HEADER SUGAR BINDING PROTEIN 17-MAY-07 2Z21 TITLE CRYSTAL STRUCTURE OF A FIVE SITE MUTATED CYANOVIRIN-N COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYANOVIRIN-N; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: CV-N; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: NOSTOC ELLIPSOSPORUM; SOURCE 3 ORGANISM_TAXID: 45916; SOURCE 4 GENE: CYANOVIRIN-N; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: M51 KEYWDS CYANOVIRIN-N, SUGAR BINDING PROTEIN, ANTI-HIV, GP120 EXPDTA X-RAY DIFFRACTION AUTHOR R.FROMME,Z.KATILENE,P.FROMME,G.GHIRLANDA REVDAT 3 24-FEB-09 2Z21 1 VERSN REVDAT 2 21-AUG-07 2Z21 1 JRNL REVDAT 1 31-JUL-07 2Z21 0 JRNL AUTH R.FROMME,Z.KATILIENE,B.GIOMARELLI,F.BOGANI, JRNL AUTH 2 J.M.MAHON,T.MORI,P.FROMME,G.GHIRLANDA JRNL TITL A MONOVALENT MUTANT OF CYANOVIRIN-N PROVIDES JRNL TITL 2 INSIGHT INTO THE ROLE OF MULTIPLE INTERACTIONS JRNL TITL 3 WITH GP120 FOR ANTIVIRAL ACTIVITY. JRNL REF BIOCHEMISTRY V. 46 9199 2007 JRNL REFN ISSN 0006-2960 JRNL PMID 17636873 JRNL DOI 10.1021/BI700666M REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0019 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.44 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 87.7 REMARK 3 NUMBER OF REFLECTIONS : 16077 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.167 REMARK 3 R VALUE (WORKING SET) : 0.164 REMARK 3 FREE R VALUE : 0.235 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200 REMARK 3 FREE R VALUE TEST SET COUNT : 881 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85 REMARK 3 REFLECTION IN BIN (WORKING SET) : 566 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 42.34 REMARK 3 BIN R VALUE (WORKING SET) : 0.1750 REMARK 3 BIN FREE R VALUE SET COUNT : 25 REMARK 3 BIN FREE R VALUE : 0.3160 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1537 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 283 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.49 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.07000 REMARK 3 B22 (A**2) : 0.04000 REMARK 3 B33 (A**2) : -0.09000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.35000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.152 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.080 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.498 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1557 ; 0.011 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2109 ; 1.230 ; 1.932 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 202 ; 6.414 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 73 ;29.598 ;26.164 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 264 ;13.832 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;20.522 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 247 ; 0.086 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1164 ; 0.004 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 686 ; 0.203 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1113 ; 0.296 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 222 ; 0.168 ; 0.200 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): 46 ; 0.208 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 47 ; 0.190 ; 0.200 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): 1036 ; 1.087 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1604 ; 1.497 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 593 ; 2.132 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 505 ; 3.284 ; 4.500 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): 1629 ; 1.548 ; 3.000 REMARK 3 SPHERICITY; FREE ATOMS (A**2): 283 ; 3.166 ; 3.000 REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 1537 ; 1.576 ; 3.000 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 : 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 2Z21 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-07. REMARK 100 THE RCSB ID CODE IS RCSB027421. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 09-NOV-05 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 6.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19361 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 55.220 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 4.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 87.7 REMARK 200 DATA REDUNDANCY : 1.900 REMARK 200 R MERGE (I) : 0.09400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84 REMARK 200 COMPLETENESS FOR SHELL (%) : 42.3 REMARK 200 DATA REDUNDANCY IN SHELL : 1.40 REMARK 200 R MERGE FOR SHELL (I) : 0.24400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.700 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER 1.3.1 ARP/WARP REMARK 200 STARTING MODEL: PDB ENTRY 1LOM REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 43.53 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 8000, 100 MM MGSO4, PH REMARK 280 6.00, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 19.07150 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLU A 103 REMARK 465 HIS A 104 REMARK 465 HIS A 105 REMARK 465 HIS A 106 REMARK 465 HIS A 107 REMARK 465 HIS A 108 REMARK 465 HIS A 109 REMARK 465 LEU B 1 REMARK 465 HIS B 104 REMARK 465 HIS B 105 REMARK 465 HIS B 106 REMARK 465 HIS B 107 REMARK 465 HIS B 108 REMARK 465 HIS B 109 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 240 O HOH B 263 2.13 REMARK 500 OE2 GLU B 41 O HOH B 268 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 HIS A 90 -8.92 -141.39 REMARK 500 GLN B 78 31.14 70.54 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2PYS RELATED DB: PDB REMARK 900 WITH MANNOSE(DIMER) REMARK 900 RELATED ID: 1LOM RELATED DB: PDB REMARK 900 DOMAIN-SWAP-DIMER REMARK 900 RELATED ID: 1M5M RELATED DB: PDB REMARK 900 MAN9 RES 2.5 A REMARK 900 RELATED ID: 2EZM RELATED DB: PDB REMARK 900 NMR REMARK 900 RELATED ID: 1IIY RELATED DB: PDB REMARK 900 NMR WITH MANNOSE MONOMER REMARK 900 RELATED ID: 1L5E RELATED DB: PDB REMARK 900 NMR DBREF 2Z21 A 1 101 UNP P81180 CVN_NOSEL 1 101 DBREF 2Z21 B 1 101 UNP P81180 CVN_NOSEL 1 101 SEQADV 2Z21 ASN A 3 UNP P81180 LYS 3 ENGINEERED SEQADV 2Z21 ALA A 7 UNP P81180 THR 7 ENGINEERED SEQADV 2Z21 ILE A 23 UNP P81180 GLU 23 ENGINEERED SEQADV 2Z21 GLY A 51 UNP P81180 PRO 51 ENGINEERED SEQADV 2Z21 ALA A 93 UNP P81180 ASN 93 ENGINEERED SEQADV 2Z21 LEU A 102 UNP P81180 CLONING ARTIFACT SEQADV 2Z21 GLU A 103 UNP P81180 CLONING ARTIFACT SEQADV 2Z21 HIS A 104 UNP P81180 EXPRESSION TAG SEQADV 2Z21 HIS A 105 UNP P81180 EXPRESSION TAG SEQADV 2Z21 HIS A 106 UNP P81180 EXPRESSION TAG SEQADV 2Z21 HIS A 107 UNP P81180 EXPRESSION TAG SEQADV 2Z21 HIS A 108 UNP P81180 EXPRESSION TAG SEQADV 2Z21 HIS A 109 UNP P81180 EXPRESSION TAG SEQADV 2Z21 ASN B 3 UNP P81180 LYS 3 ENGINEERED SEQADV 2Z21 ALA B 7 UNP P81180 THR 7 ENGINEERED SEQADV 2Z21 ILE B 23 UNP P81180 GLU 23 ENGINEERED SEQADV 2Z21 GLY B 51 UNP P81180 PRO 51 ENGINEERED SEQADV 2Z21 ALA B 93 UNP P81180 ASN 93 ENGINEERED SEQADV 2Z21 LEU B 102 UNP P81180 CLONING ARTIFACT SEQADV 2Z21 GLU B 103 UNP P81180 CLONING ARTIFACT SEQADV 2Z21 HIS B 104 UNP P81180 EXPRESSION TAG SEQADV 2Z21 HIS B 105 UNP P81180 EXPRESSION TAG SEQADV 2Z21 HIS B 106 UNP P81180 EXPRESSION TAG SEQADV 2Z21 HIS B 107 UNP P81180 EXPRESSION TAG SEQADV 2Z21 HIS B 108 UNP P81180 EXPRESSION TAG SEQADV 2Z21 HIS B 109 UNP P81180 EXPRESSION TAG SEQRES 1 A 109 LEU GLY ASN PHE SER GLN ALA CYS TYR ASN SER ALA ILE SEQRES 2 A 109 GLN GLY SER VAL LEU THR SER THR CYS ILE ARG THR ASN SEQRES 3 A 109 GLY GLY TYR ASN THR SER SER ILE ASP LEU ASN SER VAL SEQRES 4 A 109 ILE GLU ASN VAL ASP GLY SER LEU LYS TRP GLN GLY SER SEQRES 5 A 109 ASN PHE ILE GLU THR CYS ARG ASN THR GLN LEU ALA GLY SEQRES 6 A 109 SER SER GLU LEU ALA ALA GLU CYS LYS THR ARG ALA GLN SEQRES 7 A 109 GLN PHE VAL SER THR LYS ILE ASN LEU ASP ASP HIS ILE SEQRES 8 A 109 ALA ALA ILE ASP GLY THR LEU LYS TYR GLU LEU GLU HIS SEQRES 9 A 109 HIS HIS HIS HIS HIS SEQRES 1 B 109 LEU GLY ASN PHE SER GLN ALA CYS TYR ASN SER ALA ILE SEQRES 2 B 109 GLN GLY SER VAL LEU THR SER THR CYS ILE ARG THR ASN SEQRES 3 B 109 GLY GLY TYR ASN THR SER SER ILE ASP LEU ASN SER VAL SEQRES 4 B 109 ILE GLU ASN VAL ASP GLY SER LEU LYS TRP GLN GLY SER SEQRES 5 B 109 ASN PHE ILE GLU THR CYS ARG ASN THR GLN LEU ALA GLY SEQRES 6 B 109 SER SER GLU LEU ALA ALA GLU CYS LYS THR ARG ALA GLN SEQRES 7 B 109 GLN PHE VAL SER THR LYS ILE ASN LEU ASP ASP HIS ILE SEQRES 8 B 109 ALA ALA ILE ASP GLY THR LEU LYS TYR GLU LEU GLU HIS SEQRES 9 B 109 HIS HIS HIS HIS HIS FORMUL 3 HOH *283(H2 O) HELIX 1 1 ASN A 3 ALA A 7 1 5 HELIX 2 2 ASN A 37 VAL A 39 5 3 HELIX 3 3 ASN A 53 GLU A 56 5 4 HELIX 4 4 ASN B 3 GLN B 6 5 4 HELIX 5 5 ASN B 53 GLU B 56 5 4 SHEET 1 A 3 CYS A 8 GLN A 14 0 SHEET 2 A 3 VAL A 17 ILE A 23 -1 O VAL A 17 N GLN A 14 SHEET 3 A 3 TYR A 29 ASP A 35 -1 O ASN A 30 N CYS A 22 SHEET 1 B 2 GLU A 41 VAL A 43 0 SHEET 2 B 2 SER A 46 LYS A 48 -1 O SER A 46 N VAL A 43 SHEET 1 C 3 CYS A 58 ALA A 64 0 SHEET 2 C 3 GLU A 68 LYS A 74 -1 O ALA A 70 N GLN A 62 SHEET 3 C 3 PHE A 80 ASN A 86 -1 O ILE A 85 N LEU A 69 SHEET 1 D 2 ILE A 91 ILE A 94 0 SHEET 2 D 2 THR A 97 TYR A 100 -1 O LYS A 99 N ALA A 92 SHEET 1 E 3 CYS B 8 GLN B 14 0 SHEET 2 E 3 VAL B 17 ILE B 23 -1 O THR B 21 N TYR B 9 SHEET 3 E 3 TYR B 29 ASP B 35 -1 O ASN B 30 N CYS B 22 SHEET 1 F 2 ILE B 40 VAL B 43 0 SHEET 2 F 2 SER B 46 TRP B 49 -1 O SER B 46 N VAL B 43 SHEET 1 G 3 CYS B 58 ALA B 64 0 SHEET 2 G 3 GLU B 68 LYS B 74 -1 O GLU B 68 N ALA B 64 SHEET 3 G 3 PHE B 80 ASN B 86 -1 O VAL B 81 N CYS B 73 SHEET 1 H 2 ILE B 91 ILE B 94 0 SHEET 2 H 2 THR B 97 TYR B 100 -1 O LYS B 99 N ALA B 92 SSBOND 1 CYS A 8 CYS A 22 1555 1555 2.03 SSBOND 2 CYS A 58 CYS A 73 1555 1555 2.05 SSBOND 3 CYS B 8 CYS B 22 1555 1555 2.04 SSBOND 4 CYS B 58 CYS B 73 1555 1555 2.02 CRYST1 49.457 38.143 56.039 90.00 99.98 90.00 P 1 21 1 4 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 0.020220 0.000000 0.003558 0.00000 SCALE2 0.000000 0.026217 0.000000 0.00000 SCALE3 0.000000 0.000000 0.018119 0.00000 ATOM 1 N LEU A 1 29.967 13.506 11.786 1.00 31.38 N ANISOU 1 N LEU A 1 4009 3981 3930 50 8 78 N ATOM 2 CA LEU A 1 29.417 12.896 13.025 1.00 30.38 C ANISOU 2 CA LEU A 1 3854 3851 3835 -9 -12 60 C ATOM 3 C LEU A 1 30.483 12.157 13.846 1.00 28.89 C ANISOU 3 C LEU A 1 3663 3637 3674 21 0 41 C ATOM 4 O LEU A 1 30.542 12.336 15.056 1.00 28.97 O ANISOU 4 O LEU A 1 3654 3640 3713 24 -1 102 O ATOM 5 CB LEU A 1 28.185 12.009 12.713 1.00 31.37 C ANISOU 5 CB LEU A 1 3953 4000 3964 18 -31 28 C ATOM 6 CG LEU A 1 28.043 10.594 13.299 1.00 32.33 C ANISOU 6 CG LEU A 1 4111 4044 4129 -40 -14 38 C ATOM 7 CD1 LEU A 1 26.631 10.279 13.793 1.00 33.88 C ANISOU 7 CD1 LEU A 1 4132 4296 4444 17 -25 -90 C ATOM 8 CD2 LEU A 1 28.526 9.546 12.283 1.00 33.41 C ANISOU 8 CD2 LEU A 1 4234 4216 4242 -65 -54 -55 C ATOM 9 N GLY A 2 31.326 11.352 13.201 1.00 27.54 N ANISOU 9 N GLY A 2 3488 3502 3473 -26 -22 94 N ATOM 10 CA GLY A 2 32.234 10.453 13.931 1.00 25.08 C ANISOU 10 CA GLY A 2 3129 3169 3229 -29 1 29 C ATOM 11 C GLY A 2 31.427 9.436 14.729 1.00 24.09 C ANISOU 11 C GLY A 2 3007 3072 3073 33 -14 9 C ATOM 12 O GLY A 2 30.677 8.638 14.152 1.00 23.10 O ANISOU 12 O GLY A 2 2848 2987 2939 17 -29 -13 O ATOM 13 N ASN A 3 31.568 9.465 16.052 1.00 22.38 N ANISOU 13 N ASN A 3 2755 2867 2880 7 -22 20 N ATOM 14 CA ASN A 3 30.748 8.631 16.945 1.00 22.09 C ANISOU 14 CA ASN A 3 2746 2842 2803 49 -46 20 C ATOM 15 C ASN A 3 30.870 7.122 16.761 1.00 21.32 C ANISOU 15 C ASN A 3 2688 2777 2634 1 -41 19 C ATOM 16 O ASN A 3 29.912 6.388 17.000 1.00 21.16 O ANISOU 16 O ASN A 3 2656 2747 2634 18 -57 9 O ATOM 17 CB ASN A 3 29.272 9.110 16.930 1.00 22.47 C ANISOU 17 CB ASN A 3 2741 2897 2900 -1 -18 41 C ATOM 18 CG ASN A 3 29.109 10.472 17.599 1.00 24.68 C ANISOU 18 CG ASN A 3 3048 3186 3141 113 -12 -46 C ATOM 19 OD1 ASN A 3 29.810 10.773 18.569 1.00 26.05 O ANISOU 19 OD1 ASN A 3 3123 3392 3381 188 -110 -194 O ATOM 20 ND2 ASN A 3 28.189 11.306 17.086 1.00 25.52 N ANISOU 20 ND2 ASN A 3 3159 3253 3283 130 -126 4 N ATOM 21 N PHE A 4 32.062 6.649 16.392 1.00 20.62 N ANISOU 21 N PHE A 4 2648 2618 2568 6 -44 31 N ATOM 22 CA PHE A 4 32.301 5.199 16.242 1.00 20.37 C ANISOU 22 CA PHE A 4 2594 2627 2518 7 -18 30 C ATOM 23 C PHE A 4 31.954 4.435 17.523 1.00 20.52 C ANISOU 23 C PHE A 4 2602 2650 2543 -21 -7 0 C ATOM 24 O PHE A 4 31.536 3.268 17.467 1.00 20.51 O ANISOU 24 O PHE A 4 2636 2690 2466 8 -18 -34 O ATOM 25 CB PHE A 4 33.766 4.911 15.870 1.00 19.84 C ANISOU 25 CB PHE A 4 2536 2556 2446 15 -14 59 C ATOM 26 CG PHE A 4 34.690 4.885 17.047 1.00 18.62 C ANISOU 26 CG PHE A 4 2361 2363 2347 -65 37 28 C ATOM 27 CD1 PHE A 4 35.035 3.669 17.651 1.00 17.37 C ANISOU 27 CD1 PHE A 4 2180 2178 2238 -80 9 0 C ATOM 28 CD2 PHE A 4 35.206 6.073 17.575 1.00 18.06 C ANISOU 28 CD2 PHE A 4 2324 2231 2307 4 27 56 C ATOM 29 CE1 PHE A 4 35.873 3.635 18.765 1.00 16.99 C ANISOU 29 CE1 PHE A 4 2128 2203 2124 -129 155 201 C ATOM 30 CE2 PHE A 4 36.038 6.054 18.681 1.00 16.60 C ANISOU 30 CE2 PHE A 4 1982 2130 2194 4 -32 -38 C ATOM 31 CZ PHE A 4 36.377 4.824 19.282 1.00 16.91 C ANISOU 31 CZ PHE A 4 2261 2108 2054 -107 -1 8 C ATOM 32 N SER A 5 32.144 5.080 18.678 1.00 20.43 N ANISOU 32 N SER A 5 2534 2621 2606 14 -2 -43 N ATOM 33 CA SER A 5 31.983 4.379 19.954 1.00 20.27 C ANISOU 33 CA SER A 5 2549 2565 2586 10 6 -18 C ATOM 34 C SER A 5 30.556 3.868 20.167 1.00 21.15 C ANISOU 34 C SER A 5 2634 2664 2734 -3 -20 -27 C ATOM 35 O SER A 5 30.340 2.914 20.913 1.00 19.64 O ANISOU 35 O SER A 5 2358 2469 2635 36 -63 65 O ATOM 36 CB SER A 5 32.425 5.241 21.145 1.00 20.41 C ANISOU 36 CB SER A 5 2582 2536 2636 5 3 -40 C ATOM 37 OG SER A 5 31.453 6.232 21.425 1.00 18.30 O ANISOU 37 OG SER A 5 2336 2363 2253 -81 67 -65 O ATOM 38 N GLN A 6 29.582 4.502 19.523 1.00 21.63 N ANISOU 38 N GLN A 6 2752 2701 2765 49 -24 0 N ATOM 39 CA GLN A 6 28.206 4.039 19.673 1.00 24.02 C ANISOU 39 CA GLN A 6 3026 3013 3085 64 -23 21 C ATOM 40 C GLN A 6 27.893 2.817 18.792 1.00 23.97 C ANISOU 40 C GLN A 6 2984 3037 3086 -9 -35 42 C ATOM 41 O GLN A 6 26.934 2.095 19.053 1.00 25.08 O ANISOU 41 O GLN A 6 3121 3206 3200 -90 -5 81 O ATOM 42 CB GLN A 6 27.196 5.193 19.495 1.00 25.00 C ANISOU 42 CB GLN A 6 3070 3202 3225 28 -30 44 C ATOM 43 CG GLN A 6 27.028 5.735 18.090 1.00 26.92 C ANISOU 43 CG GLN A 6 3402 3353 3472 187 -23 94 C ATOM 44 CD GLN A 6 26.021 6.901 18.017 1.00 29.63 C ANISOU 44 CD GLN A 6 3655 3613 3991 -38 -24 -27 C ATOM 45 OE1 GLN A 6 25.502 7.360 19.040 1.00 29.54 O ANISOU 45 OE1 GLN A 6 3792 3724 3708 213 174 -162 O ATOM 46 NE2 GLN A 6 25.747 7.372 16.796 1.00 30.16 N ANISOU 46 NE2 GLN A 6 3991 3776 3692 119 -213 240 N ATOM 47 N ALA A 7 28.720 2.588 17.773 1.00 22.93 N ANISOU 47 N ALA A 7 2829 2907 2974 24 -36 3 N ATOM 48 CA ALA A 7 28.593 1.436 16.865 1.00 22.36 C ANISOU 48 CA ALA A 7 2775 2816 2905 -8 -45 -3 C ATOM 49 C ALA A 7 29.560 0.287 17.174 1.00 21.98 C ANISOU 49 C ALA A 7 2725 2784 2842 -23 -29 -36 C ATOM 50 O ALA A 7 29.476 -0.802 16.558 1.00 21.62 O ANISOU 50 O ALA A 7 2645 2675 2892 -126 -115 -75 O ATOM 51 CB ALA A 7 28.794 1.890 15.432 1.00 22.83 C ANISOU 51 CB ALA A 7 2847 2866 2961 14 -66 3 C ATOM 52 N CYS A 8 30.483 0.523 18.108 1.00 20.98 N ANISOU 52 N CYS A 8 2626 2635 2707 -21 -31 -23 N ATOM 53 CA CYS A 8 31.635 -0.364 18.304 1.00 20.18 C ANISOU 53 CA CYS A 8 2555 2553 2561 -12 -21 14 C ATOM 54 C CYS A 8 31.856 -0.724 19.776 1.00 19.95 C ANISOU 54 C CYS A 8 2494 2545 2540 -8 23 24 C ATOM 55 O CYS A 8 31.313 -0.085 20.677 1.00 19.17 O ANISOU 55 O CYS A 8 2377 2420 2485 29 18 -21 O ATOM 56 CB CYS A 8 32.921 0.261 17.726 1.00 19.69 C ANISOU 56 CB CYS A 8 2525 2461 2494 -24 -12 43 C ATOM 57 SG CYS A 8 32.781 0.830 15.999 1.00 20.65 S ANISOU 57 SG CYS A 8 2761 2514 2571 -108 -157 -26 S ATOM 58 N TYR A 9 32.675 -1.746 20.003 1.00 19.12 N ANISOU 58 N TYR A 9 2351 2463 2447 -33 36 64 N ATOM 59 CA TYR A 9 32.979 -2.188 21.351 1.00 19.64 C ANISOU 59 CA TYR A 9 2407 2516 2539 -5 22 49 C ATOM 60 C TYR A 9 34.283 -2.962 21.331 1.00 18.59 C ANISOU 60 C TYR A 9 2296 2358 2406 -5 23 37 C ATOM 61 O TYR A 9 34.807 -3.269 20.251 1.00 16.95 O ANISOU 61 O TYR A 9 2085 2087 2265 44 -57 -9 O ATOM 62 CB TYR A 9 31.844 -3.066 21.901 1.00 20.80 C ANISOU 62 CB TYR A 9 2586 2637 2679 -62 73 35 C ATOM 63 CG TYR A 9 31.550 -4.283 21.055 1.00 23.27 C ANISOU 63 CG TYR A 9 2923 2988 2927 -68 42 -5 C ATOM 64 CD1 TYR A 9 32.105 -5.525 21.377 1.00 23.69 C ANISOU 64 CD1 TYR A 9 2810 3053 3139 45 79 -65 C ATOM 65 CD2 TYR A 9 30.706 -4.204 19.945 1.00 23.26 C ANISOU 65 CD2 TYR A 9 2857 3005 2974 -28 74 0 C ATOM 66 CE1 TYR A 9 31.834 -6.656 20.612 1.00 24.35 C ANISOU 66 CE1 TYR A 9 2866 3239 3144 -128 15 -126 C ATOM 67 CE2 TYR A 9 30.440 -5.340 19.164 1.00 24.62 C ANISOU 67 CE2 TYR A 9 3088 3115 3151 -80 60 -69 C ATOM 68 CZ TYR A 9 31.004 -6.553 19.513 1.00 24.93 C ANISOU 68 CZ TYR A 9 3115 3176 3181 -77 94 -109 C ATOM 69 OH TYR A 9 30.735 -7.691 18.767 1.00 26.61 O ANISOU 69 OH TYR A 9 3300 3397 3412 -169 21 -291 O ATOM 70 N ASN A 10 34.796 -3.246 22.532 1.00 17.76 N ANISOU 70 N ASN A 10 2219 2213 2315 -51 31 30 N ATOM 71 CA ASN A 10 36.068 -3.925 22.723 1.00 17.69 C ANISOU 71 CA ASN A 10 2205 2228 2288 -57 13 6 C ATOM 72 C ASN A 10 37.227 -3.126 22.142 1.00 17.76 C ANISOU 72 C ASN A 10 2218 2262 2265 -46 19 19 C ATOM 73 O ASN A 10 38.227 -3.692 21.712 1.00 17.30 O ANISOU 73 O ASN A 10 2163 2239 2170 -81 55 -53 O ATOM 74 CB ASN A 10 36.029 -5.346 22.149 1.00 17.95 C ANISOU 74 CB ASN A 10 2204 2296 2317 -62 28 -40 C ATOM 75 CG ASN A 10 35.173 -6.277 22.982 1.00 18.75 C ANISOU 75 CG ASN A 10 2469 2284 2367 -70 10 44 C ATOM 76 OD1 ASN A 10 34.806 -5.957 24.123 1.00 19.32 O ANISOU 76 OD1 ASN A 10 2527 2276 2537 -195 99 -99 O ATOM 77 ND2 ASN A 10 34.839 -7.430 22.421 1.00 19.81 N ANISOU 77 ND2 ASN A 10 2847 2304 2374 -45 29 36 N ATOM 78 N SER A 11 37.076 -1.804 22.149 1.00 17.23 N ANISOU 78 N SER A 11 2170 2197 2178 -58 -5 -39 N ATOM 79 CA SER A 11 38.055 -0.915 21.541 1.00 17.26 C ANISOU 79 CA SER A 11 2158 2203 2195 -41 -21 16 C ATOM 80 C SER A 11 39.382 -0.937 22.309 1.00 17.55 C ANISOU 80 C SER A 11 2163 2257 2248 -44 3 17 C ATOM 81 O SER A 11 39.415 -1.203 23.527 1.00 16.48 O ANISOU 81 O SER A 11 1992 2165 2104 -122 12 80 O ATOM 82 CB SER A 11 37.496 0.502 21.475 1.00 17.91 C ANISOU 82 CB SER A 11 2206 2299 2299 5 -34 42 C ATOM 83 OG SER A 11 36.278 0.518 20.733 1.00 17.02 O ANISOU 83 OG SER A 11 1976 2247 2243 -3 -45 38 O ATOM 84 N ALA A 12 40.476 -0.685 21.589 1.00 17.19 N ANISOU 84 N ALA A 12 2162 2123 2243 -48 9 39 N ATOM 85 CA ALA A 12 41.772 -0.588 22.225 1.00 17.47 C ANISOU 85 CA ALA A 12 2163 2192 2281 -52 3 14 C ATOM 86 C ALA A 12 42.687 0.359 21.464 1.00 17.94 C ANISOU 86 C ALA A 12 2251 2241 2324 -46 -11 39 C ATOM 87 O ALA A 12 42.527 0.582 20.253 1.00 17.46 O ANISOU 87 O ALA A 12 2168 2217 2248 -119 -38 15 O ATOM 88 CB ALA A 12 42.428 -1.973 22.366 1.00 17.50 C ANISOU 88 CB ALA A 12 2175 2213 2259 -52 32 26 C ATOM 89 N ILE A 13 43.651 0.907 22.190 1.00 18.28 N ANISOU 89 N ILE A 13 2313 2282 2348 -51 -50 -6 N ATOM 90 CA ILE A 13 44.705 1.719 21.593 1.00 18.98 C ANISOU 90 CA ILE A 13 2339 2440 2430 -13 10 23 C ATOM 91 C ILE A 13 46.036 1.021 21.817 1.00 18.91 C ANISOU 91 C ILE A 13 2352 2414 2416 -7 -9 26 C ATOM 92 O ILE A 13 46.351 0.638 22.932 1.00 18.39 O ANISOU 92 O ILE A 13 2257 2325 2404 62 -21 122 O ATOM 93 CB ILE A 13 44.759 3.145 22.220 1.00 19.47 C ANISOU 93 CB ILE A 13 2424 2485 2487 -75 -12 6 C ATOM 94 CG1 ILE A 13 43.613 4.011 21.699 1.00 20.69 C ANISOU 94 CG1 ILE A 13 2478 2706 2676 14 46 6 C ATOM 95 CG2 ILE A 13 46.110 3.849 21.919 1.00 19.79 C ANISOU 95 CG2 ILE A 13 2301 2734 2482 -71 51 34 C ATOM 96 CD1 ILE A 13 43.761 4.434 20.255 1.00 21.97 C ANISOU 96 CD1 ILE A 13 2759 2839 2748 -101 -55 92 C ATOM 97 N GLN A 14 46.807 0.871 20.744 1.00 19.05 N ANISOU 97 N GLN A 14 2377 2419 2440 31 -9 6 N ATOM 98 CA GLN A 14 48.158 0.364 20.815 1.00 19.58 C ANISOU 98 CA GLN A 14 2385 2526 2529 -19 29 29 C ATOM 99 C GLN A 14 49.001 1.241 19.885 1.00 18.75 C ANISOU 99 C GLN A 14 2316 2323 2484 -27 -12 36 C ATOM 100 O GLN A 14 48.739 1.329 18.673 1.00 17.22 O ANISOU 100 O GLN A 14 2024 2240 2278 -106 34 -20 O ATOM 101 CB GLN A 14 48.201 -1.110 20.380 1.00 20.18 C ANISOU 101 CB GLN A 14 2503 2520 2644 -35 19 73 C ATOM 102 CG GLN A 14 46.972 -1.927 20.858 1.00 25.08 C ANISOU 102 CG GLN A 14 3126 3167 3235 -19 27 72 C ATOM 103 CD GLN A 14 45.985 -2.314 19.740 1.00 26.63 C ANISOU 103 CD GLN A 14 3410 3338 3368 -14 -205 -68 C ATOM 104 OE1 GLN A 14 45.350 -1.462 19.060 1.00 24.69 O ANISOU 104 OE1 GLN A 14 3357 3038 2983 -82 103 9 O ATOM 105 NE2 GLN A 14 45.812 -3.609 19.587 1.00 28.02 N ANISOU 105 NE2 GLN A 14 3626 3446 3574 202 -42 144 N ATOM 106 N GLY A 15 50.005 1.899 20.452 1.00 17.75 N ANISOU 106 N GLY A 15 2185 2174 2385 5 3 19 N ATOM 107 CA GLY A 15 50.718 2.938 19.704 1.00 17.80 C ANISOU 107 CA GLY A 15 2211 2243 2307 -54 23 43 C ATOM 108 C GLY A 15 49.749 3.986 19.208 1.00 17.25 C ANISOU 108 C GLY A 15 2197 2122 2235 -113 12 15 C ATOM 109 O GLY A 15 48.987 4.542 19.991 1.00 17.10 O ANISOU 109 O GLY A 15 2074 2182 2238 -73 26 36 O ATOM 110 N SER A 16 49.755 4.247 17.900 1.00 17.38 N ANISOU 110 N SER A 16 2241 2134 2225 -149 25 30 N ATOM 111 CA SER A 16 48.773 5.178 17.318 1.00 17.11 C ANISOU 111 CA SER A 16 2164 2127 2209 -88 12 25 C ATOM 112 C SER A 16 47.578 4.478 16.656 1.00 17.39 C ANISOU 112 C SER A 16 2239 2180 2188 -64 12 15 C ATOM 113 O SER A 16 46.765 5.120 15.977 1.00 16.95 O ANISOU 113 O SER A 16 2083 2171 2187 -55 108 61 O ATOM 114 CB SER A 16 49.434 6.167 16.348 1.00 17.43 C ANISOU 114 CB SER A 16 2298 2138 2185 -47 23 -8 C ATOM 115 OG SER A 16 50.114 5.515 15.298 1.00 16.68 O ANISOU 115 OG SER A 16 2188 1953 2194 -56 -7 50 O ATOM 116 N VAL A 17 47.458 3.172 16.876 1.00 16.75 N ANISOU 116 N VAL A 17 2125 2124 2113 -36 35 43 N ATOM 117 CA VAL A 17 46.435 2.380 16.185 1.00 16.58 C ANISOU 117 CA VAL A 17 2116 2104 2076 -42 57 24 C ATOM 118 C VAL A 17 45.234 2.086 17.099 1.00 16.59 C ANISOU 118 C VAL A 17 2105 2099 2100 -16 42 -15 C ATOM 119 O VAL A 17 45.386 1.522 18.174 1.00 16.33 O ANISOU 119 O VAL A 17 2120 1979 2104 -7 82 39 O ATOM 120 CB VAL A 17 47.020 1.096 15.538 1.00 16.15 C ANISOU 120 CB VAL A 17 2022 2095 2019 -22 65 57 C ATOM 121 CG1 VAL A 17 45.913 0.110 15.117 1.00 16.18 C ANISOU 121 CG1 VAL A 17 2110 2013 2023 7 19 3 C ATOM 122 CG2 VAL A 17 47.903 1.456 14.327 1.00 17.05 C ANISOU 122 CG2 VAL A 17 2202 2187 2087 22 147 -33 C ATOM 123 N LEU A 18 44.062 2.520 16.647 1.00 16.81 N ANISOU 123 N LEU A 18 2121 2103 2163 37 41 -24 N ATOM 124 CA LEU A 18 42.780 2.196 17.266 1.00 16.54 C ANISOU 124 CA LEU A 18 2076 2093 2114 46 -11 7 C ATOM 125 C LEU A 18 42.234 0.938 16.605 1.00 16.94 C ANISOU 125 C LEU A 18 2099 2134 2202 65 -13 17 C ATOM 126 O LEU A 18 42.111 0.869 15.378 1.00 16.93 O ANISOU 126 O LEU A 18 2129 2107 2196 137 -24 1 O ATOM 127 CB LEU A 18 41.783 3.339 17.035 1.00 16.40 C ANISOU 127 CB LEU A 18 2092 2057 2080 80 49 -39 C ATOM 128 CG LEU A 18 40.328 3.138 17.497 1.00 16.26 C ANISOU 128 CG LEU A 18 2015 2188 1972 8 -57 -75 C ATOM 129 CD1 LEU A 18 40.206 3.044 19.030 1.00 15.15 C ANISOU 129 CD1 LEU A 18 1842 2133 1778 55 33 44 C ATOM 130 CD2 LEU A 18 39.426 4.253 16.956 1.00 15.51 C ANISOU 130 CD2 LEU A 18 2025 1973 1893 77 -47 22 C ATOM 131 N THR A 19 41.903 -0.053 17.420 1.00 17.36 N ANISOU 131 N THR A 19 2131 2203 2261 0 -28 26 N ATOM 132 CA THR A 19 41.227 -1.248 16.932 1.00 17.55 C ANISOU 132 CA THR A 19 2196 2220 2250 -6 -17 11 C ATOM 133 C THR A 19 39.871 -1.289 17.621 1.00 17.68 C ANISOU 133 C THR A 19 2205 2216 2293 -54 -18 31 C ATOM 134 O THR A 19 39.739 -0.878 18.765 1.00 17.63 O ANISOU 134 O THR A 19 2170 2250 2278 -126 -8 16 O ATOM 135 CB THR A 19 42.014 -2.530 17.265 1.00 17.56 C ANISOU 135 CB THR A 19 2197 2260 2215 15 -7 68 C ATOM 136 OG1 THR A 19 42.241 -2.575 18.681 1.00 18.94 O ANISOU 136 OG1 THR A 19 2404 2398 2393 -134 -81 -29 O ATOM 137 CG2 THR A 19 43.369 -2.544 16.552 1.00 15.15 C ANISOU 137 CG2 THR A 19 2002 1951 1802 62 -119 75 C ATOM 138 N SER A 20 38.851 -1.746 16.913 1.00 18.19 N ANISOU 138 N SER A 20 2304 2266 2339 -46 -26 12 N ATOM 139 CA SER A 20 37.532 -1.881 17.529 1.00 18.10 C ANISOU 139 CA SER A 20 2266 2244 2367 -24 -73 -52 C ATOM 140 C SER A 20 36.733 -2.885 16.751 1.00 18.37 C ANISOU 140 C SER A 20 2313 2256 2408 -53 -65 -40 C ATOM 141 O SER A 20 37.013 -3.121 15.572 1.00 18.41 O ANISOU 141 O SER A 20 2390 2210 2393 -140 -139 -119 O ATOM 142 CB SER A 20 36.781 -0.546 17.580 1.00 18.21 C ANISOU 142 CB SER A 20 2280 2284 2354 1 -33 16 C ATOM 143 OG SER A 20 35.707 -0.659 18.497 1.00 18.05 O ANISOU 143 OG SER A 20 2280 2254 2322 109 -35 -59 O ATOM 144 N THR A 21 35.740 -3.452 17.425 1.00 18.35 N ANISOU 144 N THR A 21 2339 2247 2384 -57 -91 -3 N ATOM 145 CA THR A 21 34.818 -4.409 16.822 1.00 18.59 C ANISOU 145 CA THR A 21 2325 2281 2456 -99 -70 10 C ATOM 146 C THR A 21 33.502 -3.673 16.598 1.00 19.15 C ANISOU 146 C THR A 21 2368 2331 2574 -100 -41 2 C ATOM 147 O THR A 21 32.871 -3.206 17.548 1.00 18.86 O ANISOU 147 O THR A 21 2299 2264 2602 -57 -91 -65 O ATOM 148 CB THR A 21 34.638 -5.626 17.738 1.00 18.33 C ANISOU 148 CB THR A 21 2332 2294 2339 -87 -38 -2 C ATOM 149 OG1 THR A 21 35.921 -6.222 17.966 1.00 18.11 O ANISOU 149 OG1 THR A 21 2378 2327 2173 -154 -196 72 O ATOM 150 CG2 THR A 21 33.722 -6.675 17.086 1.00 17.22 C ANISOU 150 CG2 THR A 21 2162 2161 2219 -198 5 61 C ATOM 151 N CYS A 22 33.107 -3.545 15.339 1.00 20.00 N ANISOU 151 N CYS A 22 2453 2444 2701 -111 -115 -40 N ATOM 152 CA CYS A 22 31.967 -2.694 15.010 1.00 22.12 C ANISOU 152 CA CYS A 22 2684 2789 2930 -56 -104 -32 C ATOM 153 C CYS A 22 30.854 -3.465 14.317 1.00 23.76 C ANISOU 153 C CYS A 22 2903 3008 3117 -80 -119 -42 C ATOM 154 O CYS A 22 31.108 -4.437 13.607 1.00 23.27 O ANISOU 154 O CYS A 22 2762 3036 3043 -78 -124 -59 O ATOM 155 CB CYS A 22 32.397 -1.508 14.159 1.00 21.49 C ANISOU 155 CB CYS A 22 2608 2768 2787 -95 -162 -9 C ATOM 156 SG CYS A 22 33.753 -0.529 14.849 1.00 20.71 S ANISOU 156 SG CYS A 22 2443 2628 2797 -160 -210 -1 S ATOM 157 N ILE A 23 29.626 -3.016 14.543 1.00 26.42 N ANISOU 157 N ILE A 23 3252 3343 3443 -32 -50 -22 N ATOM 158 CA ILE A 23 28.422 -3.677 14.011 1.00 29.37 C ANISOU 158 CA ILE A 23 3636 3725 3796 -56 -50 -54 C ATOM 159 C ILE A 23 28.321 -3.633 12.476 1.00 31.20 C ANISOU 159 C ILE A 23 3891 3977 3984 -8 -56 -10 C ATOM 160 O ILE A 23 28.642 -2.628 11.856 1.00 30.67 O ANISOU 160 O ILE A 23 3790 3875 3985 -76 -65 -120 O ATOM 161 CB ILE A 23 27.141 -3.098 14.681 1.00 29.26 C ANISOU 161 CB ILE A 23 3590 3739 3788 -37 -77 -9 C ATOM 162 CG1 ILE A 23 25.949 -4.043 14.508 1.00 29.57 C ANISOU 162 CG1 ILE A 23 3688 3714 3832 -45 -9 33 C ATOM 163 CG2 ILE A 23 26.851 -1.666 14.203 1.00 29.14 C ANISOU 163 CG2 ILE A 23 3572 3693 3806 -81 -43 -32 C ATOM 164 CD1 ILE A 23 24.760 -3.657 15.378 1.00 30.05 C ANISOU 164 CD1 ILE A 23 3743 3835 3839 -3 -10 -17 C ATOM 165 N ARG A 24 27.882 -4.744 11.881 1.00 33.97 N ANISOU 165 N ARG A 24 4272 4281 4353 -24 -66 -66 N ATOM 166 CA ARG A 24 27.655 -4.835 10.437 1.00 37.18 C ANISOU 166 CA ARG A 24 4713 4721 4691 8 -35 -39 C ATOM 167 C ARG A 24 26.153 -4.915 10.154 1.00 38.69 C ANISOU 167 C ARG A 24 4875 4915 4908 -14 -35 -43 C ATOM 168 O ARG A 24 25.417 -5.604 10.866 1.00 39.00 O ANISOU 168 O ARG A 24 4945 4895 4976 -53 -61 -56 O ATOM 169 CB ARG A 24 28.298 -6.105 9.872 1.00 37.66 C ANISOU 169 CB ARG A 24 4801 4744 4762 14 -13 -30 C ATOM 170 CG ARG A 24 29.795 -6.196 10.012 1.00 40.16 C ANISOU 170 CG ARG A 24 5009 5051 5197 9 -79 -84 C ATOM 171 CD ARG A 24 30.496 -5.656 8.787 1.00 43.81 C ANISOU 171 CD ARG A 24 5564 5604 5475 -25 117 80 C ATOM 172 NE ARG A 24 30.106 -6.352 7.561 1.00 47.33 N ANISOU 172 NE ARG A 24 5987 6029 5967 -19 -68 -46 N ATOM 173 CZ ARG A 24 30.648 -7.489 7.129 1.00 49.74 C ANISOU 173 CZ ARG A 24 6312 6207 6379 23 11 -44 C ATOM 174 NH1 ARG A 24 31.608 -8.096 7.827 1.00 50.35 N ANISOU 174 NH1 ARG A 24 6343 6383 6403 20 -76 -3 N ATOM 175 NH2 ARG A 24 30.221 -8.030 5.997 1.00 49.77 N ANISOU 175 NH2 ARG A 24 6303 6303 6303 -7 -55 -63 N ATOM 176 N THR A 25 25.708 -4.225 9.106 1.00 40.48 N ANISOU 176 N THR A 25 5118 5138 5122 0 -41 -21 N ATOM 177 CA THR A 25 24.282 -4.218 8.734 1.00 42.17 C ANISOU 177 CA THR A 25 5318 5350 5353 0 -29 -15 C ATOM 178 C THR A 25 23.712 -5.602 8.390 1.00 42.66 C ANISOU 178 C THR A 25 5385 5410 5411 -17 -26 -25 C ATOM 179 O THR A 25 22.499 -5.800 8.439 1.00 42.89 O ANISOU 179 O THR A 25 5411 5453 5432 -13 -16 -23 O ATOM 180 CB THR A 25 23.986 -3.243 7.590 1.00 42.32 C ANISOU 180 CB THR A 25 5363 5360 5357 8 -34 3 C ATOM 181 OG1 THR A 25 25.083 -3.232 6.671 1.00 43.47 O ANISOU 181 OG1 THR A 25 5417 5534 5563 36 32 -13 O ATOM 182 CG2 THR A 25 23.776 -1.843 8.138 1.00 42.95 C ANISOU 182 CG2 THR A 25 5477 5410 5429 13 -49 -38 C ATOM 183 N ASN A 26 24.581 -6.553 8.055 1.00 43.21 N ANISOU 183 N ASN A 26 5458 5463 5495 -8 -23 -32 N ATOM 184 CA ASN A 26 24.139 -7.924 7.833 1.00 43.64 C ANISOU 184 CA ASN A 26 5527 5508 5543 -11 -12 -17 C ATOM 185 C ASN A 26 23.763 -8.620 9.145 1.00 43.41 C ANISOU 185 C ASN A 26 5496 5480 5515 0 -25 -17 C ATOM 186 O ASN A 26 23.209 -9.727 9.143 1.00 43.90 O ANISOU 186 O ASN A 26 5533 5546 5601 -15 -53 -26 O ATOM 187 CB ASN A 26 25.168 -8.725 7.007 1.00 44.04 C ANISOU 187 CB ASN A 26 5578 5558 5594 -11 0 -18 C ATOM 188 CG ASN A 26 26.425 -9.092 7.791 1.00 45.21 C ANISOU 188 CG ASN A 26 5707 5680 5789 -38 -4 19 C ATOM 189 OD1 ASN A 26 26.575 -8.767 8.971 1.00 46.44 O ANISOU 189 OD1 ASN A 26 6031 5813 5800 -94 -10 -73 O ATOM 190 ND2 ASN A 26 27.334 -9.792 7.126 1.00 44.92 N ANISOU 190 ND2 ASN A 26 5661 5701 5705 -26 75 7 N ATOM 191 N GLY A 27 24.053 -7.947 10.260 1.00 42.70 N ANISOU 191 N GLY A 27 5401 5390 5432 -7 -23 -6 N ATOM 192 CA GLY A 27 23.739 -8.445 11.599 1.00 41.59 C ANISOU 192 CA GLY A 27 5228 5273 5298 16 -20 -12 C ATOM 193 C GLY A 27 24.951 -8.993 12.330 1.00 40.60 C ANISOU 193 C GLY A 27 5104 5164 5157 -11 -3 -19 C ATOM 194 O GLY A 27 24.846 -9.438 13.480 1.00 41.08 O ANISOU 194 O GLY A 27 5168 5248 5192 -3 -5 -16 O ATOM 195 N GLY A 28 26.101 -8.974 11.656 1.00 39.23 N ANISOU 195 N GLY A 28 4924 4975 5005 -6 -48 -40 N ATOM 196 CA GLY A 28 27.343 -9.453 12.242 1.00 37.11 C ANISOU 196 CA GLY A 28 4646 4693 4761 -33 -29 -64 C ATOM 197 C GLY A 28 28.204 -8.317 12.768 1.00 35.76 C ANISOU 197 C GLY A 28 4454 4533 4598 0 -58 -65 C ATOM 198 O GLY A 28 27.705 -7.257 13.154 1.00 35.30 O ANISOU 198 O GLY A 28 4368 4458 4584 -24 -115 -74 O ATOM 199 N TYR A 29 29.507 -8.550 12.791 1.00 34.22 N ANISOU 199 N TYR A 29 4280 4343 4376 -37 -38 -89 N ATOM 200 CA TYR A 29 30.451 -7.574 13.315 1.00 33.26 C ANISOU 200 CA TYR A 29 4129 4238 4267 -14 -14 -40 C ATOM 201 C TYR A 29 31.787 -7.787 12.630 1.00 31.61 C ANISOU 201 C TYR A 29 3960 4022 4026 -51 -47 -41 C ATOM 202 O TYR A 29 32.056 -8.859 12.092 1.00 31.20 O ANISOU 202 O TYR A 29 3832 3957 4065 -45 -74 -87 O ATOM 203 CB TYR A 29 30.582 -7.689 14.845 1.00 33.98 C ANISOU 203 CB TYR A 29 4287 4284 4337 -1 -21 -17 C ATOM 204 CG TYR A 29 30.939 -9.083 15.352 1.00 36.12 C ANISOU 204 CG TYR A 29 4586 4553 4582 -19 -27 14 C ATOM 205 CD1 TYR A 29 32.275 -9.503 15.438 1.00 37.47 C ANISOU 205 CD1 TYR A 29 4747 4741 4747 -6 34 -23 C ATOM 206 CD2 TYR A 29 29.940 -9.974 15.759 1.00 37.63 C ANISOU 206 CD2 TYR A 29 4812 4731 4754 -43 1 31 C ATOM 207 CE1 TYR A 29 32.606 -10.780 15.909 1.00 37.55 C ANISOU 207 CE1 TYR A 29 4803 4641 4822 -11 17 92 C ATOM 208 CE2 TYR A 29 30.256 -11.253 16.225 1.00 37.50 C ANISOU 208 CE2 TYR A 29 4803 4633 4811 -3 -18 39 C ATOM 209 CZ TYR A 29 31.583 -11.649 16.297 1.00 37.56 C ANISOU 209 CZ TYR A 29 4829 4640 4799 10 -27 55 C ATOM 210 OH TYR A 29 31.889 -12.911 16.763 1.00 37.77 O ANISOU 210 OH TYR A 29 4749 4710 4889 -116 -22 -47 O ATOM 211 N ASN A 30 32.624 -6.760 12.657 1.00 29.42 N ANISOU 211 N ASN A 30 3675 3775 3728 -36 -52 -31 N ATOM 212 CA ASN A 30 33.888 -6.794 11.971 1.00 27.67 C ANISOU 212 CA ASN A 30 3501 3526 3486 -74 -74 -71 C ATOM 213 C ASN A 30 34.897 -6.105 12.869 1.00 26.32 C ANISOU 213 C ASN A 30 3314 3354 3332 -62 -46 -19 C ATOM 214 O ASN A 30 34.588 -5.063 13.443 1.00 24.11 O ANISOU 214 O ASN A 30 3070 3078 3011 -145 -32 -54 O ATOM 215 CB ASN A 30 33.768 -6.026 10.660 1.00 28.13 C ANISOU 215 CB ASN A 30 3536 3637 3513 -40 -69 -44 C ATOM 216 CG ASN A 30 35.066 -5.973 9.896 1.00 30.07 C ANISOU 216 CG ASN A 30 3784 3953 3686 -37 -58 -32 C ATOM 217 OD1 ASN A 30 35.652 -7.011 9.578 1.00 31.89 O ANISOU 217 OD1 ASN A 30 4062 4058 3996 69 -2 -124 O ATOM 218 ND2 ASN A 30 35.530 -4.762 9.593 1.00 29.99 N ANISOU 218 ND2 ASN A 30 3935 3831 3627 -30 -20 59 N ATOM 219 N THR A 31 36.069 -6.715 13.016 1.00 24.87 N ANISOU 219 N THR A 31 3186 3115 3148 -47 17 -50 N ATOM 220 CA THR A 31 37.151 -6.097 13.764 1.00 24.74 C ANISOU 220 CA THR A 31 3131 3103 3166 6 0 -25 C ATOM 221 C THR A 31 38.000 -5.321 12.773 1.00 24.07 C ANISOU 221 C THR A 31 3028 3044 3073 5 14 -68 C ATOM 222 O THR A 31 38.406 -5.847 11.726 1.00 24.09 O ANISOU 222 O THR A 31 3057 3069 3027 11 82 -87 O ATOM 223 CB THR A 31 37.997 -7.121 14.529 1.00 25.47 C ANISOU 223 CB THR A 31 3253 3179 3242 -4 16 -22 C ATOM 224 OG1 THR A 31 38.514 -8.088 13.603 1.00 28.28 O ANISOU 224 OG1 THR A 31 3502 3484 3760 9 16 -84 O ATOM 225 CG2 THR A 31 37.142 -7.832 15.560 1.00 24.49 C ANISOU 225 CG2 THR A 31 3064 3111 3127 -89 -5 11 C ATOM 226 N SER A 32 38.222 -4.049 13.061 1.00 22.63 N ANISOU 226 N SER A 32 2828 2889 2882 -19 -12 -64 N ATOM 227 CA SER A 32 39.050 -3.255 12.188 1.00 21.60 C ANISOU 227 CA SER A 32 2685 2723 2798 -21 -64 -46 C ATOM 228 C SER A 32 39.968 -2.334 12.971 1.00 20.51 C ANISOU 228 C SER A 32 2580 2551 2661 -67 -22 -20 C ATOM 229 O SER A 32 39.928 -2.286 14.190 1.00 18.73 O ANISOU 229 O SER A 32 2335 2250 2531 -240 6 -64 O ATOM 230 CB SER A 32 38.205 -2.483 11.171 1.00 22.20 C ANISOU 230 CB SER A 32 2742 2822 2870 -21 -109 -63 C ATOM 231 OG SER A 32 37.627 -1.337 11.752 1.00 22.30 O ANISOU 231 OG SER A 32 2574 2864 3034 248 -196 -165 O ATOM 232 N SER A 33 40.814 -1.624 12.239 1.00 20.34 N ANISOU 232 N SER A 33 2543 2559 2625 -67 2 -30 N ATOM 233 CA SER A 33 41.837 -0.781 12.835 1.00 19.68 C ANISOU 233 CA SER A 33 2460 2422 2594 -44 -20 -8 C ATOM 234 C SER A 33 42.050 0.451 11.978 1.00 19.17 C ANISOU 234 C SER A 33 2395 2415 2472 -23 10 -13 C ATOM 235 O SER A 33 41.751 0.457 10.773 1.00 19.12 O ANISOU 235 O SER A 33 2409 2345 2511 -59 -54 -25 O ATOM 236 CB SER A 33 43.151 -1.562 13.008 1.00 19.87 C ANISOU 236 CB SER A 33 2496 2422 2629 -48 23 -33 C ATOM 237 OG SER A 33 43.623 -2.028 11.760 1.00 20.38 O ANISOU 237 OG SER A 33 2539 2451 2751 -90 87 55 O ATOM 238 N ILE A 34 42.530 1.512 12.615 1.00 18.10 N ANISOU 238 N ILE A 34 2262 2267 2349 -14 -42 30 N ATOM 239 CA ILE A 34 42.872 2.736 11.906 1.00 17.64 C ANISOU 239 CA ILE A 34 2201 2228 2271 15 -6 34 C ATOM 240 C ILE A 34 44.084 3.347 12.571 1.00 17.07 C ANISOU 240 C ILE A 34 2140 2138 2208 -8 15 41 C ATOM 241 O ILE A 34 44.197 3.324 13.801 1.00 16.33 O ANISOU 241 O ILE A 34 2066 2033 2102 -39 40 118 O ATOM 242 CB ILE A 34 41.669 3.741 11.840 1.00 17.45 C ANISOU 242 CB ILE A 34 2258 2170 2202 63 5 46 C ATOM 243 CG1 ILE A 34 42.005 4.944 10.947 1.00 18.02 C ANISOU 243 CG1 ILE A 34 2238 2333 2273 47 -50 43 C ATOM 244 CG2 ILE A 34 41.192 4.166 13.268 1.00 17.76 C ANISOU 244 CG2 ILE A 34 2285 2117 2342 101 -1 -116 C ATOM 245 CD1 ILE A 34 40.755 5.715 10.462 1.00 16.84 C ANISOU 245 CD1 ILE A 34 2064 2084 2248 74 -18 85 C ATOM 246 N ASP A 35 45.011 3.847 11.748 1.00 16.98 N ANISOU 246 N ASP A 35 2142 2149 2158 -3 28 107 N ATOM 247 CA ASP A 35 46.197 4.555 12.242 1.00 15.91 C ANISOU 247 CA ASP A 35 2039 1986 2017 -35 -1 32 C ATOM 248 C ASP A 35 45.862 6.032 12.499 1.00 16.18 C ANISOU 248 C ASP A 35 2062 2033 2052 -19 36 36 C ATOM 249 O ASP A 35 45.765 6.839 11.554 1.00 15.89 O ANISOU 249 O ASP A 35 2091 2002 1944 -33 -31 88 O ATOM 250 CB ASP A 35 47.352 4.449 11.225 1.00 16.73 C ANISOU 250 CB ASP A 35 2041 2065 2250 -5 -23 2 C ATOM 251 CG ASP A 35 48.635 5.122 11.719 1.00 17.05 C ANISOU 251 CG ASP A 35 2110 2143 2223 -20 -44 -21 C ATOM 252 OD1 ASP A 35 48.686 5.529 12.903 1.00 17.07 O ANISOU 252 OD1 ASP A 35 1990 2113 2380 280 40 -129 O ATOM 253 OD2 ASP A 35 49.603 5.213 10.929 1.00 18.61 O ANISOU 253 OD2 ASP A 35 2301 2277 2490 -150 -23 -31 O ATOM 254 N LEU A 36 45.709 6.390 13.770 1.00 14.70 N ANISOU 254 N LEU A 36 1966 1779 1838 -72 15 -30 N ATOM 255 CA LEU A 36 45.309 7.767 14.152 1.00 15.27 C ANISOU 255 CA LEU A 36 1950 1900 1950 33 53 26 C ATOM 256 C LEU A 36 46.418 8.782 13.857 1.00 15.17 C ANISOU 256 C LEU A 36 1993 1849 1918 2 35 -3 C ATOM 257 O LEU A 36 46.194 9.991 13.857 1.00 15.38 O ANISOU 257 O LEU A 36 1996 1966 1882 119 40 128 O ATOM 258 CB LEU A 36 44.953 7.827 15.633 1.00 14.69 C ANISOU 258 CB LEU A 36 1900 1763 1917 30 49 -46 C ATOM 259 CG LEU A 36 43.793 6.939 16.115 1.00 15.83 C ANISOU 259 CG LEU A 36 2047 1915 2050 -45 83 -40 C ATOM 260 CD1 LEU A 36 43.842 6.894 17.650 1.00 18.98 C ANISOU 260 CD1 LEU A 36 2526 2346 2336 -133 66 -14 C ATOM 261 CD2 LEU A 36 42.449 7.463 15.615 1.00 17.68 C ANISOU 261 CD2 LEU A 36 2171 2229 2318 -148 181 -45 C ATOM 262 N ASN A 37 47.622 8.278 13.613 1.00 14.98 N ANISOU 262 N ASN A 37 1863 1905 1923 -20 -17 46 N ATOM 263 CA ASN A 37 48.764 9.140 13.316 1.00 15.28 C ANISOU 263 CA ASN A 37 1973 1926 1908 -32 15 21 C ATOM 264 C ASN A 37 48.605 9.900 11.999 1.00 15.65 C ANISOU 264 C ASN A 37 2007 2004 1932 -25 10 0 C ATOM 265 O ASN A 37 49.273 10.904 11.794 1.00 15.17 O ANISOU 265 O ASN A 37 2152 1822 1788 -45 2 -3 O ATOM 266 CB ASN A 37 50.068 8.340 13.313 1.00 14.24 C ANISOU 266 CB ASN A 37 1852 1796 1762 -53 -44 -4 C ATOM 267 CG ASN A 37 51.297 9.229 13.414 1.00 15.07 C ANISOU 267 CG ASN A 37 1955 1900 1870 31 -39 69 C ATOM 268 OD1 ASN A 37 51.318 10.206 14.178 1.00 12.46 O ANISOU 268 OD1 ASN A 37 1582 1283 1867 -3 -114 6 O ATOM 269 ND2 ASN A 37 52.333 8.882 12.674 1.00 16.53 N ANISOU 269 ND2 ASN A 37 2211 2012 2057 120 142 -43 N ATOM 270 N SER A 38 47.741 9.407 11.104 1.00 16.24 N ANISOU 270 N SER A 38 2044 2068 2057 -82 30 -29 N ATOM 271 CA SER A 38 47.450 10.109 9.850 1.00 16.68 C ANISOU 271 CA SER A 38 2087 2159 2091 -55 5 -96 C ATOM 272 C SER A 38 46.618 11.367 10.078 1.00 16.63 C ANISOU 272 C SER A 38 2047 2120 2150 -62 -17 -28 C ATOM 273 O SER A 38 46.589 12.260 9.220 1.00 16.67 O ANISOU 273 O SER A 38 2090 2194 2048 -54 11 -78 O ATOM 274 CB SER A 38 46.689 9.193 8.893 1.00 17.67 C ANISOU 274 CB SER A 38 2199 2290 2223 -60 35 -107 C ATOM 275 OG SER A 38 45.461 8.790 9.456 1.00 17.18 O ANISOU 275 OG SER A 38 2153 2158 2215 -100 -81 -137 O ATOM 276 N VAL A 39 45.953 11.449 11.235 1.00 15.84 N ANISOU 276 N VAL A 39 2010 2008 1997 -54 -62 -64 N ATOM 277 CA VAL A 39 44.905 12.472 11.414 1.00 16.18 C ANISOU 277 CA VAL A 39 2056 2081 2009 -53 -20 -58 C ATOM 278 C VAL A 39 44.995 13.288 12.700 1.00 16.19 C ANISOU 278 C VAL A 39 2057 2006 2086 -61 -17 -42 C ATOM 279 O VAL A 39 44.202 14.213 12.900 1.00 16.16 O ANISOU 279 O VAL A 39 2069 1966 2104 -120 -4 -107 O ATOM 280 CB VAL A 39 43.471 11.895 11.224 1.00 15.96 C ANISOU 280 CB VAL A 39 2026 2008 2028 -9 -12 -40 C ATOM 281 CG1 VAL A 39 43.260 11.485 9.779 1.00 17.03 C ANISOU 281 CG1 VAL A 39 2120 2289 2058 -47 -96 2 C ATOM 282 CG2 VAL A 39 43.188 10.721 12.190 1.00 15.73 C ANISOU 282 CG2 VAL A 39 1890 2107 1977 -22 -48 46 C ATOM 283 N ILE A 40 45.970 12.954 13.545 1.00 15.44 N ANISOU 283 N ILE A 40 1976 1897 1993 -54 -29 -11 N ATOM 284 CA ILE A 40 46.198 13.700 14.776 1.00 15.46 C ANISOU 284 CA ILE A 40 1978 1942 1950 -12 -22 23 C ATOM 285 C ILE A 40 47.605 14.276 14.843 1.00 15.80 C ANISOU 285 C ILE A 40 2034 1985 1982 -33 -35 -22 C ATOM 286 O ILE A 40 48.590 13.569 14.604 1.00 14.32 O ANISOU 286 O ILE A 40 1928 1768 1744 -72 -69 -140 O ATOM 287 CB ILE A 40 45.862 12.854 16.025 1.00 15.40 C ANISOU 287 CB ILE A 40 1983 1927 1941 3 -19 37 C ATOM 288 CG1 ILE A 40 44.383 12.418 15.947 1.00 16.00 C ANISOU 288 CG1 ILE A 40 1993 2082 2003 -46 33 106 C ATOM 289 CG2 ILE A 40 46.267 13.615 17.356 1.00 14.02 C ANISOU 289 CG2 ILE A 40 1741 1732 1853 -8 -7 87 C ATOM 290 CD1 ILE A 40 43.872 11.515 17.069 1.00 15.47 C ANISOU 290 CD1 ILE A 40 2009 1922 1947 57 3 145 C ATOM 291 N GLU A 41 47.676 15.562 15.213 1.00 16.51 N ANISOU 291 N GLU A 41 2145 2042 2086 -1 -61 -12 N ATOM 292 CA GLU A 41 48.921 16.300 15.310 1.00 17.67 C ANISOU 292 CA GLU A 41 2249 2228 2234 -97 -49 -11 C ATOM 293 C GLU A 41 49.216 16.654 16.776 1.00 17.64 C ANISOU 293 C GLU A 41 2261 2239 2201 -59 -42 -41 C ATOM 294 O GLU A 41 48.291 16.891 17.553 1.00 17.63 O ANISOU 294 O GLU A 41 2173 2280 2242 -98 -89 -90 O ATOM 295 CB GLU A 41 48.819 17.596 14.487 1.00 18.46 C ANISOU 295 CB GLU A 41 2366 2379 2267 -75 -74 -19 C ATOM 296 CG GLU A 41 50.130 18.404 14.419 1.00 19.36 C ANISOU 296 CG GLU A 41 2442 2487 2425 -188 -10 135 C ATOM 297 CD GLU A 41 50.068 19.683 13.560 1.00 21.18 C ANISOU 297 CD GLU A 41 2703 2586 2758 -56 -57 -13 C ATOM 298 OE1 GLU A 41 48.992 20.052 13.037 1.00 21.02 O ANISOU 298 OE1 GLU A 41 2712 2314 2960 -100 -82 177 O ATOM 299 OE2 GLU A 41 51.140 20.319 13.407 1.00 21.92 O ANISOU 299 OE2 GLU A 41 2847 2633 2845 -273 47 148 O ATOM 300 N ASN A 42 50.497 16.672 17.145 1.00 17.31 N ANISOU 300 N ASN A 42 2214 2199 2162 -33 -40 -63 N ATOM 301 CA ASN A 42 50.932 17.264 18.424 1.00 17.51 C ANISOU 301 CA ASN A 42 2251 2208 2193 -11 -33 -13 C ATOM 302 C ASN A 42 51.223 18.753 18.179 1.00 17.81 C ANISOU 302 C ASN A 42 2300 2256 2210 -20 -24 -7 C ATOM 303 O ASN A 42 52.190 19.103 17.497 1.00 17.12 O ANISOU 303 O ASN A 42 2226 2198 2080 -42 0 14 O ATOM 304 CB ASN A 42 52.176 16.543 18.980 1.00 17.20 C ANISOU 304 CB ASN A 42 2219 2169 2145 -12 -51 -18 C ATOM 305 CG ASN A 42 52.775 17.238 20.198 1.00 17.71 C ANISOU 305 CG ASN A 42 2269 2248 2210 21 10 51 C ATOM 306 OD1 ASN A 42 52.132 18.082 20.815 1.00 17.97 O ANISOU 306 OD1 ASN A 42 2414 2238 2175 32 -80 -86 O ATOM 307 ND2 ASN A 42 54.006 16.859 20.566 1.00 16.76 N ANISOU 307 ND2 ASN A 42 2098 2201 2066 34 11 5 N ATOM 308 N VAL A 43 50.367 19.614 18.716 1.00 18.02 N ANISOU 308 N VAL A 43 2342 2256 2248 -11 -26 52 N ATOM 309 CA VAL A 43 50.583 21.045 18.647 1.00 18.92 C ANISOU 309 CA VAL A 43 2506 2324 2356 11 -45 -1 C ATOM 310 C VAL A 43 50.975 21.561 20.037 1.00 18.25 C ANISOU 310 C VAL A 43 2408 2215 2311 -12 -45 44 C ATOM 311 O VAL A 43 50.134 21.703 20.934 1.00 18.44 O ANISOU 311 O VAL A 43 2443 2144 2417 14 -62 -5 O ATOM 312 CB VAL A 43 49.366 21.795 18.037 1.00 19.00 C ANISOU 312 CB VAL A 43 2497 2319 2402 0 -99 -50 C ATOM 313 CG1 VAL A 43 49.660 23.286 17.897 1.00 20.39 C ANISOU 313 CG1 VAL A 43 2753 2494 2499 -24 -57 84 C ATOM 314 CG2 VAL A 43 48.991 21.205 16.649 1.00 19.70 C ANISOU 314 CG2 VAL A 43 2763 2437 2284 157 19 52 C ATOM 315 N ASP A 44 52.272 21.788 20.216 1.00 18.23 N ANISOU 315 N ASP A 44 2388 2256 2282 -9 -2 73 N ATOM 316 CA ASP A 44 52.809 22.357 21.465 1.00 18.04 C ANISOU 316 CA ASP A 44 2337 2275 2242 -36 -6 71 C ATOM 317 C ASP A 44 52.363 21.546 22.700 1.00 17.87 C ANISOU 317 C ASP A 44 2306 2244 2238 -22 -9 63 C ATOM 318 O ASP A 44 52.072 22.114 23.754 1.00 16.55 O ANISOU 318 O ASP A 44 2214 1952 2120 -39 4 95 O ATOM 319 CB ASP A 44 52.388 23.820 21.604 1.00 18.92 C ANISOU 319 CB ASP A 44 2452 2417 2317 -28 -56 55 C ATOM 320 CG ASP A 44 53.228 24.580 22.627 1.00 20.53 C ANISOU 320 CG ASP A 44 2641 2644 2514 -75 -68 50 C ATOM 321 OD1 ASP A 44 54.417 24.249 22.790 1.00 20.61 O ANISOU 321 OD1 ASP A 44 2568 2725 2535 -5 -85 198 O ATOM 322 OD2 ASP A 44 52.692 25.506 23.259 1.00 21.77 O ANISOU 322 OD2 ASP A 44 2762 2801 2708 95 -169 -1 O ATOM 323 N GLY A 45 52.300 20.220 22.541 1.00 17.72 N ANISOU 323 N GLY A 45 2258 2202 2273 -30 7 61 N ATOM 324 CA GLY A 45 51.946 19.319 23.642 1.00 18.08 C ANISOU 324 CA GLY A 45 2328 2265 2275 -26 36 22 C ATOM 325 C GLY A 45 50.504 18.835 23.653 1.00 18.57 C ANISOU 325 C GLY A 45 2409 2307 2338 -39 31 -24 C ATOM 326 O GLY A 45 50.175 17.900 24.396 1.00 18.85 O ANISOU 326 O GLY A 45 2476 2337 2347 -90 5 6 O ATOM 327 N SER A 46 49.638 19.485 22.875 1.00 18.46 N ANISOU 327 N SER A 46 2388 2368 2256 -74 5 -31 N ATOM 328 CA SER A 46 48.207 19.153 22.842 1.00 19.39 C ANISOU 328 CA SER A 46 2479 2479 2407 -4 -3 -67 C ATOM 329 C SER A 46 47.868 18.383 21.568 1.00 18.77 C ANISOU 329 C SER A 46 2366 2408 2357 12 -19 -34 C ATOM 330 O SER A 46 48.303 18.754 20.484 1.00 18.77 O ANISOU 330 O SER A 46 2370 2428 2332 41 -32 -67 O ATOM 331 CB SER A 46 47.350 20.423 22.926 1.00 19.84 C ANISOU 331 CB SER A 46 2521 2586 2430 23 11 -100 C ATOM 332 OG SER A 46 47.482 21.047 24.203 1.00 21.81 O ANISOU 332 OG SER A 46 2669 2821 2794 -68 -14 -208 O ATOM 333 N LEU A 47 47.111 17.304 21.706 1.00 18.15 N ANISOU 333 N LEU A 47 2272 2301 2324 80 -31 -34 N ATOM 334 CA LEU A 47 46.630 16.565 20.551 1.00 18.07 C ANISOU 334 CA LEU A 47 2298 2295 2270 54 -15 -15 C ATOM 335 C LEU A 47 45.510 17.338 19.840 1.00 18.37 C ANISOU 335 C LEU A 47 2330 2339 2311 29 -48 4 C ATOM 336 O LEU A 47 44.567 17.812 20.480 1.00 18.07 O ANISOU 336 O LEU A 47 2381 2306 2178 43 -75 -25 O ATOM 337 CB LEU A 47 46.137 15.181 20.973 1.00 17.68 C ANISOU 337 CB LEU A 47 2281 2218 2218 66 -26 10 C ATOM 338 CG LEU A 47 47.188 14.269 21.625 1.00 16.90 C ANISOU 338 CG LEU A 47 2241 2042 2138 39 34 -22 C ATOM 339 CD1 LEU A 47 46.468 13.072 22.301 1.00 15.75 C ANISOU 339 CD1 LEU A 47 2091 1951 1941 -14 -39 12 C ATOM 340 CD2 LEU A 47 48.241 13.819 20.594 1.00 17.25 C ANISOU 340 CD2 LEU A 47 2110 2178 2265 -70 8 16 C ATOM 341 N LYS A 48 45.611 17.445 18.519 1.00 18.76 N ANISOU 341 N LYS A 48 2408 2358 2363 -22 -55 -6 N ATOM 342 CA LYS A 48 44.666 18.241 17.731 1.00 19.35 C ANISOU 342 CA LYS A 48 2478 2448 2424 -37 -72 -10 C ATOM 343 C LYS A 48 44.377 17.518 16.419 1.00 19.47 C ANISOU 343 C LYS A 48 2504 2433 2459 -48 -58 -8 C ATOM 344 O LYS A 48 45.231 16.776 15.921 1.00 19.14 O ANISOU 344 O LYS A 48 2410 2476 2384 -34 -165 -59 O ATOM 345 CB LYS A 48 45.257 19.648 17.421 1.00 19.98 C ANISOU 345 CB LYS A 48 2580 2449 2561 -21 -81 -28 C ATOM 346 CG LYS A 48 45.417 20.593 18.634 1.00 22.14 C ANISOU 346 CG LYS A 48 2851 2866 2693 -38 -108 -59 C ATOM 347 CD LYS A 48 44.061 21.066 19.128 1.00 26.64 C ANISOU 347 CD LYS A 48 3306 3396 3418 48 85 -83 C ATOM 348 CE LYS A 48 44.103 21.542 20.580 1.00 29.47 C ANISOU 348 CE LYS A 48 3713 3917 3568 20 32 -46 C ATOM 349 NZ LYS A 48 42.722 21.594 21.165 1.00 29.79 N ANISOU 349 NZ LYS A 48 3805 3670 3844 13 154 7 N ATOM 350 N TRP A 49 43.185 17.746 15.865 1.00 19.14 N ANISOU 350 N TRP A 49 2429 2414 2429 -31 -58 2 N ATOM 351 CA TRP A 49 42.853 17.306 14.506 1.00 19.87 C ANISOU 351 CA TRP A 49 2518 2517 2512 -25 0 7 C ATOM 352 C TRP A 49 43.489 18.258 13.464 1.00 20.43 C ANISOU 352 C TRP A 49 2584 2568 2608 18 4 13 C ATOM 353 O TRP A 49 44.177 19.211 13.832 1.00 20.04 O ANISOU 353 O TRP A 49 2612 2410 2590 70 60 -3 O ATOM 354 CB TRP A 49 41.324 17.235 14.318 1.00 19.63 C ANISOU 354 CB TRP A 49 2496 2509 2452 -14 -30 -2 C ATOM 355 CG TRP A 49 40.588 16.346 15.328 1.00 19.71 C ANISOU 355 CG TRP A 49 2424 2494 2569 -44 -38 2 C ATOM 356 CD1 TRP A 49 39.829 16.763 16.385 1.00 19.79 C ANISOU 356 CD1 TRP A 49 2525 2466 2525 -2 -44 -34 C ATOM 357 CD2 TRP A 49 40.544 14.906 15.352 1.00 19.54 C ANISOU 357 CD2 TRP A 49 2450 2505 2468 10 -110 3 C ATOM 358 NE1 TRP A 49 39.301 15.681 17.061 1.00 20.74 N ANISOU 358 NE1 TRP A 49 2598 2666 2614 71 -99 -71 N ATOM 359 CE2 TRP A 49 39.726 14.528 16.455 1.00 19.38 C ANISOU 359 CE2 TRP A 49 2404 2449 2511 -1 -95 -37 C ATOM 360 CE3 TRP A 49 41.107 13.905 14.555 1.00 18.36 C ANISOU 360 CE3 TRP A 49 2281 2417 2276 4 -104 35 C ATOM 361 CZ2 TRP A 49 39.465 13.185 16.781 1.00 19.69 C ANISOU 361 CZ2 TRP A 49 2448 2585 2446 34 -46 -16 C ATOM 362 CZ3 TRP A 49 40.840 12.562 14.877 1.00 20.02 C ANISOU 362 CZ3 TRP A 49 2523 2525 2558 0 -33 -12 C ATOM 363 CH2 TRP A 49 40.034 12.221 15.984 1.00 19.74 C ANISOU 363 CH2 TRP A 49 2514 2452 2533 17 -34 -8 C ATOM 364 N GLN A 50 43.270 17.971 12.175 1.00 20.84 N ANISOU 364 N GLN A 50 2672 2598 2646 64 -10 46 N ATOM 365 CA GLN A 50 43.799 18.780 11.053 1.00 21.91 C ANISOU 365 CA GLN A 50 2775 2771 2777 59 -7 47 C ATOM 366 C GLN A 50 45.318 18.696 10.890 1.00 21.15 C ANISOU 366 C GLN A 50 2724 2622 2689 -1 -23 35 C ATOM 367 O GLN A 50 45.945 19.597 10.333 1.00 21.83 O ANISOU 367 O GLN A 50 2804 2736 2752 18 -76 84 O ATOM 368 CB GLN A 50 43.329 20.240 11.149 1.00 23.00 C ANISOU 368 CB GLN A 50 3003 2838 2896 55 -18 64 C ATOM 369 CG GLN A 50 41.837 20.369 11.542 1.00 27.75 C ANISOU 369 CG GLN A 50 3362 3486 3695 79 56 66 C ATOM 370 CD GLN A 50 40.882 20.078 10.403 1.00 35.44 C ANISOU 370 CD GLN A 50 4396 4749 4318 35 -21 -123 C ATOM 371 OE1 GLN A 50 40.375 18.959 10.269 1.00 37.20 O ANISOU 371 OE1 GLN A 50 4773 4386 4975 -187 -94 3 O ATOM 372 NE2 GLN A 50 40.613 21.090 9.583 1.00 34.88 N ANISOU 372 NE2 GLN A 50 4590 4260 4401 128 -46 207 N ATOM 373 N GLY A 51 45.901 17.595 11.348 1.00 19.70 N ANISOU 373 N GLY A 51 2518 2491 2475 -2 -69 91 N ATOM 374 CA GLY A 51 47.302 17.317 11.074 1.00 18.22 C ANISOU 374 CA GLY A 51 2366 2244 2311 -13 -68 5 C ATOM 375 C GLY A 51 47.670 15.872 11.272 1.00 17.94 C ANISOU 375 C GLY A 51 2277 2251 2285 2 -17 -22 C ATOM 376 O GLY A 51 46.796 15.011 11.293 1.00 17.30 O ANISOU 376 O GLY A 51 2163 2137 2272 61 -53 -30 O ATOM 377 N SER A 52 48.969 15.607 11.407 1.00 17.33 N ANISOU 377 N SER A 52 2240 2162 2183 51 -81 -5 N ATOM 378 CA SER A 52 49.468 14.234 11.495 1.00 17.38 C ANISOU 378 CA SER A 52 2229 2211 2162 8 -15 -13 C ATOM 379 C SER A 52 50.726 14.156 12.364 1.00 16.63 C ANISOU 379 C SER A 52 2136 2137 2046 40 18 1 C ATOM 380 O SER A 52 51.228 15.184 12.862 1.00 16.29 O ANISOU 380 O SER A 52 2030 2082 2075 45 -51 -3 O ATOM 381 CB SER A 52 49.775 13.661 10.091 1.00 17.77 C ANISOU 381 CB SER A 52 2311 2256 2186 18 -16 -27 C ATOM 382 OG SER A 52 48.778 13.994 9.131 1.00 18.75 O ANISOU 382 OG SER A 52 2436 2353 2332 -150 -1 84 O ATOM 383 N ASN A 53 51.218 12.930 12.543 1.00 15.57 N ANISOU 383 N ASN A 53 2029 2024 1862 -6 73 31 N ATOM 384 CA ASN A 53 52.571 12.684 13.042 1.00 15.94 C ANISOU 384 CA ASN A 53 2063 2062 1932 0 27 10 C ATOM 385 C ASN A 53 52.797 12.875 14.546 1.00 15.64 C ANISOU 385 C ASN A 53 2087 1929 1924 5 25 35 C ATOM 386 O ASN A 53 53.940 12.972 14.972 1.00 15.54 O ANISOU 386 O ASN A 53 2159 1937 1807 -58 -5 30 O ATOM 387 CB ASN A 53 53.610 13.533 12.272 1.00 15.04 C ANISOU 387 CB ASN A 53 1909 1869 1934 -28 33 60 C ATOM 388 CG ASN A 53 53.549 13.317 10.785 1.00 16.08 C ANISOU 388 CG ASN A 53 2020 2025 2061 -22 -15 5 C ATOM 389 OD1 ASN A 53 53.529 14.288 10.001 1.00 19.17 O ANISOU 389 OD1 ASN A 53 2457 2213 2612 -88 -76 73 O ATOM 390 ND2 ASN A 53 53.522 12.044 10.366 1.00 13.02 N ANISOU 390 ND2 ASN A 53 1617 1680 1650 10 -24 138 N ATOM 391 N PHE A 54 51.729 12.870 15.337 1.00 16.27 N ANISOU 391 N PHE A 54 2164 1966 2049 32 53 -5 N ATOM 392 CA PHE A 54 51.858 13.067 16.791 1.00 16.16 C ANISOU 392 CA PHE A 54 2046 2028 2065 0 31 -7 C ATOM 393 C PHE A 54 52.727 12.001 17.478 1.00 16.82 C ANISOU 393 C PHE A 54 2122 2096 2173 -5 31 -29 C ATOM 394 O PHE A 54 53.347 12.270 18.512 1.00 14.64 O ANISOU 394 O PHE A 54 1847 1760 1954 65 -11 -4 O ATOM 395 CB PHE A 54 50.477 13.161 17.455 1.00 17.25 C ANISOU 395 CB PHE A 54 2134 2173 2247 22 14 -69 C ATOM 396 CG PHE A 54 49.815 11.821 17.714 1.00 16.23 C ANISOU 396 CG PHE A 54 1990 2045 2132 12 55 61 C ATOM 397 CD1 PHE A 54 49.940 11.190 18.973 1.00 17.98 C ANISOU 397 CD1 PHE A 54 2163 2228 2440 61 70 64 C ATOM 398 CD2 PHE A 54 49.066 11.193 16.720 1.00 14.85 C ANISOU 398 CD2 PHE A 54 1810 1791 2041 249 104 39 C ATOM 399 CE1 PHE A 54 49.326 9.951 19.228 1.00 17.87 C ANISOU 399 CE1 PHE A 54 2139 2371 2280 112 96 27 C ATOM 400 CE2 PHE A 54 48.435 9.954 16.970 1.00 16.18 C ANISOU 400 CE2 PHE A 54 1979 1983 2183 88 90 54 C ATOM 401 CZ PHE A 54 48.580 9.332 18.231 1.00 16.78 C ANISOU 401 CZ PHE A 54 1891 2239 2242 -2 117 -60 C ATOM 402 N ILE A 55 52.796 10.795 16.905 1.00 17.08 N ANISOU 402 N ILE A 55 2086 2176 2227 -8 42 -90 N ATOM 403 CA ILE A 55 53.546 9.724 17.570 1.00 17.99 C ANISOU 403 CA ILE A 55 2312 2245 2278 -7 23 -53 C ATOM 404 C ILE A 55 55.037 10.019 17.659 1.00 17.94 C ANISOU 404 C ILE A 55 2291 2272 2251 0 16 -84 C ATOM 405 O ILE A 55 55.725 9.460 18.507 1.00 18.63 O ANISOU 405 O ILE A 55 2356 2416 2304 -24 0 -8 O ATOM 406 CB ILE A 55 53.366 8.340 16.910 1.00 18.18 C ANISOU 406 CB ILE A 55 2298 2347 2260 -19 -13 -77 C ATOM 407 CG1 ILE A 55 54.097 8.270 15.551 1.00 17.90 C ANISOU 407 CG1 ILE A 55 2404 2230 2167 60 -6 -119 C ATOM 408 CG2 ILE A 55 51.912 8.006 16.831 1.00 18.88 C ANISOU 408 CG2 ILE A 55 2406 2301 2466 -25 56 -65 C ATOM 409 CD1 ILE A 55 53.883 6.936 14.790 1.00 20.43 C ANISOU 409 CD1 ILE A 55 2640 2559 2563 33 -38 -97 C ATOM 410 N GLU A 56 55.535 10.871 16.767 1.00 17.28 N ANISOU 410 N GLU A 56 2305 2150 2108 -17 0 -112 N ATOM 411 CA GLU A 56 56.965 11.175 16.725 1.00 17.65 C ANISOU 411 CA GLU A 56 2333 2241 2131 -13 47 -94 C ATOM 412 C GLU A 56 57.420 11.913 17.977 1.00 17.85 C ANISOU 412 C GLU A 56 2316 2202 2263 -41 -12 -86 C ATOM 413 O GLU A 56 58.588 11.877 18.315 1.00 17.87 O ANISOU 413 O GLU A 56 2275 2226 2286 25 44 -162 O ATOM 414 CB GLU A 56 57.280 12.028 15.497 1.00 17.94 C ANISOU 414 CB GLU A 56 2395 2197 2223 21 26 -79 C ATOM 415 CG GLU A 56 57.104 11.263 14.226 1.00 18.20 C ANISOU 415 CG GLU A 56 2255 2463 2195 -27 -30 -23 C ATOM 416 CD GLU A 56 57.390 12.107 13.012 1.00 21.72 C ANISOU 416 CD GLU A 56 2931 2744 2574 -59 3 95 C ATOM 417 OE1 GLU A 56 57.789 13.289 13.159 1.00 22.78 O ANISOU 417 OE1 GLU A 56 2983 2859 2812 -289 -39 65 O ATOM 418 OE2 GLU A 56 57.188 11.600 11.910 1.00 20.95 O ANISOU 418 OE2 GLU A 56 2896 2487 2575 -144 60 -228 O ATOM 419 N THR A 57 56.484 12.581 18.651 1.00 17.53 N ANISOU 419 N THR A 57 2263 2187 2210 -30 50 -77 N ATOM 420 CA THR A 57 56.828 13.450 19.789 1.00 17.87 C ANISOU 420 CA THR A 57 2351 2207 2230 -46 10 -30 C ATOM 421 C THR A 57 55.945 13.199 21.017 1.00 18.07 C ANISOU 421 C THR A 57 2345 2254 2265 -9 -12 -63 C ATOM 422 O THR A 57 55.887 14.022 21.930 1.00 18.53 O ANISOU 422 O THR A 57 2460 2269 2309 -74 40 -20 O ATOM 423 CB THR A 57 56.740 14.935 19.390 1.00 18.83 C ANISOU 423 CB THR A 57 2428 2401 2325 0 1 -53 C ATOM 424 OG1 THR A 57 55.449 15.200 18.842 1.00 20.35 O ANISOU 424 OG1 THR A 57 2657 2635 2437 95 -18 93 O ATOM 425 CG2 THR A 57 57.828 15.298 18.377 1.00 17.91 C ANISOU 425 CG2 THR A 57 2398 2234 2174 -67 28 -3 C ATOM 426 N CYS A 58 55.261 12.058 21.039 1.00 17.15 N ANISOU 426 N CYS A 58 2263 2096 2156 -16 -13 -9 N ATOM 427 CA CYS A 58 54.400 11.697 22.149 1.00 17.84 C ANISOU 427 CA CYS A 58 2345 2175 2256 12 10 -31 C ATOM 428 C CYS A 58 54.768 10.290 22.623 1.00 18.04 C ANISOU 428 C CYS A 58 2387 2217 2249 24 23 2 C ATOM 429 O CYS A 58 55.514 9.567 21.951 1.00 18.50 O ANISOU 429 O CYS A 58 2484 2238 2304 84 116 7 O ATOM 430 CB CYS A 58 52.901 11.747 21.759 1.00 17.87 C ANISOU 430 CB CYS A 58 2369 2186 2233 -13 -22 -47 C ATOM 431 SG CYS A 58 52.256 13.327 21.138 1.00 17.86 S ANISOU 431 SG CYS A 58 2394 2249 2140 -96 -6 -65 S ATOM 432 N ARG A 59 54.242 9.898 23.773 1.00 17.64 N ANISOU 432 N ARG A 59 2353 2166 2182 -3 45 -47 N ATOM 433 CA ARG A 59 54.532 8.580 24.322 1.00 18.25 C ANISOU 433 CA ARG A 59 2382 2305 2247 -24 17 27 C ATOM 434 C ARG A 59 53.332 8.126 25.138 1.00 18.51 C ANISOU 434 C ARG A 59 2380 2342 2311 -31 12 43 C ATOM 435 O ARG A 59 52.449 8.930 25.447 1.00 17.68 O ANISOU 435 O ARG A 59 2355 2192 2168 -37 83 79 O ATOM 436 CB ARG A 59 55.792 8.634 25.206 1.00 17.76 C ANISOU 436 CB ARG A 59 2286 2215 2246 -50 8 36 C ATOM 437 CG ARG A 59 55.566 9.432 26.491 1.00 17.89 C ANISOU 437 CG ARG A 59 2299 2241 2257 -5 -70 13 C ATOM 438 CD ARG A 59 56.829 9.711 27.292 1.00 19.00 C ANISOU 438 CD ARG A 59 2483 2377 2359 -76 -63 2 C ATOM 439 NE ARG A 59 56.489 10.547 28.447 1.00 19.57 N ANISOU 439 NE ARG A 59 2570 2419 2443 111 -34 -13 N ATOM 440 CZ ARG A 59 57.369 11.199 29.208 1.00 20.15 C ANISOU 440 CZ ARG A 59 2549 2528 2577 -12 -14 -86 C ATOM 441 NH1 ARG A 59 58.671 11.127 28.956 1.00 20.98 N ANISOU 441 NH1 ARG A 59 2654 2549 2766 81 -13 -57 N ATOM 442 NH2 ARG A 59 56.940 11.936 30.228 1.00 19.93 N ANISOU 442 NH2 ARG A 59 2559 2541 2470 54 -107 -88 N ATOM 443 N ASN A 60 53.316 6.837 25.485 1.00 18.72 N ANISOU 443 N ASN A 60 2424 2304 2382 -8 9 55 N ATOM 444 CA ASN A 60 52.370 6.298 26.476 1.00 19.27 C ANISOU 444 CA ASN A 60 2399 2446 2473 -18 -5 14 C ATOM 445 C ASN A 60 50.909 6.550 26.077 1.00 19.06 C ANISOU 445 C ASN A 60 2396 2422 2423 21 -18 27 C ATOM 446 O ASN A 60 50.091 7.021 26.883 1.00 18.85 O ANISOU 446 O ASN A 60 2321 2441 2398 -8 -8 40 O ATOM 447 CB ASN A 60 52.691 6.821 27.885 1.00 19.82 C ANISOU 447 CB ASN A 60 2503 2509 2519 -15 -29 30 C ATOM 448 CG ASN A 60 54.098 6.417 28.359 1.00 22.18 C ANISOU 448 CG ASN A 60 2776 2827 2824 21 -24 40 C ATOM 449 OD1 ASN A 60 54.579 5.332 28.041 1.00 23.98 O ANISOU 449 OD1 ASN A 60 3069 2838 3203 54 -170 42 O ATOM 450 ND2 ASN A 60 54.767 7.304 29.104 1.00 23.59 N ANISOU 450 ND2 ASN A 60 3052 2910 2998 -137 -116 36 N ATOM 451 N THR A 61 50.610 6.243 24.814 1.00 18.84 N ANISOU 451 N THR A 61 2323 2418 2417 -3 -68 14 N ATOM 452 CA THR A 61 49.240 6.355 24.299 1.00 18.97 C ANISOU 452 CA THR A 61 2396 2438 2372 5 -67 -8 C ATOM 453 C THR A 61 48.351 5.342 24.983 1.00 18.71 C ANISOU 453 C THR A 61 2384 2408 2315 -5 -75 -40 C ATOM 454 O THR A 61 48.776 4.211 25.280 1.00 17.91 O ANISOU 454 O THR A 61 2261 2212 2330 38 -99 -49 O ATOM 455 CB THR A 61 49.138 6.141 22.766 1.00 18.48 C ANISOU 455 CB THR A 61 2313 2434 2272 19 -73 2 C ATOM 456 OG1 THR A 61 49.729 4.890 22.409 1.00 18.18 O ANISOU 456 OG1 THR A 61 2536 2305 2064 -113 11 -23 O ATOM 457 CG2 THR A 61 49.821 7.272 21.994 1.00 18.72 C ANISOU 457 CG2 THR A 61 2334 2380 2396 -118 -58 -13 C ATOM 458 N GLN A 62 47.117 5.755 25.241 1.00 19.02 N ANISOU 458 N GLN A 62 2441 2421 2364 41 -58 -97 N ATOM 459 CA GLN A 62 46.136 4.922 25.924 1.00 20.01 C ANISOU 459 CA GLN A 62 2562 2548 2490 1 -46 -34 C ATOM 460 C GLN A 62 44.745 5.329 25.469 1.00 19.19 C ANISOU 460 C GLN A 62 2435 2478 2376 -34 -16 -29 C ATOM 461 O GLN A 62 44.499 6.493 25.106 1.00 18.13 O ANISOU 461 O GLN A 62 2224 2353 2310 -63 -2 -19 O ATOM 462 CB GLN A 62 46.188 5.098 27.454 1.00 21.19 C ANISOU 462 CB GLN A 62 2681 2749 2619 -18 -24 23 C ATOM 463 CG GLN A 62 47.483 4.678 28.174 1.00 22.61 C ANISOU 463 CG GLN A 62 2917 3035 2637 67 -46 -59 C ATOM 464 CD GLN A 62 47.429 5.045 29.655 1.00 26.71 C ANISOU 464 CD GLN A 62 3266 3682 3200 -138 -54 -47 C ATOM 465 OE1 GLN A 62 47.142 6.194 30.010 1.00 28.83 O ANISOU 465 OE1 GLN A 62 3888 3340 3723 243 106 -180 O ATOM 466 NE2 GLN A 62 47.676 4.058 30.527 1.00 27.83 N ANISOU 466 NE2 GLN A 62 3761 3347 3465 157 -170 372 N ATOM 467 N LEU A 63 43.831 4.369 25.503 1.00 18.26 N ANISOU 467 N LEU A 63 2322 2356 2260 -44 -7 13 N ATOM 468 CA LEU A 63 42.422 4.682 25.373 1.00 18.47 C ANISOU 468 CA LEU A 63 2333 2316 2367 -10 -23 -38 C ATOM 469 C LEU A 63 41.824 4.936 26.769 1.00 18.92 C ANISOU 469 C LEU A 63 2383 2390 2413 -3 -9 -24 C ATOM 470 O LEU A 63 41.976 4.118 27.692 1.00 19.09 O ANISOU 470 O LEU A 63 2407 2436 2409 61 -19 -7 O ATOM 471 CB LEU A 63 41.679 3.541 24.663 1.00 18.23 C ANISOU 471 CB LEU A 63 2279 2264 2384 -27 -59 -65 C ATOM 472 CG LEU A 63 40.205 3.806 24.353 1.00 17.86 C ANISOU 472 CG LEU A 63 2235 2239 2312 -70 -18 -65 C ATOM 473 CD1 LEU A 63 40.018 4.818 23.222 1.00 17.60 C ANISOU 473 CD1 LEU A 63 2183 2155 2347 -88 1 -37 C ATOM 474 CD2 LEU A 63 39.511 2.488 24.015 1.00 17.30 C ANISOU 474 CD2 LEU A 63 2180 2134 2257 -250 12 2 C ATOM 475 N ALA A 64 41.151 6.073 26.921 1.00 18.76 N ANISOU 475 N ALA A 64 2363 2370 2393 14 6 -21 N ATOM 476 CA ALA A 64 40.511 6.407 28.187 1.00 19.43 C ANISOU 476 CA ALA A 64 2440 2438 2501 36 -22 -49 C ATOM 477 C ALA A 64 38.995 6.371 27.972 1.00 19.52 C ANISOU 477 C ALA A 64 2483 2460 2473 -17 -5 -62 C ATOM 478 O ALA A 64 38.482 7.016 27.052 1.00 19.04 O ANISOU 478 O ALA A 64 2363 2462 2408 29 -9 0 O ATOM 479 CB ALA A 64 40.984 7.785 28.658 1.00 19.51 C ANISOU 479 CB ALA A 64 2409 2535 2469 -30 -70 -72 C ATOM 480 N GLY A 65 38.285 5.598 28.794 1.00 19.38 N ANISOU 480 N GLY A 65 2517 2465 2379 -27 -21 -92 N ATOM 481 CA GLY A 65 36.862 5.364 28.569 1.00 19.11 C ANISOU 481 CA GLY A 65 2497 2353 2409 -5 -13 -93 C ATOM 482 C GLY A 65 36.659 4.701 27.211 1.00 19.12 C ANISOU 482 C GLY A 65 2487 2356 2419 -21 13 -53 C ATOM 483 O GLY A 65 37.497 3.921 26.764 1.00 18.87 O ANISOU 483 O GLY A 65 2392 2252 2525 14 -82 -99 O ATOM 484 N SER A 66 35.557 5.029 26.550 1.00 18.65 N ANISOU 484 N SER A 66 2398 2283 2404 15 -7 -44 N ATOM 485 CA SER A 66 35.233 4.441 25.252 1.00 19.88 C ANISOU 485 CA SER A 66 2516 2451 2584 -10 -10 33 C ATOM 486 C SER A 66 35.875 5.088 24.031 1.00 19.60 C ANISOU 486 C SER A 66 2476 2435 2537 -19 -18 25 C ATOM 487 O SER A 66 36.008 4.436 22.995 1.00 19.39 O ANISOU 487 O SER A 66 2387 2426 2554 -93 -18 30 O ATOM 488 CB SER A 66 33.726 4.382 25.065 1.00 20.44 C ANISOU 488 CB SER A 66 2569 2580 2615 -83 -37 13 C ATOM 489 OG SER A 66 33.239 3.172 25.611 1.00 23.14 O ANISOU 489 OG SER A 66 2912 2891 2988 37 23 212 O ATOM 490 N SER A 67 36.258 6.365 24.129 1.00 19.41 N ANISOU 490 N SER A 67 2431 2400 2542 -83 -52 27 N ATOM 491 CA SER A 67 36.639 7.094 22.901 1.00 19.03 C ANISOU 491 CA SER A 67 2376 2382 2472 -47 6 14 C ATOM 492 C SER A 67 37.740 8.141 23.024 1.00 19.36 C ANISOU 492 C SER A 67 2458 2399 2497 -38 -10 18 C ATOM 493 O SER A 67 38.007 8.862 22.064 1.00 18.95 O ANISOU 493 O SER A 67 2425 2392 2381 -63 32 42 O ATOM 494 CB SER A 67 35.407 7.767 22.286 1.00 18.97 C ANISOU 494 CB SER A 67 2376 2328 2501 -78 -21 10 C ATOM 495 OG SER A 67 34.933 8.794 23.150 1.00 18.99 O ANISOU 495 OG SER A 67 2146 2502 2566 -18 21 61 O ATOM 496 N GLU A 68 38.363 8.248 24.187 1.00 19.46 N ANISOU 496 N GLU A 68 2488 2374 2533 8 -1 33 N ATOM 497 CA GLU A 68 39.364 9.281 24.383 1.00 20.52 C ANISOU 497 CA GLU A 68 2549 2594 2652 -1 -37 30 C ATOM 498 C GLU A 68 40.769 8.736 24.115 1.00 19.73 C ANISOU 498 C GLU A 68 2464 2491 2541 13 -24 27 C ATOM 499 O GLU A 68 41.169 7.732 24.700 1.00 19.73 O ANISOU 499 O GLU A 68 2450 2469 2577 -7 -55 66 O ATOM 500 CB GLU A 68 39.253 9.827 25.801 1.00 21.18 C ANISOU 500 CB GLU A 68 2659 2694 2693 13 -25 25 C ATOM 501 CG GLU A 68 39.827 11.207 25.981 1.00 26.90 C ANISOU 501 CG GLU A 68 3495 3243 3483 -79 -20 49 C ATOM 502 CD GLU A 68 39.016 12.040 26.959 1.00 34.48 C ANISOU 502 CD GLU A 68 4438 4304 4355 93 123 -137 C ATOM 503 OE1 GLU A 68 38.240 11.472 27.761 1.00 36.24 O ANISOU 503 OE1 GLU A 68 4658 4506 4603 -123 223 74 O ATOM 504 OE2 GLU A 68 39.154 13.276 26.923 1.00 37.09 O ANISOU 504 OE2 GLU A 68 4888 4261 4943 8 58 51 O ATOM 505 N LEU A 69 41.510 9.377 23.218 1.00 18.82 N ANISOU 505 N LEU A 69 2307 2388 2454 40 -67 22 N ATOM 506 CA LEU A 69 42.931 9.072 23.122 1.00 18.58 C ANISOU 506 CA LEU A 69 2337 2391 2331 -41 -16 -10 C ATOM 507 C LEU A 69 43.653 9.935 24.136 1.00 17.67 C ANISOU 507 C LEU A 69 2190 2272 2252 -70 -44 -11 C ATOM 508 O LEU A 69 43.513 11.150 24.114 1.00 15.88 O ANISOU 508 O LEU A 69 1981 2031 2020 -20 -76 82 O ATOM 509 CB LEU A 69 43.489 9.337 21.731 1.00 18.87 C ANISOU 509 CB LEU A 69 2396 2489 2284 -49 -6 -50 C ATOM 510 CG LEU A 69 45.025 9.374 21.607 1.00 17.98 C ANISOU 510 CG LEU A 69 2311 2323 2197 40 -30 -89 C ATOM 511 CD1 LEU A 69 45.677 8.025 21.943 1.00 19.58 C ANISOU 511 CD1 LEU A 69 2434 2536 2468 48 -23 -18 C ATOM 512 CD2 LEU A 69 45.397 9.831 20.204 1.00 19.46 C ANISOU 512 CD2 LEU A 69 2532 2457 2405 -88 126 126 C ATOM 513 N ALA A 70 44.414 9.290 25.019 1.00 17.46 N ANISOU 513 N ALA A 70 2238 2159 2237 -85 -28 22 N ATOM 514 CA ALA A 70 45.269 9.994 25.981 1.00 17.67 C ANISOU 514 CA ALA A 70 2226 2265 2219 -53 -38 36 C ATOM 515 C ALA A 70 46.743 9.697 25.691 1.00 16.96 C ANISOU 515 C ALA A 70 2138 2154 2152 -61 1 5 C ATOM 516 O ALA A 70 47.088 8.604 25.254 1.00 17.67 O ANISOU 516 O ALA A 70 2155 2229 2328 -129 -94 14 O ATOM 517 CB ALA A 70 44.911 9.586 27.407 1.00 17.94 C ANISOU 517 CB ALA A 70 2287 2328 2201 -5 50 -11 C ATOM 518 N ALA A 71 47.614 10.675 25.919 1.00 16.78 N ANISOU 518 N ALA A 71 2119 2174 2080 -36 -5 1 N ATOM 519 CA ALA A 71 49.033 10.486 25.684 1.00 15.91 C ANISOU 519 CA ALA A 71 2057 2038 1949 -81 -22 -8 C ATOM 520 C ALA A 71 49.832 11.546 26.435 1.00 16.17 C ANISOU 520 C ALA A 71 2090 2063 1989 -55 -28 6 C ATOM 521 O ALA A 71 49.261 12.455 27.037 1.00 15.79 O ANISOU 521 O ALA A 71 2014 2028 1955 -110 -51 -52 O ATOM 522 CB ALA A 71 49.343 10.536 24.158 1.00 15.79 C ANISOU 522 CB ALA A 71 2068 1987 1945 -85 0 68 C ATOM 523 N GLU A 72 51.150 11.402 26.411 1.00 16.20 N ANISOU 523 N GLU A 72 2125 2095 1935 -91 -5 -1 N ATOM 524 CA GLU A 72 52.047 12.427 26.922 1.00 16.74 C ANISOU 524 CA GLU A 72 2146 2127 2084 -72 5 16 C ATOM 525 C GLU A 72 52.821 12.948 25.713 1.00 16.57 C ANISOU 525 C GLU A 72 2117 2134 2043 -40 -8 0 C ATOM 526 O GLU A 72 53.391 12.160 24.968 1.00 17.09 O ANISOU 526 O GLU A 72 2199 2173 2120 -9 67 18 O ATOM 527 CB GLU A 72 52.966 11.840 27.997 1.00 16.86 C ANISOU 527 CB GLU A 72 2205 2111 2089 -43 -37 -22 C ATOM 528 CG GLU A 72 52.185 11.398 29.249 1.00 17.57 C ANISOU 528 CG GLU A 72 2273 2145 2258 -67 46 9 C ATOM 529 CD GLU A 72 52.829 10.264 30.050 1.00 20.81 C ANISOU 529 CD GLU A 72 2611 2666 2627 12 -51 5 C ATOM 530 OE1 GLU A 72 53.994 9.900 29.812 1.00 19.16 O ANISOU 530 OE1 GLU A 72 2410 2464 2405 -122 38 10 O ATOM 531 OE2 GLU A 72 52.133 9.720 30.937 1.00 23.74 O ANISOU 531 OE2 GLU A 72 3040 2959 3019 -87 -16 160 O ATOM 532 N CYS A 73 52.816 14.256 25.508 1.00 16.07 N ANISOU 532 N CYS A 73 1980 2096 2030 -27 -44 -24 N ATOM 533 CA CYS A 73 53.404 14.841 24.300 1.00 16.74 C ANISOU 533 CA CYS A 73 2142 2047 2170 -72 -28 -27 C ATOM 534 C CYS A 73 54.330 15.984 24.652 1.00 17.50 C ANISOU 534 C CYS A 73 2220 2169 2261 -49 -36 -32 C ATOM 535 O CYS A 73 54.071 16.711 25.611 1.00 17.35 O ANISOU 535 O CYS A 73 2213 2145 2232 -60 -16 -75 O ATOM 536 CB CYS A 73 52.316 15.373 23.372 1.00 16.15 C ANISOU 536 CB CYS A 73 2053 2012 2068 -73 -32 -12 C ATOM 537 SG CYS A 73 51.207 14.139 22.704 1.00 17.47 S ANISOU 537 SG CYS A 73 2332 2134 2170 -172 -21 -42 S ATOM 538 N LYS A 74 55.379 16.148 23.847 1.00 17.59 N ANISOU 538 N LYS A 74 2236 2128 2316 -31 -19 28 N ATOM 539 CA LYS A 74 56.356 17.200 24.056 1.00 18.71 C ANISOU 539 CA LYS A 74 2391 2307 2411 10 -36 8 C ATOM 540 C LYS A 74 55.826 18.535 23.545 1.00 18.72 C ANISOU 540 C LYS A 74 2424 2264 2422 -24 -26 15 C ATOM 541 O LYS A 74 55.265 18.635 22.449 1.00 17.35 O ANISOU 541 O LYS A 74 2269 2040 2282 -37 -20 19 O ATOM 542 CB LYS A 74 57.679 16.864 23.353 1.00 19.18 C ANISOU 542 CB LYS A 74 2388 2401 2498 -16 -26 28 C ATOM 543 CG LYS A 74 58.423 15.708 23.993 1.00 21.59 C ANISOU 543 CG LYS A 74 2723 2618 2861 55 -33 -15 C ATOM 544 CD LYS A 74 59.887 15.641 23.546 1.00 25.52 C ANISOU 544 CD LYS A 74 2957 3198 3538 39 9 47 C ATOM 545 CE LYS A 74 60.035 14.787 22.305 1.00 28.87 C ANISOU 545 CE LYS A 74 3597 3677 3692 126 79 -158 C ATOM 546 NZ LYS A 74 61.441 14.308 22.140 1.00 31.04 N ANISOU 546 NZ LYS A 74 3747 3834 4210 123 -34 -141 N ATOM 547 N THR A 75 56.026 19.559 24.357 1.00 19.31 N ANISOU 547 N THR A 75 2525 2414 2396 -2 -6 -33 N ATOM 548 CA THR A 75 55.803 20.925 23.939 1.00 20.16 C ANISOU 548 CA THR A 75 2670 2511 2477 -16 -29 7 C ATOM 549 C THR A 75 56.905 21.351 22.971 1.00 21.32 C ANISOU 549 C THR A 75 2755 2693 2652 -6 -29 0 C ATOM 550 O THR A 75 57.898 20.631 22.767 1.00 20.70 O ANISOU 550 O THR A 75 2723 2640 2503 -10 -13 -50 O ATOM 551 CB THR A 75 55.806 21.869 25.158 1.00 20.41 C ANISOU 551 CB THR A 75 2655 2566 2533 -14 -12 -28 C ATOM 552 OG1 THR A 75 57.114 21.873 25.763 1.00 19.95 O ANISOU 552 OG1 THR A 75 2698 2475 2404 -73 -46 -13 O ATOM 553 CG2 THR A 75 54.762 21.416 26.166 1.00 19.61 C ANISOU 553 CG2 THR A 75 2744 2446 2258 -100 -34 10 C ATOM 554 N ARG A 76 56.732 22.520 22.362 1.00 22.47 N ANISOU 554 N ARG A 76 2926 2798 2814 -32 -14 66 N ATOM 555 CA ARG A 76 57.780 23.052 21.486 1.00 23.79 C ANISOU 555 CA ARG A 76 3093 2982 2962 -8 3 61 C ATOM 556 C ARG A 76 59.120 23.235 22.207 1.00 24.47 C ANISOU 556 C ARG A 76 3150 3045 3101 -12 37 60 C ATOM 557 O ARG A 76 60.190 23.046 21.612 1.00 24.53 O ANISOU 557 O ARG A 76 3182 3035 3101 0 75 64 O ATOM 558 CB ARG A 76 57.300 24.332 20.822 1.00 23.93 C ANISOU 558 CB ARG A 76 3124 2956 3010 -36 13 80 C ATOM 559 CG ARG A 76 56.408 24.031 19.648 1.00 25.10 C ANISOU 559 CG ARG A 76 3286 3099 3151 -5 -111 100 C ATOM 560 CD ARG A 76 56.176 25.262 18.806 1.00 25.52 C ANISOU 560 CD ARG A 76 3326 3233 3136 -9 -90 175 C ATOM 561 NE ARG A 76 55.270 26.205 19.453 1.00 25.53 N ANISOU 561 NE ARG A 76 3270 3253 3177 17 -45 173 N ATOM 562 CZ ARG A 76 53.953 26.261 19.231 1.00 25.63 C ANISOU 562 CZ ARG A 76 3313 3270 3154 -66 91 167 C ATOM 563 NH1 ARG A 76 53.366 25.416 18.381 1.00 25.21 N ANISOU 563 NH1 ARG A 76 3263 3172 3143 -174 69 216 N ATOM 564 NH2 ARG A 76 53.226 27.169 19.857 1.00 23.31 N ANISOU 564 NH2 ARG A 76 3041 2889 2927 -20 90 320 N ATOM 565 N ALA A 77 59.033 23.554 23.502 1.00 24.65 N ANISOU 565 N ALA A 77 3195 3078 3090 -6 -13 -15 N ATOM 566 CA ALA A 77 60.174 23.685 24.403 1.00 24.99 C ANISOU 566 CA ALA A 77 3193 3116 3183 24 -8 18 C ATOM 567 C ALA A 77 60.661 22.325 24.958 1.00 24.88 C ANISOU 567 C ALA A 77 3202 3119 3130 -1 -22 24 C ATOM 568 O ALA A 77 61.510 22.279 25.854 1.00 24.92 O ANISOU 568 O ALA A 77 3206 3084 3175 -57 -76 18 O ATOM 569 CB ALA A 77 59.824 24.642 25.544 1.00 24.67 C ANISOU 569 CB ALA A 77 3166 3080 3125 -4 -81 -40 C ATOM 570 N GLN A 78 60.116 21.236 24.414 1.00 23.89 N ANISOU 570 N GLN A 78 3036 3042 3000 -6 16 33 N ATOM 571 CA GLN A 78 60.628 19.873 24.624 1.00 23.56 C ANISOU 571 CA GLN A 78 3009 3017 2923 -7 18 26 C ATOM 572 C GLN A 78 60.364 19.292 26.015 1.00 22.88 C ANISOU 572 C GLN A 78 2920 2930 2842 11 13 8 C ATOM 573 O GLN A 78 61.106 18.448 26.483 1.00 22.32 O ANISOU 573 O GLN A 78 2877 2874 2727 50 85 -48 O ATOM 574 CB GLN A 78 62.129 19.779 24.273 1.00 23.94 C ANISOU 574 CB GLN A 78 3041 3066 2988 32 46 39 C ATOM 575 CG GLN A 78 62.497 20.280 22.860 1.00 24.59 C ANISOU 575 CG GLN A 78 3143 3179 3020 25 -33 119 C ATOM 576 CD GLN A 78 61.744 19.562 21.746 1.00 27.51 C ANISOU 576 CD GLN A 78 3696 3474 3281 -18 12 -46 C ATOM 577 OE1 GLN A 78 61.133 20.202 20.891 1.00 29.50 O ANISOU 577 OE1 GLN A 78 3908 3813 3488 27 -188 19 O ATOM 578 NE2 GLN A 78 61.778 18.243 21.755 1.00 25.96 N ANISOU 578 NE2 GLN A 78 3589 3304 2970 -44 87 94 N ATOM 579 N GLN A 79 59.305 19.743 26.668 1.00 22.67 N ANISOU 579 N GLN A 79 2909 2895 2807 9 -12 9 N ATOM 580 CA GLN A 79 58.888 19.136 27.923 1.00 22.31 C ANISOU 580 CA GLN A 79 2814 2829 2833 -25 -22 -19 C ATOM 581 C GLN A 79 57.555 18.391 27.734 1.00 21.77 C ANISOU 581 C GLN A 79 2831 2694 2745 -9 -22 7 C ATOM 582 O GLN A 79 56.715 18.792 26.931 1.00 20.38 O ANISOU 582 O GLN A 79 2640 2493 2611 -47 -40 -53 O ATOM 583 CB GLN A 79 58.795 20.189 29.030 1.00 23.13 C ANISOU 583 CB GLN A 79 2956 2946 2884 1 22 47 C ATOM 584 CG GLN A 79 60.137 20.887 29.384 1.00 23.73 C ANISOU 584 CG GLN A 79 3062 3003 2950 -29 -19 -151 C ATOM 585 CD GLN A 79 60.027 21.858 30.570 1.00 27.68 C ANISOU 585 CD GLN A 79 3687 3451 3377 24 -4 82 C ATOM 586 OE1 GLN A 79 58.932 22.300 30.939 1.00 28.38 O ANISOU 586 OE1 GLN A 79 3415 3862 3503 106 248 -40 O ATOM 587 NE2 GLN A 79 61.176 22.213 31.153 1.00 28.45 N ANISOU 587 NE2 GLN A 79 3317 3765 3727 -239 -287 -132 N ATOM 588 N PHE A 80 57.378 17.295 28.465 1.00 20.87 N ANISOU 588 N PHE A 80 2665 2633 2629 -12 -9 35 N ATOM 589 CA PHE A 80 56.178 16.477 28.329 1.00 19.81 C ANISOU 589 CA PHE A 80 2552 2461 2513 -13 17 -5 C ATOM 590 C PHE A 80 55.009 16.988 29.167 1.00 19.27 C ANISOU 590 C PHE A 80 2470 2393 2459 -48 10 -10 C ATOM 591 O PHE A 80 55.178 17.324 30.348 1.00 18.39 O ANISOU 591 O PHE A 80 2371 2252 2364 -99 95 -133 O ATOM 592 CB PHE A 80 56.470 15.009 28.681 1.00 20.63 C ANISOU 592 CB PHE A 80 2623 2601 2614 3 27 24 C ATOM 593 CG PHE A 80 57.121 14.231 27.565 1.00 19.95 C ANISOU 593 CG PHE A 80 2618 2372 2589 55 -4 30 C ATOM 594 CD1 PHE A 80 56.351 13.563 26.618 1.00 21.05 C ANISOU 594 CD1 PHE A 80 2780 2522 2693 101 34 82 C ATOM 595 CD2 PHE A 80 58.506 14.169 27.466 1.00 21.89 C ANISOU 595 CD2 PHE A 80 2713 2830 2774 107 28 44 C ATOM 596 CE1 PHE A 80 56.948 12.840 25.581 1.00 21.27 C ANISOU 596 CE1 PHE A 80 2739 2750 2593 -76 0 -53 C ATOM 597 CE2 PHE A 80 59.123 13.431 26.433 1.00 22.37 C ANISOU 597 CE2 PHE A 80 2869 2890 2737 20 -82 -165 C ATOM 598 CZ PHE A 80 58.331 12.763 25.488 1.00 22.54 C ANISOU 598 CZ PHE A 80 2900 2879 2783 34 -22 2 C ATOM 599 N VAL A 81 53.825 17.008 28.550 1.00 18.30 N ANISOU 599 N VAL A 81 2422 2187 2341 -17 23 5 N ATOM 600 CA VAL A 81 52.565 17.269 29.244 1.00 18.06 C ANISOU 600 CA VAL A 81 2348 2197 2315 -57 -33 7 C ATOM 601 C VAL A 81 51.581 16.128 28.923 1.00 18.53 C ANISOU 601 C VAL A 81 2380 2313 2347 -52 -21 0 C ATOM 602 O VAL A 81 51.769 15.423 27.933 1.00 17.81 O ANISOU 602 O VAL A 81 2325 2115 2326 -45 7 -2 O ATOM 603 CB VAL A 81 51.980 18.664 28.868 1.00 18.45 C ANISOU 603 CB VAL A 81 2378 2299 2330 -31 -23 -32 C ATOM 604 CG1 VAL A 81 52.952 19.770 29.269 1.00 17.24 C ANISOU 604 CG1 VAL A 81 2318 1999 2232 -48 -13 -54 C ATOM 605 CG2 VAL A 81 51.668 18.753 27.366 1.00 16.97 C ANISOU 605 CG2 VAL A 81 2269 2070 2106 -13 -71 92 C ATOM 606 N SER A 82 50.577 15.923 29.775 1.00 18.31 N ANISOU 606 N SER A 82 2305 2297 2354 11 6 -37 N ATOM 607 CA SER A 82 49.516 14.949 29.485 1.00 18.88 C ANISOU 607 CA SER A 82 2387 2387 2399 2 -17 -20 C ATOM 608 C SER A 82 48.457 15.643 28.644 1.00 18.79 C ANISOU 608 C SER A 82 2404 2383 2352 -3 0 -31 C ATOM 609 O SER A 82 48.134 16.814 28.874 1.00 19.46 O ANISOU 609 O SER A 82 2544 2439 2409 -62 -27 -139 O ATOM 610 CB SER A 82 48.876 14.388 30.765 1.00 18.62 C ANISOU 610 CB SER A 82 2420 2366 2286 63 -44 -11 C ATOM 611 OG SER A 82 49.813 13.611 31.496 1.00 22.76 O ANISOU 611 OG SER A 82 2817 2914 2916 87 -43 87 O ATOM 612 N THR A 83 47.928 14.922 27.660 1.00 18.50 N ANISOU 612 N THR A 83 2352 2273 2401 -61 11 -63 N ATOM 613 CA THR A 83 46.970 15.488 26.743 1.00 18.34 C ANISOU 613 CA THR A 83 2352 2302 2311 -84 -9 -79 C ATOM 614 C THR A 83 45.939 14.436 26.337 1.00 19.37 C ANISOU 614 C THR A 83 2487 2418 2453 -69 -45 -67 C ATOM 615 O THR A 83 46.148 13.229 26.533 1.00 18.62 O ANISOU 615 O THR A 83 2422 2355 2297 -97 -160 -115 O ATOM 616 CB THR A 83 47.669 16.182 25.519 1.00 18.34 C ANISOU 616 CB THR A 83 2374 2219 2373 -82 -26 -93 C ATOM 617 OG1 THR A 83 46.693 16.747 24.630 1.00 17.60 O ANISOU 617 OG1 THR A 83 2347 2050 2290 -173 14 -118 O ATOM 618 CG2 THR A 83 48.584 15.226 24.762 1.00 16.79 C ANISOU 618 CG2 THR A 83 2176 2260 1941 -99 104 3 C ATOM 619 N LYS A 84 44.809 14.905 25.819 1.00 20.06 N ANISOU 619 N LYS A 84 2567 2527 2528 -26 -41 -83 N ATOM 620 CA LYS A 84 43.754 13.995 25.368 1.00 21.15 C ANISOU 620 CA LYS A 84 2689 2653 2694 -46 19 -45 C ATOM 621 C LYS A 84 42.936 14.597 24.239 1.00 20.06 C ANISOU 621 C LYS A 84 2543 2494 2584 -50 -5 -43 C ATOM 622 O LYS A 84 42.970 15.810 24.000 1.00 19.97 O ANISOU 622 O LYS A 84 2521 2501 2563 26 -47 -106 O ATOM 623 CB LYS A 84 42.864 13.551 26.537 1.00 21.91 C ANISOU 623 CB LYS A 84 2750 2731 2842 -66 8 -24 C ATOM 624 CG LYS A 84 42.284 14.716 27.316 1.00 24.14 C ANISOU 624 CG LYS A 84 3201 3015 2957 -18 184 -15 C ATOM 625 CD LYS A 84 41.573 14.297 28.601 1.00 26.99 C ANISOU 625 CD LYS A 84 3424 3500 3331 -121 39 23 C ATOM 626 CE LYS A 84 40.715 15.457 29.113 1.00 30.76 C ANISOU 626 CE LYS A 84 3867 3770 4047 242 145 -115 C ATOM 627 NZ LYS A 84 39.898 16.037 28.004 1.00 35.17 N ANISOU 627 NZ LYS A 84 4342 4545 4476 84 -76 41 N ATOM 628 N ILE A 85 42.235 13.730 23.515 1.00 18.77 N ANISOU 628 N ILE A 85 2423 2324 2384 -28 -26 14 N ATOM 629 CA ILE A 85 41.386 14.144 22.402 1.00 17.99 C ANISOU 629 CA ILE A 85 2315 2210 2307 -10 -5 -29 C ATOM 630 C ILE A 85 40.255 13.123 22.254 1.00 17.46 C ANISOU 630 C ILE A 85 2201 2198 2235 -28 31 1 C ATOM 631 O ILE A 85 40.482 11.916 22.426 1.00 16.88 O ANISOU 631 O ILE A 85 2092 2090 2231 -90 -70 14 O ATOM 632 CB ILE A 85 42.224 14.304 21.093 1.00 17.39 C ANISOU 632 CB ILE A 85 2264 2103 2240 -3 50 59 C ATOM 633 CG1 ILE A 85 41.395 14.890 19.939 1.00 17.54 C ANISOU 633 CG1 ILE A 85 2161 2220 2282 -22 2 -110 C ATOM 634 CG2 ILE A 85 42.945 12.999 20.704 1.00 17.90 C ANISOU 634 CG2 ILE A 85 2400 2113 2286 78 41 110 C ATOM 635 CD1 ILE A 85 42.238 15.541 18.861 1.00 17.79 C ANISOU 635 CD1 ILE A 85 2334 2197 2225 -1 -34 27 C ATOM 636 N ASN A 86 39.057 13.605 21.929 1.00 16.47 N ANISOU 636 N ASN A 86 2062 2088 2106 3 32 -38 N ATOM 637 CA ASN A 86 37.900 12.732 21.808 1.00 17.68 C ANISOU 637 CA ASN A 86 2167 2241 2308 25 23 -48 C ATOM 638 C ASN A 86 37.810 12.196 20.396 1.00 17.66 C ANISOU 638 C ASN A 86 2143 2249 2315 -29 10 -34 C ATOM 639 O ASN A 86 37.415 12.933 19.482 1.00 17.09 O ANISOU 639 O ASN A 86 2040 2127 2325 48 -43 -73 O ATOM 640 CB ASN A 86 36.587 13.466 22.174 1.00 17.80 C ANISOU 640 CB ASN A 86 2164 2269 2328 36 25 -4 C ATOM 641 CG ASN A 86 35.413 12.519 22.267 1.00 18.84 C ANISOU 641 CG ASN A 86 2326 2459 2371 9 28 0 C ATOM 642 OD1 ASN A 86 35.523 11.353 21.899 1.00 19.73 O ANISOU 642 OD1 ASN A 86 2437 2544 2513 -150 92 24 O ATOM 643 ND2 ASN A 86 34.288 13.005 22.771 1.00 20.42 N ANISOU 643 ND2 ASN A 86 2512 2684 2562 45 22 -74 N ATOM 644 N LEU A 87 38.186 10.924 20.221 1.00 17.44 N ANISOU 644 N LEU A 87 2109 2183 2334 31 -43 22 N ATOM 645 CA LEU A 87 38.186 10.279 18.897 1.00 18.22 C ANISOU 645 CA LEU A 87 2262 2241 2417 45 -34 0 C ATOM 646 C LEU A 87 36.800 10.251 18.232 1.00 18.53 C ANISOU 646 C LEU A 87 2313 2278 2448 36 -39 27 C ATOM 647 O LEU A 87 36.696 10.195 17.008 1.00 18.69 O ANISOU 647 O LEU A 87 2330 2292 2477 19 -9 -73 O ATOM 648 CB LEU A 87 38.768 8.857 18.972 1.00 18.08 C ANISOU 648 CB LEU A 87 2245 2233 2390 52 -40 67 C ATOM 649 CG LEU A 87 40.198 8.770 19.537 1.00 17.62 C ANISOU 649 CG LEU A 87 2249 2178 2268 41 -66 -44 C ATOM 650 CD1 LEU A 87 40.683 7.309 19.636 1.00 18.78 C ANISOU 650 CD1 LEU A 87 2475 2273 2387 64 0 87 C ATOM 651 CD2 LEU A 87 41.141 9.595 18.692 1.00 17.22 C ANISOU 651 CD2 LEU A 87 2084 2187 2270 -60 -75 -65 C ATOM 652 N ASP A 88 35.748 10.283 19.046 1.00 19.09 N ANISOU 652 N ASP A 88 2404 2348 2498 60 -6 19 N ATOM 653 CA ASP A 88 34.373 10.383 18.540 1.00 19.09 C ANISOU 653 CA ASP A 88 2380 2370 2501 16 -69 25 C ATOM 654 C ASP A 88 34.110 11.666 17.718 1.00 19.53 C ANISOU 654 C ASP A 88 2442 2411 2568 12 -67 18 C ATOM 655 O ASP A 88 33.098 11.751 17.028 1.00 18.92 O ANISOU 655 O ASP A 88 2303 2314 2570 -8 -99 55 O ATOM 656 CB ASP A 88 33.361 10.293 19.684 1.00 18.91 C ANISOU 656 CB ASP A 88 2344 2388 2453 24 -50 -16 C ATOM 657 CG ASP A 88 32.949 8.860 20.012 1.00 19.06 C ANISOU 657 CG ASP A 88 2312 2460 2469 35 -24 -12 C ATOM 658 OD1 ASP A 88 33.153 7.943 19.190 1.00 18.57 O ANISOU 658 OD1 ASP A 88 2134 2555 2366 -118 -160 -115 O ATOM 659 OD2 ASP A 88 32.400 8.642 21.115 1.00 20.33 O ANISOU 659 OD2 ASP A 88 2704 2537 2482 51 6 -104 O ATOM 660 N ASP A 89 35.011 12.646 17.797 1.00 19.90 N ANISOU 660 N ASP A 89 2453 2419 2686 2 -60 41 N ATOM 661 CA ASP A 89 34.924 13.867 16.987 1.00 20.82 C ANISOU 661 CA ASP A 89 2615 2590 2703 -40 -36 36 C ATOM 662 C ASP A 89 34.927 13.546 15.498 1.00 21.25 C ANISOU 662 C ASP A 89 2673 2651 2748 -29 -42 16 C ATOM 663 O ASP A 89 34.179 14.151 14.739 1.00 21.99 O ANISOU 663 O ASP A 89 2790 2672 2893 67 -6 16 O ATOM 664 CB ASP A 89 36.109 14.826 17.271 1.00 20.16 C ANISOU 664 CB ASP A 89 2606 2434 2618 -62 -46 4 C ATOM 665 CG ASP A 89 36.040 15.471 18.642 1.00 20.91 C ANISOU 665 CG ASP A 89 2686 2525 2732 -34 -7 30 C ATOM 666 OD1 ASP A 89 35.065 15.246 19.387 1.00 20.58 O ANISOU 666 OD1 ASP A 89 2640 2413 2767 -48 102 -148 O ATOM 667 OD2 ASP A 89 36.988 16.213 18.979 1.00 20.92 O ANISOU 667 OD2 ASP A 89 2709 2489 2751 -17 -19 -49 O ATOM 668 N HIS A 90 35.760 12.588 15.089 1.00 20.96 N ANISOU 668 N HIS A 90 2618 2612 2731 0 -30 33 N ATOM 669 CA HIS A 90 36.008 12.339 13.668 1.00 21.58 C ANISOU 669 CA HIS A 90 2724 2678 2795 18 -38 51 C ATOM 670 C HIS A 90 36.147 10.868 13.261 1.00 21.08 C ANISOU 670 C HIS A 90 2665 2657 2685 14 -59 31 C ATOM 671 O HIS A 90 36.193 10.564 12.071 1.00 21.39 O ANISOU 671 O HIS A 90 2764 2634 2730 127 9 86 O ATOM 672 CB HIS A 90 37.237 13.141 13.200 1.00 21.65 C ANISOU 672 CB HIS A 90 2691 2734 2799 14 -45 17 C ATOM 673 CG HIS A 90 36.988 14.615 13.085 1.00 23.56 C ANISOU 673 CG HIS A 90 2956 2906 3088 -17 -4 53 C ATOM 674 ND1 HIS A 90 37.428 15.523 14.027 1.00 25.40 N ANISOU 674 ND1 HIS A 90 3263 3092 3295 -5 -114 29 N ATOM 675 CD2 HIS A 90 36.332 15.337 12.144 1.00 23.89 C ANISOU 675 CD2 HIS A 90 2993 3014 3069 80 -35 79 C ATOM 676 CE1 HIS A 90 37.061 16.742 13.667 1.00 25.53 C ANISOU 676 CE1 HIS A 90 3233 3087 3378 -38 -68 52 C ATOM 677 NE2 HIS A 90 36.395 16.657 12.529 1.00 25.63 N ANISOU 677 NE2 HIS A 90 3326 3088 3324 -42 -71 101 N ATOM 678 N ILE A 91 36.216 9.952 14.227 1.00 20.43 N ANISOU 678 N ILE A 91 2530 2604 2627 -24 -57 42 N ATOM 679 CA ILE A 91 36.302 8.544 13.879 1.00 19.98 C ANISOU 679 CA ILE A 91 2488 2552 2551 -22 -69 67 C ATOM 680 C ILE A 91 34.915 7.928 13.864 1.00 20.33 C ANISOU 680 C ILE A 91 2547 2572 2604 -34 -67 55 C ATOM 681 O ILE A 91 34.200 7.952 14.878 1.00 19.46 O ANISOU 681 O ILE A 91 2499 2439 2453 -78 -127 89 O ATOM 682 CB ILE A 91 37.255 7.719 14.806 1.00 19.99 C ANISOU 682 CB ILE A 91 2481 2525 2587 -32 -62 53 C ATOM 683 CG1 ILE A 91 38.622 8.410 14.954 1.00 18.98 C ANISOU 683 CG1 ILE A 91 2380 2386 2443 17 -108 90 C ATOM 684 CG2 ILE A 91 37.410 6.293 14.269 1.00 19.54 C ANISOU 684 CG2 ILE A 91 2394 2552 2475 -38 -55 1 C ATOM 685 CD1 ILE A 91 39.386 8.557 13.662 1.00 19.85 C ANISOU 685 CD1 ILE A 91 2477 2478 2588 -49 -15 46 C ATOM 686 N ALA A 92 34.547 7.381 12.702 1.00 20.87 N ANISOU 686 N ALA A 92 2641 2683 2605 -36 -37 118 N ATOM 687 CA ALA A 92 33.235 6.773 12.531 1.00 22.10 C ANISOU 687 CA ALA A 92 2801 2827 2767 -27 -100 28 C ATOM 688 C ALA A 92 33.406 5.320 12.188 1.00 22.79 C ANISOU 688 C ALA A 92 2894 2928 2834 26 -56 16 C ATOM 689 O ALA A 92 34.494 4.894 11.829 1.00 23.13 O ANISOU 689 O ALA A 92 2885 2991 2912 47 -56 5 O ATOM 690 CB ALA A 92 32.438 7.492 11.435 1.00 21.63 C ANISOU 690 CB ALA A 92 2721 2738 2757 -17 -130 36 C ATOM 691 N ALA A 93 32.326 4.562 12.306 1.00 23.78 N ANISOU 691 N ALA A 93 3032 3055 2946 7 -37 10 N ATOM 692 CA ALA A 93 32.291 3.208 11.799 1.00 24.95 C ANISOU 692 CA ALA A 93 3173 3174 3132 -11 -12 3 C ATOM 693 C ALA A 93 31.259 3.175 10.680 1.00 25.85 C ANISOU 693 C ALA A 93 3295 3296 3227 -17 -19 3 C ATOM 694 O ALA A 93 30.128 3.618 10.858 1.00 25.03 O ANISOU 694 O ALA A 93 3188 3225 3096 -4 -5 -36 O ATOM 695 CB ALA A 93 31.941 2.231 12.908 1.00 24.90 C ANISOU 695 CB ALA A 93 3166 3200 3093 -21 -45 21 C ATOM 696 N ILE A 94 31.669 2.705 9.507 1.00 27.36 N ANISOU 696 N ILE A 94 3481 3510 3404 28 14 -32 N ATOM 697 CA ILE A 94 30.751 2.577 8.385 1.00 29.00 C ANISOU 697 CA ILE A 94 3658 3744 3615 13 -25 -35 C ATOM 698 C ILE A 94 30.771 1.114 7.979 1.00 29.44 C ANISOU 698 C ILE A 94 3744 3782 3658 16 -32 -38 C ATOM 699 O ILE A 94 31.822 0.599 7.587 1.00 28.96 O ANISOU 699 O ILE A 94 3665 3821 3517 21 -53 -109 O ATOM 700 CB ILE A 94 31.165 3.445 7.162 1.00 29.42 C ANISOU 700 CB ILE A 94 3735 3769 3674 1 -52 13 C ATOM 701 CG1 ILE A 94 31.464 4.911 7.551 1.00 30.42 C ANISOU 701 CG1 ILE A 94 3889 3889 3778 15 -42 -17 C ATOM 702 CG2 ILE A 94 30.121 3.328 6.040 1.00 30.17 C ANISOU 702 CG2 ILE A 94 3727 3915 3819 30 -65 -23 C ATOM 703 CD1 ILE A 94 30.265 5.745 7.965 1.00 32.00 C ANISOU 703 CD1 ILE A 94 4001 4043 4114 105 32 -27 C ATOM 704 N ASP A 95 29.614 0.458 8.087 1.00 30.07 N ANISOU 704 N ASP A 95 3775 3892 3756 34 -23 -36 N ATOM 705 CA ASP A 95 29.465 -0.987 7.834 1.00 30.85 C ANISOU 705 CA ASP A 95 3882 3972 3867 8 -24 -34 C ATOM 706 C ASP A 95 30.565 -1.850 8.488 1.00 30.47 C ANISOU 706 C ASP A 95 3828 3933 3815 19 -23 -48 C ATOM 707 O ASP A 95 31.067 -2.795 7.880 1.00 30.17 O ANISOU 707 O ASP A 95 3758 3929 3776 -4 -55 -32 O ATOM 708 CB ASP A 95 29.355 -1.270 6.323 1.00 31.89 C ANISOU 708 CB ASP A 95 3995 4106 4014 41 -23 -69 C ATOM 709 CG ASP A 95 28.896 -2.695 6.018 1.00 34.96 C ANISOU 709 CG ASP A 95 4400 4372 4511 -16 -99 -45 C ATOM 710 OD1 ASP A 95 28.136 -3.283 6.822 1.00 36.54 O ANISOU 710 OD1 ASP A 95 4586 4647 4651 -90 17 -51 O ATOM 711 OD2 ASP A 95 29.313 -3.234 4.968 1.00 37.58 O ANISOU 711 OD2 ASP A 95 4895 4770 4612 47 2 -270 O ATOM 712 N GLY A 96 30.938 -1.512 9.725 1.00 29.65 N ANISOU 712 N GLY A 96 3703 3840 3722 -11 -12 -49 N ATOM 713 CA GLY A 96 31.875 -2.327 10.496 1.00 28.89 C ANISOU 713 CA GLY A 96 3656 3731 3588 -45 -24 -84 C ATOM 714 C GLY A 96 33.338 -1.944 10.336 1.00 28.38 C ANISOU 714 C GLY A 96 3631 3655 3498 -31 -7 -80 C ATOM 715 O GLY A 96 34.223 -2.645 10.821 1.00 28.37 O ANISOU 715 O GLY A 96 3629 3661 3487 -44 -32 -129 O ATOM 716 N THR A 97 33.595 -0.834 9.654 1.00 27.91 N ANISOU 716 N THR A 97 3564 3558 3481 -50 -38 -112 N ATOM 717 CA THR A 97 34.969 -0.407 9.377 1.00 27.56 C ANISOU 717 CA THR A 97 3525 3506 3437 -30 -19 -86 C ATOM 718 C THR A 97 35.185 0.995 9.928 1.00 26.91 C ANISOU 718 C THR A 97 3430 3410 3383 -6 -24 -43 C ATOM 719 O THR A 97 34.370 1.892 9.698 1.00 26.66 O ANISOU 719 O THR A 97 3355 3394 3380 35 -13 -107 O ATOM 720 CB THR A 97 35.281 -0.440 7.857 1.00 27.87 C ANISOU 720 CB THR A 97 3538 3564 3486 9 -18 -47 C ATOM 721 OG1 THR A 97 35.354 -1.803 7.421 1.00 27.93 O ANISOU 721 OG1 THR A 97 3641 3587 3385 -89 -145 -146 O ATOM 722 CG2 THR A 97 36.608 0.244 7.546 1.00 28.47 C ANISOU 722 CG2 THR A 97 3685 3616 3515 -111 -30 -87 C ATOM 723 N LEU A 98 36.285 1.171 10.653 1.00 25.82 N ANISOU 723 N LEU A 98 3290 3256 3262 22 -17 -29 N ATOM 724 CA LEU A 98 36.618 2.468 11.214 1.00 25.14 C ANISOU 724 CA LEU A 98 3187 3201 3163 6 -30 4 C ATOM 725 C LEU A 98 37.099 3.359 10.089 1.00 25.69 C ANISOU 725 C LEU A 98 3235 3297 3229 -17 -8 1 C ATOM 726 O LEU A 98 37.894 2.935 9.244 1.00 24.76 O ANISOU 726 O LEU A 98 3128 3186 3094 45 37 15 O ATOM 727 CB LEU A 98 37.674 2.346 12.312 1.00 24.63 C ANISOU 727 CB LEU A 98 3136 3121 3101 24 -10 33 C ATOM 728 CG LEU A 98 37.257 1.588 13.586 1.00 21.21 C ANISOU 728 CG LEU A 98 2726 2581 2752 -9 11 14 C ATOM 729 CD1 LEU A 98 38.493 1.176 14.314 1.00 19.75 C ANISOU 729 CD1 LEU A 98 2609 2377 2516 -83 57 29 C ATOM 730 CD2 LEU A 98 36.329 2.402 14.513 1.00 19.28 C ANISOU 730 CD2 LEU A 98 2531 2326 2469 -147 -127 100 C ATOM 731 N LYS A 99 36.577 4.574 10.055 1.00 26.15 N ANISOU 731 N LYS A 99 3302 3345 3287 19 0 -36 N ATOM 732 CA LYS A 99 36.940 5.546 9.027 1.00 28.09 C ANISOU 732 CA LYS A 99 3575 3594 3502 -12 -5 -12 C ATOM 733 C LYS A 99 37.094 6.933 9.645 1.00 27.99 C ANISOU 733 C LYS A 99 3557 3572 3506 -22 -3 -8 C ATOM 734 O LYS A 99 36.446 7.247 10.643 1.00 27.86 O ANISOU 734 O LYS A 99 3542 3618 3424 -53 43 -2 O ATOM 735 CB LYS A 99 35.872 5.596 7.929 1.00 28.14 C ANISOU 735 CB LYS A 99 3597 3578 3515 0 0 9 C ATOM 736 CG LYS A 99 35.557 4.248 7.263 1.00 29.62 C ANISOU 736 CG LYS A 99 3859 3779 3615 -7 -95 -18 C ATOM 737 CD LYS A 99 34.865 4.425 5.894 1.00 31.28 C ANISOU 737 CD LYS A 99 3999 3967 3916 -34 -58 -29 C ATOM 738 CE LYS A 99 35.881 4.444 4.750 1.00 34.05 C ANISOU 738 CE LYS A 99 4301 4552 4085 -55 92 -88 C ATOM 739 NZ LYS A 99 36.699 3.199 4.750 1.00 36.14 N ANISOU 739 NZ LYS A 99 4619 4514 4599 94 -74 -20 N ATOM 740 N TYR A 100 37.946 7.763 9.056 1.00 27.94 N ANISOU 740 N TYR A 100 3541 3611 3464 -3 -10 19 N ATOM 741 CA TYR A 100 37.988 9.171 9.417 1.00 28.31 C ANISOU 741 CA TYR A 100 3565 3616 3572 -20 -23 49 C ATOM 742 C TYR A 100 36.923 9.934 8.611 1.00 29.67 C ANISOU 742 C TYR A 100 3707 3777 3789 -31 -40 49 C ATOM 743 O TYR A 100 36.818 9.755 7.393 1.00 29.10 O ANISOU 743 O TYR A 100 3616 3716 3723 -19 -47 64 O ATOM 744 CB TYR A 100 39.375 9.730 9.133 1.00 27.86 C ANISOU 744 CB TYR A 100 3499 3556 3529 32 -58 39 C ATOM 745 CG TYR A 100 39.562 11.182 9.466 1.00 26.36 C ANISOU 745 CG TYR A 100 3198 3448 3367 -43 -43 35 C ATOM 746 CD1 TYR A 100 39.705 11.591 10.781 1.00 25.80 C ANISOU 746 CD1 TYR A 100 3097 3372 3333 17 38 87 C ATOM 747 CD2 TYR A 100 39.622 12.152 8.462 1.00 25.78 C ANISOU 747 CD2 TYR A 100 3151 3340 3301 29 -33 17 C ATOM 748 CE1 TYR A 100 39.910 12.910 11.101 1.00 25.65 C ANISOU 748 CE1 TYR A 100 3202 3250 3292 51 19 -14 C ATOM 749 CE2 TYR A 100 39.821 13.498 8.782 1.00 25.91 C ANISOU 749 CE2 TYR A 100 3248 3270 3324 3 17 60 C ATOM 750 CZ TYR A 100 39.957 13.861 10.108 1.00 26.45 C ANISOU 750 CZ TYR A 100 3357 3365 3326 10 -27 35 C ATOM 751 OH TYR A 100 40.149 15.176 10.479 1.00 28.52 O ANISOU 751 OH TYR A 100 3716 3549 3571 -16 -114 52 O ATOM 752 N GLU A 101 36.146 10.768 9.298 1.00 31.54 N ANISOU 752 N GLU A 101 3967 3972 4045 -38 4 20 N ATOM 753 CA GLU A 101 35.060 11.554 8.681 1.00 34.03 C ANISOU 753 CA GLU A 101 4309 4299 4320 0 -34 34 C ATOM 754 C GLU A 101 35.301 13.052 8.797 1.00 35.64 C ANISOU 754 C GLU A 101 4536 4460 4543 -15 -43 38 C ATOM 755 O GLU A 101 35.824 13.515 9.803 1.00 35.23 O ANISOU 755 O GLU A 101 4506 4374 4505 2 -95 83 O ATOM 756 CB GLU A 101 33.723 11.240 9.349 1.00 34.09 C ANISOU 756 CB GLU A 101 4269 4330 4354 -14 -33 -14 C ATOM 757 CG GLU A 101 33.024 10.019 8.799 1.00 35.00 C ANISOU 757 CG GLU A 101 4452 4388 4457 -28 10 -15 C ATOM 758 CD GLU A 101 31.573 9.913 9.244 1.00 35.16 C ANISOU 758 CD GLU A 101 4415 4501 4444 59 -9 -24 C ATOM 759 OE1 GLU A 101 31.188 10.539 10.258 1.00 31.70 O ANISOU 759 OE1 GLU A 101 3978 4059 4005 39 -132 52 O ATOM 760 OE2 GLU A 101 30.816 9.168 8.582 1.00 37.42 O ANISOU 760 OE2 GLU A 101 4709 4827 4679 -32 -137 -127 O ATOM 761 N LEU A 102 34.851 13.802 7.784 1.00 37.98 N ANISOU 761 N LEU A 102 4836 4801 4792 -10 -51 53 N ATOM 762 CA LEU A 102 35.110 15.244 7.658 1.00 39.44 C ANISOU 762 CA LEU A 102 5022 4959 5002 -13 0 38 C ATOM 763 C LEU A 102 36.598 15.528 7.791 1.00 40.17 C ANISOU 763 C LEU A 102 5074 5094 5094 -5 1 65 C ATOM 764 O LEU A 102 37.224 16.061 6.875 1.00 41.22 O ANISOU 764 O LEU A 102 5204 5243 5213 -8 11 78 O ATOM 765 CB LEU A 102 34.317 16.067 8.686 1.00 40.19 C ANISOU 765 CB LEU A 102 5106 5076 5087 2 13 32 C ATOM 766 CG LEU A 102 33.072 16.857 8.244 1.00 41.91 C ANISOU 766 CG LEU A 102 5224 5353 5346 0 -64 27 C ATOM 767 CD1 LEU A 102 32.340 17.436 9.449 1.00 42.79 C ANISOU 767 CD1 LEU A 102 5369 5498 5390 25 39 -40 C ATOM 768 CD2 LEU A 102 33.412 17.985 7.247 1.00 42.50 C ANISOU 768 CD2 LEU A 102 5478 5258 5410 -72 0 64 C TER 769 LEU A 102 ATOM 770 N GLY A 2 47.220 -11.878 11.655 1.00 20.04 N ANISOU 770 N GLY B 2 2600 2634 2378 3 103 -87 N ATOM 771 CA GLY A 2 48.449 -11.417 10.907 1.00 19.31 C ANISOU 771 CA GLY B 2 2466 2491 2377 -15 42 -63 C ATOM 772 C GLY A 2 48.682 -12.230 9.641 1.00 19.34 C ANISOU 772 C GLY B 2 2478 2453 2415 0 6 -40 C ATOM 773 O GLY A 2 47.754 -12.440 8.850 1.00 18.89 O ANISOU 773 O GLY B 2 2343 2410 2422 -2 -11 -84 O ATOM 774 N ASN A 3 49.921 -12.688 9.458 1.00 18.27 N ANISOU 774 N ASN B 3 2376 2287 2275 -22 5 5 N ATOM 775 CA ASN A 3 50.276 -13.602 8.366 1.00 18.80 C ANISOU 775 CA ASN B 3 2481 2370 2291 -10 0 35 C ATOM 776 C ASN A 3 50.116 -13.001 6.971 1.00 18.44 C ANISOU 776 C ASN B 3 2387 2308 2309 1 -5 54 C ATOM 777 O ASN A 3 49.813 -13.732 6.009 1.00 18.35 O ANISOU 777 O ASN B 3 2478 2264 2227 31 -32 55 O ATOM 778 CB ASN A 3 49.451 -14.899 8.451 1.00 19.40 C ANISOU 778 CB ASN B 3 2511 2452 2405 -60 38 36 C ATOM 779 CG ASN A 3 49.808 -15.741 9.657 1.00 21.66 C ANISOU 779 CG ASN B 3 2839 2777 2611 0 -45 40 C ATOM 780 OD1 ASN A 3 48.942 -16.394 10.271 1.00 25.09 O ANISOU 780 OD1 ASN B 3 3247 3121 3165 -104 134 32 O ATOM 781 ND2 ASN A 3 51.084 -15.755 9.994 1.00 21.43 N ANISOU 781 ND2 ASN B 3 2716 2877 2549 -76 -76 91 N ATOM 782 N PHE A 4 50.320 -11.688 6.854 1.00 17.53 N ANISOU 782 N PHE B 4 2224 2200 2236 -8 -4 62 N ATOM 783 CA PHE A 4 50.262 -11.050 5.522 1.00 17.64 C ANISOU 783 CA PHE B 4 2295 2177 2228 -43 -33 21 C ATOM 784 C PHE A 4 51.199 -11.719 4.506 1.00 17.52 C ANISOU 784 C PHE B 4 2226 2177 2252 -18 -27 0 C ATOM 785 O PHE A 4 50.905 -11.711 3.306 1.00 17.66 O ANISOU 785 O PHE B 4 2297 2182 2229 53 -13 110 O ATOM 786 CB PHE A 4 50.594 -9.556 5.592 1.00 17.21 C ANISOU 786 CB PHE B 4 2263 2106 2168 20 -18 29 C ATOM 787 CG PHE A 4 52.057 -9.275 5.596 1.00 16.81 C ANISOU 787 CG PHE B 4 2232 1990 2164 -19 18 -39 C ATOM 788 CD1 PHE A 4 52.718 -8.914 4.411 1.00 16.58 C ANISOU 788 CD1 PHE B 4 2200 1956 2143 7 -48 66 C ATOM 789 CD2 PHE A 4 52.800 -9.427 6.770 1.00 14.60 C ANISOU 789 CD2 PHE B 4 2023 1542 1980 -24 -40 50 C ATOM 790 CE1 PHE A 4 54.098 -8.671 4.411 1.00 16.21 C ANISOU 790 CE1 PHE B 4 2210 1830 2116 -10 2 -93 C ATOM 791 CE2 PHE A 4 54.178 -9.191 6.776 1.00 16.56 C ANISOU 791 CE2 PHE B 4 2191 1891 2208 43 14 -14 C ATOM 792 CZ PHE A 4 54.825 -8.817 5.601 1.00 18.00 C ANISOU 792 CZ PHE B 4 2360 2095 2381 6 -17 31 C ATOM 793 N SER A 5 52.331 -12.272 4.957 1.00 17.70 N ANISOU 793 N SER B 5 2362 2115 2246 -35 -35 62 N ATOM 794 CA SER A 5 53.344 -12.765 4.001 1.00 17.75 C ANISOU 794 CA SER B 5 2349 2180 2214 -6 -25 2 C ATOM 795 C SER A 5 52.835 -13.922 3.143 1.00 18.74 C ANISOU 795 C SER B 5 2460 2331 2328 -22 -37 0 C ATOM 796 O SER A 5 53.408 -14.215 2.082 1.00 18.78 O ANISOU 796 O SER B 5 2481 2348 2303 -1 7 -93 O ATOM 797 CB SER A 5 54.661 -13.151 4.678 1.00 17.67 C ANISOU 797 CB SER B 5 2336 2146 2229 -13 53 24 C ATOM 798 OG SER A 5 54.493 -14.260 5.538 1.00 17.64 O ANISOU 798 OG SER B 5 2418 2151 2133 162 -121 0 O ATOM 799 N GLN A 6 51.766 -14.566 3.607 1.00 18.45 N ANISOU 799 N GLN B 6 2373 2355 2281 5 -50 14 N ATOM 800 CA GLN A 6 51.177 -15.724 2.910 1.00 19.57 C ANISOU 800 CA GLN B 6 2571 2422 2442 -5 -69 42 C ATOM 801 C GLN A 6 50.291 -15.349 1.709 1.00 19.12 C ANISOU 801 C GLN B 6 2487 2358 2419 27 -80 30 C ATOM 802 O GLN A 6 49.815 -16.225 0.969 1.00 18.93 O ANISOU 802 O GLN B 6 2712 2111 2368 82 -98 37 O ATOM 803 CB GLN A 6 50.425 -16.608 3.905 1.00 19.72 C ANISOU 803 CB GLN B 6 2521 2456 2513 -49 -54 3 C ATOM 804 CG GLN A 6 51.398 -17.429 4.791 1.00 20.12 C ANISOU 804 CG GLN B 6 2608 2500 2536 -55 -78 127 C ATOM 805 CD GLN A 6 50.714 -18.332 5.815 1.00 21.59 C ANISOU 805 CD GLN B 6 2779 2715 2706 -43 -54 22 C ATOM 806 OE1 GLN A 6 49.674 -17.982 6.394 1.00 20.65 O ANISOU 806 OE1 GLN B 6 2824 2451 2571 -55 169 -80 O ATOM 807 NE2 GLN A 6 51.306 -19.511 6.042 1.00 21.99 N ANISOU 807 NE2 GLN B 6 2877 2697 2778 46 -62 156 N ATOM 808 N ALA A 7 50.055 -14.053 1.525 1.00 18.75 N ANISOU 808 N ALA B 7 2467 2274 2384 -35 -51 -4 N ATOM 809 CA ALA A 7 49.189 -13.587 0.429 1.00 18.24 C ANISOU 809 CA ALA B 7 2337 2229 2363 26 -1 42 C ATOM 810 C ALA A 7 49.806 -12.450 -0.379 1.00 17.96 C ANISOU 810 C ALA B 7 2315 2194 2315 11 5 -14 C ATOM 811 O ALA A 7 49.173 -11.932 -1.310 1.00 17.29 O ANISOU 811 O ALA B 7 2299 2003 2266 -53 16 31 O ATOM 812 CB ALA A 7 47.806 -13.161 0.986 1.00 18.83 C ANISOU 812 CB ALA B 7 2444 2292 2415 34 88 -11 C ATOM 813 N CYS A 8 51.046 -12.099 -0.039 1.00 17.41 N ANISOU 813 N CYS B 8 2259 2106 2247 30 -16 -27 N ATOM 814 CA CYS A 8 51.703 -10.880 -0.519 1.00 17.42 C ANISOU 814 CA CYS B 8 2235 2151 2231 60 -2 22 C ATOM 815 C CYS A 8 53.060 -11.154 -1.140 1.00 17.70 C ANISOU 815 C CYS B 8 2278 2184 2262 20 -24 -1 C ATOM 816 O CYS A 8 53.670 -12.184 -0.862 1.00 17.43 O ANISOU 816 O CYS B 8 2257 2095 2270 54 11 147 O ATOM 817 CB CYS A 8 51.873 -9.899 0.642 1.00 17.18 C ANISOU 817 CB CYS B 8 2193 2099 2232 32 -69 50 C ATOM 818 SG CYS A 8 50.331 -9.456 1.431 1.00 17.62 S ANISOU 818 SG CYS B 8 2312 2067 2314 151 -54 57 S ATOM 819 N TYR A 9 53.528 -10.197 -1.946 1.00 17.09 N ANISOU 819 N TYR B 9 2256 2133 2103 17 -8 -7 N ATOM 820 CA TYR A 9 54.670 -10.357 -2.833 1.00 17.64 C ANISOU 820 CA TYR B 9 2286 2187 2226 31 -30 36 C ATOM 821 C TYR A 9 55.438 -9.053 -2.951 1.00 17.21 C ANISOU 821 C TYR B 9 2225 2170 2141 -11 -34 -24 C ATOM 822 O TYR A 9 54.847 -7.964 -2.825 1.00 16.54 O ANISOU 822 O TYR B 9 2146 2054 2083 92 -2 97 O ATOM 823 CB TYR A 9 54.169 -10.752 -4.230 1.00 17.79 C ANISOU 823 CB TYR B 9 2329 2198 2230 -17 -12 -82 C ATOM 824 CG TYR A 9 53.430 -12.062 -4.203 1.00 18.46 C ANISOU 824 CG TYR B 9 2421 2357 2234 -6 -16 34 C ATOM 825 CD1 TYR A 9 54.123 -13.259 -4.336 1.00 18.84 C ANISOU 825 CD1 TYR B 9 2610 2305 2243 47 31 -69 C ATOM 826 CD2 TYR A 9 52.053 -12.108 -3.996 1.00 16.98 C ANISOU 826 CD2 TYR B 9 2116 2268 2065 -1 -67 -89 C ATOM 827 CE1 TYR A 9 53.474 -14.464 -4.275 1.00 18.87 C ANISOU 827 CE1 TYR B 9 2449 2382 2338 -82 -3 -98 C ATOM 828 CE2 TYR A 9 51.384 -13.327 -3.920 1.00 17.73 C ANISOU 828 CE2 TYR B 9 2349 2145 2242 65 -75 18 C ATOM 829 CZ TYR A 9 52.105 -14.503 -4.073 1.00 19.05 C ANISOU 829 CZ TYR B 9 2473 2438 2327 53 -34 -66 C ATOM 830 OH TYR A 9 51.482 -15.728 -4.008 1.00 17.92 O ANISOU 830 OH TYR B 9 2365 2198 2246 -19 -10 73 O ATOM 831 N ASN A 10 56.745 -9.161 -3.195 1.00 16.86 N ANISOU 831 N ASN B 10 2214 2117 2075 60 -31 -46 N ATOM 832 CA ASN A 10 57.595 -7.980 -3.446 1.00 17.45 C ANISOU 832 CA ASN B 10 2197 2248 2185 14 11 -15 C ATOM 833 C ASN A 10 57.526 -6.947 -2.327 1.00 17.32 C ANISOU 833 C ASN B 10 2199 2223 2158 -1 -5 7 C ATOM 834 O ASN A 10 57.414 -5.735 -2.559 1.00 17.17 O ANISOU 834 O ASN B 10 2270 2172 2080 -56 23 -30 O ATOM 835 CB ASN A 10 57.218 -7.360 -4.781 1.00 17.77 C ANISOU 835 CB ASN B 10 2273 2268 2209 17 63 16 C ATOM 836 CG ASN A 10 57.083 -8.412 -5.875 1.00 20.75 C ANISOU 836 CG ASN B 10 2735 2602 2547 7 54 -47 C ATOM 837 OD1 ASN A 10 57.920 -9.313 -5.984 1.00 20.86 O ANISOU 837 OD1 ASN B 10 2841 2574 2511 207 246 -116 O ATOM 838 ND2 ASN A 10 56.014 -8.325 -6.654 1.00 23.01 N ANISOU 838 ND2 ASN B 10 2999 3033 2708 -88 -110 -96 N ATOM 839 N SER A 11 57.581 -7.456 -1.106 1.00 17.10 N ANISOU 839 N SER B 11 2097 2243 2156 -14 -12 31 N ATOM 840 CA SER A 11 57.546 -6.637 0.084 1.00 16.45 C ANISOU 840 CA SER B 11 2071 2086 2089 -61 -17 2 C ATOM 841 C SER A 11 58.859 -5.893 0.231 1.00 16.87 C ANISOU 841 C SER B 11 2094 2189 2127 -49 -45 -15 C ATOM 842 O SER A 11 59.925 -6.376 -0.198 1.00 16.79 O ANISOU 842 O SER B 11 2038 2190 2150 -67 -48 -92 O ATOM 843 CB SER A 11 57.291 -7.496 1.321 1.00 16.36 C ANISOU 843 CB SER B 11 2122 2064 2029 -53 -44 12 C ATOM 844 OG SER A 11 56.055 -8.158 1.198 1.00 15.99 O ANISOU 844 OG SER B 11 2108 1989 1976 -81 -35 134 O ATOM 845 N ALA A 12 58.773 -4.714 0.815 1.00 16.14 N ANISOU 845 N ALA B 12 2051 2069 2010 -79 -43 -21 N ATOM 846 CA ALA A 12 59.960 -3.892 1.014 1.00 17.26 C ANISOU 846 CA ALA B 12 2286 2146 2126 -103 -33 -59 C ATOM 847 C ALA A 12 59.772 -3.037 2.255 1.00 16.95 C ANISOU 847 C ALA B 12 2222 2133 2085 -62 23 -81 C ATOM 848 O ALA A 12 58.660 -2.629 2.567 1.00 16.74 O ANISOU 848 O ALA B 12 2211 2047 2102 -108 -17 -137 O ATOM 849 CB ALA A 12 60.210 -2.997 -0.214 1.00 17.14 C ANISOU 849 CB ALA B 12 2315 2109 2089 -171 44 -47 C ATOM 850 N ILE A 13 60.870 -2.768 2.947 1.00 17.05 N ANISOU 850 N ILE B 13 2201 2130 2143 -59 30 -116 N ATOM 851 CA ILE A 13 60.851 -1.831 4.068 1.00 17.58 C ANISOU 851 CA ILE B 13 2259 2180 2240 -79 -16 -32 C ATOM 852 C ILE A 13 61.758 -0.655 3.709 1.00 17.36 C ANISOU 852 C ILE B 13 2180 2175 2240 -71 23 -74 C ATOM 853 O ILE A 13 62.875 -0.860 3.245 1.00 15.69 O ANISOU 853 O ILE B 13 1874 1942 2146 3 100 -109 O ATOM 854 CB ILE A 13 61.246 -2.511 5.392 1.00 17.68 C ANISOU 854 CB ILE B 13 2283 2197 2236 -68 20 -63 C ATOM 855 CG1 ILE A 13 60.108 -3.454 5.844 1.00 17.65 C ANISOU 855 CG1 ILE B 13 2275 2179 2252 -87 -149 65 C ATOM 856 CG2 ILE A 13 61.617 -1.441 6.492 1.00 17.32 C ANISOU 856 CG2 ILE B 13 2155 2209 2214 -53 -52 -100 C ATOM 857 CD1 ILE A 13 60.465 -4.393 6.997 1.00 19.11 C ANISOU 857 CD1 ILE B 13 2523 2319 2418 -88 -66 71 C ATOM 858 N GLN A 14 61.231 0.559 3.867 1.00 16.17 N ANISOU 858 N GLN B 14 2096 1977 2071 -8 -23 -4 N ATOM 859 CA GLN A 14 62.019 1.792 3.743 1.00 16.88 C ANISOU 859 CA GLN B 14 2186 2153 2072 -3 10 -15 C ATOM 860 C GLN A 14 61.704 2.652 4.975 1.00 16.13 C ANISOU 860 C GLN B 14 2099 1995 2033 12 10 -6 C ATOM 861 O GLN A 14 60.530 2.982 5.233 1.00 14.47 O ANISOU 861 O GLN B 14 1871 1803 1822 25 -45 80 O ATOM 862 CB GLN A 14 61.663 2.530 2.444 1.00 17.66 C ANISOU 862 CB GLN B 14 2278 2246 2186 -16 26 30 C ATOM 863 CG GLN A 14 62.449 3.824 2.213 1.00 21.81 C ANISOU 863 CG GLN B 14 2843 2701 2740 -20 79 88 C ATOM 864 CD GLN A 14 63.952 3.591 2.081 1.00 26.21 C ANISOU 864 CD GLN B 14 3103 3442 3412 13 92 55 C ATOM 865 OE1 GLN A 14 64.386 2.604 1.491 1.00 27.34 O ANISOU 865 OE1 GLN B 14 3440 3382 3562 64 184 -29 O ATOM 866 NE2 GLN A 14 64.747 4.498 2.635 1.00 27.52 N ANISOU 866 NE2 GLN B 14 3259 3535 3661 -51 22 -57 N ATOM 867 N GLY A 15 62.740 2.990 5.739 1.00 15.67 N ANISOU 867 N GLY B 15 2072 2001 1880 23 32 -45 N ATOM 868 CA GLY A 15 62.547 3.640 7.042 1.00 15.92 C ANISOU 868 CA GLY B 15 2069 2050 1930 20 1 -94 C ATOM 869 C GLY A 15 61.575 2.827 7.880 1.00 16.05 C ANISOU 869 C GLY B 15 2100 2064 1934 10 -29 -69 C ATOM 870 O GLY A 15 61.828 1.658 8.159 1.00 16.94 O ANISOU 870 O GLY B 15 2248 2174 2013 12 0 -147 O ATOM 871 N SER A 16 60.457 3.426 8.290 1.00 15.75 N ANISOU 871 N SER B 16 2042 2016 1925 12 -11 -79 N ATOM 872 CA SER A 16 59.470 2.682 9.104 1.00 15.04 C ANISOU 872 CA SER B 16 1990 1873 1849 -10 -42 -37 C ATOM 873 C SER A 16 58.294 2.070 8.307 1.00 15.12 C ANISOU 873 C SER B 16 1966 1904 1874 -18 -34 -9 C ATOM 874 O SER A 16 57.325 1.573 8.895 1.00 14.62 O ANISOU 874 O SER B 16 2043 1763 1746 -20 -12 20 O ATOM 875 CB SER A 16 58.958 3.537 10.277 1.00 14.91 C ANISOU 875 CB SER B 16 1963 1845 1855 24 -55 6 C ATOM 876 OG SER A 16 58.197 4.651 9.837 1.00 13.99 O ANISOU 876 OG SER B 16 1930 1625 1759 23 -60 -23 O ATOM 877 N VAL A 17 58.377 2.110 6.975 1.00 14.16 N ANISOU 877 N VAL B 17 1883 1717 1779 -41 -11 -56 N ATOM 878 CA VAL A 17 57.219 1.775 6.139 1.00 13.91 C ANISOU 878 CA VAL B 17 1834 1678 1773 -1 -22 -33 C ATOM 879 C VAL A 17 57.412 0.419 5.465 1.00 13.97 C ANISOU 879 C VAL B 17 1779 1676 1850 -3 -16 -20 C ATOM 880 O VAL A 17 58.395 0.207 4.766 1.00 12.57 O ANISOU 880 O VAL B 17 1551 1391 1831 -51 -5 -86 O ATOM 881 CB VAL A 17 56.973 2.850 5.035 1.00 14.73 C ANISOU 881 CB VAL B 17 1943 1783 1868 -7 -20 -59 C ATOM 882 CG1 VAL A 17 55.752 2.488 4.190 1.00 14.43 C ANISOU 882 CG1 VAL B 17 1958 1849 1672 3 -41 20 C ATOM 883 CG2 VAL A 17 56.795 4.272 5.663 1.00 15.71 C ANISOU 883 CG2 VAL B 17 2119 1883 1966 -5 50 -124 C ATOM 884 N LEU A 18 56.436 -0.468 5.653 1.00 13.69 N ANISOU 884 N LEU B 18 1733 1634 1834 16 -5 28 N ATOM 885 CA LEU A 18 56.333 -1.705 4.897 1.00 14.70 C ANISOU 885 CA LEU B 18 1868 1811 1906 11 14 33 C ATOM 886 C LEU A 18 55.364 -1.508 3.745 1.00 14.36 C ANISOU 886 C LEU B 18 1842 1779 1831 -35 -10 -38 C ATOM 887 O LEU A 18 54.242 -1.028 3.942 1.00 14.52 O ANISOU 887 O LEU B 18 1927 1809 1781 -29 40 -73 O ATOM 888 CB LEU A 18 55.808 -2.833 5.804 1.00 15.01 C ANISOU 888 CB LEU B 18 1881 1803 2018 4 -25 114 C ATOM 889 CG LEU A 18 55.362 -4.114 5.091 1.00 14.20 C ANISOU 889 CG LEU B 18 1778 1762 1855 18 -43 82 C ATOM 890 CD1 LEU A 18 56.562 -4.902 4.551 1.00 15.17 C ANISOU 890 CD1 LEU B 18 2048 1725 1989 29 -20 131 C ATOM 891 CD2 LEU A 18 54.523 -4.969 6.043 1.00 14.49 C ANISOU 891 CD2 LEU B 18 1775 1824 1904 11 -46 56 C ATOM 892 N THR A 19 55.808 -1.837 2.535 1.00 15.15 N ANISOU 892 N THR B 19 1963 1837 1954 21 10 11 N ATOM 893 CA THR A 19 54.945 -1.832 1.361 1.00 15.42 C ANISOU 893 CA THR B 19 2013 1917 1929 -50 12 -22 C ATOM 894 C THR A 19 54.901 -3.216 0.746 1.00 15.92 C ANISOU 894 C THR B 19 2061 1979 2009 -53 -3 9 C ATOM 895 O THR A 19 55.924 -3.880 0.608 1.00 15.41 O ANISOU 895 O THR B 19 2031 1931 1891 -57 17 -132 O ATOM 896 CB THR A 19 55.484 -0.829 0.296 1.00 15.75 C ANISOU 896 CB THR B 19 2125 1890 1969 -42 1 43 C ATOM 897 OG1 THR A 19 55.535 0.478 0.878 1.00 15.96 O ANISOU 897 OG1 THR B 19 2108 1940 2016 -90 63 33 O ATOM 898 CG2 THR A 19 54.615 -0.826 -0.979 1.00 15.61 C ANISOU 898 CG2 THR B 19 1914 1942 2075 -51 73 -21 C ATOM 899 N SER A 20 53.708 -3.664 0.379 1.00 16.79 N ANISOU 899 N SER B 20 2189 2071 2116 -73 -8 -21 N ATOM 900 CA SER A 20 53.618 -4.967 -0.259 1.00 17.04 C ANISOU 900 CA SER B 20 2236 2056 2182 -53 -14 -7 C ATOM 901 C SER A 20 52.549 -5.004 -1.311 1.00 16.70 C ANISOU 901 C SER B 20 2164 2074 2105 -56 5 25 C ATOM 902 O SER A 20 51.648 -4.148 -1.329 1.00 16.23 O ANISOU 902 O SER B 20 2232 1801 2133 -100 34 -57 O ATOM 903 CB SER A 20 53.364 -6.070 0.773 1.00 17.61 C ANISOU 903 CB SER B 20 2334 2185 2169 -9 -31 18 C ATOM 904 OG SER A 20 53.686 -7.332 0.212 1.00 17.60 O ANISOU 904 OG SER B 20 2411 1864 2411 94 -78 222 O ATOM 905 N THR A 21 52.647 -6.021 -2.169 1.00 15.77 N ANISOU 905 N THR B 21 2043 1965 1982 -42 7 0 N ATOM 906 CA THR A 21 51.648 -6.274 -3.216 1.00 16.28 C ANISOU 906 CA THR B 21 2079 2053 2051 -56 -17 -24 C ATOM 907 C THR A 21 50.963 -7.611 -2.915 1.00 15.95 C ANISOU 907 C THR B 21 2091 2015 1953 -30 -42 1 C ATOM 908 O THR A 21 51.609 -8.662 -2.888 1.00 15.67 O ANISOU 908 O THR B 21 2122 1889 1941 -152 -4 15 O ATOM 909 CB THR A 21 52.293 -6.243 -4.607 1.00 16.25 C ANISOU 909 CB THR B 21 2070 2086 2016 -48 -93 9 C ATOM 910 OG1 THR A 21 52.915 -4.963 -4.799 1.00 17.68 O ANISOU 910 OG1 THR B 21 2299 2196 2220 -61 -69 20 O ATOM 911 CG2 THR A 21 51.256 -6.506 -5.733 1.00 16.01 C ANISOU 911 CG2 THR B 21 2009 2048 2025 -26 -34 -81 C ATOM 912 N CYS A 22 49.655 -7.544 -2.679 1.00 16.48 N ANISOU 912 N CYS B 22 2146 2023 2091 -63 -42 50 N ATOM 913 CA CYS A 22 48.897 -8.643 -2.084 1.00 16.99 C ANISOU 913 CA CYS B 22 2222 2068 2164 -35 -74 7 C ATOM 914 C CYS A 22 47.717 -9.068 -2.938 1.00 16.50 C ANISOU 914 C CYS B 22 2140 2034 2093 -28 -56 -31 C ATOM 915 O CYS A 22 47.070 -8.251 -3.590 1.00 16.36 O ANISOU 915 O CYS B 22 2219 1961 2034 -33 -117 -129 O ATOM 916 CB CYS A 22 48.416 -8.262 -0.677 1.00 17.38 C ANISOU 916 CB CYS B 22 2277 2093 2233 -14 -84 27 C ATOM 917 SG CYS A 22 49.767 -7.752 0.465 1.00 16.28 S ANISOU 917 SG CYS B 22 2251 1902 2030 -44 -172 73 S ATOM 918 N ILE A 23 47.427 -10.360 -2.904 1.00 16.81 N ANISOU 918 N ILE B 23 2142 2104 2139 31 -43 -14 N ATOM 919 CA ILE A 23 46.294 -10.920 -3.647 1.00 16.75 C ANISOU 919 CA ILE B 23 2138 2041 2185 -50 -35 -13 C ATOM 920 C ILE A 23 44.975 -10.500 -2.982 1.00 16.61 C ANISOU 920 C ILE B 23 2132 2023 2155 -13 -38 -11 C ATOM 921 O ILE A 23 44.776 -10.738 -1.791 1.00 16.74 O ANISOU 921 O ILE B 23 2145 2015 2198 15 -97 -8 O ATOM 922 CB ILE A 23 46.411 -12.465 -3.752 1.00 16.77 C ANISOU 922 CB ILE B 23 2100 2083 2187 47 -29 0 C ATOM 923 CG1 ILE A 23 47.617 -12.847 -4.623 1.00 17.02 C ANISOU 923 CG1 ILE B 23 2120 2101 2246 -33 56 26 C ATOM 924 CG2 ILE A 23 45.115 -13.085 -4.321 1.00 15.81 C ANISOU 924 CG2 ILE B 23 2081 1883 2041 -124 9 83 C ATOM 925 CD1 ILE A 23 48.013 -14.361 -4.580 1.00 16.61 C ANISOU 925 CD1 ILE B 23 2158 2002 2147 -32 -38 10 C ATOM 926 N ARG A 24 44.094 -9.856 -3.753 1.00 17.06 N ANISOU 926 N ARG B 24 2212 2047 2221 -5 -14 23 N ATOM 927 CA ARG A 24 42.764 -9.452 -3.284 1.00 17.28 C ANISOU 927 CA ARG B 24 2216 2174 2174 -16 -30 69 C ATOM 928 C ARG A 24 41.889 -10.694 -3.119 1.00 17.22 C ANISOU 928 C ARG B 24 2194 2200 2148 -42 -13 25 C ATOM 929 O ARG A 24 42.118 -11.716 -3.769 1.00 16.48 O ANISOU 929 O ARG B 24 2081 2152 2029 -112 36 -24 O ATOM 930 CB ARG A 24 42.118 -8.443 -4.259 1.00 17.06 C ANISOU 930 CB ARG B 24 2168 2108 2206 4 -67 34 C ATOM 931 CG ARG A 24 42.986 -7.206 -4.567 1.00 18.04 C ANISOU 931 CG ARG B 24 2358 2168 2325 56 20 154 C ATOM 932 CD ARG A 24 42.335 -6.237 -5.583 1.00 18.99 C ANISOU 932 CD ARG B 24 2310 2403 2501 11 -2 154 C ATOM 933 NE ARG A 24 42.013 -6.873 -6.864 1.00 22.63 N ANISOU 933 NE ARG B 24 3045 2765 2785 97 -6 98 N ATOM 934 CZ ARG A 24 41.979 -6.255 -8.051 1.00 24.77 C ANISOU 934 CZ ARG B 24 3268 3052 3092 33 35 72 C ATOM 935 NH1 ARG A 24 42.273 -4.963 -8.150 1.00 23.89 N ANISOU 935 NH1 ARG B 24 3279 2851 2945 -53 40 68 N ATOM 936 NH2 ARG A 24 41.656 -6.941 -9.150 1.00 23.21 N ANISOU 936 NH2 ARG B 24 3072 2794 2952 67 30 45 N ATOM 937 N THR A 25 40.891 -10.613 -2.247 1.00 18.11 N ANISOU 937 N THR B 25 2314 2302 2264 -44 3 -35 N ATOM 938 CA THR A 25 40.080 -11.785 -1.885 1.00 18.84 C ANISOU 938 CA THR B 25 2317 2456 2385 -65 15 4 C ATOM 939 C THR A 25 39.518 -12.515 -3.111 1.00 19.31 C ANISOU 939 C THR B 25 2450 2477 2407 -45 22 4 C ATOM 940 O THR A 25 39.572 -13.744 -3.198 1.00 19.17 O ANISOU 940 O THR B 25 2440 2496 2344 -31 0 9 O ATOM 941 CB THR A 25 38.936 -11.373 -0.934 1.00 19.55 C ANISOU 941 CB THR B 25 2513 2494 2419 -118 70 -33 C ATOM 942 OG1 THR A 25 39.502 -10.836 0.261 1.00 19.08 O ANISOU 942 OG1 THR B 25 2134 2763 2352 -56 -3 20 O ATOM 943 CG2 THR A 25 38.029 -12.561 -0.581 1.00 20.14 C ANISOU 943 CG2 THR B 25 2444 2656 2550 -99 77 79 C ATOM 944 N ASN A 26 39.004 -11.745 -4.063 1.00 19.28 N ANISOU 944 N ASN B 26 2371 2496 2455 -30 5 20 N ATOM 945 CA ASN A 26 38.329 -12.315 -5.233 1.00 19.49 C ANISOU 945 CA ASN B 26 2473 2441 2491 -33 33 3 C ATOM 946 C ASN A 26 39.204 -12.400 -6.486 1.00 18.42 C ANISOU 946 C ASN B 26 2346 2272 2381 24 -10 -7 C ATOM 947 O ASN A 26 38.736 -12.790 -7.537 1.00 17.70 O ANISOU 947 O ASN B 26 2217 2196 2310 -15 8 7 O ATOM 948 CB ASN A 26 37.048 -11.529 -5.515 1.00 20.22 C ANISOU 948 CB ASN B 26 2512 2559 2610 -29 34 -39 C ATOM 949 CG ASN A 26 35.974 -11.771 -4.460 1.00 25.27 C ANISOU 949 CG ASN B 26 3081 3220 3300 -31 152 18 C ATOM 950 OD1 ASN A 26 35.422 -10.828 -3.881 1.00 29.58 O ANISOU 950 OD1 ASN B 26 3860 3700 3677 52 308 -275 O ATOM 951 ND2 ASN A 26 35.665 -13.023 -4.219 1.00 24.59 N ANISOU 951 ND2 ASN B 26 2854 3084 3403 4 142 153 N ATOM 952 N GLY A 27 40.474 -12.018 -6.361 1.00 17.27 N ANISOU 952 N GLY B 27 2264 2078 2218 14 12 30 N ATOM 953 CA GLY A 27 41.405 -12.085 -7.471 1.00 16.77 C ANISOU 953 CA GLY B 27 2175 2027 2168 58 -31 -3 C ATOM 954 C GLY A 27 42.080 -10.771 -7.791 1.00 15.85 C ANISOU 954 C GLY B 27 2063 1966 1991 -2 -38 -9 C ATOM 955 O GLY A 27 41.579 -9.692 -7.436 1.00 15.98 O ANISOU 955 O GLY B 27 2104 2005 1960 78 -20 58 O ATOM 956 N GLY A 28 43.211 -10.862 -8.477 1.00 15.32 N ANISOU 956 N GLY B 28 2012 1852 1955 30 -67 -37 N ATOM 957 CA GLY A 28 44.032 -9.691 -8.790 1.00 15.12 C ANISOU 957 CA GLY B 28 1968 1866 1910 13 -72 -40 C ATOM 958 C GLY A 28 44.801 -9.157 -7.587 1.00 15.63 C ANISOU 958 C GLY B 28 1985 1950 2001 0 -41 -41 C ATOM 959 O GLY A 28 44.794 -9.756 -6.494 1.00 14.72 O ANISOU 959 O GLY B 28 1881 1794 1915 -14 -103 55 O ATOM 960 N TYR A 29 45.456 -8.016 -7.781 1.00 15.27 N ANISOU 960 N TYR B 29 1962 1891 1948 -10 1 -45 N ATOM 961 CA TYR A 29 46.407 -7.531 -6.776 1.00 15.62 C ANISOU 961 CA TYR B 29 2001 1925 2007 1 -38 -22 C ATOM 962 C TYR A 29 46.186 -6.077 -6.378 1.00 15.79 C ANISOU 962 C TYR B 29 2050 1979 1970 22 -3 -33 C ATOM 963 O TYR A 29 45.673 -5.271 -7.155 1.00 15.39 O ANISOU 963 O TYR B 29 2024 1889 1934 97 -56 -38 O ATOM 964 CB TYR A 29 47.836 -7.665 -7.291 1.00 15.90 C ANISOU 964 CB TYR B 29 2048 1955 2037 -19 5 0 C ATOM 965 CG TYR A 29 48.311 -9.066 -7.608 1.00 15.59 C ANISOU 965 CG TYR B 29 1980 1994 1948 -35 35 19 C ATOM 966 CD1 TYR A 29 48.989 -9.826 -6.651 1.00 14.00 C ANISOU 966 CD1 TYR B 29 1654 1791 1872 -82 58 -31 C ATOM 967 CD2 TYR A 29 48.088 -9.627 -8.873 1.00 16.56 C ANISOU 967 CD2 TYR B 29 2156 2034 2101 -52 34 -14 C ATOM 968 CE1 TYR A 29 49.448 -11.114 -6.942 1.00 15.45 C ANISOU 968 CE1 TYR B 29 2093 1953 1823 -83 145 44 C ATOM 969 CE2 TYR A 29 48.548 -10.906 -9.186 1.00 16.74 C ANISOU 969 CE2 TYR B 29 2186 2014 2159 4 -3 -17 C ATOM 970 CZ TYR A 29 49.222 -11.644 -8.214 1.00 16.96 C ANISOU 970 CZ TYR B 29 2234 2024 2183 -74 -32 -80 C ATOM 971 OH TYR A 29 49.686 -12.891 -8.524 1.00 17.51 O ANISOU 971 OH TYR B 29 2321 2077 2254 21 78 65 O ATOM 972 N ASN A 30 46.575 -5.758 -5.151 1.00 15.75 N ANISOU 972 N ASN B 30 2011 1952 2019 -1 -54 -50 N ATOM 973 CA ASN A 30 46.613 -4.381 -4.696 1.00 16.25 C ANISOU 973 CA ASN B 30 2094 2002 2077 -19 -22 9 C ATOM 974 C ASN A 30 47.959 -4.127 -4.025 1.00 16.02 C ANISOU 974 C ASN B 30 2046 2002 2037 -5 -15 -6 C ATOM 975 O ASN A 30 48.530 -5.021 -3.414 1.00 15.95 O ANISOU 975 O ASN B 30 2024 1972 2064 -48 -69 28 O ATOM 976 CB ASN A 30 45.462 -4.091 -3.727 1.00 15.95 C ANISOU 976 CB ASN B 30 2089 1938 2033 46 -48 11 C ATOM 977 CG ASN A 30 45.376 -2.626 -3.361 1.00 17.97 C ANISOU 977 CG ASN B 30 2354 2210 2262 9 21 14 C ATOM 978 OD1 ASN A 30 45.298 -1.778 -4.236 1.00 18.92 O ANISOU 978 OD1 ASN B 30 2599 2235 2353 258 5 192 O ATOM 979 ND2 ASN A 30 45.420 -2.323 -2.070 1.00 16.71 N ANISOU 979 ND2 ASN B 30 2215 2118 2015 -169 49 25 N ATOM 980 N THR A 31 48.468 -2.908 -4.176 1.00 15.73 N ANISOU 980 N THR B 31 2001 1953 2019 -47 -14 -36 N ATOM 981 CA THR A 31 49.656 -2.467 -3.462 1.00 15.75 C ANISOU 981 CA THR B 31 1969 2016 1997 -9 3 -30 C ATOM 982 C THR A 31 49.253 -1.447 -2.388 1.00 15.69 C ANISOU 982 C THR B 31 1968 1941 2051 -30 -2 -19 C ATOM 983 O THR A 31 48.422 -0.552 -2.622 1.00 15.27 O ANISOU 983 O THR B 31 1850 1936 2015 0 -92 52 O ATOM 984 CB THR A 31 50.729 -1.937 -4.441 1.00 15.64 C ANISOU 984 CB THR B 31 1951 2010 1982 -34 0 -32 C ATOM 985 OG1 THR A 31 51.121 -3.011 -5.313 1.00 16.29 O ANISOU 985 OG1 THR B 31 2091 2115 1982 -164 42 -84 O ATOM 986 CG2 THR A 31 51.996 -1.384 -3.700 1.00 15.25 C ANISOU 986 CG2 THR B 31 1896 1976 1922 -30 22 -68 C ATOM 987 N SER A 32 49.821 -1.618 -1.202 1.00 15.50 N ANISOU 987 N SER B 32 1984 1948 1954 -6 4 -22 N ATOM 988 CA SER A 32 49.501 -0.782 -0.033 1.00 16.20 C ANISOU 988 CA SER B 32 2075 2008 2073 4 12 -60 C ATOM 989 C SER A 32 50.720 -0.676 0.883 1.00 15.93 C ANISOU 989 C SER B 32 2022 2007 2022 -20 11 -46 C ATOM 990 O SER A 32 51.648 -1.495 0.800 1.00 15.40 O ANISOU 990 O SER B 32 1923 1915 2013 -108 -25 6 O ATOM 991 CB SER A 32 48.299 -1.356 0.737 1.00 16.03 C ANISOU 991 CB SER B 32 2070 2011 2009 33 40 -20 C ATOM 992 OG SER A 32 48.652 -2.517 1.491 1.00 18.04 O ANISOU 992 OG SER B 32 2426 2132 2295 74 70 24 O ATOM 993 N SER A 33 50.714 0.336 1.748 1.00 15.86 N ANISOU 993 N SER B 33 2011 1992 2020 -42 -11 -37 N ATOM 994 CA SER A 33 51.808 0.565 2.685 1.00 15.64 C ANISOU 994 CA SER B 33 1987 1982 1973 35 28 -21 C ATOM 995 C SER A 33 51.244 0.655 4.091 1.00 15.57 C ANISOU 995 C SER B 33 1995 1978 1943 -13 15 15 C ATOM 996 O SER A 33 50.072 1.007 4.289 1.00 15.29 O ANISOU 996 O SER B 33 2050 1920 1839 103 21 9 O ATOM 997 CB SER A 33 52.561 1.869 2.356 1.00 16.00 C ANISOU 997 CB SER B 33 2002 2079 1998 -6 48 -24 C ATOM 998 OG SER A 33 53.262 1.782 1.122 1.00 15.63 O ANISOU 998 OG SER B 33 2148 1838 1952 10 23 -63 O ATOM 999 N ILE A 34 52.073 0.331 5.066 1.00 15.38 N ANISOU 999 N ILE B 34 1983 1878 1980 52 45 70 N ATOM 1000 CA ILE A 34 51.712 0.535 6.462 1.00 15.83 C ANISOU 1000 CA ILE B 34 2046 1980 1986 7 40 47 C ATOM 1001 C ILE A 34 52.906 1.076 7.216 1.00 15.52 C ANISOU 1001 C ILE B 34 2043 1898 1953 -1 33 67 C ATOM 1002 O ILE A 34 54.035 0.602 7.039 1.00 14.85 O ANISOU 1002 O ILE B 34 1916 1861 1864 -43 -22 32 O ATOM 1003 CB ILE A 34 51.171 -0.764 7.107 1.00 16.32 C ANISOU 1003 CB ILE B 34 2133 1990 2075 44 55 43 C ATOM 1004 CG1 ILE A 34 50.679 -0.508 8.543 1.00 17.07 C ANISOU 1004 CG1 ILE B 34 2179 2129 2175 -101 48 36 C ATOM 1005 CG2 ILE A 34 52.223 -1.922 6.986 1.00 17.53 C ANISOU 1005 CG2 ILE B 34 2264 2158 2235 157 43 71 C ATOM 1006 CD1 ILE A 34 49.695 -1.567 9.065 1.00 16.72 C ANISOU 1006 CD1 ILE B 34 2171 2176 2004 -53 112 82 C ATOM 1007 N ASP A 35 52.658 2.079 8.050 1.00 15.32 N ANISOU 1007 N ASP B 35 2028 1861 1932 -39 1 40 N ATOM 1008 CA ASP A 35 53.742 2.710 8.792 1.00 15.27 C ANISOU 1008 CA ASP B 35 2000 1852 1950 -6 -53 -11 C ATOM 1009 C ASP A 35 53.938 1.953 10.091 1.00 14.96 C ANISOU 1009 C ASP B 35 1914 1823 1946 -53 -45 -51 C ATOM 1010 O ASP A 35 53.151 2.076 11.024 1.00 15.57 O ANISOU 1010 O ASP B 35 1957 1888 2068 -88 -34 -61 O ATOM 1011 CB ASP A 35 53.458 4.203 9.044 1.00 15.58 C ANISOU 1011 CB ASP B 35 2055 1895 1968 -64 -85 6 C ATOM 1012 CG ASP A 35 54.603 4.894 9.749 1.00 16.34 C ANISOU 1012 CG ASP B 35 2179 1997 2031 -22 -67 -4 C ATOM 1013 OD1 ASP A 35 55.627 4.219 10.050 1.00 14.26 O ANISOU 1013 OD1 ASP B 35 1916 1681 1819 0 -85 -128 O ATOM 1014 OD2 ASP A 35 54.479 6.111 9.998 1.00 17.06 O ANISOU 1014 OD2 ASP B 35 2334 2027 2121 99 -133 -131 O ATOM 1015 N LEU A 36 54.992 1.152 10.141 1.00 14.60 N ANISOU 1015 N LEU B 36 1878 1776 1893 -24 -35 -29 N ATOM 1016 CA LEU A 36 55.236 0.313 11.303 1.00 14.17 C ANISOU 1016 CA LEU B 36 1811 1804 1766 39 -20 3 C ATOM 1017 C LEU A 36 55.551 1.116 12.571 1.00 14.31 C ANISOU 1017 C LEU B 36 1836 1788 1811 76 45 -15 C ATOM 1018 O LEU A 36 55.495 0.568 13.667 1.00 14.36 O ANISOU 1018 O LEU B 36 1898 1865 1691 61 103 4 O ATOM 1019 CB LEU A 36 56.370 -0.672 11.016 1.00 13.85 C ANISOU 1019 CB LEU B 36 1838 1696 1728 30 7 -1 C ATOM 1020 CG LEU A 36 56.133 -1.590 9.817 1.00 15.27 C ANISOU 1020 CG LEU B 36 2015 1881 1905 47 -12 -63 C ATOM 1021 CD1 LEU A 36 57.405 -2.354 9.479 1.00 17.51 C ANISOU 1021 CD1 LEU B 36 2160 2194 2296 190 -86 57 C ATOM 1022 CD2 LEU A 36 54.941 -2.547 10.097 1.00 15.87 C ANISOU 1022 CD2 LEU B 36 2071 1895 2062 -62 -191 -95 C ATOM 1023 N ASN A 37 55.909 2.391 12.413 1.00 14.49 N ANISOU 1023 N ASN B 37 1829 1888 1786 45 46 -1 N ATOM 1024 CA ASN A 37 56.215 3.268 13.542 1.00 14.77 C ANISOU 1024 CA ASN B 37 1882 1849 1880 -18 -13 10 C ATOM 1025 C ASN A 37 54.987 3.476 14.441 1.00 14.84 C ANISOU 1025 C ASN B 37 1938 1831 1869 22 -11 -8 C ATOM 1026 O ASN A 37 55.110 3.810 15.626 1.00 14.22 O ANISOU 1026 O ASN B 37 1877 1792 1730 -67 -75 18 O ATOM 1027 CB ASN A 37 56.762 4.618 13.049 1.00 14.53 C ANISOU 1027 CB ASN B 37 1837 1850 1834 4 -39 -1 C ATOM 1028 CG ASN A 37 57.567 5.326 14.108 1.00 15.27 C ANISOU 1028 CG ASN B 37 1909 1841 2049 -84 -16 36 C ATOM 1029 OD1 ASN A 37 58.404 4.703 14.789 1.00 13.84 O ANISOU 1029 OD1 ASN B 37 1703 1668 1888 -200 -126 16 O ATOM 1030 ND2 ASN A 37 57.321 6.630 14.275 1.00 14.23 N ANISOU 1030 ND2 ASN B 37 1828 1736 1843 28 51 -9 N ATOM 1031 N SER A 38 53.806 3.270 13.861 1.00 14.62 N ANISOU 1031 N SER B 38 1933 1768 1854 -16 -39 -16 N ATOM 1032 CA SER A 38 52.546 3.347 14.584 1.00 15.39 C ANISOU 1032 CA SER B 38 2035 1871 1940 44 -22 -61 C ATOM 1033 C SER A 38 52.382 2.274 15.668 1.00 15.41 C ANISOU 1033 C SER B 38 1997 1900 1955 42 2 -11 C ATOM 1034 O SER A 38 51.654 2.487 16.620 1.00 15.59 O ANISOU 1034 O SER B 38 2089 1923 1910 110 -4 41 O ATOM 1035 CB SER A 38 51.364 3.249 13.617 1.00 15.71 C ANISOU 1035 CB SER B 38 2058 1903 2008 39 -47 -94 C ATOM 1036 OG SER A 38 51.278 1.938 13.062 1.00 17.19 O ANISOU 1036 OG SER B 38 2300 2099 2130 -47 68 -230 O ATOM 1037 N VAL A 39 53.060 1.133 15.524 1.00 14.84 N ANISOU 1037 N VAL B 39 1894 1851 1891 40 -53 0 N ATOM 1038 CA VAL A 39 52.731 -0.037 16.348 1.00 14.73 C ANISOU 1038 CA VAL B 39 1828 1847 1921 20 0 -40 C ATOM 1039 C VAL A 39 53.911 -0.795 16.962 1.00 14.72 C ANISOU 1039 C VAL B 39 1839 1868 1886 -4 -23 -46 C ATOM 1040 O VAL A 39 53.723 -1.832 17.624 1.00 13.14 O ANISOU 1040 O VAL B 39 1507 1720 1763 -123 -37 1 O ATOM 1041 CB VAL A 39 51.810 -1.037 15.586 1.00 15.27 C ANISOU 1041 CB VAL B 39 1818 2013 1969 5 -53 6 C ATOM 1042 CG1 VAL A 39 50.403 -0.488 15.497 1.00 14.72 C ANISOU 1042 CG1 VAL B 39 1834 1784 1975 115 -25 -25 C ATOM 1043 CG2 VAL A 39 52.376 -1.397 14.187 1.00 14.10 C ANISOU 1043 CG2 VAL B 39 1828 1684 1844 -10 -34 -85 C ATOM 1044 N ILE A 40 55.127 -0.283 16.756 1.00 14.47 N ANISOU 1044 N ILE B 40 1830 1770 1895 -19 -4 -99 N ATOM 1045 CA ILE A 40 56.315 -0.966 17.261 1.00 15.46 C ANISOU 1045 CA ILE B 40 1959 1965 1947 -14 8 -67 C ATOM 1046 C ILE A 40 57.157 0.054 18.028 1.00 16.56 C ANISOU 1046 C ILE B 40 2098 2118 2073 -18 -7 -58 C ATOM 1047 O ILE A 40 57.292 1.215 17.590 1.00 15.50 O ANISOU 1047 O ILE B 40 2029 1998 1859 5 -8 -3 O ATOM 1048 CB ILE A 40 57.113 -1.604 16.094 1.00 15.59 C ANISOU 1048 CB ILE B 40 1918 1931 2072 6 0 -53 C ATOM 1049 CG1 ILE A 40 56.262 -2.697 15.405 1.00 15.19 C ANISOU 1049 CG1 ILE B 40 2003 1890 1876 71 -37 -128 C ATOM 1050 CG2 ILE A 40 58.473 -2.127 16.577 1.00 14.55 C ANISOU 1050 CG2 ILE B 40 1839 1878 1811 55 -91 -79 C ATOM 1051 CD1 ILE A 40 56.844 -3.258 14.091 1.00 16.68 C ANISOU 1051 CD1 ILE B 40 2170 2151 2016 -8 157 -17 C ATOM 1052 N GLU A 41 57.683 -0.367 19.179 1.00 17.32 N ANISOU 1052 N GLU B 41 2221 2194 2164 13 12 32 N ATOM 1053 CA GLU A 41 58.562 0.484 19.982 1.00 18.71 C ANISOU 1053 CA GLU B 41 2384 2403 2322 -25 2 -22 C ATOM 1054 C GLU A 41 59.927 -0.173 20.203 1.00 18.98 C ANISOU 1054 C GLU B 41 2430 2419 2362 -32 -10 0 C ATOM 1055 O GLU A 41 60.098 -1.374 19.998 1.00 18.88 O ANISOU 1055 O GLU B 41 2419 2404 2349 17 -50 -38 O ATOM 1056 CB GLU A 41 57.920 0.869 21.331 1.00 19.51 C ANISOU 1056 CB GLU B 41 2385 2494 2532 -7 -12 18 C ATOM 1057 CG GLU A 41 57.602 -0.293 22.263 1.00 20.26 C ANISOU 1057 CG GLU B 41 2613 2644 2440 -6 94 28 C ATOM 1058 CD GLU A 41 57.300 0.137 23.726 1.00 22.71 C ANISOU 1058 CD GLU B 41 2935 2990 2700 9 -37 -33 C ATOM 1059 OE1 GLU A 41 57.578 1.286 24.130 1.00 23.22 O ANISOU 1059 OE1 GLU B 41 3328 2620 2874 176 162 0 O ATOM 1060 OE2 GLU A 41 56.817 -0.717 24.482 1.00 24.06 O ANISOU 1060 OE2 GLU B 41 3191 3128 2820 -205 222 184 O ATOM 1061 N ASN A 42 60.896 0.646 20.593 1.00 19.08 N ANISOU 1061 N ASN B 42 2430 2489 2331 -68 -1 -29 N ATOM 1062 CA ASN A 42 62.205 0.180 20.974 1.00 19.31 C ANISOU 1062 CA ASN B 42 2474 2442 2419 -28 40 -23 C ATOM 1063 C ASN A 42 62.283 0.180 22.502 1.00 20.00 C ANISOU 1063 C ASN B 42 2534 2565 2497 -18 6 -45 C ATOM 1064 O ASN A 42 62.315 1.246 23.134 1.00 19.62 O ANISOU 1064 O ASN B 42 2502 2534 2416 5 48 -118 O ATOM 1065 CB ASN A 42 63.278 1.105 20.364 1.00 19.79 C ANISOU 1065 CB ASN B 42 2455 2535 2527 -41 56 -44 C ATOM 1066 CG ASN A 42 64.669 0.825 20.887 1.00 20.15 C ANISOU 1066 CG ASN B 42 2565 2528 2561 -70 36 -65 C ATOM 1067 OD1 ASN A 42 64.949 -0.257 21.398 1.00 21.37 O ANISOU 1067 OD1 ASN B 42 2513 2653 2953 27 -54 44 O ATOM 1068 ND2 ASN A 42 65.562 1.814 20.753 1.00 19.69 N ANISOU 1068 ND2 ASN B 42 2348 2615 2517 -205 67 -87 N ATOM 1069 N VAL A 43 62.300 -1.017 23.075 1.00 20.04 N ANISOU 1069 N VAL B 43 2539 2609 2465 -52 23 -3 N ATOM 1070 CA VAL A 43 62.513 -1.204 24.511 1.00 21.25 C ANISOU 1070 CA VAL B 43 2719 2747 2608 -61 -2 30 C ATOM 1071 C VAL A 43 63.917 -1.744 24.744 1.00 21.22 C ANISOU 1071 C VAL B 43 2685 2747 2630 -61 -2 34 C ATOM 1072 O VAL A 43 64.176 -2.924 24.533 1.00 20.71 O ANISOU 1072 O VAL B 43 2596 2730 2540 -125 -77 -14 O ATOM 1073 CB VAL A 43 61.476 -2.165 25.157 1.00 21.23 C ANISOU 1073 CB VAL B 43 2667 2782 2616 -46 7 63 C ATOM 1074 CG1 VAL A 43 61.655 -2.172 26.688 1.00 21.92 C ANISOU 1074 CG1 VAL B 43 2853 2877 2596 -37 52 61 C ATOM 1075 CG2 VAL A 43 60.053 -1.759 24.812 1.00 21.47 C ANISOU 1075 CG2 VAL B 43 2791 2791 2576 10 -51 162 C ATOM 1076 N ASP A 44 64.826 -0.861 25.159 1.00 22.46 N ANISOU 1076 N ASP B 44 2876 2868 2790 -41 -41 5 N ATOM 1077 CA ASP A 44 66.212 -1.231 25.457 1.00 23.32 C ANISOU 1077 CA ASP B 44 2959 2947 2954 -84 -32 42 C ATOM 1078 C ASP A 44 66.895 -2.019 24.328 1.00 22.85 C ANISOU 1078 C ASP B 44 2897 2822 2963 -106 -79 3 C ATOM 1079 O ASP A 44 67.564 -3.010 24.580 1.00 23.50 O ANISOU 1079 O ASP B 44 3072 2796 3058 -113 -106 31 O ATOM 1080 CB ASP A 44 66.269 -1.988 26.806 1.00 23.97 C ANISOU 1080 CB ASP B 44 3051 3010 3044 -95 -44 84 C ATOM 1081 CG ASP A 44 67.678 -2.123 27.374 1.00 25.03 C ANISOU 1081 CG ASP B 44 3170 3093 3244 -40 -34 117 C ATOM 1082 OD1 ASP A 44 68.530 -1.196 27.249 1.00 23.81 O ANISOU 1082 OD1 ASP B 44 3118 2947 2979 -192 -32 185 O ATOM 1083 OD2 ASP A 44 67.915 -3.183 27.989 1.00 24.80 O ANISOU 1083 OD2 ASP B 44 3136 3176 3108 57 -32 214 O ATOM 1084 N GLY A 45 66.753 -1.558 23.085 1.00 21.67 N ANISOU 1084 N GLY B 45 2739 2661 2833 -143 -61 11 N ATOM 1085 CA GLY A 45 67.464 -2.160 21.956 1.00 21.13 C ANISOU 1085 CA GLY B 45 2587 2658 2782 -133 -58 -5 C ATOM 1086 C GLY A 45 66.698 -3.252 21.231 1.00 21.07 C ANISOU 1086 C GLY B 45 2628 2658 2719 -68 -20 -19 C ATOM 1087 O GLY A 45 67.176 -3.787 20.228 1.00 20.84 O ANISOU 1087 O GLY B 45 2479 2648 2788 -107 -33 -13 O ATOM 1088 N SER A 46 65.496 -3.542 21.731 1.00 20.25 N ANISOU 1088 N SER B 46 2511 2584 2596 -72 -62 32 N ATOM 1089 CA SER A 46 64.637 -4.602 21.219 1.00 20.42 C ANISOU 1089 CA SER B 46 2564 2580 2613 -51 -46 26 C ATOM 1090 C SER A 46 63.334 -4.049 20.681 1.00 19.65 C ANISOU 1090 C SER B 46 2476 2461 2527 -55 -30 3 C ATOM 1091 O SER A 46 62.612 -3.352 21.388 1.00 19.99 O ANISOU 1091 O SER B 46 2541 2491 2563 -111 -76 -4 O ATOM 1092 CB SER A 46 64.296 -5.581 22.331 1.00 20.75 C ANISOU 1092 CB SER B 46 2574 2633 2678 -24 -39 56 C ATOM 1093 OG SER A 46 65.352 -6.484 22.519 1.00 24.14 O ANISOU 1093 OG SER B 46 2995 3015 3162 81 31 89 O ATOM 1094 N LEU A 47 63.032 -4.395 19.434 1.00 19.12 N ANISOU 1094 N LEU B 47 2444 2389 2431 -17 -13 27 N ATOM 1095 CA LEU A 47 61.759 -4.068 18.811 1.00 18.59 C ANISOU 1095 CA LEU B 47 2375 2354 2335 12 -19 -4 C ATOM 1096 C LEU A 47 60.645 -4.900 19.431 1.00 18.75 C ANISOU 1096 C LEU B 47 2391 2391 2343 -8 -61 3 C ATOM 1097 O LEU A 47 60.748 -6.123 19.514 1.00 19.14 O ANISOU 1097 O LEU B 47 2393 2406 2472 -75 -42 11 O ATOM 1098 CB LEU A 47 61.816 -4.339 17.300 1.00 18.31 C ANISOU 1098 CB LEU B 47 2338 2320 2297 27 13 12 C ATOM 1099 CG LEU A 47 62.770 -3.511 16.438 1.00 17.30 C ANISOU 1099 CG LEU B 47 2247 2117 2206 67 3 52 C ATOM 1100 CD1 LEU A 47 62.929 -4.221 15.119 1.00 17.27 C ANISOU 1100 CD1 LEU B 47 2229 2329 2001 -75 -24 56 C ATOM 1101 CD2 LEU A 47 62.259 -2.077 16.230 1.00 17.34 C ANISOU 1101 CD2 LEU B 47 2354 2058 2176 -10 104 4 C ATOM 1102 N LYS A 48 59.581 -4.229 19.852 1.00 18.68 N ANISOU 1102 N LYS B 48 2378 2431 2288 1 -33 -36 N ATOM 1103 CA LYS A 48 58.450 -4.868 20.512 1.00 19.48 C ANISOU 1103 CA LYS B 48 2471 2536 2393 -24 -50 21 C ATOM 1104 C LYS A 48 57.128 -4.295 20.034 1.00 19.01 C ANISOU 1104 C LYS B 48 2418 2485 2318 -10 -72 8 C ATOM 1105 O LYS A 48 57.053 -3.117 19.701 1.00 18.65 O ANISOU 1105 O LYS B 48 2328 2451 2307 -3 -157 2 O ATOM 1106 CB LYS A 48 58.548 -4.659 22.033 1.00 20.11 C ANISOU 1106 CB LYS B 48 2550 2707 2381 -25 0 8 C ATOM 1107 CG LYS A 48 59.841 -5.229 22.597 1.00 23.45 C ANISOU 1107 CG LYS B 48 2743 3252 2912 37 -42 76 C ATOM 1108 CD LYS A 48 59.700 -5.910 23.921 1.00 28.18 C ANISOU 1108 CD LYS B 48 3534 3676 3494 10 -36 236 C ATOM 1109 CE LYS A 48 61.025 -6.583 24.271 1.00 30.30 C ANISOU 1109 CE LYS B 48 3649 3995 3867 41 -89 52 C ATOM 1110 NZ LYS A 48 61.226 -7.929 23.611 1.00 31.36 N ANISOU 1110 NZ LYS B 48 3933 3965 4016 24 46 -98 N ATOM 1111 N TRP A 49 56.080 -5.116 20.039 1.00 19.31 N ANISOU 1111 N TRP B 49 2463 2507 2365 5 -53 19 N ATOM 1112 CA TRP A 49 54.723 -4.631 19.744 1.00 19.91 C ANISOU 1112 CA TRP B 49 2521 2546 2495 -7 4 -1 C ATOM 1113 C TRP A 49 54.178 -3.856 20.949 1.00 21.37 C ANISOU 1113 C TRP B 49 2741 2725 2651 -32 22 -19 C ATOM 1114 O TRP A 49 54.855 -3.758 21.963 1.00 21.66 O ANISOU 1114 O TRP B 49 2771 2798 2661 34 60 71 O ATOM 1115 CB TRP A 49 53.792 -5.800 19.435 1.00 18.85 C ANISOU 1115 CB TRP B 49 2407 2409 2346 -19 -1 -4 C ATOM 1116 CG TRP A 49 54.202 -6.664 18.264 1.00 17.43 C ANISOU 1116 CG TRP B 49 2250 2168 2204 -61 22 20 C ATOM 1117 CD1 TRP A 49 54.725 -7.927 18.322 1.00 16.49 C ANISOU 1117 CD1 TRP B 49 1978 2114 2170 -35 -2 -17 C ATOM 1118 CD2 TRP A 49 54.113 -6.333 16.866 1.00 17.31 C ANISOU 1118 CD2 TRP B 49 2118 2228 2231 6 -1 17 C ATOM 1119 NE1 TRP A 49 54.966 -8.400 17.049 1.00 16.85 N ANISOU 1119 NE1 TRP B 49 2190 2012 2197 -51 -47 39 N ATOM 1120 CE2 TRP A 49 54.591 -7.451 16.137 1.00 16.65 C ANISOU 1120 CE2 TRP B 49 2033 2144 2149 -90 2 42 C ATOM 1121 CE3 TRP A 49 53.668 -5.211 16.163 1.00 16.91 C ANISOU 1121 CE3 TRP B 49 2157 2113 2152 -63 59 61 C ATOM 1122 CZ2 TRP A 49 54.646 -7.473 14.731 1.00 17.19 C ANISOU 1122 CZ2 TRP B 49 2167 2190 2173 -28 -43 16 C ATOM 1123 CZ3 TRP A 49 53.702 -5.238 14.762 1.00 17.29 C ANISOU 1123 CZ3 TRP B 49 2112 2295 2163 -3 43 58 C ATOM 1124 CH2 TRP A 49 54.188 -6.356 14.066 1.00 16.62 C ANISOU 1124 CH2 TRP B 49 2067 2086 2160 -28 -62 25 C ATOM 1125 N GLN A 50 52.970 -3.297 20.822 1.00 23.01 N ANISOU 1125 N GLN B 50 2939 2928 2875 -46 1 -37 N ATOM 1126 CA GLN A 50 52.259 -2.595 21.921 1.00 24.67 C ANISOU 1126 CA GLN B 50 3230 3020 3121 -92 43 -10 C ATOM 1127 C GLN A 50 52.882 -1.245 22.327 1.00 24.60 C ANISOU 1127 C GLN B 50 3169 3103 3074 -44 28 -24 C ATOM 1128 O GLN A 50 52.769 -0.814 23.469 1.00 25.00 O ANISOU 1128 O GLN B 50 3304 3044 3151 -33 74 -98 O ATOM 1129 CB GLN A 50 52.067 -3.500 23.157 1.00 25.81 C ANISOU 1129 CB GLN B 50 3303 3296 3206 16 -28 -78 C ATOM 1130 CG GLN A 50 51.210 -4.744 22.908 1.00 26.87 C ANISOU 1130 CG GLN B 50 3582 3297 3327 -156 44 153 C ATOM 1131 CD GLN A 50 51.070 -5.642 24.128 1.00 31.75 C ANISOU 1131 CD GLN B 50 3876 4099 4088 101 31 -10 C ATOM 1132 OE1 GLN A 50 51.380 -5.247 25.270 1.00 35.04 O ANISOU 1132 OE1 GLN B 50 4735 4481 4097 -209 -130 -203 O ATOM 1133 NE2 GLN A 50 50.584 -6.864 23.901 1.00 32.76 N ANISOU 1133 NE2 GLN B 50 4405 3676 4365 -263 -98 -232 N ATOM 1134 N GLY A 51 53.538 -0.589 21.383 1.00 23.56 N ANISOU 1134 N GLY B 51 3045 2933 2972 -67 36 -6 N ATOM 1135 CA GLY A 51 54.060 0.758 21.601 1.00 21.77 C ANISOU 1135 CA GLY B 51 2816 2710 2743 -53 34 -31 C ATOM 1136 C GLY A 51 54.218 1.444 20.259 1.00 20.74 C ANISOU 1136 C GLY B 51 2661 2542 2676 -45 18 -9 C ATOM 1137 O GLY A 51 53.667 0.990 19.256 1.00 20.53 O ANISOU 1137 O GLY B 51 2629 2536 2633 -53 27 32 O ATOM 1138 N SER A 52 55.000 2.519 20.215 1.00 19.27 N ANISOU 1138 N SER B 52 2447 2403 2472 -34 18 -32 N ATOM 1139 CA SER A 52 55.187 3.238 18.961 1.00 18.11 C ANISOU 1139 CA SER B 52 2272 2239 2368 -38 1 -41 C ATOM 1140 C SER A 52 56.518 3.975 18.957 1.00 17.30 C ANISOU 1140 C SER B 52 2179 2144 2249 -13 14 4 C ATOM 1141 O SER A 52 57.175 4.100 19.999 1.00 16.39 O ANISOU 1141 O SER B 52 2005 2035 2187 -109 -37 -59 O ATOM 1142 CB SER A 52 54.026 4.234 18.729 1.00 18.45 C ANISOU 1142 CB SER B 52 2343 2254 2412 -7 -7 -36 C ATOM 1143 OG SER A 52 53.879 5.117 19.848 1.00 18.83 O ANISOU 1143 OG SER B 52 2414 2424 2317 -89 123 -80 O ATOM 1144 N ASN A 53 56.896 4.464 17.783 1.00 16.34 N ANISOU 1144 N ASN B 53 2082 1990 2137 10 -24 -22 N ATOM 1145 CA ASN A 53 58.037 5.376 17.624 1.00 15.90 C ANISOU 1145 CA ASN B 53 2029 1960 2052 -2 6 31 C ATOM 1146 C ASN A 53 59.409 4.729 17.756 1.00 15.84 C ANISOU 1146 C ASN B 53 2032 1972 2011 3 -6 5 C ATOM 1147 O ASN A 53 60.381 5.393 18.124 1.00 15.77 O ANISOU 1147 O ASN B 53 2037 1868 2085 35 47 -64 O ATOM 1148 CB ASN A 53 57.903 6.638 18.510 1.00 15.93 C ANISOU 1148 CB ASN B 53 2053 1937 2061 -19 -9 -7 C ATOM 1149 CG ASN A 53 58.610 7.868 17.902 1.00 16.80 C ANISOU 1149 CG ASN B 53 2144 2067 2172 -42 34 -11 C ATOM 1150 OD1 ASN A 53 58.830 7.933 16.701 1.00 17.62 O ANISOU 1150 OD1 ASN B 53 2215 2042 2436 -97 -168 -61 O ATOM 1151 ND2 ASN A 53 58.974 8.837 18.746 1.00 19.18 N ANISOU 1151 ND2 ASN B 53 2324 2419 2545 -62 9 -97 N ATOM 1152 N PHE A 54 59.504 3.444 17.410 1.00 15.38 N ANISOU 1152 N PHE B 54 1950 1922 1971 21 4 14 N ATOM 1153 CA PHE A 54 60.807 2.781 17.395 1.00 16.31 C ANISOU 1153 CA PHE B 54 2087 2036 2073 22 -10 -5 C ATOM 1154 C PHE A 54 61.801 3.531 16.489 1.00 16.73 C ANISOU 1154 C PHE B 54 2149 2095 2113 8 -11 -16 C ATOM 1155 O PHE A 54 63.009 3.535 16.742 1.00 16.97 O ANISOU 1155 O PHE B 54 2150 2233 2065 9 -94 67 O ATOM 1156 CB PHE A 54 60.676 1.305 16.963 1.00 15.45 C ANISOU 1156 CB PHE B 54 1965 1941 1961 -5 12 -45 C ATOM 1157 CG PHE A 54 60.537 1.113 15.459 1.00 15.84 C ANISOU 1157 CG PHE B 54 1948 2053 2015 -8 -12 -56 C ATOM 1158 CD1 PHE A 54 61.672 0.858 14.662 1.00 15.83 C ANISOU 1158 CD1 PHE B 54 2109 2066 1837 15 126 -23 C ATOM 1159 CD2 PHE A 54 59.283 1.152 14.849 1.00 14.99 C ANISOU 1159 CD2 PHE B 54 2011 1867 1814 72 26 86 C ATOM 1160 CE1 PHE A 54 61.556 0.674 13.275 1.00 15.04 C ANISOU 1160 CE1 PHE B 54 1940 1840 1934 45 -9 20 C ATOM 1161 CE2 PHE A 54 59.151 0.953 13.469 1.00 14.40 C ANISOU 1161 CE2 PHE B 54 1857 1826 1786 99 -17 -135 C ATOM 1162 CZ PHE A 54 60.298 0.716 12.675 1.00 14.72 C ANISOU 1162 CZ PHE B 54 1896 1771 1925 -68 45 50 C ATOM 1163 N ILE A 55 61.292 4.185 15.440 1.00 17.18 N ANISOU 1163 N ILE B 55 2221 2131 2175 6 -33 -39 N ATOM 1164 CA ILE A 55 62.178 4.769 14.439 1.00 18.28 C ANISOU 1164 CA ILE B 55 2325 2283 2334 -10 -10 -1 C ATOM 1165 C ILE A 55 63.003 5.943 14.991 1.00 18.63 C ANISOU 1165 C ILE B 55 2360 2340 2377 -19 -58 10 C ATOM 1166 O ILE A 55 64.066 6.257 14.460 1.00 18.62 O ANISOU 1166 O ILE B 55 2250 2371 2451 25 -82 -19 O ATOM 1167 CB ILE A 55 61.422 5.152 13.139 1.00 18.42 C ANISOU 1167 CB ILE B 55 2336 2356 2306 -14 5 -13 C ATOM 1168 CG1 ILE A 55 62.354 5.115 11.907 1.00 18.76 C ANISOU 1168 CG1 ILE B 55 2309 2434 2385 -30 76 0 C ATOM 1169 CG2 ILE A 55 60.675 6.500 13.286 1.00 17.83 C ANISOU 1169 CG2 ILE B 55 2307 2164 2302 -30 7 -53 C ATOM 1170 CD1 ILE A 55 62.956 3.743 11.614 1.00 18.55 C ANISOU 1170 CD1 ILE B 55 2318 2413 2316 -70 137 -33 C ATOM 1171 N GLU A 56 62.500 6.575 16.048 1.00 19.15 N ANISOU 1171 N GLU B 56 2437 2372 2464 31 -49 -5 N ATOM 1172 CA GLU A 56 63.209 7.668 16.732 1.00 20.82 C ANISOU 1172 CA GLU B 56 2649 2580 2679 -11 -30 -31 C ATOM 1173 C GLU A 56 64.601 7.247 17.175 1.00 20.54 C ANISOU 1173 C GLU B 56 2641 2558 2605 -27 -45 -34 C ATOM 1174 O GLU A 56 65.540 8.054 17.125 1.00 20.85 O ANISOU 1174 O GLU B 56 2667 2527 2725 -25 -34 39 O ATOM 1175 CB GLU A 56 62.406 8.146 17.953 1.00 22.10 C ANISOU 1175 CB GLU B 56 2863 2757 2774 -5 -25 -75 C ATOM 1176 CG GLU A 56 63.039 9.321 18.736 1.00 25.60 C ANISOU 1176 CG GLU B 56 3327 3137 3262 -114 -139 -54 C ATOM 1177 CD GLU A 56 62.636 10.692 18.215 1.00 30.30 C ANISOU 1177 CD GLU B 56 4009 3573 3930 24 -169 3 C ATOM 1178 OE1 GLU A 56 62.059 10.792 17.097 1.00 32.03 O ANISOU 1178 OE1 GLU B 56 4272 3877 4018 -106 -137 50 O ATOM 1179 OE2 GLU A 56 62.907 11.681 18.929 1.00 30.67 O ANISOU 1179 OE2 GLU B 56 3969 3765 3917 3 -199 -142 O ATOM 1180 N THR A 57 64.734 5.983 17.589 1.00 19.75 N ANISOU 1180 N THR B 57 2555 2469 2477 -24 -28 -39 N ATOM 1181 CA THR A 57 65.981 5.476 18.171 1.00 19.72 C ANISOU 1181 CA THR B 57 2534 2462 2496 -38 -13 -46 C ATOM 1182 C THR A 57 66.565 4.217 17.499 1.00 19.33 C ANISOU 1182 C THR B 57 2461 2394 2486 -21 1 -25 C ATOM 1183 O THR A 57 67.383 3.509 18.093 1.00 19.87 O ANISOU 1183 O THR B 57 2520 2471 2556 -13 -9 -140 O ATOM 1184 CB THR A 57 65.783 5.196 19.655 1.00 19.68 C ANISOU 1184 CB THR B 57 2539 2464 2472 -65 -7 -5 C ATOM 1185 OG1 THR A 57 64.719 4.242 19.822 1.00 18.88 O ANISOU 1185 OG1 THR B 57 2386 2412 2373 -118 -66 -7 O ATOM 1186 CG2 THR A 57 65.428 6.510 20.398 1.00 19.96 C ANISOU 1186 CG2 THR B 57 2682 2499 2402 -66 18 -15 C ATOM 1187 N CYS A 58 66.122 3.941 16.281 1.00 19.25 N ANISOU 1187 N CYS B 58 2441 2374 2496 -28 16 7 N ATOM 1188 CA CYS A 58 66.602 2.810 15.492 1.00 19.46 C ANISOU 1188 CA CYS B 58 2467 2461 2463 6 15 -23 C ATOM 1189 C CYS A 58 66.973 3.291 14.091 1.00 19.92 C ANISOU 1189 C CYS B 58 2530 2488 2550 -27 4 17 C ATOM 1190 O CYS A 58 66.505 4.330 13.642 1.00 20.53 O ANISOU 1190 O CYS B 58 2677 2560 2562 -10 54 -22 O ATOM 1191 CB CYS A 58 65.533 1.706 15.377 1.00 19.21 C ANISOU 1191 CB CYS B 58 2410 2418 2469 42 5 44 C ATOM 1192 SG CYS A 58 64.867 1.067 16.922 1.00 19.03 S ANISOU 1192 SG CYS B 58 2383 2494 2352 23 -50 -69 S ATOM 1193 N ARG A 59 67.788 2.508 13.391 1.00 19.71 N ANISOU 1193 N ARG B 59 2446 2518 2522 -59 15 -6 N ATOM 1194 CA ARG A 59 68.299 2.890 12.079 1.00 20.47 C ANISOU 1194 CA ARG B 59 2527 2622 2627 -43 -17 -8 C ATOM 1195 C ARG A 59 68.537 1.630 11.267 1.00 20.26 C ANISOU 1195 C ARG B 59 2500 2603 2594 -42 -10 -20 C ATOM 1196 O ARG A 59 68.476 0.523 11.810 1.00 19.95 O ANISOU 1196 O ARG B 59 2540 2517 2522 18 12 -86 O ATOM 1197 CB ARG A 59 69.616 3.660 12.232 1.00 21.07 C ANISOU 1197 CB ARG B 59 2580 2709 2716 -64 35 27 C ATOM 1198 CG ARG A 59 70.743 2.797 12.771 1.00 21.42 C ANISOU 1198 CG ARG B 59 2527 2728 2880 -90 -44 -18 C ATOM 1199 CD ARG A 59 72.106 3.506 12.837 1.00 22.74 C ANISOU 1199 CD ARG B 59 2740 3003 2894 -97 44 42 C ATOM 1200 NE ARG A 59 73.143 2.476 12.922 1.00 25.18 N ANISOU 1200 NE ARG B 59 2860 3259 3447 72 -65 12 N ATOM 1201 CZ ARG A 59 74.432 2.707 13.148 1.00 28.02 C ANISOU 1201 CZ ARG B 59 3367 3583 3696 -34 -30 -10 C ATOM 1202 NH1 ARG A 59 74.859 3.948 13.326 1.00 26.10 N ANISOU 1202 NH1 ARG B 59 3099 3242 3575 -96 34 -1 N ATOM 1203 NH2 ARG A 59 75.291 1.685 13.204 1.00 27.67 N ANISOU 1203 NH2 ARG B 59 3302 3473 3736 73 -85 13 N ATOM 1204 N ASN A 60 68.826 1.804 9.979 1.00 20.10 N ANISOU 1204 N ASN B 60 2454 2576 2605 -61 -22 -46 N ATOM 1205 CA ASN A 60 69.187 0.686 9.095 1.00 20.61 C ANISOU 1205 CA ASN B 60 2501 2643 2685 -21 0 -25 C ATOM 1206 C ASN A 60 68.125 -0.400 9.047 1.00 20.02 C ANISOU 1206 C ASN B 60 2438 2582 2586 15 1 -7 C ATOM 1207 O ASN A 60 68.403 -1.597 9.163 1.00 20.02 O ANISOU 1207 O ASN B 60 2370 2605 2630 0 -30 15 O ATOM 1208 CB ASN A 60 70.573 0.143 9.467 1.00 21.27 C ANISOU 1208 CB ASN B 60 2634 2671 2775 -3 -18 0 C ATOM 1209 CG ASN A 60 71.678 1.161 9.187 1.00 24.62 C ANISOU 1209 CG ASN B 60 3059 3067 3225 -67 66 -60 C ATOM 1210 OD1 ASN A 60 71.581 1.951 8.242 1.00 27.40 O ANISOU 1210 OD1 ASN B 60 3548 3452 3408 -56 -62 97 O ATOM 1211 ND2 ASN A 60 72.714 1.159 10.008 1.00 27.12 N ANISOU 1211 ND2 ASN B 60 3369 3562 3372 -31 -124 -57 N ATOM 1212 N THR A 61 66.883 0.037 8.869 1.00 19.58 N ANISOU 1212 N THR B 61 2352 2554 2533 -4 -38 34 N ATOM 1213 CA THR A 61 65.769 -0.900 8.837 1.00 18.81 C ANISOU 1213 CA THR B 61 2271 2452 2422 20 -29 -8 C ATOM 1214 C THR A 61 65.820 -1.651 7.527 1.00 19.82 C ANISOU 1214 C THR B 61 2401 2581 2548 18 -33 10 C ATOM 1215 O THR A 61 66.176 -1.081 6.473 1.00 18.48 O ANISOU 1215 O THR B 61 2130 2457 2432 -51 62 29 O ATOM 1216 CB THR A 61 64.430 -0.174 8.952 1.00 18.37 C ANISOU 1216 CB THR B 61 2253 2389 2335 26 -53 -36 C ATOM 1217 OG1 THR A 61 64.321 0.753 7.872 1.00 16.88 O ANISOU 1217 OG1 THR B 61 1920 2261 2230 72 -15 73 O ATOM 1218 CG2 THR A 61 64.331 0.586 10.301 1.00 18.22 C ANISOU 1218 CG2 THR B 61 2216 2410 2295 33 20 -93 C ATOM 1219 N GLN A 62 65.448 -2.924 7.598 1.00 20.50 N ANISOU 1219 N GLN B 62 2522 2605 2661 11 -4 50 N ATOM 1220 CA GLN A 62 65.472 -3.810 6.448 1.00 22.55 C ANISOU 1220 CA GLN B 62 2784 2864 2917 -17 1 -15 C ATOM 1221 C GLN A 62 64.382 -4.847 6.591 1.00 21.79 C ANISOU 1221 C GLN B 62 2643 2826 2808 36 27 19 C ATOM 1222 O GLN A 62 64.001 -5.198 7.709 1.00 20.74 O ANISOU 1222 O GLN B 62 2482 2801 2597 -22 18 121 O ATOM 1223 CB GLN A 62 66.795 -4.584 6.371 1.00 22.80 C ANISOU 1223 CB GLN B 62 2857 2855 2951 -21 18 -54 C ATOM 1224 CG GLN A 62 68.037 -3.757 6.211 1.00 26.07 C ANISOU 1224 CG GLN B 62 3178 3320 3405 -7 63 -67 C ATOM 1225 CD GLN A 62 69.282 -4.609 6.136 1.00 28.26 C ANISOU 1225 CD GLN B 62 3428 3701 3607 61 6 -7 C ATOM 1226 OE1 GLN A 62 69.213 -5.843 6.036 1.00 32.35 O ANISOU 1226 OE1 GLN B 62 4032 3790 4467 34 73 -12 O ATOM 1227 NE2 GLN A 62 70.432 -3.958 6.174 1.00 32.00 N ANISOU 1227 NE2 GLN B 62 3767 4035 4355 -212 -25 -55 N ATOM 1228 N LEU A 63 63.909 -5.345 5.455 1.00 20.92 N ANISOU 1228 N LEU B 63 2559 2716 2671 36 0 -24 N ATOM 1229 CA LEU A 63 63.132 -6.576 5.435 1.00 22.20 C ANISOU 1229 CA LEU B 63 2782 2814 2836 43 -10 -6 C ATOM 1230 C LEU A 63 64.094 -7.763 5.392 1.00 22.56 C ANISOU 1230 C LEU B 63 2817 2863 2890 31 -22 -9 C ATOM 1231 O LEU A 63 64.898 -7.874 4.471 1.00 22.46 O ANISOU 1231 O LEU B 63 2797 2861 2875 130 7 -69 O ATOM 1232 CB LEU A 63 62.202 -6.621 4.211 1.00 22.14 C ANISOU 1232 CB LEU B 63 2742 2813 2857 3 -10 17 C ATOM 1233 CG LEU A 63 61.282 -7.844 4.135 1.00 22.40 C ANISOU 1233 CG LEU B 63 2920 2748 2841 40 -32 -1 C ATOM 1234 CD1 LEU A 63 60.208 -7.814 5.251 1.00 22.18 C ANISOU 1234 CD1 LEU B 63 2745 2668 3011 179 51 17 C ATOM 1235 CD2 LEU A 63 60.647 -7.959 2.761 1.00 22.58 C ANISOU 1235 CD2 LEU B 63 2921 2758 2897 97 -74 -46 C ATOM 1236 N ALA A 64 64.017 -8.626 6.397 1.00 22.98 N ANISOU 1236 N ALA B 64 2904 2889 2936 13 -41 1 N ATOM 1237 CA ALA A 64 64.775 -9.881 6.412 1.00 23.52 C ANISOU 1237 CA ALA B 64 2998 2942 2996 -4 -36 -12 C ATOM 1238 C ALA A 64 63.834 -11.034 6.046 1.00 23.46 C ANISOU 1238 C ALA B 64 3019 2920 2974 -13 -16 -21 C ATOM 1239 O ALA A 64 62.759 -11.179 6.627 1.00 23.06 O ANISOU 1239 O ALA B 64 2971 2805 2984 -9 -5 7 O ATOM 1240 CB ALA A 64 65.412 -10.101 7.784 1.00 24.43 C ANISOU 1240 CB ALA B 64 3105 3070 3107 34 -57 -6 C ATOM 1241 N GLY A 65 64.217 -11.816 5.045 1.00 23.64 N ANISOU 1241 N GLY B 65 2992 2884 3103 -15 -8 -51 N ATOM 1242 CA GLY A 65 63.324 -12.847 4.491 1.00 23.19 C ANISOU 1242 CA GLY B 65 2968 2882 2961 5 -37 -84 C ATOM 1243 C GLY A 65 61.985 -12.284 4.022 1.00 22.69 C ANISOU 1243 C GLY B 65 2922 2843 2853 -6 -1 -108 C ATOM 1244 O GLY A 65 61.906 -11.206 3.411 1.00 22.43 O ANISOU 1244 O GLY B 65 3008 2782 2732 -40 9 -134 O ATOM 1245 N SER A 66 60.922 -13.013 4.314 1.00 21.64 N ANISOU 1245 N SER B 66 2809 2695 2716 -7 11 -123 N ATOM 1246 CA SER A 66 59.593 -12.624 3.855 1.00 21.92 C ANISOU 1246 CA SER B 66 2781 2750 2796 -41 -4 -99 C ATOM 1247 C SER A 66 58.835 -11.673 4.773 1.00 21.14 C ANISOU 1247 C SER B 66 2681 2661 2688 -23 -29 -75 C ATOM 1248 O SER A 66 57.983 -10.904 4.303 1.00 20.52 O ANISOU 1248 O SER B 66 2719 2567 2508 75 -88 -81 O ATOM 1249 CB SER A 66 58.753 -13.875 3.631 1.00 22.38 C ANISOU 1249 CB SER B 66 2806 2804 2891 -81 -26 -134 C ATOM 1250 OG SER A 66 59.189 -14.499 2.448 1.00 24.61 O ANISOU 1250 OG SER B 66 3027 3155 3165 -158 50 -224 O ATOM 1251 N SER A 67 59.111 -11.727 6.076 1.00 20.43 N ANISOU 1251 N SER B 67 2543 2595 2623 -33 -50 1 N ATOM 1252 CA SER A 67 58.219 -11.064 7.021 1.00 20.55 C ANISOU 1252 CA SER B 67 2605 2596 2605 0 -57 -36 C ATOM 1253 C SER A 67 58.878 -10.406 8.223 1.00 20.95 C ANISOU 1253 C SER B 67 2628 2629 2701 0 -42 -15 C ATOM 1254 O SER A 67 58.187 -9.915 9.114 1.00 19.20 O ANISOU 1254 O SER B 67 2424 2391 2478 31 -135 4 O ATOM 1255 CB SER A 67 57.164 -12.065 7.505 1.00 20.94 C ANISOU 1255 CB SER B 67 2687 2632 2634 17 -47 3 C ATOM 1256 OG SER A 67 57.770 -13.104 8.264 1.00 21.42 O ANISOU 1256 OG SER B 67 2857 2584 2696 112 -50 -76 O ATOM 1257 N GLU A 68 60.207 -10.388 8.253 1.00 21.46 N ANISOU 1257 N GLU B 68 2691 2649 2813 -1 -55 -37 N ATOM 1258 CA GLU A 68 60.892 -9.866 9.423 1.00 22.21 C ANISOU 1258 CA GLU B 68 2827 2752 2857 -44 -37 -15 C ATOM 1259 C GLU A 68 61.427 -8.469 9.202 1.00 21.71 C ANISOU 1259 C GLU B 68 2775 2716 2757 -37 -21 -12 C ATOM 1260 O GLU A 68 62.112 -8.201 8.202 1.00 21.13 O ANISOU 1260 O GLU B 68 2718 2601 2709 -95 23 46 O ATOM 1261 CB GLU A 68 62.008 -10.811 9.879 1.00 23.39 C ANISOU 1261 CB GLU B 68 2953 2913 3022 -23 -43 -56 C ATOM 1262 CG GLU A 68 61.483 -12.061 10.578 1.00 28.17 C ANISOU 1262 CG GLU B 68 3615 3455 3633 -38 21 47 C ATOM 1263 CD GLU A 68 62.488 -12.651 11.549 1.00 33.67 C ANISOU 1263 CD GLU B 68 4274 4261 4255 106 -118 115 C ATOM 1264 OE1 GLU A 68 62.143 -12.776 12.745 1.00 35.68 O ANISOU 1264 OE1 GLU B 68 4671 4517 4369 51 56 79 O ATOM 1265 OE2 GLU A 68 63.621 -12.965 11.117 1.00 35.89 O ANISOU 1265 OE2 GLU B 68 4446 4565 4623 149 -7 6 O ATOM 1266 N LEU A 69 61.092 -7.589 10.148 1.00 20.26 N ANISOU 1266 N LEU B 69 2597 2487 2610 -19 0 -10 N ATOM 1267 CA LEU A 69 61.726 -6.284 10.263 1.00 19.49 C ANISOU 1267 CA LEU B 69 2460 2460 2482 13 -29 -14 C ATOM 1268 C LEU A 69 63.016 -6.444 11.061 1.00 19.56 C ANISOU 1268 C LEU B 69 2471 2479 2480 -26 -45 -14 C ATOM 1269 O LEU A 69 62.976 -6.837 12.220 1.00 18.48 O ANISOU 1269 O LEU B 69 2325 2345 2350 -87 -97 -12 O ATOM 1270 CB LEU A 69 60.805 -5.287 10.987 1.00 18.72 C ANISOU 1270 CB LEU B 69 2427 2338 2347 25 15 -46 C ATOM 1271 CG LEU A 69 61.439 -3.959 11.438 1.00 18.56 C ANISOU 1271 CG LEU B 69 2336 2389 2324 -23 17 26 C ATOM 1272 CD1 LEU A 69 62.056 -3.181 10.259 1.00 18.31 C ANISOU 1272 CD1 LEU B 69 2440 2296 2219 5 -43 1 C ATOM 1273 CD2 LEU A 69 60.418 -3.090 12.205 1.00 17.23 C ANISOU 1273 CD2 LEU B 69 2248 2117 2179 55 4 3 C ATOM 1274 N ALA A 70 64.143 -6.138 10.423 1.00 19.58 N ANISOU 1274 N ALA B 70 2461 2531 2444 -29 -37 23 N ATOM 1275 CA ALA A 70 65.425 -6.060 11.104 1.00 20.02 C ANISOU 1275 CA ALA B 70 2504 2539 2563 -9 0 13 C ATOM 1276 C ALA A 70 65.860 -4.590 11.212 1.00 20.08 C ANISOU 1276 C ALA B 70 2530 2538 2559 22 2 -9 C ATOM 1277 O ALA A 70 65.624 -3.797 10.308 1.00 20.33 O ANISOU 1277 O ALA B 70 2620 2471 2632 -63 -4 2 O ATOM 1278 CB ALA A 70 66.470 -6.903 10.359 1.00 19.77 C ANISOU 1278 CB ALA B 70 2559 2509 2443 29 4 8 C ATOM 1279 N ALA A 71 66.450 -4.227 12.342 1.00 19.88 N ANISOU 1279 N ALA B 71 2466 2464 2623 17 -15 -31 N ATOM 1280 CA ALA A 71 66.949 -2.881 12.544 1.00 20.36 C ANISOU 1280 CA ALA B 71 2534 2532 2667 -15 -38 -9 C ATOM 1281 C ALA A 71 68.117 -2.903 13.536 1.00 20.98 C ANISOU 1281 C ALA B 71 2609 2614 2746 -31 -60 20 C ATOM 1282 O ALA A 71 68.432 -3.945 14.123 1.00 21.16 O ANISOU 1282 O ALA B 71 2603 2625 2810 -42 -76 20 O ATOM 1283 CB ALA A 71 65.799 -1.943 13.042 1.00 19.35 C ANISOU 1283 CB ALA B 71 2426 2332 2594 -59 -14 -23 C ATOM 1284 N GLU A 72 68.775 -1.760 13.683 1.00 20.77 N ANISOU 1284 N GLU B 72 2618 2599 2674 -65 -47 -33 N ATOM 1285 CA GLU A 72 69.753 -1.555 14.746 1.00 20.91 C ANISOU 1285 CA GLU B 72 2599 2639 2707 -11 -21 -23 C ATOM 1286 C GLU A 72 69.121 -0.522 15.676 1.00 20.72 C ANISOU 1286 C GLU B 72 2570 2626 2674 -49 -28 -25 C ATOM 1287 O GLU A 72 68.737 0.550 15.223 1.00 20.46 O ANISOU 1287 O GLU B 72 2601 2542 2631 27 35 -33 O ATOM 1288 CB GLU A 72 71.075 -1.051 14.154 1.00 21.32 C ANISOU 1288 CB GLU B 72 2672 2709 2719 -30 -64 -42 C ATOM 1289 CG GLU A 72 71.759 -2.051 13.220 1.00 21.59 C ANISOU 1289 CG GLU B 72 2530 2832 2841 41 -3 -14 C ATOM 1290 CD GLU A 72 72.914 -1.460 12.411 1.00 22.76 C ANISOU 1290 CD GLU B 72 2838 2943 2866 4 -98 37 C ATOM 1291 OE1 GLU A 72 73.173 -0.247 12.488 1.00 23.54 O ANISOU 1291 OE1 GLU B 72 2939 2858 3147 7 -79 56 O ATOM 1292 OE2 GLU A 72 73.575 -2.228 11.689 1.00 24.01 O ANISOU 1292 OE2 GLU B 72 2832 3139 3152 137 47 -2 O ATOM 1293 N CYS A 73 68.949 -0.863 16.949 1.00 20.45 N ANISOU 1293 N CYS B 73 2519 2601 2648 -16 -49 -31 N ATOM 1294 CA CYS A 73 68.257 0.021 17.891 1.00 21.31 C ANISOU 1294 CA CYS B 73 2652 2710 2732 -34 -53 -8 C ATOM 1295 C CYS A 73 69.148 0.343 19.082 1.00 22.10 C ANISOU 1295 C CYS B 73 2762 2844 2790 -20 -64 -5 C ATOM 1296 O CYS A 73 69.934 -0.501 19.524 1.00 21.52 O ANISOU 1296 O CYS B 73 2645 2836 2695 -49 -118 -24 O ATOM 1297 CB CYS A 73 66.944 -0.607 18.388 1.00 21.26 C ANISOU 1297 CB CYS B 73 2632 2777 2669 12 -27 2 C ATOM 1298 SG CYS A 73 65.667 -0.779 17.125 1.00 20.03 S ANISOU 1298 SG CYS B 73 2440 2585 2582 89 -46 -47 S ATOM 1299 N LYS A 74 69.007 1.560 19.603 1.00 22.84 N ANISOU 1299 N LYS B 74 2824 2940 2914 -37 -88 1 N ATOM 1300 CA LYS A 74 69.772 1.968 20.762 1.00 24.60 C ANISOU 1300 CA LYS B 74 3116 3133 3095 -32 -34 4 C ATOM 1301 C LYS A 74 69.244 1.333 22.036 1.00 24.70 C ANISOU 1301 C LYS B 74 3152 3147 3086 -34 -23 23 C ATOM 1302 O LYS A 74 68.046 1.381 22.327 1.00 24.18 O ANISOU 1302 O LYS B 74 3101 3084 3003 -35 -83 46 O ATOM 1303 CB LYS A 74 69.816 3.492 20.887 1.00 24.52 C ANISOU 1303 CB LYS B 74 3111 3093 3111 -63 -60 29 C ATOM 1304 CG LYS A 74 70.935 4.112 20.030 1.00 26.10 C ANISOU 1304 CG LYS B 74 3231 3362 3322 8 31 43 C ATOM 1305 CD LYS A 74 70.990 5.617 20.178 1.00 27.60 C ANISOU 1305 CD LYS B 74 3559 3388 3538 -38 -97 0 C ATOM 1306 CE LYS A 74 70.002 6.305 19.251 1.00 28.82 C ANISOU 1306 CE LYS B 74 3671 3652 3627 45 -88 -21 C ATOM 1307 NZ LYS A 74 69.850 7.744 19.597 1.00 29.80 N ANISOU 1307 NZ LYS B 74 3858 3607 3859 -9 -94 4 N ATOM 1308 N THR A 75 70.155 0.709 22.773 1.00 25.92 N ANISOU 1308 N THR B 75 3217 3334 3296 -25 -31 -6 N ATOM 1309 CA THR A 75 69.877 0.251 24.132 1.00 26.97 C ANISOU 1309 CA THR B 75 3357 3503 3387 -28 -44 47 C ATOM 1310 C THR A 75 69.820 1.489 25.028 1.00 28.05 C ANISOU 1310 C THR B 75 3500 3596 3558 -5 -46 16 C ATOM 1311 O THR A 75 70.125 2.598 24.579 1.00 27.97 O ANISOU 1311 O THR B 75 3517 3627 3483 -10 -64 25 O ATOM 1312 CB THR A 75 70.976 -0.699 24.656 1.00 27.14 C ANISOU 1312 CB THR B 75 3376 3494 3441 -4 -12 19 C ATOM 1313 OG1 THR A 75 72.245 -0.025 24.629 1.00 26.14 O ANISOU 1313 OG1 THR B 75 3230 3455 3245 45 -95 113 O ATOM 1314 CG2 THR A 75 71.053 -1.969 23.831 1.00 26.69 C ANISOU 1314 CG2 THR B 75 3270 3508 3362 -86 -50 46 C ATOM 1315 N ARG A 76 69.436 1.305 26.289 1.00 29.38 N ANISOU 1315 N ARG B 76 3718 3748 3696 -25 -8 36 N ATOM 1316 CA ARG A 76 69.448 2.395 27.265 1.00 31.27 C ANISOU 1316 CA ARG B 76 3993 3946 3941 7 0 -4 C ATOM 1317 C ARG A 76 70.856 2.933 27.498 1.00 31.80 C ANISOU 1317 C ARG B 76 4084 4010 3988 -9 -25 -6 C ATOM 1318 O ARG A 76 71.019 4.093 27.860 1.00 32.48 O ANISOU 1318 O ARG B 76 4204 4074 4061 11 -34 -63 O ATOM 1319 CB ARG A 76 68.816 1.955 28.583 1.00 31.47 C ANISOU 1319 CB ARG B 76 4041 3981 3932 19 0 -29 C ATOM 1320 CG ARG A 76 67.312 1.922 28.540 1.00 34.13 C ANISOU 1320 CG ARG B 76 4282 4318 4367 -27 -45 -86 C ATOM 1321 CD ARG A 76 66.716 1.298 29.800 1.00 36.94 C ANISOU 1321 CD ARG B 76 4748 4745 4543 -57 77 50 C ATOM 1322 NE ARG A 76 65.309 0.962 29.589 1.00 38.97 N ANISOU 1322 NE ARG B 76 4840 5052 4914 -12 24 -44 N ATOM 1323 CZ ARG A 76 64.764 -0.234 29.807 1.00 40.96 C ANISOU 1323 CZ ARG B 76 5220 5183 5159 -31 57 -7 C ATOM 1324 NH1 ARG A 76 65.490 -1.240 30.277 1.00 41.54 N ANISOU 1324 NH1 ARG B 76 5156 5319 5307 21 21 13 N ATOM 1325 NH2 ARG A 76 63.473 -0.417 29.568 1.00 41.51 N ANISOU 1325 NH2 ARG B 76 5133 5365 5273 -98 -22 3 N ATOM 1326 N ALA A 77 71.863 2.093 27.253 1.00 32.34 N ANISOU 1326 N ALA B 77 4154 4073 4059 2 -12 14 N ATOM 1327 CA ALA A 77 73.276 2.483 27.313 1.00 32.83 C ANISOU 1327 CA ALA B 77 4183 4159 4131 -5 -11 48 C ATOM 1328 C ALA A 77 73.756 3.228 26.049 1.00 33.13 C ANISOU 1328 C ALA B 77 4201 4199 4185 -13 -4 45 C ATOM 1329 O ALA A 77 74.915 3.650 25.980 1.00 32.97 O ANISOU 1329 O ALA B 77 4158 4178 4190 -13 -26 46 O ATOM 1330 CB ALA A 77 74.164 1.255 27.585 1.00 32.68 C ANISOU 1330 CB ALA B 77 4200 4129 4087 1 5 17 C ATOM 1331 N GLN A 78 72.856 3.391 25.074 1.00 32.94 N ANISOU 1331 N GLN B 78 4174 4171 4170 -42 -49 33 N ATOM 1332 CA GLN A 78 73.120 4.144 23.835 1.00 33.15 C ANISOU 1332 CA GLN B 78 4172 4213 4207 -29 -43 -1 C ATOM 1333 C GLN A 78 74.092 3.428 22.901 1.00 32.70 C ANISOU 1333 C GLN B 78 4108 4181 4133 -50 -74 12 C ATOM 1334 O GLN A 78 74.855 4.057 22.162 1.00 32.98 O ANISOU 1334 O GLN B 78 4125 4235 4171 -83 -40 -9 O ATOM 1335 CB GLN A 78 73.563 5.594 24.130 1.00 33.70 C ANISOU 1335 CB GLN B 78 4255 4264 4283 -41 -62 10 C ATOM 1336 CG GLN A 78 72.582 6.386 25.008 1.00 35.56 C ANISOU 1336 CG GLN B 78 4517 4478 4516 -23 -6 -11 C ATOM 1337 CD GLN A 78 71.134 6.240 24.566 1.00 38.79 C ANISOU 1337 CD GLN B 78 4769 4922 5044 20 -38 -24 C ATOM 1338 OE1 GLN A 78 70.321 5.618 25.254 1.00 39.70 O ANISOU 1338 OE1 GLN B 78 4962 4998 5121 -71 79 116 O ATOM 1339 NE2 GLN A 78 70.811 6.799 23.406 1.00 38.88 N ANISOU 1339 NE2 GLN B 78 4937 4934 4902 -48 -61 71 N ATOM 1340 N GLN A 79 74.042 2.101 22.961 1.00 31.73 N ANISOU 1340 N GLN B 79 3974 4063 4019 -44 -63 -32 N ATOM 1341 CA GLN A 79 74.744 1.214 22.057 1.00 31.30 C ANISOU 1341 CA GLN B 79 3910 4009 3973 -53 -66 11 C ATOM 1342 C GLN A 79 73.702 0.714 21.049 1.00 30.16 C ANISOU 1342 C GLN B 79 3788 3861 3810 -25 -58 6 C ATOM 1343 O GLN A 79 72.635 0.243 21.455 1.00 29.61 O ANISOU 1343 O GLN B 79 3671 3828 3751 -57 -74 64 O ATOM 1344 CB GLN A 79 75.318 0.027 22.857 1.00 31.46 C ANISOU 1344 CB GLN B 79 3934 4043 3973 -25 -61 -16 C ATOM 1345 CG GLN A 79 76.100 -1.017 22.048 1.00 32.31 C ANISOU 1345 CG GLN B 79 4064 4094 4117 12 -60 13 C ATOM 1346 CD GLN A 79 77.509 -0.568 21.707 1.00 32.36 C ANISOU 1346 CD GLN B 79 4040 4229 4023 91 2 -1 C ATOM 1347 OE1 GLN A 79 77.885 -0.523 20.537 1.00 32.57 O ANISOU 1347 OE1 GLN B 79 4148 4155 4070 235 17 -33 O ATOM 1348 NE2 GLN A 79 78.287 -0.202 22.728 1.00 31.11 N ANISOU 1348 NE2 GLN B 79 3863 3997 3960 81 -14 8 N ATOM 1349 N PHE A 80 73.989 0.848 19.754 1.00 28.90 N ANISOU 1349 N PHE B 80 3610 3685 3685 -22 -30 14 N ATOM 1350 CA PHE A 80 73.159 0.205 18.719 1.00 27.89 C ANISOU 1350 CA PHE B 80 3473 3541 3579 -37 -31 26 C ATOM 1351 C PHE A 80 73.340 -1.311 18.743 1.00 27.30 C ANISOU 1351 C PHE B 80 3381 3472 3519 -57 -14 28 C ATOM 1352 O PHE A 80 74.462 -1.821 18.780 1.00 26.67 O ANISOU 1352 O PHE B 80 3230 3332 3568 -52 -91 79 O ATOM 1353 CB PHE A 80 73.475 0.731 17.309 1.00 28.14 C ANISOU 1353 CB PHE B 80 3473 3616 3601 -56 -30 -11 C ATOM 1354 CG PHE A 80 72.865 2.066 17.012 1.00 27.93 C ANISOU 1354 CG PHE B 80 3544 3579 3488 -44 -24 56 C ATOM 1355 CD1 PHE A 80 71.516 2.175 16.693 1.00 27.45 C ANISOU 1355 CD1 PHE B 80 3577 3534 3317 -81 4 14 C ATOM 1356 CD2 PHE A 80 73.629 3.218 17.079 1.00 29.03 C ANISOU 1356 CD2 PHE B 80 3681 3686 3663 -75 -29 12 C ATOM 1357 CE1 PHE A 80 70.938 3.405 16.426 1.00 27.71 C ANISOU 1357 CE1 PHE B 80 3523 3570 3435 -23 48 -37 C ATOM 1358 CE2 PHE A 80 73.060 4.464 16.812 1.00 29.84 C ANISOU 1358 CE2 PHE B 80 3719 3765 3852 19 -64 -27 C ATOM 1359 CZ PHE A 80 71.709 4.555 16.484 1.00 29.51 C ANISOU 1359 CZ PHE B 80 3720 3718 3772 -12 -16 -31 C ATOM 1360 N VAL A 81 72.226 -2.031 18.714 1.00 26.53 N ANISOU 1360 N VAL B 81 3301 3390 3388 -41 -10 41 N ATOM 1361 CA VAL A 81 72.264 -3.490 18.687 1.00 25.73 C ANISOU 1361 CA VAL B 81 3215 3276 3283 -41 -7 -2 C ATOM 1362 C VAL A 81 71.274 -3.996 17.641 1.00 25.46 C ANISOU 1362 C VAL B 81 3192 3248 3232 -46 14 37 C ATOM 1363 O VAL A 81 70.230 -3.382 17.418 1.00 25.05 O ANISOU 1363 O VAL B 81 3199 3116 3200 -25 3 72 O ATOM 1364 CB VAL A 81 71.968 -4.145 20.084 1.00 25.65 C ANISOU 1364 CB VAL B 81 3198 3317 3230 -7 -38 8 C ATOM 1365 CG1 VAL A 81 73.069 -3.800 21.123 1.00 25.42 C ANISOU 1365 CG1 VAL B 81 3149 3257 3251 -63 33 -47 C ATOM 1366 CG2 VAL A 81 70.581 -3.777 20.618 1.00 25.57 C ANISOU 1366 CG2 VAL B 81 3220 3232 3261 -57 -36 -40 C ATOM 1367 N SER A 82 71.615 -5.115 17.010 1.00 25.01 N ANISOU 1367 N SER B 82 3117 3171 3214 -76 38 29 N ATOM 1368 CA SER A 82 70.743 -5.749 16.027 1.00 25.03 C ANISOU 1368 CA SER B 82 3120 3182 3205 -47 -5 46 C ATOM 1369 C SER A 82 69.517 -6.300 16.741 1.00 23.86 C ANISOU 1369 C SER B 82 2961 3050 3052 -39 -39 38 C ATOM 1370 O SER A 82 69.612 -6.863 17.837 1.00 22.86 O ANISOU 1370 O SER B 82 2770 2961 2955 -26 -64 121 O ATOM 1371 CB SER A 82 71.457 -6.892 15.305 1.00 25.72 C ANISOU 1371 CB SER B 82 3221 3259 3292 -10 16 46 C ATOM 1372 OG SER A 82 72.505 -6.418 14.470 1.00 30.17 O ANISOU 1372 OG SER B 82 3772 3690 3999 -80 40 20 O ATOM 1373 N THR A 83 68.368 -6.127 16.110 1.00 22.48 N ANISOU 1373 N THR B 83 2798 2833 2909 22 -43 59 N ATOM 1374 CA THR A 83 67.113 -6.627 16.642 1.00 21.61 C ANISOU 1374 CA THR B 83 2718 2735 2755 0 -41 46 C ATOM 1375 C THR A 83 66.192 -6.939 15.473 1.00 21.20 C ANISOU 1375 C THR B 83 2640 2706 2706 9 -24 -1 C ATOM 1376 O THR A 83 66.299 -6.309 14.407 1.00 20.26 O ANISOU 1376 O THR B 83 2466 2673 2555 47 -45 -11 O ATOM 1377 CB THR A 83 66.447 -5.607 17.613 1.00 21.44 C ANISOU 1377 CB THR B 83 2708 2708 2728 -27 -43 16 C ATOM 1378 OG1 THR A 83 65.149 -6.062 18.009 1.00 21.63 O ANISOU 1378 OG1 THR B 83 2753 2653 2810 24 -90 56 O ATOM 1379 CG2 THR A 83 66.324 -4.217 16.980 1.00 20.84 C ANISOU 1379 CG2 THR B 83 2615 2600 2700 3 -96 34 C ATOM 1380 N LYS A 84 65.305 -7.911 15.673 1.00 20.69 N ANISOU 1380 N LYS B 84 2639 2590 2632 22 18 22 N ATOM 1381 CA LYS A 84 64.309 -8.286 14.667 1.00 20.69 C ANISOU 1381 CA LYS B 84 2562 2645 2653 38 40 -34 C ATOM 1382 C LYS A 84 62.953 -8.539 15.315 1.00 20.05 C ANISOU 1382 C LYS B 84 2505 2579 2532 38 -13 5 C ATOM 1383 O LYS A 84 62.859 -8.849 16.512 1.00 19.14 O ANISOU 1383 O LYS B 84 2300 2505 2465 63 -17 96 O ATOM 1384 CB LYS A 84 64.730 -9.556 13.905 1.00 21.43 C ANISOU 1384 CB LYS B 84 2672 2719 2751 -47 0 -11 C ATOM 1385 CG LYS A 84 66.044 -9.453 13.158 1.00 22.94 C ANISOU 1385 CG LYS B 84 2958 2824 2933 142 92 -77 C ATOM 1386 CD LYS A 84 66.370 -10.747 12.445 1.00 25.98 C ANISOU 1386 CD LYS B 84 3346 3217 3308 28 -21 -89 C ATOM 1387 CE LYS A 84 67.374 -10.500 11.310 1.00 28.17 C ANISOU 1387 CE LYS B 84 3359 3782 3561 -30 279 56 C ATOM 1388 NZ LYS A 84 67.537 -11.736 10.495 1.00 31.45 N ANISOU 1388 NZ LYS B 84 3903 4038 4008 75 -54 -205 N ATOM 1389 N ILE A 85 61.907 -8.408 14.500 1.00 18.39 N ANISOU 1389 N ILE B 85 2271 2380 2334 30 4 24 N ATOM 1390 CA ILE A 85 60.539 -8.698 14.907 1.00 17.61 C ANISOU 1390 CA ILE B 85 2220 2278 2192 36 28 21 C ATOM 1391 C ILE A 85 59.782 -9.272 13.707 1.00 17.47 C ANISOU 1391 C ILE B 85 2183 2229 2223 39 14 -6 C ATOM 1392 O ILE A 85 59.957 -8.819 12.576 1.00 17.84 O ANISOU 1392 O ILE B 85 2231 2332 2213 88 -77 45 O ATOM 1393 CB ILE A 85 59.837 -7.438 15.511 1.00 17.09 C ANISOU 1393 CB ILE B 85 2148 2177 2167 61 91 18 C ATOM 1394 CG1 ILE A 85 58.530 -7.797 16.227 1.00 16.66 C ANISOU 1394 CG1 ILE B 85 2132 2103 2092 25 -68 34 C ATOM 1395 CG2 ILE A 85 59.621 -6.317 14.466 1.00 18.28 C ANISOU 1395 CG2 ILE B 85 2342 2390 2213 -33 72 25 C ATOM 1396 CD1 ILE A 85 57.935 -6.599 16.958 1.00 15.79 C ANISOU 1396 CD1 ILE B 85 1938 2115 1943 94 84 24 C ATOM 1397 N ASN A 86 58.977 -10.295 13.946 1.00 17.22 N ANISOU 1397 N ASN B 86 2137 2182 2224 54 -7 2 N ATOM 1398 CA ASN A 86 58.210 -10.899 12.865 1.00 17.14 C ANISOU 1398 CA ASN B 86 2208 2115 2186 11 -37 -15 C ATOM 1399 C ASN A 86 56.920 -10.124 12.571 1.00 16.40 C ANISOU 1399 C ASN B 86 2106 2031 2092 -13 -48 -36 C ATOM 1400 O ASN A 86 55.971 -10.157 13.359 1.00 16.27 O ANISOU 1400 O ASN B 86 2034 2006 2139 68 -150 -47 O ATOM 1401 CB ASN A 86 57.895 -12.367 13.169 1.00 17.48 C ANISOU 1401 CB ASN B 86 2247 2179 2216 6 -23 -14 C ATOM 1402 CG ASN A 86 57.345 -13.091 11.969 1.00 19.42 C ANISOU 1402 CG ASN B 86 2622 2331 2423 -103 -68 -28 C ATOM 1403 OD1 ASN A 86 57.178 -12.502 10.888 1.00 19.00 O ANISOU 1403 OD1 ASN B 86 2596 2154 2466 -110 -104 114 O ATOM 1404 ND2 ASN A 86 57.072 -14.385 12.136 1.00 19.78 N ANISOU 1404 ND2 ASN B 86 2666 2240 2608 -118 -135 -60 N ATOM 1405 N LEU A 87 56.890 -9.444 11.427 1.00 15.90 N ANISOU 1405 N LEU B 87 2020 1973 2047 -1 -96 -53 N ATOM 1406 CA LEU A 87 55.715 -8.651 11.033 1.00 16.33 C ANISOU 1406 CA LEU B 87 2103 2047 2053 4 -2 36 C ATOM 1407 C LEU A 87 54.445 -9.515 10.885 1.00 16.60 C ANISOU 1407 C LEU B 87 2138 2110 2059 7 -31 56 C ATOM 1408 O LEU A 87 53.331 -9.027 11.073 1.00 17.01 O ANISOU 1408 O LEU B 87 2311 2061 2088 3 69 69 O ATOM 1409 CB LEU A 87 56.006 -7.823 9.779 1.00 15.73 C ANISOU 1409 CB LEU B 87 1984 1946 2045 -5 -28 43 C ATOM 1410 CG LEU A 87 57.156 -6.806 9.982 1.00 15.18 C ANISOU 1410 CG LEU B 87 1984 2028 1753 -164 -5 67 C ATOM 1411 CD1 LEU A 87 57.437 -5.961 8.722 1.00 13.68 C ANISOU 1411 CD1 LEU B 87 1743 1800 1652 -118 -51 195 C ATOM 1412 CD2 LEU A 87 56.926 -5.878 11.201 1.00 15.77 C ANISOU 1412 CD2 LEU B 87 1856 2003 2132 -60 61 -74 C ATOM 1413 N ASP A 88 54.620 -10.804 10.605 1.00 17.36 N ANISOU 1413 N ASP B 88 2263 2191 2140 12 -3 29 N ATOM 1414 CA ASP A 88 53.492 -11.740 10.513 1.00 18.38 C ANISOU 1414 CA ASP B 88 2356 2305 2322 63 -57 9 C ATOM 1415 C ASP A 88 52.685 -11.887 11.808 1.00 18.29 C ANISOU 1415 C ASP B 88 2330 2329 2289 60 -31 -23 C ATOM 1416 O ASP A 88 51.542 -12.344 11.779 1.00 17.78 O ANISOU 1416 O ASP B 88 2303 2223 2228 2 -169 -69 O ATOM 1417 CB ASP A 88 53.951 -13.122 10.003 1.00 18.85 C ANISOU 1417 CB ASP B 88 2423 2426 2311 49 -27 -68 C ATOM 1418 CG ASP A 88 53.952 -13.207 8.487 1.00 19.33 C ANISOU 1418 CG ASP B 88 2485 2486 2371 68 -32 -3 C ATOM 1419 OD1 ASP A 88 53.349 -12.321 7.836 1.00 18.29 O ANISOU 1419 OD1 ASP B 88 2207 2234 2507 84 36 56 O ATOM 1420 OD2 ASP A 88 54.557 -14.160 7.948 1.00 18.03 O ANISOU 1420 OD2 ASP B 88 2464 2302 2084 78 -89 -42 O ATOM 1421 N ASP A 89 53.278 -11.513 12.947 1.00 18.55 N ANISOU 1421 N ASP B 89 2322 2332 2394 31 -25 -19 N ATOM 1422 CA ASP A 89 52.557 -11.551 14.225 1.00 18.33 C ANISOU 1422 CA ASP B 89 2363 2335 2263 59 -9 -9 C ATOM 1423 C ASP A 89 51.279 -10.692 14.218 1.00 17.82 C ANISOU 1423 C ASP B 89 2252 2294 2223 37 -59 21 C ATOM 1424 O ASP A 89 50.261 -11.056 14.808 1.00 18.25 O ANISOU 1424 O ASP B 89 2354 2250 2330 41 -150 33 O ATOM 1425 CB ASP A 89 53.440 -11.041 15.355 1.00 18.17 C ANISOU 1425 CB ASP B 89 2222 2400 2281 37 -29 65 C ATOM 1426 CG ASP A 89 54.745 -11.814 15.495 1.00 20.23 C ANISOU 1426 CG ASP B 89 2536 2616 2534 106 16 35 C ATOM 1427 OD1 ASP A 89 54.876 -12.950 14.929 1.00 20.40 O ANISOU 1427 OD1 ASP B 89 2544 2498 2708 85 -126 144 O ATOM 1428 OD2 ASP A 89 55.643 -11.238 16.166 1.00 20.61 O ANISOU 1428 OD2 ASP B 89 2568 2639 2623 38 -44 138 O ATOM 1429 N HIS A 90 51.350 -9.523 13.603 1.00 17.35 N ANISOU 1429 N HIS B 90 2235 2214 2143 57 -45 -4 N ATOM 1430 CA HIS A 90 50.230 -8.568 13.697 1.00 17.50 C ANISOU 1430 CA HIS B 90 2209 2262 2176 32 -60 47 C ATOM 1431 C HIS A 90 49.813 -7.910 12.398 1.00 17.21 C ANISOU 1431 C HIS B 90 2217 2151 2171 27 6 71 C ATOM 1432 O HIS A 90 48.766 -7.276 12.357 1.00 18.18 O ANISOU 1432 O HIS B 90 2364 2317 2227 178 -54 134 O ATOM 1433 CB HIS A 90 50.510 -7.487 14.733 1.00 17.24 C ANISOU 1433 CB HIS B 90 2263 2140 2147 71 -35 41 C ATOM 1434 CG HIS A 90 50.337 -7.937 16.155 1.00 18.43 C ANISOU 1434 CG HIS B 90 2388 2352 2261 -28 19 74 C ATOM 1435 ND1 HIS A 90 49.102 -8.081 16.753 1.00 18.44 N ANISOU 1435 ND1 HIS B 90 2412 2383 2209 -5 -70 149 N ATOM 1436 CD2 HIS A 90 51.252 -8.234 17.107 1.00 19.32 C ANISOU 1436 CD2 HIS B 90 2557 2465 2318 -30 17 69 C ATOM 1437 CE1 HIS A 90 49.262 -8.470 18.005 1.00 20.14 C ANISOU 1437 CE1 HIS B 90 2522 2753 2375 -45 45 65 C ATOM 1438 NE2 HIS A 90 50.556 -8.569 18.247 1.00 21.05 N ANISOU 1438 NE2 HIS B 90 2713 2903 2381 -39 38 92 N ATOM 1439 N ILE A 91 50.591 -8.064 11.340 1.00 16.42 N ANISOU 1439 N ILE B 91 2113 2075 2051 19 12 16 N ATOM 1440 CA ILE A 91 50.253 -7.402 10.077 1.00 16.05 C ANISOU 1440 CA ILE B 91 2076 2030 1992 15 -36 -12 C ATOM 1441 C ILE A 91 49.544 -8.432 9.201 1.00 16.50 C ANISOU 1441 C ILE B 91 2147 2095 2024 0 -7 -10 C ATOM 1442 O ILE A 91 50.111 -9.486 8.917 1.00 14.69 O ANISOU 1442 O ILE B 91 1985 1858 1736 -17 11 -145 O ATOM 1443 CB ILE A 91 51.504 -6.799 9.354 1.00 16.79 C ANISOU 1443 CB ILE B 91 2200 2082 2097 30 -45 19 C ATOM 1444 CG1 ILE A 91 52.307 -5.887 10.302 1.00 16.63 C ANISOU 1444 CG1 ILE B 91 2238 2082 1999 48 -103 19 C ATOM 1445 CG2 ILE A 91 51.106 -6.037 8.045 1.00 14.66 C ANISOU 1445 CG2 ILE B 91 1894 1933 1741 79 34 -34 C ATOM 1446 CD1 ILE A 91 51.528 -4.683 10.857 1.00 19.43 C ANISOU 1446 CD1 ILE B 91 2556 2404 2423 89 -79 -14 C ATOM 1447 N ALA A 92 48.293 -8.125 8.843 1.00 16.11 N ANISOU 1447 N ALA B 92 2018 2127 1974 -32 8 -23 N ATOM 1448 CA ALA A 92 47.476 -8.947 7.951 1.00 16.88 C ANISOU 1448 CA ALA B 92 2142 2190 2080 -35 37 2 C ATOM 1449 C ALA A 92 47.326 -8.306 6.561 1.00 17.25 C ANISOU 1449 C ALA B 92 2212 2219 2120 -4 20 9 C ATOM 1450 O ALA A 92 47.509 -7.096 6.395 1.00 16.72 O ANISOU 1450 O ALA B 92 2193 2144 2013 41 91 -35 O ATOM 1451 CB ALA A 92 46.115 -9.144 8.556 1.00 16.56 C ANISOU 1451 CB ALA B 92 2028 2152 2109 -51 -4 -31 C ATOM 1452 N ALA A 93 47.009 -9.138 5.571 1.00 17.85 N ANISOU 1452 N ALA B 93 2332 2270 2178 -15 10 18 N ATOM 1453 CA ALA A 93 46.534 -8.668 4.279 1.00 18.71 C ANISOU 1453 CA ALA B 93 2389 2394 2324 -21 -11 -9 C ATOM 1454 C ALA A 93 45.019 -8.871 4.284 1.00 19.44 C ANISOU 1454 C ALA B 93 2477 2489 2418 -27 -23 -1 C ATOM 1455 O ALA A 93 44.534 -10.011 4.333 1.00 19.33 O ANISOU 1455 O ALA B 93 2396 2409 2539 -104 -70 1 O ATOM 1456 CB ALA A 93 47.198 -9.461 3.146 1.00 18.72 C ANISOU 1456 CB ALA B 93 2412 2488 2212 -6 -3 11 C ATOM 1457 N ILE A 94 44.279 -7.767 4.319 1.00 19.52 N ANISOU 1457 N ILE B 94 2475 2507 2433 -16 -44 82 N ATOM 1458 CA ILE A 94 42.817 -7.828 4.301 1.00 20.93 C ANISOU 1458 CA ILE B 94 2654 2680 2618 8 -32 51 C ATOM 1459 C ILE A 94 42.339 -7.315 2.958 1.00 20.29 C ANISOU 1459 C ILE B 94 2555 2594 2560 0 -31 18 C ATOM 1460 O ILE A 94 42.480 -6.130 2.659 1.00 20.12 O ANISOU 1460 O ILE B 94 2515 2564 2563 41 -69 -13 O ATOM 1461 CB ILE A 94 42.199 -7.049 5.468 1.00 21.22 C ANISOU 1461 CB ILE B 94 2674 2686 2700 15 1 82 C ATOM 1462 CG1 ILE A 94 42.663 -7.671 6.790 1.00 23.93 C ANISOU 1462 CG1 ILE B 94 2995 3238 2859 23 -48 48 C ATOM 1463 CG2 ILE A 94 40.686 -7.078 5.380 1.00 22.89 C ANISOU 1463 CG2 ILE B 94 2836 2958 2901 60 -71 139 C ATOM 1464 CD1 ILE A 94 42.475 -6.789 7.978 1.00 26.86 C ANISOU 1464 CD1 ILE B 94 3506 3357 3342 54 -58 -173 C ATOM 1465 N ASP A 95 41.816 -8.236 2.145 1.00 20.36 N ANISOU 1465 N ASP B 95 2591 2528 2616 -46 -21 26 N ATOM 1466 CA ASP A 95 41.431 -7.967 0.754 1.00 19.83 C ANISOU 1466 CA ASP B 95 2551 2478 2504 -30 -26 -25 C ATOM 1467 C ASP A 95 42.495 -7.175 -0.014 1.00 19.76 C ANISOU 1467 C ASP B 95 2575 2461 2469 7 -28 -62 C ATOM 1468 O ASP A 95 42.188 -6.216 -0.741 1.00 19.67 O ANISOU 1468 O ASP B 95 2544 2376 2553 52 4 -63 O ATOM 1469 CB ASP A 95 40.059 -7.270 0.695 1.00 20.65 C ANISOU 1469 CB ASP B 95 2670 2556 2617 -10 -51 21 C ATOM 1470 CG ASP A 95 39.491 -7.193 -0.726 1.00 21.55 C ANISOU 1470 CG ASP B 95 2752 2735 2698 26 -60 -33 C ATOM 1471 OD1 ASP A 95 39.876 -8.012 -1.593 1.00 19.93 O ANISOU 1471 OD1 ASP B 95 2546 2499 2527 64 -53 -73 O ATOM 1472 OD2 ASP A 95 38.656 -6.296 -0.972 1.00 22.58 O ANISOU 1472 OD2 ASP B 95 2882 2790 2905 160 -106 -104 O ATOM 1473 N GLY A 96 43.744 -7.596 0.137 1.00 18.83 N ANISOU 1473 N GLY B 96 2460 2349 2346 -3 -53 -89 N ATOM 1474 CA GLY A 96 44.846 -7.025 -0.610 1.00 19.03 C ANISOU 1474 CA GLY B 96 2476 2401 2353 33 15 2 C ATOM 1475 C GLY A 96 45.439 -5.755 -0.034 1.00 18.93 C ANISOU 1475 C GLY B 96 2425 2438 2329 -15 -8 -5 C ATOM 1476 O GLY A 96 46.275 -5.124 -0.676 1.00 19.24 O ANISOU 1476 O GLY B 96 2507 2558 2245 -28 70 19 O ATOM 1477 N THR A 97 45.009 -5.366 1.168 1.00 19.08 N ANISOU 1477 N THR B 97 2478 2419 2352 -13 0 27 N ATOM 1478 CA THR A 97 45.547 -4.169 1.852 1.00 18.80 C ANISOU 1478 CA THR B 97 2400 2378 2366 -11 -4 46 C ATOM 1479 C THR A 97 46.153 -4.495 3.218 1.00 19.02 C ANISOU 1479 C THR B 97 2429 2409 2390 -8 -10 23 C ATOM 1480 O THR A 97 45.543 -5.208 4.018 1.00 20.19 O ANISOU 1480 O THR B 97 2483 2631 2556 -58 18 79 O ATOM 1481 CB THR A 97 44.457 -3.077 2.008 1.00 18.53 C ANISOU 1481 CB THR B 97 2407 2310 2322 8 1 51 C ATOM 1482 OG1 THR A 97 44.046 -2.632 0.705 1.00 17.38 O ANISOU 1482 OG1 THR B 97 2150 2181 2270 48 -85 44 O ATOM 1483 CG2 THR A 97 44.980 -1.872 2.819 1.00 17.84 C ANISOU 1483 CG2 THR B 97 2182 2381 2213 54 9 70 C ATOM 1484 N LEU A 98 47.346 -3.972 3.490 1.00 18.45 N ANISOU 1484 N LEU B 98 2363 2334 2312 39 33 0 N ATOM 1485 CA LEU A 98 48.047 -4.264 4.758 1.00 18.15 C ANISOU 1485 CA LEU B 98 2320 2293 2281 39 1 -17 C ATOM 1486 C LEU A 98 47.386 -3.568 5.950 1.00 18.83 C ANISOU 1486 C LEU B 98 2419 2415 2319 3 -6 -6 C ATOM 1487 O LEU A 98 47.177 -2.359 5.935 1.00 18.20 O ANISOU 1487 O LEU B 98 2420 2309 2185 139 48 12 O ATOM 1488 CB LEU A 98 49.525 -3.867 4.662 1.00 18.12 C ANISOU 1488 CB LEU B 98 2350 2287 2245 77 55 -33 C ATOM 1489 CG LEU A 98 50.358 -4.632 3.618 1.00 15.52 C ANISOU 1489 CG LEU B 98 2008 1931 1956 68 20 25 C ATOM 1490 CD1 LEU A 98 51.690 -3.948 3.498 1.00 14.06 C ANISOU 1490 CD1 LEU B 98 1871 1606 1862 91 -121 -142 C ATOM 1491 CD2 LEU A 98 50.511 -6.125 4.002 1.00 13.66 C ANISOU 1491 CD2 LEU B 98 1820 1740 1629 65 -39 -179 C ATOM 1492 N LYS A 99 47.064 -4.329 6.990 1.00 19.40 N ANISOU 1492 N LYS B 99 2474 2460 2436 -30 -64 5 N ATOM 1493 CA LYS A 99 46.373 -3.759 8.133 1.00 21.31 C ANISOU 1493 CA LYS B 99 2696 2740 2661 11 -28 46 C ATOM 1494 C LYS A 99 46.891 -4.382 9.406 1.00 20.91 C ANISOU 1494 C LYS B 99 2649 2680 2616 -12 11 23 C ATOM 1495 O LYS A 99 47.229 -5.553 9.416 1.00 20.11 O ANISOU 1495 O LYS B 99 2604 2588 2448 60 -55 23 O ATOM 1496 CB LYS A 99 44.857 -3.965 8.007 1.00 22.21 C ANISOU 1496 CB LYS B 99 2852 2800 2787 -3 27 6 C ATOM 1497 CG LYS A 99 44.217 -3.060 6.941 1.00 23.63 C ANISOU 1497 CG LYS B 99 2865 3106 3005 8 -97 106 C ATOM 1498 CD LYS A 99 42.783 -3.412 6.628 1.00 25.89 C ANISOU 1498 CD LYS B 99 3218 3330 3287 0 11 -4 C ATOM 1499 CE LYS A 99 42.252 -2.544 5.485 1.00 28.56 C ANISOU 1499 CE LYS B 99 3732 3597 3519 125 -78 218 C ATOM 1500 NZ LYS A 99 42.466 -1.089 5.742 1.00 30.87 N ANISOU 1500 NZ LYS B 99 3970 3811 3946 -3 130 -40 N ATOM 1501 N TYR A 100 46.967 -3.587 10.467 1.00 20.90 N ANISOU 1501 N TYR B 100 2657 2635 2648 0 -5 5 N ATOM 1502 CA TYR A 100 47.318 -4.106 11.771 1.00 21.98 C ANISOU 1502 CA TYR B 100 2811 2796 2741 -19 17 -19 C ATOM 1503 C TYR A 100 46.140 -4.888 12.321 1.00 23.10 C ANISOU 1503 C TYR B 100 2945 2929 2902 -65 -13 -11 C ATOM 1504 O TYR A 100 44.981 -4.439 12.235 1.00 21.37 O ANISOU 1504 O TYR B 100 2747 2732 2640 -63 -35 64 O ATOM 1505 CB TYR A 100 47.658 -2.968 12.744 1.00 21.70 C ANISOU 1505 CB TYR B 100 2767 2726 2750 -35 0 -37 C ATOM 1506 CG TYR A 100 48.128 -3.451 14.095 1.00 21.43 C ANISOU 1506 CG TYR B 100 2806 2594 2742 -44 37 -72 C ATOM 1507 CD1 TYR A 100 49.446 -3.877 14.279 1.00 21.12 C ANISOU 1507 CD1 TYR B 100 2639 2683 2700 -99 16 -11 C ATOM 1508 CD2 TYR A 100 47.260 -3.493 15.196 1.00 21.47 C ANISOU 1508 CD2 TYR B 100 2759 2543 2854 -86 25 -32 C ATOM 1509 CE1 TYR A 100 49.899 -4.310 15.517 1.00 21.29 C ANISOU 1509 CE1 TYR B 100 2699 2602 2785 -29 17 29 C ATOM 1510 CE2 TYR A 100 47.708 -3.935 16.438 1.00 21.71 C ANISOU 1510 CE2 TYR B 100 2722 2727 2799 -86 48 -18 C ATOM 1511 CZ TYR A 100 49.031 -4.352 16.586 1.00 21.81 C ANISOU 1511 CZ TYR B 100 2818 2686 2781 15 5 2 C ATOM 1512 OH TYR A 100 49.498 -4.796 17.808 1.00 22.09 O ANISOU 1512 OH TYR B 100 2837 2820 2733 -77 38 8 O ATOM 1513 N GLU A 101 46.455 -6.022 12.939 1.00 24.70 N ANISOU 1513 N GLU B 101 3177 3127 3079 -4 -30 -29 N ATOM 1514 CA GLU A 101 45.441 -6.893 13.486 1.00 27.99 C ANISOU 1514 CA GLU B 101 3578 3511 3543 -34 -14 -8 C ATOM 1515 C GLU A 101 45.753 -7.256 14.938 1.00 30.02 C ANISOU 1515 C GLU B 101 3862 3775 3769 -33 -19 41 C ATOM 1516 O GLU A 101 46.852 -7.745 15.245 1.00 28.89 O ANISOU 1516 O GLU B 101 3669 3691 3617 -71 29 80 O ATOM 1517 CB GLU A 101 45.360 -8.149 12.623 1.00 28.15 C ANISOU 1517 CB GLU B 101 3621 3527 3545 -52 -38 -30 C ATOM 1518 CG GLU A 101 43.993 -8.428 12.126 1.00 29.90 C ANISOU 1518 CG GLU B 101 3731 3797 3832 -28 -21 -4 C ATOM 1519 CD GLU A 101 43.949 -9.634 11.211 1.00 31.98 C ANISOU 1519 CD GLU B 101 4140 3990 4019 -94 43 -75 C ATOM 1520 OE1 GLU A 101 44.778 -10.562 11.379 1.00 31.32 O ANISOU 1520 OE1 GLU B 101 4166 3806 3925 -171 -56 -81 O ATOM 1521 OE2 GLU A 101 43.081 -9.646 10.319 1.00 34.07 O ANISOU 1521 OE2 GLU B 101 4314 4346 4285 -136 -133 58 O ATOM 1522 N LEU A 102 44.788 -6.985 15.818 1.00 33.09 N ANISOU 1522 N LEU B 102 4193 4216 4163 27 32 -6 N ATOM 1523 CA LEU A 102 44.858 -7.364 17.236 1.00 36.23 C ANISOU 1523 CA LEU B 102 4618 4615 4530 24 -4 14 C ATOM 1524 C LEU A 102 44.189 -8.717 17.452 1.00 38.10 C ANISOU 1524 C LEU B 102 4870 4815 4789 7 -7 28 C ATOM 1525 O LEU A 102 44.768 -9.606 18.068 1.00 38.93 O ANISOU 1525 O LEU B 102 5001 4964 4827 25 -42 31 O ATOM 1526 CB LEU A 102 44.219 -6.280 18.136 1.00 35.64 C ANISOU 1526 CB LEU B 102 4582 4544 4416 23 26 21 C ATOM 1527 CG LEU A 102 43.868 -6.556 19.616 1.00 35.68 C ANISOU 1527 CG LEU B 102 4547 4546 4462 1 47 -41 C ATOM 1528 CD1 LEU A 102 45.094 -6.805 20.520 1.00 35.76 C ANISOU 1528 CD1 LEU B 102 4639 4588 4358 37 -6 22 C ATOM 1529 CD2 LEU A 102 43.011 -5.415 20.170 1.00 36.41 C ANISOU 1529 CD2 LEU B 102 4660 4613 4560 68 21 -40 C ATOM 1530 N GLU A 103 42.971 -8.869 16.938 1.00 40.27 N ANISOU 1530 N GLU B 103 5091 5146 5061 22 -16 49 N ATOM 1531 CA GLU A 103 42.267 -10.152 16.972 1.00 41.77 C ANISOU 1531 CA GLU B 103 5281 5290 5299 -10 34 10 C ATOM 1532 C GLU A 103 41.618 -10.486 15.629 1.00 42.60 C ANISOU 1532 C GLU B 103 5371 5438 5375 -11 -1 49 C ATOM 1533 O GLU A 103 41.444 -9.612 14.769 1.00 42.79 O ANISOU 1533 O GLU B 103 5432 5455 5372 -12 1 82 O ATOM 1534 CB GLU A 103 41.230 -10.193 18.106 1.00 42.64 C ANISOU 1534 CB GLU B 103 5401 5411 5389 -19 -4 38 C ATOM 1535 CG GLU A 103 40.240 -9.026 18.129 1.00 43.49 C ANISOU 1535 CG GLU B 103 5432 5531 5560 18 84 37 C ATOM 1536 CD GLU A 103 39.025 -9.284 19.015 1.00 45.91 C ANISOU 1536 CD GLU B 103 5689 6004 5749 8 -77 120 C ATOM 1537 OE1 GLU A 103 38.521 -10.433 19.029 1.00 45.77 O ANISOU 1537 OE1 GLU B 103 5728 5548 6115 -150 -27 -20 O ATOM 1538 OE2 GLU A 103 38.565 -8.331 19.689 1.00 44.78 O ANISOU 1538 OE2 GLU B 103 5774 5451 5787 170 47 -211 O TER 1539 GLU B 103 HETATM 1540 O HOH A 110 34.788 2.352 22.016 1.00 16.25 O ANISOU 1540 O HOH A 110 1541 2027 2603 -136 -35 -73 O HETATM 1541 O HOH A 111 54.805 10.284 12.085 1.00 16.72 O ANISOU 1541 O HOH A 111 2469 1898 1983 -24 -111 -39 O HETATM 1542 O HOH A 112 52.566 16.097 15.125 1.00 15.32 O ANISOU 1542 O HOH A 112 2062 1923 1833 -109 165 155 O HETATM 1543 O HOH A 113 49.722 15.039 6.900 1.00 18.02 O ANISOU 1543 O HOH A 113 2464 2422 1960 -39 38 413 O HETATM 1544 O HOH A 114 44.079 17.717 26.747 1.00 20.30 O ANISOU 1544 O HOH A 114 2657 2243 2811 369 -149 -276 O HETATM 1545 O HOH A 115 38.438 16.322 21.485 1.00 24.20 O ANISOU 1545 O HOH A 115 3114 2679 3399 225 180 223 O HETATM 1546 O HOH A 116 50.739 17.883 10.731 1.00 20.74 O ANISOU 1546 O HOH A 116 2651 2598 2630 -97 47 -85 O HETATM 1547 O HOH A 117 60.164 13.523 31.209 1.00 22.00 O ANISOU 1547 O HOH A 117 3254 2710 2395 -187 -93 -101 O HETATM 1548 O HOH A 118 35.788 8.287 26.282 1.00 23.44 O ANISOU 1548 O HOH A 118 3031 2657 3216 5 149 -126 O HETATM 1549 O HOH A 119 59.616 16.745 30.305 1.00 23.27 O ANISOU 1549 O HOH A 119 2861 2966 3013 146 73 213 O HETATM 1550 O HOH A 120 43.408 0.214 25.102 1.00 23.83 O ANISOU 1550 O HOH A 120 2999 3418 2637 63 -42 -60 O HETATM 1551 O HOH A 121 41.579 19.877 17.152 1.00 25.50 O ANISOU 1551 O HOH A 121 3179 2925 3585 158 -80 -288 O HETATM 1552 O HOH A 122 39.758 2.497 27.786 1.00 20.36 O ANISOU 1552 O HOH A 122 2570 2370 2794 161 184 80 O HETATM 1553 O HOH A 123 48.156 19.429 28.454 1.00 30.30 O ANISOU 1553 O HOH A 123 3658 3661 4192 93 57 -178 O HETATM 1554 O HOH A 124 44.926 3.809 8.840 1.00 20.90 O ANISOU 1554 O HOH A 124 2484 2703 2752 -135 -95 -300 O HETATM 1555 O HOH A 125 55.684 5.283 24.565 1.00 30.30 O ANISOU 1555 O HOH A 125 4009 3694 3809 93 57 -176 O HETATM 1556 O HOH A 126 55.112 15.250 16.295 1.00 21.60 O ANISOU 1556 O HOH A 126 2559 2839 2806 195 46 92 O HETATM 1557 O HOH A 127 42.660 15.532 10.861 1.00 25.19 O ANISOU 1557 O HOH A 127 3270 3384 2917 41 92 -50 O HETATM 1558 O HOH A 128 44.917 1.931 26.675 1.00 26.04 O ANISOU 1558 O HOH A 128 3247 3169 3475 -42 -174 190 O HETATM 1559 O HOH A 129 29.841 -0.062 11.944 1.00 29.53 O ANISOU 1559 O HOH A 129 3680 3799 3739 -90 -114 -226 O HETATM 1560 O HOH A 130 50.208 26.216 22.937 1.00 27.15 O ANISOU 1560 O HOH A 130 3679 3083 3554 122 -157 -134 O HETATM 1561 O HOH A 131 46.269 19.221 25.841 1.00 19.00 O ANISOU 1561 O HOH A 131 2626 2425 2168 2 -46 -158 O HETATM 1562 O HOH A 132 49.731 22.620 24.731 1.00 25.51 O ANISOU 1562 O HOH A 132 3480 2994 3217 85 -4 -84 O HETATM 1563 O HOH A 133 39.455 6.390 6.840 1.00 31.67 O ANISOU 1563 O HOH A 133 4077 4171 3782 -103 -7 33 O HETATM 1564 O HOH A 134 48.343 23.655 21.479 1.00 30.73 O ANISOU 1564 O HOH A 134 3946 3619 4109 72 54 134 O HETATM 1565 O HOH A 135 44.283 18.139 23.270 1.00 21.40 O ANISOU 1565 O HOH A 135 2716 2659 2753 -135 -34 86 O HETATM 1566 O HOH A 136 27.883 5.268 15.195 1.00 28.16 O ANISOU 1566 O HOH A 136 3587 3600 3512 -174 -27 18 O HETATM 1567 O HOH A 137 53.706 27.650 24.540 1.00 29.87 O ANISOU 1567 O HOH A 137 3870 3564 3914 -117 -69 -143 O HETATM 1568 O HOH A 138 50.456 2.251 23.341 1.00 23.72 O ANISOU 1568 O HOH A 138 3413 3185 2412 -70 -58 33 O HETATM 1569 O HOH A 139 31.210 13.513 16.949 1.00 26.28 O ANISOU 1569 O HOH A 139 3335 3295 3354 76 32 12 O HETATM 1570 O HOH A 140 56.553 25.177 24.418 1.00 24.89 O ANISOU 1570 O HOH A 140 3208 2905 3343 -232 -161 -38 O HETATM 1571 O HOH A 141 33.272 6.282 28.150 1.00 29.66 O ANISOU 1571 O HOH A 141 3621 4038 3610 126 -123 -128 O HETATM 1572 O HOH A 142 45.176 15.257 8.938 1.00 26.63 O ANISOU 1572 O HOH A 142 3486 3098 3532 17 101 157 O HETATM 1573 O HOH A 143 55.013 7.460 20.419 1.00 27.65 O ANISOU 1573 O HOH A 143 3508 3320 3676 -13 163 -84 O HETATM 1574 O HOH A 144 38.460 -5.346 18.683 1.00 32.38 O ANISOU 1574 O HOH A 144 4094 3957 4249 -62 -92 179 O HETATM 1575 O HOH A 145 43.398 20.425 23.926 1.00 38.49 O ANISOU 1575 O HOH A 145 4934 4802 4885 -42 111 -10 O HETATM 1576 O HOH A 146 30.010 6.100 13.418 1.00 24.19 O ANISOU 1576 O HOH A 146 2941 2962 3285 -169 140 5 O HETATM 1577 O HOH A 147 60.130 9.438 27.097 1.00 28.01 O ANISOU 1577 O HOH A 147 2977 3879 3787 204 -218 -26 O HETATM 1578 O HOH A 148 60.831 25.725 19.831 1.00 39.53 O ANISOU 1578 O HOH A 148 4823 5122 5072 -32 0 -39 O HETATM 1579 O HOH A 149 35.458 -2.257 13.102 1.00 21.48 O ANISOU 1579 O HOH A 149 2641 2778 2742 97 -61 -194 O HETATM 1580 O HOH A 150 45.600 22.085 7.694 1.00 37.43 O ANISOU 1580 O HOH A 150 4827 4833 4561 -152 -32 -150 O HETATM 1581 O HOH A 151 33.105 -9.851 23.095 1.00 32.40 O ANISOU 1581 O HOH A 151 4202 4120 3986 -122 42 93 O HETATM 1582 O HOH A 152 44.542 16.976 29.393 1.00 22.65 O ANISOU 1582 O HOH A 152 2765 2728 3111 -86 -56 149 O HETATM 1583 O HOH A 153 57.580 23.364 27.806 1.00 26.44 O ANISOU 1583 O HOH A 153 3328 3430 3287 20 106 -114 O HETATM 1584 O HOH A 154 57.147 15.814 14.484 1.00 25.40 O ANISOU 1584 O HOH A 154 3524 3410 2715 -216 62 46 O HETATM 1585 O HOH A 155 53.951 16.807 11.006 1.00 25.50 O ANISOU 1585 O HOH A 155 3536 3256 2896 86 -220 -85 O HETATM 1586 O HOH A 156 31.010 1.284 22.405 1.00 26.11 O ANISOU 1586 O HOH A 156 3520 3454 2945 133 51 117 O HETATM 1587 O HOH A 157 56.368 19.165 19.846 1.00 31.48 O ANISOU 1587 O HOH A 157 4025 4220 3713 -227 -61 143 O HETATM 1588 O HOH A 158 59.848 11.947 21.214 1.00 39.01 O ANISOU 1588 O HOH A 158 4803 5051 4967 66 -225 -132 O HETATM 1589 O HOH A 159 50.050 11.046 32.028 1.00 32.80 O ANISOU 1589 O HOH A 159 4013 4269 4178 -131 125 -35 O HETATM 1590 O HOH A 160 42.098 18.746 20.712 1.00 32.28 O ANISOU 1590 O HOH A 160 3898 3999 4366 -75 -90 -73 O HETATM 1591 O HOH A 161 29.569 9.133 20.651 1.00 36.97 O ANISOU 1591 O HOH A 161 4765 4711 4570 98 83 -14 O HETATM 1592 O HOH A 162 50.717 26.203 17.838 1.00 34.28 O ANISOU 1592 O HOH A 162 4479 4156 4389 -17 90 188 O HETATM 1593 O HOH A 163 38.533 -8.011 8.400 1.00 43.87 O ANISOU 1593 O HOH A 163 5537 5569 5562 -3 182 19 O HETATM 1594 O HOH A 164 23.383 -5.071 12.211 1.00 44.54 O ANISOU 1594 O HOH A 164 5703 5543 5675 -47 -63 -141 O HETATM 1595 O HOH A 165 51.084 22.896 13.012 1.00 31.29 O ANISOU 1595 O HOH A 165 4017 3722 4148 -174 -170 159 O HETATM 1596 O HOH A 166 40.180 -3.723 19.827 1.00 32.04 O ANISOU 1596 O HOH A 166 4109 4008 4056 33 179 3 O HETATM 1597 O HOH A 167 54.198 21.976 17.986 1.00 37.13 O ANISOU 1597 O HOH A 167 4652 4812 4643 -10 208 -356 O HETATM 1598 O HOH A 168 32.611 13.977 19.555 1.00 32.65 O ANISOU 1598 O HOH A 168 4200 4052 4151 63 88 -68 O HETATM 1599 O HOH A 169 57.299 28.137 20.976 1.00 29.49 O ANISOU 1599 O HOH A 169 3537 3988 3677 85 -129 178 O HETATM 1600 O HOH A 170 58.114 9.190 21.592 1.00 39.93 O ANISOU 1600 O HOH A 170 4986 5333 4852 -47 -5 75 O HETATM 1601 O HOH A 171 34.492 16.796 21.400 1.00 40.48 O ANISOU 1601 O HOH A 171 5146 5109 5126 16 -54 -85 O HETATM 1602 O HOH A 172 46.786 -1.957 24.022 1.00 32.27 O ANISOU 1602 O HOH A 172 4100 4118 4043 66 56 30 O HETATM 1603 O HOH A 173 53.034 20.879 15.598 1.00 36.33 O ANISOU 1603 O HOH A 173 4718 4702 4382 14 -56 107 O HETATM 1604 O HOH A 174 55.139 18.171 17.337 1.00 30.93 O ANISOU 1604 O HOH A 174 3915 3962 3874 -69 138 127 O HETATM 1605 O HOH A 175 60.089 23.096 18.593 1.00 33.53 O ANISOU 1605 O HOH A 175 4043 4226 4469 177 31 -1 O HETATM 1606 O HOH A 176 48.805 8.492 28.651 1.00 36.21 O ANISOU 1606 O HOH A 176 4646 4710 4400 101 151 20 O HETATM 1607 O HOH A 177 57.631 7.042 30.136 1.00 48.22 O ANISOU 1607 O HOH A 177 6011 6200 6109 32 -88 41 O HETATM 1608 O HOH A 178 46.145 22.166 9.864 1.00 32.30 O ANISOU 1608 O HOH A 178 4030 4406 3833 -22 52 211 O HETATM 1609 O HOH A 179 45.418 -1.283 10.040 1.00 39.73 O ANISOU 1609 O HOH A 179 5191 4997 4907 67 -13 8 O HETATM 1610 O HOH A 180 46.715 20.836 13.764 1.00 33.26 O ANISOU 1610 O HOH A 180 4410 3955 4271 3 -160 6 O HETATM 1611 O HOH A 181 28.322 2.062 12.024 1.00 29.07 O ANISOU 1611 O HOH A 181 3772 3754 3519 -129 -129 -180 O HETATM 1612 O HOH A 182 45.282 14.706 30.403 1.00 32.72 O ANISOU 1612 O HOH A 182 3857 4407 4165 78 188 39 O HETATM 1613 O HOH A 183 43.163 8.265 7.868 1.00 34.86 O ANISOU 1613 O HOH A 183 4357 4578 4308 30 61 127 O HETATM 1614 O HOH A 184 41.410 -3.103 9.640 1.00 32.91 O ANISOU 1614 O HOH A 184 3849 4478 4177 103 53 -64 O HETATM 1615 O HOH A 185 28.541 6.583 10.818 1.00 41.79 O ANISOU 1615 O HOH A 185 5157 5444 5277 -221 -98 99 O HETATM 1616 O HOH A 186 50.622 3.313 26.989 1.00 29.40 O ANISOU 1616 O HOH A 186 3727 3460 3983 38 -163 134 O HETATM 1617 O HOH A 187 27.254 0.998 9.424 1.00 44.85 O ANISOU 1617 O HOH A 187 5480 5775 5785 22 48 29 O HETATM 1618 O HOH A 188 31.869 10.513 22.923 1.00 33.83 O ANISOU 1618 O HOH A 188 4231 4334 4288 66 -112 104 O HETATM 1619 O HOH A 189 25.942 -7.633 15.445 1.00 39.37 O ANISOU 1619 O HOH A 189 4910 5019 5029 59 106 -65 O HETATM 1620 O HOH A 190 34.219 11.746 5.307 1.00 37.08 O ANISOU 1620 O HOH A 190 4698 4701 4687 62 14 31 O HETATM 1621 O HOH A 191 44.497 1.330 8.061 1.00 38.60 O ANISOU 1621 O HOH A 191 4928 4927 4809 -6 6 44 O HETATM 1622 O HOH A 192 44.997 21.917 25.785 1.00 37.07 O ANISOU 1622 O HOH A 192 4663 4977 4444 70 -8 29 O HETATM 1623 O HOH A 193 58.961 17.833 20.366 1.00 44.67 O ANISOU 1623 O HOH A 193 5664 5675 5633 -251 -4 -126 O HETATM 1624 O HOH A 194 33.299 -4.086 7.582 1.00 48.31 O ANISOU 1624 O HOH A 194 6077 6139 6138 51 1 -143 O HETATM 1625 O HOH A 195 36.878 9.179 28.379 1.00 45.39 O ANISOU 1625 O HOH A 195 5621 5771 5852 133 159 16 O HETATM 1626 O HOH A 196 53.906 18.502 13.616 1.00 56.71 O ANISOU 1626 O HOH A 196 7114 7254 7179 -31 -57 33 O HETATM 1627 O HOH A 197 32.855 0.885 23.933 1.00 29.70 O ANISOU 1627 O HOH A 197 3688 3822 3774 -156 39 -93 O HETATM 1628 O HOH A 198 37.701 17.621 8.972 1.00 50.35 O ANISOU 1628 O HOH A 198 6434 6448 6248 46 47 108 O HETATM 1629 O HOH A 199 22.981 8.447 17.638 1.00 43.72 O ANISOU 1629 O HOH A 199 5575 5587 5449 -9 -16 -60 O HETATM 1630 O HOH A 200 30.316 5.839 23.704 1.00 37.88 O ANISOU 1630 O HOH A 200 4794 4995 4603 22 60 24 O HETATM 1631 O HOH A 201 57.247 4.818 26.716 1.00 42.04 O ANISOU 1631 O HOH A 201 5313 5429 5231 49 -43 36 O HETATM 1632 O HOH A 202 60.919 26.304 22.299 1.00 39.61 O ANISOU 1632 O HOH A 202 4957 4953 5140 -44 -113 15 O HETATM 1633 O HOH A 203 53.993 29.454 21.972 1.00 41.51 O ANISOU 1633 O HOH A 203 5246 5432 5094 57 -25 183 O HETATM 1634 O HOH A 204 37.620 19.580 14.390 1.00 51.97 O ANISOU 1634 O HOH A 204 6721 6408 6615 23 -29 114 O HETATM 1635 O HOH A 205 62.003 17.885 29.250 1.00 45.71 O ANISOU 1635 O HOH A 205 5549 5871 5944 -1 -18 -6 O HETATM 1636 O HOH A 206 38.928 -3.573 7.852 1.00 44.55 O ANISOU 1636 O HOH A 206 5539 5757 5630 24 53 126 O HETATM 1637 O HOH A 207 33.071 0.630 5.388 1.00 40.82 O ANISOU 1637 O HOH A 207 5255 5320 4932 51 1 24 O HETATM 1638 O HOH A 208 57.967 27.143 23.240 1.00 32.86 O ANISOU 1638 O HOH A 208 4238 3995 4252 -57 -128 118 O HETATM 1639 O HOH A 209 47.815 1.530 29.438 1.00 61.49 O ANISOU 1639 O HOH A 209 7837 7773 7752 -2 -19 -41 O HETATM 1640 O HOH A 210 43.265 4.924 29.971 1.00 46.28 O ANISOU 1640 O HOH A 210 5875 5952 5755 0 82 59 O HETATM 1641 O HOH A 211 26.196 -0.297 6.624 1.00 41.49 O ANISOU 1641 O HOH A 211 5153 5284 5326 6 -32 19 O HETATM 1642 O HOH A 212 40.562 17.410 24.251 1.00 40.20 O ANISOU 1642 O HOH A 212 5066 4967 5241 14 -54 -49 O HETATM 1643 O HOH A 213 34.235 -6.305 6.160 1.00 48.62 O ANISOU 1643 O HOH A 213 6157 6244 6072 -22 -7 -107 O HETATM 1644 O HOH A 214 53.644 2.917 27.101 1.00 43.96 O ANISOU 1644 O HOH A 214 5606 5417 5678 -31 -7 79 O HETATM 1645 O HOH A 215 38.402 13.544 4.948 1.00 53.97 O ANISOU 1645 O HOH A 215 6869 6809 6827 55 13 -17 O HETATM 1646 O HOH A 216 63.006 16.512 26.035 1.00 46.17 O ANISOU 1646 O HOH A 216 5806 5767 5968 31 -117 -12 O HETATM 1647 O HOH A 217 48.010 10.813 29.698 1.00 33.66 O ANISOU 1647 O HOH A 217 4345 4618 3825 -46 51 -119 O HETATM 1648 O HOH A 218 58.137 20.796 18.783 1.00 53.54 O ANISOU 1648 O HOH A 218 6912 6807 6624 39 -13 92 O HETATM 1649 O HOH A 219 43.569 22.099 13.851 1.00 38.84 O ANISOU 1649 O HOH A 219 4978 4814 4963 46 36 3 O HETATM 1650 O HOH A 220 50.216 27.052 19.996 1.00 49.35 O ANISOU 1650 O HOH A 220 6260 6289 6202 87 63 75 O HETATM 1651 O HOH A 221 44.342 18.996 6.867 1.00 55.51 O ANISOU 1651 O HOH A 221 7028 7039 7022 58 4 67 O HETATM 1652 O HOH A 222 36.991 18.658 17.895 1.00 40.38 O ANISOU 1652 O HOH A 222 5201 4911 5229 102 -9 126 O HETATM 1653 O HOH A 223 38.373 10.123 5.213 1.00 47.95 O ANISOU 1653 O HOH A 223 6092 6140 5987 6 48 -37 O HETATM 1654 O HOH A 224 39.600 0.018 9.182 1.00 44.86 O ANISOU 1654 O HOH A 224 5784 5894 5366 -51 -119 -92 O HETATM 1655 O HOH A 225 32.828 18.580 19.096 1.00 43.67 O ANISOU 1655 O HOH A 225 5571 5399 5622 -42 -3 -15 O HETATM 1656 O HOH A 226 38.999 15.105 24.645 1.00 55.02 O ANISOU 1656 O HOH A 226 6883 7027 6993 -82 43 56 O HETATM 1657 O HOH A 227 59.509 24.487 29.245 1.00 40.18 O ANISOU 1657 O HOH A 227 4975 5307 4983 -78 39 -69 O HETATM 1658 O HOH A 228 32.362 14.243 11.208 1.00 48.63 O ANISOU 1658 O HOH A 228 6215 6067 6193 32 -18 -53 O HETATM 1659 O HOH A 229 63.352 16.473 22.353 1.00 39.91 O ANISOU 1659 O HOH A 229 5161 4847 5153 43 -23 -64 O HETATM 1660 O HOH A 230 31.121 15.390 18.312 1.00 41.43 O ANISOU 1660 O HOH A 230 5097 5367 5275 156 -32 -60 O HETATM 1661 O HOH A 231 28.347 15.028 16.934 1.00 52.18 O ANISOU 1661 O HOH A 231 6581 6583 6662 -1 -21 -28 O HETATM 1662 O HOH B 110 65.309 1.674 5.461 1.00 19.51 O ANISOU 1662 O HOH B 110 2929 2477 2004 100 56 113 O HETATM 1663 O HOH B 111 48.909 -4.739 -0.173 1.00 15.86 O ANISOU 1663 O HOH B 111 1832 1934 2259 -23 -26 54 O HETATM 1664 O HOH B 112 58.386 -11.428 16.469 1.00 18.58 O ANISOU 1664 O HOH B 112 2677 2235 2145 -105 182 194 O HETATM 1665 O HOH B 113 58.021 0.870 1.956 1.00 16.04 O ANISOU 1665 O HOH B 113 2091 1868 2135 -73 -8 -12 O HETATM 1666 O HOH B 114 46.180 0.585 -1.486 1.00 16.76 O ANISOU 1666 O HOH B 114 2339 1857 2170 291 -94 43 O HETATM 1667 O HOH B 115 52.840 -14.898 -0.472 1.00 20.21 O ANISOU 1667 O HOH B 115 2945 2336 2398 17 70 -15 O HETATM 1668 O HOH B 116 52.145 6.212 11.524 1.00 15.85 O ANISOU 1668 O HOH B 116 2352 1676 1993 -28 130 17 O HETATM 1669 O HOH B 117 47.030 0.019 7.358 1.00 21.65 O ANISOU 1669 O HOH B 117 2916 2817 2493 47 216 12 O HETATM 1670 O HOH B 118 47.791 -0.481 4.043 1.00 21.67 O ANISOU 1670 O HOH B 118 2774 2694 2766 -38 83 -144 O HETATM 1671 O HOH B 119 60.812 -13.578 7.342 1.00 25.66 O ANISOU 1671 O HOH B 119 3405 3223 3121 28 164 125 O HETATM 1672 O HOH B 120 56.677 -10.735 1.877 1.00 19.51 O ANISOU 1672 O HOH B 120 2463 2364 2585 147 -185 -139 O HETATM 1673 O HOH B 121 50.090 -16.482 -1.774 1.00 21.35 O ANISOU 1673 O HOH B 121 2686 2904 2521 -46 -150 -120 O HETATM 1674 O HOH B 122 46.672 -11.908 6.249 1.00 21.62 O ANISOU 1674 O HOH B 122 2852 2569 2792 76 -74 -107 O HETATM 1675 O HOH B 123 55.727 7.571 11.798 1.00 17.97 O ANISOU 1675 O HOH B 123 2337 2167 2322 39 150 -194 O HETATM 1676 O HOH B 124 41.007 -15.319 -1.483 1.00 15.99 O ANISOU 1676 O HOH B 124 2471 1830 1772 -114 -25 21 O HETATM 1677 O HOH B 125 50.484 -16.833 -6.458 1.00 16.53 O ANISOU 1677 O HOH B 125 1922 2213 2143 -59 -135 192 O HETATM 1678 O HOH B 126 47.378 -17.368 1.197 1.00 17.53 O ANISOU 1678 O HOH B 126 2610 2212 1837 223 -249 -169 O HETATM 1679 O HOH B 127 49.977 3.084 8.798 1.00 20.27 O ANISOU 1679 O HOH B 127 2502 2396 2801 -22 -31 -409 O HETATM 1680 O HOH B 128 51.625 -21.578 7.966 1.00 21.48 O ANISOU 1680 O HOH B 128 2830 2508 2823 -215 -160 51 O HETATM 1681 O HOH B 129 52.962 -16.580 7.729 1.00 24.67 O ANISOU 1681 O HOH B 129 2956 3101 3314 -101 -46 -37 O HETATM 1682 O HOH B 130 58.225 -10.340 -0.557 1.00 22.29 O ANISOU 1682 O HOH B 130 2937 2980 2549 7 -40 89 O HETATM 1683 O HOH B 131 60.267 9.695 15.414 1.00 21.58 O ANISOU 1683 O HOH B 131 2816 2460 2923 -251 -87 55 O HETATM 1684 O HOH B 132 68.797 6.603 15.471 1.00 24.75 O ANISOU 1684 O HOH B 132 2450 3415 3538 90 -325 -163 O HETATM 1685 O HOH B 133 57.904 -11.601 -3.034 1.00 18.85 O ANISOU 1685 O HOH B 133 2439 2191 2532 246 99 -84 O HETATM 1686 O HOH B 134 63.268 -3.753 1.414 1.00 24.46 O ANISOU 1686 O HOH B 134 2596 3174 3521 -93 -15 49 O HETATM 1687 O HOH B 135 38.329 -8.936 -3.766 1.00 19.61 O ANISOU 1687 O HOH B 135 2175 2635 2640 7 -56 -78 O HETATM 1688 O HOH B 136 40.812 -4.009 2.977 1.00 30.65 O ANISOU 1688 O HOH B 136 3700 3783 4160 40 -10 -22 O HETATM 1689 O HOH B 137 62.204 5.118 20.183 1.00 26.62 O ANISOU 1689 O HOH B 137 3322 3295 3497 -40 154 -7 O HETATM 1690 O HOH B 138 49.265 1.530 10.964 1.00 24.20 O ANISOU 1690 O HOH B 138 2786 3277 3132 21 -75 -295 O HETATM 1691 O HOH B 139 58.409 7.252 10.876 1.00 22.15 O ANISOU 1691 O HOH B 139 2726 2659 3030 -27 -188 -145 O HETATM 1692 O HOH B 140 53.036 -17.795 -3.655 1.00 21.06 O ANISOU 1692 O HOH B 140 2956 2360 2685 77 -85 -58 O HETATM 1693 O HOH B 141 60.861 -16.036 5.689 1.00 36.75 O ANISOU 1693 O HOH B 141 4683 4726 4553 -88 44 45 O HETATM 1694 O HOH B 142 39.266 -8.497 -6.536 1.00 24.97 O ANISOU 1694 O HOH B 142 3161 3035 3290 157 14 203 O HETATM 1695 O HOH B 143 36.731 -11.622 -9.227 1.00 26.22 O ANISOU 1695 O HOH B 143 3010 3265 3686 72 -74 -91 O HETATM 1696 O HOH B 144 66.063 5.849 11.459 1.00 28.86 O ANISOU 1696 O HOH B 144 3635 3501 3829 77 -79 308 O HETATM 1697 O HOH B 145 42.769 -2.874 -6.196 1.00 31.50 O ANISOU 1697 O HOH B 145 4220 3948 3798 64 -223 127 O HETATM 1698 O HOH B 146 54.788 -5.364 -6.824 1.00 23.66 O ANISOU 1698 O HOH B 146 3074 3015 2899 -25 269 36 O HETATM 1699 O HOH B 147 75.739 -1.081 10.611 1.00 26.11 O ANISOU 1699 O HOH B 147 3185 3537 3197 -52 163 -78 O HETATM 1700 O HOH B 148 44.634 -10.136 0.956 1.00 24.46 O ANISOU 1700 O HOH B 148 3497 2828 2966 -79 -281 96 O HETATM 1701 O HOH B 149 55.034 -3.878 -3.299 1.00 21.49 O ANISOU 1701 O HOH B 149 2681 2928 2554 -74 71 -85 O HETATM 1702 O HOH B 150 60.054 3.271 20.923 1.00 23.18 O ANISOU 1702 O HOH B 150 3147 3027 2632 -129 133 -14 O HETATM 1703 O HOH B 151 51.554 -2.756 18.697 1.00 25.47 O ANISOU 1703 O HOH B 151 3009 3171 3495 49 -31 46 O HETATM 1704 O HOH B 152 52.541 -1.751 -7.551 1.00 24.61 O ANISOU 1704 O HOH B 152 3389 2852 3109 -121 123 56 O HETATM 1705 O HOH B 153 64.342 1.797 25.781 1.00 30.52 O ANISOU 1705 O HOH B 153 3699 3658 4236 176 -10 -74 O HETATM 1706 O HOH B 154 56.331 -15.989 4.964 1.00 23.42 O ANISOU 1706 O HOH B 154 3314 2784 2801 176 96 40 O HETATM 1707 O HOH B 155 56.855 -14.785 15.282 1.00 29.51 O ANISOU 1707 O HOH B 155 3603 3683 3925 5 -57 157 O HETATM 1708 O HOH B 156 64.073 -5.089 25.996 1.00 29.47 O ANISOU 1708 O HOH B 156 4185 3664 3345 6 -36 -50 O HETATM 1709 O HOH B 157 57.073 6.004 22.335 1.00 29.83 O ANISOU 1709 O HOH B 157 3783 3871 3678 115 60 -80 O HETATM 1710 O HOH B 158 68.919 4.244 8.715 1.00 29.88 O ANISOU 1710 O HOH B 158 4107 3593 3653 -101 -7 116 O HETATM 1711 O HOH B 159 47.552 -13.906 4.485 1.00 25.70 O ANISOU 1711 O HOH B 159 3201 3451 3112 -23 -194 -139 O HETATM 1712 O HOH B 160 63.923 9.311 12.305 1.00 49.68 O ANISOU 1712 O HOH B 160 6172 6351 6351 -29 -38 61 O HETATM 1713 O HOH B 161 61.588 -15.871 3.353 1.00 52.08 O ANISOU 1713 O HOH B 161 6577 6405 6804 121 9 -92 O HETATM 1714 O HOH B 162 61.963 7.321 21.761 1.00 24.79 O ANISOU 1714 O HOH B 162 2644 3238 3536 -92 -100 -218 O HETATM 1715 O HOH B 163 59.464 0.520 -0.317 1.00 23.57 O ANISOU 1715 O HOH B 163 3249 2846 2858 -58 262 -16 O HETATM 1716 O HOH B 164 55.742 -13.138 1.148 1.00 26.52 O ANISOU 1716 O HOH B 164 3378 3150 3546 279 -76 -86 O HETATM 1717 O HOH B 165 56.848 -3.892 -6.194 1.00 31.63 O ANISOU 1717 O HOH B 165 4016 3994 4006 16 -52 -43 O HETATM 1718 O HOH B 166 45.472 1.529 1.064 1.00 18.75 O ANISOU 1718 O HOH B 166 2513 2073 2539 -2 -94 -39 O HETATM 1719 O HOH B 167 59.284 -13.832 16.327 1.00 24.29 O ANISOU 1719 O HOH B 167 3158 3000 3069 -185 43 47 O HETATM 1720 O HOH B 168 65.844 -8.049 20.078 1.00 29.52 O ANISOU 1720 O HOH B 168 3752 3524 3938 117 205 161 O HETATM 1721 O HOH B 169 41.955 -2.911 -3.616 1.00 37.91 O ANISOU 1721 O HOH B 169 4698 4837 4869 1 -10 62 O HETATM 1722 O HOH B 170 47.475 -16.714 5.656 1.00 28.42 O ANISOU 1722 O HOH B 170 3649 3983 3165 -159 209 -166 O HETATM 1723 O HOH B 171 56.408 -7.696 21.456 1.00 30.86 O ANISOU 1723 O HOH B 171 3690 3893 4143 62 -418 -66 O HETATM 1724 O HOH B 172 65.255 -4.118 2.966 1.00 31.53 O ANISOU 1724 O HOH B 172 4123 3942 3911 55 44 27 O HETATM 1725 O HOH B 173 74.093 -6.529 17.729 1.00 29.34 O ANISOU 1725 O HOH B 173 3736 3502 3908 21 -169 -40 O HETATM 1726 O HOH B 174 51.892 -14.144 -7.448 1.00 30.62 O ANISOU 1726 O HOH B 174 4096 3884 3652 -72 -84 36 O HETATM 1727 O HOH B 175 37.413 -9.813 1.795 1.00 28.41 O ANISOU 1727 O HOH B 175 3595 3720 3479 -154 -88 -279 O HETATM 1728 O HOH B 176 58.262 -15.556 7.258 1.00 33.40 O ANISOU 1728 O HOH B 176 4265 4091 4331 -95 138 -208 O HETATM 1729 O HOH B 177 53.568 -14.694 13.258 1.00 37.93 O ANISOU 1729 O HOH B 177 4877 4466 5068 128 -30 -18 O HETATM 1730 O HOH B 178 55.999 -15.849 9.703 1.00 20.66 O ANISOU 1730 O HOH B 178 2602 2542 2704 16 54 -95 O HETATM 1731 O HOH B 179 65.872 -1.304 3.662 1.00 36.00 O ANISOU 1731 O HOH B 179 4845 4498 4331 -90 11 5 O HETATM 1732 O HOH B 180 35.898 -8.159 19.866 1.00 32.15 O ANISOU 1732 O HOH B 180 4233 3637 4346 148 -95 101 O HETATM 1733 O HOH B 181 43.578 1.168 5.505 1.00 38.86 O ANISOU 1733 O HOH B 181 5028 4836 4900 -32 69 -39 O HETATM 1734 O HOH B 182 62.547 -6.026 -0.005 1.00 32.97 O ANISOU 1734 O HOH B 182 4070 4140 4314 285 100 -280 O HETATM 1735 O HOH B 183 51.439 -8.577 20.798 1.00 33.71 O ANISOU 1735 O HOH B 183 4370 4369 4070 -95 -130 221 O HETATM 1736 O HOH B 184 53.125 2.143 -3.393 1.00 28.24 O ANISOU 1736 O HOH B 184 3792 3550 3385 -118 102 45 O HETATM 1737 O HOH B 185 63.978 3.449 23.305 1.00 26.92 O ANISOU 1737 O HOH B 185 3520 3189 3519 -162 -112 108 O HETATM 1738 O HOH B 186 52.688 4.944 22.437 1.00 32.58 O ANISOU 1738 O HOH B 186 4023 4171 4183 148 77 -39 O HETATM 1739 O HOH B 187 68.112 5.922 22.908 1.00 40.30 O ANISOU 1739 O HOH B 187 5077 5015 5218 -92 -88 -79 O HETATM 1740 O HOH B 188 62.644 -7.912 18.986 1.00 32.20 O ANISOU 1740 O HOH B 188 4515 4038 3681 13 -25 90 O HETATM 1741 O HOH B 189 41.675 -11.967 13.134 1.00 62.69 O ANISOU 1741 O HOH B 189 7913 7808 8096 1 -26 83 O HETATM 1742 O HOH B 190 55.924 -13.814 -1.849 1.00 29.52 O ANISOU 1742 O HOH B 190 3840 3632 3742 -141 -111 268 O HETATM 1743 O HOH B 191 41.572 -11.977 1.397 1.00 42.31 O ANISOU 1743 O HOH B 191 5442 5409 5222 196 -29 163 O HETATM 1744 O HOH B 192 44.881 -2.155 -7.982 1.00 34.41 O ANISOU 1744 O HOH B 192 4358 4200 4513 -64 55 -102 O HETATM 1745 O HOH B 193 66.200 2.946 8.176 1.00 35.82 O ANISOU 1745 O HOH B 193 4507 4460 4640 -50 -301 97 O HETATM 1746 O HOH B 194 42.275 -6.408 14.999 1.00 30.52 O ANISOU 1746 O HOH B 194 3461 4206 3926 163 127 -139 O HETATM 1747 O HOH B 195 66.539 -11.633 3.193 1.00 42.26 O ANISOU 1747 O HOH B 195 5216 5372 5467 -25 0 -149 O HETATM 1748 O HOH B 196 77.021 -2.731 18.518 1.00 37.33 O ANISOU 1748 O HOH B 196 4517 4938 4727 133 -211 36 O HETATM 1749 O HOH B 197 66.937 7.448 14.328 1.00 38.73 O ANISOU 1749 O HOH B 197 4889 4799 5027 -27 75 10 O HETATM 1750 O HOH B 198 41.652 -4.149 -10.698 1.00 36.69 O ANISOU 1750 O HOH B 198 4785 4566 4590 170 59 -26 O HETATM 1751 O HOH B 199 43.528 -0.079 0.363 1.00 29.64 O ANISOU 1751 O HOH B 199 4013 3659 3588 153 2 12 O HETATM 1752 O HOH B 200 55.606 3.347 22.975 1.00 36.35 O ANISOU 1752 O HOH B 200 4860 4592 4357 -54 -134 -66 O HETATM 1753 O HOH B 201 64.202 -1.652 -0.060 1.00 39.49 O ANISOU 1753 O HOH B 201 5229 4817 4958 -135 21 74 O HETATM 1754 O HOH B 202 43.307 -12.905 -0.491 1.00 31.86 O ANISOU 1754 O HOH B 202 4157 3898 4047 14 178 152 O HETATM 1755 O HOH B 203 59.944 -13.688 0.034 1.00 44.01 O ANISOU 1755 O HOH B 203 5694 5627 5400 42 -75 13 O HETATM 1756 O HOH B 204 55.796 -1.804 -4.445 1.00 31.35 O ANISOU 1756 O HOH B 204 4233 3883 3792 -10 183 -11 O HETATM 1757 O HOH B 205 69.648 -3.889 9.859 1.00 34.06 O ANISOU 1757 O HOH B 205 4007 4455 4479 217 85 55 O HETATM 1758 O HOH B 206 60.391 9.104 10.389 1.00 37.66 O ANISOU 1758 O HOH B 206 4880 4618 4809 -87 -42 -44 O HETATM 1759 O HOH B 207 73.430 6.570 13.754 1.00 38.32 O ANISOU 1759 O HOH B 207 4942 4753 4863 -135 -111 31 O HETATM 1760 O HOH B 208 62.929 -9.450 20.979 1.00 35.36 O ANISOU 1760 O HOH B 208 4658 4370 4405 36 -92 61 O HETATM 1761 O HOH B 209 62.446 0.239 -0.238 1.00 52.42 O ANISOU 1761 O HOH B 209 6608 6602 6705 10 51 8 O HETATM 1762 O HOH B 210 55.014 -6.227 23.983 1.00 52.23 O ANISOU 1762 O HOH B 210 6618 6673 6554 -10 -10 35 O HETATM 1763 O HOH B 211 55.202 0.657 -4.343 1.00 36.04 O ANISOU 1763 O HOH B 211 4763 4374 4556 109 -35 51 O HETATM 1764 O HOH B 212 71.063 -0.836 28.349 1.00 42.62 O ANISOU 1764 O HOH B 212 5533 5521 5139 -11 -49 -14 O HETATM 1765 O HOH B 213 42.260 -3.797 -0.691 1.00 32.44 O ANISOU 1765 O HOH B 213 4030 4043 4250 -209 -253 -7 O HETATM 1766 O HOH B 214 64.212 5.962 9.129 1.00 39.39 O ANISOU 1766 O HOH B 214 5100 4959 4907 -123 -31 30 O HETATM 1767 O HOH B 215 60.501 -8.941 -0.672 1.00 34.74 O ANISOU 1767 O HOH B 215 4399 4344 4456 -6 -110 -133 O HETATM 1768 O HOH B 216 67.790 -5.454 23.858 1.00 31.67 O ANISOU 1768 O HOH B 216 4261 3897 3875 -13 -174 121 O HETATM 1769 O HOH B 217 48.604 -19.164 8.467 1.00 31.98 O ANISOU 1769 O HOH B 217 4333 3682 4134 24 204 117 O HETATM 1770 O HOH B 218 45.596 -14.971 12.519 1.00 36.43 O ANISOU 1770 O HOH B 218 4803 4593 4443 75 93 148 O HETATM 1771 O HOH B 219 59.392 -8.435 20.233 1.00 28.91 O ANISOU 1771 O HOH B 219 3810 3410 3764 7 -26 163 O HETATM 1772 O HOH B 220 41.119 0.588 -5.085 1.00 32.38 O ANISOU 1772 O HOH B 220 4102 3954 4247 -118 -54 -49 O HETATM 1773 O HOH B 221 42.477 -5.080 10.820 1.00 40.11 O ANISOU 1773 O HOH B 221 4929 4966 5343 -98 -41 34 O HETATM 1774 O HOH B 222 74.044 -1.575 25.793 1.00 40.88 O ANISOU 1774 O HOH B 222 4870 5222 5441 -23 -176 85 O HETATM 1775 O HOH B 223 68.395 0.185 5.486 1.00 31.40 O ANISOU 1775 O HOH B 223 3803 3972 4152 -159 40 17 O HETATM 1776 O HOH B 224 34.549 -11.495 -1.112 1.00 43.65 O ANISOU 1776 O HOH B 224 5522 5575 5485 -87 -60 -74 O HETATM 1777 O HOH B 225 68.243 -6.143 20.681 1.00 35.71 O ANISOU 1777 O HOH B 225 4526 4449 4591 63 -63 170 O HETATM 1778 O HOH B 226 41.053 -10.726 3.630 1.00 42.33 O ANISOU 1778 O HOH B 226 5370 5303 5409 -94 -7 -34 O HETATM 1779 O HOH B 227 44.929 -12.217 2.793 1.00 37.02 O ANISOU 1779 O HOH B 227 4886 4567 4611 -77 -18 -3 O HETATM 1780 O HOH B 228 59.481 -10.501 18.790 1.00 27.74 O ANISOU 1780 O HOH B 228 3660 3532 3348 -65 -75 80 O HETATM 1781 O HOH B 229 57.035 -17.673 8.122 1.00 44.49 O ANISOU 1781 O HOH B 229 5655 5507 5740 69 73 -2 O HETATM 1782 O HOH B 230 60.849 10.213 12.948 1.00 40.74 O ANISOU 1782 O HOH B 230 5311 4937 5231 2 -33 68 O HETATM 1783 O HOH B 231 67.705 9.010 18.746 1.00 37.93 O ANISOU 1783 O HOH B 231 4714 4845 4852 -22 -125 56 O HETATM 1784 O HOH B 232 63.039 -3.099 -2.843 1.00 54.46 O ANISOU 1784 O HOH B 232 6957 6921 6811 11 -11 -25 O HETATM 1785 O HOH B 233 43.871 0.320 -4.684 1.00 37.38 O ANISOU 1785 O HOH B 233 4771 4572 4860 43 -45 -29 O HETATM 1786 O HOH B 234 63.881 -7.874 25.291 1.00 46.97 O ANISOU 1786 O HOH B 234 6070 5843 5933 39 12 -47 O HETATM 1787 O HOH B 235 63.908 -13.683 8.240 1.00 43.11 O ANISOU 1787 O HOH B 235 5441 5303 5636 79 -8 -10 O HETATM 1788 O HOH B 236 43.658 -11.872 6.380 1.00 52.40 O ANISOU 1788 O HOH B 236 6580 6648 6678 -5 51 24 O HETATM 1789 O HOH B 237 66.728 3.307 23.461 1.00 44.10 O ANISOU 1789 O HOH B 237 5379 5640 5735 -142 -90 -123 O HETATM 1790 O HOH B 238 41.272 -0.188 1.865 1.00 42.66 O ANISOU 1790 O HOH B 238 5013 5650 5546 21 -66 -78 O HETATM 1791 O HOH B 239 48.004 -13.874 12.138 1.00 26.33 O ANISOU 1791 O HOH B 239 3872 3311 2820 -122 137 105 O HETATM 1792 O HOH B 240 54.719 -17.189 2.482 1.00 32.75 O ANISOU 1792 O HOH B 240 4260 4199 3982 149 53 -72 O HETATM 1793 O HOH B 241 42.197 -0.380 -2.078 1.00 28.50 O ANISOU 1793 O HOH B 241 3527 3551 3749 59 -221 88 O HETATM 1794 O HOH B 242 54.678 -18.401 7.337 1.00 37.25 O ANISOU 1794 O HOH B 242 4822 4635 4694 -68 20 -99 O HETATM 1795 O HOH B 243 70.184 -5.586 11.818 1.00 37.69 O ANISOU 1795 O HOH B 243 4846 4708 4765 67 -9 -79 O HETATM 1796 O HOH B 244 74.681 -3.647 24.298 1.00 36.37 O ANISOU 1796 O HOH B 244 4355 4827 4636 49 -223 28 O HETATM 1797 O HOH B 245 55.290 3.890 0.514 1.00 39.41 O ANISOU 1797 O HOH B 245 5147 4790 5034 33 17 91 O HETATM 1798 O HOH B 246 34.132 -10.410 19.151 1.00 48.44 O ANISOU 1798 O HOH B 246 6195 5899 6310 -44 -109 -77 O HETATM 1799 O HOH B 247 59.542 3.119 23.977 1.00 53.56 O ANISOU 1799 O HOH B 247 6877 6756 6717 -29 3 -116 O HETATM 1800 O HOH B 248 63.893 5.382 -0.833 1.00 44.39 O ANISOU 1800 O HOH B 248 5813 5494 5558 37 19 -44 O HETATM 1801 O HOH B 249 63.886 -10.366 1.850 1.00 51.32 O ANISOU 1801 O HOH B 249 6644 6463 6391 26 53 -22 O HETATM 1802 O HOH B 250 45.104 -12.694 9.230 1.00 37.03 O ANISOU 1802 O HOH B 250 4557 4640 4870 -195 -137 -120 O HETATM 1803 O HOH B 251 62.396 -11.408 17.314 1.00 43.74 O ANISOU 1803 O HOH B 251 5645 5446 5529 20 -22 75 O HETATM 1804 O HOH B 252 52.861 3.392 24.361 1.00 51.30 O ANISOU 1804 O HOH B 252 6408 6525 6557 0 -21 -117 O HETATM 1805 O HOH B 253 37.514 -7.924 3.631 1.00 59.63 O ANISOU 1805 O HOH B 253 7479 7521 7654 -28 23 0 O HETATM 1806 O HOH B 254 67.145 4.836 25.564 1.00 41.24 O ANISOU 1806 O HOH B 254 5259 5146 5262 80 -41 -51 O HETATM 1807 O HOH B 255 75.613 2.925 8.708 1.00 48.54 O ANISOU 1807 O HOH B 255 6147 6101 6192 32 -13 20 O HETATM 1808 O HOH B 256 33.741 -13.092 -6.745 1.00 44.55 O ANISOU 1808 O HOH B 256 5444 5738 5744 -42 -54 -202 O HETATM 1809 O HOH B 257 46.273 -10.886 15.045 1.00 61.45 O ANISOU 1809 O HOH B 257 7835 7752 7761 -6 17 36 O HETATM 1810 O HOH B 258 52.219 -17.818 10.972 1.00 34.00 O ANISOU 1810 O HOH B 258 4210 4525 4180 1 -42 103 O HETATM 1811 O HOH B 259 57.003 -15.233 -3.631 1.00 51.16 O ANISOU 1811 O HOH B 259 6337 6530 6571 73 6 118 O HETATM 1812 O HOH B 260 58.254 -0.923 -2.334 1.00 42.26 O ANISOU 1812 O HOH B 260 5275 5326 5454 -71 -164 107 O HETATM 1813 O HOH B 261 54.698 0.157 26.125 1.00 46.31 O ANISOU 1813 O HOH B 261 5981 5870 5743 3 22 -20 O HETATM 1814 O HOH B 262 75.813 -5.101 18.924 1.00 44.99 O ANISOU 1814 O HOH B 262 5713 5847 5532 18 -82 63 O HETATM 1815 O HOH B 263 56.596 -17.541 3.420 1.00 31.78 O ANISOU 1815 O HOH B 263 4376 3760 3935 -34 -175 -53 O HETATM 1816 O HOH B 264 65.743 -9.283 18.191 1.00 30.15 O ANISOU 1816 O HOH B 264 3386 3894 4175 -68 -289 295 O HETATM 1817 O HOH B 265 61.303 -11.070 0.615 1.00 38.27 O ANISOU 1817 O HOH B 265 4840 4854 4846 73 12 -15 O HETATM 1818 O HOH B 266 39.234 -5.450 -4.172 1.00 54.64 O ANISOU 1818 O HOH B 266 7003 6761 6997 46 -51 41 O HETATM 1819 O HOH B 267 68.026 3.434 6.248 1.00 59.23 O ANISOU 1819 O HOH B 267 7568 7383 7550 -20 -27 -59 O HETATM 1820 O HOH B 268 55.944 -2.686 24.097 1.00 31.87 O ANISOU 1820 O HOH B 268 3890 4255 3963 -36 -172 -34 O HETATM 1821 O HOH B 269 69.030 -9.022 8.427 1.00 44.60 O ANISOU 1821 O HOH B 269 5491 5748 5705 -35 -70 -101 O HETATM 1822 O HOH B 270 58.493 -9.206 25.099 1.00 59.18 O ANISOU 1822 O HOH B 270 7629 7451 7404 -18 0 34 O CONECT 57 156 CONECT 156 57 CONECT 431 537 CONECT 537 431 CONECT 818 917 CONECT 917 818 CONECT 1192 1298 CONECT 1298 1192 MASTER 286 0 0 5 20 0 0 6 1820 2 8 18 END