66 C ANISOU 126 CD2 TYR A 16 4017 3776 4235 162 177 -274 C ATOM 127 CE1 TYR A 16 -9.313 19.924 46.440 1.00 32.36 C ANISOU 127 CE1 TYR A 16 4086 3803 4403 -17 85 -68 C ATOM 128 CE2 TYR A 16 -11.159 20.613 47.820 1.00 34.40 C ANISOU 128 CE2 TYR A 16 4381 4038 4649 -21 160 -127 C ATOM 129 CZ TYR A 16 -9.998 20.922 47.132 1.00 33.83 C ANISOU 129 CZ TYR A 16 4451 4014 4389 1 213 -128 C ATOM 130 OH TYR A 16 -9.496 22.215 47.048 1.00 38.24 O ANISOU 130 OH TYR A 16 5306 3994 5230 -54 105 -260 O ATOM 131 N LYS A 17 -11.158 13.748 48.715 1.00 26.49 N ANISOU 131 N LYS A 17 3405 3338 3320 37 95 -64 N ATOM 132 CA LYS A 17 -11.685 12.380 48.816 1.00 27.09 C ANISOU 132 CA LYS A 17 3451 3463 3376 -29 97 -26 C ATOM 133 C LYS A 17 -12.437 11.921 47.558 1.00 26.27 C ANISOU 133 C LYS A 17 3388 3292 3300 -53 148 -63 C ATOM 134 O LYS A 17 -13.324 11.084 47.643 1.00 27.50 O ANISOU 134 O LYS A 17 3593 3457 3399 -245 282 -135 O ATOM 135 CB LYS A 17 -12.560 12.222 50.093 1.00 28.12 C ANISOU 135 CB LYS A 17 3556 3626 3502 13 154 -5 C ATOM 136 CG LYS A 17 -11.936 12.729 51.388 1.00 32.53 C ANISOU 136 CG LYS A 17 4203 4153 4005 -69 -20 -129 C ATOM 137 CD LYS A 17 -10.649 12.039 51.751 1.00 37.55 C ANISOU 137 CD LYS A 17 4670 4804 4791 98 9 12 C ATOM 138 CE LYS A 17 -10.199 12.331 53.211 1.00 40.69 C ANISOU 138 CE LYS A 17 5248 5162 5048 -13 -112 -15 C ATOM 139 NZ LYS A 17 -8.717 12.084 53.364 1.00 42.20 N ANISOU 139 NZ LYS A 17 5271 5312 5450 -56 -79 86 N ATOM 140 N ARG A 18 -12.097 12.512 46.407 1.00 23.69 N ANISOU 140 N ARG A 18 3162 2858 2980 -63 110 -55 N ATOM 141 CA ARG A 18 -12.667 12.152 45.119 1.00 23.18 C ANISOU 141 CA ARG A 18 3024 2821 2960 -43 76 -5 C ATOM 142 C ARG A 18 -11.685 12.535 44.062 1.00 20.23 C ANISOU 142 C ARG A 18 2741 2354 2592 27 11 -55 C ATOM 143 O ARG A 18 -10.788 13.342 44.323 1.00 19.78 O ANISOU 143 O ARG A 18 2767 2209 2538 2 249 -315 O ATOM 144 CB ARG A 18 -14.040 12.753 44.869 1.00 24.81 C ANISOU 144 CB ARG A 18 3150 3231 3043 -7 63 -15 C ATOM 145 CG ARG A 18 -14.100 14.241 44.865 1.00 30.98 C ANISOU 145 CG ARG A 18 4046 3741 3984 61 68 -16 C ATOM 146 CD ARG A 18 -15.421 14.792 44.343 1.00 39.18 C ANISOU 146 CD ARG A 18 4701 5177 5006 160 -107 87 C ATOM 147 NE ARG A 18 -15.304 16.250 44.306 1.00 46.73 N ANISOU 147 NE ARG A 18 5939 5704 6109 72 -63 48 N ATOM 148 CZ ARG A 18 -15.325 17.079 45.383 1.00 51.25 C ANISOU 148 CZ ARG A 18 6565 6456 6450 18 -46 -102 C ATOM 149 NH1 ARG A 18 -15.491 16.633 46.643 1.00 53.44 N ANISOU 149 NH1 ARG A 18 6801 6790 6712 12 9 47 N ATOM 150 NH2 ARG A 18 -15.177 18.382 45.189 1.00 52.77 N ANISOU 150 NH2 ARG A 18 6758 6523 6768 8 -19 2 N ATOM 151 N LEU A 19 -11.813 11.959 42.877 1.00 17.74 N ANISOU 151 N LEU A 19 2554 1762 2425 -25 63 -56 N ATOM 152 CA LEU A 19 -10.967 12.378 41.756 1.00 16.10 C ANISOU 152 CA LEU A 19 2386 1481 2247 38 31 -69 C ATOM 153 C LEU A 19 -11.358 13.764 41.256 1.00 16.54 C ANISOU 153 C LEU A 19 2333 1522 2428 41 36 -39 C ATOM 154 O LEU A 19 -12.529 14.173 41.362 1.00 17.04 O ANISOU 154 O LEU A 19 2528 1204 2739 -89 112 -194 O ATOM 155 CB LEU A 19 -11.125 11.406 40.542 1.00 16.16 C ANISOU 155 CB LEU A 19 2251 1669 2220 281 -91 -144 C ATOM 156 CG LEU A 19 -10.384 10.079 40.855 1.00 14.79 C ANISOU 156 CG LEU A 19 2290 1205 2122 -66 -11 136 C ATOM 157 CD1 LEU A 19 -10.872 9.095 39.760 1.00 16.62 C ANISOU 157 CD1 LEU A 19 2678 1331 2304 22 -25 25 C ATOM 158 CD2 LEU A 19 -8.859 10.169 40.875 1.00 15.58 C ANISOU 158 CD2 LEU A 19 2429 1138 2350 234 23 -48 C ATOM 159 N PRO A 20 -10.401 14.448 40.640 1.00 16.32 N ANISOU 159 N PRO A 20 2374 1454 2371 -27 32 -31 N ATOM 160 CA PRO A 20 -10.743 15.715 39.967 1.00 16.89 C ANISOU 160 CA PRO A 20 2453 1609 2354 85 5 -76 C ATOM 161 C PRO A 20 -11.766 15.503 38.835 1.00 17.94 C ANISOU 161 C PRO A 20 2591 1753 2470 99 -73 -75 C ATOM 162 O PRO A 20 -11.963 14.375 38.335 1.00 18.06 O ANISOU 162 O PRO A 20 2849 1246 2764 214 41 -242 O ATOM 163 CB PRO A 20 -9.418 16.207 39.404 1.00 18.65 C ANISOU 163 CB PRO A 20 2489 2028 2566 -129 -150 33 C ATOM 164 CG PRO A 20 -8.367 15.309 39.808 1.00 17.76 C ANISOU 164 CG PRO A 20 2609 1494 2643 -133 143 -58 C ATOM 165 CD PRO A 20 -8.987 14.126 40.538 1.00 15.27 C ANISOU 165 CD PRO A 20 2371 1111 2319 -108 54 87 C ATOM 166 N ASN A 21 -12.357 16.591 38.347 1.00 18.81 N ANISOU 166 N ASN A 21 2692 1661 2793 262 -43 -116 N ATOM 167 CA ASN A 21 -13.458 16.547 37.395 1.00 20.69 C ANISOU 167 CA ASN A 21 2815 2110 2933 168 -60 -19 C ATOM 168 C ASN A 21 -13.152 16.129 35.981 1.00 19.05 C ANISOU 168 C ASN A 21 2623 1827 2787 156 -140 110 C ATOM 169 O ASN A 21 -14.075 15.872 35.187 1.00 21.28 O ANISOU 169 O ASN A 21 2816 1978 3291 290 -281 -104 O ATOM 170 CB ASN A 21 -14.206 17.934 37.379 1.00 23.31 C ANISOU 170 CB ASN A 21 3071 2362 3422 366 -73 -66 C ATOM 171 CG ASN A 21 -14.872 18.289 38.700 1.00 30.29 C ANISOU 171 CG ASN A 21 4012 3594 3901 132 63 -86 C ATOM 172 OD1 ASN A 21 -15.139 17.449 39.566 1.00 37.35 O ANISOU 172 OD1 ASN A 21 4980 4561 4651 116 152 134 O ATOM 173 ND2 ASN A 21 -15.178 19.603 38.850 1.00 35.66 N ANISOU 173 ND2 ASN A 21 4844 3817 4888 361 -7 -134 N ATOM 174 N ASP A 22 -11.873 15.969 35.665 1.00 17.72 N ANISOU 174 N ASP A 22 2602 1678 2453 12 14 95 N ATOM 175 CA ASP A 22 -11.412 15.550 34.365 1.00 17.20 C ANISOU 175 CA ASP A 22 2571 1515 2448 56 -15 40 C ATOM 176 C ASP A 22 -11.410 14.031 34.263 1.00 15.90 C ANISOU 176 C ASP A 22 2580 1256 2203 222 114 -9 C ATOM 177 O ASP A 22 -11.080 13.549 33.198 1.00 17.92 O ANISOU 177 O ASP A 22 3222 1154 2433 250 151 222 O ATOM 178 CB ASP A 22 -10.008 16.099 34.010 1.00 17.37 C ANISOU 178 CB ASP A 22 2693 1252 2652 -12 -35 107 C ATOM 179 CG ASP A 22 -8.954 15.802 35.043 1.00 19.17 C ANISOU 179 CG ASP A 22 2628 1927 2727 -166 -87 7 C ATOM 180 OD1 ASP A 22 -7.895 15.141 34.752 1.00 23.18 O ANISOU 180 OD1 ASP A 22 3291 2053 3462 -110 -30 88 O ATOM 181 OD2 ASP A 22 -9.133 16.179 36.184 1.00 24.07 O ANISOU 181 OD2 ASP A 22 3148 3054 2943 222 -341 -49 O ATOM 182 N TYR A 23 -11.815 13.329 35.337 1.00 13.69 N ANISOU 182 N TYR A 23 2299 747 2154 -22 59 -94 N ATOM 183 CA TYR A 23 -11.875 11.852 35.324 1.00 12.77 C ANISOU 183 CA TYR A 23 1915 962 1973 22 -36 -98 C ATOM 184 C TYR A 23 -13.283 11.286 35.126 1.00 13.81 C ANISOU 184 C TYR A 23 1923 1211 2112 63 35 -44 C ATOM 185 O TYR A 23 -14.252 11.720 35.761 1.00 15.22 O ANISOU 185 O TYR A 23 2392 958 2430 28 92 -257 O ATOM 186 CB TYR A 23 -11.273 11.273 36.610 1.00 13.57 C ANISOU 186 CB TYR A 23 2135 982 2036 -20 -53 72 C ATOM 187 CG TYR A 23 -9.793 11.323 36.613 1.00 12.69 C ANISOU 187 CG TYR A 23 2029 912 1878 19 -8 -60 C ATOM 188 CD1 TYR A 23 -9.078 12.392 37.176 1.00 14.61 C ANISOU 188 CD1 TYR A 23 2123 1089 2339 27 -286 97 C ATOM 189 CD2 TYR A 23 -9.052 10.326 35.932 1.00 12.83 C ANISOU 189 CD2 TYR A 23 1916 895 2061 81 -38 -18 C ATOM 190 CE1 TYR A 23 -7.690 12.446 37.086 1.00 14.00 C ANISOU 190 CE1 TYR A 23 2141 1096 2080 -43 -79 -56 C ATOM 191 CE2 TYR A 23 -7.666 10.376 35.859 1.00 13.30 C ANISOU 191 CE2 TYR A 23 1925 1131 1995 107 -14 76 C ATOM 192 CZ TYR A 23 -6.977 11.447 36.439 1.00 13.79 C ANISOU 192 CZ TYR A 23 1994 1381 1863 39 45 -18 C ATOM 193 OH TYR A 23 -5.620 11.527 36.387 1.00 16.32 O ANISOU 193 OH TYR A 23 2228 1455 2517 83 -192 -280 O ATOM 194 N ILE A 24 -13.340 10.264 34.244 1.00 12.58 N ANISOU 194 N ILE A 24 1859 1006 1912 -103 13 -11 N ATOM 195 CA ILE A 24 -14.555 9.543 33.921 1.00 13.25 C ANISOU 195 CA ILE A 24 1839 1212 1981 66 -41 -31 C ATOM 196 C ILE A 24 -14.227 8.039 33.931 1.00 12.08 C ANISOU 196 C ILE A 24 1749 996 1844 11 74 177 C ATOM 197 O ILE A 24 -13.135 7.632 33.545 1.00 12.61 O ANISOU 197 O ILE A 24 2050 848 1892 -63 143 118 O ATOM 198 CB ILE A 24 -15.220 9.949 32.630 1.00 14.53 C ANISOU 198 CB ILE A 24 1972 1419 2130 -5 -61 -3 C ATOM 199 CG1 ILE A 24 -14.272 9.906 31.454 1.00 14.83 C ANISOU 199 CG1 ILE A 24 2262 1195 2177 98 -48 -139 C ATOM 200 CG2 ILE A 24 -15.848 11.346 32.792 1.00 15.79 C ANISOU 200 CG2 ILE A 24 2120 1540 2338 0 -194 -14 C ATOM 201 CD1 ILE A 24 -14.906 10.245 30.081 1.00 16.78 C ANISOU 201 CD1 ILE A 24 2670 1449 2256 -119 -149 -92 C ATOM 202 N THR A 25 -15.178 7.238 34.363 1.00 11.88 N ANISOU 202 N THR A 25 1723 919 1871 17 45 -135 N ATOM 203 CA THR A 25 -14.964 5.798 34.318 1.00 12.13 C ANISOU 203 CA THR A 25 1809 947 1852 21 -30 67 C ATOM 204 C THR A 25 -15.039 5.273 32.891 1.00 11.92 C ANISOU 204 C THR A 25 1885 858 1783 14 -84 51 C ATOM 205 O THR A 25 -15.523 5.932 31.973 1.00 12.11 O ANISOU 205 O THR A 25 2193 812 1593 -217 -119 -83 O ATOM 206 CB THR A 25 -15.971 5.064 35.187 1.00 12.78 C ANISOU 206 CB THR A 25 1831 1059 1966 58 -16 56 C ATOM 207 OG1 THR A 25 -17.313 5.309 34.707 1.00 13.50 O ANISOU 207 OG1 THR A 25 1747 1023 2359 -34 -112 -24 O ATOM 208 CG2 THR A 25 -15.853 5.459 36.638 1.00 14.15 C ANISOU 208 CG2 THR A 25 2162 1017 2195 -89 125 160 C ATOM 209 N LYS A 26 -14.648 3.997 32.705 1.00 12.52 N ANISOU 209 N LYS A 26 2115 872 1770 85 -128 45 N ATOM 210 CA LYS A 26 -14.685 3.404 31.386 1.00 13.20 C ANISOU 210 CA LYS A 26 2097 1088 1828 140 -8 66 C ATOM 211 C LYS A 26 -16.098 3.380 30.784 1.00 12.61 C ANISOU 211 C LYS A 26 2066 943 1781 112 35 -80 C ATOM 212 O LYS A 26 -16.267 3.661 29.608 1.00 13.93 O ANISOU 212 O LYS A 26 2449 915 1928 225 -176 -61 O ATOM 213 CB LYS A 26 -14.126 1.976 31.436 1.00 13.68 C ANISOU 213 CB LYS A 26 2172 1005 2020 170 -102 32 C ATOM 214 CG LYS A 26 -12.644 1.923 31.629 1.00 16.94 C ANISOU 214 CG LYS A 26 2206 1601 2627 67 -20 99 C ATOM 215 CD LYS A 26 -12.086 0.475 31.681 1.00 22.98 C ANISOU 215 CD LYS A 26 3126 2299 3305 285 -45 -71 C ATOM 216 CE LYS A 26 -12.400 -0.184 32.951 1.00 28.34 C ANISOU 216 CE LYS A 26 3733 3334 3701 114 69 42 C ATOM 217 NZ LYS A 26 -11.905 -1.644 32.910 1.00 36.25 N ANISOU 217 NZ LYS A 26 4890 3999 4883 368 -59 -40 N ATOM 218 N SER A 27 -17.118 3.051 31.549 1.00 12.24 N ANISOU 218 N SER A 27 1941 872 1836 145 -9 -16 N ATOM 219 CA SER A 27 -18.469 2.993 31.028 1.00 13.77 C ANISOU 219 CA SER A 27 2014 1284 1931 76 -73 -38 C ATOM 220 C SER A 27 -18.983 4.390 30.684 1.00 12.81 C ANISOU 220 C SER A 27 1873 1120 1872 -37 -165 45 C ATOM 221 O SER A 27 -19.692 4.535 29.719 1.00 14.27 O ANISOU 221 O SER A 27 2260 1036 2125 41 -230 55 O ATOM 222 CB SER A 27 -19.428 2.330 31.970 1.00 14.52 C ANISOU 222 CB SER A 27 2008 1418 2088 -66 -60 -56 C ATOM 223 OG SER A 27 -19.622 3.042 33.154 1.00 15.17 O ANISOU 223 OG SER A 27 2279 1407 2076 327 -128 -125 O ATOM 224 N GLN A 28 -18.559 5.398 31.450 1.00 12.84 N ANISOU 224 N GLN A 28 1989 1120 1769 15 -199 67 N ATOM 225 CA GLN A 28 -18.953 6.788 31.141 1.00 13.17 C ANISOU 225 CA GLN A 28 1862 1325 1816 7 -82 78 C ATOM 226 C GLN A 28 -18.285 7.223 29.839 1.00 13.62 C ANISOU 226 C GLN A 28 1976 1329 1867 51 -46 -30 C ATOM 227 O GLN A 28 -18.936 7.805 28.988 1.00 14.71 O ANISOU 227 O GLN A 28 2162 1439 1987 181 -90 90 O ATOM 228 CB AGLN A 28 -18.607 7.700 32.312 0.50 12.63 C ANISOU 228 CB AGLN A 28 1828 1183 1787 42 -13 -18 C ATOM 229 CG AGLN A 28 -18.976 9.211 32.129 0.50 11.91 C ANISOU 229 CG AGLN A 28 1836 968 1719 -34 -39 45 C ATOM 230 CD AGLN A 28 -20.457 9.503 32.235 0.50 13.05 C ANISOU 230 CD AGLN A 28 1872 1161 1923 -69 59 -13 C ATOM 231 OE1AGLN A 28 -21.269 8.621 32.470 0.50 13.64 O ANISOU 231 OE1AGLN A 28 2103 836 2241 170 256 -51 O ATOM 232 NE2AGLN A 28 -20.822 10.751 32.043 0.50 15.30 N ANISOU 232 NE2AGLN A 28 2184 1153 2473 229 26 -154 N ATOM 233 CB BGLN A 28 -18.537 7.695 32.293 0.50 13.17 C ANISOU 233 CB BGLN A 28 1874 1297 1830 37 -14 -41 C ATOM 234 CG BGLN A 28 -18.953 9.167 32.132 0.50 13.64 C ANISOU 234 CG BGLN A 28 2047 1253 1880 -17 -45 47 C ATOM 235 CD BGLN A 28 -20.415 9.267 32.054 0.50 16.24 C ANISOU 235 CD BGLN A 28 2158 1651 2360 58 108 -64 C ATOM 236 OE1BGLN A 28 -21.079 8.925 33.022 0.50 17.88 O ANISOU 236 OE1BGLN A 28 2630 1770 2391 89 151 -12 O ATOM 237 NE2BGLN A 28 -20.948 9.623 30.883 0.50 20.39 N ANISOU 237 NE2BGLN A 28 2569 2561 2616 -4 -31 -17 N ATOM 238 N ALA A 29 -16.995 6.936 29.685 1.00 12.72 N ANISOU 238 N ALA A 29 1926 1046 1862 31 3 80 N ATOM 239 CA ALA A 29 -16.293 7.203 28.441 1.00 14.38 C ANISOU 239 CA ALA A 29 2082 1493 1887 -7 9 23 C ATOM 240 C ALA A 29 -16.969 6.523 27.227 1.00 15.06 C ANISOU 240 C ALA A 29 2164 1627 1931 14 18 54 C ATOM 241 O ALA A 29 -17.162 7.103 26.163 1.00 14.97 O ANISOU 241 O ALA A 29 2372 1401 1912 103 41 65 O ATOM 242 CB ALA A 29 -14.857 6.797 28.582 1.00 14.71 C ANISOU 242 CB ALA A 29 2111 1451 2026 -38 102 7 C ATOM 243 N SER A 30 -17.377 5.275 27.409 1.00 14.96 N ANISOU 243 N SER A 30 2146 1555 1982 -7 -113 23 N ATOM 244 CA SER A 30 -18.062 4.550 26.352 1.00 16.26 C ANISOU 244 CA SER A 30 2239 1842 2095 -26 -112 28 C ATOM 245 C SER A 30 -19.369 5.254 25.944 1.00 15.96 C ANISOU 245 C SER A 30 2162 1774 2125 -14 -46 -15 C ATOM 246 O SER A 30 -19.695 5.316 24.758 1.00 17.10 O ANISOU 246 O SER A 30 2453 1731 2313 101 -55 60 O ATOM 247 CB SER A 30 -18.366 3.152 26.816 1.00 15.93 C ANISOU 247 CB SER A 30 2208 1756 2086 58 -1 -97 C ATOM 248 OG ASER A 30 -18.804 2.352 25.748 0.64 17.86 O ANISOU 248 OG ASER A 30 2837 1827 2121 -38 -275 21 O ATOM 249 OG BSER A 30 -17.176 2.384 26.736 0.36 14.60 O ANISOU 249 OG BSER A 30 2209 1123 2215 -86 -122 -33 O ATOM 250 N ALA A 31 -20.114 5.755 26.940 1.00 15.89 N ANISOU 250 N ALA A 31 2027 1935 2076 -48 -48 52 N ATOM 251 CA ALA A 31 -21.368 6.473 26.691 1.00 17.12 C ANISOU 251 CA ALA A 31 2220 1989 2294 -2 -60 73 C ATOM 252 C ALA A 31 -21.149 7.692 25.826 1.00 17.70 C ANISOU 252 C ALA A 31 2303 2096 2323 81 -73 201 C ATOM 253 O ALA A 31 -22.070 8.038 25.064 1.00 19.51 O ANISOU 253 O ALA A 31 2493 2065 2854 135 -229 331 O ATOM 254 CB ALA A 31 -22.056 6.867 27.955 1.00 17.36 C ANISOU 254 CB ALA A 31 2248 1968 2380 37 69 196 C ATOM 255 N LEU A 32 -19.974 8.309 25.936 1.00 18.24 N ANISOU 255 N LEU A 32 2330 2142 2457 135 -55 173 N ATOM 256 CA LEU A 32 -19.584 9.463 25.147 1.00 20.30 C ANISOU 256 CA LEU A 32 2609 2432 2669 99 3 191 C ATOM 257 C LEU A 32 -18.985 9.154 23.797 1.00 20.31 C ANISOU 257 C LEU A 32 2729 2358 2627 55 -12 175 C ATOM 258 O LEU A 32 -18.714 10.073 23.045 1.00 22.45 O ANISOU 258 O LEU A 32 3201 2404 2925 38 -20 535 O ATOM 259 CB LEU A 32 -18.654 10.414 25.944 1.00 20.52 C ANISOU 259 CB LEU A 32 2659 2333 2803 53 -7 181 C ATOM 260 CG LEU A 32 -19.118 10.932 27.288 1.00 23.27 C ANISOU 260 CG LEU A 32 3114 2724 3001 -55 3 204 C ATOM 261 CD1 LEU A 32 -18.016 11.555 28.100 1.00 27.75 C ANISOU 261 CD1 LEU A 32 3613 3378 3552 -101 -32 -66 C ATOM 262 CD2 LEU A 32 -20.273 11.868 27.105 1.00 26.80 C ANISOU 262 CD2 LEU A 32 3316 3413 3452 74 161 25 C ATOM 263 N GLY A 33 -18.758 7.891 23.483 1.00 19.21 N ANISOU 263 N GLY A 33 2552 2263 2481 124 19 88 N ATOM 264 CA GLY A 33 -18.287 7.455 22.195 1.00 19.36 C ANISOU 264 CA GLY A 33 2639 2303 2414 126 -7 118 C ATOM 265 C GLY A 33 -16.902 6.857 22.171 1.00 18.98 C ANISOU 265 C GLY A 33 2471 2375 2363 28 -13 -21 C ATOM 266 O GLY A 33 -16.382 6.597 21.080 1.00 20.19 O ANISOU 266 O GLY A 33 2669 2568 2433 261 91 -21 O ATOM 267 N TRP A 34 -16.294 6.633 23.329 1.00 17.89 N ANISOU 267 N TRP A 34 2457 2082 2258 184 37 60 N ATOM 268 CA TRP A 34 -14.959 6.036 23.391 1.00 17.95 C ANISOU 268 CA TRP A 34 2327 2148 2344 11 6 33 C ATOM 269 C TRP A 34 -15.027 4.569 22.946 1.00 19.18 C ANISOU 269 C TRP A 34 2468 2279 2539 -4 -89 -32 C ATOM 270 O TRP A 34 -15.890 3.832 23.409 1.00 20.86 O ANISOU 270 O TRP A 34 2641 2371 2914 -85 -80 -3 O ATOM 271 CB TRP A 34 -14.420 6.052 24.821 1.00 17.28 C ANISOU 271 CB TRP A 34 2349 2016 2197 41 -38 16 C ATOM 272 CG TRP A 34 -13.088 5.407 24.998 1.00 17.10 C ANISOU 272 CG TRP A 34 2336 1924 2238 -31 -37 69 C ATOM 273 CD1 TRP A 34 -11.944 5.679 24.329 1.00 18.39 C ANISOU 273 CD1 TRP A 34 2487 2155 2345 114 -13 45 C ATOM 274 CD2 TRP A 34 -12.769 4.348 25.909 1.00 17.31 C ANISOU 274 CD2 TRP A 34 2363 2023 2188 70 -137 -56 C ATOM 275 NE1 TRP A 34 -10.914 4.907 24.789 1.00 18.74 N ANISOU 275 NE1 TRP A 34 2369 2380 2370 234 -16 -97 N ATOM 276 CE2 TRP A 34 -11.401 4.041 25.723 1.00 18.89 C ANISOU 276 CE2 TRP A 34 2597 2223 2356 141 -138 -29 C ATOM 277 CE3 TRP A 34 -13.505 3.619 26.825 1.00 19.71 C ANISOU 277 CE3 TRP A 34 2678 2429 2379 144 51 -3 C ATOM 278 CZ2 TRP A 34 -10.743 3.034 26.465 1.00 20.03 C ANISOU 278 CZ2 TRP A 34 2674 2435 2500 345 -75 19 C ATOM 279 CZ3 TRP A 34 -12.862 2.610 27.563 1.00 20.49 C ANISOU 279 CZ3 TRP A 34 2809 2475 2502 143 -30 134 C ATOM 280 CH2 TRP A 34 -11.499 2.346 27.365 1.00 21.07 C ANISOU 280 CH2 TRP A 34 2801 2566 2639 189 -124 196 C ATOM 281 N VAL A 35 -14.105 4.197 22.070 1.00 21.09 N ANISOU 281 N VAL A 35 2701 2505 2806 26 -24 -45 N ATOM 282 CA VAL A 35 -13.903 2.797 21.654 1.00 23.38 C ANISOU 282 CA VAL A 35 3026 2831 3024 67 -26 -144 C ATOM 283 C VAL A 35 -12.418 2.536 21.813 1.00 23.45 C ANISOU 283 C VAL A 35 3050 2827 3034 65 -17 -128 C ATOM 284 O VAL A 35 -11.616 3.174 21.121 1.00 24.27 O ANISOU 284 O VAL A 35 3049 2962 3208 132 61 -197 O ATOM 285 CB VAL A 35 -14.305 2.619 20.170 1.00 25.27 C ANISOU 285 CB VAL A 35 3258 3103 3239 79 -93 -171 C ATOM 286 CG1 VAL A 35 -13.992 1.144 19.702 1.00 27.75 C ANISOU 286 CG1 VAL A 35 3601 3335 3607 158 -59 -224 C ATOM 287 CG2 VAL A 35 -15.776 2.988 19.949 1.00 26.97 C ANISOU 287 CG2 VAL A 35 3402 3388 3457 84 -117 -276 C ATOM 288 N ALA A 36 -12.041 1.612 22.697 1.00 24.51 N ANISOU 288 N ALA A 36 3164 2986 3161 19 20 -128 N ATOM 289 CA ALA A 36 -10.611 1.404 23.006 1.00 24.46 C ANISOU 289 CA ALA A 36 3159 2991 3145 62 -62 -69 C ATOM 290 C ALA A 36 -9.757 1.111 21.773 1.00 24.41 C ANISOU 290 C ALA A 36 3080 2867 3327 163 -49 -69 C ATOM 291 O ALA A 36 -8.666 1.647 21.650 1.00 24.16 O ANISOU 291 O ALA A 36 3162 2558 3457 292 -20 -206 O ATOM 292 CB ALA A 36 -10.432 0.348 24.032 1.00 25.91 C ANISOU 292 CB ALA A 36 3352 3188 3303 -6 -38 -50 C ATOM 293 N SER A 37 -10.310 0.368 20.809 1.00 25.14 N ANISOU 293 N SER A 37 3211 3011 3330 143 -112 -98 N ATOM 294 CA SER A 37 -9.560 -0.024 19.590 1.00 26.34 C ANISOU 294 CA SER A 37 3270 3323 3413 69 -72 -107 C ATOM 295 C SER A 37 -9.245 1.140 18.673 1.00 26.43 C ANISOU 295 C SER A 37 3309 3360 3371 83 -31 -115 C ATOM 296 O SER A 37 -8.317 1.081 17.885 1.00 27.58 O ANISOU 296 O SER A 37 3433 3589 3455 213 -10 -402 O ATOM 297 CB SER A 37 -10.294 -1.110 18.805 1.00 27.07 C ANISOU 297 CB SER A 37 3466 3322 3494 83 -70 -183 C ATOM 298 OG SER A 37 -11.499 -0.609 18.286 1.00 30.66 O ANISOU 298 OG SER A 37 3788 3843 4019 134 -183 -286 O ATOM 299 N LYS A 38 -10.020 2.224 18.792 1.00 26.05 N ANISOU 299 N LYS A 38 3285 3241 3370 119 -49 -129 N ATOM 300 CA LYS A 38 -9.803 3.434 18.002 1.00 25.54 C ANISOU 300 CA LYS A 38 3245 3240 3217 59 23 -48 C ATOM 301 C LYS A 38 -8.849 4.435 18.686 1.00 23.94 C ANISOU 301 C LYS A 38 3098 3004 2993 108 51 -16 C ATOM 302 O LYS A 38 -8.377 5.378 18.046 1.00 24.67 O ANISOU 302 O LYS A 38 3395 3020 2956 74 4 86 O ATOM 303 CB LYS A 38 -11.160 4.099 17.713 1.00 27.32 C ANISOU 303 CB LYS A 38 3463 3452 3463 124 -40 -25 C ATOM 304 CG LYS A 38 -12.172 3.169 17.006 1.00 31.51 C ANISOU 304 CG LYS A 38 4028 3901 4042 -93 -29 -79 C ATOM 305 CD LYS A 38 -13.310 3.902 16.255 1.00 38.60 C ANISOU 305 CD LYS A 38 4832 4908 4924 124 -120 60 C ATOM 306 CE LYS A 38 -14.025 5.003 17.087 1.00 42.77 C ANISOU 306 CE LYS A 38 5388 5424 5436 91 50 -97 C ATOM 307 NZ LYS A 38 -15.310 5.541 16.427 1.00 46.07 N ANISOU 307 NZ LYS A 38 5759 5985 5757 111 -142 103 N ATOM 308 N GLY A 39 -8.569 4.288 19.973 1.00 21.63 N ANISOU 308 N GLY A 39 2802 2630 2784 186 -15 -13 N ATOM 309 CA GLY A 39 -7.716 5.244 20.695 1.00 20.02 C ANISOU 309 CA GLY A 39 2588 2388 2628 152 92 30 C ATOM 310 C GLY A 39 -8.241 6.667 20.651 1.00 19.26 C ANISOU 310 C GLY A 39 2527 2349 2441 98 54 7 C ATOM 311 O GLY A 39 -7.455 7.610 20.519 1.00 19.07 O ANISOU 311 O GLY A 39 2703 2099 2444 325 88 0 O ATOM 312 N ASP A 40 -9.556 6.800 20.741 1.00 18.95 N ANISOU 312 N ASP A 40 2585 2176 2437 143 65 60 N ATOM 313 CA ASP A 40 -10.221 8.083 20.442 1.00 18.07 C ANISOU 313 CA ASP A 40 2466 2086 2314 150 42 60 C ATOM 314 C ASP A 40 -10.686 8.903 21.642 1.00 17.73 C ANISOU 314 C ASP A 40 2461 2145 2128 161 -16 62 C ATOM 315 O ASP A 40 -11.475 9.841 21.467 1.00 17.86 O ANISOU 315 O ASP A 40 2728 1948 2110 245 -126 121 O ATOM 316 CB ASP A 40 -11.371 7.874 19.437 1.00 17.93 C ANISOU 316 CB ASP A 40 2591 1888 2332 111 23 -41 C ATOM 317 CG ASP A 40 -12.557 7.157 20.010 1.00 19.98 C ANISOU 317 CG ASP A 40 2633 2358 2599 -20 0 -12 C ATOM 318 OD1 ASP A 40 -12.412 6.496 21.090 1.00 21.56 O ANISOU 318 OD1 ASP A 40 3048 2436 2706 190 -98 -26 O ATOM 319 OD2 ASP A 40 -13.702 7.207 19.438 1.00 24.74 O ANISOU 319 OD2 ASP A 40 3138 3024 3237 262 -203 11 O ATOM 320 N LEU A 41 -10.189 8.625 22.845 1.00 16.24 N ANISOU 320 N LEU A 41 2292 1900 1975 322 6 123 N ATOM 321 CA LEU A 41 -10.756 9.286 24.032 1.00 17.10 C ANISOU 321 CA LEU A 41 2436 1951 2109 113 -66 30 C ATOM 322 C LEU A 41 -10.654 10.828 23.967 1.00 16.91 C ANISOU 322 C LEU A 41 2451 1855 2116 123 6 51 C ATOM 323 O LEU A 41 -11.626 11.515 24.281 1.00 18.80 O ANISOU 323 O LEU A 41 2675 2000 2465 190 62 200 O ATOM 324 CB LEU A 41 -10.066 8.814 25.301 1.00 16.88 C ANISOU 324 CB LEU A 41 2520 1836 2056 118 -80 193 C ATOM 325 CG LEU A 41 -10.624 9.357 26.611 1.00 19.05 C ANISOU 325 CG LEU A 41 2668 2142 2427 51 -61 47 C ATOM 326 CD1 LEU A 41 -12.046 8.995 26.786 1.00 21.80 C ANISOU 326 CD1 LEU A 41 2844 2863 2575 58 96 38 C ATOM 327 CD2 LEU A 41 -9.760 8.833 27.776 1.00 20.32 C ANISOU 327 CD2 LEU A 41 2924 2387 2410 -5 -101 85 C ATOM 328 N ALA A 42 -9.505 11.314 23.554 1.00 17.60 N ANISOU 328 N ALA A 42 2446 1908 2330 152 -43 -17 N ATOM 329 CA ALA A 42 -9.254 12.769 23.493 1.00 18.82 C ANISOU 329 CA ALA A 42 2556 2109 2484 71 -25 56 C ATOM 330 C ALA A 42 -10.114 13.467 22.447 1.00 19.37 C ANISOU 330 C ALA A 42 2680 2077 2601 145 -85 96 C ATOM 331 O ALA A 42 -10.446 14.634 22.621 1.00 20.98 O ANISOU 331 O ALA A 42 3257 1818 2897 343 -1 171 O ATOM 332 CB ALA A 42 -7.832 13.084 23.293 1.00 20.09 C ANISOU 332 CB ALA A 42 2578 2344 2709 118 -135 103 C ATOM 333 N GLU A 43 -10.526 12.756 21.421 1.00 18.65 N ANISOU 333 N GLU A 43 2617 2014 2453 264 -85 184 N ATOM 334 CA GLU A 43 -11.422 13.320 20.383 1.00 20.15 C ANISOU 334 CA GLU A 43 2653 2388 2616 151 -79 237 C ATOM 335 C GLU A 43 -12.878 13.350 20.783 1.00 20.65 C ANISOU 335 C GLU A 43 2717 2393 2734 226 -21 241 C ATOM 336 O GLU A 43 -13.591 14.332 20.482 1.00 23.17 O ANISOU 336 O GLU A 43 3154 2430 3217 373 -86 532 O ATOM 337 CB GLU A 43 -11.218 12.615 19.044 1.00 20.38 C ANISOU 337 CB GLU A 43 2654 2459 2628 172 -120 221 C ATOM 338 CG GLU A 43 -9.902 12.969 18.352 1.00 22.34 C ANISOU 338 CG GLU A 43 2823 2713 2950 84 19 134 C ATOM 339 CD GLU A 43 -8.708 12.286 19.001 1.00 22.37 C ANISOU 339 CD GLU A 43 2877 2800 2820 17 62 94 C ATOM 340 OE1 GLU A 43 -8.698 11.043 19.035 1.00 23.20 O ANISOU 340 OE1 GLU A 43 2925 2661 3225 201 69 384 O ATOM 341 OE2 GLU A 43 -7.809 12.953 19.512 1.00 24.84 O ANISOU 341 OE2 GLU A 43 3114 3331 2993 -68 -116 246 O ATOM 342 N VAL A 44 -13.364 12.341 21.504 1.00 19.28 N ANISOU 342 N VAL A 44 2566 2172 2587 197 5 254 N ATOM 343 CA VAL A 44 -14.758 12.307 21.957 1.00 19.97 C ANISOU 343 CA VAL A 44 2593 2325 2668 119 -14 134 C ATOM 344 C VAL A 44 -15.000 12.968 23.289 1.00 20.23 C ANISOU 344 C VAL A 44 2556 2460 2671 134 40 178 C ATOM 345 O VAL A 44 -16.164 13.323 23.559 1.00 22.12 O ANISOU 345 O VAL A 44 2662 2768 2971 381 101 -42 O ATOM 346 CB VAL A 44 -15.345 10.899 21.985 1.00 21.56 C ANISOU 346 CB VAL A 44 2716 2612 2863 -3 0 64 C ATOM 347 CG1 VAL A 44 -15.267 10.272 20.605 1.00 24.61 C ANISOU 347 CG1 VAL A 44 3262 3021 3066 -53 69 1 C ATOM 348 CG2 VAL A 44 -14.686 10.016 23.033 1.00 23.04 C ANISOU 348 CG2 VAL A 44 3011 2627 3116 61 -34 117 C ATOM 349 N ALA A 45 -13.967 13.092 24.126 1.00 19.38 N ANISOU 349 N ALA A 45 2581 2295 2485 126 96 135 N ATOM 350 CA ALA A 45 -14.057 13.681 25.465 1.00 19.64 C ANISOU 350 CA ALA A 45 2676 2227 2556 125 -16 135 C ATOM 351 C ALA A 45 -12.807 14.474 25.732 1.00 19.40 C ANISOU 351 C ALA A 45 2752 2068 2549 104 -3 204 C ATOM 352 O ALA A 45 -11.957 14.158 26.541 1.00 18.00 O ANISOU 352 O ALA A 45 2941 1426 2471 340 27 391 O ATOM 353 CB ALA A 45 -14.307 12.614 26.526 1.00 21.18 C ANISOU 353 CB ALA A 45 2778 2621 2645 -34 74 153 C ATOM 354 N PRO A 46 -12.681 15.612 25.052 1.00 20.14 N ANISOU 354 N PRO A 46 2924 2042 2686 115 -70 296 N ATOM 355 CA PRO A 46 -11.480 16.407 25.210 1.00 19.67 C ANISOU 355 CA PRO A 46 2860 1906 2706 119 -46 302 C ATOM 356 C PRO A 46 -11.153 16.784 26.630 1.00 18.44 C ANISOU 356 C PRO A 46 2774 1584 2646 -21 47 389 C ATOM 357 O PRO A 46 -12.064 17.133 27.386 1.00 20.89 O ANISOU 357 O PRO A 46 3405 1609 2923 224 16 232 O ATOM 358 CB PRO A 46 -11.781 17.697 24.363 1.00 20.24 C ANISOU 358 CB PRO A 46 3024 1969 2696 78 -84 421 C ATOM 359 CG PRO A 46 -13.017 17.431 23.669 1.00 22.10 C ANISOU 359 CG PRO A 46 3031 2288 3078 1 -105 309 C ATOM 360 CD PRO A 46 -13.605 16.137 24.032 1.00 22.24 C ANISOU 360 CD PRO A 46 3035 2416 2997 -10 -122 248 C ATOM 361 N GLY A 47 -9.896 16.628 27.015 1.00 18.58 N ANISOU 361 N GLY A 47 2894 1548 2617 -85 -51 224 N ATOM 362 CA GLY A 47 -9.470 16.954 28.357 1.00 19.29 C ANISOU 362 CA GLY A 47 2861 1933 2533 -79 -56 207 C ATOM 363 C GLY A 47 -9.776 15.919 29.443 1.00 19.00 C ANISOU 363 C GLY A 47 2798 2042 2376 -82 -82 232 C ATOM 364 O GLY A 47 -9.464 16.153 30.605 1.00 19.39 O ANISOU 364 O GLY A 47 3271 1542 2553 -137 -144 379 O ATOM 365 N LYS A 48 -10.440 14.846 29.075 1.00 17.13 N ANISOU 365 N LYS A 48 2649 1682 2174 23 -61 295 N ATOM 366 CA LYS A 48 -10.781 13.798 30.060 1.00 16.93 C ANISOU 366 CA LYS A 48 2476 1757 2198 31 21 225 C ATOM 367 C LYS A 48 -9.786 12.656 30.048 1.00 16.77 C ANISOU 367 C LYS A 48 2385 1892 2093 49 73 194 C ATOM 368 O LYS A 48 -9.082 12.417 29.095 1.00 17.63 O ANISOU 368 O LYS A 48 2920 1500 2276 197 24 329 O ATOM 369 CB LYS A 48 -12.152 13.249 29.744 1.00 17.95 C ANISOU 369 CB LYS A 48 2417 2050 2352 47 83 240 C ATOM 370 CG LYS A 48 -13.293 14.250 29.800 1.00 22.44 C ANISOU 370 CG LYS A 48 2909 2660 2956 204 46 286 C ATOM 371 CD LYS A 48 -13.435 14.881 31.165 1.00 26.98 C ANISOU 371 CD LYS A 48 3656 3221 3371 86 -42 -9 C ATOM 372 CE LYS A 48 -14.802 15.498 31.369 1.00 30.62 C ANISOU 372 CE LYS A 48 3832 3872 3928 23 -14 47 C ATOM 373 NZ LYS A 48 -14.934 16.639 30.495 1.00 33.91 N ANISOU 373 NZ LYS A 48 4617 4117 4148 216 61 69 N ATOM 374 N SER A 49 -9.724 11.985 31.200 1.00 14.94 N ANISOU 374 N SER A 49 2294 1275 2105 62 -21 201 N ATOM 375 CA SER A 49 -8.920 10.751 31.375 1.00 14.79 C ANISOU 375 CA SER A 49 2015 1526 2077 -20 24 249 C ATOM 376 C SER A 49 -9.792 9.715 32.027 1.00 14.08 C ANISOU 376 C SER A 49 2003 1343 2003 -91 60 -8 C ATOM 377 O SER A 49 -10.748 10.049 32.722 1.00 13.73 O ANISOU 377 O SER A 49 2044 880 2290 -20 58 91 O ATOM 378 CB SER A 49 -7.706 11.000 32.295 1.00 13.82 C ANISOU 378 CB SER A 49 1943 1276 2030 -143 32 265 C ATOM 379 OG SER A 49 -6.747 11.876 31.741 1.00 16.84 O ANISOU 379 OG SER A 49 2307 1512 2578 -414 1 510 O ATOM 380 N ILE A 50 -9.441 8.445 31.778 1.00 12.93 N ANISOU 380 N ILE A 50 2017 1059 1837 30 -3 321 N ATOM 381 CA ILE A 50 -10.131 7.335 32.444 1.00 13.20 C ANISOU 381 CA ILE A 50 1821 1295 1898 -34 79 44 C ATOM 382 C ILE A 50 -9.691 7.231 33.869 1.00 11.74 C ANISOU 382 C ILE A 50 1725 825 1909 22 64 47 C ATOM 383 O ILE A 50 -8.494 7.207 34.138 1.00 13.70 O ANISOU 383 O ILE A 50 1854 1185 2164 41 50 28 O ATOM 384 CB ILE A 50 -9.834 6.023 31.703 1.00 14.13 C ANISOU 384 CB ILE A 50 2125 1304 1939 -128 88 12 C ATOM 385 CG1 ILE A 50 -10.287 6.073 30.268 1.00 19.45 C ANISOU 385 CG1 ILE A 50 2822 1967 2598 -139 -78 170 C ATOM 386 CG2 ILE A 50 -10.454 4.833 32.448 1.00 15.38 C ANISOU 386 CG2 ILE A 50 2339 1246 2256 -215 -68 115 C ATOM 387 CD1 ILE A 50 -11.704 6.220 30.066 1.00 21.65 C ANISOU 387 CD1 ILE A 50 2794 2565 2864 26 -74 28 C ATOM 388 N GLY A 51 -10.650 7.117 34.795 1.00 11.48 N ANISOU 388 N GLY A 51 1616 1028 1718 -87 6 55 N ATOM 389 CA GLY A 51 -10.325 6.879 36.186 1.00 11.86 C ANISOU 389 CA GLY A 51 1796 928 1782 -31 21 160 C ATOM 390 C GLY A 51 -11.576 6.720 37.032 1.00 12.55 C ANISOU 390 C GLY A 51 1792 1313 1662 51 -1 -21 C ATOM 391 O GLY A 51 -12.681 7.188 36.664 1.00 14.28 O ANISOU 391 O GLY A 51 2027 1460 1939 7 -71 183 O ATOM 392 N GLY A 52 -11.394 6.055 38.170 1.00 12.00 N ANISOU 392 N GLY A 52 1765 1028 1764 82 -62 156 N ATOM 393 CA GLY A 52 -12.426 5.833 39.146 1.00 13.23 C ANISOU 393 CA GLY A 52 1857 1300 1867 29 -14 -24 C ATOM 394 C GLY A 52 -12.965 4.412 39.212 1.00 13.30 C ANISOU 394 C GLY A 52 1979 1227 1847 -44 88 116 C ATOM 395 O GLY A 52 -13.782 4.139 40.101 1.00 14.37 O ANISOU 395 O GLY A 52 2288 1031 2137 -128 194 15 O ATOM 396 N ASP A 53 -12.615 3.579 38.237 1.00 13.36 N ANISOU 396 N ASP A 53 2050 1045 1978 -209 15 174 N ATOM 397 CA ASP A 53 -13.072 2.181 38.271 1.00 12.93 C ANISOU 397 CA ASP A 53 1934 1078 1901 -78 -122 108 C ATOM 398 C ASP A 53 -12.481 1.433 39.430 1.00 14.41 C ANISOU 398 C ASP A 53 1993 1370 2110 -217 -164 194 C ATOM 399 O ASP A 53 -11.365 1.693 39.851 1.00 14.29 O ANISOU 399 O ASP A 53 2126 1208 2095 -364 -279 231 O ATOM 400 CB ASP A 53 -12.748 1.503 36.963 1.00 13.48 C ANISOU 400 CB ASP A 53 1965 1171 1985 -119 -163 142 C ATOM 401 CG ASP A 53 -13.658 1.952 35.858 1.00 14.53 C ANISOU 401 CG ASP A 53 2150 1365 2005 63 -106 88 C ATOM 402 OD1 ASP A 53 -14.878 1.671 35.940 1.00 16.99 O ANISOU 402 OD1 ASP A 53 2555 1148 2750 -233 -255 277 O ATOM 403 OD2 ASP A 53 -13.238 2.630 34.921 1.00 15.39 O ANISOU 403 OD2 ASP A 53 2499 1239 2108 80 -136 178 O ATOM 404 N VAL A 54 -13.259 0.435 39.882 1.00 14.40 N ANISOU 404 N VAL A 54 2188 1115 2164 -141 -168 315 N ATOM 405 CA VAL A 54 -12.782 -0.487 40.906 1.00 16.44 C ANISOU 405 CA VAL A 54 2292 1682 2270 -178 -130 254 C ATOM 406 C VAL A 54 -11.570 -1.221 40.382 1.00 15.96 C ANISOU 406 C VAL A 54 2422 1374 2266 -280 -96 269 C ATOM 407 O VAL A 54 -11.544 -1.699 39.234 1.00 18.37 O ANISOU 407 O VAL A 54 2849 1725 2404 -119 -230 330 O ATOM 408 CB VAL A 54 -13.939 -1.433 41.291 1.00 17.66 C ANISOU 408 CB VAL A 54 2351 1878 2478 -156 -43 257 C ATOM 409 CG1 VAL A 54 -13.446 -2.503 42.238 1.00 21.61 C ANISOU 409 CG1 VAL A 54 2955 2350 2905 -148 -95 403 C ATOM 410 CG2 VAL A 54 -15.053 -0.672 41.966 1.00 19.84 C ANISOU 410 CG2 VAL A 54 2813 2067 2656 -117 68 244 C ATOM 411 N PHE A 55 -10.585 -1.388 41.255 1.00 17.33 N ANISOU 411 N PHE A 55 2423 1707 2453 -159 -114 161 N ATOM 412 CA PHE A 55 -9.375 -2.153 40.984 1.00 17.88 C ANISOU 412 CA PHE A 55 2500 1703 2589 -57 -70 220 C ATOM 413 C PHE A 55 -9.502 -3.364 41.916 1.00 20.27 C ANISOU 413 C PHE A 55 2951 2084 2665 -28 -118 197 C ATOM 414 O PHE A 55 -9.527 -3.250 43.139 1.00 19.77 O ANISOU 414 O PHE A 55 3310 1187 3015 139 -261 390 O ATOM 415 CB PHE A 55 -8.128 -1.339 41.310 1.00 19.28 C ANISOU 415 CB PHE A 55 2506 2027 2789 -29 -75 227 C ATOM 416 CG PHE A 55 -6.852 -2.072 41.046 1.00 19.09 C ANISOU 416 CG PHE A 55 2627 1781 2845 -160 46 7 C ATOM 417 CD1 PHE A 55 -6.288 -2.180 39.762 1.00 21.78 C ANISOU 417 CD1 PHE A 55 3053 1972 3248 -188 68 206 C ATOM 418 CD2 PHE A 55 -6.220 -2.687 42.122 1.00 21.04 C ANISOU 418 CD2 PHE A 55 2869 1867 3257 -49 -90 28 C ATOM 419 CE1 PHE A 55 -5.080 -2.890 39.582 1.00 24.90 C ANISOU 419 CE1 PHE A 55 3229 2814 3417 -119 53 140 C ATOM 420 CE2 PHE A 55 -5.018 -3.355 41.943 1.00 21.48 C ANISOU 420 CE2 PHE A 55 2772 2034 3352 -106 -3 146 C ATOM 421 CZ PHE A 55 -4.466 -3.486 40.701 1.00 23.12 C ANISOU 421 CZ PHE A 55 3098 2398 3287 -83 20 44 C ATOM 422 N SER A 56 -9.679 -4.509 41.283 1.00 22.20 N ANISOU 422 N SER A 56 3265 2143 3025 64 -178 139 N ATOM 423 CA SER A 56 -9.942 -5.708 42.082 1.00 24.42 C ANISOU 423 CA SER A 56 3351 2671 3255 -121 -106 117 C ATOM 424 CB SER A 56 -10.504 -6.861 41.255 1.00 25.89 C ANISOU 424 CB SER A 56 3537 2851 3446 -176 -141 -30 C ATOM 425 OG SER A 56 -9.489 -7.412 40.440 1.00 31.54 O ANISOU 425 OG SER A 56 4070 3788 4123 16 81 -6 O ATOM 426 C ASER A 56 -9.006 -6.199 43.181 0.50 23.24 C ANISOU 426 C ASER A 56 3170 2549 3109 -47 -100 26 C ATOM 427 O ASER A 56 -9.483 -6.653 44.240 0.50 21.31 O ANISOU 427 O ASER A 56 2890 2041 3166 25 -132 152 O ATOM 428 C BSER A 56 -8.423 -6.034 42.355 0.50 24.21 C ANISOU 428 C BSER A 56 3348 2547 3303 -45 -52 34 C ATOM 429 O BSER A 56 -7.569 -6.154 41.462 0.50 25.56 O ANISOU 429 O BSER A 56 3638 2521 3551 -97 -43 -56 O ATOM 430 CA ASN A 57 -6.708 -6.506 43.957 1.00 25.28 C ANISOU 430 CA ASN A 57 3446 2649 3507 -48 -90 113 C ATOM 431 C ASN A 57 -6.798 -8.025 44.255 1.00 28.28 C ANISOU 431 C ASN A 57 3899 2925 3919 -35 -71 146 C ATOM 432 O ASN A 57 -6.388 -8.431 45.316 1.00 26.61 O ANISOU 432 O ASN A 57 3930 2059 4122 -28 -21 238 O ATOM 433 CB ASN A 57 -6.552 -5.708 45.238 1.00 25.92 C ANISOU 433 CB ASN A 57 3530 2827 3491 -66 -33 130 C ATOM 434 CG ASN A 57 -5.200 -5.873 45.877 1.00 25.05 C ANISOU 434 CG ASN A 57 3436 2503 3578 -62 -91 62 C ATOM 435 OD1 ASN A 57 -4.186 -5.996 45.172 1.00 24.93 O ANISOU 435 OD1 ASN A 57 3712 1617 4141 106 -42 -25 O ATOM 436 ND2 ASN A 57 -5.169 -5.803 47.225 1.00 25.01 N ANISOU 436 ND2 ASN A 57 3901 1993 3609 -76 7 415 N ATOM 437 N AASN A 57 -7.713 -6.044 42.977 0.50 23.52 N ANISOU 437 N AASN A 57 3216 2508 3211 -84 -67 70 N ATOM 438 N BASN A 57 -8.074 -6.175 43.582 0.50 25.07 N ANISOU 438 N BASN A 57 3405 2681 3439 -9 -51 35 N ATOM 439 N ARG A 58 -7.358 -8.781 43.318 1.00 33.17 N ANISOU 439 N ARG A 58 4373 3757 4470 0 -119 -29 N ATOM 440 CA ARG A 58 -7.594 -10.222 43.538 1.00 36.93 C ANISOU 440 CA ARG A 58 4789 4326 4916 -12 -58 51 C ATOM 441 C ARG A 58 -6.311 -11.004 43.671 1.00 38.80 C ANISOU 441 C ARG A 58 4928 4693 5119 34 -37 11 C ATOM 442 O ARG A 58 -6.306 -12.028 44.370 1.00 39.64 O ANISOU 442 O ARG A 58 5067 4615 5376 99 -102 111 O ATOM 443 CB ARG A 58 -8.465 -10.789 42.419 1.00 38.77 C ANISOU 443 CB ARG A 58 5027 4602 5100 -28 -67 -40 C ATOM 444 CG ARG A 58 -9.881 -10.300 42.549 1.00 44.49 C ANISOU 444 CG ARG A 58 5475 5506 5921 46 -27 11 C ATOM 445 CD ARG A 58 -10.621 -10.787 43.827 1.00 50.05 C ANISOU 445 CD ARG A 58 6428 6305 6280 42 134 79 C ATOM 446 NE ARG A 58 -11.999 -11.113 43.447 1.00 54.59 N ANISOU 446 NE ARG A 58 6787 6955 6999 22 -69 -36 N ATOM 447 CZ ARG A 58 -12.765 -12.098 43.915 1.00 58.03 C ANISOU 447 CZ ARG A 58 7354 7274 7420 -61 80 11 C ATOM 448 NH1 ARG A 58 -12.354 -12.944 44.863 1.00 59.41 N ANISOU 448 NH1 ARG A 58 7504 7515 7554 37 -16 24 N ATOM 449 NH2 ARG A 58 -13.988 -12.230 43.403 1.00 60.53 N ANISOU 449 NH2 ARG A 58 7579 7716 7704 13 -38 -13 N ATOM 450 N GLU A 59 -5.240 -10.493 43.059 1.00 39.87 N ANISOU 450 N GLU A 59 5117 4812 5217 18 6 -19 N ATOM 451 CA GLU A 59 -3.908 -11.085 43.162 1.00 41.25 C ANISOU 451 CA GLU A 59 5229 5127 5316 31 -41 -23 C ATOM 452 C GLU A 59 -3.117 -10.702 44.415 1.00 40.27 C ANISOU 452 C GLU A 59 5103 4972 5224 30 -14 -41 C ATOM 453 O GLU A 59 -1.996 -11.186 44.579 1.00 40.40 O ANISOU 453 O GLU A 59 5138 4791 5419 61 -112 -52 O ATOM 454 CB GLU A 59 -3.064 -10.724 41.955 1.00 42.23 C ANISOU 454 CB GLU A 59 5372 5234 5437 5 55 -7 C ATOM 455 CG GLU A 59 -3.776 -10.867 40.636 1.00 46.71 C ANISOU 455 CG GLU A 59 6005 5877 5863 3 -126 -47 C ATOM 456 CD GLU A 59 -2.805 -10.676 39.514 1.00 52.51 C ANISOU 456 CD GLU A 59 6583 6784 6584 -51 142 6 C ATOM 457 OE1 GLU A 59 -1.970 -11.583 39.349 1.00 55.97 O ANISOU 457 OE1 GLU A 59 6978 7079 7206 92 34 52 O ATOM 458 OE2 GLU A 59 -2.853 -9.623 38.832 1.00 56.56 O ANISOU 458 OE2 GLU A 59 7258 7042 7187 47 -29 136 O ATOM 459 N GLY A 60 -3.670 -9.848 45.285 1.00 38.96 N ANISOU 459 N GLY A 60 4994 4735 5072 24 -81 3 N ATOM 460 CA GLY A 60 -2.993 -9.429 46.499 1.00 37.96 C ANISOU 460 CA GLY A 60 4877 4616 4928 54 -49 29 C ATOM 461 C GLY A 60 -1.666 -8.724 46.267 1.00 37.47 C ANISOU 461 C GLY A 60 4831 4552 4851 33 -78 -12 C ATOM 462 O GLY A 60 -0.799 -8.802 47.132 1.00 36.60 O ANISOU 462 O GLY A 60 4871 4077 4957 97 -202 34 O ATOM 463 N ARG A 61 -1.494 -8.061 45.119 1.00 36.75 N ANISOU 463 N ARG A 61 4719 4433 4808 11 -63 -60 N ATOM 464 CA ARG A 61 -0.256 -7.329 44.867 1.00 36.86 C ANISOU 464 CA ARG A 61 4723 4503 4776 41 -14 -56 C ATOM 465 C ARG A 61 -0.179 -6.054 45.734 1.00 34.34 C ANISOU 465 C ARG A 61 4364 4146 4535 -7 -33 -33 C ATOM 466 O ARG A 61 0.920 -5.623 46.053 1.00 33.13 O ANISOU 466 O ARG A 61 4365 3584 4635 31 -37 -146 O ATOM 467 CB AARG A 61 -0.113 -7.034 43.384 0.50 37.91 C ANISOU 467 CB AARG A 61 4822 4743 4838 -3 -25 -30 C ATOM 468 CG AARG A 61 0.605 -8.145 42.577 0.50 40.77 C ANISOU 468 CG AARG A 61 5194 5048 5246 77 -9 -58 C ATOM 469 CD AARG A 61 1.224 -7.649 41.277 0.50 44.09 C ANISOU 469 CD AARG A 61 5661 5583 5507 0 77 -17 C ATOM 470 NE AARG A 61 2.691 -7.468 41.295 0.50 46.80 N ANISOU 470 NE AARG A 61 5828 5953 5997 33 12 -62 N ATOM 471 CZ AARG A 61 3.414 -6.598 42.041 0.50 48.10 C ANISOU 471 CZ AARG A 61 6073 6067 6135 -17 -38 -27 C ATOM 472 NH1AARG A 61 2.870 -5.770 42.929 0.50 49.40 N ANISOU 472 NH1AARG A 61 6265 6249 6255 16 -19 -39 N ATOM 473 NH2AARG A 61 4.735 -6.565 41.910 0.50 47.66 N ANISOU 473 NH2AARG A 61 6060 6018 6031 10 -14 -25 N ATOM 474 CB BARG A 61 -0.086 -6.927 43.417 0.50 38.28 C ANISOU 474 CB BARG A 61 4852 4802 4887 -3 -21 -12 C ATOM 475 CG BARG A 61 0.285 -8.078 42.485 0.50 42.28 C ANISOU 475 CG BARG A 61 5467 5201 5394 60 -35 -90 C ATOM 476 CD BARG A 61 1.438 -7.745 41.546 0.50 47.22 C ANISOU 476 CD BARG A 61 5887 5984 6069 -23 138 19 C ATOM 477 NE BARG A 61 1.146 -8.078 40.154 0.50 51.55 N ANISOU 477 NE BARG A 61 6600 6583 6402 -25 11 -72 N ATOM 478 CZ BARG A 61 0.284 -7.427 39.356 0.50 54.92 C ANISOU 478 CZ BARG A 61 6912 6998 6957 37 -47 44 C ATOM 479 NH1BARG A 61 -0.442 -6.389 39.784 0.50 55.61 N ANISOU 479 NH1BARG A 61 7076 6985 7068 -19 16 -38 N ATOM 480 NH2BARG A 61 0.131 -7.833 38.101 0.50 56.68 N ANISOU 480 NH2BARG A 61 7211 7223 7099 13 -8 -40 N ATOM 481 N LEU A 62 -1.342 -5.510 46.105 1.00 30.81 N ANISOU 481 N LEU A 62 4119 3513 4074 -31 -38 -39 N ATOM 482 CA LEU A 62 -1.417 -4.377 47.043 1.00 30.27 C ANISOU 482 CA LEU A 62 3891 3713 3896 -31 -39 -23 C ATOM 483 C LEU A 62 -1.880 -4.885 48.381 1.00 30.47 C ANISOU 483 C LEU A 62 3975 3659 3941 -64 -62 49 C ATOM 484 O LEU A 62 -2.639 -5.850 48.433 1.00 31.23 O ANISOU 484 O LEU A 62 4174 3644 4044 -216 -49 216 O ATOM 485 CB LEU A 62 -2.388 -3.304 46.533 1.00 28.67 C ANISOU 485 CB LEU A 62 3731 3386 3776 -105 -22 -43 C ATOM 486 CG LEU A 62 -1.912 -2.696 45.209 1.00 29.26 C ANISOU 486 CG LEU A 62 3795 3662 3660 -31 -60 -87 C ATOM 487 CD1 LEU A 62 -3.020 -1.878 44.613 1.00 29.26 C ANISOU 487 CD1 LEU A 62 3908 3511 3699 1 26 33 C ATOM 488 CD2 LEU A 62 -0.651 -1.847 45.404 1.00 29.87 C ANISOU 488 CD2 LEU A 62 3968 3513 3866 -37 -2 26 C ATOM 489 N PRO A 63 -1.497 -4.212 49.457 1.00 31.19 N ANISOU 489 N PRO A 63 4079 3804 3964 -112 -83 40 N ATOM 490 CA PRO A 63 -1.863 -4.665 50.794 1.00 31.99 C ANISOU 490 CA PRO A 63 4225 3859 4070 -125 0 74 C ATOM 491 C PRO A 63 -3.357 -4.688 51.046 1.00 33.61 C ANISOU 491 C PRO A 63 4327 4115 4328 -87 -86 36 C ATOM 492 O PRO A 63 -4.122 -3.809 50.653 1.00 31.30 O ANISOU 492 O PRO A 63 4266 3487 4137 -386 -6 129 O ATOM 493 CB PRO A 63 -1.135 -3.706 51.748 1.00 32.91 C ANISOU 493 CB PRO A 63 4268 4140 4096 -148 -42 105 C ATOM 494 CG PRO A 63 -0.468 -2.693 50.910 1.00 32.06 C ANISOU 494 CG PRO A 63 4284 3878 4019 -194 -53 35 C ATOM 495 CD PRO A 63 -0.694 -2.972 49.492 1.00 31.06 C ANISOU 495 CD PRO A 63 4115 3725 3958 -118 -85 73 C ATOM 496 N SER A 64 -3.770 -5.771 51.708 1.00 35.79 N ANISOU 496 N SER A 64 4697 4340 4561 -77 -27 152 N ATOM 497 CA SER A 64 -5.167 -6.052 52.018 1.00 38.48 C ANISOU 497 CA SER A 64 4903 4811 4906 -16 -17 43 C ATOM 498 C SER A 64 -5.445 -5.725 53.472 1.00 39.45 C ANISOU 498 C SER A 64 5071 4932 4985 -34 -5 85 C ATOM 499 O SER A 64 -4.540 -5.802 54.305 1.00 39.88 O ANISOU 499 O SER A 64 5182 4974 4994 -47 -46 181 O ATOM 500 CB SER A 64 -5.468 -7.521 51.743 1.00 39.33 C ANISOU 500 CB SER A 64 5041 4895 5006 -91 5 17 C ATOM 501 OG SER A 64 -5.356 -7.773 50.346 1.00 42.02 O ANISOU 501 OG SER A 64 5535 5244 5183 -50 0 31 O ATOM 502 N ALA A 65 -6.661 -5.256 53.743 1.00 40.46 N ANISOU 502 N ALA A 65 5141 5095 5136 -25 24 65 N ATOM 503 CA ALA A 65 -7.164 -5.005 55.108 1.00 41.50 C ANISOU 503 CA ALA A 65 5275 5252 5239 -21 7 41 C ATOM 504 C ALA A 65 -8.665 -5.202 55.026 1.00 41.79 C ANISOU 504 C ALA A 65 5281 5323 5273 -44 27 44 C ATOM 505 O ALA A 65 -9.242 -5.062 53.935 1.00 41.77 O ANISOU 505 O ALA A 65 5336 5331 5203 -129 56 134 O ATOM 506 CB ALA A 65 -6.818 -3.613 55.637 1.00 41.72 C ANISOU 506 CB ALA A 65 5289 5300 5264 -38 -37 25 C ATOM 507 N AGLY A 66 -9.273 -5.552 56.164 0.50 41.74 N ANISOU 507 N AGLY A 66 5274 5312 5272 -35 19 29 N ATOM 508 CA AGLY A 66 -10.705 -5.769 56.232 0.50 41.10 C ANISOU 508 CA AGLY A 66 5184 5222 5207 -16 21 36 C ATOM 509 C AGLY A 66 -11.452 -4.482 55.959 0.50 40.18 C ANISOU 509 C AGLY A 66 5087 5123 5055 -43 37 36 C ATOM 510 O AGLY A 66 -11.200 -3.435 56.572 0.50 39.84 O ANISOU 510 O AGLY A 66 5066 5140 4928 -70 39 56 O ATOM 511 N BGLY A 66 -9.316 -5.476 56.163 0.50 42.35 N ANISOU 511 N BGLY A 66 5359 5389 5343 -37 24 27 N ATOM 512 CA BGLY A 66 -10.712 -5.919 56.192 0.50 42.17 C ANISOU 512 CA BGLY A 66 5309 5363 5348 -20 22 24 C ATOM 513 C BGLY A 66 -11.708 -5.297 55.226 0.50 41.62 C ANISOU 513 C BGLY A 66 5264 5281 5267 -32 50 16 C ATOM 514 O BGLY A 66 -12.068 -5.906 54.209 0.50 42.39 O ANISOU 514 O BGLY A 66 5357 5405 5342 -63 66 -12 O ATOM 515 C SER A 67 -12.416 -2.445 53.573 1.00 37.85 C ANISOU 515 C SER A 67 4787 4795 4798 -16 70 99 C ATOM 516 O SER A 67 -13.012 -1.431 53.184 1.00 38.87 O ANISOU 516 O SER A 67 4972 4882 4914 -55 115 171 O ATOM 517 N ASER A 67 -12.344 -4.571 54.974 0.50 39.15 N ANISOU 517 N ASER A 67 4958 4947 4971 -37 55 57 N ATOM 518 CA ASER A 67 -13.112 -3.435 54.518 0.50 38.49 C ANISOU 518 CA ASER A 67 4864 4898 4863 -58 82 79 C ATOM 519 N BSER A 67 -12.137 -4.074 55.519 0.50 40.43 N ANISOU 519 N BSER A 67 5101 5155 5106 -40 58 72 N ATOM 520 CA BSER A 67 -13.043 -3.368 54.628 0.50 39.13 C ANISOU 520 CA BSER A 67 4946 4978 4942 -60 97 84 C ATOM 521 N ARG A 68 -11.194 -2.783 53.158 1.00 34.48 N ANISOU 521 N ARG A 68 4449 4353 4297 -111 116 198 N ATOM 522 CA ARG A 68 -10.428 -1.929 52.226 1.00 32.08 C ANISOU 522 CA ARG A 68 4115 4042 4030 -103 72 125 C ATOM 523 C ARG A 68 -10.704 -2.311 50.789 1.00 30.90 C ANISOU 523 C ARG A 68 4006 3823 3910 -126 68 177 C ATOM 524 O ARG A 68 -10.478 -3.458 50.374 1.00 31.03 O ANISOU 524 O ARG A 68 4095 3805 3889 -278 144 259 O ATOM 525 CB ARG A 68 -8.934 -2.043 52.462 1.00 31.58 C ANISOU 525 CB ARG A 68 4102 3980 3917 -165 110 237 C ATOM 526 CG ARG A 68 -8.084 -1.055 51.544 1.00 28.67 C ANISOU 526 CG ARG A 68 3675 3471 3745 -157 129 161 C ATOM 527 CD ARG A 68 -6.649 -1.314 51.664 1.00 27.78 C ANISOU 527 CD ARG A 68 3742 3285 3526 -195 -21 302 C ATOM 528 NE ARG A 68 -6.175 -0.793 52.929 1.00 26.65 N ANISOU 528 NE ARG A 68 3630 3085 3409 -252 102 202 N ATOM 529 CZ ARG A 68 -5.138 -1.243 53.638 1.00 28.58 C ANISOU 529 CZ ARG A 68 3680 3502 3674 -181 90 174 C ATOM 530 NH1 ARG A 68 -4.409 -2.286 53.248 1.00 28.83 N ANISOU 530 NH1 ARG A 68 3869 3440 3643 -154 21 225 N ATOM 531 NH2 ARG A 68 -4.817 -0.593 54.763 1.00 32.25 N ANISOU 531 NH2 ARG A 68 4417 4169 3668 -242 12 199 N ATOM 532 N THR A 69 -11.091 -1.312 49.998 1.00 29.16 N ANISOU 532 N THR A 69 3715 3717 3645 -213 17 102 N ATOM 533 CA THR A 69 -11.221 -1.517 48.564 1.00 26.98 C ANISOU 533 CA THR A 69 3455 3392 3402 -309 149 208 C ATOM 534 C THR A 69 -10.313 -0.513 47.859 1.00 23.28 C ANISOU 534 C THR A 69 3143 2770 2933 -294 110 163 C ATOM 535 O THR A 69 -9.832 0.410 48.473 1.00 24.05 O ANISOU 535 O THR A 69 3204 3082 2852 -520 373 172 O ATOM 536 CB THR A 69 -12.624 -1.350 48.109 1.00 27.52 C ANISOU 536 CB THR A 69 3478 3533 3444 -126 42 180 C ATOM 537 OG1 THR A 69 -13.123 -0.111 48.575 1.00 28.81 O ANISOU 537 OG1 THR A 69 3640 3551 3755 -249 214 143 O ATOM 538 CG2 THR A 69 -13.535 -2.406 48.736 1.00 29.26 C ANISOU 538 CG2 THR A 69 3649 3718 3749 -167 129 89 C ATOM 539 N TRP A 70 -10.177 -0.720 46.585 1.00 18.39 N ANISOU 539 N TRP A 70 2597 1866 2522 -420 74 259 N ATOM 540 CA TRP A 70 -9.247 0.044 45.725 1.00 16.79 C ANISOU 540 CA TRP A 70 2304 1902 2172 -240 10 184 C ATOM 541 C TRP A 70 -9.895 0.490 44.446 1.00 16.13 C ANISOU 541 C TRP A 70 2211 1578 2340 -263 -192 186 C ATOM 542 O TRP A 70 -10.771 -0.148 43.919 1.00 16.79 O ANISOU 542 O TRP A 70 2478 1414 2484 -430 -321 243 O ATOM 543 CB TRP A 70 -8.070 -0.844 45.332 1.00 16.13 C ANISOU 543 CB TRP A 70 2307 1594 2227 -180 -166 203 C ATOM 544 CG TRP A 70 -7.192 -1.283 46.463 1.00 17.83 C ANISOU 544 CG TRP A 70 2430 1964 2380 -129 -229 387 C ATOM 545 CD1 TRP A 70 -7.311 -2.447 47.198 1.00 20.94 C ANISOU 545 CD1 TRP A 70 2845 2229 2880 -278 -177 390 C ATOM 546 CD2 TRP A 70 -6.030 -0.642 46.937 1.00 16.08 C ANISOU 546 CD2 TRP A 70 2550 1186 2371 -180 -208 517 C ATOM 547 NE1 TRP A 70 -6.295 -2.523 48.120 1.00 21.70 N ANISOU 547 NE1 TRP A 70 3088 2436 2720 -143 -306 604 N ATOM 548 CE2 TRP A 70 -5.477 -1.436 47.973 1.00 19.95 C ANISOU 548 CE2 TRP A 70 2794 2245 2540 -90 -328 311 C ATOM 549 CE3 TRP A 70 -5.366 0.561 46.599 1.00 16.31 C ANISOU 549 CE3 TRP A 70 2235 1541 2421 -327 114 364 C ATOM 550 CZ2 TRP A 70 -4.312 -1.065 48.650 1.00 21.67 C ANISOU 550 CZ2 TRP A 70 2963 2538 2733 -74 -358 484 C ATOM 551 CZ3 TRP A 70 -4.232 0.904 47.276 1.00 18.99 C ANISOU 551 CZ3 TRP A 70 2754 2107 2352 -279 -7 193 C ATOM 552 CH2 TRP A 70 -3.710 0.119 48.292 1.00 21.95 C ANISOU 552 CH2 TRP A 70 2808 2688 2844 -64 -321 197 C ATOM 553 N ARG A 71 -9.453 1.659 43.949 1.00 14.41 N ANISOU 553 N ARG A 71 2166 1386 1923 -270 -104 192 N ATOM 554 CA ARG A 71 -9.838 2.200 42.643 1.00 13.34 C ANISOU 554 CA ARG A 71 1887 1325 1854 -148 -80 59 C ATOM 555 C ARG A 71 -8.576 2.630 41.925 1.00 12.98 C ANISOU 555 C ARG A 71 1887 1154 1891 29 -97 96 C ATOM 556 O ARG A 71 -7.537 2.799 42.556 1.00 14.11 O ANISOU 556 O ARG A 71 2077 1150 2133 -255 -145 302 O ATOM 557 CB ARG A 71 -10.800 3.366 42.845 1.00 14.64 C ANISOU 557 CB ARG A 71 1833 1731 1998 -31 5 191 C ATOM 558 CG ARG A 71 -12.189 2.971 43.317 1.00 16.71 C ANISOU 558 CG ARG A 71 1943 2148 2256 -133 93 124 C ATOM 559 CD ARG A 71 -13.107 4.126 43.525 1.00 18.70 C ANISOU 559 CD ARG A 71 2471 2056 2578 -96 65 150 C ATOM 560 NE ARG A 71 -14.347 3.635 44.129 1.00 22.17 N ANISOU 560 NE ARG A 71 2361 2993 3069 33 210 -20 N ATOM 561 CZ ARG A 71 -15.358 3.100 43.443 1.00 22.70 C ANISOU 561 CZ ARG A 71 2819 2751 3055 -22 101 -153 C ATOM 562 NH1 ARG A 71 -15.360 3.069 42.124 1.00 23.84 N ANISOU 562 NH1 ARG A 71 3087 2802 3167 15 -29 177 N ATOM 563 NH2 ARG A 71 -16.423 2.629 44.102 1.00 25.19 N ANISOU 563 NH2 ARG A 71 3038 3031 3499 -181 92 332 N ATOM 564 N GLU A 72 -8.667 2.855 40.617 1.00 13.16 N ANISOU 564 N GLU A 72 1850 1298 1850 -139 -110 47 N ATOM 565 CA GLU A 72 -7.517 3.208 39.811 1.00 13.35 C ANISOU 565 CA GLU A 72 1869 1338 1866 -30 -85 122 C ATOM 566 C GLU A 72 -7.832 4.449 38.941 1.00 12.99 C ANISOU 566 C GLU A 72 1772 1217 1946 -27 -93 173 C ATOM 567 O GLU A 72 -8.994 4.783 38.743 1.00 13.92 O ANISOU 567 O GLU A 72 1978 932 2376 -255 -201 364 O ATOM 568 CB GLU A 72 -7.066 2.053 38.941 1.00 15.75 C ANISOU 568 CB GLU A 72 2149 1683 2153 -4 21 104 C ATOM 569 CG GLU A 72 -8.096 1.552 37.959 1.00 15.87 C ANISOU 569 CG GLU A 72 2354 1423 2250 -54 39 127 C ATOM 570 CD GLU A 72 -7.498 0.765 36.835 1.00 22.34 C ANISOU 570 CD GLU A 72 3228 2150 3107 11 383 -144 C ATOM 571 OE1 GLU A 72 -6.682 1.288 36.064 1.00 25.70 O ANISOU 571 OE1 GLU A 72 3957 2289 3516 -91 521 -123 O ATOM 572 OE2 GLU A 72 -7.820 -0.435 36.729 1.00 26.71 O ANISOU 572 OE2 GLU A 72 3804 2416 3926 -320 240 -279 O ATOM 573 N ALA A 73 -6.778 5.107 38.508 1.00 12.31 N ANISOU 573 N ALA A 73 1795 1107 1774 79 -65 253 N ATOM 574 CA ALA A 73 -6.889 6.270 37.601 1.00 11.36 C ANISOU 574 CA ALA A 73 1726 956 1633 53 -53 76 C ATOM 575 C ALA A 73 -5.707 6.358 36.687 1.00 10.80 C ANISOU 575 C ALA A 73 1772 718 1611 64 -40 -72 C ATOM 576 O ALA A 73 -4.570 6.068 37.091 1.00 12.96 O ANISOU 576 O ALA A 73 1954 1231 1738 83 -47 99 O ATOM 577 CB ALA A 73 -7.013 7.565 38.439 1.00 13.04 C ANISOU 577 CB ALA A 73 1973 1226 1753 -27 79 -18 C ATOM 578 N ASP A 74 -5.948 6.779 35.461 1.00 11.08 N ANISOU 578 N ASP A 74 1674 883 1650 98 -77 -64 N ATOM 579 CA ASP A 74 -4.893 6.953 34.474 1.00 11.69 C ANISOU 579 CA ASP A 74 1823 986 1632 -5 45 -54 C ATOM 580 C ASP A 74 -4.166 8.246 34.777 1.00 12.92 C ANISOU 580 C ASP A 74 1810 1249 1849 -59 50 11 C ATOM 581 O ASP A 74 -4.807 9.286 35.110 1.00 14.41 O ANISOU 581 O ASP A 74 2190 1015 2267 -62 252 -112 O ATOM 582 CB ASP A 74 -5.423 7.070 33.039 1.00 12.70 C ANISOU 582 CB ASP A 74 2027 1087 1711 -48 -108 -49 C ATOM 583 CG ASP A 74 -5.874 5.765 32.422 1.00 13.10 C ANISOU 583 CG ASP A 74 2056 1304 1616 69 -32 -79 C ATOM 584 OD1 ASP A 74 -6.192 4.805 33.166 1.00 13.16 O ANISOU 584 OD1 ASP A 74 2435 856 1708 51 192 -151 O ATOM 585 OD2 ASP A 74 -6.041 5.708 31.198 1.00 13.73 O ANISOU 585 OD2 ASP A 74 2550 1057 1609 71 -11 -257 O ATOM 586 N ILE A 75 -2.856 8.201 34.585 1.00 12.07 N ANISOU 586 N ILE A 75 1681 1044 1860 -89 29 22 N ATOM 587 CA ILE A 75 -2.013 9.364 34.851 1.00 12.70 C ANISOU 587 CA ILE A 75 1898 1058 1866 -91 -21 -31 C ATOM 588 C ILE A 75 -1.246 9.710 33.604 1.00 13.87 C ANISOU 588 C ILE A 75 2084 1277 1909 -18 46 -35 C ATOM 589 O ILE A 75 -0.885 8.859 32.807 1.00 14.95 O ANISOU 589 O ILE A 75 2360 1418 1898 -107 58 -19 O ATOM 590 CB ILE A 75 -1.093 9.041 36.029 1.00 13.30 C ANISOU 590 CB ILE A 75 1848 1255 1948 24 2 -92 C ATOM 591 CG1 ILE A 75 -1.867 8.822 37.319 1.00 13.67 C ANISOU 591 CG1 ILE A 75 1945 1368 1881 73 -61 25 C ATOM 592 CG2 ILE A 75 -0.013 10.090 36.245 1.00 15.32 C ANISOU 592 CG2 ILE A 75 2182 1524 2113 -246 -164 17 C ATOM 593 CD1 ILE A 75 -2.552 10.049 37.907 1.00 15.70 C ANISOU 593 CD1 ILE A 75 2321 1746 1896 117 86 -176 C ATOM 594 N ASN A 76 -1.021 11.031 33.415 1.00 14.42 N ANISOU 594 N ASN A 76 2228 1305 1944 -190 61 19 N ATOM 595 CA ASN A 76 -0.240 11.528 32.286 1.00 16.24 C ANISOU 595 CA ASN A 76 2289 1745 2135 -124 90 123 C ATOM 596 C ASN A 76 -0.871 11.323 30.939 1.00 16.32 C ANISOU 596 C ASN A 76 2349 1696 2152 -73 84 90 C ATOM 597 O ASN A 76 -0.160 11.393 29.893 1.00 18.71 O ANISOU 597 O ASN A 76 2538 2396 2174 -96 250 227 O ATOM 598 CB ASN A 76 1.214 10.953 32.277 1.00 15.93 C ANISOU 598 CB ASN A 76 2289 1560 2203 -93 199 214 C ATOM 599 CG ASN A 76 2.021 11.337 33.494 1.00 18.24 C ANISOU 599 CG ASN A 76 2345 2173 2410 -108 161 84 C ATOM 600 OD1 ASN A 76 1.885 12.432 33.991 1.00 20.52 O ANISOU 600 OD1 ASN A 76 2781 2295 2717 -355 119 -37 O ATOM 601 ND2 ASN A 76 2.856 10.413 33.999 1.00 19.42 N ANISOU 601 ND2 ASN A 76 2478 2315 2586 -118 116 240 N ATOM 602 N TYR A 77 -2.172 11.060 30.899 1.00 15.24 N ANISOU 602 N TYR A 77 2271 1483 2035 -65 60 202 N ATOM 603 CA TYR A 77 -2.833 10.804 29.622 1.00 16.59 C ANISOU 603 CA TYR A 77 2340 1829 2134 -93 -12 166 C ATOM 604 C TYR A 77 -3.065 12.140 28.910 1.00 17.21 C ANISOU 604 C TYR A 77 2437 1810 2290 39 9 71 C ATOM 605 O TYR A 77 -3.555 13.074 29.533 1.00 17.50 O ANISOU 605 O TYR A 77 2832 1451 2365 -5 65 188 O ATOM 606 CB TYR A 77 -4.188 10.071 29.790 1.00 16.29 C ANISOU 606 CB TYR A 77 2311 1744 2132 -180 -26 54 C ATOM 607 CG TYR A 77 -4.882 9.881 28.482 1.00 14.89 C ANISOU 607 CG TYR A 77 2160 1589 1907 -118 64 192 C ATOM 608 CD1 TYR A 77 -4.416 8.957 27.554 1.00 16.45 C ANISOU 608 CD1 TYR A 77 2352 1731 2164 185 -40 57 C ATOM 609 CD2 TYR A 77 -5.939 10.660 28.113 1.00 13.85 C ANISOU 609 CD2 TYR A 77 2119 1200 1942 -122 155 40 C ATOM 610 CE1 TYR A 77 -5.017 8.781 26.334 1.00 15.85 C ANISOU 610 CE1 TYR A 77 2128 1718 2174 73 83 11 C ATOM 611 CE2 TYR A 77 -6.530 10.517 26.876 1.00 15.76 C ANISOU 611 CE2 TYR A 77 2311 1741 1934 -18 14 -91 C ATOM 612 CZ TYR A 77 -6.074 9.527 25.990 1.00 14.82 C ANISOU 612 CZ TYR A 77 2064 1491 2074 -54 63 74 C ATOM 613 OH TYR A 77 -6.648 9.386 24.754 1.00 17.14 O ANISOU 613 OH TYR A 77 2448 1774 2289 154 -105 143 O ATOM 614 N VAL A 78 -2.747 12.162 27.626 1.00 18.32 N ANISOU 614 N VAL A 78 2685 1989 2285 17 -26 294 N ATOM 615 CA VAL A 78 -2.959 13.342 26.759 1.00 20.43 C ANISOU 615 CA VAL A 78 2845 2323 2590 16 -55 229 C ATOM 616 C VAL A 78 -3.888 12.983 25.598 1.00 19.34 C ANISOU 616 C VAL A 78 2647 2213 2485 -52 1 228 C ATOM 617 O VAL A 78 -4.967 13.564 25.461 1.00 21.98 O ANISOU 617 O VAL A 78 3066 2556 2728 110 -35 205 O ATOM 618 CB VAL A 78 -1.602 13.881 26.267 1.00 21.83 C ANISOU 618 CB VAL A 78 2937 2616 2740 -85 -64 292 C ATOM 619 CG1 VAL A 78 -1.801 15.073 25.291 1.00 25.96 C ANISOU 619 CG1 VAL A 78 3724 2941 3197 -55 -90 257 C ATOM 620 CG2 VAL A 78 -0.773 14.361 27.444 1.00 23.94 C ANISOU 620 CG2 VAL A 78 3172 2735 3187 -251 -63 254 C ATOM 621 N SER A 79 -3.478 12.019 24.780 1.00 18.29 N ANISOU 621 N SER A 79 2562 2041 2343 -62 -1 294 N ATOM 622 CA SER A 79 -4.276 11.592 23.652 1.00 17.78 C ANISOU 622 CA SER A 79 2518 1966 2270 19 34 242 C ATOM 623 C SER A 79 -3.813 10.230 23.135 1.00 17.39 C ANISOU 623 C SER A 79 2360 2071 2176 75 5 146 C ATOM 624 O SER A 79 -2.740 9.712 23.535 1.00 18.77 O ANISOU 624 O SER A 79 2633 2165 2332 163 -207 200 O ATOM 625 CB SER A 79 -4.194 12.643 22.529 1.00 19.32 C ANISOU 625 CB SER A 79 2632 2367 2339 48 -2 177 C ATOM 626 OG SER A 79 -2.929 12.670 22.033 1.00 22.27 O ANISOU 626 OG SER A 79 2976 2784 2702 -111 390 582 O ATOM 627 N GLY A 80 -4.630 9.656 22.276 1.00 16.52 N ANISOU 627 N GLY A 80 2306 1895 2073 162 -56 144 N ATOM 628 CA GLY A 80 -4.342 8.375 21.644 1.00 17.18 C ANISOU 628 CA GLY A 80 2296 2040 2191 108 -42 68 C ATOM 629 C GLY A 80 -4.655 7.212 22.556 1.00 16.97 C ANISOU 629 C GLY A 80 2382 1967 2095 137 33 58 C ATOM 630 O GLY A 80 -5.515 7.312 23.447 1.00 16.87 O ANISOU 630 O GLY A 80 2521 1768 2121 245 115 267 O ATOM 631 N PHE A 81 -3.997 6.078 22.308 1.00 17.47 N ANISOU 631 N PHE A 81 2449 2059 2127 223 78 97 N ATOM 632 CA PHE A 81 -4.189 4.867 23.157 1.00 15.80 C ANISOU 632 CA PHE A 81 2270 1780 1953 115 54 -21 C ATOM 633 C PHE A 81 -3.721 5.132 24.602 1.00 15.67 C ANISOU 633 C PHE A 81 2134 1849 1970 56 45 -13 C ATOM 634 O PHE A 81 -2.829 5.979 24.875 1.00 16.74 O ANISOU 634 O PHE A 81 2365 2061 1932 -40 84 -132 O ATOM 635 CB PHE A 81 -3.398 3.681 22.566 1.00 17.11 C ANISOU 635 CB PHE A 81 2366 1907 2227 126 63 -28 C ATOM 636 CG PHE A 81 -3.923 3.258 21.250 1.00 16.14 C ANISOU 636 CG PHE A 81 2434 1559 2138 420 100 -32 C ATOM 637 CD1 PHE A 81 -3.215 3.510 20.075 1.00 21.96 C ANISOU 637 CD1 PHE A 81 3096 2649 2596 -19 -44 173 C ATOM 638 CD2 PHE A 81 -5.141 2.604 21.175 1.00 19.75 C ANISOU 638 CD2 PHE A 81 2600 2423 2480 298 -7 -212 C ATOM 639 CE1 PHE A 81 -3.743 3.119 18.856 1.00 22.05 C ANISOU 639 CE1 PHE A 81 3149 2668 2558 50 93 -80 C ATOM 640 CE2 PHE A 81 -5.677 2.234 19.931 1.00 21.29 C ANISOU 640 CE2 PHE A 81 2696 2537 2853 155 7 -207 C ATOM 641 CZ PHE A 81 -4.960 2.492 18.795 1.00 21.75 C ANISOU 641 CZ PHE A 81 3080 2575 2607 92 -129 17 C ATOM 642 N ARG A 82 -4.371 4.445 25.535 1.00 14.69 N ANISOU 642 N ARG A 82 2202 1531 1848 111 44 -85 N ATOM 643 CA ARG A 82 -4.007 4.606 26.938 1.00 15.80 C ANISOU 643 CA ARG A 82 2229 1818 1954 34 42 -12 C ATOM 644 C ARG A 82 -2.583 4.211 27.142 1.00 16.46 C ANISOU 644 C ARG A 82 2329 1964 1961 133 44 -88 C ATOM 645 O ARG A 82 -2.020 3.357 26.408 1.00 16.58 O ANISOU 645 O ARG A 82 2668 1551 2079 320 107 -282 O ATOM 646 CB ARG A 82 -4.971 3.856 27.866 1.00 16.16 C ANISOU 646 CB ARG A 82 2274 1891 1973 -31 -25 -22 C ATOM 647 CG ARG A 82 -6.375 4.449 27.871 1.00 17.52 C ANISOU 647 CG ARG A 82 2357 2187 2113 -17 3 -8 C ATOM 648 CD ARG A 82 -7.382 3.496 28.484 1.00 16.48 C ANISOU 648 CD ARG A 82 2280 1845 2134 -2 80 -200 C ATOM 649 NE ARG A 82 -7.155 3.358 29.916 1.00 15.17 N ANISOU 649 NE ARG A 82 2298 1454 2009 -195 133 -163 N ATOM 650 CZ ARG A 82 -7.554 2.365 30.708 1.00 16.06 C ANISOU 650 CZ ARG A 82 2391 1527 2183 94 49 40 C ATOM 651 NH1 ARG A 82 -8.223 1.323 30.238 1.00 20.76 N ANISOU 651 NH1 ARG A 82 3027 2110 2748 -135 -219 -256 N ATOM 652 NH2 ARG A 82 -7.324 2.447 32.010 1.00 17.68 N ANISOU 652 NH2 ARG A 82 2838 1577 2302 35 -32 11 N ATOM 653 N ASN A 83 -1.979 4.816 28.133 1.00 16.90 N ANISOU 653 N ASN A 83 2343 1976 2100 115 37 -201 N ATOM 654 CA ASN A 83 -0.563 4.622 28.466 1.00 17.28 C ANISOU 654 CA ASN A 83 2352 2133 2078 77 61 -110 C ATOM 655 C ASN A 83 -0.386 3.578 29.578 1.00 16.91 C ANISOU 655 C ASN A 83 2304 2020 2099 161 70 -191 C ATOM 656 O ASN A 83 -1.318 2.865 29.916 1.00 17.38 O ANISOU 656 O ASN A 83 2533 1881 2189 336 135 -421 O ATOM 657 CB ASN A 83 0.040 5.998 28.776 1.00 18.01 C ANISOU 657 CB ASN A 83 2453 2164 2224 9 72 -74 C ATOM 658 CG ASN A 83 -0.419 6.592 30.078 1.00 17.34 C ANISOU 658 CG ASN A 83 2352 2106 2130 7 59 3 C ATOM 659 OD1 ASN A 83 -1.026 5.933 30.897 1.00 16.76 O ANISOU 659 OD1 ASN A 83 2461 1859 2046 -36 -52 13 O ATOM 660 ND2 ASN A 83 -0.183 7.886 30.242 1.00 19.71 N ANISOU 660 ND2 ASN A 83 2726 2102 2659 -111 39 -14 N ATOM 661 N ALA A 84 0.811 3.570 30.178 1.00 17.30 N ANISOU 661 N ALA A 84 2352 2101 2119 199 91 -228 N ATOM 662 CA ALA A 84 1.167 2.615 31.215 1.00 18.33 C ANISOU 662 CA ALA A 84 2452 2272 2237 185 52 -44 C ATOM 663 C ALA A 84 1.127 3.132 32.634 1.00 17.15 C ANISOU 663 C ALA A 84 2512 1825 2176 132 -37 -122 C ATOM 664 O ALA A 84 1.474 2.400 33.553 1.00 17.24 O ANISOU 664 O ALA A 84 2923 1790 1836 514 93 -297 O ATOM 665 CB ALA A 84 2.568 2.080 30.920 1.00 20.24 C ANISOU 665 CB ALA A 84 2635 2443 2611 254 89 -57 C ATOM 666 N ASP A 85 0.729 4.395 32.829 1.00 15.22 N ANISOU 666 N ASP A 85 2131 1671 1981 371 54 -151 N ATOM 667 CA ASP A 85 0.853 5.055 34.132 1.00 14.94 C ANISOU 667 CA ASP A 85 2083 1671 1921 84 -32 -39 C ATOM 668 C ASP A 85 -0.489 5.048 34.827 1.00 13.32 C ANISOU 668 C ASP A 85 2033 1314 1713 81 -96 -158 C ATOM 669 O ASP A 85 -1.515 5.493 34.263 1.00 13.68 O ANISOU 669 O ASP A 85 2152 1157 1888 53 -123 -220 O ATOM 670 CB ASP A 85 1.271 6.504 33.943 1.00 15.19 C ANISOU 670 CB ASP A 85 2127 1659 1983 109 68 24 C ATOM 671 CG ASP A 85 2.653 6.678 33.379 1.00 18.87 C ANISOU 671 CG ASP A 85 2301 2207 2660 -38 40 0 C ATOM 672 OD1 ASP A 85 3.467 5.751 33.416 1.00 23.13 O ANISOU 672 OD1 ASP A 85 2345 3028 3415 262 210 293 O ATOM 673 OD2 ASP A 85 3.047 7.783 32.920 1.00 22.87 O ANISOU 673 OD2 ASP A 85 2894 2485 3308 -40 141 336 O ATOM 674 N ARG A 86 -0.497 4.608 36.073 1.00 12.25 N ANISOU 674 N ARG A 86 1959 906 1789 117 -70 -30 N ATOM 675 CA ARG A 86 -1.707 4.555 36.871 1.00 12.63 C ANISOU 675 CA ARG A 86 1942 1104 1752 74 -81 69 C ATOM 676 C ARG A 86 -1.447 4.905 38.312 1.00 12.11 C ANISOU 676 C ARG A 86 1811 1034 1755 44 -65 -14 C ATOM 677 O ARG A 86 -0.382 4.618 38.853 1.00 13.97 O ANISOU 677 O ARG A 86 2016 1190 2101 423 1 -177 O ATOM 678 CB ARG A 86 -2.350 3.156 36.832 1.00 13.13 C ANISOU 678 CB ARG A 86 2012 1202 1774 -21 -142 -73 C ATOM 679 CG ARG A 86 -2.627 2.559 35.463 1.00 13.87 C ANISOU 679 CG ARG A 86 2126 1259 1884 89 -160 -10 C ATOM 680 CD ARG A 86 -3.897 2.996 34.811 1.00 15.11 C ANISOU 680 CD ARG A 86 2297 1566 1878 249 -168 -44 C ATOM 681 NE ARG A 86 -4.051 2.391 33.507 1.00 14.88 N ANISOU 681 NE ARG A 86 2455 1138 2058 -78 11 -138 N ATOM 682 CZ ARG A 86 -3.542 2.805 32.375 1.00 14.20 C ANISOU 682 CZ ARG A 86 1928 1491 1973 86 -12 -101 C ATOM 683 NH1 ARG A 86 -2.767 3.897 32.314 1.00 14.27 N ANISOU 683 NH1 ARG A 86 2203 1614 1604 -51 -110 -74 N ATOM 684 NH2 ARG A 86 -3.818 2.116 31.247 1.00 18.51 N ANISOU 684 NH2 ARG A 86 2698 2112 2222 92 -49 -206 N ATOM 685 N LEU A 87 -2.458 5.461 38.948 1.00 13.04 N ANISOU 685 N LEU A 87 1890 1218 1844 61 -10 100 N ATOM 686 CA LEU A 87 -2.490 5.638 40.373 1.00 13.48 C ANISOU 686 CA LEU A 87 1896 1424 1801 22 -60 113 C ATOM 687 C LEU A 87 -3.571 4.669 40.878 1.00 14.26 C ANISOU 687 C LEU A 87 1923 1531 1960 22 -82 96 C ATOM 688 O LEU A 87 -4.627 4.544 40.281 1.00 16.12 O ANISOU 688 O LEU A 87 2273 1699 2150 -263 -202 465 O ATOM 689 CB LEU A 87 -2.881 7.098 40.654 1.00 16.30 C ANISOU 689 CB LEU A 87 2216 1854 2122 188 -6 27 C ATOM 690 CG ALEU A 87 -2.533 7.761 41.942 0.52 19.34 C ANISOU 690 CG ALEU A 87 2536 2337 2476 74 -89 -25 C ATOM 691 CD1ALEU A 87 -1.042 7.835 42.112 0.52 20.76 C ANISOU 691 CD1ALEU A 87 2545 2793 2547 -4 -1 55 C ATOM 692 CD2ALEU A 87 -3.094 9.201 41.973 0.52 18.64 C ANISOU 692 CD2ALEU A 87 2515 2121 2443 56 -112 -66 C ATOM 693 CG BLEU A 87 -2.832 7.632 42.049 0.48 17.25 C ANISOU 693 CG BLEU A 87 2275 2009 2267 -43 -63 37 C ATOM 694 CD1BLEU A 87 -2.212 9.082 42.041 0.48 15.94 C ANISOU 694 CD1BLEU A 87 2147 1744 2165 -58 34 25 C ATOM 695 CD2BLEU A 87 -4.218 7.605 42.646 0.48 17.69 C ANISOU 695 CD2BLEU A 87 2282 2165 2274 92 2 -53 C ATOM 696 N VAL A 88 -3.275 3.972 41.959 1.00 13.61 N ANISOU 696 N VAL A 88 1923 1470 1775 -29 -83 147 N ATOM 697 CA VAL A 88 -4.247 3.057 42.583 1.00 14.83 C ANISOU 697 CA VAL A 88 2000 1569 2064 -59 -39 36 C ATOM 698 C VAL A 88 -4.387 3.535 44.028 1.00 15.25 C ANISOU 698 C VAL A 88 2074 1689 2030 -128 -45 216 C ATOM 699 O VAL A 88 -3.347 3.682 44.722 1.00 17.46 O ANISOU 699 O VAL A 88 2357 2213 2062 -385 -199 169 O ATOM 700 CB VAL A 88 -3.771 1.585 42.415 1.00 16.83 C ANISOU 700 CB VAL A 88 2293 1802 2297 40 15 164 C ATOM 701 CG1 VAL A 88 -4.777 0.686 42.946 1.00 20.33 C ANISOU 701 CG1 VAL A 88 2625 2193 2906 -123 -4 -12 C ATOM 702 CG2 VAL A 88 -3.485 1.259 40.961 1.00 20.73 C ANISOU 702 CG2 VAL A 88 3043 2009 2824 109 -77 -230 C ATOM 703 N TYR A 89 -5.608 3.778 44.469 1.00 14.46 N ANISOU 703 N TYR A 89 2117 1451 1925 -230 -27 162 N ATOM 704 CA TYR A 89 -5.874 4.417 45.768 1.00 15.74 C ANISOU 704 CA TYR A 89 2140 1835 2005 -145 95 122 C ATOM 705 C TYR A 89 -6.949 3.608 46.521 1.00 16.81 C ANISOU 705 C TYR A 89 2304 1944 2139 -263 -4 151 C ATOM 706 O TYR A 89 -7.913 3.113 45.928 1.00 16.89 O ANISOU 706 O TYR A 89 2427 1837 2153 -304 -3 284 O ATOM 707 CB TYR A 89 -6.287 5.880 45.622 1.00 17.76 C ANISOU 707 CB TYR A 89 2514 1926 2306 -286 -82 62 C ATOM 708 CG TYR A 89 -7.534 6.137 44.790 1.00 16.68 C ANISOU 708 CG TYR A 89 2584 1404 2349 -188 -73 63 C ATOM 709 CD1 TYR A 89 -8.763 6.368 45.362 1.00 19.26 C ANISOU 709 CD1 TYR A 89 2773 1785 2760 -355 -53 -46 C ATOM 710 CD2 TYR A 89 -7.461 6.157 43.380 1.00 19.88 C ANISOU 710 CD2 TYR A 89 2975 2067 2510 -342 -59 14 C ATOM 711 CE1 TYR A 89 -9.905 6.673 44.586 1.00 20.24 C ANISOU 711 CE1 TYR A 89 2912 2169 2608 -238 -56 78 C ATOM 712 CE2 TYR A 89 -8.603 6.438 42.609 1.00 19.13 C ANISOU 712 CE2 TYR A 89 3043 1708 2516 -169 -20 82 C ATOM 713 CZ TYR A 89 -9.805 6.660 43.200 1.00 20.43 C ANISOU 713 CZ TYR A 89 3156 1730 2876 -77 -29 126 C ATOM 714 OH TYR A 89 -10.940 6.876 42.439 1.00 22.72 O ANISOU 714 OH TYR A 89 3748 1625 3257 -381 -341 376 O ATOM 715 N SER A 90 -6.719 3.465 47.818 1.00 17.97 N ANISOU 715 N SER A 90 2584 2111 2132 -320 47 165 N ATOM 716 CA SER A 90 -7.600 2.666 48.697 1.00 19.30 C ANISOU 716 CA SER A 90 2452 2404 2476 -310 43 74 C ATOM 717 C SER A 90 -8.646 3.511 49.379 1.00 21.68 C ANISOU 717 C SER A 90 2829 2706 2701 -221 98 97 C ATOM 718 O SER A 90 -8.553 4.710 49.436 1.00 20.91 O ANISOU 718 O SER A 90 2669 2593 2680 -397 185 80 O ATOM 719 CB SER A 90 -6.758 1.936 49.729 1.00 19.50 C ANISOU 719 CB SER A 90 2661 2250 2499 -390 94 153 C ATOM 720 OG SER A 90 -6.303 2.781 50.770 1.00 19.10 O ANISOU 720 OG SER A 90 2533 2271 2450 -343 68 138 O ATOM 721 N SER A 91 -9.643 2.853 49.983 1.00 22.52 N ANISOU 721 N SER A 91 2683 2822 3049 -314 54 31 N ATOM 722 CA SER A 91 -10.706 3.564 50.679 1.00 24.44 C ANISOU 722 CA SER A 91 3016 3156 3110 -193 86 7 C ATOM 723 C SER A 91 -10.234 4.245 51.983 1.00 25.24 C ANISOU 723 C SER A 91 3169 3253 3166 -126 125 -26 C ATOM 724 O SER A 91 -10.928 5.162 52.476 1.00 27.30 O ANISOU 724 O SER A 91 3338 3660 3375 -207 312 -4 O ATOM 725 CB SER A 91 -11.873 2.577 50.946 1.00 24.80 C ANISOU 725 CB SER A 91 3060 3158 3202 -157 114 -47 C ATOM 726 OG SER A 91 -11.338 1.396 51.481 1.00 25.60 O ANISOU 726 OG SER A 91 3241 3088 3395 -542 201 333 O ATOM 727 N ASP A 92 -9.089 3.796 52.504 1.00 25.21 N ANISOU 727 N ASP A 92 3165 3394 3018 -172 159 -24 N ATOM 728 CA ASP A 92 -8.395 4.412 53.658 1.00 25.54 C ANISOU 728 CA ASP A 92 3218 3310 3175 -118 24 2 C ATOM 729 C ASP A 92 -7.141 5.231 53.257 1.00 24.88 C ANISOU 729 C ASP A 92 3127 3282 3042 -134 0 63 C ATOM 730 O ASP A 92 -6.251 5.482 54.074 1.00 25.32 O ANISOU 730 O ASP A 92 3287 3538 2795 -279 65 45 O ATOM 731 CB ASP A 92 -8.083 3.400 54.777 1.00 26.17 C ANISOU 731 CB ASP A 92 3361 3301 3280 -176 82 92 C ATOM 732 CG ASP A 92 -7.249 2.237 54.324 1.00 28.28 C ANISOU 732 CG ASP A 92 3678 3553 3514 -17 56 -21 C ATOM 733 OD1 ASP A 92 -6.704 1.517 55.209 1.00 31.88 O ANISOU 733 OD1 ASP A 92 4449 4067 3596 -73 38 189 O ATOM 734 OD2 ASP A 92 -7.072 1.918 53.129 1.00 28.55 O ANISOU 734 OD2 ASP A 92 3952 3671 3223 -293 145 172 O ATOM 735 N TRP A 93 -7.109 5.668 51.998 1.00 24.53 N ANISOU 735 N TRP A 93 3140 3184 2994 -162 61 -56 N ATOM 736 CA TRP A 93 -6.183 6.697 51.502 1.00 24.19 C ANISOU 736 CA TRP A 93 3119 3009 3060 -125 43 -86 C ATOM 737 C TRP A 93 -4.723 6.318 51.352 1.00 22.49 C ANISOU 737 C TRP A 93 2972 2783 2787 -138 24 -95 C ATOM 738 O TRP A 93 -3.866 7.190 51.315 1.00 22.49 O ANISOU 738 O TRP A 93 2999 2393 3152 -334 90 12 O ATOM 739 CB TRP A 93 -6.445 8.088 52.209 1.00 24.94 C ANISOU 739 CB TRP A 93 3309 3031 3136 -99 53 -160 C ATOM 740 CG TRP A 93 -7.890 8.359 52.079 1.00 29.14 C ANISOU 740 CG TRP A 93 3626 3567 3877 -63 26 -102 C ATOM 741 CD1 TRP A 93 -8.852 8.225 53.056 1.00 32.94 C ANISOU 741 CD1 TRP A 93 4174 4200 4141 90 133 2 C ATOM 742 CD2 TRP A 93 -8.586 8.550 50.850 1.00 31.10 C ANISOU 742 CD2 TRP A 93 4099 3782 3934 80 17 24 C ATOM 743 NE1 TRP A 93 -10.097 8.369 52.493 1.00 35.22 N ANISOU 743 NE1 TRP A 93 4359 4492 4528 20 55 -22 N ATOM 744 CE2 TRP A 93 -9.958 8.556 51.136 1.00 34.22 C ANISOU 744 CE2 TRP A 93 4330 4253 4416 53 6 26 C ATOM 745 CE3 TRP A 93 -8.176 8.700 49.505 1.00 32.64 C ANISOU 745 CE3 TRP A 93 4215 4007 4179 -34 42 143 C ATOM 746 CZ2 TRP A 93 -10.930 8.747 50.138 1.00 34.94 C ANISOU 746 CZ2 TRP A 93 4500 4294 4479 -20 -36 66 C ATOM 747 CZ3 TRP A 93 -9.129 8.889 48.528 1.00 33.03 C ANISOU 747 CZ3 TRP A 93 4286 3953 4311 -85 -27 75 C ATOM 748 CH2 TRP A 93 -10.494 8.915 48.849 1.00 35.42 C ANISOU 748 CH2 TRP A 93 4463 4457 4537 54 32 -40 C ATOM 749 N LEU A 94 -4.443 5.039 51.156 1.00 20.33 N ANISOU 749 N LEU A 94 2680 2541 2501 -154 18 94 N ATOM 750 CA LEU A 94 -3.130 4.613 50.701 1.00 19.66 C ANISOU 750 CA LEU A 94 2616 2547 2303 -86 -41 48 C ATOM 751 C LEU A 94 -3.100 4.868 49.191 1.00 17.54 C ANISOU 751 C LEU A 94 2396 2126 2141 -204 -12 208 C ATOM 752 O LEU A 94 -4.085 4.592 48.515 1.00 18.14 O ANISOU 752 O LEU A 94 2663 2379 1849 -309 121 426 O ATOM 753 CB LEU A 94 -2.909 3.137 50.928 1.00 20.79 C ANISOU 753 CB LEU A 94 2820 2546 2532 -246 -47 24 C ATOM 754 CG LEU A 94 -2.774 2.613 52.359 1.00 24.63 C ANISOU 754 CG LEU A 94 3307 3136 2915 -74 -77 158 C ATOM 755 CD1 LEU A 94 -2.594 1.104 52.277 1.00 26.34 C ANISOU 755 CD1 LEU A 94 3582 3280 3145 -7 -25 125 C ATOM 756 CD2 LEU A 94 -1.606 3.252 53.043 1.00 28.68 C ANISOU 756 CD2 LEU A 94 3693 3768 3436 -184 -99 90 C ATOM 757 N ILE A 95 -1.987 5.378 48.673 1.00 14.91 N ANISOU 757 N ILE A 95 1962 1806 1895 18 -29 54 N ATOM 758 CA ILE A 95 -1.871 5.695 47.241 1.00 14.22 C ANISOU 758 CA ILE A 95 2005 1529 1868 -95 -56 27 C ATOM 759 C ILE A 95 -0.575 5.088 46.693 1.00 14.60 C ANISOU 759 C ILE A 95 2050 1638 1861 -114 -23 96 C ATOM 760 O ILE A 95 0.519 5.353 47.185 1.00 15.15 O ANISOU 760 O ILE A 95 2174 1474 2105 -149 -41 -116 O ATOM 761 CB ILE A 95 -1.963 7.212 46.955 1.00 14.41 C ANISOU 761 CB ILE A 95 1990 1544 1941 -139 -107 72 C ATOM 762 CG1 ILE A 95 -3.265 7.784 47.554 1.00 18.31 C ANISOU 762 CG1 ILE A 95 2388 2176 2391 -67 60 55 C ATOM 763 CG2 ILE A 95 -1.896 7.434 45.468 1.00 16.58 C ANISOU 763 CG2 ILE A 95 2374 1777 2146 -12 13 38 C ATOM 764 CD1 ILE A 95 -3.554 9.250 47.236 1.00 21.15 C ANISOU 764 CD1 ILE A 95 2846 2159 3030 28 87 -274 C ATOM 765 N TYR A 96 -0.730 4.267 45.669 1.00 14.18 N ANISOU 765 N TYR A 96 2037 1463 1886 -227 -22 99 N ATOM 766 CA TYR A 96 0.362 3.628 44.975 1.00 14.05 C ANISOU 766 CA TYR A 96 1948 1526 1861 -90 -45 -22 C ATOM 767 C TYR A 96 0.400 4.077 43.515 1.00 13.71 C ANISOU 767 C TYR A 96 1938 1408 1862 -99 -137 -43 C ATOM 768 O TYR A 96 -0.635 4.411 42.959 1.00 16.07 O ANISOU 768 O TYR A 96 2132 1846 2127 -12 -181 -79 O ATOM 769 CB TYR A 96 0.229 2.097 45.022 1.00 14.91 C ANISOU 769 CB TYR A 96 2152 1508 2005 -140 -116 57 C ATOM 770 CG TYR A 96 0.621 1.483 46.354 1.00 14.75 C ANISOU 770 CG TYR A 96 2105 1521 1977 -163 10 79 C ATOM 771 CD1 TYR A 96 -0.226 1.583 47.444 1.00 18.64 C ANISOU 771 CD1 TYR A 96 2404 2282 2396 -7 58 71 C ATOM 772 CD2 TYR A 96 1.812 0.798 46.512 1.00 16.01 C ANISOU 772 CD2 TYR A 96 2466 1488 2129 -171 -145 81 C ATOM 773 CE1 TYR A 96 0.113 1.047 48.705 1.00 19.12 C ANISOU 773 CE1 TYR A 96 2673 1977 2612 -116 -40 128 C ATOM 774 CE2 TYR A 96 2.134 0.214 47.747 1.00 18.52 C ANISOU 774 CE2 TYR A 96 2733 1998 2304 -97 -228 157 C ATOM 775 CZ TYR A 96 1.296 0.378 48.835 1.00 17.75 C ANISOU 775 CZ TYR A 96 2380 1808 2553 -291 -140 189 C ATOM 776 OH TYR A 96 1.633 -0.199 50.058 1.00 24.95 O ANISOU 776 OH TYR A 96 3763 3030 2685 2 -439 345 O ATOM 777 N LYS A 97 1.583 4.072 42.920 1.00 14.66 N ANISOU 777 N LYS A 97 2114 1622 1834 32 -121 -127 N ATOM 778 CA LYS A 97 1.771 4.362 41.497 1.00 14.84 C ANISOU 778 CA LYS A 97 2082 1641 1913 91 0 -124 C ATOM 779 C LYS A 97 2.400 3.185 40.790 1.00 15.67 C ANISOU 779 C LYS A 97 2154 1805 1994 201 -85 -197 C ATOM 780 O LYS A 97 3.139 2.387 41.387 1.00 16.32 O ANISOU 780 O LYS A 97 2554 1768 1876 286 -240 -351 O ATOM 781 CB LYS A 97 2.585 5.628 41.230 1.00 16.24 C ANISOU 781 CB LYS A 97 2328 1813 2028 1 19 -211 C ATOM 782 CG LYS A 97 3.989 5.586 41.543 1.00 19.39 C ANISOU 782 CG LYS A 97 2537 2155 2673 6 0 -154 C ATOM 783 CD LYS A 97 4.725 6.876 41.093 1.00 22.46 C ANISOU 783 CD LYS A 97 3050 2525 2959 -136 48 35 C ATOM 784 CE LYS A 97 6.163 6.906 41.525 1.00 25.41 C ANISOU 784 CE LYS A 97 3353 3059 3243 -18 102 3 C ATOM 785 NZ LYS A 97 6.799 8.193 41.063 1.00 25.66 N ANISOU 785 NZ LYS A 97 3257 2854 3637 -209 203 -106 N ATOM 786 N THR A 98 2.084 3.107 39.501 1.00 14.49 N ANISOU 786 N THR A 98 2176 1415 1914 408 -62 -135 N ATOM 787 CA THR A 98 2.746 2.178 38.562 1.00 15.32 C ANISOU 787 CA THR A 98 2042 1815 1960 207 9 -199 C ATOM 788 C THR A 98 3.033 2.969 37.294 1.00 16.47 C ANISOU 788 C THR A 98 2257 1850 2150 167 -11 -165 C ATOM 789 O THR A 98 2.181 3.730 36.839 1.00 16.77 O ANISOU 789 O THR A 98 2392 1990 1989 276 -157 -248 O ATOM 790 CB THR A 98 1.911 0.936 38.309 1.00 16.25 C ANISOU 790 CB THR A 98 2241 1821 2111 257 -33 -159 C ATOM 791 OG1 THR A 98 2.599 0.079 37.355 1.00 18.52 O ANISOU 791 OG1 THR A 98 2813 1851 2370 368 -114 -431 O ATOM 792 CG2 THR A 98 0.538 1.219 37.746 1.00 15.36 C ANISOU 792 CG2 THR A 98 2402 1138 2296 85 -65 -327 C ATOM 793 N THR A 99 4.207 2.754 36.728 1.00 17.58 N ANISOU 793 N THR A 99 2213 2104 2359 199 -10 -165 N ATOM 794 CA THR A 99 4.606 3.294 35.442 1.00 19.34 C ANISOU 794 CA THR A 99 2605 2293 2448 219 101 -175 C ATOM 795 C THR A 99 4.881 2.192 34.413 1.00 19.89 C ANISOU 795 C THR A 99 2672 2429 2457 146 92 -171 C ATOM 796 O THR A 99 5.433 2.507 33.348 1.00 22.14 O ANISOU 796 O THR A 99 3163 2654 2592 247 295 -237 O ATOM 797 CB THR A 99 5.854 4.177 35.577 1.00 21.10 C ANISOU 797 CB THR A 99 2804 2650 2560 156 52 -179 C ATOM 798 OG1 THR A 99 6.926 3.432 36.183 1.00 23.58 O ANISOU 798 OG1 THR A 99 2758 3062 3139 86 -81 -184 O ATOM 799 CG2 THR A 99 5.570 5.339 36.526 1.00 23.06 C ANISOU 799 CG2 THR A 99 3258 2485 3018 86 138 -144 C ATOM 800 N ASP A 100 4.518 0.956 34.734 1.00 19.76 N ANISOU 800 N ASP A 100 2667 2355 2484 273 73 -187 N ATOM 801 CA ASP A 100 4.732 -0.220 33.836 1.00 21.41 C ANISOU 801 CA ASP A 100 2892 2603 2640 168 -25 -153 C ATOM 802 C ASP A 100 3.485 -1.082 33.690 1.00 20.98 C ANISOU 802 C ASP A 100 2857 2451 2663 186 -81 -121 C ATOM 803 O ASP A 100 3.523 -2.344 33.601 1.00 22.62 O ANISOU 803 O ASP A 100 3262 2258 3072 471 -148 -273 O ATOM 804 CB ASP A 100 5.948 -1.013 34.321 1.00 22.35 C ANISOU 804 CB ASP A 100 2958 2665 2869 160 -45 -183 C ATOM 805 CG ASP A 100 5.842 -1.441 35.738 1.00 24.72 C ANISOU 805 CG ASP A 100 3226 3177 2988 213 -94 -112 C ATOM 806 OD1 ASP A 100 6.923 -1.874 36.287 1.00 28.76 O ANISOU 806 OD1 ASP A 100 3480 3916 3530 626 -278 -350 O ATOM 807 OD2 ASP A 100 4.752 -1.457 36.373 1.00 22.65 O ANISOU 807 OD2 ASP A 100 3075 2754 2775 490 -290 -96 O ATOM 808 N HIS A 101 2.331 -0.432 33.678 1.00 19.43 N ANISOU 808 N HIS A 101 2746 2110 2526 302 -35 -163 N ATOM 809 CA HIS A 101 1.072 -1.089 33.433 1.00 20.10 C ANISOU 809 CA HIS A 101 2679 2391 2564 171 0 -119 C ATOM 810 C HIS A 101 0.782 -2.238 34.392 1.00 20.18 C ANISOU 810 C HIS A 101 2841 2208 2616 76 -65 -113 C ATOM 811 O HIS A 101 0.502 -3.372 33.985 1.00 22.20 O ANISOU 811 O HIS A 101 3207 2307 2921 86 -231 -304 O ATOM 812 CB HIS A 101 0.959 -1.504 31.955 1.00 20.50 C ANISOU 812 CB HIS A 101 2807 2505 2474 254 -51 -50 C ATOM 813 CG HIS A 101 -0.447 -1.729 31.511 1.00 23.49 C ANISOU 813 CG HIS A 101 2843 2971 3111 39 41 63 C ATOM 814 ND1 HIS A 101 -0.997 -2.971 31.303 1.00 25.57 N ANISOU 814 ND1 HIS A 101 3215 2949 3549 403 -43 -163 N ATOM 815 CD2 HIS A 101 -1.442 -0.835 31.277 1.00 27.51 C ANISOU 815 CD2 HIS A 101 3368 3207 3878 156 -64 -13 C ATOM 816 CE1 HIS A 101 -2.266 -2.839 30.954 1.00 27.13 C ANISOU 816 CE1 HIS A 101 3378 3374 3554 42 -61 -146 C ATOM 817 NE2 HIS A 101 -2.554 -1.546 30.905 1.00 27.67 N ANISOU 817 NE2 HIS A 101 3336 3434 3743 49 -140 -28 N ATOM 818 N TYR A 102 0.948 -1.935 35.697 1.00 20.55 N ANISOU 818 N TYR A 102 3007 2162 2636 30 -42 -142 N ATOM 819 CA TYR A 102 0.549 -2.755 36.832 1.00 21.98 C ANISOU 819 CA TYR A 102 3017 2548 2785 130 -70 -73 C ATOM 820 C TYR A 102 1.547 -3.902 37.126 1.00 23.02 C ANISOU 820 C TYR A 102 3255 2571 2919 76 -111 -85 C ATOM 821 O TYR A 102 1.230 -4.723 37.977 1.00 26.27 O ANISOU 821 O TYR A 102 3923 2618 3437 119 -226 -98 O ATOM 822 CB TYR A 102 -0.868 -3.335 36.715 1.00 22.41 C ANISOU 822 CB TYR A 102 3101 2583 2829 27 -4 -62 C ATOM 823 CG TYR A 102 -2.011 -2.466 36.180 1.00 21.78 C ANISOU 823 CG TYR A 102 2939 2470 2866 99 73 -181 C ATOM 824 CD1 TYR A 102 -2.452 -2.541 34.857 1.00 22.75 C ANISOU 824 CD1 TYR A 102 3014 2528 3101 135 41 -176 C ATOM 825 CD2 TYR A 102 -2.675 -1.558 37.012 1.00 23.77 C ANISOU 825 CD2 TYR A 102 3138 2821 3071 137 267 -89 C ATOM 826 CE1 TYR A 102 -3.523 -1.788 34.383 1.00 22.59 C ANISOU 826 CE1 TYR A 102 3108 2701 2774 118 38 -203 C ATOM 827 CE2 TYR A 102 -3.743 -0.827 36.546 1.00 19.92 C ANISOU 827 CE2 TYR A 102 2792 2171 2603 -148 233 15 C ATOM 828 CZ TYR A 102 -4.187 -0.913 35.255 1.00 21.52 C ANISOU 828 CZ TYR A 102 2897 2423 2855 -44 75 -163 C ATOM 829 OH TYR A 102 -5.238 -0.130 34.742 1.00 22.46 O ANISOU 829 OH TYR A 102 3118 2125 3287 -104 -15 -463 O ATOM 830 N ALA A 103 2.742 -3.872 36.549 1.00 22.90 N ANISOU 830 N ALA A 103 3266 2501 2931 265 -216 -138 N ATOM 831 CA ALA A 103 3.774 -4.910 36.851 1.00 24.51 C ANISOU 831 CA ALA A 103 3350 2841 3120 179 -197 -27 C ATOM 832 C ALA A 103 4.352 -4.698 38.242 1.00 24.80 C ANISOU 832 C ALA A 103 3579 2752 3088 119 -234 -51 C ATOM 833 O ALA A 103 4.518 -5.673 39.042 1.00 27.22 O ANISOU 833 O ALA A 103 4192 2805 3342 313 -356 -129 O ATOM 834 CB ALA A 103 4.873 -4.871 35.819 1.00 24.44 C ANISOU 834 CB ALA A 103 3337 2762 3186 221 -197 -31 C ATOM 835 N THR A 104 4.686 -3.442 38.544 1.00 23.67 N ANISOU 835 N THR A 104 3407 2593 2991 326 -208 -63 N ATOM 836 CA THR A 104 5.255 -3.084 39.834 1.00 22.89 C ANISOU 836 CA THR A 104 3266 2500 2928 357 -114 -241 C ATOM 837 C THR A 104 4.561 -1.817 40.362 1.00 21.78 C ANISOU 837 C THR A 104 3266 2332 2675 388 -74 -185 C ATOM 838 O THR A 104 4.064 -1.049 39.579 1.00 19.96 O ANISOU 838 O THR A 104 3359 1797 2427 652 -157 -398 O ATOM 839 CB THR A 104 6.747 -2.800 39.772 1.00 23.98 C ANISOU 839 CB THR A 104 3244 2850 3017 299 -25 -175 C ATOM 840 OG1 THR A 104 7.083 -1.701 38.945 1.00 25.30 O ANISOU 840 OG1 THR A 104 3272 3076 3261 426 -68 -285 O ATOM 841 CG2 THR A 104 7.538 -3.972 39.161 1.00 26.91 C ANISOU 841 CG2 THR A 104 3491 3274 3456 423 45 -268 C ATOM 842 N PHE A 105 4.527 -1.702 41.680 1.00 21.54 N ANISOU 842 N PHE A 105 3203 2290 2688 410 -157 -234 N ATOM 843 CA PHE A 105 3.899 -0.564 42.363 1.00 20.38 C ANISOU 843 CA PHE A 105 2866 2181 2693 297 -194 -115 C ATOM 844 C PHE A 105 4.860 0.031 43.375 1.00 20.94 C ANISOU 844 C PHE A 105 2986 2304 2665 305 -296 -96 C ATOM 845 O PHE A 105 5.657 -0.687 43.986 1.00 21.63 O ANISOU 845 O PHE A 105 3136 2157 2925 524 -557 -99 O ATOM 846 CB PHE A 105 2.658 -0.977 43.091 1.00 20.53 C ANISOU 846 CB PHE A 105 2976 2155 2666 340 -176 -69 C ATOM 847 CG PHE A 105 1.576 -1.487 42.221 1.00 23.18 C ANISOU 847 CG PHE A 105 3135 2642 3028 95 -148 -74 C ATOM 848 CD1 PHE A 105 1.457 -2.874 41.975 1.00 25.64 C ANISOU 848 CD1 PHE A 105 3449 2923 3367 92 -218 10 C ATOM 849 CD2 PHE A 105 0.658 -0.616 41.629 1.00 24.50 C ANISOU 849 CD2 PHE A 105 3201 2965 3140 143 -169 21 C ATOM 850 CE1 PHE A 105 0.429 -3.353 41.170 1.00 24.50 C ANISOU 850 CE1 PHE A 105 3533 2372 3401 -104 -110 -61 C ATOM 851 CE2 PHE A 105 -0.372 -1.103 40.818 1.00 24.43 C ANISOU 851 CE2 PHE A 105 3295 2905 3082 7 -212 79 C ATOM 852 CZ PHE A 105 -0.507 -2.473 40.609 1.00 25.96 C ANISOU 852 CZ PHE A 105 3278 3203 3380 36 -189 -133 C ATOM 853 N THR A 106 4.737 1.340 43.588 1.00 18.66 N ANISOU 853 N THR A 106 2605 2028 2455 231 -203 -167 N ATOM 854 CA THR A 106 5.507 2.110 44.584 1.00 19.12 C ANISOU 854 CA THR A 106 2529 2381 2354 130 -128 -160 C ATOM 855 C THR A 106 4.510 2.953 45.381 1.00 16.98 C ANISOU 855 C THR A 106 2279 2042 2130 72 -115 -99 C ATOM 856 O THR A 106 3.668 3.605 44.797 1.00 16.86 O ANISOU 856 O THR A 106 2290 2200 1915 104 -294 -115 O ATOM 857 CB THR A 106 6.483 3.088 43.888 1.00 19.63 C ANISOU 857 CB THR A 106 2261 2657 2539 79 7 -252 C ATOM 858 OG1 THR A 106 7.440 2.314 43.081 1.00 25.23 O ANISOU 858 OG1 THR A 106 3016 3336 3233 265 33 -327 O ATOM 859 CG2 THR A 106 7.334 3.808 44.926 1.00 22.66 C ANISOU 859 CG2 THR A 106 2825 2833 2951 3 100 -265 C ATOM 860 N ARG A 107 4.595 2.914 46.702 1.00 15.35 N ANISOU 860 N ARG A 107 2072 1778 1981 116 -157 -184 N ATOM 861 CA ARG A 107 3.729 3.733 47.534 1.00 14.21 C ANISOU 861 CA ARG A 107 1942 1619 1836 -74 -55 -73 C ATOM 862 C ARG A 107 4.181 5.180 47.484 1.00 13.37 C ANISOU 862 C ARG A 107 1789 1544 1745 -39 -44 -76 C ATOM 863 O ARG A 107 5.363 5.456 47.580 1.00 15.11 O ANISOU 863 O ARG A 107 2062 1565 2113 -136 -57 -274 O ATOM 864 CB ARG A 107 3.749 3.268 48.976 1.00 14.29 C ANISOU 864 CB ARG A 107 2037 1479 1911 -141 -88 -20 C ATOM 865 CG ARG A 107 2.784 4.008 49.827 1.00 15.18 C ANISOU 865 CG ARG A 107 2274 1533 1957 -80 57 95 C ATOM 866 CD ARG A 107 2.567 3.409 51.193 1.00 19.01 C ANISOU 866 CD ARG A 107 2662 2287 2274 -171 79 213 C ATOM 867 NE ARG A 107 1.783 4.290 51.984 1.00 18.75 N ANISOU 867 NE ARG A 107 2565 2420 2136 -23 -75 150 N ATOM 868 CZ ARG A 107 1.698 4.266 53.317 1.00 20.22 C ANISOU 868 CZ ARG A 107 2491 2864 2324 -87 90 195 C ATOM 869 NH1 ARG A 107 0.984 5.193 53.927 1.00 22.44 N ANISOU 869 NH1 ARG A 107 2967 3058 2501 -156 57 37 N ATOM 870 NH2 ARG A 107 2.290 3.294 54.019 1.00 23.73 N ANISOU 870 NH2 ARG A 107 3276 3037 2701 86 89 228 N ATOM 871 N ILE A 108 3.224 6.090 47.299 1.00 14.15 N ANISOU 871 N ILE A 108 1889 1439 2046 -82 -93 -36 N ATOM 872 CA ILE A 108 3.508 7.527 47.314 1.00 14.21 C ANISOU 872 CA ILE A 108 1915 1531 1953 -146 -16 -107 C ATOM 873 C ILE A 108 2.778 8.326 48.354 1.00 14.18 C ANISOU 873 C ILE A 108 1940 1522 1925 -128 55 -124 C ATOM 874 O ILE A 108 3.157 9.481 48.565 1.00 14.76 O ANISOU 874 O ILE A 108 2262 1239 2104 -116 -49 -138 O ATOM 875 CB ILE A 108 3.407 8.157 45.928 1.00 14.29 C ANISOU 875 CB ILE A 108 1989 1421 2017 40 -21 -33 C ATOM 876 CG1 ILE A 108 1.994 8.040 45.357 1.00 15.99 C ANISOU 876 CG1 ILE A 108 2119 1871 2085 -79 -52 -56 C ATOM 877 CG2 ILE A 108 4.466 7.540 45.001 1.00 17.44 C ANISOU 877 CG2 ILE A 108 2294 2124 2207 -100 73 -107 C ATOM 878 CD1 ILE A 108 1.793 8.893 44.171 1.00 17.50 C ANISOU 878 CD1 ILE A 108 2359 1930 2359 -148 -57 42 C ATOM 879 N ARG A 109 1.692 7.809 48.919 1.00 14.64 N ANISOU 879 N ARG A 109 2119 1556 1886 -197 8 -99 N ATOM 880 CA ARG A 109 1.020 8.401 50.084 1.00 16.02 C ANISOU 880 CA ARG A 109 2226 1956 1904 -154 84 -91 C ATOM 881 C ARG A 109 0.545 7.309 51.005 1.00 17.27 C ANISOU 881 C ARG A 109 2580 2005 1973 -122 143 -100 C ATOM 882 O ARG A 109 0.282 6.206 50.510 1.00 17.76 O ANISOU 882 O ARG A 109 2715 2087 1944 -318 142 13 O ATOM 883 CB ARG A 109 -0.156 9.286 49.743 1.00 15.71 C ANISOU 883 CB ARG A 109 2264 1846 1857 -97 28 -189 C ATOM 884 CG ARG A 109 0.092 10.418 48.756 1.00 16.74 C ANISOU 884 CG ARG A 109 2254 2061 2044 25 26 -112 C ATOM 885 CD ARG A 109 0.906 11.603 49.279 1.00 16.95 C ANISOU 885 CD ARG A 109 2189 2163 2088 -20 5 -228 C ATOM 886 NE ARG A 109 0.992 12.649 48.291 1.00 17.93 N ANISOU 886 NE ARG A 109 2361 2092 2358 -61 19 -206 N ATOM 887 CZ ARG A 109 1.849 12.695 47.241 1.00 16.99 C ANISOU 887 CZ ARG A 109 2289 1986 2178 -8 -7 -5 C ATOM 888 NH1 ARG A 109 1.817 13.736 46.409 1.00 18.63 N ANISOU 888 NH1 ARG A 109 2785 1635 2658 -50 -50 -78 N ATOM 889 NH2 ARG A 109 2.752 11.734 46.997 1.00 18.36 N ANISOU 889 NH2 ARG A 109 2437 2112 2424 -13 75 -176 N ATOM 890 OXT ARG A 109 0.472 7.561 52.232 1.00 18.85 O ANISOU 890 OXT ARG A 109 3032 2396 1732 -191 89 50 O TER 891 ARG A 109 ATOM 892 N ALA A 1 -0.056 -22.413 5.725 1.00 45.22 N ANISOU 892 N ALA B 1 5784 5663 5733 -11 -62 -96 N ATOM 893 CA ALA A 1 0.996 -22.342 6.785 1.00 44.27 C ANISOU 893 CA ALA B 1 5642 5542 5634 15 0 -53 C ATOM 894 C ALA A 1 0.891 -20.960 7.364 1.00 42.59 C ANISOU 894 C ALA B 1 5418 5409 5353 -35 28 -75 C ATOM 895 O ALA A 1 1.515 -20.019 6.799 1.00 43.69 O ANISOU 895 O ALA B 1 5640 5459 5498 -49 -23 -63 O ATOM 896 CB ALA A 1 2.406 -22.553 6.182 1.00 45.07 C ANISOU 896 CB ALA B 1 5677 5716 5729 1 23 -40 C ATOM 897 N VAL A 2 0.086 -20.774 8.427 1.00 39.36 N ANISOU 897 N VAL B 2 4971 4938 5043 -41 -48 -58 N ATOM 898 CA VAL A 2 0.021 -19.422 8.980 1.00 35.54 C ANISOU 898 CA VAL B 2 4463 4544 4497 -1 -88 -69 C ATOM 899 C VAL A 2 1.264 -19.156 9.848 1.00 31.13 C ANISOU 899 C VAL B 2 4010 3876 3940 -7 -26 -29 C ATOM 900 O VAL A 2 1.641 -19.946 10.710 1.00 31.68 O ANISOU 900 O VAL B 2 4074 3755 4205 53 -248 -36 O ATOM 901 CB VAL A 2 -1.323 -18.943 9.663 1.00 36.32 C ANISOU 901 CB VAL B 2 4544 4614 4640 -41 2 12 C ATOM 902 CG1 VAL A 2 -2.552 -19.465 8.946 1.00 37.51 C ANISOU 902 CG1 VAL B 2 4709 4794 4747 -52 -72 22 C ATOM 903 CG2 VAL A 2 -1.380 -19.151 11.151 1.00 38.14 C ANISOU 903 CG2 VAL B 2 4771 4967 4754 3 -101 -27 C ATOM 904 N ILE A 3 1.845 -18.011 9.602 1.00 25.24 N ANISOU 904 N ILE B 3 3274 3235 3079 112 -67 -118 N ATOM 905 CA ILE A 3 2.944 -17.489 10.384 1.00 22.41 C ANISOU 905 CA ILE B 3 2996 2766 2753 49 -15 -125 C ATOM 906 C ILE A 3 2.288 -16.317 11.151 1.00 19.76 C ANISOU 906 C ILE B 3 2688 2452 2366 102 3 -87 C ATOM 907 O ILE A 3 1.986 -15.290 10.557 1.00 18.90 O ANISOU 907 O ILE B 3 2689 2604 1886 193 -78 -176 O ATOM 908 CB ILE A 3 4.083 -17.005 9.504 1.00 22.54 C ANISOU 908 CB ILE B 3 2866 2956 2740 69 -40 -66 C ATOM 909 CG1 ILE A 3 4.669 -18.177 8.725 1.00 25.52 C ANISOU 909 CG1 ILE B 3 3358 3170 3167 -58 117 -217 C ATOM 910 CG2 ILE A 3 5.193 -16.313 10.339 1.00 21.60 C ANISOU 910 CG2 ILE B 3 2913 2536 2758 11 -7 -88 C ATOM 911 CD1 ILE A 3 5.661 -17.746 7.653 1.00 28.22 C ANISOU 911 CD1 ILE B 3 3626 3639 3455 -85 119 50 C ATOM 912 N ASN A 4 2.106 -16.463 12.459 1.00 18.49 N ANISOU 912 N ASN B 4 2594 2158 2271 154 -97 -35 N ATOM 913 CA ASN A 4 1.448 -15.408 13.234 1.00 17.13 C ANISOU 913 CA ASN B 4 2391 2019 2096 2 -82 -69 C ATOM 914 C ASN A 4 2.003 -15.204 14.659 1.00 16.68 C ANISOU 914 C ASN B 4 2325 1951 2061 62 -75 -77 C ATOM 915 O ASN A 4 1.287 -14.740 15.516 1.00 18.68 O ANISOU 915 O ASN B 4 2611 2396 2089 131 -122 -72 O ATOM 916 CB ASN A 4 -0.055 -15.638 13.271 1.00 17.72 C ANISOU 916 CB ASN B 4 2467 2014 2249 113 -63 -183 C ATOM 917 CG ASN A 4 -0.449 -16.850 14.135 1.00 17.67 C ANISOU 917 CG ASN B 4 2276 2122 2315 -44 -33 21 C ATOM 918 OD1 ASN A 4 0.415 -17.682 14.494 1.00 20.87 O ANISOU 918 OD1 ASN B 4 2732 2155 3040 117 -13 -16 O ATOM 919 ND2 ASN A 4 -1.727 -16.936 14.527 1.00 20.02 N ANISOU 919 ND2 ASN B 4 2531 2374 2699 -72 166 -255 N ATOM 920 N THR A 5 3.230 -15.665 14.896 1.00 16.77 N ANISOU 920 N THR B 5 2271 2009 2089 112 -134 -57 N ATOM 921 CA THR A 5 3.873 -15.492 16.175 1.00 16.24 C ANISOU 921 CA THR B 5 2247 1971 1950 129 -53 15 C ATOM 922 C THR A 5 4.797 -14.310 16.135 1.00 16.01 C ANISOU 922 C THR B 5 2186 2033 1864 96 -74 62 C ATOM 923 O THR A 5 5.229 -13.869 15.075 1.00 16.07 O ANISOU 923 O THR B 5 2419 1900 1785 57 152 -94 O ATOM 924 CB THR A 5 4.676 -16.732 16.592 1.00 17.66 C ANISOU 924 CB THR B 5 2430 2057 2222 125 22 121 C ATOM 925 OG1 THR A 5 5.650 -17.039 15.597 1.00 18.97 O ANISOU 925 OG1 THR B 5 2708 2023 2475 265 121 -163 O ATOM 926 CG2 THR A 5 3.776 -17.960 16.710 1.00 19.91 C ANISOU 926 CG2 THR B 5 2665 2422 2477 -36 -85 103 C ATOM 927 N PHE A 6 5.180 -13.833 17.305 1.00 15.91 N ANISOU 927 N PHE B 6 2239 2096 1708 26 0 -88 N ATOM 928 CA PHE A 6 6.080 -12.692 17.386 1.00 15.53 C ANISOU 928 CA PHE B 6 2184 1955 1760 90 -108 102 C ATOM 929 C PHE A 6 7.401 -12.983 16.675 1.00 16.15 C ANISOU 929 C PHE B 6 2262 2076 1798 68 -76 -68 C ATOM 930 O PHE A 6 7.810 -12.201 15.820 1.00 16.45 O ANISOU 930 O PHE B 6 2367 2152 1731 22 -114 -60 O ATOM 931 CB PHE A 6 6.394 -12.249 18.804 1.00 16.20 C ANISOU 931 CB PHE B 6 2251 2201 1704 136 -32 -109 C ATOM 932 CG PHE A 6 5.260 -11.562 19.508 1.00 17.20 C ANISOU 932 CG PHE B 6 2320 2198 2014 110 29 -34 C ATOM 933 CD1 PHE A 6 4.615 -12.173 20.605 1.00 19.11 C ANISOU 933 CD1 PHE B 6 2536 2533 2192 223 246 14 C ATOM 934 CD2 PHE A 6 4.827 -10.352 19.099 1.00 18.13 C ANISOU 934 CD2 PHE B 6 2370 2431 2086 112 -58 -105 C ATOM 935 CE1 PHE A 6 3.559 -11.496 21.263 1.00 19.34 C ANISOU 935 CE1 PHE B 6 2689 2487 2169 46 232 -7 C ATOM 936 CE2 PHE A 6 3.753 -9.710 19.751 1.00 19.34 C ANISOU 936 CE2 PHE B 6 2622 2326 2398 90 67 -240 C ATOM 937 CZ PHE A 6 3.141 -10.300 20.796 1.00 19.52 C ANISOU 937 CZ PHE B 6 2699 2461 2255 181 134 -295 C ATOM 938 N ASP A 7 8.036 -14.122 17.012 1.00 16.66 N ANISOU 938 N ASP B 7 2338 2073 1916 75 -18 7 N ATOM 939 CA ASP A 7 9.313 -14.461 16.379 1.00 17.17 C ANISOU 939 CA ASP B 7 2294 2188 2041 141 -75 -48 C ATOM 940 C ASP A 7 9.153 -14.805 14.904 1.00 17.04 C ANISOU 940 C ASP B 7 2295 2122 2056 137 -55 -17 C ATOM 941 O ASP A 7 9.990 -14.399 14.091 1.00 18.18 O ANISOU 941 O ASP B 7 2418 2441 2048 244 35 -120 O ATOM 942 CB ASP A 7 10.026 -15.586 17.097 1.00 17.88 C ANISOU 942 CB ASP B 7 2468 2090 2233 129 -95 -104 C ATOM 943 CG ASP A 7 10.681 -15.110 18.367 1.00 21.15 C ANISOU 943 CG ASP B 7 2823 2760 2452 -17 -177 23 C ATOM 944 OD1 ASP A 7 10.363 -15.655 19.421 1.00 25.91 O ANISOU 944 OD1 ASP B 7 3944 3316 2585 -86 30 180 O ATOM 945 OD2 ASP A 7 11.479 -14.164 18.383 1.00 21.08 O ANISOU 945 OD2 ASP B 7 2977 2629 2402 -39 -275 -33 O ATOM 946 N GLY A 8 8.100 -15.536 14.579 1.00 17.96 N ANISOU 946 N GLY B 8 2347 2413 2063 217 -59 -17 N ATOM 947 CA GLY A 8 7.922 -15.978 13.197 1.00 17.95 C ANISOU 947 CA GLY B 8 2361 2338 2121 80 -93 -70 C ATOM 948 C GLY A 8 7.707 -14.813 12.244 1.00 16.95 C ANISOU 948 C GLY B 8 2222 2175 2043 71 2 -71 C ATOM 949 O GLY A 8 8.326 -14.752 11.170 1.00 19.40 O ANISOU 949 O GLY B 8 2640 2580 2150 121 -9 -16 O ATOM 950 N VAL A 9 6.839 -13.885 12.623 1.00 17.10 N ANISOU 950 N VAL B 9 2162 2379 1955 93 21 -102 N ATOM 951 CA VAL A 9 6.549 -12.720 11.807 1.00 17.45 C ANISOU 951 CA VAL B 9 2201 2427 2002 205 28 -152 C ATOM 952 C VAL A 9 7.754 -11.789 11.781 1.00 17.06 C ANISOU 952 C VAL B 9 2234 2278 1967 170 72 -110 C ATOM 953 O VAL A 9 8.096 -11.298 10.728 1.00 18.54 O ANISOU 953 O VAL B 9 2454 2580 2007 283 -42 -36 O ATOM 954 CB VAL A 9 5.237 -11.989 12.259 1.00 16.68 C ANISOU 954 CB VAL B 9 2100 2217 2019 203 105 -154 C ATOM 955 CG1 VAL A 9 5.007 -10.671 11.476 1.00 17.96 C ANISOU 955 CG1 VAL B 9 2314 2547 1962 105 -55 -17 C ATOM 956 CG2 VAL A 9 4.051 -12.926 12.153 1.00 17.32 C ANISOU 956 CG2 VAL B 9 2318 2200 2060 271 -15 -110 C ATOM 957 N ALA A 10 8.430 -11.556 12.931 1.00 16.80 N ANISOU 957 N ALA B 10 2121 2449 1810 128 45 -114 N ATOM 958 CA ALA A 10 9.606 -10.704 12.944 1.00 16.92 C ANISOU 958 CA ALA B 10 2186 2308 1935 105 44 -101 C ATOM 959 C ALA A 10 10.681 -11.251 11.970 1.00 18.11 C ANISOU 959 C ALA B 10 2304 2567 2007 13 18 -90 C ATOM 960 O ALA A 10 11.226 -10.492 11.222 1.00 19.72 O ANISOU 960 O ALA B 10 2428 3028 2034 126 0 -8 O ATOM 961 CB ALA A 10 10.207 -10.599 14.346 1.00 17.81 C ANISOU 961 CB ALA B 10 2239 2409 2118 29 20 -50 C ATOM 962 N ASP A 11 10.946 -12.546 12.043 1.00 19.39 N ANISOU 962 N ASP B 11 2423 2810 2132 187 0 -102 N ATOM 963 CA ASP A 11 11.989 -13.162 11.223 1.00 19.96 C ANISOU 963 CA ASP B 11 2545 2878 2161 112 48 -117 C ATOM 964 C ASP A 11 11.600 -13.146 9.740 1.00 20.77 C ANISOU 964 C ASP B 11 2557 3112 2222 123 -35 -57 C ATOM 965 O ASP A 11 12.481 -12.985 8.879 1.00 22.62 O ANISOU 965 O ASP B 11 2645 3657 2291 166 -18 -40 O ATOM 966 CB ASP A 11 12.288 -14.579 11.666 1.00 20.89 C ANISOU 966 CB ASP B 11 2649 2979 2308 140 29 -111 C ATOM 967 CG ASP A 11 13.063 -14.630 12.967 1.00 24.00 C ANISOU 967 CG ASP B 11 2903 3330 2883 92 -97 -18 C ATOM 968 OD1 ASP A 11 13.652 -13.606 13.386 1.00 24.27 O ANISOU 968 OD1 ASP B 11 2783 3862 2576 415 -359 -561 O ATOM 969 OD2 ASP A 11 13.104 -15.681 13.595 1.00 29.22 O ANISOU 969 OD2 ASP B 11 3602 4218 3279 386 -101 356 O ATOM 970 N TYR A 12 10.316 -13.343 9.475 1.00 19.87 N ANISOU 970 N TYR B 12 2551 3030 1967 201 18 -165 N ATOM 971 CA TYR A 12 9.809 -13.276 8.099 1.00 20.40 C ANISOU 971 CA TYR B 12 2565 2994 2190 117 -11 -70 C ATOM 972 C TYR A 12 10.001 -11.873 7.545 1.00 20.16 C ANISOU 972 C TYR B 12 2540 2869 2251 99 33 -58 C ATOM 973 O TYR A 12 10.409 -11.726 6.394 1.00 21.10 O ANISOU 973 O TYR B 12 2690 3236 2090 193 100 -161 O ATOM 974 CB TYR A 12 8.356 -13.694 8.045 1.00 20.00 C ANISOU 974 CB TYR B 12 2611 2955 2032 106 -79 -58 C ATOM 975 CG TYR A 12 7.853 -13.941 6.640 1.00 19.47 C ANISOU 975 CG TYR B 12 2618 2782 1995 86 -60 -34 C ATOM 976 CD1 TYR A 12 7.773 -15.251 6.156 1.00 22.88 C ANISOU 976 CD1 TYR B 12 3037 3223 2431 26 -105 -174 C ATOM 977 CD2 TYR A 12 7.405 -12.874 5.860 1.00 19.70 C ANISOU 977 CD2 TYR B 12 2751 2776 1955 151 98 -144 C ATOM 978 CE1 TYR A 12 7.270 -15.522 4.880 1.00 22.56 C ANISOU 978 CE1 TYR B 12 3173 3111 2285 187 -62 -270 C ATOM 979 CE2 TYR A 12 6.928 -13.127 4.527 1.00 21.37 C ANISOU 979 CE2 TYR B 12 2820 3133 2163 103 -176 -261 C ATOM 980 CZ TYR A 12 6.857 -14.470 4.087 1.00 21.81 C ANISOU 980 CZ TYR B 12 3183 2817 2284 41 -82 -27 C ATOM 981 OH TYR A 12 6.383 -14.782 2.806 1.00 24.38 O ANISOU 981 OH TYR B 12 3452 3760 2048 249 -74 -390 O ATOM 982 N LEU A 13 9.673 -10.819 8.309 1.00 19.56 N ANISOU 982 N LEU B 13 2400 2849 2182 161 18 -69 N ATOM 983 CA LEU A 13 9.838 -9.430 7.904 1.00 21.17 C ANISOU 983 CA LEU B 13 2607 3010 2425 -34 38 85 C ATOM 984 C LEU A 13 11.274 -9.092 7.539 1.00 22.57 C ANISOU 984 C LEU B 13 2732 3200 2641 3 22 102 C ATOM 985 O LEU A 13 11.528 -8.424 6.537 1.00 24.25 O ANISOU 985 O LEU B 13 2974 3715 2521 -61 181 294 O ATOM 986 CB LEU A 13 9.341 -8.423 8.970 1.00 20.70 C ANISOU 986 CB LEU B 13 2643 2866 2353 13 -7 162 C ATOM 987 CG LEU A 13 7.830 -8.223 9.061 1.00 20.40 C ANISOU 987 CG LEU B 13 2767 2425 2556 74 18 98 C ATOM 988 CD1 LEU A 13 7.404 -7.589 10.378 1.00 24.39 C ANISOU 988 CD1 LEU B 13 3100 3380 2787 46 87 87 C ATOM 989 CD2 LEU A 13 7.344 -7.373 7.924 1.00 22.47 C ANISOU 989 CD2 LEU B 13 2768 3264 2503 176 -45 40 C ATOM 990 N ILE A 14 12.200 -9.544 8.357 1.00 22.57 N ANISOU 990 N ILE B 14 2810 3229 2536 81 86 196 N ATOM 991 CA ILE A 14 13.605 -9.251 8.125 1.00 24.52 C ANISOU 991 CA ILE B 14 2991 3339 2986 52 -9 107 C ATOM 992 C ILE A 14 14.065 -9.998 6.846 1.00 24.91 C ANISOU 992 C ILE B 14 3077 3411 2973 50 13 120 C ATOM 993 O ILE A 14 14.832 -9.452 6.103 1.00 26.99 O ANISOU 993 O ILE B 14 3125 3980 3147 91 42 289 O ATOM 994 CB ILE A 14 14.453 -9.651 9.364 1.00 25.09 C ANISOU 994 CB ILE B 14 3095 3422 3014 -5 -17 65 C ATOM 995 CG1 ILE A 14 13.985 -8.853 10.598 1.00 26.33 C ANISOU 995 CG1 ILE B 14 3166 3512 3326 43 17 60 C ATOM 996 CG2 ILE A 14 15.989 -9.539 9.087 1.00 27.12 C ANISOU 996 CG2 ILE B 14 3248 3719 3335 40 23 50 C ATOM 997 CD1AILE A 14 14.444 -7.401 10.713 0.50 25.99 C ANISOU 997 CD1AILE B 14 3214 3382 3277 111 -6 49 C ATOM 998 CD1BILE A 14 14.814 -8.653 11.892 0.50 27.17 C ANISOU 998 CD1BILE B 14 3433 3515 3374 -48 -27 25 C ATOM 999 N ARG A 15 13.647 -11.232 6.626 1.00 25.67 N ANISOU 999 N ARG B 15 3219 3520 3013 58 66 109 N ATOM 1000 CA ARG A 15 14.125 -12.006 5.480 1.00 26.50 C ANISOU 1000 CA ARG B 15 3322 3601 3143 82 65 39 C ATOM 1001 C ARG A 15 13.476 -11.572 4.175 1.00 26.76 C ANISOU 1001 C ARG B 15 3276 3833 3055 127 112 63 C ATOM 1002 O ARG A 15 14.175 -11.469 3.150 1.00 27.87 O ANISOU 1002 O ARG B 15 3323 4287 2979 223 370 148 O ATOM 1003 CB ARG A 15 13.895 -13.492 5.687 1.00 28.43 C ANISOU 1003 CB ARG B 15 3582 3764 3455 67 -7 49 C ATOM 1004 CG ARG A 15 14.375 -14.381 4.557 1.00 33.05 C ANISOU 1004 CG ARG B 15 4224 4415 3917 201 49 -105 C ATOM 1005 CD ARG A 15 14.022 -15.820 4.828 1.00 41.77 C ANISOU 1005 CD ARG B 15 5407 5170 5291 -105 7 66 C ATOM 1006 NE ARG A 15 14.768 -16.922 4.187 1.00 49.66 N ANISOU 1006 NE ARG B 15 6331 6164 6374 152 24 -166 N ATOM 1007 CZ ARG A 15 15.388 -16.952 2.979 1.00 54.41 C ANISOU 1007 CZ ARG B 15 6929 6997 6747 15 123 -38 C ATOM 1008 NH1 ARG A 15 15.456 -15.911 2.116 1.00 56.50 N ANISOU 1008 NH1 ARG B 15 7244 7046 7177 20 12 48 N ATOM 1009 NH2 ARG A 15 15.982 -18.099 2.628 1.00 56.69 N ANISOU 1009 NH2 ARG B 15 7228 7060 7252 105 58 -5 N ATOM 1010 N TYR A 16 12.175 -11.328 4.196 1.00 25.75 N ANISOU 1010 N TYR B 16 3201 3730 2853 123 129 67 N ATOM 1011 CA TYR A 16 11.404 -11.081 2.963 1.00 25.61 C ANISOU 1011 CA TYR B 16 3220 3631 2879 57 70 19 C ATOM 1012 C TYR A 16 10.970 -9.639 2.784 1.00 25.31 C ANISOU 1012 C TYR B 16 3096 3612 2906 83 70 36 C ATOM 1013 O TYR A 16 10.449 -9.281 1.698 1.00 26.51 O ANISOU 1013 O TYR B 16 3289 4169 2612 25 174 13 O ATOM 1014 CB TYR A 16 10.234 -12.035 2.897 1.00 25.61 C ANISOU 1014 CB TYR B 16 3401 3529 2800 48 37 -21 C ATOM 1015 CG TYR A 16 10.609 -13.490 2.819 1.00 29.45 C ANISOU 1015 CG TYR B 16 3800 3829 3558 209 43 -59 C ATOM 1016 CD1 TYR A 16 11.209 -14.030 1.657 1.00 33.17 C ANISOU 1016 CD1 TYR B 16 4436 4376 3789 100 144 -126 C ATOM 1017 CD2 TYR A 16 10.393 -14.335 3.881 1.00 29.28 C ANISOU 1017 CD2 TYR B 16 3821 3886 3418 73 112 -51 C ATOM 1018 CE1 TYR A 16 11.567 -15.397 1.586 1.00 35.31 C ANISOU 1018 CE1 TYR B 16 4689 4410 4318 25 95 -11 C ATOM 1019 CE2 TYR A 16 10.736 -15.698 3.833 1.00 33.50 C ANISOU 1019 CE2 TYR B 16 4393 4225 4108 20 28 -50 C ATOM 1020 CZ TYR A 16 11.323 -16.226 2.671 1.00 36.10 C ANISOU 1020 CZ TYR B 16 4739 4594 4381 79 127 -40 C ATOM 1021 OH TYR A 16 11.653 -17.547 2.650 1.00 38.95 O ANISOU 1021 OH TYR B 16 5218 4758 4823 192 165 -53 O ATOM 1022 N LYS A 17 11.125 -8.791 3.813 1.00 24.98 N ANISOU 1022 N LYS B 17 3051 3607 2833 -30 64 124 N ATOM 1023 CA LYS A 17 10.825 -7.366 3.776 1.00 25.23 C ANISOU 1023 CA LYS B 17 3069 3470 3045 -37 87 92 C ATOM 1024 C LYS A 17 9.337 -7.043 3.476 1.00 24.89 C ANISOU 1024 C LYS B 17 3047 3378 3031 -65 95 144 C ATOM 1025 O LYS A 17 8.989 -5.959 2.994 1.00 24.74 O ANISOU 1025 O LYS B 17 2842 3551 3004 -66 262 371 O ATOM 1026 CB LYS A 17 11.790 -6.644 2.796 1.00 27.63 C ANISOU 1026 CB LYS B 17 3369 3734 3395 -88 94 108 C ATOM 1027 CG LYS A 17 13.305 -6.981 3.064 1.00 31.67 C ANISOU 1027 CG LYS B 17 3677 4222 4134 47 101 118 C ATOM 1028 CD LYS A 17 13.764 -6.470 4.412 1.00 38.02 C ANISOU 1028 CD LYS B 17 4759 4947 4738 -28 -48 -7 C ATOM 1029 CE LYS A 17 15.328 -6.435 4.566 1.00 41.31 C ANISOU 1029 CE LYS B 17 4967 5327 5400 15 8 17 C ATOM 1030 NZ LYS A 17 15.963 -7.698 4.069 1.00 43.22 N ANISOU 1030 NZ LYS B 17 5329 5451 5640 61 56 -38 N ATOM 1031 N ARG A 18 8.477 -8.000 3.822 1.00 22.77 N ANISOU 1031 N ARG B 18 2785 3188 2678 -57 35 124 N ATOM 1032 CA ARG A 18 7.034 -7.855 3.715 1.00 22.24 C ANISOU 1032 CA ARG B 18 2727 3044 2678 15 58 118 C ATOM 1033 C ARG A 18 6.405 -8.809 4.731 1.00 20.54 C ANISOU 1033 C ARG B 18 2527 2908 2369 52 76 172 C ATOM 1034 O ARG A 18 7.063 -9.743 5.183 1.00 20.84 O ANISOU 1034 O ARG B 18 2442 3285 2190 113 217 212 O ATOM 1035 CB ARG A 18 6.534 -8.163 2.301 1.00 21.48 C ANISOU 1035 CB ARG B 18 2684 2832 2646 -38 11 111 C ATOM 1036 CG ARG A 18 6.665 -9.612 1.856 1.00 22.39 C ANISOU 1036 CG ARG B 18 2865 3091 2550 86 -5 -6 C ATOM 1037 CD ARG A 18 6.266 -9.879 0.376 1.00 23.73 C ANISOU 1037 CD ARG B 18 3088 3376 2551 -15 -44 95 C ATOM 1038 NE ARG A 18 6.305 -11.290 0.138 1.00 25.31 N ANISOU 1038 NE ARG B 18 3270 3783 2562 78 64 10 N ATOM 1039 CZ ARG A 18 7.320 -11.967 -0.398 1.00 25.38 C ANISOU 1039 CZ ARG B 18 3225 3626 2790 41 -55 -106 C ATOM 1040 NH1 ARG A 18 8.421 -11.334 -0.818 1.00 26.21 N ANISOU 1040 NH1 ARG B 18 3251 3889 2817 8 107 10 N ATOM 1041 NH2 ARG A 18 7.235 -13.282 -0.501 1.00 26.92 N ANISOU 1041 NH2 ARG B 18 3471 3789 2968 2 48 16 N ATOM 1042 N LEU A 19 5.129 -8.629 5.020 1.00 20.45 N ANISOU 1042 N LEU B 19 2530 2961 2276 62 26 137 N ATOM 1043 CA LEU A 19 4.395 -9.588 5.874 1.00 19.98 C ANISOU 1043 CA LEU B 19 2476 2834 2282 100 22 77 C ATOM 1044 C LEU A 19 4.115 -10.918 5.209 1.00 19.72 C ANISOU 1044 C LEU B 19 2366 3006 2120 64 8 81 C ATOM 1045 O LEU A 19 3.997 -10.934 3.953 1.00 21.05 O ANISOU 1045 O LEU B 19 2620 3565 1813 52 106 -28 O ATOM 1046 CB LEU A 19 3.058 -8.974 6.356 1.00 19.15 C ANISOU 1046 CB LEU B 19 2405 2680 2189 182 68 98 C ATOM 1047 CG LEU A 19 3.183 -7.776 7.317 1.00 20.40 C ANISOU 1047 CG LEU B 19 2526 2657 2568 -71 -50 60 C ATOM 1048 CD1 LEU A 19 1.849 -7.078 7.488 1.00 21.24 C ANISOU 1048 CD1 LEU B 19 2792 2581 2698 -10 35 147 C ATOM 1049 CD2 LEU A 19 3.674 -8.237 8.694 1.00 21.62 C ANISOU 1049 CD2 LEU B 19 2713 2908 2594 93 53 80 C ATOM 1050 N PRO A 20 3.941 -12.013 5.971 1.00 20.17 N ANISOU 1050 N PRO B 20 2540 2935 2188 71 -25 0 N ATOM 1051 CA PRO A 20 3.489 -13.276 5.438 1.00 19.99 C ANISOU 1051 CA PRO B 20 2573 2789 2230 27 106 47 C ATOM 1052 C PRO A 20 2.127 -13.138 4.743 1.00 19.88 C ANISOU 1052 C PRO B 20 2559 2769 2224 0 75 9 C ATOM 1053 O PRO A 20 1.363 -12.163 4.948 1.00 20.08 O ANISOU 1053 O PRO B 20 2699 3036 1891 137 -7 -21 O ATOM 1054 CB PRO A 20 3.361 -14.174 6.687 1.00 21.27 C ANISOU 1054 CB PRO B 20 2709 2788 2583 -14 -33 99 C ATOM 1055 CG PRO A 20 4.029 -13.511 7.760 1.00 21.50 C ANISOU 1055 CG PRO B 20 2824 2981 2362 10 69 -82 C ATOM 1056 CD PRO A 20 4.256 -12.128 7.423 1.00 19.20 C ANISOU 1056 CD PRO B 20 2542 2848 1904 155 163 49 C ATOM 1057 N ASN A 21 1.811 -14.139 3.917 1.00 21.50 N ANISOU 1057 N ASN B 21 2751 2969 2447 33 31 -127 N ATOM 1058 CA ASN A 21 0.596 -14.079 3.074 1.00 22.10 C ANISOU 1058 CA ASN B 21 2765 3033 2600 39 -2 -123 C ATOM 1059 C ASN A 21 -0.732 -14.195 3.811 1.00 21.93 C ANISOU 1059 C ASN B 21 2782 3071 2479 64 5 -114 C ATOM 1060 O ASN A 21 -1.780 -13.880 3.254 1.00 22.47 O ANISOU 1060 O ASN B 21 2952 3463 2121 264 44 -211 O ATOM 1061 CB ASN A 21 0.643 -15.197 2.009 1.00 22.84 C ANISOU 1061 CB ASN B 21 2997 2984 2697 0 -56 -133 C ATOM 1062 CG ASN A 21 1.817 -15.045 1.040 1.00 25.43 C ANISOU 1062 CG ASN B 21 3253 3410 2999 7 -18 13 C ATOM 1063 OD1 ASN A 21 2.309 -13.960 0.825 1.00 27.15 O ANISOU 1063 OD1 ASN B 21 3836 3717 2761 -160 -44 238 O ATOM 1064 ND2 ASN A 21 2.246 -16.135 0.477 1.00 28.11 N ANISOU 1064 ND2 ASN B 21 3814 3846 3017 296 127 -283 N ATOM 1065 N ASP A 22 -0.681 -14.574 5.085 1.00 21.04 N ANISOU 1065 N ASP B 22 2657 2890 2446 72 -13 -67 N ATOM 1066 CA ASP A 22 -1.870 -14.655 5.927 1.00 20.70 C ANISOU 1066 CA ASP B 22 2589 2735 2537 59 1 -89 C ATOM 1067 C ASP A 22 -2.316 -13.273 6.484 1.00 20.16 C ANISOU 1067 C ASP B 22 2565 2648 2446 20 -12 -85 C ATOM 1068 O ASP A 22 -3.284 -13.229 7.244 1.00 22.84 O ANISOU 1068 O ASP B 22 2922 2833 2920 -55 220 -68 O ATOM 1069 CB ASP A 22 -1.686 -15.683 7.051 1.00 20.68 C ANISOU 1069 CB ASP B 22 2688 2786 2382 58 105 -134 C ATOM 1070 CG ASP A 22 -0.538 -15.390 7.929 1.00 23.19 C ANISOU 1070 CG ASP B 22 2771 3388 2648 142 -12 -122 C ATOM 1071 OD1 ASP A 22 0.591 -15.680 7.464 1.00 25.13 O ANISOU 1071 OD1 ASP B 22 3068 4273 2205 223 -116 68 O ATOM 1072 OD2 ASP A 22 -0.652 -14.917 9.111 1.00 23.98 O ANISOU 1072 OD2 ASP B 22 3307 3204 2598 161 -47 -166 O ATOM 1073 N TYR A 23 -1.651 -12.185 6.139 1.00 19.68 N ANISOU 1073 N TYR B 23 2504 2789 2184 135 43 28 N ATOM 1074 CA TYR A 23 -2.054 -10.854 6.538 1.00 18.23 C ANISOU 1074 CA TYR B 23 2434 2494 2000 159 54 116 C ATOM 1075 C TYR A 23 -2.806 -10.100 5.447 1.00 19.25 C ANISOU 1075 C TYR B 23 2525 2732 2057 185 81 113 C ATOM 1076 O TYR A 23 -2.395 -10.142 4.277 1.00 20.39 O ANISOU 1076 O TYR B 23 2878 3085 1781 291 196 302 O ATOM 1077 CB TYR A 23 -0.876 -10.032 7.007 1.00 18.11 C ANISOU 1077 CB TYR B 23 2465 2487 1928 195 75 131 C ATOM 1078 CG TYR A 23 -0.412 -10.502 8.361 1.00 15.81 C ANISOU 1078 CG TYR B 23 2164 2203 1639 315 30 -44 C ATOM 1079 CD1 TYR A 23 0.575 -11.475 8.486 1.00 17.19 C ANISOU 1079 CD1 TYR B 23 2410 2239 1881 210 -31 -31 C ATOM 1080 CD2 TYR A 23 -0.978 -9.983 9.507 1.00 16.98 C ANISOU 1080 CD2 TYR B 23 2474 2184 1793 215 -12 0 C ATOM 1081 CE1 TYR A 23 0.963 -11.952 9.731 1.00 17.75 C ANISOU 1081 CE1 TYR B 23 2352 2422 1970 288 -101 -60 C ATOM 1082 CE2 TYR A 23 -0.573 -10.409 10.735 1.00 17.95 C ANISOU 1082 CE2 TYR B 23 2472 2603 1743 222 -31 -89 C ATOM 1083 CZ TYR A 23 0.365 -11.407 10.869 1.00 18.71 C ANISOU 1083 CZ TYR B 23 2452 2660 1996 202 5 -24 C ATOM 1084 OH TYR A 23 0.766 -11.833 12.123 1.00 17.67 O ANISOU 1084 OH TYR B 23 2481 2467 1766 342 34 14 O ATOM 1085 N ILE A 24 -3.867 -9.414 5.853 1.00 18.49 N ANISOU 1085 N ILE B 24 2331 2629 2064 135 56 169 N ATOM 1086 CA ILE A 24 -4.591 -8.449 5.011 1.00 19.10 C ANISOU 1086 CA ILE B 24 2445 2589 2221 96 59 134 C ATOM 1087 C ILE A 24 -4.783 -7.168 5.798 1.00 19.63 C ANISOU 1087 C ILE B 24 2567 2578 2312 23 -41 169 C ATOM 1088 O ILE A 24 -4.892 -7.168 7.040 1.00 19.86 O ANISOU 1088 O ILE B 24 2627 2721 2198 -16 -28 358 O ATOM 1089 CB ILE A 24 -5.923 -9.018 4.477 1.00 19.38 C ANISOU 1089 CB ILE B 24 2548 2415 2399 -76 45 77 C ATOM 1090 CG1 ILE A 24 -6.935 -9.308 5.601 1.00 19.95 C ANISOU 1090 CG1 ILE B 24 2687 2476 2416 -52 144 -78 C ATOM 1091 CG2 ILE A 24 -5.672 -10.309 3.586 1.00 21.67 C ANISOU 1091 CG2 ILE B 24 2815 2897 2522 16 -4 -82 C ATOM 1092 CD1 ILE A 24 -8.328 -9.720 5.124 1.00 22.19 C ANISOU 1092 CD1 ILE B 24 2690 3084 2657 128 -1 101 C ATOM 1093 N THR A 25 -4.886 -6.040 5.100 1.00 19.39 N ANISOU 1093 N THR B 25 2652 2527 2185 -20 -98 300 N ATOM 1094 CA THR A 25 -5.066 -4.747 5.770 1.00 20.03 C ANISOU 1094 CA THR B 25 2614 2633 2363 79 -156 217 C ATOM 1095 C THR A 25 -6.507 -4.564 6.222 1.00 19.14 C ANISOU 1095 C THR B 25 2580 2490 2200 17 -78 280 C ATOM 1096 O THR A 25 -7.407 -5.306 5.807 1.00 19.38 O ANISOU 1096 O THR B 25 2673 2399 2292 188 -178 311 O ATOM 1097 CB THR A 25 -4.697 -3.587 4.852 1.00 21.42 C ANISOU 1097 CB THR B 25 2748 2851 2537 -81 -3 197 C ATOM 1098 OG1 THR A 25 -5.631 -3.559 3.741 1.00 23.36 O ANISOU 1098 OG1 THR B 25 2815 3339 2721 203 -166 202 O ATOM 1099 CG2 THR A 25 -3.293 -3.769 4.284 1.00 23.27 C ANISOU 1099 CG2 THR B 25 2880 3005 2954 60 -31 188 C ATOM 1100 N LYS A 26 -6.731 -3.577 7.064 1.00 20.67 N ANISOU 1100 N LYS B 26 2693 2613 2547 47 -155 245 N ATOM 1101 CA LYS A 26 -8.079 -3.275 7.521 1.00 22.16 C ANISOU 1101 CA LYS B 26 2861 2881 2676 14 -33 108 C ATOM 1102 C LYS A 26 -9.032 -2.982 6.355 1.00 22.76 C ANISOU 1102 C LYS B 26 2868 2903 2876 25 -78 127 C ATOM 1103 O LYS A 26 -10.162 -3.485 6.330 1.00 23.29 O ANISOU 1103 O LYS B 26 2910 3105 2832 -26 -90 216 O ATOM 1104 CB LYS A 26 -8.094 -2.138 8.521 1.00 22.69 C ANISOU 1104 CB LYS B 26 3009 2659 2952 90 -61 123 C ATOM 1105 CG LYS A 26 -7.655 -2.527 9.928 1.00 26.46 C ANISOU 1105 CG LYS B 26 3420 3494 3137 49 -101 -15 C ATOM 1106 CD LYS A 26 -7.793 -1.312 10.934 1.00 32.18 C ANISOU 1106 CD LYS B 26 4247 3887 4091 175 -79 -208 C ATOM 1107 CE LYS A 26 -6.563 -0.409 10.912 1.00 37.86 C ANISOU 1107 CE LYS B 26 4763 4739 4881 -75 18 -60 C ATOM 1108 NZ LYS A 26 -6.607 0.608 9.797 1.00 43.50 N ANISOU 1108 NZ LYS B 26 5673 5443 5412 86 13 85 N ATOM 1109 N SER A 27 -8.546 -2.260 5.362 1.00 23.58 N ANISOU 1109 N SER B 27 2960 3116 2882 67 -37 129 N ATOM 1110 CA SER A 27 -9.387 -1.908 4.189 1.00 24.99 C ANISOU 1110 CA SER B 27 3141 3274 3078 37 -73 117 C ATOM 1111 C SER A 27 -9.737 -3.159 3.358 1.00 22.88 C ANISOU 1111 C SER B 27 2864 3032 2796 55 16 191 C ATOM 1112 O SER A 27 -10.884 -3.298 2.858 1.00 23.99 O ANISOU 1112 O SER B 27 2940 3304 2870 66 -143 187 O ATOM 1113 CB SER A 27 -8.720 -0.783 3.357 1.00 26.08 C ANISOU 1113 CB SER B 27 3255 3293 3360 39 11 96 C ATOM 1114 OG ASER A 27 -7.671 -1.369 2.641 0.60 26.66 O ANISOU 1114 OG ASER B 27 3447 3376 3306 112 93 77 O ATOM 1115 OG BSER A 27 -9.239 0.421 3.868 0.40 28.30 O ANISOU 1115 OG BSER B 27 3682 3474 3595 71 -21 -103 O ATOM 1116 N GLN A 28 -8.767 -4.074 3.216 1.00 20.85 N ANISOU 1116 N GLN B 28 2645 2868 2406 45 -27 248 N ATOM 1117 CA GLN A 28 -8.983 -5.345 2.560 1.00 19.75 C ANISOU 1117 CA GLN B 28 2565 2645 2292 88 -12 228 C ATOM 1118 C GLN A 28 -9.981 -6.233 3.291 1.00 20.02 C ANISOU 1118 C GLN B 28 2595 2716 2294 33 -1 98 C ATOM 1119 O GLN A 28 -10.808 -6.895 2.676 1.00 21.18 O ANISOU 1119 O GLN B 28 2736 3141 2170 -11 42 251 O ATOM 1120 CB GLN A 28 -7.666 -6.085 2.334 1.00 19.51 C ANISOU 1120 CB GLN B 28 2427 2695 2291 -8 124 129 C ATOM 1121 CG GLN A 28 -6.768 -5.422 1.282 1.00 20.11 C ANISOU 1121 CG GLN B 28 2714 2700 2226 91 143 285 C ATOM 1122 CD GLN A 28 -5.373 -6.020 1.164 1.00 22.17 C ANISOU 1122 CD GLN B 28 2716 3269 2438 137 223 256 C ATOM 1123 OE1 GLN A 28 -4.850 -6.639 2.102 1.00 23.91 O ANISOU 1123 OE1 GLN B 28 2857 3689 2535 252 197 338 O ATOM 1124 NE2 GLN A 28 -4.749 -5.834 -0.014 1.00 22.35 N ANISOU 1124 NE2 GLN B 28 2837 3503 2152 -121 200 349 N ATOM 1125 N ALA A 29 -9.912 -6.253 4.624 1.00 20.35 N ANISOU 1125 N ALA B 29 2660 2823 2249 60 -67 75 N ATOM 1126 CA ALA A 29 -10.860 -7.042 5.408 1.00 19.71 C ANISOU 1126 CA ALA B 29 2507 2703 2278 44 -52 8 C ATOM 1127 C ALA A 29 -12.270 -6.425 5.318 1.00 21.47 C ANISOU 1127 C ALA B 29 2711 2982 2462 15 -16 43 C ATOM 1128 O ALA A 29 -13.247 -7.162 5.111 1.00 22.73 O ANISOU 1128 O ALA B 29 2812 3239 2583 -2 -12 120 O ATOM 1129 CB ALA A 29 -10.376 -7.124 6.861 1.00 19.59 C ANISOU 1129 CB ALA B 29 2523 2759 2158 188 11 131 C ATOM 1130 N SER A 30 -12.349 -5.100 5.409 1.00 22.11 N ANISOU 1130 N SER B 30 2780 3112 2508 124 -53 83 N ATOM 1131 CA SER A 30 -13.623 -4.342 5.331 1.00 23.77 C ANISOU 1131 CA SER B 30 2887 3206 2937 94 7 35 C ATOM 1132 C SER A 30 -14.305 -4.607 3.995 1.00 24.01 C ANISOU 1132 C SER B 30 2914 3272 2936 110 11 32 C ATOM 1133 O SER A 30 -15.530 -4.830 3.925 1.00 24.80 O ANISOU 1133 O SER B 30 2852 3617 2952 157 -142 75 O ATOM 1134 CB SER A 30 -13.377 -2.845 5.500 1.00 25.29 C ANISOU 1134 CB SER B 30 3089 3358 3159 146 -14 -54 C ATOM 1135 OG SER A 30 -12.938 -2.604 6.820 1.00 29.92 O ANISOU 1135 OG SER B 30 3793 3875 3698 148 -91 -176 O ATOM 1136 N ALA A 31 -13.507 -4.675 2.937 1.00 23.54 N ANISOU 1136 N ALA B 31 2921 3165 2855 111 -16 126 N ATOM 1137 CA ALA A 31 -14.070 -5.002 1.625 1.00 24.10 C ANISOU 1137 CA ALA B 31 2994 3182 2979 74 -12 0 C ATOM 1138 C ALA A 31 -14.734 -6.370 1.517 1.00 24.42 C ANISOU 1138 C ALA B 31 3053 3222 3002 20 1 66 C ATOM 1139 O ALA A 31 -15.590 -6.560 0.633 1.00 26.04 O ANISOU 1139 O ALA B 31 3158 3532 3203 -38 -235 167 O ATOM 1140 CB ALA A 31 -13.019 -4.837 0.544 1.00 23.26 C ANISOU 1140 CB ALA B 31 2992 3018 2827 36 18 96 C ATOM 1141 N LEU A 32 -14.364 -7.323 2.376 1.00 24.53 N ANISOU 1141 N LEU B 32 3046 3369 2901 62 4 52 N ATOM 1142 CA LEU A 32 -14.952 -8.653 2.394 1.00 25.24 C ANISOU 1142 CA LEU B 32 3192 3368 3028 3 -1 0 C ATOM 1143 C LEU A 32 -16.116 -8.806 3.405 1.00 24.87 C ANISOU 1143 C LEU B 32 3070 3311 3066 -31 3 10 C ATOM 1144 O LEU A 32 -16.694 -9.897 3.518 1.00 26.17 O ANISOU 1144 O LEU B 32 3344 3597 3000 -99 124 41 O ATOM 1145 CB LEU A 32 -13.889 -9.674 2.764 1.00 26.98 C ANISOU 1145 CB LEU B 32 3374 3539 3338 42 -16 -35 C ATOM 1146 CG LEU A 32 -12.672 -9.760 1.862 1.00 29.93 C ANISOU 1146 CG LEU B 32 3678 3994 3698 -9 100 13 C ATOM 1147 CD1 LEU A 32 -11.586 -10.605 2.544 1.00 32.51 C ANISOU 1147 CD1 LEU B 32 4111 4169 4069 191 55 43 C ATOM 1148 CD2 LEU A 32 -13.041 -10.358 0.527 1.00 31.65 C ANISOU 1148 CD2 LEU B 32 4149 4029 3846 -54 54 -58 C ATOM 1149 N GLY A 33 -16.401 -7.748 4.153 1.00 24.86 N ANISOU 1149 N GLY B 33 3046 3334 3064 -72 67 59 N ATOM 1150 CA GLY A 33 -17.493 -7.708 5.091 1.00 25.20 C ANISOU 1150 CA GLY B 33 3107 3388 3077 47 9 48 C ATOM 1151 C GLY A 33 -17.054 -7.720 6.534 1.00 24.97 C ANISOU 1151 C GLY B 33 3078 3344 3065 28 3 70 C ATOM 1152 O GLY A 33 -17.923 -7.836 7.406 1.00 25.62 O ANISOU 1152 O GLY B 33 2903 3714 3117 235 71 134 O ATOM 1153 N TRP A 34 -15.750 -7.613 6.826 1.00 23.52 N ANISOU 1153 N TRP B 34 2884 3228 2824 42 44 47 N ATOM 1154 CA TRP A 34 -15.338 -7.566 8.251 1.00 23.57 C ANISOU 1154 CA TRP B 34 2977 3033 2944 64 -5 31 C ATOM 1155 C TRP A 34 -15.926 -6.301 8.896 1.00 24.55 C ANISOU 1155 C TRP B 34 3089 3143 3096 119 46 -10 C ATOM 1156 O TRP A 34 -15.858 -5.244 8.288 1.00 24.88 O ANISOU 1156 O TRP B 34 3072 3305 3074 284 169 61 O ATOM 1157 CB TRP A 34 -13.822 -7.498 8.355 1.00 23.02 C ANISOU 1157 CB TRP B 34 2860 3062 2822 72 21 3 C ATOM 1158 CG TRP A 34 -13.324 -7.267 9.733 1.00 21.85 C ANISOU 1158 CG TRP B 34 2741 2961 2599 146 43 63 C ATOM 1159 CD1 TRP A 34 -13.513 -8.097 10.802 1.00 21.01 C ANISOU 1159 CD1 TRP B 34 2666 2795 2519 33 141 -8 C ATOM 1160 CD2 TRP A 34 -12.611 -6.145 10.217 1.00 21.72 C ANISOU 1160 CD2 TRP B 34 2775 2978 2498 153 82 118 C ATOM 1161 NE1 TRP A 34 -12.925 -7.553 11.924 1.00 23.48 N ANISOU 1161 NE1 TRP B 34 3073 3225 2621 -13 -103 118 N ATOM 1162 CE2 TRP A 34 -12.352 -6.368 11.596 1.00 21.06 C ANISOU 1162 CE2 TRP B 34 2547 2947 2507 163 -55 5 C ATOM 1163 CE3 TRP A 34 -12.099 -4.989 9.632 1.00 22.46 C ANISOU 1163 CE3 TRP B 34 2813 3029 2690 -6 0 136 C ATOM 1164 CZ2 TRP A 34 -11.643 -5.477 12.375 1.00 23.37 C ANISOU 1164 CZ2 TRP B 34 3004 2965 2911 66 -49 -216 C ATOM 1165 CZ3 TRP A 34 -11.411 -4.086 10.417 1.00 25.56 C ANISOU 1165 CZ3 TRP B 34 3418 3116 3174 13 -73 65 C ATOM 1166 CH2 TRP A 34 -11.192 -4.331 11.779 1.00 25.82 C ANISOU 1166 CH2 TRP B 34 3361 3405 3041 -6 55 -2 C ATOM 1167 N VAL A 35 -16.498 -6.460 10.085 1.00 25.35 N ANISOU 1167 N VAL B 35 3202 3245 3184 197 28 12 N ATOM 1168 CA VAL A 35 -16.998 -5.363 10.929 1.00 27.87 C ANISOU 1168 CA VAL B 35 3530 3633 3426 104 17 -18 C ATOM 1169 C VAL A 35 -16.443 -5.677 12.341 1.00 27.10 C ANISOU 1169 C VAL B 35 3439 3533 3322 126 110 -26 C ATOM 1170 O VAL A 35 -16.737 -6.742 12.889 1.00 26.26 O ANISOU 1170 O VAL B 35 3474 3542 2960 213 283 -67 O ATOM 1171 CB VAL A 35 -18.551 -5.299 10.920 1.00 28.88 C ANISOU 1171 CB VAL B 35 3623 3816 3531 97 76 11 C ATOM 1172 CG1 VAL A 35 -19.058 -4.221 11.890 1.00 31.33 C ANISOU 1172 CG1 VAL B 35 4008 3966 3930 125 1 -52 C ATOM 1173 CG2 VAL A 35 -19.067 -5.006 9.502 1.00 31.17 C ANISOU 1173 CG2 VAL B 35 3876 4132 3833 171 -36 -4 C ATOM 1174 N ALA A 36 -15.646 -4.754 12.878 1.00 28.30 N ANISOU 1174 N ALA B 36 3539 3715 3497 155 103 15 N ATOM 1175 CA ALA A 36 -14.944 -4.943 14.156 1.00 29.08 C ANISOU 1175 CA ALA B 36 3662 3773 3611 113 35 -4 C ATOM 1176 C ALA A 36 -15.883 -5.360 15.302 1.00 29.89 C ANISOU 1176 C ALA B 36 3810 3910 3636 158 75 35 C ATOM 1177 O ALA A 36 -15.612 -6.325 15.964 1.00 28.34 O ANISOU 1177 O ALA B 36 3682 3635 3448 465 124 -60 O ATOM 1178 CB ALA A 36 -14.108 -3.755 14.526 1.00 29.80 C ANISOU 1178 CB ALA B 36 3795 3800 3724 54 92 73 C ATOM 1179 N SER A 37 -17.044 -4.701 15.435 1.00 31.71 N ANISOU 1179 N SER B 37 4030 4077 3939 255 62 32 N ATOM 1180 CA SER A 37 -18.047 -5.075 16.454 1.00 32.62 C ANISOU 1180 CA SER B 37 4081 4199 4114 155 58 6 C ATOM 1181 C SER A 37 -18.711 -6.456 16.312 1.00 32.67 C ANISOU 1181 C SER B 37 4059 4250 4103 121 64 22 C ATOM 1182 O SER A 37 -19.271 -6.954 17.291 1.00 33.63 O ANISOU 1182 O SER B 37 4090 4404 4281 239 239 -16 O ATOM 1183 CB SER A 37 -19.127 -3.974 16.563 1.00 33.75 C ANISOU 1183 CB SER B 37 4162 4416 4243 187 46 -29 C ATOM 1184 OG SER A 37 -19.735 -3.757 15.322 1.00 35.37 O ANISOU 1184 OG SER B 37 4281 4779 4378 292 53 124 O ATOM 1185 N LYS A 38 -18.646 -7.076 15.121 1.00 32.10 N ANISOU 1185 N LYS B 38 3963 4213 4019 50 35 -21 N ATOM 1186 CA LYS A 38 -19.136 -8.441 14.883 1.00 31.33 C ANISOU 1186 CA LYS B 38 3891 4036 3978 68 85 17 C ATOM 1187 C LYS A 38 -18.110 -9.534 15.213 1.00 30.02 C ANISOU 1187 C LYS B 38 3774 3885 3747 -22 59 54 C ATOM 1188 O LYS A 38 -18.487 -10.692 15.284 1.00 30.95 O ANISOU 1188 O LYS B 38 3868 3964 3926 11 152 -44 O ATOM 1189 CB LYS A 38 -19.562 -8.662 13.415 1.00 32.03 C ANISOU 1189 CB LYS B 38 4020 4065 4082 42 32 21 C ATOM 1190 CG LYS A 38 -20.850 -7.955 12.894 1.00 35.85 C ANISOU 1190 CG LYS B 38 4409 4587 4622 58 -39 -15 C ATOM 1191 CD LYS A 38 -21.309 -8.567 11.532 1.00 37.65 C ANISOU 1191 CD LYS B 38 4777 4886 4642 12 -22 -37 C ATOM 1192 N GLY A 39 -16.823 -9.186 15.343 1.00 28.25 N ANISOU 1192 N GLY B 39 3560 3671 3502 68 46 67 N ATOM 1193 CA GLY A 39 -15.758 -10.159 15.547 1.00 27.09 C ANISOU 1193 CA GLY B 39 3446 3490 3357 9 53 54 C ATOM 1194 C GLY A 39 -15.762 -11.279 14.530 1.00 25.62 C ANISOU 1194 C GLY B 39 3184 3332 3216 2 46 78 C ATOM 1195 O GLY A 39 -15.521 -12.394 14.885 1.00 25.59 O ANISOU 1195 O GLY B 39 3116 3441 3163 37 167 51 O ATOM 1196 N ASP A 40 -16.036 -10.949 13.262 1.00 24.88 N ANISOU 1196 N ASP B 40 3113 3259 3080 18 80 14 N ATOM 1197 CA ASP A 40 -16.264 -11.931 12.191 1.00 24.46 C ANISOU 1197 CA ASP B 40 3022 3233 3037 20 57 67 C ATOM 1198 C ASP A 40 -15.108 -12.057 11.191 1.00 23.72 C ANISOU 1198 C ASP B 40 2956 3169 2884 6 52 60 C ATOM 1199 O ASP A 40 -15.327 -12.577 10.119 1.00 25.05 O ANISOU 1199 O ASP B 40 2973 3640 2904 -73 104 33 O ATOM 1200 CB ASP A 40 -17.578 -11.588 11.429 1.00 25.60 C ANISOU 1200 CB ASP B 40 3138 3408 3178 2 20 84 C ATOM 1201 CG ASP A 40 -17.480 -10.300 10.600 1.00 25.58 C ANISOU 1201 CG ASP B 40 3144 3404 3172 53 102 73 C ATOM 1202 OD1 ASP A 40 -16.618 -9.443 10.879 1.00 25.19 O ANISOU 1202 OD1 ASP B 40 3293 3411 2866 148 57 74 O ATOM 1203 OD2 ASP A 40 -18.259 -10.058 9.639 1.00 29.90 O ANISOU 1203 OD2 ASP B 40 3478 4212 3670 47 4 18 O ATOM 1204 N LEU A 41 -13.901 -11.648 11.534 1.00 22.96 N ANISOU 1204 N LEU B 41 2895 3091 2736 18 57 81 N ATOM 1205 CA LEU A 41 -12.789 -11.725 10.536 1.00 22.79 C ANISOU 1205 CA LEU B 41 2867 3061 2730 4 -13 101 C ATOM 1206 C LEU A 41 -12.577 -13.116 9.978 1.00 23.85 C ANISOU 1206 C LEU B 41 2994 3235 2831 23 -60 39 C ATOM 1207 O LEU A 41 -12.425 -13.306 8.764 1.00 23.91 O ANISOU 1207 O LEU B 41 3130 3431 2521 128 -117 225 O ATOM 1208 CB LEU A 41 -11.468 -11.177 11.087 1.00 23.06 C ANISOU 1208 CB LEU B 41 2899 3107 2753 85 -2 12 C ATOM 1209 CG LEU A 41 -10.293 -11.118 10.107 1.00 23.01 C ANISOU 1209 CG LEU B 41 2835 2973 2933 -43 48 73 C ATOM 1210 CD1 LEU A 41 -10.605 -10.256 8.886 1.00 23.87 C ANISOU 1210 CD1 LEU B 41 2967 3139 2964 6 92 107 C ATOM 1211 CD2 LEU A 41 -9.038 -10.654 10.827 1.00 23.42 C ANISOU 1211 CD2 LEU B 41 3090 2846 2960 -77 -61 171 C ATOM 1212 N ALA A 42 -12.573 -14.116 10.850 1.00 23.93 N ANISOU 1212 N ALA B 42 3186 3021 2884 -48 -65 79 N ATOM 1213 CA ALA A 42 -12.312 -15.500 10.416 1.00 25.93 C ANISOU 1213 CA ALA B 42 3394 3245 3211 4 -5 -3 C ATOM 1214 C ALA A 42 -13.448 -16.117 9.603 1.00 27.16 C ANISOU 1214 C ALA B 42 3567 3408 3343 -41 -29 21 C ATOM 1215 O ALA A 42 -13.221 -17.108 8.892 1.00 28.93 O ANISOU 1215 O ALA B 42 3796 3520 3673 -146 -82 -23 O ATOM 1216 CB ALA A 42 -11.988 -16.384 11.618 1.00 26.75 C ANISOU 1216 CB ALA B 42 3583 3311 3268 22 -40 52 C ATOM 1217 N GLU A 43 -14.639 -15.552 9.699 1.00 27.91 N ANISOU 1217 N GLU B 43 3614 3553 3434 -101 54 63 N ATOM 1218 CA GLU A 43 -15.776 -15.996 8.907 1.00 29.89 C ANISOU 1218 CA GLU B 43 3860 3822 3675 -39 -26 -1 C ATOM 1219 C GLU A 43 -15.678 -15.450 7.491 1.00 29.15 C ANISOU 1219 C GLU B 43 3795 3677 3602 0 -69 -9 C ATOM 1220 O GLU A 43 -15.988 -16.177 6.555 1.00 30.22 O ANISOU 1220 O GLU B 43 4107 3706 3668 -67 -160 -35 O ATOM 1221 CB GLU A 43 -17.093 -15.565 9.520 1.00 31.45 C ANISOU 1221 CB GLU B 43 3953 4003 3993 8 -26 -74 C ATOM 1222 CG GLU A 43 -17.395 -16.203 10.866 1.00 37.22 C ANISOU 1222 CG GLU B 43 4827 4733 4581 -76 3 51 C ATOM 1223 CD GLU A 43 -18.593 -15.556 11.568 1.00 44.47 C ANISOU 1223 CD GLU B 43 5467 5750 5678 93 166 -49 C ATOM 1224 OE1 GLU A 43 -19.590 -15.210 10.860 1.00 48.44 O ANISOU 1224 OE1 GLU B 43 5908 6347 6150 14 -85 31 O ATOM 1225 OE2 GLU A 43 -18.532 -15.365 12.823 1.00 48.66 O ANISOU 1225 OE2 GLU B 43 6283 6376 5828 -15 36 -39 O ATOM 1226 N VAL A 44 -15.276 -14.189 7.332 1.00 27.86 N ANISOU 1226 N VAL B 44 3507 3721 3355 -24 -47 18 N ATOM 1227 CA VAL A 44 -15.181 -13.570 6.001 1.00 26.99 C ANISOU 1227 CA VAL B 44 3331 3595 3328 5 -38 37 C ATOM 1228 C VAL A 44 -13.847 -13.800 5.306 1.00 26.80 C ANISOU 1228 C VAL B 44 3348 3619 3215 32 -16 16 C ATOM 1229 O VAL A 44 -13.797 -13.730 4.066 1.00 27.17 O ANISOU 1229 O VAL B 44 3336 3841 3144 3 -32 53 O ATOM 1230 CB VAL A 44 -15.575 -12.093 6.005 1.00 27.00 C ANISOU 1230 CB VAL B 44 3385 3576 3295 -2 -36 10 C ATOM 1231 CG1 VAL A 44 -16.979 -11.955 6.601 1.00 28.73 C ANISOU 1231 CG1 VAL B 44 3550 3768 3595 46 -26 -13 C ATOM 1232 CG2 VAL A 44 -14.569 -11.170 6.688 1.00 26.80 C ANISOU 1232 CG2 VAL B 44 3401 3411 3369 98 -19 35 C ATOM 1233 N ALA A 45 -12.784 -14.047 6.089 1.00 25.62 N ANISOU 1233 N ALA B 45 3200 3454 3079 3 -10 -4 N ATOM 1234 CA ALA A 45 -11.430 -14.185 5.551 1.00 24.99 C ANISOU 1234 CA ALA B 45 3148 3265 3078 41 -18 -72 C ATOM 1235 C ALA A 45 -10.717 -15.285 6.349 1.00 25.68 C ANISOU 1235 C ALA B 45 3223 3332 3201 -16 -6 -54 C ATOM 1236 O ALA A 45 -9.824 -15.011 7.168 1.00 25.29 O ANISOU 1236 O ALA B 45 3043 3415 3149 -29 -52 -135 O ATOM 1237 CB ALA A 45 -10.723 -12.844 5.638 1.00 25.30 C ANISOU 1237 CB ALA B 45 3157 3428 3028 40 53 36 C ATOM 1238 N PRO A 46 -11.147 -16.537 6.169 1.00 26.67 N ANISOU 1238 N PRO B 46 3349 3364 3418 -47 -105 -80 N ATOM 1239 CA PRO A 46 -10.576 -17.654 6.941 1.00 26.08 C ANISOU 1239 CA PRO B 46 3329 3144 3435 -67 -74 -67 C ATOM 1240 C PRO A 46 -9.053 -17.713 6.823 1.00 24.35 C ANISOU 1240 C PRO B 46 3193 2863 3195 -51 -44 -78 C ATOM 1241 O PRO A 46 -8.502 -17.515 5.732 1.00 25.19 O ANISOU 1241 O PRO B 46 3368 2942 3259 -160 -127 -133 O ATOM 1242 CB PRO A 46 -11.238 -18.932 6.343 1.00 27.65 C ANISOU 1242 CB PRO B 46 3519 3379 3606 -72 -150 -119 C ATOM 1243 CG PRO A 46 -12.200 -18.468 5.320 1.00 28.35 C ANISOU 1243 CG PRO B 46 3613 3437 3719 -25 -125 9 C ATOM 1244 CD PRO A 46 -12.217 -16.981 5.255 1.00 28.02 C ANISOU 1244 CD PRO B 46 3527 3484 3632 -60 -135 -80 C ATOM 1245 N GLY A 47 -8.397 -17.899 7.959 1.00 24.16 N ANISOU 1245 N GLY B 47 3078 2957 3144 -25 7 -56 N ATOM 1246 CA GLY A 47 -6.949 -17.972 8.030 1.00 22.92 C ANISOU 1246 CA GLY B 47 2971 2802 2933 -2 5 18 C ATOM 1247 C GLY A 47 -6.191 -16.669 8.002 1.00 21.66 C ANISOU 1247 C GLY B 47 2757 2774 2696 14 32 -34 C ATOM 1248 O GLY A 47 -4.991 -16.682 8.095 1.00 21.69 O ANISOU 1248 O GLY B 47 2775 2736 2729 43 28 58 O ATOM 1249 N LYS A 48 -6.897 -15.549 7.879 1.00 19.63 N ANISOU 1249 N LYS B 48 2610 2492 2356 -61 20 24 N ATOM 1250 CA LYS A 48 -6.244 -14.242 7.800 1.00 19.24 C ANISOU 1250 CA LYS B 48 2557 2443 2307 -29 50 -17 C ATOM 1251 C LYS A 48 -6.221 -13.500 9.142 1.00 18.68 C ANISOU 1251 C LYS B 48 2497 2472 2127 -96 -2 -11 C ATOM 1252 O LYS A 48 -7.059 -13.765 10.034 1.00 20.03 O ANISOU 1252 O LYS B 48 2625 2774 2212 -174 101 -77 O ATOM 1253 CB LYS A 48 -6.896 -13.355 6.742 1.00 20.92 C ANISOU 1253 CB LYS B 48 2706 2791 2450 -25 -47 -47 C ATOM 1254 CG LYS A 48 -6.987 -14.008 5.360 1.00 20.99 C ANISOU 1254 CG LYS B 48 2811 2892 2269 71 37 -8 C ATOM 1255 CD LYS A 48 -5.622 -14.352 4.831 1.00 24.27 C ANISOU 1255 CD LYS B 48 2955 3356 2908 77 71 -70 C ATOM 1256 CE LYS A 48 -5.738 -14.714 3.347 1.00 26.84 C ANISOU 1256 CE LYS B 48 3384 3759 3055 4 -62 -65 C ATOM 1257 NZ LYS A 48 -4.488 -15.278 2.868 1.00 29.22 N ANISOU 1257 NZ LYS B 48 3661 3934 3505 143 0 -63 N ATOM 1258 N SER A 49 -5.214 -12.656 9.288 1.00 17.85 N ANISOU 1258 N SER B 49 2413 2340 2026 -49 31 44 N ATOM 1259 CA SER A 49 -5.082 -11.698 10.391 1.00 17.99 C ANISOU 1259 CA SER B 49 2360 2358 2116 -30 3 9 C ATOM 1260 C SER A 49 -4.953 -10.311 9.811 1.00 17.65 C ANISOU 1260 C SER B 49 2325 2370 2011 62 -43 43 C ATOM 1261 O SER A 49 -4.495 -10.163 8.678 1.00 19.46 O ANISOU 1261 O SER B 49 2656 2748 1988 69 -20 330 O ATOM 1262 CB SER A 49 -3.822 -11.995 11.184 1.00 18.37 C ANISOU 1262 CB SER B 49 2527 2276 2174 10 -103 24 C ATOM 1263 OG SER A 49 -3.887 -13.297 11.762 1.00 17.94 O ANISOU 1263 OG SER B 49 2814 2005 1997 -170 -163 97 O ATOM 1264 N ILE A 50 -5.351 -9.287 10.574 1.00 17.74 N ANISOU 1264 N ILE B 50 2378 2386 1976 34 -8 143 N ATOM 1265 CA ILE A 50 -5.142 -7.901 10.208 1.00 18.01 C ANISOU 1265 CA ILE B 50 2374 2351 2116 34 -31 52 C ATOM 1266 C ILE A 50 -3.694 -7.513 10.384 1.00 17.75 C ANISOU 1266 C ILE B 50 2357 2334 2051 60 31 142 C ATOM 1267 O ILE A 50 -3.089 -7.732 11.431 1.00 17.04 O ANISOU 1267 O ILE B 50 2442 2254 1778 23 -29 78 O ATOM 1268 CB ILE A 50 -6.031 -6.958 11.070 1.00 18.63 C ANISOU 1268 CB ILE B 50 2522 2258 2295 145 24 26 C ATOM 1269 CG1 ILE A 50 -7.516 -7.278 10.893 1.00 24.32 C ANISOU 1269 CG1 ILE B 50 3099 2969 3171 -56 -53 -13 C ATOM 1270 CG2 ILE A 50 -5.688 -5.515 10.849 1.00 21.71 C ANISOU 1270 CG2 ILE B 50 2978 2582 2687 46 -4 144 C ATOM 1271 CD1 ILE A 50 -8.060 -7.150 9.578 1.00 27.03 C ANISOU 1271 CD1 ILE B 50 3511 3436 3321 24 -106 101 C ATOM 1272 N GLY A 51 -3.124 -6.916 9.333 1.00 17.17 N ANISOU 1272 N GLY B 51 2295 2377 1851 41 17 217 N ATOM 1273 CA GLY A 51 -1.813 -6.366 9.421 1.00 16.82 C ANISOU 1273 CA GLY B 51 2280 2158 1951 -15 -23 214 C ATOM 1274 C GLY A 51 -1.401 -5.610 8.179 1.00 18.10 C ANISOU 1274 C GLY B 51 2305 2526 2043 -41 76 143 C ATOM 1275 O GLY A 51 -1.956 -5.846 7.097 1.00 20.22 O ANISOU 1275 O GLY B 51 2568 2961 2153 -176 21 448 O ATOM 1276 N GLY A 52 -0.445 -4.722 8.386 1.00 17.14 N ANISOU 1276 N GLY B 52 2373 1989 2148 37 -11 270 N ATOM 1277 CA GLY A 52 0.181 -3.928 7.327 1.00 19.25 C ANISOU 1277 CA GLY B 52 2429 2560 2324 -31 147 212 C ATOM 1278 C GLY A 52 -0.240 -2.462 7.323 1.00 20.75 C ANISOU 1278 C GLY B 52 2687 2650 2546 -17 32 196 C ATOM 1279 O GLY A 52 0.297 -1.671 6.482 1.00 23.42 O ANISOU 1279 O GLY B 52 3155 2981 2761 -51 185 476 O ATOM 1280 N ASP A 53 -1.177 -2.053 8.195 1.00 21.68 N ANISOU 1280 N ASP B 53 2772 2876 2589 38 18 239 N ATOM 1281 CA ASP A 53 -1.649 -0.652 8.294 1.00 22.48 C ANISOU 1281 CA ASP B 53 2916 2817 2806 -90 -14 192 C ATOM 1282 C ASP A 53 -0.677 0.250 8.983 1.00 22.28 C ANISOU 1282 C ASP B 53 2902 2713 2849 -83 -12 188 C ATOM 1283 O ASP A 53 0.147 -0.167 9.784 1.00 21.37 O ANISOU 1283 O ASP B 53 2833 2532 2752 -287 -39 638 O ATOM 1284 CB ASP A 53 -3.004 -0.515 8.979 1.00 22.27 C ANISOU 1284 CB ASP B 53 2982 2674 2805 -23 -29 206 C ATOM 1285 CG ASP A 53 -4.092 -1.152 8.175 1.00 26.52 C ANISOU 1285 CG ASP B 53 3283 3398 3394 -94 -59 157 C ATOM 1286 OD1 ASP A 53 -4.398 -0.604 7.101 1.00 33.31 O ANISOU 1286 OD1 ASP B 53 4179 4543 3931 -25 -305 391 O ATOM 1287 OD2 ASP A 53 -4.631 -2.227 8.471 1.00 26.78 O ANISOU 1287 OD2 ASP B 53 2999 3505 3669 -316 -80 141 O ATOM 1288 N VAL A 54 -0.736 1.528 8.644 1.00 24.73 N ANISOU 1288 N VAL B 54 3142 2994 3259 92 -78 330 N ATOM 1289 CA VAL A 54 0.136 2.494 9.269 1.00 24.85 C ANISOU 1289 CA VAL B 54 3248 2864 3328 39 -121 219 C ATOM 1290 C VAL A 54 -0.254 2.735 10.735 1.00 24.68 C ANISOU 1290 C VAL B 54 3113 2843 3420 27 -29 230 C ATOM 1291 O VAL A 54 -1.437 2.815 11.085 1.00 26.30 O ANISOU 1291 O VAL B 54 3095 3092 3804 162 -126 327 O ATOM 1292 CB VAL A 54 0.128 3.865 8.456 1.00 26.66 C ANISOU 1292 CB VAL B 54 3434 3165 3530 16 -70 260 C ATOM 1293 CG1 VAL A 54 0.805 4.992 9.260 1.00 28.87 C ANISOU 1293 CG1 VAL B 54 3767 3381 3821 7 -88 165 C ATOM 1294 CG2 VAL A 54 0.775 3.630 7.125 1.00 29.24 C ANISOU 1294 CG2 VAL B 54 3904 3447 3757 28 1 170 C ATOM 1295 N PHE A 55 0.763 2.789 11.594 1.00 23.51 N ANISOU 1295 N PHE B 55 2931 2742 3258 10 -74 212 N ATOM 1296 CA PHE A 55 0.645 3.092 13.008 1.00 23.11 C ANISOU 1296 CA PHE B 55 2887 2617 3277 18 -70 168 C ATOM 1297 C PHE A 55 1.176 4.511 13.154 1.00 24.39 C ANISOU 1297 C PHE B 55 3038 2787 3442 9 24 185 C ATOM 1298 O PHE A 55 2.363 4.761 12.884 1.00 24.08 O ANISOU 1298 O PHE B 55 3043 2412 3694 -51 -101 447 O ATOM 1299 CB PHE A 55 1.514 2.096 13.827 1.00 23.33 C ANISOU 1299 CB PHE B 55 2954 2545 3364 36 -78 241 C ATOM 1300 CG PHE A 55 1.454 2.304 15.294 1.00 22.06 C ANISOU 1300 CG PHE B 55 2998 2009 3373 195 -147 180 C ATOM 1301 CD1 PHE A 55 0.300 1.979 16.038 1.00 23.91 C ANISOU 1301 CD1 PHE B 55 3322 2418 3343 70 -59 183 C ATOM 1302 CD2 PHE A 55 2.516 2.874 15.968 1.00 23.92 C ANISOU 1302 CD2 PHE B 55 3061 2494 3530 110 -211 220 C ATOM 1303 CE1 PHE A 55 0.252 2.162 17.407 1.00 24.45 C ANISOU 1303 CE1 PHE B 55 3497 2332 3460 53 -84 139 C ATOM 1304 CE2 PHE A 55 2.458 3.098 17.331 1.00 25.36 C ANISOU 1304 CE2 PHE B 55 3402 2720 3514 204 12 132 C ATOM 1305 CZ PHE A 55 1.330 2.739 18.061 1.00 25.67 C ANISOU 1305 CZ PHE B 55 3316 2835 3602 179 -171 243 C ATOM 1306 N SER A 56 0.307 5.403 13.604 1.00 23.94 N ANISOU 1306 N SER B 56 3158 2519 3416 25 -7 203 N ATOM 1307 CA SER A 56 0.649 6.847 13.671 1.00 25.35 C ANISOU 1307 CA SER B 56 3305 2825 3502 -44 29 157 C ATOM 1308 C SER A 56 1.770 7.194 14.601 1.00 25.03 C ANISOU 1308 C SER B 56 3261 2807 3441 -28 42 230 C ATOM 1309 O SER A 56 2.581 8.080 14.278 1.00 24.27 O ANISOU 1309 O SER B 56 3146 2317 3755 -25 -17 521 O ATOM 1310 CB SER A 56 -0.604 7.675 13.928 1.00 26.34 C ANISOU 1310 CB SER B 56 3383 3071 3553 26 58 121 C ATOM 1311 OG SER A 56 -0.880 7.845 15.293 1.00 28.44 O ANISOU 1311 OG SER B 56 3698 3329 3776 238 -21 193 O ATOM 1312 N ASN A 57 1.908 6.456 15.715 1.00 24.82 N ANISOU 1312 N ASN B 57 3265 2795 3369 -19 45 227 N ATOM 1313 CA ASN A 57 2.836 6.774 16.789 1.00 25.54 C ANISOU 1313 CA ASN B 57 3273 2925 3504 3 30 167 C ATOM 1314 C ASN A 57 2.609 8.163 17.378 1.00 26.21 C ANISOU 1314 C ASN B 57 3309 3037 3610 27 6 139 C ATOM 1315 O ASN A 57 3.523 8.826 17.878 1.00 26.68 O ANISOU 1315 O ASN B 57 3395 2458 4281 11 -24 261 O ATOM 1316 CB ASN A 57 4.279 6.594 16.320 1.00 25.72 C ANISOU 1316 CB ASN B 57 3250 2987 3536 -11 53 88 C ATOM 1317 CG ASN A 57 5.277 6.546 17.459 1.00 26.21 C ANISOU 1317 CG ASN B 57 3238 3200 3517 31 37 149 C ATOM 1318 OD1 ASN A 57 4.979 6.087 18.579 1.00 23.65 O ANISOU 1318 OD1 ASN B 57 2616 2676 3692 106 43 234 O ATOM 1319 ND2 ASN A 57 6.481 7.099 17.197 1.00 26.27 N ANISOU 1319 ND2 ASN B 57 3045 2924 4011 86 64 351 N ATOM 1320 N ARG A 58 1.350 8.576 17.404 1.00 26.10 N ANISOU 1320 N ARG B 58 3298 3017 3601 8 60 261 N ATOM 1321 CA ARG A 58 1.055 9.909 17.931 1.00 27.15 C ANISOU 1321 CA ARG B 58 3375 3246 3694 38 26 89 C ATOM 1322 C ARG A 58 1.328 10.078 19.398 1.00 26.85 C ANISOU 1322 C ARG B 58 3401 3084 3713 24 -15 73 C ATOM 1323 O ARG A 58 1.589 11.203 19.861 1.00 28.61 O ANISOU 1323 O ARG B 58 3729 2833 4305 137 -122 72 O ATOM 1324 CB ARG A 58 -0.352 10.340 17.558 1.00 28.37 C ANISOU 1324 CB ARG B 58 3466 3536 3775 58 -10 146 C ATOM 1325 CG AARG A 58 -1.424 9.733 18.359 0.57 26.68 C ANISOU 1325 CG AARG B 58 3280 3332 3524 54 -13 82 C ATOM 1326 CD AARG A 58 -2.681 10.504 18.214 0.57 24.88 C ANISOU 1326 CD AARG B 58 3152 3026 3272 17 16 -41 C ATOM 1327 NE AARG A 58 -3.885 9.703 18.278 0.57 22.92 N ANISOU 1327 NE AARG B 58 3017 2684 3008 27 63 45 N ATOM 1328 CZ AARG A 58 -5.104 10.183 18.524 0.57 21.55 C ANISOU 1328 CZ AARG B 58 2842 2646 2697 -48 -27 17 C ATOM 1329 NH1AARG A 58 -5.303 11.487 18.771 0.57 20.35 N ANISOU 1329 NH1AARG B 58 2766 2550 2415 65 105 208 N ATOM 1330 NH2AARG A 58 -6.142 9.346 18.526 0.57 20.69 N ANISOU 1330 NH2AARG B 58 2817 2630 2411 -103 37 264 N ATOM 1331 CG BARG A 58 -1.499 9.454 18.049 0.43 28.07 C ANISOU 1331 CG BARG B 58 3498 3518 3647 26 1 80 C ATOM 1332 CD BARG A 58 -2.912 9.874 17.605 0.43 28.30 C ANISOU 1332 CD BARG B 58 3512 3669 3570 15 -22 2 C ATOM 1333 NE BARG A 58 -3.379 11.105 18.245 0.43 28.71 N ANISOU 1333 NE BARG B 58 3517 3722 3669 -9 -8 30 N ATOM 1334 CZ BARG A 58 -4.641 11.379 18.625 0.43 26.73 C ANISOU 1334 CZ BARG B 58 3432 3410 3311 20 -14 33 C ATOM 1335 NH1BARG A 58 -5.662 10.521 18.440 0.43 26.46 N ANISOU 1335 NH1BARG B 58 3439 3372 3240 -12 2 -86 N ATOM 1336 NH2BARG A 58 -4.891 12.549 19.197 0.43 26.04 N ANISOU 1336 NH2BARG B 58 3422 3406 3064 -29 -81 77 N ATOM 1337 N GLU A 59 1.346 8.956 20.149 1.00 24.86 N ANISOU 1337 N GLU B 59 3227 2731 3487 85 22 99 N ATOM 1338 CA GLU A 59 1.614 8.959 21.569 1.00 24.34 C ANISOU 1338 CA GLU B 59 3115 2727 3405 25 -18 3 C ATOM 1339 C GLU A 59 3.125 9.075 21.871 1.00 25.45 C ANISOU 1339 C GLU B 59 3326 2798 3545 -1 -82 33 C ATOM 1340 O GLU A 59 3.482 9.212 23.016 1.00 28.67 O ANISOU 1340 O GLU B 59 3643 3094 4154 -50 -283 -63 O ATOM 1341 CB GLU A 59 1.064 7.684 22.234 1.00 23.66 C ANISOU 1341 CB GLU B 59 3046 2776 3167 80 -6 -53 C ATOM 1342 CG GLU A 59 -0.412 7.396 21.972 1.00 21.05 C ANISOU 1342 CG GLU B 59 2871 2149 2977 179 -11 -4 C ATOM 1343 CD GLU A 59 -0.724 6.691 20.653 1.00 20.09 C ANISOU 1343 CD GLU B 59 2741 2294 2596 132 47 183 C ATOM 1344 OE1 GLU A 59 -1.913 6.424 20.389 1.00 20.60 O ANISOU 1344 OE1 GLU B 59 2907 2293 2626 255 271 183 O ATOM 1345 OE2 GLU A 59 0.226 6.378 19.894 1.00 19.20 O ANISOU 1345 OE2 GLU B 59 3166 1467 2662 138 355 46 O ATOM 1346 N GLY A 60 3.961 8.904 20.867 1.00 26.10 N ANISOU 1346 N GLY B 60 3311 2844 3760 -78 -42 79 N ATOM 1347 CA GLY A 60 5.410 9.016 20.978 1.00 28.22 C ANISOU 1347 CA GLY B 60 3497 3324 3901 -56 -111 98 C ATOM 1348 C GLY A 60 6.118 7.937 21.784 1.00 29.08 C ANISOU 1348 C GLY B 60 3558 3415 4074 -59 -144 117 C ATOM 1349 O GLY A 60 7.258 8.127 22.246 1.00 29.82 O ANISOU 1349 O GLY B 60 3585 3279 4466 -172 -248 133 O ATOM 1350 N ARG A 61 5.464 6.778 21.936 1.00 27.79 N ANISOU 1350 N ARG B 61 3395 3233 3930 -41 -116 77 N ATOM 1351 CA ARG A 61 6.078 5.699 22.694 1.00 27.55 C ANISOU 1351 CA ARG B 61 3490 3291 3685 18 -53 40 C ATOM 1352 C ARG A 61 7.144 4.943 21.929 1.00 26.88 C ANISOU 1352 C ARG B 61 3366 3244 3601 27 -87 98 C ATOM 1353 O ARG A 61 7.935 4.221 22.587 1.00 28.49 O ANISOU 1353 O ARG B 61 3488 3363 3971 383 -222 187 O ATOM 1354 CB ARG A 61 5.002 4.795 23.278 1.00 28.01 C ANISOU 1354 CB ARG B 61 3495 3397 3748 -5 -12 16 C ATOM 1355 CG ARG A 61 4.280 5.515 24.444 1.00 31.06 C ANISOU 1355 CG ARG B 61 3935 3796 4069 58 136 -43 C ATOM 1356 CD ARG A 61 3.540 4.600 25.417 1.00 34.34 C ANISOU 1356 CD ARG B 61 4238 4374 4434 -12 77 33 C ATOM 1357 NE ARG A 61 2.255 4.179 24.875 1.00 34.33 N ANISOU 1357 NE ARG B 61 4179 4360 4505 78 -17 -148 N ATOM 1358 CZ ARG A 61 1.080 4.887 24.874 1.00 30.07 C ANISOU 1358 CZ ARG B 61 3956 3770 3696 -2 -48 20 C ATOM 1359 NH1 ARG A 61 0.953 6.117 25.368 1.00 31.46 N ANISOU 1359 NH1 ARG B 61 4583 3565 3806 -161 -2 71 N ATOM 1360 NH2 ARG A 61 0.016 4.322 24.357 1.00 23.03 N ANISOU 1360 NH2 ARG B 61 3019 2706 3025 226 29 126 N ATOM 1361 N LEU A 62 7.172 5.051 20.604 1.00 24.98 N ANISOU 1361 N LEU B 62 3156 2824 3510 36 -90 249 N ATOM 1362 CA LEU A 62 8.195 4.433 19.751 1.00 25.61 C ANISOU 1362 CA LEU B 62 3197 3043 3491 -46 -20 233 C ATOM 1363 C LEU A 62 9.115 5.559 19.265 1.00 27.46 C ANISOU 1363 C LEU B 62 3338 3148 3945 -87 30 235 C ATOM 1364 O LEU A 62 8.643 6.670 19.058 1.00 27.82 O ANISOU 1364 O LEU B 62 3220 3000 4349 -89 -64 190 O ATOM 1365 CB LEU A 62 7.602 3.706 18.567 1.00 25.30 C ANISOU 1365 CB LEU B 62 3180 2942 3491 -18 61 237 C ATOM 1366 CG LEU A 62 6.682 2.520 18.986 1.00 25.13 C ANISOU 1366 CG LEU B 62 3109 2920 3519 -35 3 187 C ATOM 1367 CD1 LEU A 62 5.959 1.989 17.804 1.00 27.83 C ANISOU 1367 CD1 LEU B 62 3484 3439 3649 -123 107 48 C ATOM 1368 CD2 LEU A 62 7.511 1.416 19.712 1.00 25.47 C ANISOU 1368 CD2 LEU B 62 3248 2912 3517 -63 -8 133 C ATOM 1369 N PRO A 63 10.384 5.278 19.042 1.00 29.70 N ANISOU 1369 N PRO B 63 3553 3573 4156 -53 17 211 N ATOM 1370 CA PRO A 63 11.309 6.341 18.589 1.00 31.42 C ANISOU 1370 CA PRO B 63 3837 3812 4288 -103 31 142 C ATOM 1371 C PRO A 63 10.976 6.818 17.174 1.00 33.87 C ANISOU 1371 C PRO B 63 4191 4212 4466 -56 12 109 C ATOM 1372 O PRO A 63 10.699 6.066 16.235 1.00 32.70 O ANISOU 1372 O PRO B 63 4220 3712 4490 -161 96 315 O ATOM 1373 CB PRO A 63 12.702 5.674 18.652 1.00 31.93 C ANISOU 1373 CB PRO B 63 3887 3924 4320 -53 31 62 C ATOM 1374 CG PRO A 63 12.480 4.221 18.807 1.00 31.54 C ANISOU 1374 CG PRO B 63 3743 3982 4256 -5 0 180 C ATOM 1375 CD PRO A 63 11.046 3.967 19.147 1.00 29.44 C ANISOU 1375 CD PRO B 63 3553 3587 4044 0 40 108 C ATOM 1376 N SER A 64 10.987 8.128 17.013 1.00 38.10 N ANISOU 1376 N SER B 64 4782 4676 5016 -113 7 77 N ATOM 1377 CA SER A 64 10.687 8.711 15.705 1.00 40.98 C ANISOU 1377 CA SER B 64 5184 5168 5218 -60 -18 64 C ATOM 1378 CB SER A 64 9.648 9.812 15.840 1.00 41.22 C ANISOU 1378 CB SER B 64 5270 5127 5264 -70 29 58 C ATOM 1379 OG SER A 64 9.896 10.555 16.985 1.00 43.53 O ANISOU 1379 OG SER B 64 5701 5360 5478 -66 -86 77 O ATOM 1380 C ASER A 64 11.934 9.331 15.060 0.50 42.45 C ANISOU 1380 C ASER B 64 5363 5340 5426 -73 9 47 C ATOM 1381 O ASER A 64 12.731 9.945 15.769 0.50 43.18 O ANISOU 1381 O ASER B 64 5478 5346 5580 -125 -39 55 O ATOM 1382 C BSER A 64 11.979 9.135 15.022 0.50 41.92 C ANISOU 1382 C BSER B 64 5302 5291 5335 -62 9 34 C ATOM 1383 O BSER A 64 13.065 9.196 15.624 0.50 41.83 O ANISOU 1383 O BSER B 64 5300 5224 5368 -89 -12 69 O ATOM 1384 N AALA A 65 12.087 9.149 13.739 0.50 44.02 N ANISOU 1384 N AALA B 65 5586 5569 5568 -39 12 39 N ATOM 1385 CA AALA A 65 13.186 9.742 12.935 0.50 44.73 C ANISOU 1385 CA AALA B 65 5654 5667 5673 -24 22 35 C ATOM 1386 C AALA A 65 12.684 10.634 11.749 0.50 45.35 C ANISOU 1386 C AALA B 65 5727 5779 5724 -9 1 34 C ATOM 1387 O AALA A 65 11.476 10.877 11.647 0.50 45.31 O ANISOU 1387 O AALA B 65 5708 5779 5727 22 11 33 O ATOM 1388 CB AALA A 65 14.077 8.628 12.391 0.50 44.83 C ANISOU 1388 CB AALA B 65 5685 5670 5678 -20 27 30 C ATOM 1389 N BALA A 65 11.867 9.325 13.722 0.50 43.12 N ANISOU 1389 N BALA B 65 5479 5450 5453 -43 8 56 N ATOM 1390 CA BALA A 65 13.000 9.776 12.938 0.50 43.73 C ANISOU 1390 CA BALA B 65 5539 5527 5549 -35 23 45 C ATOM 1391 C BALA A 65 12.572 10.060 11.516 0.50 44.10 C ANISOU 1391 C BALA B 65 5595 5582 5577 -46 8 43 C ATOM 1392 O BALA A 65 11.543 9.606 11.006 0.50 43.30 O ANISOU 1392 O BALA B 65 5529 5375 5547 -71 58 130 O ATOM 1393 CB BALA A 65 14.176 8.803 12.984 0.50 43.84 C ANISOU 1393 CB BALA B 65 5551 5533 5571 -32 24 29 C ATOM 1394 N AGLY A 66 13.617 11.109 10.877 0.50 45.62 N ANISOU 1394 N AGLY B 66 5776 5779 5777 -40 8 37 N ATOM 1395 CA AGLY A 66 13.302 11.864 9.638 0.50 45.41 C ANISOU 1395 CA AGLY B 66 5759 5754 5740 -17 -13 13 C ATOM 1396 C AGLY A 66 12.086 11.045 9.404 0.50 44.83 C ANISOU 1396 C AGLY B 66 5707 5637 5686 -39 26 34 C ATOM 1397 O AGLY A 66 11.040 11.599 9.698 0.50 44.68 O ANISOU 1397 O AGLY B 66 5682 5573 5719 -13 11 74 O ATOM 1398 N BGLY A 66 13.396 10.843 10.865 0.50 44.71 N ANISOU 1398 N BGLY B 66 5664 5655 5667 -53 7 36 N ATOM 1399 CA BGLY A 66 13.000 11.369 9.596 0.50 44.71 C ANISOU 1399 CA BGLY B 66 5676 5665 5647 -31 -2 34 C ATOM 1400 C BGLY A 66 13.309 10.680 8.288 0.50 44.58 C ANISOU 1400 C BGLY B 66 5648 5652 5637 -10 -6 10 C ATOM 1401 O BGLY A 66 14.356 10.066 8.258 0.50 45.17 O ANISOU 1401 O BGLY B 66 5729 5744 5689 31 -18 26 O ATOM 1402 C SER A 67 11.173 8.251 7.599 1.00 42.55 C ANISOU 1402 C SER B 67 5439 5382 5345 -59 3 42 C ATOM 1403 O SER A 67 10.989 7.426 6.713 1.00 42.57 O ANISOU 1403 O SER B 67 5479 5294 5402 -59 41 95 O ATOM 1404 N ASER A 67 12.010 9.976 8.646 0.50 44.33 N ANISOU 1404 N ASER B 67 5667 5595 5580 -40 11 13 N ATOM 1405 CA ASER A 67 12.089 9.571 7.284 0.50 43.19 C ANISOU 1405 CA ASER B 67 5521 5403 5485 -61 32 71 C ATOM 1406 N BSER A 67 12.412 10.431 7.346 0.50 44.30 N ANISOU 1406 N BSER B 67 5612 5609 5608 -27 -11 33 N ATOM 1407 CA BSER A 67 11.128 9.795 7.365 0.50 43.22 C ANISOU 1407 CA BSER B 67 5522 5427 5473 -13 -2 62 C ATOM 1408 N ARG A 68 10.933 7.972 8.885 1.00 40.73 N ANISOU 1408 N ARG B 68 5188 5055 5231 -100 23 135 N ATOM 1409 CA ARG A 68 10.604 6.651 9.413 1.00 38.56 C ANISOU 1409 CA ARG B 68 4844 4868 4939 -52 8 164 C ATOM 1410 C ARG A 68 9.100 6.583 9.588 1.00 35.86 C ANISOU 1410 C ARG B 68 4602 4457 4565 5 -2 221 C ATOM 1411 O ARG A 68 8.544 7.345 10.334 1.00 35.07 O ANISOU 1411 O ARG B 68 4446 4414 4465 126 102 481 O ATOM 1412 CB ARG A 68 11.277 6.414 10.781 1.00 38.25 C ANISOU 1412 CB ARG B 68 4792 4842 4899 -124 0 158 C ATOM 1413 CG ARG A 68 10.799 5.112 11.505 1.00 38.01 C ANISOU 1413 CG ARG B 68 4849 4713 4879 -87 -28 93 C ATOM 1414 CD ARG A 68 11.383 4.886 12.866 1.00 37.24 C ANISOU 1414 CD ARG B 68 4663 4678 4807 -83 55 140 C ATOM 1415 NE ARG A 68 12.827 4.677 12.810 1.00 36.04 N ANISOU 1415 NE ARG B 68 4586 4404 4703 -28 57 351 N ATOM 1416 CZ ARG A 68 13.720 5.090 13.712 1.00 36.45 C ANISOU 1416 CZ ARG B 68 4690 4484 4675 -11 27 131 C ATOM 1417 NH1 ARG A 68 13.388 5.756 14.823 1.00 37.00 N ANISOU 1417 NH1 ARG B 68 4656 4623 4777 -82 59 152 N ATOM 1418 NH2 ARG A 68 15.001 4.818 13.494 1.00 38.81 N ANISOU 1418 NH2 ARG B 68 4767 4928 5051 -80 8 197 N ATOM 1419 N THR A 69 8.526 5.570 8.968 1.00 33.90 N ANISOU 1419 N THR B 69 4259 4325 4293 17 -2 337 N ATOM 1420 CA THR A 69 7.113 5.241 9.036 1.00 32.39 C ANISOU 1420 CA THR B 69 4180 3919 4206 -35 45 382 C ATOM 1421 C THR A 69 7.011 3.985 9.914 1.00 29.84 C ANISOU 1421 C THR B 69 3758 3636 3942 22 130 427 C ATOM 1422 O THR A 69 7.907 3.169 9.868 1.00 29.71 O ANISOU 1422 O THR B 69 3840 3438 4009 -101 256 846 O ATOM 1423 CB THR A 69 6.644 4.950 7.614 1.00 32.60 C ANISOU 1423 CB THR B 69 4176 4014 4195 -34 29 222 C ATOM 1424 OG1 THR A 69 6.542 6.213 6.946 1.00 36.93 O ANISOU 1424 OG1 THR B 69 4730 4554 4746 9 10 418 O ATOM 1425 CG2 THR A 69 5.179 4.373 7.524 1.00 35.13 C ANISOU 1425 CG2 THR B 69 4477 4424 4447 -17 -7 133 C ATOM 1426 N TRP A 70 5.915 3.849 10.643 1.00 25.95 N ANISOU 1426 N TRP B 70 3348 3042 3467 37 6 568 N ATOM 1427 CA TRP A 70 5.652 2.586 11.416 1.00 23.79 C ANISOU 1427 CA TRP B 70 3046 2776 3216 -20 -50 317 C ATOM 1428 C TRP A 70 4.380 1.931 10.886 1.00 22.97 C ANISOU 1428 C TRP B 70 2885 2720 3120 18 -9 288 C ATOM 1429 O TRP A 70 3.433 2.639 10.496 1.00 23.15 O ANISOU 1429 O TRP B 70 2779 2782 3234 53 -5 611 O ATOM 1430 CB TRP A 70 5.421 2.915 12.865 1.00 23.01 C ANISOU 1430 CB TRP B 70 2956 2689 3096 45 -99 305 C ATOM 1431 CG TRP A 70 6.599 3.402 13.591 1.00 24.30 C ANISOU 1431 CG TRP B 70 2987 2972 3272 -41 -142 308 C ATOM 1432 CD1 TRP A 70 6.953 4.673 13.802 1.00 25.30 C ANISOU 1432 CD1 TRP B 70 3152 3032 3425 40 -288 127 C ATOM 1433 CD2 TRP A 70 7.590 2.595 14.227 1.00 24.56 C ANISOU 1433 CD2 TRP B 70 2869 2878 3584 -5 -173 208 C ATOM 1434 NE1 TRP A 70 8.110 4.741 14.544 1.00 25.82 N ANISOU 1434 NE1 TRP B 70 3067 3042 3701 -334 -229 239 N ATOM 1435 CE2 TRP A 70 8.536 3.470 14.802 1.00 24.47 C ANISOU 1435 CE2 TRP B 70 3001 3007 3288 -13 -134 196 C ATOM 1436 CE3 TRP A 70 7.779 1.200 14.369 1.00 25.06 C ANISOU 1436 CE3 TRP B 70 3013 3140 3365 -95 4 241 C ATOM 1437 CZ2 TRP A 70 9.641 3.007 15.517 1.00 25.41 C ANISOU 1437 CZ2 TRP B 70 2941 3203 3508 -88 -87 136 C ATOM 1438 CZ3 TRP A 70 8.893 0.746 15.066 1.00 23.23 C ANISOU 1438 CZ3 TRP B 70 3016 2771 3037 -210 11 570 C ATOM 1439 CH2 TRP A 70 9.786 1.647 15.644 1.00 24.75 C ANISOU 1439 CH2 TRP B 70 3140 3102 3161 -21 -222 266 C ATOM 1440 N ARG A 71 4.378 0.599 10.819 1.00 21.04 N ANISOU 1440 N ARG B 71 2666 2588 2741 36 -59 339 N ATOM 1441 CA ARG A 71 3.189 -0.200 10.490 1.00 20.15 C ANISOU 1441 CA ARG B 71 2597 2413 2645 -16 -26 410 C ATOM 1442 C ARG A 71 3.026 -1.270 11.585 1.00 20.01 C ANISOU 1442 C ARG B 71 2503 2516 2582 -42 -12 428 C ATOM 1443 O ARG A 71 3.933 -1.485 12.386 1.00 19.63 O ANISOU 1443 O ARG B 71 2405 2453 2598 -152 129 646 O ATOM 1444 CB ARG A 71 3.286 -0.883 9.151 1.00 21.63 C ANISOU 1444 CB ARG B 71 2741 2746 2730 -41 -53 388 C ATOM 1445 CG ARG A 71 3.339 0.132 7.947 1.00 23.69 C ANISOU 1445 CG ARG B 71 3252 2788 2960 -33 18 465 C ATOM 1446 CD ARG A 71 3.534 -0.518 6.645 1.00 26.68 C ANISOU 1446 CD ARG B 71 3644 3130 3362 9 -11 220 C ATOM 1447 NE ARG A 71 3.600 0.456 5.534 1.00 30.60 N ANISOU 1447 NE ARG B 71 4188 3865 3573 -25 123 446 N ATOM 1448 CZ ARG A 71 2.542 1.003 4.898 1.00 34.10 C ANISOU 1448 CZ ARG B 71 4343 4383 4228 41 -6 189 C ATOM 1449 NH1 ARG A 71 1.270 0.680 5.169 1.00 35.19 N ANISOU 1449 NH1 ARG B 71 4498 4508 4363 -81 37 343 N ATOM 1450 NH2 ARG A 71 2.771 1.896 3.931 1.00 35.71 N ANISOU 1450 NH2 ARG B 71 4686 4449 4433 -63 48 394 N ATOM 1451 N GLU A 72 1.844 -1.840 11.624 1.00 18.92 N ANISOU 1451 N GLU B 72 2447 2300 2439 -83 -83 442 N ATOM 1452 CA GLU A 72 1.500 -2.853 12.631 1.00 18.09 C ANISOU 1452 CA GLU B 72 2347 2216 2310 16 -15 311 C ATOM 1453 C GLU A 72 0.882 -4.109 12.080 1.00 17.61 C ANISOU 1453 C GLU B 72 2359 2248 2082 0 -118 244 C ATOM 1454 O GLU A 72 0.355 -4.164 10.968 1.00 17.74 O ANISOU 1454 O GLU B 72 2470 2222 2046 78 -184 495 O ATOM 1455 CB GLU A 72 0.590 -2.253 13.700 1.00 18.90 C ANISOU 1455 CB GLU B 72 2641 2307 2232 34 -30 188 C ATOM 1456 CG GLU A 72 -0.720 -1.692 13.178 1.00 18.47 C ANISOU 1456 CG GLU B 72 2448 2068 2499 4 114 92 C ATOM 1457 CD GLU A 72 -1.743 -1.440 14.254 1.00 24.05 C ANISOU 1457 CD GLU B 72 3335 2703 3098 202 409 67 C ATOM 1458 OE1 GLU A 72 -2.353 -0.362 14.265 1.00 25.78 O ANISOU 1458 OE1 GLU B 72 3603 2829 3363 395 611 310 O ATOM 1459 OE2 GLU A 72 -1.952 -2.312 15.101 1.00 27.95 O ANISOU 1459 OE2 GLU B 72 3816 3206 3595 201 594 315 O ATOM 1460 N ALA A 73 0.881 -5.143 12.919 1.00 16.32 N ANISOU 1460 N ALA B 73 2328 1919 1952 -25 -70 267 N ATOM 1461 CA ALA A 73 0.311 -6.424 12.518 1.00 15.86 C ANISOU 1461 CA ALA B 73 2151 1994 1878 5 30 159 C ATOM 1462 C ALA A 73 -0.173 -7.122 13.771 1.00 15.34 C ANISOU 1462 C ALA B 73 2074 1918 1835 -10 37 224 C ATOM 1463 O ALA A 73 0.487 -7.020 14.808 1.00 16.15 O ANISOU 1463 O ALA B 73 2214 2055 1865 -66 94 268 O ATOM 1464 CB ALA A 73 1.334 -7.291 11.797 1.00 17.96 C ANISOU 1464 CB ALA B 73 2382 2165 2277 66 67 158 C ATOM 1465 N ASP A 74 -1.322 -7.761 13.668 1.00 15.07 N ANISOU 1465 N ASP B 74 2151 1887 1687 28 44 140 N ATOM 1466 CA ASP A 74 -1.871 -8.543 14.787 1.00 13.73 C ANISOU 1466 CA ASP B 74 2024 1632 1561 112 79 74 C ATOM 1467 C ASP A 74 -1.092 -9.844 14.919 1.00 14.21 C ANISOU 1467 C ASP B 74 2188 1609 1600 139 103 107 C ATOM 1468 O ASP A 74 -0.755 -10.462 13.945 1.00 16.83 O ANISOU 1468 O ASP B 74 2609 1979 1805 254 88 12 O ATOM 1469 CB ASP A 74 -3.306 -8.936 14.565 1.00 14.36 C ANISOU 1469 CB ASP B 74 1929 1824 1701 125 188 114 C ATOM 1470 CG ASP A 74 -4.275 -7.786 14.676 1.00 14.53 C ANISOU 1470 CG ASP B 74 1970 1587 1963 98 10 110 C ATOM 1471 OD1 ASP A 74 -3.880 -6.575 14.647 1.00 16.37 O ANISOU 1471 OD1 ASP B 74 2268 1698 2252 -65 198 -124 O ATOM 1472 OD2 ASP A 74 -5.487 -8.030 14.863 1.00 16.97 O ANISOU 1472 OD2 ASP B 74 2090 1905 2453 233 196 198 O ATOM 1473 N ILE A 75 -0.901 -10.259 16.165 1.00 13.58 N ANISOU 1473 N ILE B 75 2150 1666 1342 207 109 31 N ATOM 1474 CA ILE A 75 -0.144 -11.470 16.495 1.00 13.74 C ANISOU 1474 CA ILE B 75 1916 1585 1719 104 113 107 C ATOM 1475 C ILE A 75 -1.020 -12.391 17.286 1.00 14.92 C ANISOU 1475 C ILE B 75 2047 1741 1880 66 121 43 C ATOM 1476 O ILE A 75 -1.861 -11.912 18.041 1.00 15.22 O ANISOU 1476 O ILE B 75 2340 1693 1748 35 171 -36 O ATOM 1477 CB ILE A 75 1.135 -11.076 17.273 1.00 14.64 C ANISOU 1477 CB ILE B 75 2100 1675 1784 27 79 41 C ATOM 1478 CG1 ILE A 75 2.068 -10.278 16.359 1.00 15.65 C ANISOU 1478 CG1 ILE B 75 2111 1977 1857 70 140 99 C ATOM 1479 CG2 ILE A 75 1.890 -12.295 17.858 1.00 15.81 C ANISOU 1479 CG2 ILE B 75 2081 2026 1898 54 -50 130 C ATOM 1480 CD1 ILE A 75 2.708 -11.063 15.209 1.00 17.68 C ANISOU 1480 CD1 ILE B 75 2387 2274 2057 66 159 43 C ATOM 1481 N ASN A 76 -0.837 -13.702 17.071 1.00 15.16 N ANISOU 1481 N ASN B 76 2180 1719 1860 -144 31 -2 N ATOM 1482 CA ASN A 76 -1.597 -14.718 17.816 1.00 16.80 C ANISOU 1482 CA ASN B 76 2342 1941 2100 -143 88 72 C ATOM 1483 C ASN A 76 -3.111 -14.791 17.531 1.00 16.51 C ANISOU 1483 C ASN B 76 2300 1938 2034 -67 96 122 C ATOM 1484 O ASN A 76 -3.864 -15.487 18.256 1.00 19.05 O ANISOU 1484 O ASN B 76 2720 2288 2228 -279 140 534 O ATOM 1485 CB ASN A 76 -1.322 -14.586 19.335 1.00 16.80 C ANISOU 1485 CB ASN B 76 2432 1875 2075 -204 94 64 C ATOM 1486 CG ASN A 76 0.092 -14.847 19.721 1.00 17.79 C ANISOU 1486 CG ASN B 76 2592 1916 2249 -189 27 180 C ATOM 1487 OD1 ASN A 76 0.799 -15.699 19.134 1.00 19.90 O ANISOU 1487 OD1 ASN B 76 2940 2191 2430 147 -184 341 O ATOM 1488 ND2 ASN A 76 0.556 -14.104 20.739 1.00 19.70 N ANISOU 1488 ND2 ASN B 76 3174 2129 2181 -33 6 79 N ATOM 1489 N TYR A 77 -3.570 -14.189 16.446 1.00 16.04 N ANISOU 1489 N TYR B 77 2304 1722 2067 -124 29 76 N ATOM 1490 CA TYR A 77 -4.976 -14.179 16.071 1.00 16.29 C ANISOU 1490 CA TYR B 77 2295 1874 2017 -34 72 148 C ATOM 1491 C TYR A 77 -5.314 -15.481 15.323 1.00 16.79 C ANISOU 1491 C TYR B 77 2331 1987 2058 -4 40 68 C ATOM 1492 O TYR A 77 -4.600 -15.886 14.399 1.00 17.10 O ANISOU 1492 O TYR B 77 2460 1845 2190 19 122 167 O ATOM 1493 CB TYR A 77 -5.323 -12.967 15.178 1.00 17.12 C ANISOU 1493 CB TYR B 77 2325 2114 2064 -25 -29 155 C ATOM 1494 CG TYR A 77 -6.770 -12.969 14.830 1.00 16.01 C ANISOU 1494 CG TYR B 77 2157 2022 1903 -104 46 226 C ATOM 1495 CD1 TYR A 77 -7.727 -12.581 15.760 1.00 16.63 C ANISOU 1495 CD1 TYR B 77 2289 1920 2109 38 5 5 C ATOM 1496 CD2 TYR A 77 -7.213 -13.451 13.592 1.00 16.73 C ANISOU 1496 CD2 TYR B 77 2307 2142 1907 100 229 -20 C ATOM 1497 CE1 TYR A 77 -9.078 -12.597 15.454 1.00 17.95 C ANISOU 1497 CE1 TYR B 77 2337 2249 2233 -37 43 54 C ATOM 1498 CE2 TYR A 77 -8.554 -13.506 13.280 1.00 17.96 C ANISOU 1498 CE2 TYR B 77 2461 2328 2036 -48 22 152 C ATOM 1499 CZ TYR A 77 -9.490 -13.068 14.210 1.00 17.92 C ANISOU 1499 CZ TYR B 77 2390 2181 2236 144 -38 162 C ATOM 1500 OH TYR A 77 -10.810 -13.131 13.898 1.00 19.42 O ANISOU 1500 OH TYR B 77 2477 2760 2139 85 -50 330 O ATOM 1501 N VAL A 78 -6.434 -16.078 15.714 1.00 17.06 N ANISOU 1501 N VAL B 78 2361 1960 2162 -59 -3 100 N ATOM 1502 CA VAL A 78 -7.006 -17.253 15.045 1.00 18.97 C ANISOU 1502 CA VAL B 78 2596 2259 2351 -74 -13 57 C ATOM 1503 C VAL A 78 -8.423 -16.932 14.603 1.00 19.32 C ANISOU 1503 C VAL B 78 2626 2333 2381 -109 12 19 C ATOM 1504 O VAL A 78 -8.774 -17.095 13.429 1.00 20.35 O ANISOU 1504 O VAL B 78 2797 2540 2392 -187 -61 229 O ATOM 1505 CB VAL A 78 -6.961 -18.501 15.963 1.00 20.07 C ANISOU 1505 CB VAL B 78 2676 2528 2420 -50 4 49 C ATOM 1506 CG1 VAL A 78 -7.624 -19.688 15.285 1.00 20.63 C ANISOU 1506 CG1 VAL B 78 2867 2294 2677 -90 -73 156 C ATOM 1507 CG2 VAL A 78 -5.546 -18.838 16.314 1.00 21.41 C ANISOU 1507 CG2 VAL B 78 2904 2371 2858 3 -53 205 C ATOM 1508 N SER A 79 -9.268 -16.532 15.538 1.00 19.94 N ANISOU 1508 N SER B 79 2625 2527 2424 -124 -1 99 N ATOM 1509 CA SER A 79 -10.653 -16.248 15.246 1.00 21.37 C ANISOU 1509 CA SER B 79 2784 2744 2591 -43 23 122 C ATOM 1510 C SER A 79 -11.290 -15.423 16.342 1.00 21.02 C ANISOU 1510 C SER B 79 2723 2621 2639 -30 14 30 C ATOM 1511 O SER A 79 -10.740 -15.299 17.423 1.00 22.30 O ANISOU 1511 O SER B 79 2745 3054 2673 -13 113 81 O ATOM 1512 CB SER A 79 -11.441 -17.554 15.029 1.00 22.00 C ANISOU 1512 CB SER B 79 2953 2692 2711 20 -35 49 C ATOM 1513 OG SER A 79 -11.555 -18.262 16.225 1.00 25.27 O ANISOU 1513 OG SER B 79 3277 3272 3049 -217 75 371 O ATOM 1514 N GLY A 80 -12.449 -14.855 16.050 1.00 21.91 N ANISOU 1514 N GLY B 80 2768 2884 2670 11 49 14 N ATOM 1515 CA GLY A 80 -13.170 -14.028 17.012 1.00 21.30 C ANISOU 1515 CA GLY B 80 2743 2768 2579 13 24 43 C ATOM 1516 C GLY A 80 -12.729 -12.590 16.978 1.00 21.20 C ANISOU 1516 C GLY B 80 2718 2758 2576 54 77 29 C ATOM 1517 O GLY A 80 -12.241 -12.065 15.952 1.00 20.02 O ANISOU 1517 O GLY B 80 2664 2619 2321 69 143 303 O ATOM 1518 N PHE A 81 -12.909 -11.909 18.095 1.00 21.49 N ANISOU 1518 N PHE B 81 2711 2919 2533 -13 125 67 N ATOM 1519 CA PHE A 81 -12.504 -10.512 18.228 1.00 21.32 C ANISOU 1519 CA PHE B 81 2741 2788 2571 53 55 21 C ATOM 1520 C PHE A 81 -11.001 -10.407 18.257 1.00 20.86 C ANISOU 1520 C PHE B 81 2686 2643 2596 48 58 6 C ATOM 1521 O PHE A 81 -10.317 -11.373 18.626 1.00 22.39 O ANISOU 1521 O PHE B 81 2766 2878 2860 -7 109 174 O ATOM 1522 CB PHE A 81 -13.120 -9.863 19.482 1.00 22.30 C ANISOU 1522 CB PHE B 81 2840 2972 2659 156 77 42 C ATOM 1523 CG PHE A 81 -14.598 -9.713 19.394 1.00 24.12 C ANISOU 1523 CG PHE B 81 2925 3172 3065 27 144 -36 C ATOM 1524 CD1 PHE A 81 -15.464 -10.734 19.833 1.00 27.98 C ANISOU 1524 CD1 PHE B 81 3446 3410 3772 -17 23 96 C ATOM 1525 CD2 PHE A 81 -15.128 -8.577 18.824 1.00 26.78 C ANISOU 1525 CD2 PHE B 81 3430 3396 3346 37 96 33 C ATOM 1526 CE1 PHE A 81 -16.846 -10.582 19.730 1.00 28.98 C ANISOU 1526 CE1 PHE B 81 3508 3478 4025 -52 130 127 C ATOM 1527 CE2 PHE A 81 -16.506 -8.398 18.717 1.00 28.61 C ANISOU 1527 CE2 PHE B 81 3522 3716 3631 -9 -70 72 C ATOM 1528 CZ PHE A 81 -17.369 -9.413 19.152 1.00 30.38 C ANISOU 1528 CZ PHE B 81 3625 3909 4008 58 73 199 C ATOM 1529 N ARG A 82 -10.479 -9.243 17.857 1.00 20.69 N ANISOU 1529 N ARG B 82 2583 2666 2611 14 132 46 N ATOM 1530 CA ARG A 82 -9.029 -8.991 17.881 1.00 20.66 C ANISOU 1530 CA ARG B 82 2607 2620 2623 80 75 18 C ATOM 1531 C ARG A 82 -8.568 -8.956 19.320 1.00 20.03 C ANISOU 1531 C ARG B 82 2489 2615 2506 36 120 -61 C ATOM 1532 O ARG A 82 -9.340 -8.596 20.242 1.00 21.98 O ANISOU 1532 O ARG B 82 2700 3007 2642 132 324 -50 O ATOM 1533 CB ARG A 82 -8.625 -7.702 17.149 1.00 20.66 C ANISOU 1533 CB ARG B 82 2593 2645 2611 15 119 -13 C ATOM 1534 CG ARG A 82 -8.920 -7.772 15.660 1.00 20.35 C ANISOU 1534 CG ARG B 82 2589 2502 2638 70 61 -119 C ATOM 1535 CD ARG A 82 -8.825 -6.442 14.979 1.00 22.55 C ANISOU 1535 CD ARG B 82 2788 3034 2746 -2 -47 143 C ATOM 1536 NE ARG A 82 -7.459 -5.950 14.962 1.00 19.51 N ANISOU 1536 NE ARG B 82 2481 2417 2513 182 154 149 N ATOM 1537 CZ ARG A 82 -7.075 -4.696 14.804 1.00 22.07 C ANISOU 1537 CZ ARG B 82 2746 2661 2978 160 55 -1 C ATOM 1538 NH1 ARG A 82 -7.973 -3.711 14.711 1.00 23.65 N ANISOU 1538 NH1 ARG B 82 3170 2498 3319 368 4 199 N ATOM 1539 NH2 ARG A 82 -5.795 -4.407 14.791 1.00 20.29 N ANISOU 1539 NH2 ARG B 82 2743 2131 2834 188 108 187 N ATOM 1540 N ASN A 83 -7.346 -9.415 19.511 1.00 19.06 N ANISOU 1540 N ASN B 83 2403 2503 2336 -1 191 42 N ATOM 1541 CA ASN A 83 -6.692 -9.508 20.798 1.00 17.78 C ANISOU 1541 CA ASN B 83 2266 2265 2222 -2 147 8 C ATOM 1542 C ASN A 83 -5.837 -8.260 21.100 1.00 17.95 C ANISOU 1542 C ASN B 83 2325 2286 2208 63 160 26 C ATOM 1543 O ASN A 83 -5.968 -7.267 20.419 1.00 20.02 O ANISOU 1543 O ASN B 83 2733 2401 2470 14 119 144 O ATOM 1544 CB ASN A 83 -5.937 -10.842 20.870 1.00 17.94 C ANISOU 1544 CB ASN B 83 2392 2185 2237 -4 218 108 C ATOM 1545 CG ASN A 83 -4.779 -10.927 19.935 1.00 16.73 C ANISOU 1545 CG ASN B 83 2327 1784 2245 -43 216 -76 C ATOM 1546 OD1 ASN A 83 -4.244 -9.867 19.483 1.00 16.47 O ANISOU 1546 OD1 ASN B 83 2418 1753 2085 -76 225 4 O ATOM 1547 ND2 ASN A 83 -4.378 -12.176 19.583 1.00 17.64 N ANISOU 1547 ND2 ASN B 83 2579 1891 2231 178 241 7 N ATOM 1548 N ALA A 84 -4.988 -8.334 22.115 1.00 17.32 N ANISOU 1548 N ALA B 84 2178 2193 2208 97 131 -38 N ATOM 1549 CA ALA A 84 -4.121 -7.255 22.537 1.00 17.30 C ANISOU 1549 CA ALA B 84 2202 2241 2129 18 90 3 C ATOM 1550 C ALA A 84 -2.673 -7.327 22.035 1.00 15.71 C ANISOU 1550 C ALA B 84 2116 1867 1985 13 215 -92 C ATOM 1551 O ALA A 84 -1.847 -6.486 22.409 1.00 17.28 O ANISOU 1551 O ALA B 84 2186 2132 2247 -46 380 -136 O ATOM 1552 CB ALA A 84 -4.111 -7.218 24.060 1.00 19.16 C ANISOU 1552 CB ALA B 84 2469 2558 2250 43 127 -2 C ATOM 1553 N ASP A 85 -2.354 -8.303 21.190 1.00 13.63 N ANISOU 1553 N ASP B 85 2007 1555 1617 -110 178 -8 N ATOM 1554 CA ASP A 85 -0.997 -8.547 20.808 1.00 12.98 C ANISOU 1554 CA ASP B 85 1906 1477 1548 -25 96 -6 C ATOM 1555 C ASP A 85 -0.714 -7.950 19.428 1.00 12.42 C ANISOU 1555 C ASP B 85 1866 1351 1501 9 32 24 C ATOM 1556 O ASP A 85 -1.416 -8.230 18.450 1.00 13.78 O ANISOU 1556 O ASP B 85 2123 1430 1680 -47 74 112 O ATOM 1557 CB ASP A 85 -0.772 -10.062 20.680 1.00 13.56 C ANISOU 1557 CB ASP B 85 2081 1433 1639 80 264 2 C ATOM 1558 CG ASP A 85 -0.811 -10.802 21.997 1.00 18.32 C ANISOU 1558 CG ASP B 85 2932 1993 2033 -1 115 116 C ATOM 1559 OD1 ASP A 85 -0.701 -10.194 23.076 1.00 21.86 O ANISOU 1559 OD1 ASP B 85 3711 2241 2353 -227 -174 94 O ATOM 1560 OD2 ASP A 85 -0.976 -12.032 22.029 1.00 20.65 O ANISOU 1560 OD2 ASP B 85 3424 1925 2496 -158 356 259 O ATOM 1561 N ARG A 86 0.342 -7.180 19.353 1.00 13.46 N ANISOU 1561 N ARG B 86 1993 1623 1497 -30 148 17 N ATOM 1562 CA ARG A 86 0.740 -6.526 18.105 1.00 14.64 C ANISOU 1562 CA ARG B 86 2073 1767 1721 -1 70 82 C ATOM 1563 C ARG A 86 2.237 -6.468 17.904 1.00 14.64 C ANISOU 1563 C ARG B 86 2046 1705 1808 23 -3 146 C ATOM 1564 O ARG A 86 3.007 -6.341 18.853 1.00 14.98 O ANISOU 1564 O ARG B 86 2243 1886 1561 -54 86 226 O ATOM 1565 CB ARG A 86 0.227 -5.096 18.025 1.00 14.96 C ANISOU 1565 CB ARG B 86 2115 1683 1883 17 57 90 C ATOM 1566 CG ARG A 86 -1.251 -4.841 18.294 1.00 17.02 C ANISOU 1566 CG ARG B 86 2233 2181 2050 -103 131 34 C ATOM 1567 CD ARG A 86 -2.146 -5.151 17.153 1.00 17.00 C ANISOU 1567 CD ARG B 86 2304 2120 2032 -99 27 99 C ATOM 1568 NE ARG A 86 -3.540 -4.879 17.434 1.00 18.44 N ANISOU 1568 NE ARG B 86 2481 2146 2380 161 -26 251 N ATOM 1569 CZ ARG A 86 -4.383 -5.728 18.012 1.00 17.72 C ANISOU 1569 CZ ARG B 86 2247 2154 2330 51 20 59 C ATOM 1570 NH1 ARG A 86 -4.013 -6.973 18.330 1.00 17.61 N ANISOU 1570 NH1 ARG B 86 2067 2175 2447 314 310 -60 N ATOM 1571 NH2 ARG A 86 -5.645 -5.376 18.242 1.00 20.80 N ANISOU 1571 NH2 ARG B 86 2390 2447 3062 188 58 263 N ATOM 1572 N LEU A 87 2.644 -6.559 16.647 1.00 14.62 N ANISOU 1572 N LEU B 87 2162 1598 1792 44 -19 114 N ATOM 1573 CA LEU A 87 4.006 -6.262 16.253 1.00 16.25 C ANISOU 1573 CA LEU B 87 2140 1927 2104 -4 -59 244 C ATOM 1574 C LEU A 87 3.959 -4.911 15.535 1.00 17.48 C ANISOU 1574 C LEU B 87 2284 2123 2232 -110 -141 382 C ATOM 1575 O LEU A 87 3.060 -4.661 14.730 1.00 18.20 O ANISOU 1575 O LEU B 87 2215 2072 2627 -222 -154 771 O ATOM 1576 CB LEU A 87 4.539 -7.381 15.337 1.00 18.00 C ANISOU 1576 CB LEU B 87 2587 2305 1947 92 -80 129 C ATOM 1577 CG LEU A 87 6.007 -7.618 15.229 1.00 25.21 C ANISOU 1577 CG LEU B 87 3056 3432 3088 -86 -23 -6 C ATOM 1578 CD1 LEU A 87 6.565 -8.072 16.590 1.00 28.10 C ANISOU 1578 CD1 LEU B 87 3654 3519 3504 119 -208 135 C ATOM 1579 CD2 LEU A 87 6.306 -8.738 14.278 1.00 28.70 C ANISOU 1579 CD2 LEU B 87 3587 3675 3642 69 36 -157 C ATOM 1580 N VAL A 88 4.889 -4.041 15.866 1.00 16.49 N ANISOU 1580 N VAL B 88 2214 1948 2101 -147 -170 569 N ATOM 1581 CA VAL A 88 4.941 -2.702 15.201 1.00 18.13 C ANISOU 1581 CA VAL B 88 2365 2203 2319 -24 -71 411 C ATOM 1582 C VAL A 88 6.329 -2.634 14.614 1.00 19.22 C ANISOU 1582 C VAL B 88 2398 2514 2390 -31 -72 386 C ATOM 1583 O VAL A 88 7.328 -2.831 15.331 1.00 19.83 O ANISOU 1583 O VAL B 88 2545 2554 2434 -150 -110 790 O ATOM 1584 CB VAL A 88 4.630 -1.630 16.195 1.00 19.32 C ANISOU 1584 CB VAL B 88 2538 2223 2578 24 -102 224 C ATOM 1585 CG1 VAL A 88 4.442 -0.230 15.523 1.00 22.29 C ANISOU 1585 CG1 VAL B 88 2921 2644 2902 28 19 296 C ATOM 1586 CG2 VAL A 88 3.351 -1.932 16.916 1.00 22.53 C ANISOU 1586 CG2 VAL B 88 2884 2819 2855 90 -39 28 C ATOM 1587 N TYR A 89 6.429 -2.326 13.316 1.00 19.88 N ANISOU 1587 N TYR B 89 2403 2715 2433 52 8 493 N ATOM 1588 CA TYR A 89 7.724 -2.434 12.597 1.00 20.69 C ANISOU 1588 CA TYR B 89 2505 2732 2623 5 48 422 C ATOM 1589 C TYR A 89 7.933 -1.150 11.798 1.00 22.38 C ANISOU 1589 C TYR B 89 2674 2931 2896 -67 16 486 C ATOM 1590 O TYR A 89 6.986 -0.606 11.238 1.00 22.60 O ANISOU 1590 O TYR B 89 2470 3072 3042 11 227 755 O ATOM 1591 CB TYR A 89 7.832 -3.668 11.716 1.00 21.24 C ANISOU 1591 CB TYR B 89 2581 2818 2670 -62 69 429 C ATOM 1592 CG TYR A 89 6.742 -3.847 10.693 1.00 22.92 C ANISOU 1592 CG TYR B 89 2778 3014 2914 -10 -17 188 C ATOM 1593 CD1 TYR A 89 6.961 -3.507 9.375 1.00 24.92 C ANISOU 1593 CD1 TYR B 89 3200 3291 2975 -15 51 99 C ATOM 1594 CD2 TYR A 89 5.475 -4.354 11.048 1.00 23.27 C ANISOU 1594 CD2 TYR B 89 2914 2987 2939 -139 46 198 C ATOM 1595 CE1 TYR A 89 5.960 -3.646 8.414 1.00 26.80 C ANISOU 1595 CE1 TYR B 89 3263 3604 3314 -84 -35 213 C ATOM 1596 CE2 TYR A 89 4.479 -4.487 10.119 1.00 24.88 C ANISOU 1596 CE2 TYR B 89 2952 3227 3274 -236 66 58 C ATOM 1597 CZ TYR A 89 4.718 -4.162 8.785 1.00 26.48 C ANISOU 1597 CZ TYR B 89 3291 3371 3397 -105 -62 199 C ATOM 1598 OH TYR A 89 3.747 -4.282 7.839 1.00 29.14 O ANISOU 1598 OH TYR B 89 3621 3689 3761 -225 -137 137 O ATOM 1599 N SER A 90 9.180 -0.684 11.777 1.00 23.38 N ANISOU 1599 N SER B 90 2789 3080 3011 -76 34 471 N ATOM 1600 CA SER A 90 9.515 0.589 11.105 1.00 24.41 C ANISOU 1600 CA SER B 90 3075 3047 3152 -6 -17 364 C ATOM 1601 C SER A 90 10.034 0.356 9.694 1.00 26.04 C ANISOU 1601 C SER B 90 3309 3265 3318 57 21 247 C ATOM 1602 O SER A 90 10.384 -0.742 9.305 1.00 23.94 O ANISOU 1602 O SER B 90 3119 3000 2976 83 14 680 O ATOM 1603 CB SER A 90 10.511 1.360 11.930 1.00 24.65 C ANISOU 1603 CB SER B 90 3217 2980 3166 0 69 327 C ATOM 1604 OG SER A 90 11.801 0.786 11.833 1.00 23.72 O ANISOU 1604 OG SER B 90 3073 2918 3019 59 25 908 O ATOM 1605 N SER A 91 10.053 1.427 8.891 1.00 28.26 N ANISOU 1605 N SER B 91 3532 3643 3559 14 38 369 N ATOM 1606 CA SER A 91 10.557 1.318 7.512 1.00 30.09 C ANISOU 1606 CA SER B 91 3793 3893 3744 57 13 151 C ATOM 1607 C SER A 91 12.068 0.978 7.427 1.00 31.35 C ANISOU 1607 C SER B 91 3902 4087 3920 16 33 133 C ATOM 1608 O SER A 91 12.528 0.396 6.428 1.00 32.71 O ANISOU 1608 O SER B 91 4023 4256 4150 67 8 198 O ATOM 1609 CB SER A 91 10.193 2.599 6.724 1.00 30.00 C ANISOU 1609 CB SER B 91 3823 3858 3717 17 69 261 C ATOM 1610 OG SER A 91 10.433 3.751 7.492 1.00 30.44 O ANISOU 1610 OG SER B 91 3985 3928 3652 -32 166 409 O ATOM 1611 N ASP A 92 12.788 1.285 8.509 1.00 31.60 N ANISOU 1611 N ASP B 92 3862 4110 4033 -44 33 254 N ATOM 1612 CA ASP A 92 14.185 0.870 8.675 1.00 32.17 C ANISOU 1612 CA ASP B 92 3981 4191 4048 7 21 200 C ATOM 1613 C ASP A 92 14.372 -0.385 9.576 1.00 31.92 C ANISOU 1613 C ASP B 92 3892 4175 4062 -31 -45 235 C ATOM 1614 O ASP A 92 15.431 -0.583 10.144 1.00 32.97 O ANISOU 1614 O ASP B 92 3717 4639 4170 -34 43 439 O ATOM 1615 CB ASP A 92 15.045 2.040 9.101 1.00 32.22 C ANISOU 1615 CB ASP B 92 3961 4177 4101 -34 3 183 C ATOM 1616 CG ASP A 92 14.600 2.695 10.372 1.00 32.69 C ANISOU 1616 CG ASP B 92 3999 4290 4131 -12 32 122 C ATOM 1617 OD1 ASP A 92 15.380 3.511 10.871 1.00 32.94 O ANISOU 1617 OD1 ASP B 92 3693 4290 4530 -454 350 458 O ATOM 1618 OD2 ASP A 92 13.485 2.531 10.944 1.00 32.59 O ANISOU 1618 OD2 ASP B 92 3877 4053 4453 -42 180 697 O ATOM 1619 N TRP A 93 13.324 -1.204 9.691 1.00 31.14 N ANISOU 1619 N TRP B 93 3798 4133 3900 3 12 216 N ATOM 1620 CA TRP A 93 13.368 -2.547 10.272 1.00 30.76 C ANISOU 1620 CA TRP B 93 3831 4013 3843 27 -9 126 C ATOM 1621 C TRP A 93 13.619 -2.687 11.783 1.00 27.78 C ANISOU 1621 C TRP B 93 3398 3661 3496 -13 83 92 C ATOM 1622 O TRP A 93 14.064 -3.758 12.225 1.00 28.35 O ANISOU 1622 O TRP B 93 3479 3928 3362 113 63 229 O ATOM 1623 CB TRP A 93 14.249 -3.505 9.411 1.00 31.89 C ANISOU 1623 CB TRP B 93 4032 4106 3978 0 16 102 C ATOM 1624 CG TRP A 93 13.774 -3.453 7.997 1.00 36.55 C ANISOU 1624 CG TRP B 93 4709 4824 4353 -7 -49 60 C ATOM 1625 CD1 TRP A 93 14.422 -2.886 6.923 1.00 39.91 C ANISOU 1625 CD1 TRP B 93 5027 5299 4837 -69 126 112 C ATOM 1626 CD2 TRP A 93 12.471 -3.829 7.530 1.00 38.87 C ANISOU 1626 CD2 TRP B 93 4840 5081 4845 -50 -67 51 C ATOM 1627 NE1 TRP A 93 13.619 -2.952 5.807 1.00 40.71 N ANISOU 1627 NE1 TRP B 93 5156 5418 4893 -90 32 89 N ATOM 1628 CE2 TRP A 93 12.410 -3.507 6.150 1.00 40.77 C ANISOU 1628 CE2 TRP B 93 5181 5324 4985 -66 -6 -40 C ATOM 1629 CE3 TRP A 93 11.338 -4.409 8.141 1.00 39.36 C ANISOU 1629 CE3 TRP B 93 4983 5018 4953 -68 -45 28 C ATOM 1630 CZ2 TRP A 93 11.267 -3.763 5.361 1.00 40.67 C ANISOU 1630 CZ2 TRP B 93 5072 5246 5133 4 -31 -30 C ATOM 1631 CZ3 TRP A 93 10.204 -4.656 7.359 1.00 40.74 C ANISOU 1631 CZ3 TRP B 93 5094 5242 5143 -104 -14 6 C ATOM 1632 CH2 TRP A 93 10.183 -4.341 5.980 1.00 40.92 C ANISOU 1632 CH2 TRP B 93 5176 5237 5135 -31 -36 53 C ATOM 1633 N LEU A 94 13.267 -1.665 12.548 1.00 25.40 N ANISOU 1633 N LEU B 94 3116 3344 3191 -137 -46 229 N ATOM 1634 CA LEU A 94 13.144 -1.770 14.026 1.00 23.20 C ANISOU 1634 CA LEU B 94 2788 3033 2992 -82 -17 251 C ATOM 1635 C LEU A 94 11.842 -2.552 14.239 1.00 22.02 C ANISOU 1635 C LEU B 94 2707 2848 2810 -99 -47 401 C ATOM 1636 O LEU A 94 10.848 -2.249 13.569 1.00 21.73 O ANISOU 1636 O LEU B 94 2837 2475 2942 -128 -38 793 O ATOM 1637 CB LEU A 94 13.043 -0.423 14.732 1.00 23.46 C ANISOU 1637 CB LEU B 94 2832 3078 3003 -113 -37 268 C ATOM 1638 CG LEU A 94 14.255 0.534 14.655 1.00 26.91 C ANISOU 1638 CG LEU B 94 3234 3496 3492 -162 -1 188 C ATOM 1639 CD1 LEU A 94 13.925 1.780 15.385 1.00 28.23 C ANISOU 1639 CD1 LEU B 94 3556 3422 3746 -296 81 151 C ATOM 1640 CD2 LEU A 94 15.485 -0.046 15.262 1.00 29.34 C ANISOU 1640 CD2 LEU B 94 3584 3734 3829 -16 -88 167 C ATOM 1641 N ILE A 95 11.831 -3.546 15.156 1.00 18.84 N ANISOU 1641 N ILE B 95 2392 2319 2448 92 -89 316 N ATOM 1642 CA ILE A 95 10.624 -4.334 15.399 1.00 18.26 C ANISOU 1642 CA ILE B 95 2302 2414 2220 48 -36 145 C ATOM 1643 C ILE A 95 10.355 -4.367 16.891 1.00 17.35 C ANISOU 1643 C ILE B 95 2152 2238 2203 33 -19 91 C ATOM 1644 O ILE A 95 11.218 -4.738 17.650 1.00 17.28 O ANISOU 1644 O ILE B 95 2277 2125 2164 144 9 332 O ATOM 1645 CB ILE A 95 10.664 -5.763 14.792 1.00 18.23 C ANISOU 1645 CB ILE B 95 2360 2381 2183 10 8 177 C ATOM 1646 CG1 ILE A 95 10.948 -5.686 13.268 1.00 20.69 C ANISOU 1646 CG1 ILE B 95 2721 2729 2409 -5 84 181 C ATOM 1647 CG2 ILE A 95 9.358 -6.466 15.082 1.00 19.21 C ANISOU 1647 CG2 ILE B 95 2327 2678 2292 -65 -39 119 C ATOM 1648 CD1 ILE A 95 11.048 -6.950 12.537 1.00 23.91 C ANISOU 1648 CD1 ILE B 95 3155 3213 2717 8 45 -32 C ATOM 1649 N TYR A 96 9.159 -3.922 17.271 1.00 15.57 N ANISOU 1649 N TYR B 96 2054 1758 2103 148 35 66 N ATOM 1650 CA TYR A 96 8.700 -3.896 18.662 1.00 16.33 C ANISOU 1650 CA TYR B 96 2117 1980 2107 67 -35 74 C ATOM 1651 C TYR A 96 7.426 -4.732 18.813 1.00 16.13 C ANISOU 1651 C TYR B 96 2164 1836 2128 59 -67 107 C ATOM 1652 O TYR A 96 6.675 -4.928 17.857 1.00 17.44 O ANISOU 1652 O TYR B 96 2330 2112 2185 -94 -200 423 O ATOM 1653 CB TYR A 96 8.375 -2.474 19.111 1.00 16.02 C ANISOU 1653 CB TYR B 96 2143 1783 2158 21 23 99 C ATOM 1654 CG TYR A 96 9.573 -1.563 19.368 1.00 16.36 C ANISOU 1654 CG TYR B 96 2159 1703 2352 104 -77 104 C ATOM 1655 CD1 TYR A 96 10.355 -1.120 18.309 1.00 19.58 C ANISOU 1655 CD1 TYR B 96 2452 2399 2589 -108 -46 0 C ATOM 1656 CD2 TYR A 96 9.891 -1.126 20.662 1.00 18.27 C ANISOU 1656 CD2 TYR B 96 2460 1946 2536 -61 47 104 C ATOM 1657 CE1 TYR A 96 11.444 -0.268 18.547 1.00 20.02 C ANISOU 1657 CE1 TYR B 96 2662 2239 2705 -230 25 294 C ATOM 1658 CE2 TYR A 96 10.970 -0.293 20.902 1.00 19.40 C ANISOU 1658 CE2 TYR B 96 2538 2114 2718 137 -70 -44 C ATOM 1659 CZ TYR A 96 11.718 0.143 19.851 1.00 18.33 C ANISOU 1659 CZ TYR B 96 2470 1776 2718 62 -31 34 C ATOM 1660 OH TYR A 96 12.787 0.961 20.097 1.00 24.41 O ANISOU 1660 OH TYR B 96 2875 2476 3922 -55 -180 48 O ATOM 1661 N LYS A 97 7.217 -5.256 20.015 1.00 15.94 N ANISOU 1661 N LYS B 97 1987 2100 1967 27 39 73 N ATOM 1662 CA LYS A 97 6.025 -6.006 20.344 1.00 15.13 C ANISOU 1662 CA LYS B 97 2050 1730 1968 85 36 1 C ATOM 1663 C LYS A 97 5.289 -5.288 21.502 1.00 14.35 C ANISOU 1663 C LYS B 97 1966 1672 1813 52 -10 -116 C ATOM 1664 O LYS A 97 5.905 -4.583 22.359 1.00 16.19 O ANISOU 1664 O LYS B 97 2149 1785 2217 214 27 -340 O ATOM 1665 CB LYS A 97 6.305 -7.458 20.703 1.00 15.48 C ANISOU 1665 CB LYS B 97 2203 1704 1972 41 154 -65 C ATOM 1666 CG LYS A 97 7.070 -7.684 21.903 1.00 16.89 C ANISOU 1666 CG LYS B 97 2490 1791 2136 175 24 -125 C ATOM 1667 CD LYS A 97 7.123 -9.184 22.287 1.00 18.78 C ANISOU 1667 CD LYS B 97 2788 1744 2602 22 99 127 C ATOM 1668 CE LYS A 97 7.959 -9.449 23.506 1.00 20.80 C ANISOU 1668 CE LYS B 97 3071 1971 2862 76 42 -136 C ATOM 1669 NZ LYS A 97 7.977 -10.974 23.745 1.00 23.51 N ANISOU 1669 NZ LYS B 97 3734 2106 3092 108 52 138 N ATOM 1670 N THR A 98 3.982 -5.427 21.484 1.00 14.09 N ANISOU 1670 N THR B 98 2039 1659 1655 37 73 -225 N ATOM 1671 CA THR A 98 3.134 -5.113 22.628 1.00 15.16 C ANISOU 1671 CA THR B 98 1977 1870 1911 65 102 -99 C ATOM 1672 C THR A 98 2.218 -6.262 22.889 1.00 16.06 C ANISOU 1672 C THR B 98 2125 2047 1927 16 99 -116 C ATOM 1673 O THR A 98 1.692 -6.871 21.950 1.00 15.05 O ANISOU 1673 O THR B 98 2234 1770 1713 43 235 -244 O ATOM 1674 CB THR A 98 2.391 -3.767 22.405 1.00 14.40 C ANISOU 1674 CB THR B 98 1932 1561 1976 -17 122 -73 C ATOM 1675 OG1 THR A 98 1.549 -3.515 23.546 1.00 16.12 O ANISOU 1675 OG1 THR B 98 2100 1888 2135 180 172 -192 O ATOM 1676 CG2 THR A 98 1.479 -3.797 21.189 1.00 16.13 C ANISOU 1676 CG2 THR B 98 2186 1890 2053 135 211 -3 C ATOM 1677 N THR A 99 1.991 -6.566 24.171 1.00 16.90 N ANISOU 1677 N THR B 99 2299 2203 1916 22 44 -90 N ATOM 1678 CA THR A 99 1.004 -7.567 24.582 1.00 17.67 C ANISOU 1678 CA THR B 99 2431 2202 2081 49 100 -69 C ATOM 1679 C THR A 99 -0.093 -6.929 25.426 1.00 18.03 C ANISOU 1679 C THR B 99 2479 2276 2094 47 202 -20 C ATOM 1680 O THR A 99 -0.890 -7.656 25.997 1.00 19.61 O ANISOU 1680 O THR B 99 2691 2374 2384 -7 427 -92 O ATOM 1681 CB THR A 99 1.659 -8.694 25.381 1.00 19.34 C ANISOU 1681 CB THR B 99 2534 2462 2352 116 32 -25 C ATOM 1682 OG1 THR A 99 2.355 -8.160 26.518 1.00 22.25 O ANISOU 1682 OG1 THR B 99 3277 2554 2619 -49 -212 81 O ATOM 1683 CG2 THR A 99 2.687 -9.425 24.531 1.00 22.09 C ANISOU 1683 CG2 THR B 99 2875 2723 2793 183 149 -66 C ATOM 1684 N ASP A 100 -0.152 -5.592 25.456 1.00 17.13 N ANISOU 1684 N ASP B 100 2463 2127 1915 145 314 -103 N ATOM 1685 CA ASP A 100 -1.150 -4.882 26.291 1.00 18.74 C ANISOU 1685 CA ASP B 100 2482 2379 2259 160 125 -133 C ATOM 1686 C ASP A 100 -1.826 -3.748 25.533 1.00 18.12 C ANISOU 1686 C ASP B 100 2522 2198 2162 184 4 -150 C ATOM 1687 O ASP A 100 -2.181 -2.654 26.099 1.00 19.73 O ANISOU 1687 O ASP B 100 2712 2282 2502 360 112 -367 O ATOM 1688 CB ASP A 100 -0.484 -4.411 27.589 1.00 18.75 C ANISOU 1688 CB ASP B 100 2551 2392 2179 138 39 -131 C ATOM 1689 CG ASP A 100 0.679 -3.480 27.370 1.00 19.14 C ANISOU 1689 CG ASP B 100 2521 2420 2331 131 -3 -124 C ATOM 1690 OD1 ASP A 100 1.446 -3.198 28.370 1.00 22.15 O ANISOU 1690 OD1 ASP B 100 3073 2980 2359 315 -129 -187 O ATOM 1691 OD2 ASP A 100 0.924 -2.957 26.263 1.00 17.74 O ANISOU 1691 OD2 ASP B 100 2394 1782 2562 232 120 -398 O ATOM 1692 N HIS A 101 -2.051 -3.975 24.223 1.00 18.10 N ANISOU 1692 N HIS B 101 2615 2123 2138 279 119 -214 N ATOM 1693 CA HIS A 101 -2.793 -3.025 23.406 1.00 19.65 C ANISOU 1693 CA HIS B 101 2567 2468 2429 139 33 -86 C ATOM 1694 C HIS A 101 -2.186 -1.623 23.404 1.00 19.30 C ANISOU 1694 C HIS B 101 2583 2380 2369 196 0 -154 C ATOM 1695 O HIS A 101 -2.852 -0.642 23.620 1.00 20.17 O ANISOU 1695 O HIS B 101 2621 2282 2758 454 -56 -210 O ATOM 1696 CB HIS A 101 -4.253 -3.059 23.832 1.00 21.37 C ANISOU 1696 CB HIS B 101 2768 2732 2618 138 -16 -63 C ATOM 1697 CG HIS A 101 -5.179 -2.510 22.816 1.00 24.42 C ANISOU 1697 CG HIS B 101 2964 3154 3159 280 -69 34 C ATOM 1698 ND1 HIS A 101 -5.957 -1.404 23.065 1.00 28.29 N ANISOU 1698 ND1 HIS B 101 3669 3243 3833 205 -62 -96 N ATOM 1699 CD2 HIS A 101 -5.492 -2.941 21.581 1.00 27.61 C ANISOU 1699 CD2 HIS B 101 3489 3528 3470 214 -68 -41 C ATOM 1700 CE1 HIS A 101 -6.700 -1.164 21.994 1.00 30.14 C ANISOU 1700 CE1 HIS B 101 3853 3853 3744 210 -147 -71 C ATOM 1701 NE2 HIS A 101 -6.429 -2.080 21.073 1.00 29.17 N ANISOU 1701 NE2 HIS B 101 3538 3706 3836 410 -154 -68 N ATOM 1702 N TYR A 102 -0.891 -1.567 23.172 1.00 17.99 N ANISOU 1702 N TYR B 102 2421 2083 2331 270 60 -197 N ATOM 1703 CA TYR A 102 -0.126 -0.357 22.903 1.00 19.17 C ANISOU 1703 CA TYR B 102 2440 2425 2418 117 24 -124 C ATOM 1704 C TYR A 102 0.235 0.475 24.128 1.00 20.10 C ANISOU 1704 C TYR B 102 2578 2348 2708 149 3 -190 C ATOM 1705 O TYR A 102 0.753 1.581 23.962 1.00 22.78 O ANISOU 1705 O TYR B 102 3106 2509 3040 11 17 -196 O ATOM 1706 CB TYR A 102 -0.788 0.554 21.845 1.00 19.60 C ANISOU 1706 CB TYR B 102 2566 2211 2668 225 70 -126 C ATOM 1707 CG TYR A 102 -1.350 -0.102 20.607 1.00 20.47 C ANISOU 1707 CG TYR B 102 2766 2455 2556 117 1 11 C ATOM 1708 CD1 TYR A 102 -0.522 -0.576 19.570 1.00 22.12 C ANISOU 1708 CD1 TYR B 102 2907 2644 2853 -69 141 130 C ATOM 1709 CD2 TYR A 102 -2.729 -0.276 20.472 1.00 20.77 C ANISOU 1709 CD2 TYR B 102 2713 2533 2644 279 9 -76 C ATOM 1710 CE1 TYR A 102 -1.095 -1.154 18.426 1.00 20.03 C ANISOU 1710 CE1 TYR B 102 3027 1981 2601 59 161 168 C ATOM 1711 CE2 TYR A 102 -3.298 -0.861 19.383 1.00 20.87 C ANISOU 1711 CE2 TYR B 102 2845 2301 2784 361 -76 99 C ATOM 1712 CZ TYR A 102 -2.475 -1.293 18.330 1.00 21.47 C ANISOU 1712 CZ TYR B 102 3028 2473 2656 170 78 112 C ATOM 1713 OH TYR A 102 -3.097 -1.875 17.260 1.00 22.97 O ANISOU 1713 OH TYR B 102 3306 2514 2906 80 -79 116 O ATOM 1714 N ALA A 103 0.024 -0.067 25.318 1.00 19.86 N ANISOU 1714 N ALA B 103 2589 2291 2662 172 27 -292 N ATOM 1715 CA ALA A 103 0.437 0.612 26.554 1.00 21.02 C ANISOU 1715 CA ALA B 103 2730 2506 2749 120 -58 -204 C ATOM 1716 C ALA A 103 1.951 0.591 26.746 1.00 21.64 C ANISOU 1716 C ALA B 103 2803 2485 2933 53 -10 -266 C ATOM 1717 O ALA A 103 2.568 1.607 27.093 1.00 23.41 O ANISOU 1717 O ALA B 103 3043 2528 3320 122 -44 -557 O ATOM 1718 CB ALA A 103 -0.275 -0.014 27.731 1.00 21.85 C ANISOU 1718 CB ALA B 103 2824 2600 2876 46 65 -226 C ATOM 1719 N THR A 104 2.569 -0.574 26.540 1.00 20.75 N ANISOU 1719 N THR B 104 2722 2444 2717 128 -79 -360 N ATOM 1720 CA THR A 104 4.012 -0.739 26.635 1.00 20.38 C ANISOU 1720 CA THR B 104 2615 2545 2584 62 89 -353 C ATOM 1721 C THR A 104 4.520 -1.500 25.402 1.00 19.61 C ANISOU 1721 C THR B 104 2524 2369 2555 59 100 -314 C ATOM 1722 O THR A 104 3.763 -2.247 24.783 1.00 18.09 O ANISOU 1722 O THR B 104 2425 2092 2357 260 174 -600 O ATOM 1723 CB THR A 104 4.462 -1.478 27.896 1.00 21.54 C ANISOU 1723 CB THR B 104 2646 2823 2716 67 141 -223 C ATOM 1724 OG1 THR A 104 3.983 -2.822 27.936 1.00 21.30 O ANISOU 1724 OG1 THR B 104 2763 2915 2413 149 90 -248 O ATOM 1725 CG2 THR A 104 3.913 -0.811 29.200 1.00 22.47 C ANISOU 1725 CG2 THR B 104 2875 2938 2723 260 60 -212 C ATOM 1726 N PHE A 105 5.770 -1.250 25.080 1.00 19.83 N ANISOU 1726 N PHE B 105 2571 2383 2579 105 83 -367 N ATOM 1727 CA PHE A 105 6.442 -1.904 23.958 1.00 20.18 C ANISOU 1727 CA PHE B 105 2523 2563 2579 86 76 -235 C ATOM 1728 C PHE A 105 7.795 -2.458 24.381 1.00 19.82 C ANISOU 1728 C PHE B 105 2499 2480 2548 133 -51 -252 C ATOM 1729 O PHE A 105 8.451 -1.910 25.262 1.00 21.09 O ANISOU 1729 O PHE B 105 2538 2574 2899 221 -35 -630 O ATOM 1730 CB PHE A 105 6.640 -0.934 22.822 1.00 20.39 C ANISOU 1730 CB PHE B 105 2641 2415 2690 142 -26 -174 C ATOM 1731 CG PHE A 105 5.377 -0.435 22.202 1.00 21.12 C ANISOU 1731 CG PHE B 105 2589 2628 2805 -8 41 -4 C ATOM 1732 CD1 PHE A 105 4.835 0.775 22.614 1.00 25.42 C ANISOU 1732 CD1 PHE B 105 3281 2935 3441 119 -174 -211 C ATOM 1733 CD2 PHE A 105 4.800 -1.081 21.136 1.00 21.55 C ANISOU 1733 CD2 PHE B 105 2928 2265 2995 -66 -84 83 C ATOM 1734 CE1 PHE A 105 3.677 1.259 22.040 1.00 23.92 C ANISOU 1734 CE1 PHE B 105 3239 2447 3401 139 -86 -71 C ATOM 1735 CE2 PHE A 105 3.631 -0.596 20.555 1.00 23.64 C ANISOU 1735 CE2 PHE B 105 2945 2910 3124 99 -25 -48 C ATOM 1736 CZ PHE A 105 3.107 0.621 20.980 1.00 24.72 C ANISOU 1736 CZ PHE B 105 3104 2967 3321 57 -71 -21 C ATOM 1737 N THR A 106 8.210 -3.561 23.744 1.00 18.41 N ANISOU 1737 N THR B 106 2417 2281 2297 110 -49 -236 N ATOM 1738 CA THR A 106 9.530 -4.152 23.945 1.00 17.86 C ANISOU 1738 CA THR B 106 2331 2193 2259 39 33 -81 C ATOM 1739 C THR A 106 10.131 -4.333 22.583 1.00 15.49 C ANISOU 1739 C THR B 106 2156 1638 2090 152 -51 -9 C ATOM 1740 O THR A 106 9.485 -4.910 21.717 1.00 16.95 O ANISOU 1740 O THR B 106 2268 1727 2442 102 -105 -28 O ATOM 1741 CB THR A 106 9.403 -5.542 24.606 1.00 18.75 C ANISOU 1741 CB THR B 106 2499 2387 2238 162 102 15 C ATOM 1742 OG1 THR A 106 8.807 -5.392 25.901 1.00 23.22 O ANISOU 1742 OG1 THR B 106 2996 3323 2503 -49 69 59 O ATOM 1743 CG2 THR A 106 10.780 -6.151 24.891 1.00 21.42 C ANISOU 1743 CG2 THR B 106 2672 2848 2616 34 -35 143 C ATOM 1744 N ARG A 107 11.348 -3.874 22.387 1.00 14.89 N ANISOU 1744 N ARG B 107 2048 1604 2005 216 23 -105 N ATOM 1745 CA ARG A 107 12.064 -4.097 21.116 1.00 15.59 C ANISOU 1745 CA ARG B 107 2144 1828 1951 96 -11 77 C ATOM 1746 C ARG A 107 12.515 -5.527 21.034 1.00 15.32 C ANISOU 1746 C ARG B 107 2134 1842 1844 138 -45 3 C ATOM 1747 O ARG A 107 13.075 -6.036 22.011 1.00 14.98 O ANISOU 1747 O ARG B 107 2371 1588 1731 159 -13 221 O ATOM 1748 CB ARG A 107 13.274 -3.166 20.981 1.00 15.88 C ANISOU 1748 CB ARG B 107 2182 1628 2221 112 -93 32 C ATOM 1749 CG ARG A 107 13.958 -3.311 19.704 1.00 17.87 C ANISOU 1749 CG ARG B 107 2193 2092 2504 -56 -81 165 C ATOM 1750 CD ARG A 107 14.921 -2.191 19.343 1.00 19.09 C ANISOU 1750 CD ARG B 107 2437 1960 2856 18 -93 302 C ATOM 1751 NE ARG A 107 15.645 -2.584 18.151 1.00 19.96 N ANISOU 1751 NE ARG B 107 2615 2109 2860 86 -13 354 N ATOM 1752 CZ ARG A 107 16.853 -2.100 17.773 1.00 21.71 C ANISOU 1752 CZ ARG B 107 2719 2672 2856 72 -117 247 C ATOM 1753 NH1 ARG A 107 17.459 -1.167 18.461 1.00 23.23 N ANISOU 1753 NH1 ARG B 107 3105 2537 3183 -105 -116 323 N ATOM 1754 NH2 ARG A 107 17.447 -2.568 16.694 1.00 23.07 N ANISOU 1754 NH2 ARG B 107 2862 2928 2972 15 81 282 N ATOM 1755 N ILE A 108 12.254 -6.179 19.885 1.00 13.98 N ANISOU 1755 N ILE B 108 2071 1553 1688 72 -43 38 N ATOM 1756 CA ILE A 108 12.672 -7.571 19.654 1.00 14.21 C ANISOU 1756 CA ILE B 108 1940 1673 1784 159 7 54 C ATOM 1757 C ILE A 108 13.588 -7.754 18.459 1.00 14.49 C ANISOU 1757 C ILE B 108 1946 1685 1874 188 24 37 C ATOM 1758 O ILE A 108 14.241 -8.784 18.389 1.00 14.90 O ANISOU 1758 O ILE B 108 2195 1456 2011 215 53 -102 O ATOM 1759 CB ILE A 108 11.516 -8.538 19.629 1.00 14.49 C ANISOU 1759 CB ILE B 108 1855 1746 1902 189 76 41 C ATOM 1760 CG1 ILE A 108 10.489 -8.249 18.535 1.00 15.99 C ANISOU 1760 CG1 ILE B 108 2157 1979 1940 95 25 41 C ATOM 1761 CG2 ILE A 108 10.845 -8.577 21.013 1.00 16.42 C ANISOU 1761 CG2 ILE B 108 2374 1931 1934 -62 87 66 C ATOM 1762 CD1 ILE A 108 9.590 -9.424 18.245 1.00 18.58 C ANISOU 1762 CD1 ILE B 108 2521 2306 2232 31 0 -102 C ATOM 1763 N ARG A 109 13.723 -6.760 17.550 1.00 16.21 N ANISOU 1763 N ARG B 109 2091 1920 2145 203 129 160 N ATOM 1764 CA ARG A 109 14.756 -6.796 16.490 1.00 16.91 C ANISOU 1764 CA ARG B 109 2070 2129 2225 141 53 77 C ATOM 1765 C ARG A 109 15.228 -5.412 16.212 1.00 18.21 C ANISOU 1765 C ARG B 109 2185 2253 2482 101 199 168 C ATOM 1766 O ARG A 109 16.396 -5.245 15.788 1.00 20.45 O ANISOU 1766 O ARG B 109 2295 2407 3067 32 197 289 O ATOM 1767 CB ARG A 109 14.278 -7.415 15.194 1.00 17.90 C ANISOU 1767 CB ARG B 109 2133 2365 2303 52 167 -8 C ATOM 1768 CG ARG A 109 13.735 -8.798 15.248 1.00 17.18 C ANISOU 1768 CG ARG B 109 2314 2049 2162 208 -37 113 C ATOM 1769 CD ARG A 109 14.755 -9.919 15.414 1.00 17.07 C ANISOU 1769 CD ARG B 109 2223 2210 2052 289 89 102 C ATOM 1770 NE ARG A 109 14.090 -11.218 15.387 1.00 18.40 N ANISOU 1770 NE ARG B 109 2454 2396 2140 73 23 -42 N ATOM 1771 CZ ARG A 109 13.396 -11.813 16.384 1.00 15.73 C ANISOU 1771 CZ ARG B 109 2368 1804 1804 159 -117 83 C ATOM 1772 NH1 ARG A 109 12.811 -12.980 16.139 1.00 19.41 N ANISOU 1772 NH1 ARG B 109 2786 2333 2253 71 -43 -192 N ATOM 1773 NH2 ARG A 109 13.238 -11.265 17.599 1.00 16.44 N ANISOU 1773 NH2 ARG B 109 2524 1855 1866 141 142 -55 N ATOM 1774 OXT ARG A 109 14.398 -4.494 16.409 1.00 18.11 O ANISOU 1774 OXT ARG B 109 2288 2260 2333 133 126 295 O TER 1775 ARG B 109 HETATM 1776 O HOH A2001 -9.867 20.301 38.408 1.00 59.81 O ANISOU 1776 O HOH A2001 7619 7525 7580 39 -6 -38 O HETATM 1777 O HOH A2002 2.876 17.453 39.570 1.00 42.65 O ANISOU 1777 O HOH A2002 5846 4798 5560 -232 -120 254 O HETATM 1778 O AHOH A2003 -1.455 17.845 37.921 0.50 20.56 O ANISOU 1778 O AHOH A2003 3010 1421 3378 -297 -114 260 O HETATM 1779 O HOH A2004 4.796 11.308 44.553 1.00 20.55 O ANISOU 1779 O HOH A2004 2890 2165 2751 -266 -249 228 O HETATM 1780 O HOH A2005 5.285 17.092 41.478 1.00 53.72 O ANISOU 1780 O HOH A2005 6880 6810 6722 -37 2 133 O HETATM 1781 O HOH A2006 6.801 14.646 44.527 1.00 26.98 O ANISOU 1781 O HOH A2006 3362 3293 3593 280 -325 -643 O HETATM 1782 O HOH A2007 3.843 14.189 39.805 1.00 27.56 O ANISOU 1782 O HOH A2007 3113 3640 3715 -584 13 -119 O HETATM 1783 O HOH A2008 -3.643 18.665 43.647 1.00 30.74 O ANISOU 1783 O HOH A2008 4239 2898 4542 48 -154 -267 O HETATM 1784 O HOH A2009 -3.576 17.263 49.814 1.00 35.59 O ANISOU 1784 O HOH A2009 4769 4447 4303 97 -11 -406 O HETATM 1785 O HOH A2010 -1.396 15.747 50.465 1.00 52.25 O ANISOU 1785 O HOH A2010 6495 6841 6515 1 -20 17 O HETATM 1786 O HOH A2011 2.584 16.948 47.991 1.00 30.73 O ANISOU 1786 O HOH A2011 3501 3645 4528 -304 -99 -440 O HETATM 1787 O HOH A2012 -17.418 -0.917 33.364 1.00 37.67 O ANISOU 1787 O HOH A2012 4901 4072 5339 -37 -150 96 O HETATM 1788 O HOH A2013 -19.565 4.017 20.058 1.00 51.13 O ANISOU 1788 O HOH A2013 6375 6414 6637 -99 15 -16 O HETATM 1789 O HOH A2014 -19.098 8.784 18.741 1.00 60.15 O ANISOU 1789 O HOH A2014 7585 7671 7597 42 -3 -3 O HETATM 1790 O HOH A2015 -3.725 19.864 48.180 1.00 47.53 O ANISOU 1790 O HOH A2015 5945 5705 6407 69 45 -27 O HETATM 1791 O HOH A2016 -17.158 15.417 41.849 1.00 58.39 O ANISOU 1791 O HOH A2016 7432 7150 7602 -28 -20 -34 O HETATM 1792 O HOH A2017 -13.973 10.030 42.397 1.00 24.85 O ANISOU 1792 O HOH A2017 3225 2871 3344 330 20 57 O HETATM 1793 O AHOH A2018 -17.959 -1.298 38.655 0.50 37.98 O ANISOU 1793 O AHOH A2018 4848 4752 4829 -110 0 124 O HETATM 1794 O HOH A2019 -13.514 -4.316 45.444 1.00 40.37 O ANISOU 1794 O HOH A2019 5149 4907 5282 -346 -24 201 O HETATM 1795 O HOH A2020 -15.926 13.969 34.958 1.00 37.03 O ANISOU 1795 O HOH A2020 4745 4284 5037 128 -63 -193 O HETATM 1796 O HOH A2021 -13.750 16.692 41.784 1.00 33.63 O ANISOU 1796 O HOH A2021 4307 3794 4674 -9 265 -81 O HETATM 1797 O HOH A2022 -11.804 19.156 39.691 1.00 28.10 O ANISOU 1797 O HOH A2022 4931 1525 4219 -25 -90 -15 O HETATM 1798 O HOH A2023 -8.607 18.835 36.472 1.00 40.96 O ANISOU 1798 O HOH A2023 5707 4895 4960 -150 74 199 O HETATM 1799 O HOH A2024 -14.349 12.730 38.360 1.00 30.43 O ANISOU 1799 O HOH A2024 3891 3293 4378 -252 -23 -110 O HETATM 1800 O HOH A2025 -15.617 -2.277 45.363 1.00 58.07 O ANISOU 1800 O HOH A2025 7442 7351 7270 -53 9 14 O HETATM 1801 O HOH A2026 -14.334 -1.554 35.141 1.00 41.15 O ANISOU 1801 O HOH A2026 5476 4997 5161 -97 -54 116 O HETATM 1802 O HOH A2027 -4.791 17.200 28.478 1.00 53.51 O ANISOU 1802 O HOH A2027 6773 6723 6833 23 61 108 O HETATM 1803 O HOH A2028 -19.003 12.986 31.611 1.00 36.29 O ANISOU 1803 O HOH A2028 4852 3945 4992 92 -110 34 O HETATM 1804 O HOH A2029 -23.474 10.451 28.900 1.00 26.85 O ANISOU 1804 O HOH A2029 3465 2703 4032 142 5 -32 O HETATM 1805 O HOH A2030 -16.443 0.352 28.694 1.00 39.34 O ANISOU 1805 O HOH A2030 5480 4311 5156 52 -187 -107 O HETATM 1806 O HOH A2031 -21.668 5.740 22.705 1.00 43.14 O ANISOU 1806 O HOH A2031 5503 5213 5672 -25 -197 64 O HETATM 1807 O HOH A2032 -18.649 3.892 22.582 1.00 28.36 O ANISOU 1807 O HOH A2032 3954 3178 3641 120 -11 -454 O HETATM 1808 O AHOH A2033 -19.266 0.051 28.097 0.50 30.14 O ANISOU 1808 O AHOH A2033 4038 3317 4096 -26 -23 10 O HETATM 1809 O HOH A2034 -21.988 8.909 22.385 1.00 53.74 O ANISOU 1809 O HOH A2034 6677 6986 6754 115 -178 -48 O HETATM 1810 O HOH A2035 -18.890 12.830 22.746 1.00 38.38 O ANISOU 1810 O HOH A2035 5290 4181 5112 138 -229 15 O HETATM 1811 O HOH A2036 -17.344 6.748 18.645 1.00 39.79 O ANISOU 1811 O HOH A2036 5239 5556 4323 39 -170 -108 O HETATM 1812 O HOH A2037 -13.926 0.205 24.236 1.00 37.46 O ANISOU 1812 O HOH A2037 4653 4408 5172 9 175 159 O HETATM 1813 O HOH A2038 -7.681 3.390 23.935 1.00 24.90 O ANISOU 1813 O HOH A2038 3872 2233 3356 -204 466 -421 O HETATM 1814 O HOH A2039 -6.297 -0.617 16.788 1.00 47.18 O ANISOU 1814 O HOH A2039 6118 6020 5786 -66 -49 -7 O HETATM 1815 O HOH A2040 -12.637 -1.554 21.360 1.00 40.23 O ANISOU 1815 O HOH A2040 5190 4723 5371 -39 56 3 O HETATM 1816 O HOH A2041 -7.391 10.234 21.535 1.00 20.27 O ANISOU 1816 O HOH A2041 2705 2462 2533 282 53 188 O HETATM 1817 O HOH A2042 -14.010 8.773 17.197 1.00 39.63 O ANISOU 1817 O HOH A2042 4828 5278 4950 121 -109 317 O HETATM 1818 O HOH A2043 -8.897 16.735 22.098 1.00 38.50 O ANISOU 1818 O HOH A2043 5441 4226 4958 -194 311 220 O HETATM 1819 O HOH A2044 -7.257 15.508 19.995 1.00 28.46 O ANISOU 1819 O HOH A2044 4162 3374 3275 -179 133 -20 O HETATM 1820 O HOH A2045 -15.849 15.978 21.123 1.00 49.80 O ANISOU 1820 O HOH A2045 6457 6192 6271 59 -70 74 O HETATM 1821 O HOH A2046 -15.829 13.395 18.078 1.00 50.84 O ANISOU 1821 O HOH A2046 6565 6341 6411 -57 -21 44 O HETATM 1822 O HOH A2047 -9.507 9.780 16.834 1.00 36.61 O ANISOU 1822 O HOH A2047 4750 4511 4646 -171 18 36 O HETATM 1823 O HOH A2048 -14.843 17.093 27.635 1.00 41.89 O ANISOU 1823 O HOH A2048 5115 5352 5448 232 -24 21 O HETATM 1824 O HOH A2049 -8.163 16.797 24.715 1.00 42.74 O ANISOU 1824 O HOH A2049 5546 5132 5559 89 275 41 O HETATM 1825 O HOH A2050 -7.438 14.618 31.789 1.00 19.71 O ANISOU 1825 O HOH A2050 3092 1262 3132 -87 -126 -23 O HETATM 1826 O HOH A2051 -10.842 18.604 31.508 1.00 44.03 O ANISOU 1826 O HOH A2051 5991 5393 5345 242 -79 -183 O HETATM 1827 O HOH A2052 -16.805 15.259 27.988 1.00 46.84 O ANISOU 1827 O HOH A2052 6064 5692 6040 -34 -21 -43 O HETATM 1828 O HOH A2053 -12.798 18.384 29.863 1.00 48.20 O ANISOU 1828 O HOH A2053 6104 6034 6173 24 32 -66 O HETATM 1829 O HOH A2054 -9.355 13.009 26.661 1.00 29.69 O ANISOU 1829 O HOH A2054 3887 3616 3777 224 23 -19 O HETATM 1830 O HOH A2055 -4.319 11.194 32.931 1.00 14.81 O ANISOU 1830 O HOH A2055 2316 1025 2285 -128 183 124 O HETATM 1831 O HOH A2056 -14.489 8.890 37.719 1.00 19.52 O ANISOU 1831 O HOH A2056 2603 1956 2854 -452 -185 341 O HETATM 1832 O HOH A2057 -16.838 1.568 34.153 1.00 14.93 O ANISOU 1832 O HOH A2057 2427 1176 2066 428 81 230 O HETATM 1833 O HOH A2058 -10.733 3.717 35.882 1.00 20.97 O ANISOU 1833 O HOH A2058 3228 2021 2719 -358 -54 -41 O HETATM 1834 O HOH A2059 -15.791 0.299 38.203 1.00 21.83 O ANISOU 1834 O HOH A2059 3053 1878 3362 -276 -679 371 O HETATM 1835 O HOH A2060 -13.615 -2.565 37.573 1.00 39.83 O ANISOU 1835 O HOH A2060 5127 5162 4844 -160 -227 22 O HETATM 1836 O HOH A2061 -10.064 -1.759 37.077 1.00 36.82 O ANISOU 1836 O HOH A2061 4873 4246 4869 -380 48 -340 O HETATM 1837 O HOH A2062 -10.954 -3.415 45.509 1.00 25.65 O ANISOU 1837 O HOH A2062 4180 1591 3974 -647 -26 503 O HETATM 1838 O HOH A2063 -9.207 -4.554 38.330 1.00 39.47 O ANISOU 1838 O HOH A2063 5534 4325 5137 172 -117 -234 O HETATM 1839 O HOH A2064 -7.634 -5.699 48.647 1.00 43.29 O ANISOU 1839 O HOH A2064 5524 5268 5653 107 -41 290 O HETATM 1840 O HOH A2065 -3.550 -7.427 42.934 1.00 41.62 O ANISOU 1840 O HOH A2065 5175 5296 5340 89 77 -47 O HETATM 1841 O HOH A2066 -5.127 -13.810 45.769 1.00 43.81 O ANISOU 1841 O HOH A2066 5637 5107 5901 68 -108 87 O HETATM 1842 O HOH A2067 2.352 -3.738 47.511 1.00 58.28 O ANISOU 1842 O HOH A2067 7381 7362 7399 19 -39 -47 O HETATM 1843 O HOH A2068 3.187 -4.368 45.078 1.00 62.96 O ANISOU 1843 O HOH A2068 7963 8063 7894 17 -41 68 O HETATM 1844 O HOH A2069 -2.976 -8.375 49.659 1.00 45.63 O ANISOU 1844 O HOH A2069 6018 5477 5840 -96 -45 56 O HETATM 1845 O HOH A2070 -2.798 -3.644 55.116 1.00 60.74 O ANISOU 1845 O HOH A2070 7798 7672 7608 26 -87 34 O HETATM 1846 O HOH A2071 -8.288 -5.071 50.968 1.00 49.66 O ANISOU 1846 O HOH A2071 6148 6239 6481 -79 -31 -40 O HETATM 1847 O HOH A2072 -14.606 0.319 50.998 1.00 43.57 O ANISOU 1847 O HOH A2072 5442 5585 5527 -187 259 0 O HETATM 1848 O HOH A2073 -12.759 2.156 46.993 1.00 30.09 O ANISOU 1848 O HOH A2073 3993 3311 4127 -401 149 249 O HETATM 1849 O HOH A2074 -13.425 0.007 45.104 1.00 38.95 O ANISOU 1849 O HOH A2074 4635 5158 5006 -126 112 31 O HETATM 1850 O HOH A2075 -16.977 2.393 40.088 1.00 25.16 O ANISOU 1850 O HOH A2075 3386 3245 2926 -735 -517 -64 O HETATM 1851 O HOH A2076 -6.966 -2.761 35.931 1.00 38.75 O ANISOU 1851 O HOH A2076 5204 4171 5347 35 -58 2 O HETATM 1852 O HOH A2077 -3.677 6.364 29.925 1.00 16.11 O ANISOU 1852 O HOH A2077 2679 1537 1905 332 153 -285 O HETATM 1853 O HOH A2078 -7.131 7.952 30.093 1.00 16.87 O ANISOU 1853 O HOH A2078 2243 1741 2423 -76 192 265 O HETATM 1854 O HOH A2079 -7.924 3.853 35.246 1.00 17.72 O ANISOU 1854 O HOH A2079 2887 1552 2294 -362 233 71 O HETATM 1855 O HOH A2080 1.024 14.998 33.119 1.00 32.27 O ANISOU 1855 O HOH A2080 4646 3500 4112 -193 -155 279 O HETATM 1856 O HOH A2081 5.514 10.962 35.552 1.00 39.62 O ANISOU 1856 O HOH A2081 4963 5133 4958 -161 15 85 O HETATM 1857 O HOH A2082 2.986 12.655 36.635 1.00 22.53 O ANISOU 1857 O HOH A2082 2541 3089 2929 -65 195 -31 O HETATM 1858 O HOH A2083 -5.537 14.874 29.529 1.00 26.69 O ANISOU 1858 O HOH A2083 3766 2715 3658 -251 306 511 O HETATM 1859 O HOH A2084 -5.245 16.351 24.640 1.00 42.75 O ANISOU 1859 O HOH A2084 5471 5088 5683 246 72 76 O HETATM 1860 O HOH A2085 -7.166 14.213 27.210 1.00 30.70 O ANISOU 1860 O HOH A2085 4123 3659 3882 295 -152 66 O HETATM 1861 O HOH A2086 -1.200 10.277 26.223 1.00 29.63 O ANISOU 1861 O HOH A2086 4046 3384 3828 286 256 82 O HETATM 1862 O HOH A2087 -2.129 15.610 21.713 1.00 46.77 O ANISOU 1862 O HOH A2087 6104 5833 5833 -136 54 231 O HETATM 1863 O HOH A2088 -0.395 11.838 22.693 1.00 46.27 O ANISOU 1863 O HOH A2088 5800 5711 6067 -170 104 -17 O HETATM 1864 O HOH A2089 -8.155 6.263 23.850 1.00 25.20 O ANISOU 1864 O HOH A2089 2751 3406 3417 -116 59 -443 O HETATM 1865 O HOH A2090 -1.250 7.753 25.618 1.00 44.71 O ANISOU 1865 O HOH A2090 5582 5732 5673 -112 -8 -79 O HETATM 1866 O HOH A2091 -6.264 1.844 25.015 1.00 40.02 O ANISOU 1866 O HOH A2091 4946 5519 4739 -160 -37 -128 O HETATM 1867 O HOH A2092 -8.585 0.248 33.557 1.00 32.52 O ANISOU 1867 O HOH A2092 4638 3668 4046 -302 -83 397 O HETATM 1868 O HOH A2093 -8.266 0.301 27.287 1.00 33.07 O ANISOU 1868 O HOH A2093 4730 3628 4204 -6 -205 -281 O HETATM 1869 O HOH A2094 1.604 9.417 28.236 1.00 34.03 O ANISOU 1869 O HOH A2094 4490 4292 4146 -195 414 -51 O HETATM 1870 O HOH A2095 3.264 5.197 29.807 1.00 34.00 O ANISOU 1870 O HOH A2095 3742 4607 4568 60 -39 190 O HETATM 1871 O HOH A2096 3.779 8.585 30.678 1.00 45.83 O ANISOU 1871 O HOH A2096 5838 6015 5557 106 242 11 O HETATM 1872 O HOH A2097 5.671 8.108 33.868 1.00 33.41 O ANISOU 1872 O HOH A2097 3641 4299 4754 -120 -9 -13 O HETATM 1873 O HOH A2098 5.363 4.993 31.894 1.00 32.10 O ANISOU 1873 O HOH A2098 3961 3686 4547 255 286 -181 O HETATM 1874 O HOH A2099 -13.077 7.751 43.697 1.00 34.69 O ANISOU 1874 O HOH A2099 4648 3753 4778 -50 -315 172 O HETATM 1875 O HOH A2100 -10.725 3.632 46.715 1.00 23.06 O ANISOU 1875 O HOH A2100 3188 2802 2769 -211 54 221 O HETATM 1876 O HOH A2101 -11.472 1.565 54.237 1.00 47.26 O ANISOU 1876 O HOH A2101 6120 6113 5721 -140 16 50 O HETATM 1877 O HOH A2102 -6.498 6.280 56.835 1.00 56.39 O ANISOU 1877 O HOH A2102 7198 7196 7029 -74 38 -90 O HETATM 1878 O HOH A2103 -2.156 7.818 53.264 1.00 34.32 O ANISOU 1878 O HOH A2103 4172 4653 4213 -516 193 -85 O HETATM 1879 O HOH A2104 3.381 -2.088 50.087 1.00 46.82 O ANISOU 1879 O HOH A2104 5943 5990 5856 88 -135 185 O HETATM 1880 O HOH A2105 5.335 10.223 42.021 1.00 21.24 O ANISOU 1880 O HOH A2105 3122 1945 3002 -147 -91 -213 O HETATM 1881 O HOH A2106 6.969 8.959 38.136 1.00 53.77 O ANISOU 1881 O HOH A2106 6583 6912 6934 -64 -40 -110 O HETATM 1882 O HOH A2107 9.507 8.525 41.068 1.00 58.61 O ANISOU 1882 O HOH A2107 7486 7479 7302 40 -2 -69 O HETATM 1883 O HOH A2108 6.416 1.477 30.865 1.00 44.98 O ANISOU 1883 O HOH A2108 5612 5806 5671 31 135 -216 O HETATM 1884 O HOH A2109 6.054 1.066 38.297 1.00 22.26 O ANISOU 1884 O HOH A2109 2995 2327 3134 515 -230 -68 O HETATM 1885 O HOH A2110 9.082 -2.871 35.104 1.00 44.38 O ANISOU 1885 O HOH A2110 5530 5775 5555 313 73 -72 O HETATM 1886 O HOH A2111 3.443 -4.508 32.293 1.00 32.38 O ANISOU 1886 O HOH A2111 4910 3203 4190 460 -129 -440 O HETATM 1887 O HOH A2112 8.605 0.384 36.931 1.00 56.66 O ANISOU 1887 O HOH A2112 7003 7185 7340 85 -4 -44 O HETATM 1888 O HOH A2113 0.815 -5.987 34.201 1.00 42.52 O ANISOU 1888 O HOH A2113 5706 4950 5497 35 86 -199 O HETATM 1889 O HOH A2114 -5.104 -0.420 30.993 1.00 31.36 O ANISOU 1889 O HOH A2114 3869 3216 4828 92 -264 -309 O HETATM 1890 O HOH A2115 -6.489 -1.273 32.696 1.00 55.25 O ANISOU 1890 O HOH A2115 6941 7049 7001 4 -63 -3 O HETATM 1891 O HOH A2116 5.497 -1.301 46.674 1.00 49.61 O ANISOU 1891 O HOH A2116 6450 6191 6208 -44 -34 -11 O HETATM 1892 O HOH A2117 5.354 -3.981 43.349 1.00 31.71 O ANISOU 1892 O HOH A2117 4723 3127 4197 489 -409 153 O HETATM 1893 O HOH A2118 6.275 2.846 40.565 1.00 42.25 O ANISOU 1893 O HOH A2118 5457 5806 4787 39 -54 -122 O HETATM 1894 O HOH A2119 3.013 3.944 57.045 1.00 47.29 O ANISOU 1894 O HOH A2119 6085 6190 5693 -65 -53 132 O HETATM 1895 O HOH A2120 1.132 5.836 56.680 1.00 42.95 O ANISOU 1895 O HOH A2120 5590 5723 5002 -9 -40 88 O HETATM 1896 O HOH B2001 2.644 -21.564 15.300 1.00 47.42 O ANISOU 1896 O HOH B2001 6114 5946 5955 15 -7 78 O HETATM 1897 O HOH B2002 2.951 -19.245 13.312 1.00 41.42 O ANISOU 1897 O HOH B2002 5617 5378 4740 63 6 -41 O HETATM 1898 O HOH B2003 9.936 -18.895 15.012 1.00 57.13 O ANISOU 1898 O HOH B2003 7268 7159 7280 105 51 -49 O HETATM 1899 O HOH B2004 -2.221 -19.453 16.277 1.00 35.44 O ANISOU 1899 O HOH B2004 4179 4314 4971 -18 -8 342 O HETATM 1900 O HOH B2005 0.580 -19.864 15.971 1.00 49.59 O ANISOU 1900 O HOH B2005 6326 6127 6389 -27 36 185 O HETATM 1901 O HOH B2006 7.615 -18.719 16.539 1.00 44.27 O ANISOU 1901 O HOH B2006 5513 5331 5973 174 -7 165 O HETATM 1902 O HOH B2007 5.119 -18.549 13.420 1.00 39.74 O ANISOU 1902 O HOH B2007 5362 4828 4909 -46 -72 -126 O HETATM 1903 O HOH B2008 17.087 -13.340 7.753 1.00 46.88 O ANISOU 1903 O HOH B2008 5841 6169 5799 -44 130 -80 O HETATM 1904 O HOH B2009 10.583 -18.615 19.350 1.00 50.64 O ANISOU 1904 O HOH B2009 6551 6272 6417 108 -109 -25 O HETATM 1905 O HOH B2010 13.845 -16.420 17.849 1.00 35.18 O ANISOU 1905 O HOH B2010 4972 4103 4289 134 -2 -426 O HETATM 1906 O HOH B2011 7.257 -15.957 19.223 1.00 26.60 O ANISOU 1906 O HOH B2011 3607 3517 2981 -43 -128 525 O HETATM 1907 O HOH B2012 12.904 -15.657 20.774 1.00 25.05 O ANISOU 1907 O HOH B2012 3790 2383 3342 135 -699 143 O HETATM 1908 O HOH B2013 11.578 -12.115 20.088 1.00 22.21 O ANISOU 1908 O HOH B2013 2593 2539 3307 -123 -243 98 O HETATM 1909 O HOH B2014 6.594 -2.813 4.443 1.00 57.77 O ANISOU 1909 O HOH B2014 7450 7297 7200 -89 -17 17 O HETATM 1910 O HOH B2015 9.496 -16.922 10.101 1.00 29.21 O ANISOU 1910 O HOH B2015 4102 3521 3474 327 140 -335 O HETATM 1911 O HOH B2016 15.129 -13.522 9.379 1.00 34.87 O ANISOU 1911 O HOH B2016 4125 4980 4144 20 -150 25 O HETATM 1912 O HOH B2017 15.260 -15.631 15.395 1.00 28.67 O ANISOU 1912 O HOH B2017 3962 3729 3201 -329 -121 83 O HETATM 1913 O AHOH B2018 -0.604 -5.253 0.158 0.50 56.69 O ANISOU 1913 O AHOH B2018 7192 7160 7185 13 -11 20 O HETATM 1914 O HOH B2019 -22.685 -4.341 8.878 1.00 64.11 O ANISOU 1914 O HOH B2019 8059 8124 8174 -55 14 20 O HETATM 1915 O HOH B2020 9.372 -8.638 -0.623 1.00 27.72 O ANISOU 1915 O HOH B2020 3566 3941 3025 170 -101 0 O HETATM 1916 O HOH B2021 9.778 -4.050 1.057 1.00 40.76 O ANISOU 1916 O HOH B2021 5242 5204 5041 -131 83 89 O HETATM 1917 O HOH B2022 6.455 -4.722 2.413 1.00 34.75 O ANISOU 1917 O HOH B2022 4671 4566 3965 -119 -38 15 O HETATM 1918 O HOH B2023 9.692 -13.847 -1.964 1.00 30.86 O ANISOU 1918 O HOH B2023 4140 3850 3733 137 237 9 O HETATM 1919 O HOH B2024 -0.716 -1.301 2.413 1.00 56.42 O ANISOU 1919 O HOH B2024 7136 7126 7172 -9 9 21 O HETATM 1920 O HOH B2025 2.799 -9.240 2.076 1.00 35.12 O ANISOU 1920 O HOH B2025 4477 4541 4327 324 -301 197 O HETATM 1921 O HOH B2026 3.928 -6.241 3.791 1.00 29.57 O ANISOU 1921 O HOH B2026 3837 3830 3565 183 179 360 O HETATM 1922 O HOH B2027 4.532 -12.778 1.981 1.00 24.70 O ANISOU 1922 O HOH B2027 3117 3820 2447 -56 143 -67 O HETATM 1923 O HOH B2028 3.198 7.517 8.906 1.00 45.83 O ANISOU 1923 O HOH B2028 5831 5729 5851 -66 -37 185 O HETATM 1924 O HOH B2029 -3.488 -12.598 1.555 1.00 40.36 O ANISOU 1924 O HOH B2029 5203 5305 4826 -187 -73 -164 O HETATM 1925 O HOH B2030 4.913 -15.419 -0.083 1.00 30.16 O ANISOU 1925 O HOH B2030 4032 3969 3457 -110 -9 246 O HETATM 1926 O HOH B2031 3.711 -16.306 3.665 1.00 30.54 O ANISOU 1926 O HOH B2031 3744 4158 3699 248 -19 -302 O HETATM 1927 O HOH B2032 0.335 -9.867 3.405 1.00 36.80 O ANISOU 1927 O HOH B2032 4610 4933 4436 54 65 300 O HETATM 1928 O HOH B2033 -4.954 -2.094 1.591 1.00 38.96 O ANISOU 1928 O HOH B2033 4888 5221 4692 26 83 288 O HETATM 1929 O HOH B2034 -11.144 0.290 10.247 1.00 65.32 O ANISOU 1929 O HOH B2034 8298 8236 8284 17 -18 -57 O HETATM 1930 O HOH B2035 -8.000 -1.983 -0.094 1.00 48.24 O ANISOU 1930 O HOH B2035 6282 6247 5800 -85 -78 234 O HETATM 1931 O HOH B2036 -12.367 -1.189 2.021 1.00 38.85 O ANISOU 1931 O HOH B2036 5012 4814 4932 228 -142 357 O HETATM 1932 O HOH B2037 -5.262 0.133 2.810 1.00 45.40 O ANISOU 1932 O HOH B2037 5844 5865 5541 -58 -24 -24 O HETATM 1933 O HOH B2038 -4.885 -19.873 12.085 1.00 46.51 O ANISOU 1933 O HOH B2038 5818 5910 5941 -19 216 15 O HETATM 1934 O AHOH B2039 -2.081 -5.802 -1.031 0.50 34.88 O ANISOU 1934 O AHOH B2039 4378 4500 4375 -71 121 11 O HETATM 1935 O HOH B2040 -1.900 -4.398 0.496 0.50 54.55 O ANISOU 1935 O HOH B2040 6809 6957 6958 -10 11 30 O HETATM 1936 O HOH B2041 -2.321 -7.046 2.188 1.00 35.37 O ANISOU 1936 O HOH B2041 4124 5262 4053 199 154 90 O HETATM 1937 O HOH B2042 -12.687 -12.002 22.902 1.00 54.35 O ANISOU 1937 O HOH B2042 7132 6729 6790 -11 -33 60 O HETATM 1938 O HOH B2043 -9.115 -4.163 18.267 1.00 42.10 O ANISOU 1938 O HOH B2043 5493 4997 5505 13 28 -288 O HETATM 1939 O HOH B2044 0.685 -12.179 27.037 1.00 54.65 O ANISOU 1939 O HOH B2044 7096 6733 6935 -36 28 108 O HETATM 1940 O HOH B2045 -15.422 -1.504 2.582 1.00 56.20 O ANISOU 1940 O HOH B2045 7253 7041 7057 4 -52 -6 O HETATM 1941 O HOH B2046 -20.615 -8.141 7.465 1.00 47.52 O ANISOU 1941 O HOH B2046 5720 6217 6119 38 -43 -31 O HETATM 1942 O HOH B2047 -15.113 -2.684 8.776 1.00 41.00 O ANISOU 1942 O HOH B2047 5150 5200 5226 210 126 -18 O HETATM 1943 O HOH B2048 -17.224 -4.134 6.095 1.00 35.66 O ANISOU 1943 O HOH B2048 4594 4360 4595 58 -76 26 O HETATM 1944 O HOH B2049 -14.862 -2.290 11.373 1.00 43.35 O ANISOU 1944 O HOH B2049 5623 5354 5493 -15 1 94 O HETATM 1945 O HOH B2050 -13.088 -7.540 15.403 1.00 35.55 O ANISOU 1945 O HOH B2050 4345 4419 4741 276 237 229 O HETATM 1946 O HOH B2051 -17.245 -1.780 14.182 1.00 43.48 O ANISOU 1946 O HOH B2051 5456 5470 5593 180 68 33 O HETATM 1947 O HOH B2052 7.218 -1.516 30.795 1.00 46.76 O ANISOU 1947 O HOH B2052 5794 6235 5736 101 110 -96 O HETATM 1948 O HOH B2053 -14.081 -14.419 13.625 1.00 24.20 O ANISOU 1948 O HOH B2053 3115 3297 2783 123 35 329 O HETATM 1949 O HOH B2054 -15.558 -16.729 13.571 1.00 48.96 O ANISOU 1949 O HOH B2054 6174 6134 6294 -24 84 10 O HETATM 1950 O HOH B2055 -19.939 -12.725 9.044 1.00 51.17 O ANISOU 1950 O HOH B2055 6289 6673 6479 -68 57 47 O HETATM 1951 O HOH B2056 -15.944 -13.616 2.288 1.00 48.61 O ANISOU 1951 O HOH B2056 5998 6324 6146 28 -105 -18 O HETATM 1952 O HOH B2057 -12.606 -14.491 1.764 1.00 31.37 O ANISOU 1952 O HOH B2057 4306 4097 3516 -317 66 46 O HETATM 1953 O HOH B2058 -9.090 -16.462 3.192 1.00 36.96 O ANISOU 1953 O HOH B2058 4643 5261 4138 -109 -168 49 O HETATM 1954 O HOH B2059 -5.972 -18.060 4.206 1.00 51.85 O ANISOU 1954 O HOH B2059 6617 6592 6491 30 0 -139 O HETATM 1955 O AHOH B2060 -3.887 -18.229 5.771 0.50 31.65 O ANISOU 1955 O AHOH B2060 4051 4017 3957 7 12 -227 O HETATM 1956 O AHOH B2061 -3.381 -17.360 4.322 0.50 42.05 O ANISOU 1956 O AHOH B2061 5433 5122 5420 -6 -30 -110 O HETATM 1957 O HOH B2062 -2.145 -13.047 14.020 1.00 15.80 O ANISOU 1957 O HOH B2062 2147 2028 1826 -44 37 238 O HETATM 1958 O HOH B2063 -3.467 -15.524 10.162 1.00 20.25 O ANISOU 1958 O HOH B2063 2747 2464 2480 343 64 -163 O HETATM 1959 O HOH B2064 -0.983 -6.748 4.547 1.00 28.37 O ANISOU 1959 O HOH B2064 3591 4289 2896 257 101 271 O HETATM 1960 O HOH B2065 1.670 -2.658 4.337 1.00 40.14 O ANISOU 1960 O HOH B2065 5294 5130 4826 7 115 26 O HETATM 1961 O HOH B2066 -2.889 -3.452 10.349 1.00 27.10 O ANISOU 1961 O HOH B2066 3262 3344 3689 31 66 531 O HETATM 1962 O HOH B2067 -6.300 -0.388 5.451 1.00 28.74 O ANISOU 1962 O HOH B2067 3701 3436 3783 126 -477 717 O HETATM 1963 O HOH B2068 -2.732 2.260 6.697 1.00 36.70 O ANISOU 1963 O HOH B2068 4840 4353 4748 214 -357 128 O HETATM 1964 O HOH B2069 -3.238 1.254 12.302 1.00 37.78 O ANISOU 1964 O HOH B2069 4781 4594 4979 65 5 147 O HETATM 1965 O HOH B2070 4.098 5.997 11.173 1.00 34.44 O ANISOU 1965 O HOH B2070 4218 3846 5020 100 113 551 O HETATM 1966 O HOH B2071 -2.267 4.613 15.310 1.00 43.27 O ANISOU 1966 O HOH B2071 5347 5673 5421 -7 -11 81 O HETATM 1967 O HOH B2072 4.922 8.420 12.936 1.00 47.40 O ANISOU 1967 O HOH B2072 6245 5765 5998 -49 19 -23 O HETATM 1968 O HOH B2073 6.842 8.554 14.513 1.00 40.60 O ANISOU 1968 O HOH B2073 5181 4937 5308 -195 169 344 O HETATM 1969 O HOH B2074 3.123 5.449 20.360 1.00 26.74 O ANISOU 1969 O HOH B2074 3327 2694 4137 -112 114 69 O HETATM 1970 O AHOH B2075 -5.996 6.889 17.723 0.50 25.97 O ANISOU 1970 O AHOH B2075 3181 3078 3609 37 105 64 O HETATM 1971 O AHOH B2076 -2.992 13.748 18.989 0.50 27.84 O ANISOU 1971 O AHOH B2076 3481 3501 3594 -21 -36 -73 O HETATM 1972 O HOH B2077 -3.431 6.673 18.244 1.00 28.32 O ANISOU 1972 O HOH B2077 4010 3479 3269 176 -119 99 O HETATM 1973 O HOH B2078 -0.402 5.505 17.400 1.00 25.87 O ANISOU 1973 O HOH B2078 3474 3193 3161 -133 225 -52 O HETATM 1974 O HOH B2079 3.363 7.435 26.883 1.00 48.91 O ANISOU 1974 O HOH B2079 6159 6131 6294 -108 -24 -155 O HETATM 1975 O HOH B2080 13.401 9.800 3.201 1.00 57.31 O ANISOU 1975 O HOH B2080 7290 7197 7287 95 61 1 O HETATM 1976 O HOH B2081 9.100 7.978 12.739 1.00 47.13 O ANISOU 1976 O HOH B2081 5622 5974 6309 -17 0 121 O HETATM 1977 O HOH B2082 15.684 5.434 16.391 1.00 60.36 O ANISOU 1977 O HOH B2082 7554 7775 7601 -10 53 -48 O HETATM 1978 O HOH B2083 -3.469 1.178 15.909 1.00 45.69 O ANISOU 1978 O HOH B2083 5945 5852 5563 119 30 -54 O HETATM 1979 O HOH B2084 -2.553 -4.587 13.137 1.00 20.52 O ANISOU 1979 O HOH B2084 2776 2162 2857 24 526 279 O HETATM 1980 O HOH B2085 -5.745 -9.884 17.009 1.00 17.67 O ANISOU 1980 O HOH B2085 2773 1895 2045 67 247 179 O HETATM 1981 O HOH B2086 -6.400 -10.044 13.268 1.00 18.38 O ANISOU 1981 O HOH B2086 3016 1693 2273 -192 4 220 O HETATM 1982 O HOH B2087 3.580 -15.307 19.528 1.00 22.39 O ANISOU 1982 O HOH B2087 3382 2638 2485 58 68 39 O HETATM 1983 O HOH B2088 0.266 -17.958 17.576 1.00 38.16 O ANISOU 1983 O HOH B2088 4716 4545 5235 72 -43 37 O HETATM 1984 O HOH B2089 2.877 -14.861 22.452 1.00 41.19 O ANISOU 1984 O HOH B2089 5410 5420 4819 -99 -144 7 O HETATM 1985 O HOH B2090 -4.366 -17.469 19.908 1.00 34.86 O ANISOU 1985 O HOH B2090 4642 4054 4546 -411 -46 355 O HETATM 1986 O HOH B2091 -4.697 -17.145 12.007 1.00 23.90 O ANISOU 1986 O HOH B2091 3672 2900 2508 -399 217 -274 O HETATM 1987 O HOH B2092 -7.819 -15.664 18.222 1.00 22.73 O ANISOU 1987 O HOH B2092 3254 2963 2419 14 98 35 O HETATM 1988 O HOH B2093 -7.384 -16.478 11.111 1.00 25.33 O ANISOU 1988 O HOH B2093 3925 3121 2579 86 91 -244 O HETATM 1989 O HOH B2094 -11.288 -15.910 20.041 1.00 42.67 O ANISOU 1989 O HOH B2094 5586 5424 5203 120 115 59 O HETATM 1990 O HOH B2095 -13.510 -17.654 17.901 1.00 42.52 O ANISOU 1990 O HOH B2095 5369 5259 5527 155 270 197 O HETATM 1991 O HOH B2096 -12.789 -10.018 14.061 1.00 25.66 O ANISOU 1991 O HOH B2096 3338 3500 2909 215 165 193 O HETATM 1992 O HOH B2097 -13.295 -13.540 20.563 1.00 31.19 O ANISOU 1992 O HOH B2097 4379 3847 3624 171 300 327 O HETATM 1993 O HOH B2098 -8.532 -13.371 19.341 1.00 36.58 O ANISOU 1993 O HOH B2098 4851 4346 4700 116 -147 306 O HETATM 1994 O HOH B2099 -8.436 -0.961 14.754 1.00 57.62 O ANISOU 1994 O HOH B2099 7483 7238 7171 -36 19 -30 O HETATM 1995 O HOH B2100 -10.710 -3.433 15.730 1.00 39.91 O ANISOU 1995 O HOH B2100 4500 5300 5362 251 95 -285 O HETATM 1996 O HOH B2101 -5.206 -1.645 14.014 1.00 41.13 O ANISOU 1996 O HOH B2101 5107 4996 5523 -84 -154 91 O HETATM 1997 O HOH B2102 -12.052 -6.768 17.143 1.00 34.95 O ANISOU 1997 O HOH B2102 4310 4074 4894 275 305 -22 O HETATM 1998 O HOH B2103 -5.750 -14.415 20.764 1.00 38.72 O ANISOU 1998 O HOH B2103 5158 4215 5337 -156 177 134 O HETATM 1999 O HOH B2104 -4.365 -10.645 23.927 1.00 35.66 O ANISOU 1999 O HOH B2104 4867 4538 4143 -138 -300 211 O HETATM 2000 O HOH B2105 -1.797 -10.192 25.354 1.00 29.60 O ANISOU 2000 O HOH B2105 4398 3721 3126 -238 214 -89 O HETATM 2001 O HOH B2106 0.834 -12.655 24.294 1.00 34.73 O ANISOU 2001 O HOH B2106 4827 4314 4053 99 -143 566 O HETATM 2002 O HOH B2107 -3.121 -13.318 22.845 1.00 43.02 O ANISOU 2002 O HOH B2107 5502 5196 5646 -230 214 162 O HETATM 2003 O HOH B2108 4.307 -3.750 5.354 1.00 39.99 O ANISOU 2003 O HOH B2108 5087 5053 5052 -72 14 -104 O HETATM 2004 O HOH B2109 6.935 0.012 8.328 1.00 32.42 O ANISOU 2004 O HOH B2109 3862 4738 3716 -30 79 468 O HETATM 2005 O HOH B2110 8.685 -1.524 6.934 1.00 47.77 O ANISOU 2005 O HOH B2110 6217 6127 5805 -122 183 110 O HETATM 2006 O HOH B2111 16.486 -4.214 13.231 1.00 37.25 O ANISOU 2006 O HOH B2111 4575 5138 4439 178 174 421 O HETATM 2007 O HOH B2112 15.251 1.864 19.157 1.00 47.23 O ANISOU 2007 O HOH B2112 5949 5994 6003 52 -89 42 O HETATM 2008 O HOH B2113 14.350 0.066 22.706 1.00 33.44 O ANISOU 2008 O HOH B2113 4382 3631 4690 -419 46 130 O HETATM 2009 O HOH B2114 12.754 2.272 22.381 1.00 41.52 O ANISOU 2009 O HOH B2114 5088 5308 5376 128 -203 64 O HETATM 2010 O HOH B2115 9.170 -12.684 25.751 1.00 64.21 O ANISOU 2010 O HOH B2115 7974 8362 8060 -27 -23 -51 O HETATM 2011 O HOH B2116 5.642 -11.560 24.795 1.00 48.81 O ANISOU 2011 O HOH B2116 6018 6134 6392 94 30 27 O HETATM 2012 O HOH B2117 9.768 -10.129 26.076 1.00 53.24 O ANISOU 2012 O HOH B2117 6751 6742 6735 109 5 41 O HETATM 2013 O HOH B2118 9.103 -12.153 21.454 1.00 22.28 O ANISOU 2013 O HOH B2118 3134 2351 2981 292 88 66 O HETATM 2014 O HOH B2119 3.348 -6.209 28.719 1.00 52.98 O ANISOU 2014 O HOH B2119 6871 6849 6407 59 5 -51 O HETATM 2015 O HOH B2120 -2.211 -7.577 28.496 1.00 54.44 O ANISOU 2015 O HOH B2120 7017 6927 6738 -27 168 26 O HETATM 2016 O HOH B2121 3.624 -5.209 26.104 1.00 20.22 O ANISOU 2016 O HOH B2121 3002 2421 2257 224 -77 -601 O HETATM 2017 O HOH B2122 0.750 -8.092 29.064 1.00 50.73 O ANISOU 2017 O HOH B2122 6631 6656 5986 48 127 17 O HETATM 2018 O HOH B2123 -4.042 -2.469 27.876 1.00 42.34 O ANISOU 2018 O HOH B2123 5151 5694 5240 217 179 -146 O HETATM 2019 O HOH B2124 1.398 -5.024 30.396 1.00 37.19 O ANISOU 2019 O HOH B2124 5146 4316 4668 15 -293 127 O HETATM 2020 O HOH B2125 -6.862 -2.631 18.327 1.00 30.83 O ANISOU 2020 O HOH B2125 3947 3943 3823 343 -213 119 O HETATM 2021 O HOH B2126 -3.450 1.119 25.638 1.00 20.81 O ANISOU 2021 O HOH B2126 3048 1660 3195 224 118 -358 O HETATM 2022 O HOH B2127 -7.067 -1.569 26.109 1.00 54.00 O ANISOU 2022 O HOH B2127 6733 6997 6784 -25 15 -39 O HETATM 2023 O HOH B2128 4.873 2.709 28.032 1.00 34.57 O ANISOU 2023 O HOH B2128 4228 3992 4911 73 173 -59 O HETATM 2024 O HOH B2129 5.529 -4.646 29.206 1.00 44.10 O ANISOU 2024 O HOH B2129 5587 5627 5539 119 -32 -32 O HETATM 2025 O HOH B2130 10.510 0.061 24.643 1.00 44.87 O ANISOU 2025 O HOH B2130 5646 5691 5709 -12 -26 -132 O HETATM 2026 O HOH B2131 7.004 1.143 26.465 1.00 29.36 O ANISOU 2026 O HOH B2131 3624 3476 4055 -129 171 -258 O HETATM 2027 O HOH B2132 8.340 -0.723 28.103 1.00 52.25 O ANISOU 2027 O HOH B2132 6663 6583 6605 -34 36 -74 O HETATM 2028 O HOH B2133 6.142 -6.147 25.307 1.00 36.77 O ANISOU 2028 O HOH B2133 4473 5009 4487 150 200 -252 O HETATM 2029 O HOH B2134 20.232 -1.946 15.810 1.00 44.34 O ANISOU 2029 O HOH B2134 5455 5545 5847 -234 38 -115 O HETATM 2030 O HOH B2135 18.378 -6.842 15.187 1.00 24.62 O ANISOU 2030 O HOH B2135 3322 2982 3047 -340 323 -517 O MASTER 391 0 0 8 12 0 0 6 2028 2 0 18 END